entry
stringlengths 6
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| entry_name
stringlengths 5
11
| protein_name
stringlengths 3
2.44k
| sequence
stringlengths 2
35.2k
| function
stringlengths 7
11k
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I6Y0R5
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FOLC_MYCTU
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Dihydrofolate synthase/folylpolyglutamate synthase (DHFS / FPGS) (EC 6.3.2.12) (EC 6.3.2.17) (Folylpoly-gamma-glutamate synthetase) (Tetrahydrofolylpolyglutamate synthase)
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MNSTNSGPPDSGSATGVVPTPDEIASLLQVEHLLDQRWPETRIDPSLTRISALMDLLGSPQRSYPSIHIAGTNGKTSVARMVDALVTALHRRTGRTTSPHLQSPVERISIDGKPISPAQYVATYREIEPLVALIDQQSQASAGKGGPAMSKFEVLTAMAFAAFADAPVDVAVVEVGMGGRWDATNVINAPVAVITPISIDHVDYLGADIAGIAGEKAGIITRAPDGSPDTVAVIGRQVPKVMEVLLAESVRADASVAREDSEFAVLRRQIAVGGQVLQLQGLGGVYSDIYLPLHGEHQAHNAVLALASVEAFFGAGAQRQLDGDAVRAGFAAVTSPGRLERMRSAPTVFIDAAHNPAGASALAQTLAHEFDFRFLVGVLSVLGDKDVDGILAALEPVFDSVVVTHNGSPRALDVEALALAAGERFGPDRVRTAENLRDAIDVATSLVDDAAADPDVAGDAFSRTGIVITGSVVTAGAARTLFGRDPQ
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Catalyzes the addition of a glutamate residue to dihydropteroate (7,8-dihydropteroate or H2Pte) to form dihydrofolate (7,8-dihydrofolate monoglutamate or H2Pte-Glu). Also catalyzes successive additions of L-glutamate to tetrahydrofolate, leading to folylpolyglutamate derivatives (By similarity). Is involved in the bioactivation of the antituberculous drug para-aminosalicylic acid (PAS). Is able to use hydroxy-dihydropteroate (H2PtePAS) as substrate, which is the product formed by the action of DHPS (FolP1) on PAS, leading to hydroxy-dihydrofolate (H2PtePAS-Glu). This compound inhibits dihydrofolate reductase DHFR (DfrA), the next enzyme in the folate pathway, and thus disrupts the folate-dependent metabolic pathways.
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I6Y2J4
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LIPY_MYCTU
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Triacylglycerol lipase (EC 3.1.1.3) (Esterase/lipase) (Triolein hydrolase) [Cleaved into: Cytosolic triacylglycerol lipase; Extracellular triacylglycerol lipase]
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MVSYVVALPEVMSAAATDVASIGSVVATASQGVAGATTTVLAAAEDEVSAAIAALFSGHGQDYQALSAQLAVFHERFVQALTGAAKGYAAAELANASLLQSEFASGIGNGFATIHQEIQRAPTALAAGFTQVPPFAAAQAGIFTGTPSGAAGFDIASLWPVKPLLSLSALETHFAIPNNPLLALIASDIPPLSWFLGNSPPPLLNSLLGQTVQYTTYDGMSVVQITPAHPTGEYVVAIHGGAFILPPSIFHWLNYSVTAYQTGATVQVPIYPLVQEGGTAGTVVPAMAGLISTQIAQHGVSNVSVVGDSAGGNLALAAAQYMVSQGNPVPSSMVLLSPWLDVGTWQISQAWAGNLAVNDPLVSPLYGSLNGLPPTYVYSGSLDPLAQQAVVLEHTAVVQGAPFSFVLAPWQIHDWILLTPWGLLSWPQINQQLGIAA
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Catalyzes the hydrolysis of both intracellular and extracellular triacylglycerol (TAG). In vitro, can also hydrolyze p-nitrophenyl (pNP) esters with various chain lengths, including pNP-acetate (C2), pNP-butyrate (C4), pNP-caproate (C6), pNP-caprylate (C8), pNP-laurate (C12), pNP-myristate (C14), pNP-palmitate (C16) and pNP-stearate (C18). Also hydrolyzes monobutyrin, tributyrin and trioctanoin. Overexpression results in increase of virulence characterized by reduced survival of infected mouse and increased burden of bacilli in the lungs. Hydrolyzes internal or host-derived TAG depending on its localization.
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I6Y3Q0
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CHSE5_MYCTU
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Acyl-CoA dehydrogenase FadE27 (ACAD) (EC 1.3.99.-) (3-oxocholest-4-en-26-oyl-CoA dehydrogenase beta subunit)
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MDFTTTEAAQDLGGLVDTIVDAVCTPEHQRELDKLEQRFDRELWRKLIDAGILSSAAPESLGGDGFGVLEQVAVLVALGHQLAAVPYLESVVLAAGALARFGSPELQQGWGVSAVSGDRILTVALDGEMGEGPVQAAGTGHGYRLTGTRTQVGYGPVADAFLVPAETDSGAAVFLVAAGDPGVAVTALATTGLGSVGHLELNGAKVDAARRVGGTDVAVWLGTLSTLSRTAFQLGVLERGLQMTAEYARTREQFDRPIGSFQAVGQRLADGYIDVKGLRLTLTQAAWRVAEDSLASRECPQPADIDVATAGFWAAEAGHRVAHTIVHVHGGVGVDTDHPVHRYFLAAKQTEFALGGATGQLRRIGRELAETPA
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Involved in the first cycle of side chain dehydrogenation in the beta-oxidation of cholesterol catabolism. It contributes partly to the virulence by increasing the efficiency of beta-oxidation. Catalyzes the dehydrogenation of acyl-CoA ester side chains of (25S)-3-oxo-cholest-4-en-26-oyl-CoA (3-OCS-CoA) to yield (24E)-3-oxo-cholest-4,24-dien-26-oyl-CoA. Also able to dehydrogenate steroyl-CoA such as 3-oxo-chol-4-en-24-oyl-CoA (3-OCO-CoA) as well as 3-oxo-4-pregnene-20-carboxyl-CoA (3-OPC-CoA). It dehydrogenates only (25S)-OCS-CoA diastereomer.
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I6Y4D2
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PEPAM_MYCTU
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N-acetylmuramoyl-L-alanine amidase Rv3717 (EC 3.5.1.28) (Zinc-dependent peptidoglycan amidase)
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MIVGVLVAAATPIISSASATPANIAGMVVFIDPGHNGANDASIGRQVPTGRGGTKNCQASGTSTNSGYPEHTFTWETGLRLRAALNALGVRTALSRGNDNALGPCVDERANMANALRPNAIVSLHADGGPASGRGFHVNYSAPPLNAIQAGPSVQFARIMRDQLQASGIPKANYIGQDGLYGRSDLAGLNLAQYPSILVELGNMKNPADSALMESAEGRQKYANALVRGVAGFLATQGQAR
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Cell-wall hydrolase that hydrolyzes the amide bond between N-acetylmuramic acid and L-alanine in cell-wall glycopeptides. Is able to hydrolyze the cell walls of several bacterial species (i.e. Paenibacillus sp., B.avium, E.coli DH5alpha, E.aerogenes, L.acidophilus, B.thuringiensis, B.pumilus, B.subtilis and E.coli W3110), thereby showing that it is a cell-wall hydrolase with broad-spectrum activity. May have a role in peptidoglycan fragment recycling.
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I6Y4U9
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DYP_MYCTU
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Dye-decolorizing peroxidase (DyP) (EC 1.11.1.7)
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MAVPAVSPQPILAPLTPAAIFLVATIGADGEATVHDALSKISGLVRAIGFRDPTKHLSVVVSIGSDAWDRLFAGPRPTELHPFVELTGPRHTAPATPGDLLFHIRAETMDVCFELAGRILKSMGDAVTVVDEVHGFRFFDNRDLLGFVDGTENPSGPIAIKATTIGDEDRNFAGSCYVHVQKYVHDMASWESLSVTEQERVIGRTKLDDIELDDNAKPANSHVALNVITDDDGTERKIVRHNMPFGEVGKGEYGTYFIGYSRTPTVTEQMLRNMFLGDPAGNTDRVLDFSTAVTGGLFFSPTIDFLDHPPPLPQAATPTLAAGSLSIGSLKGSPR
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Cargo of a type 1 encapsulin nanocompartment in situ this cargo protects against oxidative stress at low pH. When expressed in the cytoplasm (absence of the encapsulin shell gene) it is almost as protective as the intact nanocompartment its encapsulation has a modest yet significant effect on protection against oxidative stress at low pH. A heme-dependent peroxidase, it probably does not have deferrochelatase activity. Converts guaiacol and H2O2 to tetraguaiacol, also acts on 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) (ABTS). Retains peroxidase activity when encapsulated but has a reduced set of substrates acts on ABTS but not guaiacol.
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I6Y778
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FABG4_MYCTU
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3-oxoacyl-[acyl-carrier-protein] reductase [NADH] (EC 1.1.1.212) (Beta-ketoacyl CoA reductase) (FASII-like 3-oxoacyl-thioester reductase) (HMwFabG)
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MAPKRSSDLFSQVVNSGPGSFLARQLGVPQPETLRRYRAGEPPLTGSLLIGGAGRVVEPLRAALEKDYDLVGNNLGGRWADSFGGLVFDATGITEPAGLKGLHEFFTPVLRNLGRCGRVVVVGGTPEAAASTNERIAQRALEGFTRSLGKELRRGATTALVYLSPDAKPAATGLESTMRFLLSAKSAYVDGQVFSVGADDSTPPADWEKPLDGKVAIVTGAARGIGATIAEVFARDGAHVVAIDVESAAENLAETASKVGGTALWLDVTADDAVDKISEHLRDHHGGKADILVNNAGITRDKLLANMDDARWDAVLAVNLLAPLRLTEGLVGNGSIGEGGRVIGLSSIAGIAGNRGQTNYATTKAGMIGITQALAPGLAAKGITINAVAPGFIETQMTAAIPLATREVGRRLNSLLQGGQPVDVAEAIAYFASPASNAVTGNVIRVCGQAMIGA
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Catalyzes the NADH-dependent reduction of beta-ketoacyl derivatives. Can accept the beta-oxo fatty acyl group covalently linked with CoA or ACP for catalysis. Highly specific for NADH. Could be involved in fatty acid biosynthesis (Probable).
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I6Y9J2
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LDT2_MYCTU
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L,D-transpeptidase 2 (LDT 2) (EC 2.3.2.-) (Ldt(Mt2))
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MPKVGIAAQAGRTRVRRAWLTALMMTAVMIGAVACGSGRGPAPIKVIADKGTPFADLLVPKLTASVTDGAVGVTVDAPVSVTAADGVLAAVTMVNDNGRPVAGRLSPDGLRWSTTEQLGYNRRYTLNATALGLGGAATRQLTFQTSSPAHLTMPYVMPGDGEVVGVGEPVAIRFDENIADRGAAEKAIKITTNPPVEGAFYWLNNREVRWRPEHFWKPGTAVDVAVNTYGVDLGEGMFGEDNVQTHFTIGDEVIATADDNTKILTVRVNGEVVKSMPTSMGKDSTPTANGIYIVGSRYKHIIMDSSTYGVPVNSPNGYRTDVDWATQISYSGVFVHSAPWSVGAQGHTNTSHGCLNVSPSNAQWFYDHVKRGDIVEVVNTVGGTLPGIDGLGDWNIPWDQWRAGNAKA
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Generates 3->3 cross-links in peptidoglycan, catalyzing the cleavage of the mDap(3)-D-Ala(4) bond of a tetrapeptide donor stem and the formation of a bond between the carbonyl of mDap(3) of the donor stem and the side chain of mDap(3) of the acceptor stem. Is specific for donor substrates containing a stem tetrapeptide since it cannot use pentapeptide stems.
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I6Y9Q3
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PRPC_MYCTU
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2-methylcitrate synthase (2-MCS) (MCS) (EC 2.3.3.5) (Citrate synthase) (EC 2.3.3.16)
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MTGPLAAARSVAATKSMTAPTVDERPDIKKGLAGVVVDTTAISKVVPQTNSLTYRGYPVQDLAARCSFEQVAFLLWRGELPTDAELALFSQRERASRRVDRSMLSLLAKLPDNCHPMDVVRTAISYLGAEDPDEDDAAANRAKAMRMMAVLPTIVAIDMRRRRGLPPIAPHSGLGYAQNFLHMCFGEVPETAVVSAFEQSMILYAEHGFNASTFAARVVTSTQSDIYSAVTGAIGALKGRLHGGANEAVMHDMIEIGDPANAREWLRAKLARKEKIMGFGHRVYRHGDSRVPTMKRALERVGTVRDGQRWLDIYQVLAAEMASATGILPNLDFPTGPAYYLMGFDIASFTPIFVMSRITGWTAHIMEQATANALIRPLSAYCGHEQRVLPGTF
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Involved in the catabolism of short chain fatty acids (SCFA) via the tricarboxylic acid (TCA)(acetyl degradation route) and via the 2-methylcitrate cycle I (propionate degradation route). Catalyzes the Claisen condensation of propionyl-CoA and oxaloacetate (OAA) to yield 2-methylcitrate (2-MC) and CoA. Also catalyzes the condensation of oxaloacetate with acetyl-CoA.
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I6YCA3
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CHSE4_MYCTU
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Acyl-CoA dehydrogenase FadE26 (ACAD) (EC 1.3.99.-) (3-oxocholest-4-en-26-oyl-CoA dehydrogenase alpha subunit)
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MRISYTPQQEELRRELRSYFATLMTPERREALSSVQGEYGVGNVYRETIAQMGRDGWLALGWPKEYGGQGRSAMDQLIFTDEAAIAGAPVPFLTINSVAPTIMAYGTDEQKRFFLPRIAAGDLHFSIGYSEPGAGTDLANLRTTAVRDGDDYVVNGQKMWTSLIQYADYVWLAVRTNPESSGAKKHRGISVLIVPTTAEGFSWTPVHTMAGPDTSATYYSDVRVPVANRVGEENAGWKLVTNQLNHERVALVSPAPIFGCLREVREWAQNTKDAGGTRLIDSEWVQLNLARVHAKAEVLKLINWELASSQSGPKDAGPSPADASAAKVFGTELATEAYRLLMEVLGTAATLRQNSPGALLRGRVERMHRACLILTFGGGTNEVQRDIIGMVALGLPRANR
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Involved in the first cycle of side chain dehydrogenation in the beta-oxidation of cholesterol catabolism. It contributes partly to the virulence by increasing the efficiency of beta-oxidation. Catalyzes the dehydrogenation of acyl-CoA ester side chains of (25S)-3-oxo-cholest-4-en-26-oyl-CoA (3-OCS-CoA) to yield (24E)-3-oxo-cholest-4,24-dien-26-oyl-CoA. Also able to dehydrogenate steroyl-CoA such as 3-oxo-chol-4-en-24-oyl-CoA (3-OCO-CoA) as well as 3-oxo-4-pregnene-20-carboxyl-CoA (3-OPC-CoA). It dehydrogenates only (25S)-OCS-CoA diastereomer (Probable).
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I6YFP0
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BIRA_MYCTU
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Biotin--[acetyl-CoA-carboxylase] ligase (EC 6.3.4.15) (Biotin--[biotin carboxyl-carrier protein] ligase) (Biotin--protein ligase) (BPL) (Biotin-[acetyl-CoA carboxylase] synthetase)
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MTDRDRLRPPLDERSLRDQLIGAGSGWRQLDVVAQTGSTNADLLARAASGADIDGVVLIAEHQTAGRGRHGRGWAATARAQIILSVGVRVVDVPVQAWGWLSLAAGLAVLDSVAPLIAVPPAETGLKWPNDVLARGGKLAGILAEVAQPFVVLGVGLNVTQAPEEVDPDATSLLDLGVAAPDRNRIASRLLRELEARIIQWRNANPQLAADYRARSLTIGSRVRVELPGGQDVVGIARDIDDQGRLCLDVGGRTVVVSAGDVVHLR
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Catalyzes the transfer of biotin onto a conserved lysine residue of the biotin carboxyl carrier protein (BCCP) domain of acetyl-CoA carboxylase and converts it to active holo-BCCP. Forms an acyl-adenylate intermediate. Cannot use GTP or desthiobiotin.
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I6YG32
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RIMI_MYCTU
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N-alpha-acetyltransferase RimI (EC 2.3.1.255) (EC 2.3.1.258)
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MTADTEPVTIGALTRADAQRCAELEAQLFVGDDPWPPAAFNRELASPHNHYVGARSGGTLVGYAGISRLGRTPPFEYEVHTIGVDPAYQGRGIGRRLLRELLDFARGGVVYLEVRTDNDAALALYRSVGFQRVGLRRRYYRVSGADAYTMRRDSGDPS
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N-alpha-acetyltransferase that specifically mediates the acetylation of N-terminal residues. Able to mediate acetylation of a wide variety of N-terminal residues, with preference for hydrophobic N-termini. Acetylates GroS/GroES and GroEL1. Able to acetylate the ribosomal protein S18, but it is unclear whether it acetylates its N-terminal alanine residue.
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I7CA98
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TODT_PSEPT
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Response regulator protein TodT
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MPARWGCLFPGKYPCQTGLRHMSDRASVIYILDDDNAVLEALSSLVRSIGLSVECFSSASVFLNDVNRSACGCLILDVRMPEMSGLDVQRQLKELGEQIPIIFISGHGDIPMAVKAIKAGAVDFFTKPFREEELLGAIRAALKLAPQQRSNAPRVSELKENYESLSKREQQVLKFVLRGYLNKQTALELDISEATVKVHRHNIMRKMKVSSIQDLVRVTERLKDSLE
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Member of the two-component regulatory system TodS/TodT involved in the regulation of toluene degradation. Phosphorylated TodT activates transcription of the tod operon (todXFC1C2BADEGIH). Binds specifically to three boxes in the tod promoter region in a cooperative manner. Boxes-1 and -2 are pseudopalindromes and Box-3 is a half-palindrome.
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I7H727
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TPS2_TOOSI
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Sesquiterpene synthase 2 (TsTPS2) (Alpha-humulene synthase TPS2) (EC 4.2.3.104) (Alpha-selinene synthase TPS2) (EC 4.2.3.198) (Beta-elemene synthase TPS2) (EC 4.2.3.-) (Delta-cadinene synthase TPS2) (EC 4.2.3.-)
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MSVPVSQIPSLKAKGVIMRRNANYHPNIWGDRFINYVPVDKMNHTCHLQAIEELKDAVRRELLTATGLSQLNLIDAIQRLGVGYHFERELEEALQHVYHKNHYHDDTEDNLYSISLRFRLLRQHGYYVSCDILNKFKDEKDNFKESLTTDVPGMLSLYEAAHPGVHGEDILDEAIAFTTTHLKSLAIDHLRNPSLASQVIHALRQPLHRGVPRLENRRYISIYQDEVSHNKALVKLFKLDFNLVQSLHKKELSEISRWWKELDLANKLPFARDRLVECYFWIIGVYYEPQYSLARKILTKTIAMGSIIDDIYDVYGTPEELNLFTDAIERWDASCMDQLPEYMQIFYEALLDLYNEIEKEIAKEGWSYRVHYAKEAMKILARGYHDESKWFHNNYIPTMEEYMHVALVTSGYTMLTTSSFLGMDNIVTKETFDWVFSGPKIIRASGTIARLMDDVKSHKFEQERGHAASAVECYMEQHGVSEQEVCKEFYQQVGNAWKDINQDFLKPTDVPMTILMRVLNLARVIDVVYKEGDGYTHVGKVMKENVASLLIDPIPV
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Sesquiterpene synthase involved in the biosynthesis of volatile compounds known for their medicinal efficacy for treating enteritis, dysentery, itch and some cancers. Mediates the conversion of (2E,6E)-farnesyl diphosphate (FPP) into beta-elemene, alpha-humulene, delta-cadinene and alpha-selinene.
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I7HJS4
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ZN683_MOUSE
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Tissue-resident T-cell transcription regulator protein ZNF683 (Homolog of Blimp-1 in T-cell) (Hobit) (Zinc finger protein 683)
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MKALDGLRESLYPSLDFQLYQDDQVCSADASQPLADSVGAHDLAWSERMCPLPLAPAKSPLLACPESPDLCLCALQKTPLGRAPQDLGEDASNMRHQPPSLYKASTDSEKLTIKDSLNREEMGNEPERGAYPHLPPRTSSFPDAGLDRKSLSPLTFWPWLPPTLISKEPPIHIYPIFPGYPLLPLPYLFTYGALPSAQHPYLFMLPPHSTYPTVAGPSLLMTASGSGPRIPQEKTLLLHSGAFQSAGHTLHSQVESRSSRDTRTPGQAGVAAPTRRAVPGSRAGVIALPYPLKKENGKILYECNVCGKNFGQLSNLKVHLRVHSGERPFQCALCQKRFTQLAHLQKHHLVHTGERPHQCQVCHKRFSSSSNLKTHLRLHSGAKPSQCGLCPSYLTPNVYPKLHHRLRAPQLRGLTHTHLPLASLTCLAQWHQGALDLVEKKMGWTVDKVSSESKGKQG
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Transcription factor that mediates a transcriptional program in various innate and adaptive immune tissue-resident lymphocyte T-cell types such as tissue-resident memory T (Trm), natural killer (trNK) and natural killer T (NKT) cells and negatively regulates gene expression of proteins that promote the egress of tissue-resident T-cell populations from non-lymphoid organs. Plays a role in the development, retention and long-term establishment of adaptive and innate tissue-resident lymphocyte T-cell types in non-lymphoid organs, such as the skin and gut, but also in other nonbarrier tissues like liver and kidney, and therefore may provide immediate immunological protection against reactivating infections or viral reinfection. Also plays a role in the differentiation of both thymic and peripheral NKT cells. Negatively regulates the accumulation of interferon-gamma (IFN-gamma) in NKT cells at steady state or after antigenic stimulation. Positively regulates granzyme B production in NKT cells after innate stimulation. Associates with the transcriptional repressor PRDM1/BLIMP1 to chromatin at gene promoter regions.
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J3KML8
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GFY_MOUSE
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Golgi-associated olfactory signaling regulator (Golgi protein in olfactory neurons) (Goofy)
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MQPFSPIFFHLLFLLNGLSSRAAPSPGQPVVADLQGMLQPSGMPTGTLENLTRDQPTPGSSASHPPEHSETPPSASPHISTKILRETPSPSPFLSLETPIPDQLTSVAESQGTSQMSPSRATLGKPSETPKPDPTGISPSDSPETPKPNPSNTSPPESPESVYTDPTPTLHHESPEISKRDTPKLSPGEESKIPSPRPTQFLSSKSLETYDPSATRHLNSALEPTTHPDPTESPQSVFLTTHNSNPTVVPQTQFPTSPSQNVTETARTSDLEPSSSLPTQPTTFREEATTPSEPGLSPSPEAPAVTRVATPGLSTSDSPGTKELHVPQNSDPKGPDIPLPSARIAGPPAPLEHPNQVAPAPQRHSRGDTVNTIIVVERVKETGVTLVSRPRGSVGGALCLFFAGTGLLIGIFLLLWCLYRRASRHRSFAHHRLRDSGDEPVLHLDAPKDPLDLYFYAPDAWVPSHIATQPPPSTPPLPPKLPPPPRGPQRLEALSPAALSPNFF
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Required for proper function of the olfactory system. May be involved in establishing the acuity of olfactory sensory signaling.
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J3QMI4
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CAHM3_MOUSE
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Calcium homeostasis modulator protein 3
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MDRFRMLFQHLQSSSESVMNGICLLLAAVTVKIYSSLDFNCPCLERYNALYGLGLLLTPPLALFLCGLLVNRQSVLMVEEWRRPAGHRRKDLGIIRYMCSSVLQRALAAPLVWILLALLDGKCFVCAFSNSVDPEKFLDFANMTPRQVQLFLAKVPCKEDELVKNSPARKAVSRYLRCLSQAIGWSITLLVIVVAFLARCLRPCFDQTVFLQRRYWSNYMDLEQKLFDETCCEHARDFAHRCVLHFFANMQSELRALGLRRDPAGGIPESQESSEPPELREDRDSGNGKAHLRAISSREQVDQLLSTWYSSKPPLDLAASPRRWGPGLNHRAPIAAPGTKLCHQLNV
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Pore-forming subunit of a voltage-gated ion channel, also permeable to larger molecules including ATP. Together with CALHM1, forms a fast-activating voltage-gated ATP-release channel in type II taste bud cells (TBCs). CALHM1-CALHM3-mediated ATP released acts as a neurotransmitter to gustatory neurons in response to GPCR-mediated tastes, including sweet, bitter and umami substances.
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J3QMK6
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AL3B3_MOUSE
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Aldehyde dehydrogenase family 3 member B3 (EC 1.2.1.3)
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MSTKGKHPRADQGTDPFEEKLQRLKEAFNTGKTKTAKFRAEQLQSLGRFLQDNSKQLHDALDGDLGKSGFESDMSEIILCENEVDLALKNLQTWMKDEPVSTNLLTKLSTAFIRKEPFGLVLIIAPWNYPVNLMIIPLVGAIAAGNCVVLKPSEISKNTEKVLAELLPQYLDQSCFAVMLGGPEETGQLLEHKFDYIFFTGSPRVGKIVMTAAAKHLTPITLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVAPDYILCSQEMQEQLVPALQNAITRFYGDNPQTSPNLGRIINQKHFKRLQGLLGCGRVAIGGQSDEGERYIAPTVLVDVQETEPVMQEEIFGPILPLVTVRSLDEAIEFMNQREKPLALYAYSNNAEVIKQVLARTSSGGFCGNDGFMYMTLSSLPFGGVGSSGMGRYHGKFSFDTFSNQRACLLSCPGMEKLNGLRYPPYSPRRQQLLRWAIGSESCTLL
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Oxidizes medium and long chain aldehydes into non-toxic fatty acids.
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J3QMY9
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TO6BL_MOUSE
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Type 2 DNA topoisomerase 6 subunit B-like (TOP6B like initiator of meiotic double strand breaks) (Type 2 DNA topoisomerase VI subunit B-like) (TOPOVIBL)
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MERTALAVCEILRYLIIHWKCEAGTAKGTLLDGQLVISIEALRSKHLPDSLHCIITIASTRSVYGGLNFKKFLQEIQPALPRLSAKLALASEEGGRSQDASGIAPCQVTFEVDENSQSLMTDCLVIKHFLRKIIIVHHKLKFSFSVAVNGTLSAETFGAENEPTLRLDNGVTLVVGFQRYVSKPKLNWSEAHCSRIHPVLGHPAPLFIPDAKADTGLLGELTLTPAAALCPSPKGFSSQLCRISSVSIFLYGPLGLPLLSSDQDQPSTAVFRDTSYFIDWKKYNLFMVPNLDLNLDTQSVLPDVNYKAESPEGNQSQNMNAQGPALLLFLFVDFQSDVPVQQAKIWGLHTLLTAHLSAILSESRSTVQQSIQSAVDQVWQLYHHDAKTQQRLQASLSVAVNSIMSVLTGSTRSSFRKTCLQALEAADTQEFGVKLHRIFYDITQHQFLKHCSCDTEQHLTPEKNISAQNTKDQHKNIAQEFPEESIGQAENKRPKRGSPNHGREESRVLGSARDRSPPKSATRDRELTEVSLTARGSQTQAAHGRAQAAEAASPAGGLEDLWLQEVSNLSEWLNPGHRS
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Component of a topoisomerase 6 complex specifically required for meiotic recombination. Together with SPO11, mediates DNA cleavage that forms the double-strand breaks (DSB) that initiate meiotic recombination. The complex promotes relaxation of negative and positive supercoiled DNA and DNA decatenation through cleavage and ligation cycles.
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J3QPC3
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ACTMP_MOUSE
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Actin maturation protease (EC 3.4.11.-) (Actin aminopeptidase ACTMAP)
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MTSPCSFPLKPTISPIIHETPDTNIPPPLPLNPPDLALPSPPCSLHTSISSPLPPPPPPPAPPPPPPPPPLPSAVEPVLPHVYGLKNSQLLKEALEKAGPAPKGKEDVKRLLKLHKDRFRSDLQWILFCADLPSCIQEGPQCGLVALWMAEALLSTPDSVSLERLVQVAKERGYTAQGEMFSVADMAKLAQETLDCQAELLCGGLGGPNRERVLQHLITGHPLLIPYDEDFNHEPCQKKGHKAHWAVSAGVLIGVQNVPSPGYIEDSELPGLFHPVPGAPHQPPSFPEESSPGALFLLSKQGKSWHYQLWDYSQVRESNLQLTDFSPARAADGQVYVVPAGGVEAGLCGQALLLRPQEGSH
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Actin maturation protease that specifically mediates the cleavage of immature acetylated N-terminal actin, thereby contributing to actin maturation. Cleaves N-terminal acetylated methionine of immature cytoplasmic beta- and gamma-actins Actb and Actg1 after translation. Cleaves N-terminal acetylated cysteine of muscle alpha-actins Acta1, Actc1 and Acta2 after canonical removal of N-terminal methionine.
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J3S6Y1
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TSEAR_MOUSE
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Thrombospondin-type laminin G domain and EAR repeat-containing protein (TSP-EAR)
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MSALLMLCAVLLLLGTPSRGARPWEPCTDLRPLDILAEVVPLNGATSGIRMVQVEGVRGLQFSATEPRTTSFPASRIFSSCDFFPEEFSIIVTLRVPNLPPKKNEYLLSLLAEERDTLLLGLRYSPTQLHFLFLSEDLAGAWQTRVSFWSPGLMDSRWHTLILAVSQGSFSLTTDCGLPVDIMADVSFPPTLSVRGARFFIGSRKRTKGLFTGVIRQLVLLPGSDATPQLCPSRNARLAELSIPQVLKRLTGKPDDNEVLNYPYEADMKVTLGSRPPCTKAEGAQFWFDAAQKGLYLCAGSEWVSVLAAKTKLDYVEEHQSLHTNSETLGIEVFSIPGVGLFAAAANRKARSAIYKWTDGKFVSYQNIATHQAQSWRHFTIGKKIFLAVANFGPNERGQEFSVIYKWSPRKLKFTLYQRIATHSARDWEAFEVDGEHFLVVANHREGDNHNIDSMVYRWNPSSQLFEANQSIATSGAYDWEFFTVGPYSFLVVANTFNGTSTQVHSHLYIWLVGAFQLFQSFLTFGAADWEVFHIGERIFLAVANSHSYDVQMQAQNDSYVLSSVIYELNITAQTFVKFQDIPTCSALDWEFFSVGEDHFLVVANSFDGNTFSVNSIIYRWQGYEGFVAVHKLPTFGCRDWEAFNTTAGSYLIYSSAKEPLSRVLKLRTG
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Plays a critical role in tooth and hair follicle morphogenesis through regulation of the Notch signaling pathway. May play a role in development or function of the auditory system.
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J3TRD1
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L_HTRV
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RNA-directed RNA polymerase L (Protein L) (EC 2.7.7.48) (Large structural protein) (Replicase) (Transcriptase) [Includes: cap-snatching endonuclease (EC 3.1.-.-)]
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MNLEALCSRVLSERGLSTGEPGVYDQIFERPGLPNLEVTVDSTGVVVDVGAIPDSASQLGSSINAGVLTIPLSEAYKINHDFTFSGLTKTTDRKLSEVFPLVHDGSDSMTPDVIHTRLDGTVVVIEFTTTRSTNMGGLEAAYRSKLEKYRDPLNRRTDIMPDASIYFGIIVVSASGVLTNMPLTQDEAEELMFRFCVANEIYSQARAMDAEVELQKSEEEYEAISRARAFFTLFDYDDGKLSEAFPNSDIEMLRRFLSQPVDTSFVTTTLKEKEQEAYKRMCEEHYLKSGMSTKERLEANRSDAIDKTRALMERLHNMSSKELHSNKSTVKLPPWVVKPSDRTLDVKTDTGSGELLNHGPYGELWSRCFLEIVLGNVEGVISSPEKELEIAISDDPEADTPKAAKIKYHRFRPELSLESKHEFSLQGIEGKRWKHSARNVLKDEMSHKTMSPFVDVSNIEEFLIMNNLLNDTSFNREGLQETINLLLEKATEMHQNGLSTALNDSFKRNFNTNVVQWSMWVSCLAQELASALKQHCKPGEFIIKKLMHWPIFVIIKPTKSSSHIFYSLAIKKANIKRRLIGDVFTDTIDAGEWEFSEFKSLKTCKLTNLINLPCTMLNSIAFWREKMGVAPWISRKACSELREQVAITFLMSLEDKSTTEELVTLTRYSQMEGFVSPPLLPKPQKMVEKLEVPLRTKLQVFLFRRHLDAIVRVAASPFPIVARDGRVEWTGTFNAITGRSTGLENMVNNWYIGYYKNKEESTELNALGEMYKKIVEIEAEKPTSSEYLGWGDTSSPKRHEFSRSFLKSACISLEKEIEMRHGKSWKQSLEERVLKELGSKNLLDLATMKATSNFSKEWEAFSEVRTKEYHRSKLLEKMAELIEHGLMWYVDAAGHAWKAVLDDKCMRICLFKKNQHGGLREIYVTNANARLVQFGVETMARCVCELSPHETIANPRLKSSIIENHGLKSARQLGQGTINVNSSNDAKKWSQGHYTTKLAMVLCWFMPAKFHRFIWAGISMFRCKKMMMDLRFLEKLSTKANQKTDDDFRKDLAGAFHGNVEVPWMTQGATYLQTETGMMQGILHFTSSLLHSCVQSFYKAYFLSRLKEGIAGRTIKAAIDVLEGSDDSAIMISLKPASDNEEAMARFLTANLLYSVRVINPLFGIYSSEKSTVNTLFCVEYNSEFHFHKHLVRPTIRWVAASHQISESEALASRQEDYANLLTQCLEGGSSFSLTYLIQCAQLVHHYMLLGLCLHPLFGTFVGMLIEDPDPALGFFIMDNPAFAGGAGFRFNLWRSCKFTNLGKKYAFFFNEIQGKTKGDADYRALDATTGGTLSHSVMTYWGDRRKYQHLLDRMGLPKDWVERIDENPSILYRRPENKQELILRLAEKVHSPGVTSSFSKGHVVPRVVAAGVYLLSRHCFRYTASIHGRGASQKASLIKLLVMSSTSAERNQGRLNPNQERMLFPQVQEYERVLTLLDEVTALTGKFVVRERNIVKSRVELFQEPVDLRCKAENLIAEMWFGLKRTKLGPRLLKEEWDKLRASFSWLSTDHKETLDVGPFLSHVQFRNFIAHVDAKSRSVRLLGAPVKKSGGVTTVSQVVKSNFFPGFILDSSESLDDQERVEGVSILKHILFMTLNGPYTDEQKKAMVLETFQYFALPHAAEVVKRSRSLTLCLMKNFIEQRGGSILDQIEKAQSGTVGGFSKPQKPYRKQSGGIGYKGKGVWSGIMENTNVQILIDGDGSSNWIEEIRLSSESRLFDVIESVRRLCDDINVNNRVTSSFRGHCMVRLSNFKVKPASRVEGCPVRLMPSSFRIKELQNPDEVFLRVRGDILNLSILLQEDRVMNLLSYRARDTDISESAASYLWMNRTDFSFGKKEPSCSWMCLKTLDSWAWNQAARVLERNIKTPGIDNTAMGNIFKDCLESSLRKQGLLRSRIAEMVERHVIPLTSQELVDILEEDVDFSEMMQSDIMEGDLDIDILMEGSPMLWAAEVEEMGEAMVILSQSGKYYHLKLMDQAATTLSTILGKDGCRLLLGRPTGRSNLREQVKPYLTLLQIREGDVNWVSEYKDDTRGLDEDSAEMWG
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RNA-dependent RNA polymerase, which is responsible for the replication and transcription of the viral RNA genome using antigenomic RNA as an intermediate (By similarity). During transcription, synthesizes subgenomic RNAs and assures their capping by a cap-snatching mechanism, which involves the endonuclease activity cleaving the host capped pre-mRNAs. These short capped RNAs are then used as primers for viral transcription. The 3'-end of subgenomic mRNAs molecules are not polyadenylated. During replication, the polymerase binds the 5' and 3' vRNA extremities at distinct sites (By similarity). In turn, significant conformational changes occur in the polymerase and in vRNA to initiate active RNA synthesis (By similarity). As a consequence of the use of the same enzyme for both transcription and replication, these mechanisms need to be well coordinated (By similarity).
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J3WAX0
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GP_HTRV
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Envelopment polyprotein (M polyprotein) [Cleaved into: Glycoprotein N (Gn) (Glycoprotein G1); Glycoprotein C (Gc) (Glycoprotein G2)]
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MIVPIVLFLTLCPSELSAWGSPGDPIVCGVRTETNKSIQIEWKEGRSEKLCQIDRLGHVTSWLRNHSSFQGLIGQVKGRPSVSYFPEGASYPRWSGLLSPCDAEWLGLIAVSKAGDTDMIVPGPTYKGKIFVERPTYNGYKGWGCADGKSLSHSGTYCETDSSVSSGLIQGDRVLWVGEVVCQRGTPVPEDVFSELVSLSQSEFPDVCKIDGVALNQCEQESIPQPLDVAWIDVGRSHKVLMREHKTKWVQESSAKDFVCFKVGQGPCSKQEEDDCMSKGNCHGDEVFCRMAGCSARMQDNQEGCRCELLQKPGEIIVNYGGVSVRPTCYGFSRMMATLEVHKPDRELTGCTGCHLECIEGGVKIVTLTSELRSATVCASHFCASAKGGSKTTDILFHTGALVGPNSIRITGQLLDGSKFSFDGHCIFPDGCMALDCTFCKEFLRNPQCYPVKKWLFLVVVIMCCYCALMLLTNILRAIGVWGTWVFAPIKLALALGLRLAKLSKKGLVAVVTRGQMIVNDELHQVRVERGEQNEGRQGYGPRGPIRHWLYSPALILILTTSICSGCDELVHAESKSITCKSASGNEKECSVTGRALLPAVNPGQEACLHFSVPGSPDSKCLKIKVKSINLRCKQASSYYVPEAKARCTSVRRCRWAGDCQSGCPTYFSSNSFSDDWANRMDRAGLGMSGCSDGCGGAACGCFNAAPSCIFWRKWVENPSNRVWKVSPCASWVLAATIELTLPSGEVKTLEPVTGQATQMFKGVAITYLGSSIEIVGMTRLCEMKEMGTGIMALAPCNDPGHAIMGNVGEIQCSSIESAKHIRSDGCIWNADLVGIELRVDDAVCFSKLTSVEAVANFSKIPATISGVRFDQGNHGESRIYGSPLDITRVSGEFSVSFRGMRLKLSEISASCTGEITNVSGCYSCMTGASVSIKLHSSKNTTGHLKCDSDETAFSVMEGTHTYRPHMSFDKAVIDEECVLNCGGHSSKLLLKGSLVFMDVPRFVDGSYVQTYHSKVPAGGRVPNPVDWLNALFGDGITRWILGIIGVLLACVMLFVVVVAITRRLIKGLTQRAKVA
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[Glycoprotein N]: Structural component of the virion that interacts with glycoprotein C (By similarity). It shields the hydrophobic fusion loops of the glycoprotein C, preventing premature fusion (By similarity). The glycoprotein protrusions are arranged on an icosahedral lattice, with T=12 triangulation (By similarity). They are able to attach the virion to the host cell receptor CD209/DC-SIGN and to promote fusion of membranes with the late endosome after endocytosis of the virion (Probable). Plays a role in the packaging of ribonucleoproteins during virus assembly (By similarity). [Glycoprotein C]: Structural component of the virion that interacts with glycoprotein N (By similarity). Acts as a class II fusion protein that is activated upon acidification and subsequent repositioning of the glycoprotein N. The glycoprotein protrusions are arranged on an icosahedral lattice, with T=12 triangulation (By similarity). They are able to attach the virion to the host cell receptor CD209/DC-SIGN and to promote fusion of membranes with the late endosome after endocytosis of the virion (Probable).
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J4KMC1
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TENS_BEAB2
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Tenellin synthetase (TENS) (EC 2.3.1.-) (EC 6.3.2.-) (Hybrid PKS-NRPS synthetase tenS) (Tenellin biosynthesis protein S)
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MSPMKQNESESHSVSEPIAIVGSAYRFPGGCNTPSKLWDLLQQPRDILKELDPERLNLRRYYHPDGETHGSTDVSNKAYTLEEDISRFDASFFGISPLEAASMDPQQRTLLEVVYESTETAGIPLDKLRGSLTSVHVGVMTTDWAQVQRRDPETMPQYTATGIASSIISNRISYIFDLKGASETIDTACSSSLVALHNAARALQSGDCEKAIVAGVNLILDPDPFIYESKLHMLSPDARSRMWDAAANGYARGEGAAAVVLKTLGHALRDGDRIEGVIRSTFVNSDGLSSGLTMPSSAAQTALIRQTYRKAGLDPVRDRPQFFECHGTGTRAGDPVEARAISDAFLPSHRTNGGGAATTVDDPLYVGSIKTVVGHLEGCAGLAGLVKVLLSLKHGIIPPNLWFDKLNPEIARYYGPLQIPTKAIPWPELAPGTPLRASVNSFGFGGTNAHAIIERYDASQSYCSQWRRDMTEEKTIARTQNNDDVEIPVPLVLTAKTGGALWRTVDAYAQHLRQHPKLRVANLSQFMHSRRSTHRVRASFSGASREELVENMANFVQAHAADAKSPASQNRIGYSPLLIDPKEVSGILGIFTGQGAQWPAMGRDMMHQSPLFRKTIADCESVLQALPLKDAPAWSLSEELKKDASTSRLGEAEISQPLCTAVQLALVNVLTASGVYFDAVVGHSSGEIAATYASGIINLKAAMQIAYYRGLYAKLARGQSDEAGGMMAAGLSMDDAVKLCRLPEFEGRIQVAASNAPQSVTLSGDKEAIKAAKAKLDADGVFARELKVDTAYHSHHMLPCAEPYLKALLACDIQVSAPTKTPGRKCMWSSSVRGDAELLRRDRNLDSLKGPYWVANMVQTVQFSRAIQSTIWHGGPFDLAVEVGPHPALKGPTEQTLKAVYGSAPLYTGVLSRGANDAVAFSTAIGNIWSHLGPAFVDITGYQSIFSGTCEGHGGSEAPFISDLPLYPWDHDEEYWRESRISRRYRTGKDESHELLGRRMPDDNEREIRWRNLLKVSELPWTQGHRVLGEVLLPGAAYISMAIEAGRRLALDQGREVSLLEVSDVDILRPVVVADNKEGTETLFTVRLLDEYASTGKKSDELMTASFSFYIYNSPASTSIVHTCEGRIAVHLGAKLGSEAAANSTPQLPPREPSVSNLQQLDCEKLYSVFETIGLEYSGAFRRIVSSSRCLGHATATASWPTADLNDCYLVHPAILDVAFQTIFVARAHPDSGQLSSALLPSRIERVRVVPSLAMGSKLQNNENFNAAIDSWALNQTASSLTGNINVYDADSERALIQVEGFEVRAVGEPDASKDRLLFYETVWGRDISIMGLSDPIRDETSDAMVQNLSEAIERVSLFYVRQLMGELSTADRRQANWYHTRMLAAFDHHLAKVHEETHLHLRPEWLADDWTVIQTIDEAYPDAVELQMLHAVGQNVADVIRGKKHLLEVLRVDNLLDRLYTEDKGMHMANLFLANALKEITFKFPRCKILEIGAGTGATTWAALSAIGEAFDTYTYTDLSVGFFENAVERFSAFRHRMVFRALDIEKDPASQSFDLNSYDIIIATNVLHATRNLGVTLGNVRSLLKPGGYLLLNEKTGPDSLRATFNFGGLEGWWLAEEKERQLSPLMSPDGWDAQLQKAQFSGVDHIVHDVQEDQQDKQQNSMIMSQAVDDTFYARLSPLSEMANLLPMNEPLLIIGGQTTATLKMIKEIQKLLPRQWRHKVRLIASVNHLEAEGVPAHSNVICLQELDRGLFTTAMTSKCLDALKTLFINTRNLLWVTNAQHSSSMTPRASMFRGITRVLDGEIPHIRTQVLGIEPRATSSATARNLLEAFLRLRSDDGRHAANVDEDGADGSSQQVLWLHEPEAELLSNGTMMIPRVKARKSLNDTYLASTRAISTTVDARCVSVQAVAGPAKMLLRPVEDFAVEHAISSQSTDSKVHIQVESTLHIPEALDGTCLYLVCGWTRTAETSVPVIALSTSNASIVAVESKAVAMIDEADVKPETLFRVFQHMAMQALDSAVGRHGQGQSTALIYGADEELAKLTSERFAVRESKVYFASTRTSAPGDWLKVQPLLSKFALSQMMPADVEVFIDCLGDTESFDACRTLESCLSTTSTVHRLDACLLSRMSQCSPDTLADAYSHAKTQSNAEFSWNGNVQTFTAAELAGKLSHSLMHSVYMTDWQEKDSILVTVPPLQTRGLFKSDRTYLMVGAAGGLGTSICRWMVRNGARHVVVTSRNPKADPEMLNEARRYGAAVKVVPMDACSKDCVQTVVDMIRDTMPPIAGVCNAAMVLRDKLFLDMNVDHMNNVLGPKMQGTEHLDSIFAQEPLDFFVLLSSSAAILNNTGQSNYHCANLYMDSLVTNRRSRGLAASIIHVGHVCDTGYVARLVDDSKVQMSLGTTRVMSVSETDVHHAFAEAVRGGQPDSRSGSHNIIMGIEPPTKPLDVAKRKPVWISDPRLGHMLPFSTLENQMVASEQAAASAADSLAQQVSEATTDEEAAAAALKGFATKLEGILLLPLGSIGEDSAGRPVTDLGIDSLVAVEIRTWFLKQLRVDVPVMKILGGSTVGQLSALAAKLARQDAKKRAQLEEASGNQPVALPPLNDKETGPSKKGKAQEFPETVQVVGTAAERTEPLVLEASDRGGSSTANFTTSSSVSELDDSLQESTLQSSENNGESTPSKSSNCNSDSGSDNQAPREISSNGFFTQPAATARPNVLREAPMSPAQSRIWFLSKHIAEPDAYNMVFHYRVRGPLSMVRLRHALQTVTNHHECLCMCFYASADNGQPMQGLLASSASQMTIVPGGEEQDLQRELRKLKTRVWSVESGQTLELVVVGPRPGTAAAEEEEFSLLFGYHHIVMDAISFSIFLADLDKAYRMLPLDKASAGSHLDLAAHQRQQEHAGAWKESLEFWQAEFETIPEMLPPLSVALPTLQRGAVGTHRVLRELAHEQGGDAAIKKTCKNLRVSPFNLHIAVLQVVIARLGSIEDVCVGIVDANRSDSRASRMVGCFVNMLPVRSRILPSATLADVARAASSKALAAFAHGQVPLDSILDKVKAPRPAGSTPLFQVALNYRPAAAIASKQSLGGECEMELLADDFKDAENPFEISVLVSEMPGGRIAVEVVCQKSRYTMQATEALLDAYLNVLAGFLSDTAQSVGDCVVHDQSKVEHALDLGKGAQKSFGWPRTLSERVMSICQQHSTKSAIKDGRNELSYAQLASKVNHTASALVNAGCSVGSRIAVLCNPSIDAIVAMLAILHIGGVYVPLDTSLPEARHQSLASNCTPSLIISHAATRERAHKLSAVISAPGHEPARELTLDDLSPDETGYMAPLNAEPNAPAILLYTSGSTGTPKGVLLTQANFGNHIALKTDILGLQRGECVLQQSSLGFDMSLVQVFCALANGGCLVIVPQDVRRDPMELTSLMAQHKVSLTIATPSEYLAWLQYGSDALAQATSWKHLCMGGEPIPQLLKDELRRRLERKDLVVVSNCYGPTETTAAISFQSIALDSQDSHEQLPGESELANYAVGKALPNYSIRIRDPAGGAWLPVNHTGEIVIGGAGVALGYLDMPEETRARFLQTPGEEDGMLLYRTGDKGRLLSDGTLLCFGRITGDNQVKLRGLRIELGEVEAALLQASQGLIHTAVVSRRGDVLVAHCARSHESSRETTGGGGEQQDAATAILRRVSELLPQYSVPAAIALLPSLPTNANGKLDRTAIAALPLSPQDEAAAATSPSNDNNNNNTPSGGGGEKMTVRQGELRLLWERVLPRDATTTTTTNSVRITPESDFFLRGGNSLLLMKLQAAIRESMGVRVSTKALYQASTLSGMARCVAEQRSDDDEAEEDIDWAAEVAVPPSMLAQIEKLQHSSASSSSSSSSSSAGSSSTQRPRKTSGLQILLTGATGFLGGQLLERLVQSPRVSTVHCVAVPVDEQSLLEPFLQQQADGTRRKVRCYIGNLAAPALGLTAADQTALSQTADVIVHAGSMGHCLNTYATLSAPNFASTRHLCALALSRSPPIPLAFASSNRVALLTGSTAPPPGSAAAFPPPPGAQGFTASKWASEAFLEKLTASMSDVSKTKTKTTTTVMPWRVSIHRPCALISDRAPNSDALNAILRYSTSMRCVPSLPEHRAEGYLDFGQVDKVVEEMVGDILGLADERPQEGPAVVYRHHSGGVKVPIHEFREHMESVYGGRFESVQLGQWIIRAVDAGMDPLISAYLETFLEGDASMVFPYMGEQAV
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Hybrid PKS-NRPS synthetase part of the gene cluster that mediates the biosynthesis of tenellin-type 2-pyridones, iron-chelating compounds involved in iron stress tolerance, competition with the natural competitor fungus Metarhizium robertsii and insect hosts infection. TenS catalyzes the assembly of the polyketide-amino acid backbone. Because tenS lacks a designated enoylreductase (ER) domain, the required activity is provided the enoyl reductase tenC. Upon formation of the polyketide backbone on the thiotemplate, the triketide is transferred to the NRPS module and linked to tyrosine to produce the pyrrolidine-2-dione intermediates, including pretellinin A, 11-hydropretellenin A, 12-hydropretellenin A, 13-hydropretellenin A, 14-hydropretellenin A, 12-oxopretellenin A and prototellinin D. The pathway begins with the assembly of the polyketide-amino acid backbone by the hybrid PKS-NRPS tenS with the help of the enoyl reductase tenC. These enzymes catalyze the synthesis of the pyrrolidine-2-dione intermediates pretellinin A, 11-hydropretellenin A, 12-hydropretellenin A, 13-hydropretellenin A, 14-hydropretellenin A, 12-oxopretellenin A and prototellinin D. The cytochrome P450 monooxygenase tenA then catalyzes an oxidative ring expansion of pretenellin A and 14-hydropretellenin A to form the 2-pyridone core, leading to pretenellin B and pyridovericin, respectively. The cytochrome P450 monooxygenase tenB is then required for the selective N-hydroxylation of the 2-pyridone nitrogen of yield tellinin and 15-hydroxytellenin (15-HT), respectively. The UDP-glucosyltransferase GT1 and the methyltransferase MT1, located outside the tenS gene cluster, contribute to the stepwise glycosylation and methylation of 15-HT to obtain the glycoside pyridovericin-N-O-(4-O-methyl-beta-D-glucopyranoside) (PMGP). Additional related compounds such as 1-O-methyl-15-HT, (8Z)-1-O-methyl-15-HT, and O-methyltenellin A are also produced but the enzymes involved in their biosynthesis have still to be determined.
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J4W0G2
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ATG1_BEAB2
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Serine/threonine-protein kinase ATG1 (EC 2.7.11.1) (Autophagy-related protein 1)
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MTSRQEGASSHGSRRSSRHVGSFIIDREIGKGSFAQVYMGWHKESKAAVAIKSVELERLNKKLKENLYGEIQILKTLRHPHIVALHDCVESSTHINLIMEYCELGDLSLFIKKRDKLITHPATHDMARKYPSAPNSGLHEVVIRHFLKQLSSALEFLRAKNYVHRDVKPQNLLLLPSQAFREERALPIMEASQDSLIPISGLASLPMLKLADFGFARVLPSTSLADTLCGSPLYMAPEILRYERYDAKADLWSVGTVLYEMITGRPPFRARNHVELLRKIEAAEDVIKFPREVSVTPDLKALVRSLLKRSPVERLSFENFFAHHVVTGDILGLVEDDIPKPPKRELETIRQGEALPSSPRVQMARQLSSDPRDTRSSPKSPRSSPRSSTVNSSADAAPRRQSQNAERRLSISSHNSGQGLGIQRPAPPIQSHTAPNHPRAADRSGREPQPSSLRVARQPSDVSLTEEEKAAQDVMFERDYVVVERRHVEVNALADELAANEKLGQNNSSAKSSPLQRRYTQQGSATSTTGAIPTPASRTALVAQGRAGQDRRSSYEKALSASPGSASSAISKAIQDASLRLFGYKVNTMRQKGSSPPLYQPFPAYPTPTSAGLLSDGKGSQVSDEDAKAAQAIEEFATRSDCVYGFAEVKYKQLLPMAPSMDYGLGGVSPDKGTSEEDGLTVDATVALSEEALVLYVKSLTLLARAMDIASLWWSKKTRAESSVVSQTLVQRINAVVQWVRQRFNEVLEKSEVVRLKLTEAQKLLPEDHPSNPAHQGEDSIASSAVGAKQVYLTPGISAEKLMYDRALEMSRAAAIDEVTNENLPGCEISYLTAIRMLEAVLDSDDEATARNISSGKEIAKDATQEGSDLDTEEAAHVRKMITMITGRLNMVRKKQQMIAEANNQAKHVSAMRRLSGDVTPRSVPSYGST
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Serine/threonine protein kinase involved in the cytoplasm to vacuole transport (Cvt) and found to be essential in autophagy, where it is required for the formation of autophagosomes. Involved in the clearance of protein aggregates which cannot be efficiently cleared by the proteasome (By similarity). Required for selective autophagic degradation of the nucleus (nucleophagy) as well as for mitophagy which contributes to regulate mitochondrial quantity and quality by eliminating the mitochondria to a basal level to fulfill cellular energy requirements and preventing excess ROS production (By similarity). Also involved in endoplasmic reticulum-specific autophagic process, in selective removal of ER-associated degradation (ERAD) substrates (By similarity). Plays a key role in ATG9 and ATG23 cycling through the pre-autophagosomal structure and is necessary to promote ATG18 binding to ATG9 through phosphorylation of ATG9. Catalyzes phosphorylation of ATG4, decreasing the interaction between ATG4 and ATG8 and impairing deconjugation of PE-conjugated forms of ATG8 (By similarity). Contributes to conidiation by regulating the conidial levels of the conidiation-related protein CP15 and mediates fungal oxidation resistance by controlling total superoxide dismutase (SOD) activity.
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J5JV76
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BSLS_BEAB2
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Bassianolide nonribosomal cyclodepsipeptide synthetase (BSLS) [Includes: Nonribosomal peptide synthetase (EC 6.1.2.-); S-adenosyl-L-methionine-dependent N-methyltransferase (EC 2.1.1.-)]
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MEPPNNANTGQLGPTLPNGTVDLPTDLSREITRHFGLEQDEIEEILPCTPFQRDVIECASDDKRRAVGHVVYEIPEDVDTERLAAAWKATVRYTPALRTCIFTSETGNAFQVVLRDCFIFARMYCPSAHLKSAIVKDEATAAVAGPRCNRYVLTGEPNSKRRVLVWTFSHSFVDSAFQGRILQQVLAAYKDEHGRVFSLQPTTDLVESENGDCLSTPASERTVGIERATQFWQEKLHGLDASVFPHLPSHKRVPAIDARADHYLPCPPFIQHEWSSTTVCRTALAILLARYTHSSEALFGVVTEQSHEEHPLLLDGPTSTVVPFRVLCAPNQSVSEVMEAITTYDHDMRQFAHAGLCNISRIGDDASAACGFQTVLMVTDSRTASADEIHHVLEEPEKFIPCTDRALLLSCQMTDEGVLLVARYDQSILEPLQMARFLRQLGFLINKLQSTDGSPCVGQLDVLAPEDRTEIEGWNSEPLQTQDCLIHSEVVKNADDTPNKPAVCAWDGEWTYSELNNVSSRLASYISSLDLGQQLIVPIYLEKSKWVMAAILAVLKAGHAFTLIDPNDPPARTAQIIKQASASIALTSALHQSKMQTVVGRCITVDDDLFQTLTTFEGSQVASAAKPGDLAYVIFTSGSTGDPKGIMIEHRAFYSSVVKFGKALGIRSSTRALQFATHGFGAFLLEVLTTLIHGGCICIPSDHDRMHNIPGFIRQSQINWMMATPSYMTTMKPEDVPGLETLVLVGEQMSSSINDVWLSELQLLDGYGQSESSSICFVGKISDSSRDPNNLGRAIGSHSWIVNPDNPDQLVPIGAIGELLIESPGIARGYLFSQSTETPFLERAPAWYASKQPPYGVKFYRTGDLARYAPDGTVICLGRMDSQVKIRGQRVELDAIENLLRRQFPSDVTVVAEAVKRSDLPSSVVITGFLISSEYVVGAPSTEDTYILDQAVTQEINAKMRQILPAHSIPSFYICMKSLPRTATGKVDRRKLRSIGSSLLALQAQSTAPRSSQAPDASAGVTKLEEVWMDIFNLTPNSHNIGGNFFALGGDSITAIKMVNMARAAGIQLKVSDIFQNPTLASLQAAIGGSSMTVTSIPALALDGPVEQSYSQGRLWFLDQLEIGANWYTIPYAVRLRGPLDVDALNRALLALEKRHETLRTTFEDQDGVGVQIIHETLLDQLRIINADHADYVQLLKQEQTAPFNLASESGWRVSLIRLDDDDNILSIVMHHIISDGWSIDVLRRELGQLYAAALHGADLFGSALSPLPIQYRDFSVWQKQDAQVAEHERQLQYWQKQLADCSPAKLPTDFHRPALLSGKATTVPVTITSELYYRLQEFCSTFNTTSFVVLLATFRAAHYRLTGVDDAVIGTPIANRNRHELENLIGFFVNTQCMRITINEDEETFESLVRQVRSTTTAAFEHEDVPFERVVSAMLPGSRDLSQNPLAQLVFAIHSHKDLGKFELEALESEPLQNEVYTRFDAEFHFFQAPDGLTGYINFATELFKVETIQNVVSVFLQILRHGLEHPQTLISVVPLTDGLAELRSMGLLEIKKVEYPRDSSVVDVFATQVASYPDTLAVVDSSSRLTYAELDHQSDLLATWLRQQNLPTEALVVVLAPRSCETIITFLGILKANLAYLPLDIRSPITRMRDVLSTLPGRTIALLCSDEVAPDFQLPSIELVRIADALEEAAGMTSLNGHEHVPVPSPSPTSLAYVLYTSGSTGRPKGVMIEHRAIVRLARSDIIPDYRPACGDTMAHMFNTAFDGATYEIYTMLLNGGTLVCVDYMDTLSPKSLEAVFKKEQVNATIMAPALLKLYLADARDALKGLDVLISGGDRFDPQDAVDAQSLVRGSCYNGYGPTENGVFSTVYKVDKNDPFVNGVPLGRAVNNSGAYVVDRNQQLVGPGIIGELVVTGDGLARGYTERAFDQNRFIQLKIEGQSVRGYRTGDRVRYRVGEGLIEFFGRMDFQFKIRSNRIEAGEVEAAILSHPAVRNAAVILHVQEKLEPEIVGFVVAEHDDTAEQEEAGDQVEGWQAFFESTTYTELDTVSSSEIGKDFKGWTSMYDGNEIDKAEMQEWLDDTIHTLTDGQALGHVLEIGTGSGMVLFNLGSGLQSFVGLEPSKSAAAFVNNAIKSTPALAGKAHVFVGTATDTNKLDDLHPDLVIFNSVLQYFPTRDYLEQVVDALVHLRSAKRIFFGDVRSYATNRHFLAARAIYTLGNHTTKDEVRKKMAEMEEREEEFLVEPAFFTTLVNRLPDVRHVEIIPKNMQATNELSAYRYAAVVHLRGPDELTRPVHLIKMDDWVDFQASHMHKDALREYLRLAENTKTVAISNIPYGKTIFERQVVESLDDTSEDAPHASLDGAAWISAVRSDAKARSSLSVPDLVLLAKETGFRVEVSAARQWSQSGALDAVFHRYHPAEPDVRTLFQFPTDNDVRMSALLTNQPLQRLQKRRVAVQVREWLQDRIPSYMIPSHIVALDQMPLNTSGKVDRKELSRQAKAIKKVQKSAPPTAPAFPLSEVEVMLCEELTKTFEMDVNITDDFFQLGGHSLLATRLVARISHRLGARLTVKDVFDYPVFSELADIIRQQLASKNTLLPTASAGGGGQDKKESAGVAPTTDMEAMLCEEFANILGMDVGITDNFFDLGGHSLMATRLAARIGHRLNTTISVKDIFSHPVIFQLSAKLEVSQLESSSGGTDIKMPDYTAFQLIPAADAEKFMQDHIYPQINFSQDMVQDVYLATHLQQCFLRDVFGRPKPLVPFYVEFPPDSNPHTLATACTSLVDKYDIFRTIFVEAEGNLYQVVLKHLNLDIDVVETDANVHKTSSDLVDAIAKEPVRLGQPMIQVKVLKQTSSVRVLLWLSHALYDGLSWEHIVRDLHILSKERSLPPATQFSRYMQYVDHTRGPGCDFWRDVLQNAPITNLSDAGSGGRPTKAGDPRVWHAGKVISGPSQAIRSSITQATVFNAACAIVLSKETGTDNVVFGRIVSGRQGLPVRWQNIIGPCTNAVPVRAVVDAHGNHQQMLRDLQEQYLLSLPYETIGFDEIKRSCTDWPDSARNYGCCVTYQNFEYHPESEVDQQRVEMGILAKKAELIKEEPLYNVAIAGEVEPDGVHLQVTVVVDSQLFSQEGATHLMEQVCNTFQALNASL
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Bassianolide nonribosomal synthetase that mediates the biosynthesis of bassianolide (BSL), a non-ribosomal cyclodepsipeptide that shows insecticidal and cancer cell antiproliferative activity. BSLS first catalyzes the iterative synthesis of an enzyme-bound dipeptidol monomer intermediate from D-2-hydroxyisovalerate and L-leucine before performing the condensation and cyclization of 4 dipeptidol monomers to yield the cyclic tetrameric ester bassianolide. The N-methyltransferase MT domain is responsible for the methylation of the leucine residues of bassianolide. BSLS is flexible with both the amino acid and hydroxyl acid precursors, and produces bassianolide as the major product (containing N-methyl-L-Leu), together with small amounts of beauvericin and its analogs beauvericins A-C (containing N-methyl-L-Phe).
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J7FIX8
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IDTG_CLAPA
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Geranylgeranyl pyrophosphate synthase idtG (GGPP synthase) (GGPPSase) (EC 2.5.1.-) ((2E,6E)-farnesyl diphosphate synthase) (Dimethylallyltranstransferase) (EC 2.5.1.1) (Farnesyl diphosphate synthase) (Farnesyltranstransferase) (EC 2.5.1.29) (Geranylgeranyl diphosphate synthase) (Geranyltranstransferase) (EC 2.5.1.10) (Indole-diterpene biosynthesis cluster protein G)
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MAPSPIMPRYHVGPMASTRRAISKKGFPRTRSFPVLTAPLDYLRDSPGKDIRSGLTDAFNEFLCVPEDKVVTIKRIIDLLHNASLLIDDIQDDSKLRRGVPVAHSIFGIAQTINSANLAYFLAQQELKKLSNPDAFAIYTDELINLHRGQGMELHWRESLHCPTEEEYMRMVQNKTGGLFRLAIRLLQGESRSDRDYVPLVDTLGTLFQIRDDYQNLQSDVYSKNKGFCEDISEGKFSYPVIHSIRARPGDLRLLNILKQRSEDLMVKQYAVSYINSTGSFEFCRGKIDCLAQWANLQLAALEEAEGAGRGDKLRAVLRLLDMKASGKQADVAS
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Geranylgeranyl pyrophosphate synthase part of the gene cluster that mediates the biosynthesis of paspalitrems, indole-diterpene (IDT) mycotoxins that are potent tremorgens in mammals. The geranylgeranyl diphosphate (GGPP) synthase idtG is proposed to catalyze the first step in IDT biosynthesis via catalysis of a series of iterative condensations of isopentenyl diphosphate (IPP) with dimethylallyl diphosphate (DMAPP), geranyl diphosphate (GPP), and farnesyl diphosphate (FPP), to form GGPP (Probable). Condensation of indole-3-glycerol phosphate with GGPP by the prenyltransferase idtC then forms 3-geranylgeranylindole (3-GGI) (Probable). Epoxidation of the two terminal alkenes of the geranylgeranyl moiety by the FAD-dependent monooxygenase idtM, and cyclization by the terpene cyclase idtB then leads to the production of paspaline (Probable). The cytochrome P450 monooxygenase idtP then catalyzes oxidative elimination of the pendant methyl group at C-12 of paspaline and generates the C-10 ketone to yield 13-desoxypaxilline. The cytochrome P450 monooxygenase idtQ may catalyze the C-13 oxidation of 13-desoxypaxilline to afford paxilline (Probable). Considering that both paspalicine and paxilline were detected in C.paspali, idtQ also catalyzes the formation of paspalinine from 13-desoxypaxilline via paspalicine as an intermediate (Probable). Finally, the alpha-prenyltransferase idtF prenylates paspalinine at the C-20 or the C-21 positions to yield paspalitrems A and C, respectively. The hydroxylation of paspalitrem A at C-32 by a still unknown oxidase affords paspalitrem B (Probable).
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J7GQ11
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TYRDC_LEVBR
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L-tyrosine decarboxylase (TDC) (EC 4.1.1.25)
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MEKSNRSLKDLDLNALFIGDKAENGQLYKDLLNKLVDEHLGWRKNYIPSDPNMIGPEDQNSPAFKKTVGHMKTVLDQLSERIRTESVPWHSAGRYWGHMNSETLMPALLAYNYAMLWNGNNVAYESSPATSQMEEEVGQEFARLMGYDYGWGHIVADGSLANLEGLWYARNIKSLPFAMKEVNPELVAGKSDWELLNMPTKEIMDLLENAGSQIDEVKKRSARSGKNLQRLGKWLVPQTKHYSWMKAADIIGIGLDQVVPVPIDSNYRMDIQALESIIRKYAAEKTPILGVVGVAGSTEEGAVDGIDKIVALRQKLQKEGIYFYLHVDAAYGGYARALFLDEDDQFIPYKNLQKVHAENHVFTEDKEYIKPEVYAAYKAFDQAESITIDPHKMGYVPYSAGGIVIQDIRMRDTISYFATYVFEKGADIPALLGAYILEGSKAGATAASVWAAHHTLPLNVTGYGKLEGASIEGAHRYYDFLKNLKFEVAGKRISVHPLISPDFNMVDYVLKEDGNDDLIEMNRLNHAFYEQASYVKGSLYGKEYIVSHTDFAIPDYGDSPLAFVESLGFSEVEWRHAGKVTIIRASVMTPYMNQRENFDYFAPRIKKAIQADLEKVYASVNQKENV
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Catalyzes the decarboxylation of L-tyrosine to produce tyramine. Cannot use other aromatic L-amino acids as substrates like L-phenylalanine, L-tryptophan and L-glutamate.
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J7H670
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OXLA_LACMT
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L-amino acid oxidase Lm29 (LmLAAO) (LAO) (EC 1.4.3.2)
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MNVFFMFSLLFLAALGSCADDRNPLGECFRETDYEEFLEIAKNGLRATSNPKHVVIVGAGMSGLSAAYVLAEAGHQVTVLEASERAGGRVRTYRNDKEGWYANLGPMRLPEKHRIVREYIRKFGLQLNEFHQENDNAWHFIKNIRKRVGEVKEDPGLLQYPVKPSEEGKSAGQLYEESLGKVAEELKRTNCSYILNKYDTYSTKEYLLKEGNLSPGAVDMIGDLLNEDSGYYVSFIESLKHDDIFGYEKRFDEIVDGMDKLPTSMYQAIKEKVRFNARVIKIQQNDREVTVTYQTSANEMSPVTADYVIVCTTSRATRRITFEPPLPPKKAHALRSVHYRSGTKIFLTCTKKFWEDDGIRGGKSTTDLPSRFIYYPNHNFTSGVGVIIAYGIGDDANFFQALDFKDCGDIVINDLSLIHQLPKKDIQTFCYPSMIQRWSLDKYAMGGITTFTPYQFQHFSEALTAPFKRIYFAGEYTAQFHGWIDSTIKSGLTAARDVNRASENPSGIHLSNDNEL
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Catalyzes an oxidative deamination of predominantly hydrophobic and aromatic L-amino acids, thus producing hydrogen peroxide that may contribute to the diverse toxic effects of this enzyme. Is highly active on L-Met=L-Leu>>L-Phe>L-Trp>L-Tyr>L-Ile, and weakly or not active on L-His, L-Arg, L-Val, L-Gln, L-Thr, L-Lys, and L-Ser. Exhibits a low myotoxicity (a mild myonecrosis is observed after injection in mice quadriceps muscle). In vitro, is cytotoxic to a lot of human cell lines, including AGS (IC(50)=22.7 ug/ml), MCF-7 (IC(50)=1.4 ug/ml), HL-60, HeLa and Jurkat cells, as well as to the parasite Leishmania brasiliensis (IC(50)=2.22 ug/ml). This cytotoxicity is dependent on the production of hydrogen peroxyde, since it is inhibited by catalase, a hydrogen peroxyde scavenger.
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J7I4B7
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WBDD_ECOLX
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O-antigen chain terminator bifunctional methyltransferase/kinase WbdD [Includes: 3-O-phospho-polymannosyl GlcNAc-diphospho-ditrans,octacis-undecaprenol 3-phospho-methyltransferase (EC 2.1.1.294); Polymannosyl GlcNAc-diphospho-ditrans,octacis-undecaprenol kinase (EC 2.7.1.181)]
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MTKDLNTLVSELPEIYQTIFGHPEWDGDAARDCNQRLDLITEQYDNLSRALGRPLNVLDLGCAQGFFSLSLASKGATIVGIDFQQENINVCRALAEENPDFAAEFRVGRIEEVIAALEEGEFDLAIGLSVFHHIVHLHGIDEVKRLLSRLADVTQAVILELAVKEEPFYWGVSQPDDPRELIEQCAFYRLIGEFDTHLSPVPRPMYLVSNHRVLINDFNQPFQHWQNQPYAGAGLAHKRSRRYFFGEDYVCKFFYYDMPHGILTAEESQRNKYELHNEIKFLTQPPAGFDAPAVLAHGENAQSGWLVMEKLPGRLLSDMLAAGEEIDREKILGSLLRSLAALEKQGFWHDDVRPWNVMVDARQHARLIDFGSIVTTPQDCSWPTNLVQSFFVFVNELFAENKSWNGFWRSAPVHPFNLPQPWSNWLYAVWQEPVERWNFVLLLALFEKKAKLPSAEQQRGATEQWIIAQETVLLELQSRVRNESAGSEALRGQIHTLEQQMAQLQSAQDAFVEKAQQQVEVSHELTWLGENMEQLAALLQTAQAHAQADVQPELPPETAELLQRLEAANREIHHLSNENQQLRQEIEKIHRSRSWRMTKGYRYLGLQIHLLRQYGFVQRCKHFIKRVLRFVFSFMRKHPQVKHTAVNGLHKLGLYQPAYRLYRRMNPLPHSQYQADAQILSQTELQVMHPELLPPEVYEIYLKLTKNK
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Regulates the length of the LPS O-antigen polysaccharide chain. Stops the polymerization of the chain by phosphorylating and then methylating the phosphate on the terminal sugar. This terminal modification is essential for export of the O-antigen across the inner membrane. WbdD is also required for correct localization of the WbdA mannosyltransferase.
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J7QLC0
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CYAA_BORP1
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Bifunctional hemolysin/adenylate cyclase (AC-HLY) (ACT) (Cyclolysin) [Cleaved into: Calmodulin-sensitive adenylate cyclase (EC 4.6.1.1) (ATP pyrophosphate-lyase) (Adenylyl cyclase); Hemolysin]
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MQQSHQAGYANAADRESGIPAAVLDGIKAVAKEKNATLMFRLVNPHSTSLIAEGVATKGLGVHAKSSDWGLQAGYIPVNPNLSKLFGRAPEVIARADNDVNSSLAHGHTAVDLTLSKERLDYLRQAGLVTGMADGVVASNHAGYEQFEFRVKETSDGRYAVQYRRKGGDDFEAVKVIGNAAGIPLTADIDMFAIMPHLSNFRDSARSSVTSGDSVTDYLARTRRAASEATGGLDRERIDLLWKIARAGARSAVGTEARRQFRYDGDMNIGVITDFELEVRNALNRRAHAVGAQDVVQHGTEQNNPFPEADEKIFVVSATGESQMLTRGQLKEYIGQQRGEGYVFYENRAYGVAGKSLFDDGLGAAPGVPSGRSKFSPDVLETVPASPGLRRPSLGAVERQDSGYDSLDGVGSRSFSLGEVSDMAAVEAAELEMTRQVLHAGARQDDAEPGVSGASAHWGQRALQGAQAVAAAQRLVHAIALMTQFGRAGSTNTPQEAASLSAAVFGLGEASSAVAETVSGFFRGSSRWAGGFGVAGGAMALGGGIAAAVGAGMSLTDDAPAGQKAAAGAEIALQLTGGTVELASSIALALAAARGVTSGLQVAGASAGAAAGALAAALSPMEIYGLVQQSHYADQLDKLAQESSAYGYEGDALLAQLYRDKTAAEGAVAGVSAVLSTVGAAVSIAAAASVVGAPVAVVTSLLTGALNGILRGVQQPIIEKLANDYARKIDELGGPQAYFEKNLQARHEQLANSDGLRKMLADLQAGWNASSVIGVQTTEISKSALELAAITGNADNLKSVDVFVDRFVQGERVAGQPVVLDVAAGGIDIASRKGERPALTFITPLAAPGEEQRRRTKTGKSEFTTFVEIVGKQDRWRIRDGAADTTIDLAKVVSQLVDANGVLKHSIKLDVIGGDGDDVVLANASRIHYDGGAGTNTVSYAALGRQDSITVSADGERFNVRKQLNNANVYREGVATQTTAYGKRTENVQYRHVELARVGQLVEVDTLEHVQHIIGGAGNDSITGNAHDNFLAGGSGDDRLDGGAGNDTLVGGEGQNTVIGGAGDDVFLQDLGVWSNQLDGGAGVDTVKYNVHQPSEERLERMGDTGIHADLQKGTVEKWPALNLFSVDHVKNIENLHGSRLNDRIAGDDQDNELWGHDGNDTIRGRGGDDILRGGLGLDTLYGEDGNDIFLQDDETVSDDIDGGAGLDTVDYSAMIHPGRIVAPHEYGFGIEADLSREWVRKASALGVDYYDNVRNVENVIGTSMKDVLIGDAQANTLMGQGGDDTVRGGDGDDLLFGGDGNDMLYGDAGNDTLYGGLGDDTLEGGAGNDWFGQTQAREHDVLRGGDGVDTVDYSQTGAHAGIAAGRIGLGILADLGAGRVDKLGEAGSSAYDTVSGIENVVGTELADRITGDAQANVLRGAGGADVLAGGEGDDVLLGGDGDDQLSGDAGRDRLYGEAGDDWFFQDAANAGNLLDGGDGRDTVDFSGPGRGLDAGAKGVFLSLGKGFASLMDEPETSNVLRNIENAVGSARDDVLIGDAGANVLNGLAGNDVLSGGAGDDVLLGDEGSDLLSGDAGNDDLFGGQGDDTYLFGVGYGHDTIYESGGGHDTIRINAGADQLWFARQGNDLEIRILGTDDALTVHDWYRDADHRVEIIHAANQAVDQAGIEKLVEAMAQYPDPGAAAAAPPAARVPDTLMQSLAVNWR
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Bifunctional adenylate cyclase toxin-hemolysin that plays a crucial role in host colonization. It causes whooping cough by acting on mammalian cells by elevating cAMP-concentration and thus disrupts normal cell function. [Calmodulin-sensitive adenylate cyclase]: Adenylate cyclase that is activated by host intracellular calmodulin and catalyzes un-regulated conversion of ATP to cAMP, thereby impairing microbicidal functions of immune effector cells and inducing apoptosis of lung macrophages. [Hemolysin]: Hemolysin that forms small cation-selective membrane channels, leading to hemolytic activity. The hemolytic activity of CyaA is weak compared with that of the HlyA of E.coli.
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J7RUA5
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CAS9_STAAU
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CRISPR-associated endonuclease Cas9 (EC 3.1.-.-) (SaCas9)
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MKRNYILGLDIGITSVGYGIIDYETRDVIDAGVRLFKEANVENNEGRRSKRGARRLKRRRRHRIQRVKKLLFDYNLLTDHSELSGINPYEARVKGLSQKLSEEEFSAALLHLAKRRGVHNVNEVEEDTGNELSTKEQISRNSKALEEKYVAELQLERLKKDGEVRGSINRFKTSDYVKEAKQLLKVQKAYHQLDQSFIDTYIDLLETRRTYYEGPGEGSPFGWKDIKEWYEMLMGHCTYFPEELRSVKYAYNADLYNALNDLNNLVITRDENEKLEYYEKFQIIENVFKQKKKPTLKQIAKEILVNEEDIKGYRVTSTGKPEFTNLKVYHDIKDITARKEIIENAELLDQIAKILTIYQSSEDIQEELTNLNSELTQEEIEQISNLKGYTGTHNLSLKAINLILDELWHTNDNQIAIFNRLKLVPKKVDLSQQKEIPTTLVDDFILSPVVKRSFIQSIKVINAIIKKYGLPNDIIIELAREKNSKDAQKMINEMQKRNRQTNERIEEIIRTTGKENAKYLIEKIKLHDMQEGKCLYSLEAIPLEDLLNNPFNYEVDHIIPRSVSFDNSFNNKVLVKQEENSKKGNRTPFQYLSSSDSKISYETFKKHILNLAKGKGRISKTKKEYLLEERDINRFSVQKDFINRNLVDTRYATRGLMNLLRSYFRVNNLDVKVKSINGGFTSFLRRKWKFKKERNKGYKHHAEDALIIANADFIFKEWKKLDKAKKVMENQMFEEKQAESMPEIETEQEYKEIFITPHQIKHIKDFKDYKYSHRVDKKPNRELINDTLYSTRKDDKGNTLIVNNLNGLYDKDNDKLKKLINKSPEKLLMYHHDPQTYQKLKLIMEQYGDEKNPLYKYYEETGNYLTKYSKKDNGPVIKKIKYYGNKLNAHLDITDDYPNSRNKVVKLSLKPYRFDVYLDNGVYKFVTVKNLDVIKKENYYEVNSKCYEEAKKLKKISNQAEFIASFYNNDLIKINGELYRVIGVNNDLLNRIEVNMIDITYREYLENMNDKRPPRIIKTIASKTQSIKKYSTDILGNLYEVKSKKHPQIIKKG
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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). In type II CRISPR systems correct processing of pre-crRNA requires a trans-encoded small RNA (tracrRNA), endogenous ribonuclease 3 (rnc) and this protein. The tracrRNA serves as a guide for ribonuclease 3-aided processing of pre-crRNA. Subsequently Cas9/crRNA/tracrRNA endonucleolytically cleaves linear or circular dsDNA target complementary to the spacer Cas9 is inactive in the absence of the 2 guide RNAs (gRNA). Cas9 recognizes the protospacer adjacent motif (PAM) in the CRISPR repeat sequences to help distinguish self versus nonself, as targets within the bacterial CRISPR locus do not have PAMs. PAM recognition is also required for catalytic activity. {ECO:0000255|HAMAP-Rule:MF_01480, ECO:0000269|PubMed:25830891, ECO:0000269|PubMed:26098369}.
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J7SHB8
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FLDH_CLOS1
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Aromatic 2-oxoacid reductase (EC 1.1.1.110) (Indolelactate dehydrogenase)
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MKILAYCVRPDEIDSFKNFSEKYGHTVDLIPDSFGPNVAHLAKGYDGISILGNDTCNREALEKIKDCGIKYLATRTAGVNNIDFDAAKEFGINVANVPAYSPNSVSEFTVGLALSLTRKIPFALKRVELNNFALGGLIGVELRNLTLGVIGTGRIGLKVIEGFSGFGMKKMIGYDIFENEKAKEYIEYKSLDEVYKEADIITLHAPLTDDNYHMIGKESIAKMKDGVFIINAARGALIDSEALIEGLKSGKIAGAALDSYEYEQGVFHNNKMNEIMKDDTLERLKSFPNVVITPHLGFYTDEAVSNMVEITLMNLQEFELKGTCKNQRVCK
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Essential for the reductive metabolism of L-phenylalanine, L-tyrosine and L-tryptophan. Catalyzes the conversion of phenylpyruvic acid to phenyllactic acid, 4-hydroxy-phenylpyruvic acid to 4-hydroxy-phenyllactic acid, and indolepyruvic acid to indolelactic acid.
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J8G6Z1
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THSA_BACCS
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NAD(+) hydrolase ThsA (BcThsA) (NADase ThsA) (EC 3.2.2.5) (Thoeris protein ThsA)
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MKMNPIVELFIKDFTKEVMEENAAIFAGAGLSMSVGYVSWAKLLEPIAQEIGLDVNKENDLVSLAQYYCNENQGNRGRINQIILDEFSRKVDLTENHKILARLPIHTYWTTNYDRLIEKALEEENKIADVKYTVKQLATTKVKRDAVVYKMHGDVEHPSEAVLIKDDYEKYSIKMDPYIKALSGDLVSKTFLFVGFSFTDPNLDYILSRVRSAYERDQRRHYCLIKKEERRPDELEADFEYRVRKQELFISDLSRFNIKTIVLNNYNEITEILQRIENNIKTKTVFLSGSAVEYNHWETEHAEQFIHQLSKELIRKDFNIVSGFGLGVGSFVINGVLEELYMNQGTIDDDRLILRPFPQGKKGEEQWDKYRRDMITRTGVSIFLYGNKIDKGQVVKAKGVQSEFNISFEQNNYVVPVGATGYIAKDLWNKVNEEFETYYPGADARMKKLFGELNNEALSIEELINTIIEFVEILSN
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NAD(+) hydrolyzing component (NADase) of the Thoeris antiviral defense system, composed of ThsA and ThsB. Activated by a signal molecule generated by endogenous ThsB (AC J8G8J6) or ThsB' (AC J8CSK2, probably 3'cADPR), by TIR1 and TIR2 from B.dafuensis or by BdTIR from B.distachyon (AC I1GTC2, probably 2'cADPR). Upon activation binds and hydrolyzes NAD(+), leading to cell death and inhibition of phage replication. Not seen to bind DNA. Activation is 50-100x more sensitive to 3' cyclic ADP-D-ribose (3'cADPR) than 2'cADPR. In another paper ThsA is not activated by any tested cADPR isomer, although it binds 3'cADPR it was suggested the protein is already in a fully active state. Expression of ThsA and ThsB in B.subtilis (strain BEST7003) confers resistance to phages phi29, SBSphiC, SBSphiJ and SPO1. At multiplicity of infection (MOI) of 0.05 Thoeris-encoding cultures grow normally when infected with SPO1, at MOI 5 cultures collapse prematurely by 90 minutes post-infection, thus the phage are not able to complete a replication cycle. NAD(+) levels fall and ADP-D-ribose levels rise 60 minutes post-infection. Thoeris cultures eventually recover, but retain the same susceptibility to SPO1.
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J8H9C1
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GAJA_BACC6
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Endonuclease GajA (EC 3.1.-.-) (Gabija protein GajA) (Nicking endonuclease GajA)
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MKFSNITIKNFRNFEKVNINLDNKNVIFGMNDIGKTNFLYALRFLLDKEIRKFGFNKSDYHKHDTSKKIEIILTLDLSNYEKDEDTKKLISVVKGARTSANADVFYIALESKYDDKELYGNIILKWGSELDNLIDIPGRGNINALDNVFKVIYINPLVDLDKLFAQNKKYIFEESQGNESDEGILNNIKSLTDQVNQQIGEMTIIKGFQQEITSEYRSLKKEEVSIELKSEMAIKGFFSDIIPYIKKDGDSNYYPTSGDGRRKMLSYSIYNYLAKKKYEDKIVIYLIEEPEISLHRSMQIALSKQLFEQSTYKYFFLSTHSPELLYEMDNTRLIRVHSTEKVVCSSHMYNVEEAYGSVKKKLNKALSSALFAERVLLIEGPSEKILFEKVLDEVEPEYELNGGFLLEVGGTYFNHYVCTLNDLGITHIIKTDNDLKSKKGKKGVYELLGLNRCLNLLGRENLDEITIDIPEDIKGKKKKERLNERKKEIFKQYKNEVGEFLGERIYLSEIDLENDLYSAIGESMKRIFENEDPVHYLQKSKLFNMVELVNNLSTKDCFDVFEHEKFACLKELVGSDRG
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Component of antiviral defense system Gabija type I, composed of GajA and GajB. Expression of Gabija type I in B.subtilis (strain BEST7003) confers resistance to phages phi105, phi29, rho14, SpBeta and SBSphiC. An endonuclease that nicks double-stranded DNA within the sequence 5'-TNNNCGGGNNA-3' in the absence of nucleotides (NTP, dNTP and NDPs), cleaving after C-1. Has no detected ATPase activity. Expression of Gabija type I in E.coli B (strain ATCC 11303) confers resistance to phage T7. It is thought that this enzyme is strongly suppressed during physiological growth (in E.coli total nucleotide concentration is over 8.7 mM in mid-log phase), but during viral replication, when nucleotides are rapidly consumed, it is de-suppressed and degrades target DNA (Probable).
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J9VE33
|
CRZ1_CRYNH
|
Transcriptional regulator CRZ1
|
MADPASPPSFDAIFAQQPVRRSSSTSTSSFANYTYSALQQHQQFNSDAPLVDEPQSLSEQARKQQRDPSKDGNNKRYLDMMSGLADGYGVINGRRQESLRKESLPFNPQEDSTLIATAPKRGERNGLGRNGYSSPIGDIMFGPEQTIPNQPQQPSQQPPWGEGRMSEQSVHYASVQQPQYSSFQSSGPGAGSAGIDYLPRGTTSSMNDSMLSSQISPYLNHDVASEGQPPQQQQQQQQQQQGEWGQEFIGVEQQQQYAQGEGQSNGMEDMLTMGDESPFESELQRVISNTSHPSQYPSRTSSPFPQQSQSNMVPASTVNQTRTESFPASRSPSPFAPQQASQTEASNHVVSTPSMGQPTYPRASSSPRTNPNSPFFNKPQSPPALIIPNSPVLPNIVTQSTSNNHSKGLNQPHTRHASNGAGGLFPPSNPALEHLTGMAGISPIAPNADGPMICIQPSTPISGLKEGRGLFDAALRRAGAARGAQRQGPQGQGESQEDRRQDGFNVPSPQSHPLPRTLSSDQVNQGVEMQGMDFAAQMQSYEQQGWANDTLRIAGPSRPRAKSDSIIPSPTADSFDRQAFLAFIGAGNAQPPPPNVEMQPGYVDVSEQWRNTVSAWKAGLGEGELNSQPTLDPRLLPGRESNEAVYQQLLMQQQTGQMPRLDPDQLHQLTQLEGQRARFSLNTNIAPPKYEPGEISPTSMVFYQSMGLYPHAAPELSGTVSAPWSQTAFGQVPGPGPVGHPATAGPAQQHFLTPTLSHATVRRRSFGGGEHPAMGAGTPGYGMEFSSPFAGKSVGQIRGVNMGHRRAARSEDFGRGGTGWGVGAGGSTAEFLQSITGDDGSLLPPSNRGHAMSHSRHSSTSSIRSASPALSISSQGSSFSHHSPRMDMPDSIYPGHPIIAPATPLQVSGLYEEQQTPARVAKMKVTSVATEVASTSRRTNSGIFKCPVPGCGSTFTRHFNLKGHLRSHNDERPFKCLYEGCPKAIVGFARQHDCKRHMLLHEGLRLFECEGCGKKFARLDALTRHHKSEQGQECAITHPLPTNFDGSPMSESQYKTYKGIKSTPEGSGRRLSSTASGSGSGKRRSKKSETSEED
|
DNA-binding transcriptional activator that interacts with calcineurin-dependent response element (CDRE) promoters. Activates expression of genes required to maintain cell wall integrity during stress. Activates expression of genes required for transepithelial migration through the host blood-brain barrier. Required for adaptation to host temperature during infection.
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J9VHN6
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BIM1_CRYNH
|
Copper acquisition factor BIM1 (BCS-inducible membrane protein 1) (Lytic polysaccharide monooxygenase-like protein BIM1) (LPMO-like protein BIM1) (EC 1.14.99.-)
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MFALKSILVTSLITSTALAHFTLDYPQSRGFVDDTENQFCGGFNTVEARQPFPLGSGPVHIDSHHALATIVAFISTSSNPTSFDDFNTTSNGTAIPLASSIFQVPQGEKCFNIDLQSLNVGLTNGSEVTLQIQYDGGDGNLYQCSDLVLIEGYEVPSNETCTNDASKASNATSTSSGSATATSAAATSSSSGTSGAIKEVVGFGALSLALGIAGLIIL
|
Cell surface-bound protein that functions in the copper-accumulation pathway shared by the CUF1-dependent copper transporter CTR1. Binds Cu(2+) with an estimated 1:1 stoichiometry and might serve as an extracellular copper ligand. FRE4 and FRE7 metalloreductases probably function together with CTR1 and BIM1 to liberate the Cu(2+) bound to the BIM1 copper-binding site for subsequent import of Cu(+) into the cell by CTR1, via the reduction of BIM1-bound Cu(2+) to Cu(+) to reduce binding affinity for BIM1 but increase affinity for CTR1 (Probable). Facilitates copper acquisition in the brain of mammalian hosts and acts as a copper-dependent virulence trait in fungal meningitis. While BIM1 plays a critical role in cryptococcal meningitis, at least in part through its role in copper acquisition, it could play additional roles during copper limitation or as a means to invade and colonize host tissues in the brain, by compromising host carbohydrate integrity via its lytic polysaccharide monooxygenase (LPMO) activity, which has still to be determined (Probable).
|
J9VI03
|
DMT5_CRYNH
|
DNA (cytosine-5-)-methyltransferase DMT5 (EC 3.6.4.-)
|
MTTALTFGGGLFKDNTKFDIDMRGTADGAVNGGNIPNSQSQKRKRASPSPEIESEEDGDDWYEIDYIADSRVIRRKGRQILQYLIHWAGYAVHERTWEDEDGIGGEDCALVQEFYRKNPGKPRLSPSSVRKEVKLARMVEVVITTRRIDGKSRAASSTDQPSPHRLGITSPQANNIGGEDPNPSLTRRPVRSTVSEIAKRPTSKKVHPNKKCKASSDDESDFVFEEGEWDEDEDDDNDVDFRSSEDDEDDEQERSAEEPESDEEIIKPAKKTKSSLPKAKLRPKPANLGGFVTGVRPLNQGLDIKAAVRNMSDDLPPISDIEAMFDHLVSRIPDIVELVRQLNGRKLRVATMCSGTESPLLALNMIAKAIKAQHGLTLAFEHVFSCEIEPFKQAYIERNFTPPILFRDVTELGKKRAHTAYGSMVDVPGDVDILIAGTSCVDYSNLNNVQQDIDANGESGRTFRGMLQWVKKHQPPIVILENVCNAPWDKVVEYFGQIDYDAQYTRLDTKEFYIPHTRTRVYLFATPSSSESDDLPEKWAQTVKDLRRPWSSPFEAFLLHTDDPNIHRARLELASARAQTDGTSRKTTDWNRCESRHQRARQDEALGLLRPLTSWQEAGVCKGLDWTWNDWLLAQTERVVDLLEISTLRMAKDGIDSGFKACIWNVSQNVDRQTGSSKTALAPCLTPNMIPWVTIRGGPVTGREALALQGIPVRELLLTSENEDQLADLAGNAMTTTVVGSAMIAALKVACHKITEGANPEKEAALILEKEAVDDEQVANRIIGEDYLEHHDLDLAKVTKSNLSEILDLACRSSRHCQCEGQSGTAPNILECQECSYRACKSCGGRPEHVYAPCANQRVEPAEFEKRFKGLLPMRVRIAGLTDQCLNAVRKAAEKSNKGSVNDNDWQLWSTALLEGIHDAEFRFRYLKRQSTWTAVYEARRAMLSLVLRNQIPEWRLTIKAPASEPNNSQLRALLLHPVARLQIDIAGQDVLCGPWELCIPSMKTIDIEITGKGELLPSWQASLGLQGPFANTTRWSEVEISLQAEDENTLDRKLSGTYQLLPRCGQAMSSLHKKRPDLSDDGLPQLYFFLDPTRCGESREDRYVFSTSTERLDYGTERPVIARLDSHWREGNEKQRKVKLDVSGAWVKCPEAHLTAIGGDDIAVVANDAAANEIHRDRATFAIPSSASAISASLTTEGCSHAMALLSCRVPLDPTHSESMWRRGAWAEIDLSHQGNTTFANLAWITERLPPLDGLKNWAHIADDVSEHVCERCAPRPPKIHWIKREGKANKKGNKTKSTIIAFEDKLEAGQYEHALKHRPSPFVVQLRLDQDIGSFRIGLNIVSLAHRALSRLPPTTSEHKISLSWRLTPGHVTESPQPRRVFILPSNKQDPENSQPEAFKLPLRKEQLRSLWWMLEQEKATGKTHTFVEEEISESLLPAVGWRAEGKAERPVMVRGGVIADQVGYGKTVISIALVAQTLSLPAPEPATPGLIDLKATLIVVPGHLSKQWPNEIARFTGSMFKVIVIQGMKDLQEKTIAELGKADIIVMASEIFESDVYWSRLEYLSAQPREWLHDTQGGRFFCDRLDAAMESLVSQTKILKEKGSEAAMRAMEDKKKSLVDNVGSKKEVHTAVNFGKRMKGQAYRDKHDSDSKAKPITKEELERWEASEDEDDDENSKTYIPIPKFHSFTGSESIFSASVKKDYKLLPNPVLHMFRFRRVIADEFTYLQKKSLAAVLRLSSSYRWILSGTPPVSDFAAIRSIATFMGIHLGVEDDGEGDVQYQKARAKDQTQAEKFHAFREVHSRAWHNRRDELAQEFLNVFVRQNIAEIEDIPTVEHIHTFKLPASEGAVYLELEHHLQALEMQARKETKFKNVSQGDRNARLEEALSDSKTAEEALLKRCCHFTLDLSDKTQDAKSAQEACDHITSARARQLLACQEDLSRSVNQAIALHGWIKKKGGFSKNDDERQPFAEWIAFSSNISKHQGDIEAARILLKVIEKCGVKDGNIPPSPSDKQSPSIASGAKMDDVKWQLREQTHLLRKLVKELVARVRSLRFFEVVRKIQKGKSDAQIVLESSECGHKPSTNPDIEMAILSCCGHVACHKCMRKAAASQRCVKSGECQAAVRPTNIVKVSSLGVEGELSSGRYGAKLEHLVNLIHSIPKNERVLVFLQWEDLAGKVSEALSAGRIPHVTLSGSAKSRANTLDRFQSTNADSARVLLLKMNDASAAGSNLTTANHAVFLGPLFTNSLFNYRAVETQAIGRVRRYGQQKKVHIHRLLALDTIDMTIFNARRTELKEKTDWEEIPQEEYKGRGSSISMTNEKRTPTLTVKSNPFKRSSSWALASSFRSKKRSMEARDAEGVSDDDENSELSDII
|
ATP-dependent cytosine methylase that maintains DNA methylation by acting at hemimethylated palindromic 5'-CG-3' sites to produce symmetrically methylated DNA strands. DNA methylation may play a role in transcriptional silencing, particularly at transposable elements.
|
J9VJ99
|
PFA4_CRYNH
|
Palmitoyltransferase PFA4 (EC 2.3.1.225) (Protein S-acyltransferase) (PAT) (Protein fatty acyltransferase 4)
|
MAARNWSRVWVGGTVILISFIAFSSQIFVIWPWYGREISLDLLMLLVPLNLAAFMIFWNYRLCVITSPGTVPEGWRPNIGAMDGMEVKKGTHTPRYCKNCAHYKPPRAHHCRQCKTCWLKLDHHCPWIGNCVGFYNQGHFIRFLLWVDIGTTFHLIIMVRRVLYIAEYYHEPTLADVLFLVFNFATCVPVWLCVGMFSIYHVYLACGNSTTIEGWEKDKVATLIRRGKIKEVKYPYNIGIYKNIKSVLGPNPLLWLWPQKMQGDGLSFPVNPSAGDHMTQYFWPPQDPSRLPNPPPIPAHASPFVYGNNGFNPNLRPTNSLRARRSSTPRIDEDEYSHEQGRHYSSGDERDNGSISASSSPEPYLSDYDHYDEGPMYPGERMTTLVPRVRRGSEGWEVAPGGGWNAYAGMMDEEVGWDDEAGYDEAPGEDPYVERPWEMRGRYNVYDPEEESGYTH
|
Mediates the reversible addition of palmitate to target proteins, thereby regulating their membrane association and biological function. Responsible for the modification of a subset of proteins that are critical in cryptococcal pathogenesis, with substrates involved in cell wall synthesis, signal transduction, and membrane trafficking. Palmitoylates chitin synthase CHS3. {ECO:0000255|HAMAP-Rule:MF_03199, ECO:0000269|PubMed:25970403}.
|
J9VJP1
|
PUR9_CRYNH
|
Bifunctional purine biosynthesis protein ADE16 [Includes: Phosphoribosylaminoimidazolecarboxamide formyltransferase (EC 2.1.2.3) (5-aminoimidazole-4-carboxamide ribonucleotide formyltransferase) (AICAR transformylase); Inosine 5'-monophosphate cyclohydrolase (IMP cyclohydrolase) (EC 3.5.4.10) (ATIC) (IMP synthase) (Inosinicase)]
|
MSSEAPIALLSVYDKTGLLPFAKSLKELGFRLLGSGGTAKMIREAGMEIEDVSNITKAPEMLGGRVKTLHPAVHGGILSRDIPSDLADLATNKISPITLVVCNLYPFVLQTAKPDCTLAGAIEEIDIGGVTLLRAAAKNHGRVSIISSPSDYETIVAELRAKGEVSAETRRGLAIKAFEDTKSYDEAISDYFRKVYATPGVEEEMKAGAGVGYQRLGLRYGANPHQKPAQAFVEQGEMPIKVLSGSPGYINLLDALNSWALVKELAAGLDLPAAASFKHVSPAGAAVGLPLDERAAKVFGVEDLKELSPLACAYARARGADRMSSFGDFIALSHTVDTPTAKIISREVSDGVIAPGYEPEALEILSKKKGGKYCVLQMDPTYVPPEIETRQVYGISLQQKRNDCKIDESLFKNVVTANKDLPKSAVTDLVVATLALKYTQSNSVCYALNGTVIGLGAGQQSRIHCTRLAGDKADNWWLRHHPRVLELPFKKGTKRADKANAIDLFVTGQAFEAEGGERAQWESLFETVPEPLTKEEREKHMKELTGVACASDAFFPFPDNVHRAKRSGATYLAAPSGSIMDKECIKAADESNLVFCHTDLRLFHH
|
Bifunctional enzyme that catalyzes the last two steps of purine biosynthesis. Acts as a transformylase that incorporates a formyl group to the AMP analog AICAR (5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide) to produce the intermediate formyl-AICAR (FAICAR). Also catalyzes the cyclization of FAICAR to IMP.
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J9VLJ9
|
SODC_CRYNH
|
Superoxide dismutase [Cu-Zn] (EC 1.15.1.1) (CnSOD1)
|
MVKAVVVLKGESYVHGTVCFTQESENAPVCITGEIKDMDADAKRGMHVHEFGDNTNGCTSAGPHYNPFKKHHGAPTDSERHVGDLGNIQTNSCGAAQLDFSDKIISLYGPHSIIGRSLVVHASTDDLGKGGNEESLKTGNAGARLACGVIGIST
|
Destroys radicals which are normally produced within the cells and which are toxic to biological systems. Destroys radicals produced by host defense mechanisms.
|
J9VND2
|
CDA2_CRYNH
|
Chitin deacetylase 2 (EC 3.5.1.41)
|
MIPSTAAALLTLTAGAAFAHTGCGGHEIGRRNVGGPMLYRRAVTDEASAAVSTDINTECTAYSYAPVTELISSFPTIWQTASIPSNDTEAQQLFGKINSTLNTKIPNDVPHGTPTGDWTGVNYSNSDPDCWWTHNKCTTPSNDTGLQADISIAPEPMTWGLGFDDGPNCSHNALYDLLLENNQKATMFFIGSNVLDWPLQAMRAHDEGHEICVHTWSHQYMTALSNEVVFAELYYTQKAIKAVLGVTPQCWRPPYGDVDNRVRMIAEGLNLTTIIWSDDTDDWAAGTNGVTEQDVTNNYQSVIDKAGNGTYTTHGPVVLNHELTNYTMSVFMTMFPKIKSAFNYIVPICTAYNITQPYAESNITCPNFETYISGVTNISSSTTQKDGSSSTNTASGSGAAGSASATSSSDDSSSSGGSSGSSGSNNASSGALGMFDSLSGVGLILGGVVAGVMLL
|
Hydrolyzes the N-acetamido groups of N-acetyl-D-glucosamine residues in chitin to form chitosan and acetate. Chitosan is required to anchor melanin to the cell wall, for maintenance of cell wall integrity, and for proper cytokinesis. Chitosan offers an advantage during infection as it is less readily detected than chitin by host immunosurveillance mechanisms.
|
J9VNT4
|
CHS5_CRYNH
|
Chitin synthase 5 (EC 2.4.1.16)
|
MAQQPPPSRFLGVTDLSSLAVTEDTVLVTLQERYISHKPYTSLSPAALVFLSPYSHLPIDDEESLLHYVEEYYQCNNEEGGSRNEQGWWKKKMEQPHVFQLALSAYYNMRRTGQDQVIIASGPTGSGKSELKRLAIEAITQVSLANPGKKGSKIGLQVSSAEFILKCFGNAHTLSNDEASRFGTYTELQFNERGRLEGLKTIVYYFERSRVSQAPINGERNFHAFYYLVSGAPEEERNFLKLGDVSDYRYLNCRVRRVGVDDRHRYSQLRQAFKLMGISSRLIAQIFQLLASILHIGNLRFSPSDGIQEGASVINVETLDIVAEFLGVHSESLAEIFSLKTVLVRKEVCTTFLGPEQAEQVRDELARTLYSLLFSWINEHINTKLCKDSFGSFIALVDLPGIQRNSGSMGSFNSVDQFCLNFAAEKMHNWVLHRVHETTRQEAETERLLISRVPYFDNSECLGMLSNPRGGLISVIDDLSQKKRSESNLLESLGKRFHNHPSMSISPQGNRSSASFTINHYDGPVTYSTSNFLERNANETSTDIIQLLRGDTTSRSQVSTTEGHGSSNPFIKGLFGMKNIAMQTHPRSDSTIVAAQQSVRPVRAPSTRRKKMMSLVPVSEEGGEETSDFQVGGGNDESYSSKELHCIAGQHWAAVDSLLKSFDQTQTWYIFALRPNDSQLPSQFDLRSMKQQVRSFGLVEMAQQLQTSWEVRLSHKEACERYNEELLYRGIPEGTGDVERLRDLKRLMSLNDADMGIGLQRVFLSHDLFRFLEDRLRAKEPGEQHAYEDLGHRKLQTDPFSPHRYQPTSFDSQDHVYKDPSIRPVDSSANLPLMEHAQPIVNSSLEIEDRESSAAPYVSYGGRSITDIEGYASSRDLLASSIHKSEKDPLDTEPQAGETTEVYRESIARRRWVWLCSILTWWIPGFLLSKIAGMKRQDIRQAWREKLAINMIIWFICGCAIFVIAILGPVICPTQHVYSTNELASHSYTLDPNNAFVAIRGEVFDLSQFAPTHLTAVSVVPTKSIMQYGGLDASELLPVQVSALCGGVSGSISQYVTLDSTNTTDVYSQYHDFRAFTNDSRPDWYAEMMIMMRHRFRVGFMGYTKKDLKKMAAQGKAVAIYDNLVYDMSNYIRQNGGGLKAPDGVNLTAQDQADRQFMSDQVVSLFKYNSGKDITTLLDNLGSTIGTDVVDRQKTCLRNLFILGKLDTRDSAQCQFSTYILLALSCVMVAVIGFKFLSALHFGSVRAPESHDKFVICQVPCYTEGEESLRRTIDSLCKLRYDDKRKLILVICDGNIKGFGNDKPTPAIVLDILGVDVNSDPEPLSFQSLGEGAKQHNMGKVYAGLYECAGHVVPYLVVAKVGKPNERQKPGNRGKRDSQMLVMHFLNKVHFSAPMNPLELEMYHQIKNVIGVNPSFYEYLFMVDADTTVDEMSLNRLVSAMRHDKKIIGVCGETSIANAKQSIVTMSQVYEYFISHHLSKAFESLFGSITCLPGCFSMYRLRSPDTNKPLFISHGIIQDYSENRVDTLHLKNLLHLGEDRYLTTLVLKHFQDYKTKFVRHAYAKTVAPDSIKVLLSQRRRWINSTVHNLAELVFLDQLCGFCCFSMRFVVFIDLLSTIIAPVTVAYIVYLIYLIVHDGSSIPTLSIIMLAAIYGLQAMIFIFRMRWDMIAWMIFYICAIPVFSFLLPLYSFWKMDDFSWGSTRLVVGDKGKKIVIHDEGKFDPSSIPLRSWEEYENELWDQESVHSGSYMPPKAEYSYDYPRTRSTYSHGGYAYGQPIHPMQTRSTSPVSSRYQMSQFRQSPYQSPYQGPYGGSTADFRSSRMDMAHRPSLDDTSSFHQPYQPAPRPQSSYAFNLPDPSSDSFTAPAVDYLGAQAITDSQLERSIRKICANAELDKLTKKGVRKELEREYGVELTERREAINRLVEKVLTE
|
Polymerizes chitin, a structural polymer of the cell wall and septum, by transferring the sugar moiety of UDP-GlcNAc to the non-reducing end of the growing chitin polymer. Produces a large proportion of the chitin that is not deacetylated to chitosan.
|
J9VPD7
|
CDA1_CRYNH
|
Chitin deacetylase 1 (EC 3.5.1.41)
|
MFTFAAFSALLISLAGVVAQTTGTSVDSSILTKTADSTGPSGFSIPALSELTSGAPTDSTVALYSTFAAGATPTVSGAPVLPTSALTIADYPALDVTPPTNSSLVKDWMAKIDLSKVPSYNVTTGDCSTDAAAISDGRCWWTCGGCTRETDIVECPDKNVWGLSYDDGPSPFTPLLIDYLQEKNIKTTFFVVGSRVLSRPEMLQTEYMSGHQISIHTWSHPALTTLTNEEIVAELGWTMKVIKDTLGVTPNTFRPPYGDIDDRVRAIAAQMGLTPVIWTSYTDGSTTVNFDTNDWHISGGTATGASSYETFEKILTEYAPKLDTGFITLEHDIYQQSVDLAVGYILPQVLANGTYQLKSIINCLGKDTSEAYIETSSNQTTTQITAATGSQSTFFQPIVGTATGAEVSAPSEATGSTAAGSAASTTSGSGASASTGAASNTSSSGSGRSATMGGALIALAAVAVGMVYVA
|
Hydrolyzes the N-acetamido groups of N-acetyl-D-glucosamine residues in chitin to form chitosan and acetate. Chitosan is required to anchor melanin to the cell wall, for maintenance of cell wall integrity, and for proper cytokinesis. Plays a major role in synthesizing cell wall chitosan during host infection chitosan offers an advantage during infection as it is less readily detected than chitin by host immunosurveillance mechanisms.
|
J9VWU3
|
ATM1_CRYNH
|
Iron-sulfur clusters transporter ATM1, mitochondrial (EC 7.-.-.-)
|
MGFGSCSRHALFTPAAFSGSFTTMTTSCFKRVYTAQIHGGDALGKRLPSVSSFSGQLPRHGLHRQSLAFFSTSHRRQTSPPPSPRTTSQSPTVPSKASTTPPTSLNTSKPIATESQDKTDWSIIVKLAGNIWPKNNPNVKFRVIGALTLLVAGKVLNVQVPFFFKTIVDSLNVPITESTTVWVLAGASIAGYGAARILTTLFGELRNAVFASVAQNAIRKVARETFEHLLNMDMKFHLERQTGGLTRAIDRGTKGISFILSSIVFHVIPTALEISMVCGILSWKFGWDFAAVTAITMLLYTWFTIKTTAWRTTFRKQANAADNKGATVAVDSLINYEAVKSFNNEKYEVAQYDTTLKAYEKASVKIATSLAALNSGQNFIFSSALTMMMLLGAQGIVKGTMTVGDLVLVNQLVFQLSLPLNFLGTVYRELRQSLIDMDVMFNLQSLNSAIKDTPTAKPLHLKGGEIEFRNVAFAYHPERPIFRDLSFKIPAGQKVAIVGPSGCGKSTVFRLLFRFYDSNSGQILIDGQDIKTVTLDSLRRSIGVVPQDTPLFHADILHNIRYGNLEATDEQVYEAARKAHVEGTIQRLPEKYATKVGERGLMISGGEKQRLAVARVLLKDPPVLFFDEATSALDVYTETELMRNINSILTGQGKTSVFIAHRLRTISDADLIIVLQDGYVAEQGTHEQLLAMPGGVYHRLWQAQLTESTQPTDEEIERQREELEVVDEKKKQ
|
Performs an essential function in the generation of cytoplasmic iron-sulfur proteins by mediating the ATP-dependent export of mitochondrial Fe/S cluster precursors synthesized by NFS1 and other mitochondrial proteins. Hydrolyzes ATP (By similarity). Binds glutathione and may function by transporting a glutathione-conjugated iron-sulfur compound (By similarity). Plays a role during copper stress, in a manner dependent on the copper metalloregulatory transcription factor CUF1.
|
J9VWW9
|
SODM_CRYNH
|
Superoxide dismutase [Mn], mitochondrial (EC 1.15.1.1)
|
MITAITRTALPRATLRTSLATMSTIRAKHTLPPLPYAYDALEPSISAEIMNLHHTKHHQTYVNGLNAAEESLQKASADGDFKTAISLQPALKFNGGGHINHSLFWKNLAPTGSAQVKVPTSGVFYDQVQADFGGFENLKKEMNAKTAAIQGSGWGWLGYNKATKKLEIVTTPNQDPLLSHVPIIGIDIWEHAFYLQYKNVKPDYLNAIWNVINYEEAESRLKAAQ
|
Destroys radicals which are normally produced within the cells and which are toxic to biological systems.
|
J9VXM5
|
CHS3_CRYNH
|
Chitin synthase 3 (EC 2.4.1.16) (Chitin-UDP acetyl-glucosaminyl transferase 3) (Class-IV chitin synthase 3)
|
MSRPHLQQNVSFQDTKPPSRRAGRDDIPPRPPTKSDPSKASLTTTTTVQSVGGYNNHQLDFDDNAYVDAGSSNPQGFSDYNGVRRKKSMVRPERERIDPNHRLWHYREHAAEDQVDIQPSSTGNQPYNQYNNQRPGANLRRGKSLLARETDDVDDSSGLNIFKRGATIRRKASRATPRQAPTGAQSNRVSAGQKEDEECCCLGNFAPGPKNCWMIYCYLLTICIPGFVIAKVFGKKTPDAQRAWREKIGIVSIVLYLMGAVGFITFGFTQTVCGDTQLRLPGGSANTGSLVINGYDYDFSTWRHPVAGDTFNGTTSPLYMDQYMAGGMDASFLFQNVNQNCLGLITPASGTGIDHDGDQMGWYFPCNLHDQNGTSAANLTGITDRTNCHVSSYARSNFSAVVPTAEIYYTWDRVKDESRNLAVYKSAVIDMNLLQWLDDTQVSYPEFFNTIKNRNDSYAGKDITALIERAGLSQYARCLTDVIQIGFVDTITIGCIMSELVLYVSLVFILGAVFIKFGMAVVFGWFLSWRMGNFKGESYQERMKRAAEIENWTDDIYRPAPGYLRPNATGTARTGVKKNFLPTTSRFSRAEPMLVSSSRPSTSYGMVGETRRQGSSIYGNKLGPPAHTTPPGSPLLRNSRSSTSLPFRDDSRHSISDRSVNNNVPCPFPLGNVVPQPAPDFEPFGYPLIHSICLVTAYSESIEGLRTTLDSLATTDYPNSHKLILVICDGMVRGSGSKQYTPEIVLGMMKELVTPAEEVEAHSYVAIADGHKRHNMAKVYAGFYAYDSETVEASKQQRVPMVLVSKVGNPLEVNDAKPGNRGKRDSQIVLMSFLQKVMFDERMTTLEYEFFNAVWRCTGIPPDRYETVLCVDADTKVFPDSLTRMNACMVNDHEIMGLCGETKIANKSETWVTMIQVFEYYISHHNTKAFESVFGGVTCLPGCFSMYRIKAPKGERGFWVPILANPDICEHYAENVVDTLHKKNLLLLGEDRYLSTLMLKTFPKRKMVFCPQAVCKTIVPDTFRVLLSQRRRWINSTVHNLCELILVRDLCGTFCFSMQFVVFMDLVGTLVLPAAISFTLYIIMISIIPQSVTGMPRPYVSLVLLAFILGLPGVLIVITSRKIAYVGWMLVYLISLPVWNLILPAYSYWHMDDFTWGETRKIAGEVKEEAHGGKEGTFDSSHIVMKKWAEFERERRWRTGTASRDSQYFDVVQRANSPRSGIPSNRYSIVSTSETFNSGLGTAESNHLFRQSQSFASMSQVAPSPETNYGNVPQLALPPPRGASIGREHSPSSTESGTSNNYAYGSTEEPTASNVDPYYQPFTNEVYQDEAEQPILPSEYTTTSPEPVYQTAPARVRQPSQRGVSLVDTGPVRSAQAAPHDAVRRVSRHQRRSSSKNQLVSPISSGGHTGSLPPGAAPPQY
|
Polymerizes chitin, a structural polymer of the cell wall and septum, by transferring the sugar moiety of UDP-GlcNAc to the non-reducing end of the growing chitin polymer. Activated by CSR2, it produces chitin that is deacetyled to chitosan, which is required to maintain cell wall integrity. Conversion of chitin to chitosan offers an advantage during infection, as chitosan is less readily detected by host immunosurveillance mechanisms.
|
J9VYP5
|
PUR2_CRYNH
|
Bifunctional purine biosynthetic protein ADE5,7 [Includes: Phosphoribosylamine--glycine ligase (EC 6.3.4.13) (Glycinamide ribonucleotide synthetase) (GAR synthetase) (GARS) (Phosphoribosylglycinamide synthetase); Phosphoribosylformylglycinamidine cyclo-ligase (EC 6.3.3.1) (AIR synthase) (AIR synthetase) (AIRS) (Phosphoribosyl-aminoimidazole synthetase)]
|
MPEITAFPQPKSDLSILLLGAGGREHALAFKLAQSSRVARIVVCPGNGGTALMGGKVSNLALPWGAPPAFRSIVEWAQKENIDLVVPGPEQPLVDGVEGAFKKVGIPVFGPSPAAAMLEGSKSLSKEFMARHNIPTAAFRSFTSTQYEDAVAYIKSKPFTSGRSVIKASGLAAGKGVLIPETDEEAFAALKSVMVDKEFGDAGDEVVVEEYLSGPEISVLAFSDGYTIVPMPAAQDHKRIGEGDTGLNTGGMGAYAPAPIATKEIMERCVKDVLEPTIKGMREDGYPFVGMLFTGFMITADGPRVLEYNVRFGDPETQALMLLLDEQTDLAEVLLACVERRLDSIKLGYKQGYAVSVVLASEGYPGSYPKGLPMTLNPTPEGVEVFHAGTKRSDNVTVTDGGRVLAVCASAPTLRAAVDLAYSGISQISFQGQTFRRDIAYRALSSEPPAEPKGLTYAAAGVSVDAGNDLVEAIKPVVKATRRPGADSDIGGFGGAFDLAKAGYKDPILVSGTDGVGTKLRVALDHGKHNTVGIDLVAMSVNDLIVQGAEPLYFLDYYACSKLDVPVAADVITGIAEGCLQAGCALIGGETAEMPGMYHGDDYDLAGFAVGVVERAQILPTPDIASGDVLLALSSSGPHSNGFSLIRKIVSLSNLSLHDTAPWDKNTSVGDALLTPTKVYIKPLLPGIKSGLYKGMSHITGGGFTENIPRIFSSASNLGVKLDLTSYSLPAIWKWLMRAGNVEAKEMVRTFNCGVGMIIIVAKDKADAALSSLKENGEEAWVIGEVQEKKGVEYVGLDKFGL
|
Catalyzes the second and fifth step in the 'de novo' purine biosynthesis pathway contains phosphoribosylamine--glycine ligase (GARS) and phosphoribosylformylglycinamidine cyclo-ligase (AIRS) activities.
|
J9W0G9
|
YPK1_CRYNH
|
Serine/threonine-protein kinase YPK1 (EC 2.7.11.1)
|
MMSWKFGKKFKEGGFLSGKHHSSNNNSPSDTSRSTTPTPGNPHPEDAVKPPVPRSGMLKIRVTAAKGLSLPQGVSVPAPVQEALTTHPTLASRIATSPPTAIVKAAGANRDSLQRRQVWWLPYLVLEFDKNEVLVDALGGDLASPVWMYSATFDVSRISEISATVYLRTREPHAEGREKSNGEGEGEDMGNSDLCLGSIRFTPNLDSLRVTDDWVTVQGGGGSGSINVQVSFKPASGQILTIDSFELLKVIGKGSFGKVMQVRKRDTLRIYALKTIRKAHIVSRSEVTHTLAERTVLAQVNCPFIVPLKFSFQSKEKLYLVLAFINGGELFHHLQREGKFNETRSRFYSAQLLLALEHLHSFNVIYRDLKPENILLDYAGNIALCDFGLCKLNMSNSDTTNTFCGTPEYLAPELLSGHGYTKCVDWWTLGVLLYEMLTGLPPFYDENTNEMYRKILTEPLRFPDGVRSEARSLLTGLLNRDPRQRLGVNGAQDIKNHPFFAKHINFTKLWNKQIQPPFKPAVASAIDTSNFDEEFTNEVPLDSVVDDSHLSQTVQQQFEGFSWSVSPLGESVGRY
|
Probable serine/threonine-protein kinase which may act in the sphingolipid-mediated signaling pathway. May act downstream of TORC2 (TOR complex 2) and PDK1 to regulate sphingolipid metabolism.
|
K0I210
|
FOMT4_OCIBA
|
Flavonoid 6-O-methyltransferase 4 (ObFOMT4) (EC 2.1.1.-) (Ladanein 6-O-methyltransferase) (EC 2.1.1.-) (Scutellarein-7-methyl ether 6-O-methyltransferase) (EC 2.1.1.-)
|
MAVDKEVELHAQAWDHALSYITPTALSAAVELEIPDILEDHGGLMSLSELSAASGCPREPLYRLMRFLIFHGIFTKSNDCYAQSPLSRVFTRENLGPYMLMQATPVTRSPAGLSGEALKTGTPLYLKSIRGEDSWNDPAYGFHMRAFTNGMAAHARLTAAAIVTNYPTAFNGVRSVVDVGGRHGMAIGKLVEAFPWVRGIAFDLPEVVADAPPRKGVDFVGGDMFESLPKADAVMLMWVLHDWSDDKCIEILKKCKEAIPTSTGKVMIVDAIINEEGEGDEFSGARLSLDMTMMAMTTQGKERSYKEWVHLLNEAGFSKHTVKNIKTIEFVIEAYP
|
Flavonoid 6-O-methyltransferase involved in the biosynthesis of polymethoxylated flavonoids natural products such as nevadensin and salvigenin (SALV), aroma compounds which contribute to the flavor of sweet basil, and exhibit pharmacological activities such as anti-allergic, anti-oxidant, antibacterial, anti-proliferative, and anti-inflammatory effects. Catalyzes S-adenosylmethionine-dependent regioselective 6-O-methylation of flavonoids active on various hydroxylated flavonoid substrates, including scutellarein-7-methyl ether (SCU7Me) and ladanein (LAD).
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K0I7Q2
|
FOMT3_OCIBA
|
Flavonoid 4'-O-methyltransferase 3 (ObFOMT3) (EC 2.1.1.-) (Cirsiliol 4'-O-methyltransferase) (EC 2.1.1.-) (Cirsimaritin 4'-O-methyltransferase) (EC 2.1.1.-) (Genkwanin 4'-O-methyltransferase) (EC 2.1.1.-) (Scutellarein-7-methyl ether 4'-O-methyltransferase) (EC 2.1.1.-)
|
MAVDKEVQLHAQAWEHALSYINSTALSAAVELEIPDILEDHGGLMSLSELSAASGCPREPLYRLMRFLIFHGIFTKSDDCYAQSPLSRLFTRENLGPYMLMQATPVTRSPAGLSGEALKTGTSLYLKSIRGEDSWSDPAYGYHMKAFTNAMIAHARLTAAAIVSNYPAAFDGLRSVVDVGGRHGTAIGRLVEAFPWVRGIAFDLPEIVADAPPRKGVDFVGGDMFESVPKADAVMLMWILHDWSDDKCIEILKKCKEAIPASTGKVMIVDAIINEDGEGDEFSGARLSLDMIMLAVMAQGKERTYKEWVHLLNEAGFSKHTVKNIKSIESVIEAYP
|
Flavonoid 4'-O-methyltransferase involved in the biosynthesis of polymethoxylated flavonoids natural products such as nevadensin and salvigenin, aroma compounds which contribute to the flavor of sweet basil, and exhibit pharmacological activities such as anti-allergic, anti-oxidant, antibacterial, anti-proliferative, and anti-inflammatory effects. Catalyzes S-adenosylmethionine-dependent regioselective 4'-O-methylation of flavonoids active on various hydroxylated flavonoid substrates, including scutellarein-7-methyl ether (SCU7Me) and cirsimaritin (CIRM), and, with a lower efficiency, hispidulin, ladanein (LAD), cirsioliol (CIRL) and genkwanin (GENK).
|
K0I977
|
FOMT1_OCIBA
|
Flavonoid 7-O-methyltransferase 1 (ObFOMT1) (EC 2.1.1.-) (4'-methylscutellarein 7-O-methyltransferase) (EC 2.1.1.-) (Acacetin 7-O-methyltransferase) (EC 2.1.1.-) (Apigenin 7-O-methyltransferase) (EC 2.1.1.-) (Chrysoeriol 7-O-methyltransferase) (EC 2.1.1.-) (Diosmetin 7-O-methyltransferase) (EC 2.1.1.-) (Luteolin 7-O-methyltransferase) (EC 2.1.1.-) (Naringenin 7-O-methyltransferase) (EC 2.1.1.232) (Scutellarein 7-O-methyltransferase) (EC 2.1.1.-)
|
MGRDEEAAAQAEAWNHGFGFIKTSVIKTAIELEIPDILHNQGGPLSLSALSSAVGVPPDRLHRIMRFLAHHGVSKKTASPPGESDYYYAETAVSRSLTKDNLGPFVLLQGAQRGPSACITAQGLKSRERPGVEELGSDPLYEDPIFTEKVFRDAMTCHARVTTSAVIENYGEGFRGVGSLVDVGGSYGMTLGMLVEAFPWIRGICYDLPPVVAKAKPLHGVEFVAGSMFESVPKADVIMLMFVLHNWSDNECIDILKRCKEAIPAETGRLMIIDAIIDEDGEGDEFAGARLGLDVTMMAVTYEGKERTHREWAYILTEAGFRKYVVNNIKALESLIEAYP
|
Flavonoid 7-O-methyltransferase involved in the biosynthesis of polymethoxylated flavonoids natural products such as nevadensin and salvigenin, aroma compounds which contribute to the flavor of sweet basil, and exhibit pharmacological activities such as anti-allergic, anti-oxidant, antibacterial, anti-proliferative, and anti-inflammatory effects. Catalyzes S-adenosylmethionine-dependent regioselective 7-O-methylation of flavonoids active on various hydroxylated flavonoid substrates, including apigenin (API) and luteolin (LUT), and, with a lower efficiency, scutellarein (SCU), naringenin (NAR), chrysoeriol (CHRYS), diosmetin (DIOS), acacetin (ACA) and scutellarein-7-methyl ether (SCU7Me).
|
K0ICR0
|
FOMT5_OCIBA
|
Flavonoid 4'-O-methyltransferase 5 (ObFOMT5) (EC 2.1.1.-) (Cirsiliol 4'-O-methyltransferase) (EC 2.1.1.-) (Cirsimaritin 4'-O-methyltransferase) (EC 2.1.1.-) (Genkwanin 4'-O-methyltransferase) (EC 2.1.1.-) (Sakuranetin 4'-O-methyltransferase) (EC 2.1.1.-) (Scutellarein-7-methyl ether 4'-O-methyltransferase) (EC 2.1.1.-)
|
MVADEEAQLHAQAWDHALSYIKPTALSAAVELEIPDILENHGGPMTLSELSAASGCPREPLYRLMRFLIFHGIFTKSDDCYAQSPLSRLFTTENLGPYMLMQATPVTRCPTGLSGEALKTGTSLYLKSIRGEDSWSDPAYGYHMKAFTNAMTAHARLTAAAIVRNYPAAFDGVQSVVDVGSRHGTAIGKLVEAFPWVRGIAFDLPEIVADAPPRKGVDFVGGDMFESVPKADAVMLMWILHDWSDDKCIEILKKCKEAIPANIGKVMIVDAIINEDGEGDEFSGTRLSLDMIMLAVMAQGKERTYKEWVHLLNEAGFSKHTIKNIKAMEFVIEAYP
|
Flavonoid 4'-O-methyltransferase involved in the biosynthesis of polymethoxylated flavonoids natural products such as nevadensin and salvigenin, aroma compounds which contribute to the flavor of sweet basil, and exhibit pharmacological activities such as anti-allergic, anti-oxidant, antibacterial, anti-proliferative, and anti-inflammatory effects. Catalyzes S-adenosylmethionine-dependent regioselective 4'-O-methylation of flavonoids active on various hydroxylated flavonoid substrates, including scutellarein-7-methyl ether (SCU7Me) and, with a lower efficiency, cirsimaritin (CIRM), sakuranetin (NAR7Me), ladanein (LAD) and genkwanin (GENK).
|
K0II72
|
FOMT2_OCIBA
|
Flavonoid 7-O-methyltransferase 2 (ObFOMT2) (EC 2.1.1.-) (4'-methylscutellarein 7-O-methyltransferase) (EC 2.1.1.-) (Acacetin 7-O-methyltransferase) (EC 2.1.1.-) (Apigenin 7-O-methyltransferase) (EC 2.1.1.-) (Chrysoeriol 7-O-methyltransferase) (EC 2.1.1.-) (Diosmetin 7-O-methyltransferase) (EC 2.1.1.-) (Luteolin 7-O-methyltransferase) (EC 2.1.1.-) (Naringenin 7-O-methyltransferase) (EC 2.1.1.232) (Scutellarein 7-O-methyltransferase) (EC 2.1.1.-)
|
MGRDEEAAARAEAWNHGFGFIKTSVIKTAIELEIPDILHNHGAPLSLSALSSAVGVPPDRLHRIMRFLTHHGVSKKTASPPGESDYYYAETAVSRSLTKDNLGAFVLLQGAQRGPSACITAQGLKSRERPGVEELGSDPLYEDPIFTKMVFRDAMACHARLTTSAVIENYGEGFRGVGSLVDVGGSYGMTLGMLVEAFPWIRGICYDLPQVVAKAKPLHGVEFVAGSMFESVPEADVVMLMFVLHNWSDNECIDILKRCKEAIPRETGKVMIIDAIIEEDGEGDEFAEARLGLDVTMMAVTFEGKERTHREWAFILKEAGFRKYVVKNIKALESLIEAYP
|
Flavonoid 7-O-methyltransferase involved in the biosynthesis of polymethoxylated flavonoids natural products such as nevadensin and salvigenin, aroma compounds which contribute to the flavor of sweet basil, and exhibit pharmacological activities such as anti-allergic, anti-oxidant, antibacterial, anti-proliferative, and anti-inflammatory effects. Catalyzes S-adenosylmethionine-dependent regioselective 7-O-methylation of flavonoids active on various hydroxylated flavonoid substrates, including apigenin (API) and luteolin (LUT), and, with a lower efficiency, scutellarein (SCU), naringenin (NAR), chrysoeriol (CHRYS), diosmetin (DIOS), acacetin (ACA) and scutellarein-7-methyl ether (SCU7Me).
|
K0J4Q8
|
AHPC_AMPXN
|
Alkyl hydroperoxide reductase C (EC 1.11.1.26) (Peroxiredoxin) (Thioredoxin peroxidase)
|
MSLIGTEVQPFRAQAFQSGKDFFEVTEADLKGKWSIVVFYPADFSFVCPTELEDVQKEYAELKKLGVEVYSVSTDTHFVHKAWHENSPAVGSIEYIMIGDPSQTISRQFDVLNEETGLADRGTFIIDPDGVIQAIEINADGIGRDASTLINKVKAAQYVRENPGEVCPAKWEEGGETLKPSLDIVGKI
|
Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides.
|
K0P2S0
|
IF4E1_ARAHY
|
Eukaryotic translation initiation factor 4E-1 (PeaeIF4E) (eIF-4E-1) (eIF-4F 25 kDa subunit) (eIF-4F p26 subunit) (mRNA cap-binding protein)
|
MVVEDTQKSSITDDQITANPNNENEDLEEGEILDDDDSSATSRPPSSSGALARNPHPLENSWTFWFDNPSAKSKQAAWGSSIRPIYTFATVEEFWSIYNNIHHPSKLAVGADFHCFKHKIEPKWEDPICANGGKWTMTFPRGKSDTSWLYTLLGMIGEQFDHGDEICGAVVNVRNRQEKIALWTKNAANEAAQVSIGKQWKEFLDYNDTIGFIFHEDAKKHDRAAKNKYVI
|
Component of the protein complex eIF4F, which is involved in the recognition of the mRNA cap, ATP-dependent unwinding of 5'-terminal secondary structure and recruitment of mRNA to the ribosome (By similarity). Recognizes and binds the 7-methylguanosine-containing mRNA cap during an early step in the initiation of protein synthesis and facilitates ribosome binding by inducing the unwinding of the mRNAs secondary structures (By similarity). Key component of recessive resistance to potyviruses such as peanut stripe virus (PStV).
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K4BNG7
|
NAP2_SOLLC
|
NAC domain-containing protein 2 (SlNAP2)
|
MVGKNNSNHLPPGFRFHPTDEELIMYYLRNQATSKPCPSSIIPEVDVYKFDPWELPEKTEFGEKEWYFFTPRDRKYPNGVRPNRAAVSGYWKATGTDKGIYSGTKYVGIKKALVFYKGKPPKGIKTDWIMHEYRLSESRTQPTRPNGSMRLDDWVLCRIYKKKNLERAIEMMKVEEDTQEPQIMSVTNPIHEVVASNGQQTLKLPRTCSLSHLLEMDYFGSISQLFDDNNSYNTISQNNTLMTNVNGYVMPHQAMEKFQLGEVSQISMNPSYQFQ
|
Transcription factor that binds DNA motifs 5'-CGT[AG](5N)NACG[ACT][AC][AT][ACG][ACT]-3' and 5'-CACG[ACT][AC][AT][AGT][CT]-3' in target genes promoters. Promotes leaf senescence (developmental, light-induced and ABA-induced senescence) and regulates fruit yield and sugar content, probably by establishing abscisic acid (ABA) homeostasis. Activates the expression of senescence and ABA associated genes including NCED1, ABCG40, CYP707A2, SAG113, SGR1 and PAO, by directly binding to their promoters.
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K4C9E2
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NSY_SOLLC
|
Neoxanthin synthase, chloroplastic (EC 5.3.99.9) (Lycopene beta-cyclase) (EC 5.5.1.19)
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METLLKPFPSLLLSSPTPYRSIVQQNPSFLSPTTKKKSRKCLLRNKSSKLFCSFLDLAPTSKPESLDVNISWVDPNSNRAQFDVIIIGAGPAGLRLAEQVSKYGIKVCCVDPSPLSMWPNNYGVWVDEFENLGLEDCLDHKWPMTCVHINDNKTKYLGRPYGRVSRKKLKLKLLNSCVENRVKFYKAKVWKVEHEEFESSIVCDDGKKIRGSLVVDASGFASDFIEYDRPRNHGYQIAHGVLVEVDNHPFDLDKMVLMDWRDSHLGNEPYLRVNNAKEPTFLYAMPFDRDLVFLEETSLVSRPVLSYMEVKRRMVARLRHLGIKVKSVIEEEKCVIPMGGPLPRIPQNVMAIGGNSGIVHPSTGYMVARSMALAPVLAEAIVEGLGSTRMIRGSQLYHRVWNGLWPLDRRCVRECYSFGMETLLKLDLKGTRRLFDAFFDLDPKYWQGFLSSRLSVKELGLLSLCLFGHGSNMTRLDIVTKCPLPLVRLIGNLAIESL
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Involved in the synthesis of neoxanthin, the last product of carotenoid synthesis and a precursor of abscisic acid. Involved in the beta-carotene biosynthesis.
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K4CI52
|
ABAH2_SOLLC
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Abscisic acid 8'-hydroxylase CYP707A2 (ABA 8'-hydroxylase CYP707A2) (SlCYP707A2) (EC 1.14.14.137) (Cytochrome P450 707A2)
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MEFVSMLCLFTFISLTLLLIHSIFKFLAFASKKLPLPPGTLGLPYIGETFQLYSQNPNVFFASKVKKYGSIFKTYILGCPCVMISSPEAAKQVLVTKANLFKPTFPASKERMLGKQAIFFHQGDYHAKLRKLVLQAFKPDSIRNIIPDIESIAITSLESFQGRLINTYQEMKTYTFNVALISIFGKDEFLYREELKKCYYILEKGYNSMPINLPGTLFNKAMKARKELAKIVAKIISTRREMKIDHGDLLGSFMGDKEGLTDEQIADNVIGVIFAARDTTASVLTWILKYLGENPSVLQAVTEEQENIMRKKEVNGEEKVLNWQDTRQMPMTTRVIQETLRVASILSFTFREAVEDVEFEGYLIPKGWKVLPLFRNIHHSPDNFPEPEKFDPSRFEVSPKPNTFMPFGNGVHSCPGNDLAKLEILILVHHLTTKYRWSMVGPQNGIQYGPFALPQNGLPIKLSLKTSST
|
Negative regulator of fruit ripening involved in the oxidative degradation of abscisic acid (ABA).
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K4CWS6
|
U75C1_SOLLC
|
UDP-glycosyltransferase 75C1 (Abscisic acid beta-glucosyltransferase) (Indole-3-acetate beta-glucosyltransferase) (SlUGT75C1) (EC 2.4.1.121) (EC 2.4.1.263)
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MVQPHVLLVTFPAQGHINPSLQFAKRLIEMGIEVTFTTSVFAHRRMAKIAASTAPKGLNLAAFSDGFDDGFKSNVDDSKRYMSEIRSRGSQTLRDVILKSSDEGRPVTSLVYTLLLPWAAEVARELHIPSALLWIQPATVLDIYYYYFNGYEDEMKCSSSNDPNWSIQLPRLPLLKSQDLPSFLVSSSSKDDKYSFALPTFKEQLDTLDGEENPKVLVNTFDALELEPLKAIEKYNLIGIGPLIPSSFLGGKDSLESSFGGDLFQKSNDDYMEWLNTKPKSSIVYISFGSLLNLSRNQKEEIAKGLIEIQRPFLWVIRDQEEEKEEEKLSCMMELEKQGKIVPWCSQLEVLTHPSLGCFVSHCGWNSTLESLSSGVPVVAFPHWTDQGTNAKLIEDVWKTGVRMRVNEDGVVESDEIKRCIEIVMDGGEKGEEMRKNAQKWKELARAAVKEGGSSEVNLKAFVLQVSKSC
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Glucosyltransferase acting on both abscisic acid (ABA) and auxin (IAA). Required for ABA-mediated fruit ripening, seed germination, and negative responses to drought.
|
K4L7X3
|
SPCAD_ADVMD
|
3-sulfinopropanoyl-CoA desulfinase (EC 3.13.1.4) (3-sulfinopropionyl coenzyme A desulfinase) (3-sulfinopropionyl-CoA desulfinase) (3SP-CoA desulfinase)
|
MYELTPEQRTLQTQARELAQSVFASTAVQTDLTEQYPWDNVAQLRDAGFMGMMLPTSVGGRGLSTLDTVIVIEEMAKACATMGRITVDSNLGAIGAITKYGSEEQIKLAADLVLAGDKPAICISEPNAGSAASEMTTRADKNGDHYILNGEKYWITGGGVSKLHLIFARVFDDGVEQGIGAFITVLDDHGPEGLKVGRRLYAMGVRGIPETHLEFHDLKIHKSMMITFPDGLKRGFAALMSAYNAQRVGAGAVALGIAQCAFEEGVAYLKRREQFGRPLAEFQGLQWMVADMSVQLEAARLMLRSAAVSGETFPDINKAAQAKIFAAETANKVTNDALQFFGSSGYGRHNPMERHVRDARMFTIAGGTAQILRTQVASKILDMKLPQTRDGYLKAAQNSKR
|
Catalyzes the conversion 3-sulfinopropanoyl-CoA (3SP-CoA) to propanoyl-CoA by abstraction of sulfite. Does not show dehydrogenase activity. Involved in the degradation of 3,3'-dithiodipropionate (DTDP), a sulfur-containing precursor substrate for biosynthesis of polythioesters (PTEs).
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K4LLQ2
|
VSP_BOTBA
|
Thrombin-like enzyme barnettobin (Bb-TLE) (SVTLE) (EC 3.4.21.-) (Snake venom serine protease) (SVSP)
|
APKELQVSYAHKSSELVIGGDECDINEHPFLAFLYSRGNFCGLTLINQEWVLTAAHCDRRFMPIYLGIHTLSVPNDDEVIRYPKDNFICPNNNIIDEKDKDIMLIRLNRPVKNSEHIAPISLPSNLPSVGSVCRVMGWGSITAPNDTFPDVPHCANINLFNDTVCHGAYKRFPVKSRTLCAGVLQGGKDKCMGDSGGPLICNGPFHGILFWGDDPCALPRKPALYTKGFEYPPWIQSIIAKNTTETCPP
|
Thrombin-like snake venom serine protease that releases only fibrinopeptide A from human Aalpha chain of fibrinogen (specific coagulant activity was 251.7 NIH thrombin units/mg). Also shows fibrino(geno)lytic activities in vitro and defibrinogenating effects in vivo.
|
K4REZ6
|
ROSB_STRDJ
|
8-demethyl-8-aminoriboflavin-5'-phosphate synthase (AFP synthase) (EC 2.6.1.114) (8-amino-flavin synthase)
|
MALKALILNTTLRRSPSRSQTQGLIDKAVPLYEKEGIETEVVRVIDHDIEQEYWDDYDDWNAGEKARREDEWPWLLEKIREADILVIATPITLNMCTSAAHVILEKLNLMDELNGDTKQFPLYNKVAGLLMCGNEDGAHHVAGTVLNNLGRLGYSVPPNAAAYWLGPAGTGPGYIEGKGDRHFHTNKLIRFMVANTSHLARMLQETPYTTDLEACAQAAREESDDVFAIRVNVNTPAIRYKRFQKLGEVKVEESQLG
|
Involved in the biosynthesis of the riboflavin analog antibiotic roseoflavin (3,8-dimethylamino-riboflavin). Catalyzes the site-specific substitution of the C-8 methyl group of riboflavin-5'-phosphate (FMN) by an amino group to yield 8-amino-8-demethylriboflavin 5'-phosphate, via a combined oxidation, decarboxylation and transamination reaction. The catalysis is initiated by an oxidation step in which the C-8 methyl group on the dimethylbenzene ring of FMN is converted to a formyl group to yield the 8-demethyl-8-formylriboflavin-5'-phosphate (OHC-RP) intermediate. In the presence of thiamine, the formyl group is oxidized into a carboxyl group to yield the 8-demethyl-8-carboxyriboflavin-5'-phosphate (HO2C-RP) intermediate. Finally, in the presence of L-glutamate as an amino donor, decarboxylation and aminotransfer occur, resulting in production of 8-demethyl-8-aminoriboflavin-5'-phosphate. Addition of NAD (but not NADP) to the reaction increases the yield 1.7-fold. The reaction also proceeds without the addition of any electron acceptor, and it is possible that molecular oxygen serves this role.
|
K4ZRC1
|
PPEP2_PAEA2
|
Pro-Pro endopeptidase (PPEP-2) (EC 3.4.24.89)
|
MKWDKRVVALILAVMIVCPLFAAPAHAQEQSILDKLVVLPSGEYNHSEAAAMKQRLEKIPTSILDALYSKGVKIKLTQGAITNEPELAYLKGVVPRGWEGTGLTWDDVPGVSERVVAVRIGYSEKGKGHNSLNLEIHETLHAVDRLVLNEVSGTDEFINIFNKEASVKYKGDGYVSAYPTEYFAEAASLYLYSDATRSDLKDSMPLTYEFMAKLFAN
|
Zinc-dependent endoprotease with a unique preference for proline residues surrounding the scissile bond, which cleaves in a PLP-|-PVP motif. Cleaves the cell surface protein encoded by an adjacent gene, which contains two PPEP-2 cleaving sites and putative extracellular matrix-binding domains. Thereby, may have a role in the regulation of P.alvei adhesion. Is not able to cleave within the PVP-|-PVQ motif, and only shows a very poor cleavage of the VNP-|-PVP motif in vitro, which is the optimal substrate peptide for PPEP-1 from P.difficile.
|
K5B7F3
|
MET1_MYCHD
|
MMP 1-O-methyltransferase (EC 2.1.1.365) (3-O-methylmannose polysaccharide 1-O-methyltransferase)
|
MTDIRDTDALFALADRVTGFMPADEGRTLYETAVRYLGDGVGVEIGTYCGKSTVLLGAAARQTGGVVFTVDHHHGSEEHQPGWEYHDPSLVDPVTGLFDTLPRLRHTLDEADLYDHVVAVVGKSAVVARGWRTPLRFLFIDGGHTEEAAQRDFDGWARWVEVGGALVIHDVFPDPKDGGQAPFHIYQRALNTGDFREVNAYGSMRVLERTSGIAGQPL
|
Involved in the biosynthesis of 3-O-methylmannose polysaccharides (MMP), which are intracellular polymethylated polysaccharides implicated in the modulation of fatty acid metabolism in non-tuberculous mycobacteria. Specifically methylates the 1-OH position of 3,3'-di-O-methyl-4alpha-mannobiose, a probable early precursor of MMP, yielding the reducing end dimannoside of MMP.
|
K5BDL0
|
GGH_MYCHD
|
Glucosylglycerate hydrolase (GG hydrolase) (EC 3.2.1.208)
|
MPHDPSFTPTQLAARAAYLLRGNDLGTMTTAAPLLYPHMWSWDAAFVAIGLAPLSVERAVVELDTLLSAQWRNGMIPHIVFANGVDGYFPGPARWATATLADNAPRNRLTSGITQPPVHAIAVQRILEHARTRGRSTRAVAEAFLDRRWGDLMRWHRWLAECRDRNERGRITLYHGWESGMDNSPRWDSAYANVVPGKLPEYQRADNVIITDPSQRPSDGEYDRYLWLLEEMKAVRYDDERLPSVMSFQVEDVFFSAIFSVACQVLAEIGEDYKRPHADVKDLYLWAERFRAGVVETTDQRTGAARDFDVLAEKWLVTETAAQFAPLLCGGLPHDRERALLKLLEGPRFCGHPDLKYGLIPSTSPVSRDFRPREYWRGPVWPVLTWLFSWCFARRGWAERARLLRQEGLRQASDGSFAEYYEPFTGEPLGSMQQSWTAAAVLDWLG
|
Catalyzes the hydrolysis of glucosylglycerate (GG) to glycerate and glucose. Involved in recovery from nitrogen starvation by promoting the rapid mobilization of the glucosylglycerate that accumulates under these conditions. Can also hydrolyze mannosylglycerate (MG), with tenfold lower efficiency.
|
K7EJ46
|
SIM22_HUMAN
|
Small integral membrane protein 22 (Cancer-associated small integral membrane open reading frame 1)
|
MAVSTEELEATVQEVLGRLKSHQFFQSTWDTVAFIVFLTFMGTVLLLLLLVVAHCCCCSSPGPRRESPRKERPKGVDNLALEP
|
May modulate lipid droplet formation throught interaction with SQLE.
|
K7FQW8
|
SCNNB_PELSI
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Amiloride-sensitive sodium channel subunit beta (Beta-NaCH) (Epithelial Na(+) channel subunit beta) (Beta-ENaC) (Nonvoltage-gated sodium channel 1 subunit beta) (SCNEB)
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MNLKKYFIRVLHRLQKGPGYTYKELLVWYCDNTNTHGPKRIIREGPKKKFIWFFLTLLFASLVFWQWGILITTYLSYSVSSSLSIGFKTMKFPAVTVCNASPFKYSKVRHLLRELDELTEAALERILQSKNRDATSALPLNSSETPSQTLNLRLWNQIPLVLIDESDPERPVIIDLFETDESGSGAQPNNSSPALVNVTSEAKKQKVAMKLCSRKALPNCIYRNFTSAAQAVTEWYILQSTSIFAKIPRNETVEMGYQPEDMILACLYGAEPCSYRNFTPIYHPDHGNCYIFNWGKDEEALFSSNPGAEFGLKLILDISQQDYIPYLTSTAGARLMLHEQRSFPFLKDLGIYAMSGTETSIGVLVDELERMGFPYSDCTMNGSDVPVKNLYNEYNTTYSIQACLRSCFQAQMFETCGCGHYLFPLPEGVSYCNSEDDPDWAYCYSSLRSSIGHRQFCIDSCKETCNDIQYKMTISMADWPSEASEEFQYMQHPLTYERDQSRNATLDRNGIIKLNIYFQEYNYRTISESAATTIVWLLSSLGGQFGFWMGGSVLCLIEFGEIIIDFLWITVIKISNWGKGLKQKRARAQYPDAPPTVSELVEAHINL
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Sodium permeable non-voltage-sensitive ion channel inhibited by the diuretic amiloride. Mediates the electrodiffusion of the luminal sodium (and water, which follows osmotically) through the apical membrane of epithelial cells. Plays an essential role in electrolyte and blood pressure homeostasis, but also in airway surface liquid homeostasis, which is important for proper clearance of mucus.
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K7MTW9
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TAP1_SOYBN
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Histone acetyltransferase TAP1 (GmTAP1) (EC 2.3.1.48)
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MSMLSLLRSQLFNFMPIIHCLLKLNSTRKFKSFQLKAGFWESIKSGLMKNNSMQVIDPPSTDEENVEPLSQDFVLVEKTEPDGTIEQIIFSSGGDVDVYDLQALCDKVGWPRRPLSKLAAALKNSYIVASLHSIRKSHGSEGNEQKRLIGMARATSDHAFNATIWDVLVDPGYQGQGLGKALIEKLIRTLLQRDIGNITLFADSQVVEFYRNLGFEADPEGIKGMFWYPNH
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Acetylates histones H2A and H3 in vitro. (Microbial infection) Acts as negative regulator of immunity when hijacked and relocated to the nucleus by the effector Avh52 from the pathogen Phytophtora sojae. Acts as a susceptibility factor that is hijacked by Avh52 in order to promote acetylation of histones H2A and H3 during early infection by Phytophtora sojae. These epigenetic modifications may up-regulate the expression of potential plant susceptibility genes, thereby promoting susceptibility to Phytophtora sojae.
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K7N5M8
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DYP2_AMYS7
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Multifunctional dye peroxidase DyP2 (EC 1.11.1.16) (EC 1.11.1.19) (EC 1.11.1.7) (Dye decolorizing peroxidase 2) (DyP2) (Manganese peroxidase)
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MPVDLSTTLSWKSATGEAATMLDELQPNILKAHVRDRLTVLFLGFGDAAEARTFLNGLSGLMKSARTHLQEVEAHKLTKAVGTPYLGVGLTAHGYATLGVTAPADPSFTAGAKAAVEKLADPAVTEWEGHYQQTIDAVLLLGDATAGPVRTLRRQVEALRPASVTVVGEESGLGLANANGDGIEHFGYVDGRSQPLFLTEDVDAERDTTDGVNDWDPSAPLEQVLVPDPAAPDPTVHFGSYFVFRKLEQNVRLFKEAERDLAHDLGLRGEDRERAGAMLVGRFEDGTPLTAQSAPGSHHPVGNDFSYDSDKLGQKCPFHAHIRKTNPRGSGGAEAPEEERKHLMARRGQTYGRRHDDPNADLPPRLRPAKDVGLLFMAFNSNLGNQFEFTQQIWANNPAFPFPPDGSQPGLDPVIGQGARAPQKYAPEWGHNNVAEATDPIPQAVTMKGGEYFFMPSLAFLRSL
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Displays both high peroxidase and manganese peroxidase activity. Is likely involved in lignin degradation. Also has a Mn-dependent oxidase mode of action that expands its substrate scope in vitro is thus able to catalyze the O(2)- and Mn-dependent oxidative decarboxylation of 4-methoxymandelate to anisaldehyde.
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K7N6K2
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TR34B_MOUSE
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E3 ubiquitin-protein ligase TRIM34B (EC 2.3.2.27) (Tripartite motif-containing protein 34B)
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MASTGPTNIQEKTTCPVCQELLTKALSLGCGHLVCQACLISNKNAVINPRGKSSCPVCGTRFSLENLQANKHLANVVERLGEVKLKPDIGTKRDLCVHHGEKLLLFCKEDKKVICWVCERSQEHRGHHTFLWEEAVRECQENLQKALTRLRKEQEKVETLEADIKEDRLSWKRQVQTERQRIQTGFNQLRRILDKEEQRELKRLREEEQMILDSLAGAEAELAQQSQLVEELISDLELRREWSDTELLQDMSGILKWSQIWTLKKPKAVSKKLSMVFQAPDLSGMLQKFRELSAVRAYWDNFTFNPENLNLNLILSEDHRQVTSVSIWPFKCCNNGILGSKCFSSGKHYWEVDVSEKNAWTLGVYTRKRTLRFDVRQRKGQPNGYHRYKPQNGYWVIGLQHGSKYSIFEDSSNCDPTVLNPFVATPLHRVGIFLDCEEGTVSFLNVTNHGSLIYKFSQCCFSQPAYPYFNPWDCPAPMTLCPLNS
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Functions as antiviral protein and contributes to the defense against retroviral infections (By similarity). Acts as a capsid-specific restriction factor with the help of TRIM5 and prevents infection from non-host-adapted retroviruses. During influenza A virus infection, promotes programmed cell death by targeting ZBP1 for 'Lys-63'-linked polyubiquitination. In turn, promotes ZBP1 recruitment of RIPK3 to mediate virus-induced programmed necrosis (By similarity). Negatively regulates the function of mitochondria by enhancing mitochondrial depolarization leading to cytochrome c release and mitochondria-dependent apoptosis. Promotes also the formation of multinucleated giant cells by means of cell fusion and phagocytosis in epithelial cells (By similarity). Regulates intestinal inflammation by controlling the exocytosis of the major component of colonic mucus MUC2 from colonic goblet cells.
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K7NBW3
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74AC1_SIRGR
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Mogroside IE synthase (EC 2.4.1.350) (UDP-glycosyltransferase 74AC1)
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MEKGDTHILVFPFPSQGHINPLLQLSKRLIAKGIKVSLVTTLHVSNHLQLQGAYSNSVKIEVISDGSEDRLETDTMRQTLDRFRQKMTKNLEDFLQKAMVSSNPPKFILYDSTMPWVLEVAKEFGLDRAPFYTQSCALNSINYHVLHGQLKLPPETPTISLPSMPLLRPSDLPAYDFDPASTDTIIDLLTSQYSNIQDANLLFCNTFDKLEGEIIQWMETLGRPVKTVGPTVPSAYLDKRVENDKHYGLSLFKPNEDVCLKWLDSKPSGSVLYVSYGSLVEMGEEQLKELALGIKETGKFFLWVVRDTEAEKLPPNFVESVAEKGLVVSWCSQLEVLAHPSVGCFFTHCGWNSTLEALCLGVPVVAFPQWADQVTNAKFLEDVWKVGKRVKRNEQRLASKEEVRSCIWEVMEGERASEFKSNSMEWKKWAKEAVDEGGSSDKNIEEFVAMLKQT
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Catalyzes the transfer of a glucose moiety to the C-3 hydroxyl of mogrol to form mogroside IE (PubMed:25759326, Ref.3). Besides mogrol, UGT74AC1 also shows activity in vitro with quercetin and naringenin as substrate.
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K7QHS5
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BCAT2_HUMLU
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Branched-chain amino acid aminotransferase 2, chloroplastic (HlBCAT2) (EC 2.6.1.42)
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MDCAAALLPGFHPNYLLCPSRHFSSLLPKTDLSSPLKFQLQNKQLSLASSHGFSPVICNATLSDTYSETVELADIDWDNLGFGFLPTDYMYNMKCAQGESFSNGELQRFGNIELSPSAGVLNYGQGLFEGLKAYRKEDGNILLFRPEENALRMRLGAERMCMPSPTVDQFVDAVKATVLANKRWIPPVGKGSLYIRPLLMGSGAVLGLAPAPEYTFLIYVSPVGNYFKEGVAPIHLIVEDNLHRATPGGTGGVKTIGNYAAVLKAQSAAKEQGYSDVLYLDCVHKKYLEEVSSCNIFVVKGNLIFTPAIKGTILPGITRKSIIDVARTLGFQVEERLVHVDELLDADEVFCTGTAVVVSPVGSITYHGERVPYNEGGVGAVSQQLYSALTRLQMGFIKDNMNWTVELS
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Converts 2-oxo acids to branched-chain amino acids. Shows no kinetic preferences corresponding to anabolic or catabolic functions, but likely involved in BCAA biosynthesis.
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K7QKH1
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BCAT1_HUMLU
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Branched-chain amino acid aminotransferase 1, mitochondrial (HlBCAT1) (EC 2.6.1.42)
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MIHRGLWLHNLVQSYRVGSSSSSSTLFKLVYRYNSSTSLAKSSLKQSCELSCKSNTEPSNMDWDKLGFKLMPTDYVYSMKCSNEGNFEQGRLELHGNIELSPAAAVLNYGQGIFEGTKAYRKEDGSLLLFRPDQNGVRMRIGAERMCMPSPSVDQFVDAVKQTAIANRRWVPPSGKGSLYIRPLLMGTGAVLGVAPAPQYTFLAYASPVGNYFKEGLAPLRLYVEDEFDRASPGGTGFVKTIGNYSRCLAALSRAKNKGFSDVLFLDSVHKKYVEELSSCNIFIVQGNQISTPAANGTILSGVTRSSIIEIARDHGFKVEERKIAVDELMEAEEVFCTGTAVGVASVGSITYHNKRVEFKTGSQSVSQKFYSTLIGIQTGVVEDKKGWIVEID
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Converts 2-oxo acids to branched-chain amino acids (BCAA). Shows no kinetic preferences corresponding to anabolic or catabolic functions, but likely involved in BCAA catabolism.
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K7QRJ5
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PYRE3_STRRG
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Dialkyldecalin synthase (EC 5.5.1.-) (FAD-dependent [4+2] cyclase)
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MSDTVIIAGGGPVGLMLACELGLAGVDTVVLERHDAPREPSRGGAINATVVELFTQRGIMESLRDDGFEFRMAHFAHIPLAPERVPGDRAFSFAVPHAQVERRLEERARSLGVRVRRSTEITSVRQTPDGVQVTTGDGEVVEGAYLVGCDGSASLVREQAGIPFPGVDPDFHGLWGDIKVEPGAPVLERIGARQYELGLCMVAPIGPDTVRVITGEFDVPSPPADQEVGFDELRAAVARIAGVELDGVPGWLSRWTATSRQAERYREGRILLAGDAAHTLFPLGGQALGTGIEDAVNLGWKLAATVQGWAPPSLLDSYHEERHAAGARACASTRAQTTIMRSLARVGELRALLTELAGLEEVNAYLVRMVGGIDGSRLPDVPLVTAEGETSVYRLLEAGRGVLLDLGAGLPAVRHPQVTYVRAEPTNRLDATAVLLRPDGVVAWRAPQDGLEAALETWFGPAA
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Involved in the biosynthesis of the spirotetramate antibiotics pyrroindomycins. Catalyzes the intramolecular cyclization forming the dialkyldecalin moiety in pyrroindomycins, via an endo-selective [4+2] cycloaddition reaction.
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K7QVW7
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PYRI4_STRRG
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Spiro-conjugate synthase (EC 5.-.-.-) ([4+2] cyclase PyrI4)
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MTTPQIDERAMEAGAAALQETIVDPGPLDVTALAVAAALAAGLHSAADDPAAALDKCIVLDELTEFAEKLVVHDRPGGIGTTVEYVEVYEDASGVRLGTATGNAVVLKMEPHMWQFHQSVSELADGSFEAVGVIDCTAMLRRMTQVLRVTGRSGRYAGKSGFMTLAISDPNQRPPHYSVQVVLC
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Involved in the biosynthesis of the spirotetramate antibiotics pyrroindomycins. Catalyzes the intramolecular cyclization forming the spiro-conjugate moiety in pyrroindomycins, via an exo-selective [4+2] cycloaddition reaction.
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K7TLS0
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MYB69_MAIZE
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MYB transcription factor 69 (ZmMYB69) (Myb-related protein 306)
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MGRPPCCDKAGVKKGPWTPEEDIVLVSYVQEHGPGNWRAVPVSTGLMRCSKSCRLRWTNYLRPGIRRGNFTPHEEGIIVHLQALLGNRWAAIASYLPQRTDNDIKNYWNTHLKKKLRKQQAIGAIFAPPRPSEPTAGHADCRRHDMTRSSKDSHAACPADSTPAADEVVTQLIAQQFAATDGDTSSSSSYSYASSTDNISKLLNGFMMKSASPARDDATDTIKTSSAIDIDPFDHKSGGAALPPPKKRQQQQHLSSIENWLFDDATEQLVVQLMEEISGGSCSVPMLLY
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Transcription factor that binds to the promoter of MYB31 and MYB42 and activates directly their expression, thus repressing lignin biosynthesis.
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K7U9N8
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OP1_MAIZE
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Protein OPAQUE1 (Myosin XI motor protein)
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MSYRKGLKVWVEEKGEGWVEAEVVEAKERAVVVFSSQRKKITVSPEKLLPRDTDEDLGGGHVDDMTKLTYLNEPGVLYNLKKRYALNEIYTYTGSILIAVNPFTRLPHLYNEYMMEQYKGIRLGELSPHVFAVADASYSRAMVNDSRSQSILVSGESGAGKTETTKLIMQYLTFVGGRAALDDRTVEQQVLESNPLLEAFGNAKTVRNDNSSRFGKFVEIQFDSSGRISGAAIRTYLLERSRVVQITDPERNFHCFYQLCASGKDAELYKLGHISSFHYLNQSNTHDLEGTNNEDEYWKTKRAMDIVGISREDQDAIFRTLAAILHLGNIEFVPGKDADSSKIKDSTSNFHLQTAAKLFMCDSDLLVSTLCSRSIHTREGIIVKALDCAAAAANRDALAKTVYARLFDWLVENINKSIGQDVDSKLQIGVLDIYGFESFKNNSFEQFCINFANEKLQQHFNEHVFKMEQEEYKSEEINWSYIEFIDNQDVLDLIEKKPIGIIALLDEACMFPKSTHETFATKMFRNFSSHLRLERTKFSETDFTISHYAGKVTYQTDSFLEKNRDYIVAEHCNLLSSSRCPFVSGLFTSLPEESIRSSYKFSSVASRFKLQLQALMETLNSTEPHYVRCVKPNSANRPQLFENQSVLHQLRCGGVLEAVRISLAGYPTRRTYAEFVDRFAVLVPELMIGSYDEKMMTKGILEKMKLENFQLGKTKVFLRAGQIAILDMRRAEILDNAARHIQGRFRTFITRKEFVKTREASISIQAYCRGCLARKMFANRRETAAAVIVQKYVRRWLLRRAHLQACLAALLIQSYIRGFIARRYFSVIREHKAATVIQSTWRRRKFVILFQNYRQATVAIQCSWRQKLARKELRKLKMAANEAGALREAKNKLEKKMDDLALRLTLERRLRASSEESKSVEILKRDKIIESLSAECAAAKSAAQNEHAKKLLLQKQLDDSLREITMLQSKKIMSAEAAEENSNLKNLVESLSTKNSILENELIVTRKSSDDTMEKLKEVEGKCNHLQQNLDKLQEKLTNLENENHVLRQKAFNMPTMNNLSVAPKTLSEKFSASIGLPNSEPKHIYESPTPTKYLASLPQTLSTSRRSRLPVERHEQNHEILLRCIKENLGYKDGKPVAACIIYKCLLHWRAFESERTAIFDHVIEAINDVLKGNEADGRLPYWLSNTSALLCLLQRNLRSNGLFTTPSRRSGGALGKIAQTLRSPSKFIGRSDTLPHVDARYPAILFKQQLTACVEKIFGQLRDNLKKEISPLLNVCIQAPKSTRGQSGKASKSSGVGAHPASNSNWDNIVNFLDLLMDTLRENYVPSFFIRKLITQLFSFINIQLFNSLLLRRECCTFSNGEYVKAGLSLLEKWITDVTDEFAGTSWHELNYIRQAVGFLVIHQKRKKTLEEIKQDLCPSLSVRQIYRICSMYWDDKYGTQGISTEVVAAMREMVNKDTQNLVSNSFLLDDDLSIPFSTEDLSMAIPSIDYADVDLPESLQHYTSVQFLLRQQDPQPAQ
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Myosin XI motor protein required for endoplasmic reticulum motility and protein body formation. May function by binding with its tail domain to receptor proteins on membranes and exerting force with its N-terminal motor domain against actin filaments, thereby transporting its cargo along polarized actin cables (By similarity).
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K7W9N9
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CPT6_SOLLC
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(2Z,6Z)-farnesyl diphosphate synthase CPT6, chloroplastic (EC 2.5.1.92) (Cis-prenyltransferase 6) (SlCPT6)
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MNSLFVGRPIVKSSYNVYTLPSSICGGHFFKVSNSLSLYDDHRRTRIEIIRNSELIPKHVAIIMDGNRRWAKARGLPVQEGHKFLAPNLKNICNISSKLGIQVITAFAFSTENWNRSSEEVDFLMRLFEEFFEEFMRLGVRVSLIGGKSKLPTKLQQVIELTEEVTKSNEGLHLMMALNYGGQYDMLQATKNIASKVKDGLIKLEDIDYTLFEQELTTKCAKFPKPDLLIRTGGEQRISNFLLWQLAYSELYFTNTLFPDFGEEALMDAIFSFQRRHRRFGGHTY
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Uses neryl diphosphate to catalyze the cis-prenyl chain elongation and produce the 15 carbon product (2Z,6Z)-farnesyl diphosphate.
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K7WDL7
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IRIS_CATRO
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(S)-8-oxocitronellyl enol synthase (EC 1.3.1.122) (Iridoid synthase) (ISY)
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MSWWWKRSIGAGKNLPNQNKENGVCKSYKSVALVVGVTGIVGSSLAEVLKLPDTPGGPWKVYGVARRPCPVWLAKKPVEYIQCDVSDNQETISKLSPLKDITHIFYVSWIGSEDCQTNATMFKNILNSVIPNASNLQHVCLQTGIKHYFGIFEEGSKVVPHDSPFTEDLPRLNVPNFYHDLEDILYEETGKNNLTWSVHRPALVFGFSPCSMMNIVSTLCVYATICKHENKALVYPGSKNSWNCYADAVDADLVAEHEIWAAVDPKAKNQVLNCNNGDVFKWKHIWKKLAEEFGIEMVGYVEGKEQVSLAELMKDKDQVWDEIVKKNNLVPTKLKEIAAFWFADIAFCSENLISSMNKSKELGFLGFRNSMKSFVSCIDKMRDYRFIP
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Iridoid synthase that catalyzes the first step in generation of the iridoid ring scaffold using the linear monoterpene (6E)-8-oxogeranial as substrate. Iridoids comprise a large family of distinctive bicyclic monoterpenes that possess a wide range of pharmacological activities, including anticancer, anti-inflammatory, antifungal and antibacterial activities.
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K7WIZ6
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RIBRX_MAIZE
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Riboflavin biosynthesis protein PYRR, chloroplastic [Includes: Inactive diaminohydroxyphosphoribosylaminopyrimidine deaminase (DRAP deaminase) (Riboflavin-specific deaminase); 5-amino-6-(5-phosphoribosylamino)uracil reductase (EC 1.1.1.193) (HTP reductase); Riboflavin biosynthesis intermediates N-glycosidase (EC 3.2.2.-)]
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MPLPQPLLGGASPAPARAASSFLHPLLHTRHRVSTAPAAASSFVPASHSSHANDAMLLRRAADVADRSAGLTSPHPNFGCVIARPQLNTDSADSWVVGEGFLYAQGTPCAELLASQEAGEHARGGTAYLNLEPGDCFGDNTAVGSLVQAGITRVVVGLRHPLKHLRGKAIQALRNEGIQVDVVGEDLQSKLFKEALKSCLTVNAPLLYRAAFHVPFSVLKYAMTADGKIAASSGHASWISGKASRGRVFELRGRSDAVIVGGNTVRFDDPRLTARHVKGHVPVRIVMSQSLNLPEEANLWNLNDAYTIVATQRGARRDFQRKLAMKGVEVVEFDMLNPRAVMSYCYDRGYLAVLWECGGTLAASAISASVIHKVYAFWAPKIIGGLNAPTPVGELGMSQMTQAINLIDVSYEQIDRDMLMSGFIEPIPDLSPVIPSVEEIPSIDPEVSPYETNIISFYKTWDIFGAFSNFSPHSIQMPDENGDYFTWPTVEHYYQAHKFVGVDNPQARDIVQEIKLAKSPEEAARIGRTRQKGFPELVRTDWESTKIDVMYRAIKCKFSTYPHLTNMLLSTAGSVLVEASPHDLFWGGGREGEGLNYLGRLLMQLRSEILGTVPASAEVGEAD
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Pyrimidine reductase involved in the riboflavin biosynthesis pathway. Has also a non-functional N-terminal deaminase domain that lacks the catalytically essential zinc-binding residues. 39% activity when NADH replaces NADPH. No evidence for a phosphatase activity conferred by the N-terminal domain. Catalyzes the hydrolysis of the N-glycosidic bond in the first two intermediates of riboflavin biosynthesis, which are highly reactive metabolites, yielding relatively innocuous products. Thus, can divert a surplus of harmful intermediates into relatively harmless products and pre-empt the damage these intermediates would otherwise do. Has no activity against GTP, nucleoside monophosphates or ADP-ribose.
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K7WQ45
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CPT2_SOLLC
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Nerylneryl diphosphate synthase CPT2, chloroplastic (EC 2.5.1.142) (Cis-prenyltransferase 2) (SlCPT2)
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MNSSIVSQHFFISLKSSLDLQCWKSSSPSSISMGEFKGIHDKLQILKLPLTMSDRGLSKISCSLSLQTEKLRYDNDDNDDLELHEELIPKHIALIMDGNRRWAKAKGLEVYEGHKLIIPKLKEICDISSKLGIQVITAFAFSTENWKRSKEEVDFLMQLFEEFFNEFLRFGVRVSVIGCKSNLPMTLQKCIALTEETTKGNKGLHLVIALNYGGYYDILQATKSIVNKAMNGLLDVEDINKNLFEQELESKCPNPDLLIRTGGEQRVSNFLLWQLAYTEFYFTNTLFPDFGEKDLKKAILNFQQRHRRFGGHTY
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Uses dimethylallyl diphosphate and isopentenyl diphosphate to catalyze the cis-prenyl chain elongation and produce the 20 carbon product nerylneryl diphosphate.
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K7ZP88
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ATAA_ACIS5
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Trimeric autotransporter adhesin AtaA (TAA AtaA) (Type 5 secretion system autotransporter AtaA)
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MNKIYKVIWNATLLAWVAVSELAKGKTKSTTSKSKAKSLSSSVIVGGIILTTPLSLIAATVQVGGGTNSGTTATASTNCADLYNYQNPENSGSGAAGNYNAGNPSVCSIAIGENAQGGTSGTGGSPGIAIGGNSKATGGLSVAIGGYAQATNVGSIALGTAALSSGFNSLAISRQAAATNNYSIAIGTTSVSKGVGSIAMGHSTNASGDQSIAIGSSDAVNSATATTTYDGTTNTQASGSKSIAIGASAKASTNNSIALGAGSVTSAQSGNSYLTGVGASATNGVVSVGTSTATRRIQNVADGSAASDAVTVAQLDKAYDDTNGRLAAALGTGSGAAYNAANNTYTAPTNIGGTGKNTIDDAIKATQRSVVAGSNIVVTPTTASDGSISYSVATSATPTFTSITVNNAPTAGTDATNKTYVDSKAAASRTEVAAGSNVSGVVKTTGANGQDVYTVNANGTTASAGSSAVTVTPGTKDANNVTDYKVDLSATTKTDIQKGVDAKNAVDTAGLKFKGDTATTSNTKKLGDTVSITGDTNISTVATTDGVQVKLNPNLDLGATGSVKTGNTTINNAGVTADQVTVGGVVINNTSGINAGGKAITNVAAPTNNTDAANKKYVDDAGTALTNLGFGLKAQDGTTVNKKLGEAVDIVGSNSNISTKVNAGKVEVALSNTLDLGTTGSVTTGSTVINNAGVTATQVTANKVTINNAPTAGTDATNKTYVDSKAAASRTEVAAGSNVSGVVKTTGANGQDIYAVNANGTTASAGSSAVTVTPGTKDANNVTDYKVDLSATTKTDIQKGVDAKNAVDTAGLKFKGDTATTSNTKKLGDTVSITGDTNISTVATTDGVQVKLNPNLDLGATGSVKTGNTTINNAGVTADQVTVGGVVINNTSGINAGGKAITNVAAPTNNTDAANKKYVDDAGTALTNLGFGLKAQDGTTVNKKLGEAVDIVGSNSNISTKVNAGKVEVALSNTLDLGTTGSVTTGSTVINNAGVTATQVTANKVTVNNAPTAGTDATNKTYVDSKAAASRTEVAAGSNVSGVVKTTGANGQDVYTVNANGTTASAGSSAVTVTPGTKDANNVTDYKVDLSATTKTDIQKGVDAKNAVDTAGLKFKGDTATTSNTKKLGDTVSITGDTNISTVATTDGVQVKLNPNLDLGATGSVKTGNTTINNAGVTADQVTVGGVVINNTSGINAGGKAITNVAAPTNNTDAANKKYVDDAGTALTNLGFGLKAQDGTTVNKKLGEAVEVVGADSNITTKVAGGQVAIELNKNLNNLTGITVNDGTNGTNGSTVIGKDGISVKDGSGNTIAGVDNTALTVKDGSGNTETSINQAINTLNAAQGETDKFAVKYDKNADGSVNYNNITLAGTTASSTQDATTGKITTTGGTSLNNVASAGDYKDVANASKGVNAGDLNNAVVDATNAATSKGFALQAADGAKVQKNLGEAVEVVGADSNITTKVAGGQVAIELNKNLNNLTGITVNDGTNGTNGSTVIGKDGISVKDGSGNTIAGVDNTALTVKDGSGNTETSINQAINTLNAAQGETDKFAVKYDKNTDGSTNYNSITAGNGNGTAATIGTDTAGNSVVTSGGTKISNVANGVNASDAVNKGQLDSLSTGLTNTGFGLKAADGNTVNKKLGEAVDVVGADSNITTKVAGGQVAIELNKNLNNLTGITVNDGTNGTNGSTVIGKDGISIKDGSGNTIAGVDNTALTVKDGSGNTETSINQAINTLNAAQGETDKFAVKYDKNADGSANYNNITLAGTTASSTQDATTGKITTTGGTSLNNVASAGDYKDVANASKGVNAGDLNNAVVDATNAATSKGFALQAADGAKVQKNLGEAVEVVGADSNITTKVVGGQVAIELNKNLNNLTGITVNDGTNGTNGSTVIGKDGISVKDGSGNTIAGVDNTALTVKDGSGNTETSINQAINTLNAAQGETDKFAVKYDKNADGSVNYNNITLAGTTASSTQDATTGKITTTGGTSLNNVASAGDYKDVANASKGVNAGDLNNAVVDATNAATSKGFALQAADGAKVQKNLGEAVEVVGADSNITTKVAGGQVAIELNKNLNNLTGITVNDGTNGTNGSTVIGKDGISVKDGSGNTIAGVDNTALTVKDGSGNTETSINQAINTLNAAQGETDKFAVKYDKNADGSVNYNNITLAGTTASSTQDATTGKITTTGGTSLNNVASAGDYKDVANASKGVNAGDLNNAVVDATNAATSKGFALQAADGAKVQKNLGEAVEVVGADSNITTKVAGGQVAIELNKNLNNLTGITVNDGTNGTNGSTVIGKDGISVKDGSGNTIAGVDNTALTVKDGSGNTETSINQAINTLNAAQGETDKFAVKYDKNADGSANYNNVTLAGTNGTIISNVKAGAVTSTSTDAINGSQLYGVANSVKNAIGGSTTIDATTGAITTTNIGGTGSNTIDGAISSIKDSATKAKTTVSAGDNVVVTSGTNADGSTNYEVATAKDVNFDKVTVGSVVVDKSSNTIKGLSNTTWNGTAVSGQAATEDQLKTVSDAQGETDKFAVKYDKNADGSANYNSITAGNGNGTAATIGTDTAGNSVVTSGGTKISNVANGVNASDAVNKGQLDSLSTGLTNTGFGLKAADGNTVNKKLGEAVDVVGADSNITTKVAGGQVAIELNKNLNNLTGITVNDGTNGTNGSTVIGKDGISIKDGSGNTIAGVDNTALTVKDSSGNTETSINQAINTLNAAQGETDKFAVKYDKNADGSVNYNNVTLAGTNGTIIRNVKAGAVTSTSTDAINGSQLYDIANSVKNAIGGSTTRDVTTGAITTTNIGGTGSNTIDGAISSIKDSATKAKTTISAGDNVVVTSGTNADGSTNYEVATAKDVNFDKVTVGNVVVDKANDTIQGLSNKDLNSTDFATKGRAATEEQLKAVITSNITEVVDGNGNKVNIIDQVVNTKPDNKNQDSLFLTYDKQGQETTDRLTIGQTVQKMNTDGIKFFHTNADTSKGDLGTTNDSSAGGLNSTAIGVNAIVANGADSSVALGHNTKVNGKQSIAIGSGAEALGNQSISIGTGNKVTGDHSGAIGDPTIVNGANSYSVGNNNQVLTDDTFVLGNNVTKTIAGSVVLGNGSAATTGAGEAGYALSVATNADKAAITKTTSSTGAVAVGDASSGIYRQITGVAAGSVDSDAVNVAQLKAVGNQVVTTQTTLVNSLGGNAKVNADGTITGPTYNVAQGNQTNVGDALTALDNAINTAATTSKSTVSNGQNIVVSKSKNADGSDNYEVSTAKDLTVDSVKAGDTVLNNAGITIGNNAVVLNNTGLTISGGPSVTLAGIDAGNKTIQNVANAVNATDAVNKGQLDSAINNVNNNVNELANNAVKYDDASKDKITLGGGATGTTITNVKDGTVAQGSKDAVNGGQLWNVQQQVDQNTTDISNIKNDINNGTVGLVQQAGKDAPVTVAKDTGGTTVNVAGTDGNRVVTGVKEGAVNATSKDAVNGSQLNTTNQAVVNYLGGGAGYDNITGSFTAPSYTVGDSKYNNVGGAIDALNQADQALNSKIDNVSNKLDNAFRITNNRIDDVEKKANAGIAAAMALESAPYVPGKYTYAAGAAYHGGENAVGVTLRKTADNGRWSITGGVAAASQGDASVRIGISGVID
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Responsible for autoagglutination, and for adhesion to abiotic and biotic surfaces such as polystyrene (PS), type I collagen, polypropylene (PP), polyvinylchloride (PVC), glass and stainless steel (SS). Adhesion is much stronger than that mediated by Yersinia YadA in a comparative assay. Confers autoagglutination and binding to PS, type I collagen, PP, PVC, glass and SS upon expression in Acinetobacter baylyi strain ADP1. Involved in rapid, irreversible adherence to polyurethane. Forms an unusual biofilm. An extended, surface exposed fiber binds to quartz crystals, PS and glass. It can be removed by washing in distilled water.
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K8DWB5
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CA1D_CONTE
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Alpha-conotoxin TxID (Alpha-conotoxin TxIC)
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FDGRNAAGNDKMSALMALTTRGCCSHPVCSAMSPICG
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Alpha-conotoxins act on postsynaptic membranes, they bind to the nicotinic acetylcholine receptors (nAChR) and thus inhibit them. This toxin inhibits alpha-3-beta-4/CHRNA3-CHRNB4 (IC(50)=3.6-18.38 nM), alpha-6/alpha-3-beta-4 (CHRNA6/CHRNA3-CHRNB2-CHRNB4) (IC(50)=33.9-94.1 nM), and alpha-2-beta-4/CHRNA2-CHRNB4 (IC(50)=4550 nM) nAChRs. The toxin competes with agonists in the orthosteric binding site of alpha-3-beta-4/CHRNA3-CHRNB4 and alpha-6-beta-4/CHRNA6-CHRNB4.
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K8ERR8
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LSY12_CAEEL
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Histone acetyltransferase lsy-12 (EC 2.3.1.48)
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MGKKRKPSPERSSDEDEVSTPSPKDRTARPTAAARRENVALSQAVALSLEDASNFCSLAFSLERIKREPVDTDYDDPNQPGPSSVPVSARTDHVLPIRFKIKAEPQEYDSDEYGKDHGAVQIANKEVPAISPIEEVSQKRRGRPRKTDAAQHLFFPHVSIKQEPDDGFINFHESRCVGIAQDPEMQHLHDVNESHSSEIAIFRETKKITERKKKKTEAEKLWDNMSLTEKEVFQSHTRRRRTTRLPIIQNFEETEEGCIVEVPIPLIDLDNDAVESVTGPQHENVTVSENVLSTESTDQEVTETKRLHDSSRDFNPPRIQDTPSTVIRPEGDQKDPMSSTSSKRRNTNNSRCASLLSNPHSTPVTRLMRGILDSENSDNDEMLSNDQSEIAKRPRTPRPRYSPEAQRRTNSRLSALTIDTNRSNDLNVDGSAPSSSSAASCGLSTPDPDRTSQQRRKGNQSAARSRKIKTPSPPLSQEDEPMELDSDDDPVNELDNLPIVIDDPSYVLTKEHKEIFEQVKKSVSDRNEFSPAQISEIYRSSKGEQARLPERIHFGAFIMKTWYGSPFPAEFINVKKLFICEFCFFYARSDEIMQNHAKKCMLRAPPGLEIYRKGDISVFEVDGRLQKEYCQTLCLVSRMFLESKTVFYDTEPFFFYIVTINDDIGCHFAGYFSKEKYEPDVNNLSCIMTLPCYQEMGLGRFLIDISYALSRKEKWFGGPEQPLSELGRKAYGGYWRTTIASCLGRLKDELEFGSGISIKMIADDTGVNCHDILEVVCSLGWAKPVDPDEKNHYKLEWDVDWDMVSIILRESEASKETKVQYDPECLDWVPRKMRPSMDGYHELSKEEIEQDEQRRKSIQKTPVHVSMEKATPTSTTSLPVGSVKKELRSRGHNRSVGRNLKHEVNRKVKVPEWAAARDLTDEEITVEENKKQQKQNRKIFTRCADSVLDKSNIREETPEDDEPGPSTKPSGKRQRGNKCNNTESEPNPSGRKTSATSSGRGKYRNRRTDGTEEEEEDDDPTDSEPLTTDDEKPFETSVNKEKNEKSRRGKKVSKKRRSVAGKKFPPNFGVRDRDEPKKAENSEDGEGLESKPGPSTEMILVEKVEEEEAKVTVSDINMQASESKIEGIEQTSEVDIPKSDEDHQSTEAYDRVEDEVPITDYNIPTPDSYHSSPPHSPTPSPQPQLMQAQQNIYQDNDCHFAENDSKPPHLVSEVDDPAAPQPTVTLQSGPSDAPPLSHNSVDGYSTGDDDAPPNLSPQIGKSENNEEEMPLIAPIVQHNGITHHEESTAQHYHDSMNAGPSTSSHVTPQMSMINTTPQQPPFSHPNSQQQATPGSGGVPSCGPAYTHHTPEQQSQQFMSPPMAGMPASVASNHSIHNSNSIEMVGGPASLQHTPQQYEMGHSMAQMSQESAIGGINTVPSIEQQNQLMLQHHQFSSPPAAPPPSQQQQVVQPPIPPAPTTANGRRRSESAATQRTKARQQHQHQQQQPQQPQQRIAAPGVPQGVHPQMQFPMNAMNMMPAYPPFYPYTNYPNIWQPPYQNYPYNQVDYQQPWLYNNGHIPHQTNGTATNQFHPGHMGYFPNNNGR
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Probable histone acetyltransferase (Probable). Required to initiate and then maintain lateralized gene expression in the ASE sensory neurons. Involved in determining cell fate in the ASE neurons.
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K8ESC5
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ATG41_CAEEL
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Cysteine protease atg-4.1 (EC 3.4.22.-) (Autophagy-related protein 4 homolog 1)
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MLSILPLAYSNFSRILQYFEQLPVVDKMTEEILKQGVGIVETSLTFEPPFCESFERISIDNFPIFALGKEISKEDGIEAMKKYVTSRFWFTYRRDFSPIGGTGPSTDQGWGCMLRCAQMLLGEVLLRRHIGRHFEWDIEKTSEIYEKILQMFFDEKDALYSIHQIAQMGVTEGKEVSKWFGPNTAAQVMKKLTIFDDWSNIAVHVALDNILVKEDAITMATSYPSEDAVKLIMENGLVDKNRLSLSPGNIIPEWRPLLLMIPLRLGLTTINPCYLSAIQEFFKIPQCVGIIGGRPNHALYFVGMSGSKLFYLDPHYCRPKTESTAKMYAEKDSTATTDDVGFSHLEELVPLPSQTADVYTKMDDSTYHCQMMLWIEYENVDPSLALAMFCETRDEFENLCETLQKTTLPASQPPMFEFLQRRPKYLPKFEPYTGVSMKIEMKEFDDIGAANVKIDDDFEVLDVHTEEEDADEDNDDDVANA
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Cysteine protease required for autophagy. Cleaves the C-terminal amino acid of ATG8 family proteins lgg-1, to reveal a C-terminal glycine. Exposure of the glycine at the C-terminus is essential for ATG8 proteins conjugation to phosphatidylethanolamine (PE) and insertion to membranes, which is necessary for autophagy (Probable). Its cleavage activity is functionally redundant to atg-4.2, but it cleaves lgg-1 precursors more efficiently than atg-4.2 (Probable). Acts redundantly with atg-4.2 to promote the lgg-1 delipidation to release the protein from membranes, which facilitates multiple events during macroautophagy. Unlike atg-4.2 does not seem to be required for autophagosome maturation.
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K8FE10
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SYT2_CAEEL
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Synaptotagmin 2
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MWATGAIVCSPVFRILSTCCPIRRGVPTSNGYHPRPKHVDIGNGAVPILSSKPITVQPTNSDYYEPVNNGTLPLSSSGALIKQYGNIHFRVEYDFEQSKLSVTIVSASDLPAMDRNGMSDPYVKVYVLPERKQKFETRIIRNTLNPTYNETFQFSIPFNELHSKTLMLVVYDYDRLSKDDKMGQLSVPLESIDFGITTDIERPLQKPEKDDEKECRLGDICFSTRYRPATGTVTLTIMEARNLKKMDVGGSSDPYVKIYLHHGRKLLSKKKTSRKYKTLNPYYNESFQFKIEPHMIEKVHLIVSVWDYDKMSKNDFIGEVTLGSKHLNLPQITHACSEQWAEMMTSRRPVVQWHTLQERMEKEKKKDDD
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Ca(2+) sensor involved in Ca(2+)-dependent secretion of the nlp-40 neuropeptide from intestinal cells. Involved in the defecation motor program, which is a coordinated series of three muscle contractions that occurs every 45 seconds.
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K9IMD0
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TRLF_DESRO
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Lactotransferrin (Lactoferrin) (EC 3.4.21.-) (Draculin) (Draculin-1)
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MKLLFLALLSLLALGPSLAARRRGVRWCTISKPEAAKCSKLQQNLKRVRGPSLSCISRKSYLECIQAIAAKRADAMSLDAGLVYEAGQDPYRLRPVAAEVYGTEGAPRTHYYAVALVKKDSNLQLNQLQGVRSCHTGLNRSAGWKIPVGTLRPYLGWAGPPAPLQEAVANFFSASCVPCADGNQYPNLCRLCAGTGADKCACSSKEPYFGYSGAFKCLKDGAGDVAFVKDSTVFENLPNKAERDQYELLCPDNTRKPVDEFEQCHLARVPSHAVVARSVGGKEDSIWRLLSKAQEKFGKGTSGSFQLFSSPPGQKDLLFKDGAQGFLRIPSRVDAELYLGPSYLTVIKNLKESAAEVEARGARVVWCAVGPEELRKCQQWSGQSNGTVTCTTAADTEDCIALVLKGEADAMSLDGGVIYIAGKCGLAPVLAESQRSEGGSNLDCVNRPLEGDRAVAVVRKSSAGLTWNSRRGTKSCHTAVGRTAGWNIPMGLLFNQTRSCNFDEFFSQSCAPGADPNSNLCALCVGNEQGQDKCAPNSNERYFSYAGSFRCLVENAGDVAFVKASTVLENPDGRGTEAWAKDLKLEDFELLCLDGTRKPVSEFETCHLARAPSHGVVSRKDRVQYLEQVLLDQQGKFGRNGPLCPGKFCLFQSETKNLLFNDNTECLAKLQGKTTYEKYLGPEYVTAVANLRQCSTSPLLEACTFLRN
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Transferrins are iron binding transport proteins which can bind two Fe(3+) ions in association with the binding of an anion, usually bicarbonate. [Lactotransferrin]: Major iron-binding and multifunctional protein found in exocrine fluids such as breast milk and mucosal secretions. Has antimicrobial activity. Antimicrobial properties may include bacteriostasis, which is related to its ability to sequester free iron and thus inhibit microbial growth, as well as direct bactericidal properties leading to the release of lipopolysaccharides from the bacterial outer membrane. May have anabolic, differentiating and anti-apoptotic effects on osteoblasts and may also inhibit osteoclastogenesis, possibly playing a role in the regulation of bone growth. May interfere with the lipopolysaccharide (LPS)-stimulated TLR4 signaling. The lactotransferrin transferrin-like domain 1 functions as a serine protease of the peptidase S60 family that cuts arginine rich regions. This function contributes to the antimicrobial activity. Shows a preferential cleavage at -Arg-Ser-Arg-Arg-|- and -Arg-Arg-Ser-Arg-|-, and of Z-Phe-Arg-|-aminomethylcoumarin sites.
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K9JHZ4
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TET3B_XENLA
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Methylcytosine dioxygenase tet3-B (EC 1.14.11.80)
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METQPASVPCVLPQDVYEFSEDRESLGRLRVSEMPSELNGGGDGSKGDGAAVVATEVSQQSNKKRKRCGVCVPCLRKEPCGTCYNCVNRSTSHQICKMRKCEQLKKKRVVPMKGVEAVDKDDAKNQAKEQVPSVKNCSESILVDGPKTDQMEAGPVNHVQEGRLKQECDSTLPSKGSEDLANQLLMEANSWLSNTAAPQDPCNKLNWDKPIIPNHIAANNNSNLEDAKNLVAFSAVAEAMSNYGMPASGTPSSISMQLYEKFNYETNQDNSGHSEGNAPSCPEDLNTLKEALALAKHGVKPPNCNCDGPECPDYLEWLENKIKSTGKGSQESPFPSLGQVSKKLVQKSYHKEQVLNLENTNVTCPSGNLPFSQNALSLAKEKNISLQTAIAIEALTQLSSALPQTNNEYPNAPSQPLINHNDQLTHFPTAKGNQLPMLPLSCNELFQNQQAQLYTGKNALPVPQSPRQASWEQNKKPGYQESEYIPENLSQSSSVLPSDASTPQKKEFLQQWVQNADLLKSPSDPMTGLKQLLGNTDEYIKSAFKGPEGLSKKIKNVKSKHTIKSIKKESADFTKMSPDQQLSQLLQGNDFHRNTQAALQQHLHHKRNLFVDSNTMEACTQEQQNWWVPNSQQAPVSKTTEKPVKERKKRRQSPSQKQVEPKPKPPRKQVQIKKPRVKEGNAVFMPVSQISLDSFRRVEKEENQVKELDLENSLPINVQPDLLGSQSIQLTGSQANLENQKTVNTQETCNENQTSIGKANNFALCVNKTNSLVAKGRCPTPSTGDSSSGQGDSANQHTNLTDVPGQNDLSCIDDKFEDLIKQFAAEFGEDFSLPGSEVPSQNGERPPKQQTSGVPQFKMPFPSQLPSENATHSNPALSNNLLTHNASHKFDSLFSSKSPKQIKIESSGAITVVSTTCSYSEENQHLDGTPTKSELPFNPTLSGFLESPLKYLTSPTKSLIDTPAKMAQAEFPTCDCVEQINEKDEGPYYTHLGSGPTVASIRELMEERFGEKGEAIRIEKVIYTGKEGKSSRGCPIAKWVIRRQSEDEKLMCLVRQRAGHHCENAVIIILIMAWEGIPRALGDSLYDDISGTITKYGNPTSRRCGLNDDRTCACQGKDPNTCGASFSFGCSWSMYFNGCKYARSKTPRKFRLIGDNPKEEEFLKDSFQDLATKVAPVYKMLAPQAYQNQANNEDVAIDCRLGLEEGRPFSGVTACMDFCAHAHKDQHNLYNGCTVVCTLTKEDNRMIGKIAEDEQLHVLPLYKVSTTDEFGSEERQLEKIRKGGIQVLSSFPREVRKLSEPAKSCRQRQLDAKKATAEKKKLQKEKLVSPDKTKQEPSDTKTCQQNPGVPQQQTKPCVKVEPSNHYNTFKYNGNGVVESYSVLGSCRPSDPYSMNSVYSYHSFYAQPNLPSVNGFHSKFALPPFGFYSFPNNPVVPNQFMNYGTGDARNSGWMNNSFEKKPELQSLADGMNQSYGSELPEQNYRRSSEVPHHYSLQNSNSQKSVGVPHRTTPAPMETTPYSNVPCYNKVIKKEPVCDPLVDPFQRSNSVHSQSPGVNHSLQTNDLSYKANGALPSSGRTNKEGPCSMFLPSDKNGLEKRDYFGVHSNVPGLKEKQWTPYGIDVPVGQRDSLDSQCSGKVWSSCKLSDSPAVMPSTVQDKNWTGRQASLNQGVKEPMPFQEKLWNSVAASGRCSTTPNDRSSVTPCAELQDKNWMSFPNPAVNSLKTDSSQNHWDPYSLDDNMDDGQSKSVKEEEDEEEIWSDSEHNFLDGNIGGVAVAPGHGSILIECARRELHATTPLKKPNRCHPTRISLVFYQHKNLNQPNHGLALWEAKMKQLAERARVKEEEAAKLGIKQEVKSLGKKRKWGGAATTETPPVEKKDFIPTRQAATSLTDSTTTAFSYAYTKVTGPYSRFI
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Dioxygenase that catalyzes the conversion of the modified genomic base 5-methylcytosine (5mC) into 5-hydroxymethylcytosine (5hmC) and plays a key role in epigenetic chromatin reprogramming during embryonic development. Conversion of 5mC into 5hmC probably constitutes the first step in cytosine demethylation. Selectively binds to the promoter region of target genes and contributes to regulate the expression of numerous developmental genes, including pax6, rax, sox9 and six3. May also contribute to the regulation of target genes in ways that do not require its enzyme activity.
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K9M1U5
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IFNL4_HUMAN
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Interferon lambda-4 (IFN-lambda-4)
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MRPSVWAAVAAGLWVLCTVIAAAPRRCLLSHYRSLEPRTLAAAKALRDRYEEEALSWGQRNCSFRPRRDPPRPSSCARLRHVARGIADAQAVLSGLHRSELLPGAGPILELLAAAGRDVAACLELARPGSSRKVPGAQKRRHKPRRADSPRCRKASVVFNLLRLLTWELRLAAHSGPCL
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Cytokine that may trigger an antiviral response activating the JAK-STAT pathway and up-regulating specifically some interferon-stimulated genes.
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K9N4V7
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NCAP_MERS1
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Nucleoprotein (Nucleocapsid protein) (NC) (Protein N)
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MASPAAPRAVSFADNNDITNTNLSRGRGRNPKPRAAPNNTVSWYTGLTQHGKVPLTFPPGQGVPLNANSTPAQNAGYWRRQDRKINTGNGIKQLAPRWYFYYTGTGPEAALPFRAVKDGIVWVHEDGATDAPSTFGTRNPNNDSAIVTQFAPGTKLPKNFHIEGTGGNSQSSSRASSVSRNSSRSSSQGSRSGNSTRGTSPGPSGIGAVGGDLLYLDLLNRLQALESGKVKQSQPKVITKKDAAAAKNKMRHKRTSTKSFNMVQAFGLRGPGDLQGNFGDLQLNKLGTEDPRWPQIAELAPTASAFMGMSQFKLTHQNNDDHGNPVYFLRYSGAIKLDPKNPNYNKWLELLEQNIDAYKTFPKKEKKQKAPKEESTDQMSEPPKEHRVQGTQRTRTRPSVQPGPMIDVNTD
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Packages the positive strand viral genome RNA into a helical ribonucleocapsid (RNP) and plays a fundamental role during virion assembly through its interactions with the viral genome and membrane protein M. Plays an important role in enhancing the efficiency of subgenomic viral RNA transcription as well as viral replication. {ECO:0000255|HAMAP-Rule:MF_04096}.
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K9N5Q8
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SPIKE_MERS1
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Spike glycoprotein (S glycoprotein) (E2) (Peplomer protein) [Cleaved into: Spike protein S1; Spike protein S2; Spike protein S2']
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MIHSVFLLMFLLTPTESYVDVGPDSVKSACIEVDIQQTFFDKTWPRPIDVSKADGIIYPQGRTYSNITITYQGLFPYQGDHGDMYVYSAGHATGTTPQKLFVANYSQDVKQFANGFVVRIGAAANSTGTVIISPSTSATIRKIYPAFMLGSSVGNFSDGKMGRFFNHTLVLLPDGCGTLLRAFYCILEPRSGNHCPAGNSYTSFATYHTPATDCSDGNYNRNASLNSFKEYFNLRNCTFMYTYNITEDEILEWFGITQTAQGVHLFSSRYVDLYGGNMFQFATLPVYDTIKYYSIIPHSIRSIQSDRKAWAAFYVYKLQPLTFLLDFSVDGYIRRAIDCGFNDLSQLHCSYESFDVESGVYSVSSFEAKPSGSVVEQAEGVECDFSPLLSGTPPQVYNFKRLVFTNCNYNLTKLLSLFSVNDFTCSQISPAAIASNCYSSLILDYFSYPLSMKSDLSVSSAGPISQFNYKQSFSNPTCLILATVPHNLTTITKPLKYSYINKCSRFLSDDRTEVPQLVNANQYSPCVSIVPSTVWEDGDYYRKQLSPLEGGGWLVASGSTVAMTEQLQMGFGITVQYGTDTNSVCPKLEFANDTKIASQLGNCVEYSLYGVSGRGVFQNCTAVGVRQQRFVYDAYQNLVGYYSDDGNYYCLRACVSVPVSVIYDKETKTHATLFGSVACEHISSTMSQYSRSTRSMLKRRDSTYGPLQTPVGCVLGLVNSSLFVEDCKLPLGQSLCALPDTPSTLTPRSVRSVPGEMRLASIAFNHPIQVDQLNSSYFKLSIPTNFSFGVTQEYIQTTIQKVTVDCKQYVCNGFQKCEQLLREYGQFCSKINQALHGANLRQDDSVRNLFASVKSSQSSPIIPGFGGDFNLTLLEPVSISTGSRSARSAIEDLLFDKVTIADPGYMQGYDDCMQQGPASARDLICAQYVAGYKVLPPLMDVNMEAAYTSSLLGSIAGVGWTAGLSSFAAIPFAQSIFYRLNGVGITQQVLSENQKLIANKFNQALGAMQTGFTTTNEAFHKVQDAVNNNAQALSKLASELSNTFGAISASIGDIIQRLDVLEQDAQIDRLINGRLTTLNAFVAQQLVRSESAALSAQLAKDKVNECVKAQSKRSGFCGQGTHIVSFVVNAPNGLYFMHVGYYPSNHIEVVSAYGLCDAANPTNCIAPVNGYFIKTNNTRIVDEWSYTGSSFYAPEPITSLNTKYVAPQVTYQNISTNLPPPLLGNSTGIDFQDELDEFFKNVSTSIPNFGSLTQINTTLLDLTYEMLSLQQVVKALNESYIDLKELGNYTYYNKWPWYIWLGFIAGLVALALCVFFILCCTGCGTNCMGKLKCNRCCDRYEEYDLEPHKVHVH
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[Spike protein S1]: Attaches the virion to the cell membrane by interacting with host receptor, initiating the infection (By similarity). Interacts with host DPP4 to mediate virla entry. {ECO:0000255|HAMAP-Rule:MF_04099, ECO:0000269|PubMed:23486063}. [Spike protein S2]: Mediates fusion of the virion and cellular membranes by acting as a class I viral fusion protein. Under the current model, the protein has at least three conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During viral and target cell membrane fusion, the coiled coil regions (heptad repeats) assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and target cell membranes. {ECO:0000255|HAMAP-Rule:MF_04099}. [Spike protein S2']: Acts as a viral fusion peptide which is unmasked following S2 cleavage occurring upon virus endocytosis. {ECO:0000255|HAMAP-Rule:MF_04099}.
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K9N638
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R1A_MERS1
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Replicase polyprotein 1a (pp1a) (ORF1a polyprotein) [Cleaved into: Host translation inhibitor nsp1 (nsp1) (Leader protein); Non-structural protein 2 (nsp2) (p65 homolog); Papain-like protease nsp3 (PL-PRO) (EC 3.4.19.12) (EC 3.4.22.-) (Non-structural protein 3) (nsp3) (PL2-PRO); Non-structural protein 4 (nsp4); 3C-like proteinase nsp5 (3CL-PRO) (3CLp) (EC 3.4.22.69) (nsp5); Non-structural protein 6 (nsp6); Non-structural protein 7 (nsp7); Non-structural protein 8 (nsp8); RNA-capping enzyme subunit nsp9 (Non-structural protein 9) (nsp9) (EC 2.7.7.50); Non-structural protein 10 (nsp10) (Growth factor-like peptide) (GFL); Non-structural protein 11 (nsp11)]
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MSFVAGVTAQGARGTYRAALNSEKHQDHVSLTVPLCGSGNLVEKLSPWFMDGENAYEVVKAMLLKKEPLLYVPIRLAGHTRHLPGPRVYLVERLIACENPFMVNQLAYSSSANGSLVGTTLQGKPIGMFFPYDIELVTGKQNILLRKYGRGGYHYTPFHYERDNTSCPEWMDDFEADPKGKYAQNLLKKLIGGDVTPVDQYMCGVDGKPISAYAFLMAKDGITKLADVEADVAARADDEGFITLKNNLYRLVWHVERKDVPYPKQSIFTINSVVQKDGVENTPPHYFTLGCKILTLTPRNKWSGVSDLSLKQKLLYTFYGKESLENPTYIYHSAFIECGSCGNDSWLTGNAIQGFACGCGASYTANDVEVQSSGMIKPNALLCATCPFAKGDSCSSNCKHSVAQLVSYLSERCNVIADSKSFTLIFGGVAYAYFGCEEGTMYFVPRAKSVVSRIGDSIFTGCTGSWNKVTQIANMFLEQTQHSLNFVGEFVVNDVVLAILSGTTTNVDKIRQLLKGVTLDKLRDYLADYDVAVTAGPFMDNAINVGGTGLQYAAITAPYVVLTGLGESFKKVATIPYKVCNSVKDTLTYYAHSVLYRVFPYDMDSGVSSFSELLFDCVDLSVASTYFLVRLLQDKTGDFMSTIITSCQTAVSKLLDTCFEATEATFNFLLDLAGLFRIFLRNAYVYTSQGFVVVNGKVSTLVKQVLDLLNKGMQLLHTKVSWAGSNISAVIYSGRESLIFPSGTYYCVTTKAKSVQQDLDVILPGEFSKKQLGLLQPTDNSTTVSVTVSSNMVETVVGQLEQTNMHSPDVIVGDYVIISEKLFVRSKEEDGFAFYPACTNGHAVPTLFRLKGGAPVKKVAFGGDQVHEVAAVRSVTVEYNIHAVLDTLLASSSLRTFVVDKSLSIEEFADVVKEQVSDLLVKLLRGMPIPDFDLDDFIDAPCYCFNAEGDASWSSTMIFSLHPVECDEECSEVEASDLEEGESECISETSTEQVDVSHEISDDEWAAAVDEAFPLDEAEDVTESVQEEAQPVEVPVEDIAQVVIADTLQETPVVSDTVEVPPQVVKLPSEPQTIQPEVKEVAPVYEADTEQTQSVTVKPKRLRKKRNVDPLSNFEHKVITECVTIVLGDAIQVAKCYGESVLVNAANTHLKHGGGIAGAINAASKGAVQKESDEYILAKGPLQVGDSVLLQGHSLAKNILHVVGPDARAKQDVSLLSKCYKAMNAYPLVVTPLVSAGIFGVKPAVSFDYLIREAKTRVLVVVNSQDVYKSLTIVDIPQSLTFSYDGLRGAIRKAKDYGFTVFVCTDNSANTKVLRNKGVDYTKKFLTVDGVQYYCYTSKDTLDDILQQANKSVGIISMPLGYVSHGLDLIQAGSVVRRVNVPYVCLLANKEQEAILMSEDVKLNPSEDFIKHVRTNGGYNSWHLVEGELLVQDLRLNKLLHWSDQTICYKDSVFYVVKNSTAFPFETLSACRAYLDSRTTQQLTIEVLVTVDGVNFRTVVLNNKNTYRSQLGCVFFNGADISDTIPDEKQNGHSLYLADNLTADETKALKELYGPVDPTFLHRFYSLKAAVHKWKMVVCDKVRSLKLSDNNCYLNAVIMTLDLLKDIKFVIPALQHAFMKHKGGDSTDFIALIMAYGNCTFGAPDDASRLLHTVLAKAELCCSARMVWREWCNVCGIKDVVLQGLKACCYVGVQTVEDLRARMTYVCQCGGERHRQIVEHTTPWLLLSGTPNEKLVTTSTAPDFVAFNVFQGIETAVGHYVHARLKGGLILKFDSGTVSKTSDWKCKVTDVLFPGQKYSSDCNVVRYSLDGNFRTEVDPDLSAFYVKDGKYFTSEPPVTYSPATILAGSVYTNSCLVSSDGQPGGDAISLSFNNLLGFDSSKPVTKKYTYSFLPKEDGDVLLAEFDTYDPIYKNGAMYKGKPILWVNKASYDTNLNKFNRASLRQIFDVAPIELENKFTPLSVESTPVEPPTVDVVALQQEMTIVKCKGLNKPFVKDNVSFVADDSGTPVVEYLSKEDLHTLYVDPKYQVIVLKDNVLSSMLRLHTVESGDINVVAASGSLTRKVKLLFRASFYFKEFATRTFTATTAVGSCIKSVVRHLGVTKGILTGCFSFVKMLFMLPLAYFSDSKLGTTEVKVSALKTAGVVTGNVVKQCCTAAVDLSMDKLRRVDWKSTLRLLLMLCTTMVLLSSVYHLYVFNQVLSSDVMFEDAQGLKKFYKEVRAYLGISSACDGLASAYRANSFDVPTFCANRSAMCNWCLISQDSITHYPALKMVQTHLSHYVLNIDWLWFAFETGLAYMLYTSAFNWLLLAGTLHYFFAQTSIFVDWRSYNYAVSSAFWLFTHIPMAGLVRMYNLLACLWLLRKFYQHVINGCKDTACLLCYKRNRLTRVEASTVVCGGKRTFYITANGGISFCRRHNWNCVDCDTAGVGNTFICEEVANDLTTALRRPINATDRSHYYVDSVTVKETVVQFNYRRDGQPFYERFPLCAFTNLDKLKFKEVCKTTTGIPEYNFIIYDSSDRGQESLARSACVYYSQVLCKSILLVDSSLVTSVGDSSEIATKMFDSFVNSFVSLYNVTRDKLEKLISTARDGVRRGDNFHSVLTTFIDAARGPAGVESDVETNEIVDSVQYAHKHDIQITNESYNNYVPSYVKPDSVSTSDLGSLIDCNAASVNQIVLRNSNGACIWNAAAYMKLSDALKRQIRIACRKCNLAFRLTTSKLRANDNILSVRFTANKIVGGAPTWFNALRDFTLKGYVLATIIVFLCAVLMYLCLPTFSMVPVEFYEDRILDFKVLDNGIIRDVNPDDKCFANKHRSFTQWYHEHVGGVYDNSITCPLTVAVIAGVAGARIPDVPTTLAWVNNQIIFFVSRVFANTGSVCYTPIDEIPYKSFSDSGCILPSECTMFRDAEGRMTPYCHDPTVLPGAFAYSQMRPHVRYDLYDGNMFIKFPEVVFESTLRITRTLSTQYCRFGSCEYAQEGVCITTNGSWAIFNDHHLNRPGVYCGSDFIDIVRRLAVSLFQPITYFQLTTSLVLGIGLCAFLTLLFYYINKVKRAFADYTQCAVIAVVAAVLNSLCICFVASIPLCIVPYTALYYYATFYFTNEPAFIMHVSWYIMFGPIVPIWMTCVYTVAMCFRHFFWVLAYFSKKHVEVFTDGKLNCSFQDAASNIFVINKDTYAALRNSLTNDAYSRFLGLFNKYKYFSGAMETAAYREAAACHLAKALQTYSETGSDLLYQPPNCSITSGVLQSGLVKMSHPSGDVEACMVQVTCGSMTLNGLWLDNTVWCPRHVMCPADQLSDPNYDALLISMTNHSFSVQKHIGAPANLRVVGHAMQGTLLKLTVDVANPSTPAYTFTTVKPGAAFSVLACYNGRPTGTFTVVMRPNYTIKGSFLCGSCGSVGYTKEGSVINFCYMHQMELANGTHTGSAFDGTMYGAFMDKQVHQVQLTDKYCSVNVVAWLYAAILNGCAWFVKPNRTSVVSFNEWALANQFTEFVGTQSVDMLAVKTGVAIEQLLYAIQQLYTGFQGKQILGSTMLEDEFTPEDVNMQIMGVVMQSGVRKVTYGTAHWLFATLVSTYVIILQATKFTLWNYLFETIPTQLFPLLFVTMAFVMLLVKHKHTFLTLFLLPVAICLTYANIVYEPTTPISSALIAVANWLAPTNAYMRTTHTDIGVYISMSLVLVIVVKRLYNPSLSNFALALCSGVMWLYTYSIGEASSPIAYLVFVTTLTSDYTITVFVTVNLAKVCTYAIFAYSPQLTLVFPEVKMILLLYTCLGFMCTCYFGVFSLLNLKLRAPMGVYDFKVSTQEFRFMTANNLTAPRNSWEAMALNFKLIGIGGTPCIKVAAMQSKLTDLKCTSVVLLSVLQQLHLEANSRAWAFCVKCHNDILAATDPSEAFEKFVSLFATLMTFSGNVDLDALASDIFDTPSVLQATLSEFSHLATFAELEAAQKAYQEAMDSGDTSPQVLKALQKAVNIAKNAYEKDKAVARKLERMADQAMTSMYKQARAEDKKAKIVSAMQTMLFGMIKKLDNDVLNGIISNARNGCIPLSVIPLCASNKLRVVIPDFTVWNQVVTYPSLNYAGALWDITVINNVDNEIVKSSDVVDSNENLTWPLVLECTRASTSAVKLQNNEIKPSGLKTMVVSAGQEQTNCNTSSLAYYEPVQGRKMLMALLSDNAYLKWARVEGKDGFVSVELQPPCKFLIAGPKGPEIRYLYFVKNLNNLHRGQVLGHIAATVRLQAGSNTEFASNSSVLSLVNFTVDPQKAYLDFVNAGGAPLTNCVKMLTPKTGTGIAISVKPESTADQETYGGASVCLYCRAHIEHPDVSGVCKYKGKFVQIPAQCVRDPVGFCLSNTPCNVCQYWIGYGCNCDSLRQAALPQSKDSNFLNESGVLL
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The replicase polyprotein of coronaviruses is a multifunctional protein: it contains the activities necessary for the transcription of negative stranded RNA, leader RNA, subgenomic mRNAs and progeny virion RNA as well as proteinases responsible for the cleavage of the polyprotein into functional products. [Host translation inhibitor nsp1]: Promotes the degradation of host mRNAs by inducing an endonucleolytic RNA cleavage in template mRNAs, and inhibits of host mRNA translation, a function that is separable from its RNA cleavage activity. By suppressing host gene expression, nsp1 facilitates efficient viral gene expression in infected cells and evasion from host immune response. [Non-structural protein 2]: May play a role in the modulation of host cell survival signaling pathway by interacting with host PHB and PHB2. Indeed, these two proteins play a role in maintaining the functional integrity of the mitochondria and protecting cells from various stresses. [Papain-like protease nsp3]: Responsible for the cleavages located at the N-terminus of the replicase polyprotein. In addition, PL-PRO possesses a deubiquitinating/deISGylating activity and processes both 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains from cellular substrates. Participates, together with nsp4, in the assembly of virally induced cytoplasmic double-membrane vesicles necessary for viral replication. Antagonizes innate immune induction of type I interferon by blocking the phosphorylation, dimerization and subsequent nuclear translocation of host IRF3. Prevents also host NF-kappa-B. signaling. [Non-structural protein 6]: Plays a role in the initial induction of autophagosomes from host reticulum endoplasmic. Later, limits the expansion of these phagosomes that are no longer able to deliver viral components to lysosomes. [Non-structural protein 7]: Forms a hexadecamer with nsp8 (8 subunits of each) that may participate in viral replication by acting as a primase. Alternatively, may synthesize substantially longer products than oligonucleotide primers. [Non-structural protein 8]: Forms a hexadecamer with nsp7 (8 subunits of each) that may participate in viral replication by acting as a primase. Alternatively, may synthesize substantially longer products than oligonucleotide primers. [RNA-capping enzyme subunit nsp9]: Catalytic subunit of viral RNA capping enzyme which catalyzes the RNA guanylyltransferase reaction for genomic and sub-genomic RNAs. The kinase-like NiRAN domain of NSP12 transfers RNA to the amino terminus of NSP9, forming a covalent RNA-protein intermediate. Subsequently, the NiRAN domain transfers RNA to GDP, forming the core cap structure GpppA-RNA. The NSP14 and NSP16 methyltransferases then add methyl groups to form functional cap structures.
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K9N7C7
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R1AB_MERS1
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Replicase polyprotein 1ab (pp1ab) (ORF1ab polyprotein) [Cleaved into: Host translation inhibitor nsp1 (nsp1) (Leader protein); Non-structural protein 2 (nsp2) (p65 homolog); Papain-like proteinase nsp3 (PL-PRO) (EC 3.4.19.12) (EC 3.4.22.-) (Non-structural protein 3) (nsp3); Non-structural protein 4 (nsp4); 3C-like proteinase nsp5 (3CL-PRO) (3CLp) (EC 3.4.22.-) (nsp5); Non-structural protein 6 (nsp6); Non-structural protein 7 (nsp7); Non-structural protein 8 (nsp8); RNA-capping enzyme subunit nsp9 (Non-structural protein 9) (nsp9) (EC 2.7.7.50) (p12); Non-structural protein 10 (nsp10) (Growth factor-like peptide) (GFL); RNA-directed RNA polymerase nsp12 (Pol) (RdRp) (EC 2.7.7.48) (nsp12); Helicase nsp13 (Hel) (EC 3.6.4.12) (EC 3.6.4.13) (nsp13); Guanine-N7 methyltransferase nsp14 (ExoN) (EC 2.1.1.56) (EC 3.1.13.-) (nsp14); Uridylate-specific endoribonuclease nsp15 (EC 4.6.1.-) (NendoU) (nsp15); 2'-O-methyltransferase nsp16 (EC 2.1.1.57) (nsp16)]
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MSFVAGVTAQGARGTYRAALNSEKHQDHVSLTVPLCGSGNLVEKLSPWFMDGENAYEVVKAMLLKKEPLLYVPIRLAGHTRHLPGPRVYLVERLIACENPFMVNQLAYSSSANGSLVGTTLQGKPIGMFFPYDIELVTGKQNILLRKYGRGGYHYTPFHYERDNTSCPEWMDDFEADPKGKYAQNLLKKLIGGDVTPVDQYMCGVDGKPISAYAFLMAKDGITKLADVEADVAARADDEGFITLKNNLYRLVWHVERKDVPYPKQSIFTINSVVQKDGVENTPPHYFTLGCKILTLTPRNKWSGVSDLSLKQKLLYTFYGKESLENPTYIYHSAFIECGSCGNDSWLTGNAIQGFACGCGASYTANDVEVQSSGMIKPNALLCATCPFAKGDSCSSNCKHSVAQLVSYLSERCNVIADSKSFTLIFGGVAYAYFGCEEGTMYFVPRAKSVVSRIGDSIFTGCTGSWNKVTQIANMFLEQTQHSLNFVGEFVVNDVVLAILSGTTTNVDKIRQLLKGVTLDKLRDYLADYDVAVTAGPFMDNAINVGGTGLQYAAITAPYVVLTGLGESFKKVATIPYKVCNSVKDTLTYYAHSVLYRVFPYDMDSGVSSFSELLFDCVDLSVASTYFLVRLLQDKTGDFMSTIITSCQTAVSKLLDTCFEATEATFNFLLDLAGLFRIFLRNAYVYTSQGFVVVNGKVSTLVKQVLDLLNKGMQLLHTKVSWAGSNISAVIYSGRESLIFPSGTYYCVTTKAKSVQQDLDVILPGEFSKKQLGLLQPTDNSTTVSVTVSSNMVETVVGQLEQTNMHSPDVIVGDYVIISEKLFVRSKEEDGFAFYPACTNGHAVPTLFRLKGGAPVKKVAFGGDQVHEVAAVRSVTVEYNIHAVLDTLLASSSLRTFVVDKSLSIEEFADVVKEQVSDLLVKLLRGMPIPDFDLDDFIDAPCYCFNAEGDASWSSTMIFSLHPVECDEECSEVEASDLEEGESECISETSTEQVDVSHEISDDEWAAAVDEAFPLDEAEDVTESVQEEAQPVEVPVEDIAQVVIADTLQETPVVSDTVEVPPQVVKLPSEPQTIQPEVKEVAPVYEADTEQTQSVTVKPKRLRKKRNVDPLSNFEHKVITECVTIVLGDAIQVAKCYGESVLVNAANTHLKHGGGIAGAINAASKGAVQKESDEYILAKGPLQVGDSVLLQGHSLAKNILHVVGPDARAKQDVSLLSKCYKAMNAYPLVVTPLVSAGIFGVKPAVSFDYLIREAKTRVLVVVNSQDVYKSLTIVDIPQSLTFSYDGLRGAIRKAKDYGFTVFVCTDNSANTKVLRNKGVDYTKKFLTVDGVQYYCYTSKDTLDDILQQANKSVGIISMPLGYVSHGLDLIQAGSVVRRVNVPYVCLLANKEQEAILMSEDVKLNPSEDFIKHVRTNGGYNSWHLVEGELLVQDLRLNKLLHWSDQTICYKDSVFYVVKNSTAFPFETLSACRAYLDSRTTQQLTIEVLVTVDGVNFRTVVLNNKNTYRSQLGCVFFNGADISDTIPDEKQNGHSLYLADNLTADETKALKELYGPVDPTFLHRFYSLKAAVHKWKMVVCDKVRSLKLSDNNCYLNAVIMTLDLLKDIKFVIPALQHAFMKHKGGDSTDFIALIMAYGNCTFGAPDDASRLLHTVLAKAELCCSARMVWREWCNVCGIKDVVLQGLKACCYVGVQTVEDLRARMTYVCQCGGERHRQIVEHTTPWLLLSGTPNEKLVTTSTAPDFVAFNVFQGIETAVGHYVHARLKGGLILKFDSGTVSKTSDWKCKVTDVLFPGQKYSSDCNVVRYSLDGNFRTEVDPDLSAFYVKDGKYFTSEPPVTYSPATILAGSVYTNSCLVSSDGQPGGDAISLSFNNLLGFDSSKPVTKKYTYSFLPKEDGDVLLAEFDTYDPIYKNGAMYKGKPILWVNKASYDTNLNKFNRASLRQIFDVAPIELENKFTPLSVESTPVEPPTVDVVALQQEMTIVKCKGLNKPFVKDNVSFVADDSGTPVVEYLSKEDLHTLYVDPKYQVIVLKDNVLSSMLRLHTVESGDINVVAASGSLTRKVKLLFRASFYFKEFATRTFTATTAVGSCIKSVVRHLGVTKGILTGCFSFVKMLFMLPLAYFSDSKLGTTEVKVSALKTAGVVTGNVVKQCCTAAVDLSMDKLRRVDWKSTLRLLLMLCTTMVLLSSVYHLYVFNQVLSSDVMFEDAQGLKKFYKEVRAYLGISSACDGLASAYRANSFDVPTFCANRSAMCNWCLISQDSITHYPALKMVQTHLSHYVLNIDWLWFAFETGLAYMLYTSAFNWLLLAGTLHYFFAQTSIFVDWRSYNYAVSSAFWLFTHIPMAGLVRMYNLLACLWLLRKFYQHVINGCKDTACLLCYKRNRLTRVEASTVVCGGKRTFYITANGGISFCRRHNWNCVDCDTAGVGNTFICEEVANDLTTALRRPINATDRSHYYVDSVTVKETVVQFNYRRDGQPFYERFPLCAFTNLDKLKFKEVCKTTTGIPEYNFIIYDSSDRGQESLARSACVYYSQVLCKSILLVDSSLVTSVGDSSEIATKMFDSFVNSFVSLYNVTRDKLEKLISTARDGVRRGDNFHSVLTTFIDAARGPAGVESDVETNEIVDSVQYAHKHDIQITNESYNNYVPSYVKPDSVSTSDLGSLIDCNAASVNQIVLRNSNGACIWNAAAYMKLSDALKRQIRIACRKCNLAFRLTTSKLRANDNILSVRFTANKIVGGAPTWFNALRDFTLKGYVLATIIVFLCAVLMYLCLPTFSMVPVEFYEDRILDFKVLDNGIIRDVNPDDKCFANKHRSFTQWYHEHVGGVYDNSITCPLTVAVIAGVAGARIPDVPTTLAWVNNQIIFFVSRVFANTGSVCYTPIDEIPYKSFSDSGCILPSECTMFRDAEGRMTPYCHDPTVLPGAFAYSQMRPHVRYDLYDGNMFIKFPEVVFESTLRITRTLSTQYCRFGSCEYAQEGVCITTNGSWAIFNDHHLNRPGVYCGSDFIDIVRRLAVSLFQPITYFQLTTSLVLGIGLCAFLTLLFYYINKVKRAFADYTQCAVIAVVAAVLNSLCICFVASIPLCIVPYTALYYYATFYFTNEPAFIMHVSWYIMFGPIVPIWMTCVYTVAMCFRHFFWVLAYFSKKHVEVFTDGKLNCSFQDAASNIFVINKDTYAALRNSLTNDAYSRFLGLFNKYKYFSGAMETAAYREAAACHLAKALQTYSETGSDLLYQPPNCSITSGVLQSGLVKMSHPSGDVEACMVQVTCGSMTLNGLWLDNTVWCPRHVMCPADQLSDPNYDALLISMTNHSFSVQKHIGAPANLRVVGHAMQGTLLKLTVDVANPSTPAYTFTTVKPGAAFSVLACYNGRPTGTFTVVMRPNYTIKGSFLCGSCGSVGYTKEGSVINFCYMHQMELANGTHTGSAFDGTMYGAFMDKQVHQVQLTDKYCSVNVVAWLYAAILNGCAWFVKPNRTSVVSFNEWALANQFTEFVGTQSVDMLAVKTGVAIEQLLYAIQQLYTGFQGKQILGSTMLEDEFTPEDVNMQIMGVVMQSGVRKVTYGTAHWLFATLVSTYVIILQATKFTLWNYLFETIPTQLFPLLFVTMAFVMLLVKHKHTFLTLFLLPVAICLTYANIVYEPTTPISSALIAVANWLAPTNAYMRTTHTDIGVYISMSLVLVIVVKRLYNPSLSNFALALCSGVMWLYTYSIGEASSPIAYLVFVTTLTSDYTITVFVTVNLAKVCTYAIFAYSPQLTLVFPEVKMILLLYTCLGFMCTCYFGVFSLLNLKLRAPMGVYDFKVSTQEFRFMTANNLTAPRNSWEAMALNFKLIGIGGTPCIKVAAMQSKLTDLKCTSVVLLSVLQQLHLEANSRAWAFCVKCHNDILAATDPSEAFEKFVSLFATLMTFSGNVDLDALASDIFDTPSVLQATLSEFSHLATFAELEAAQKAYQEAMDSGDTSPQVLKALQKAVNIAKNAYEKDKAVARKLERMADQAMTSMYKQARAEDKKAKIVSAMQTMLFGMIKKLDNDVLNGIISNARNGCIPLSVIPLCASNKLRVVIPDFTVWNQVVTYPSLNYAGALWDITVINNVDNEIVKSSDVVDSNENLTWPLVLECTRASTSAVKLQNNEIKPSGLKTMVVSAGQEQTNCNTSSLAYYEPVQGRKMLMALLSDNAYLKWARVEGKDGFVSVELQPPCKFLIAGPKGPEIRYLYFVKNLNNLHRGQVLGHIAATVRLQAGSNTEFASNSSVLSLVNFTVDPQKAYLDFVNAGGAPLTNCVKMLTPKTGTGIAISVKPESTADQETYGGASVCLYCRAHIEHPDVSGVCKYKGKFVQIPAQCVRDPVGFCLSNTPCNVCQYWIGYGCNCDSLRQAALPQSKDSNFLKRVRGSIVNARIEPCSSGLSTDVVFRAFDICNYKAKVAGIGKYYKTNTCRFVELDDQGHHLDSYFVVKRHTMENYELEKHCYDLLRDCDAVAPHDFFIFDVDKVKTPHIVRQRLTEYTMMDLVYALRHFDQNSEVLKAILVKYGCCDVTYFENKLWFDFVENPSVIGVYHKLGERVRQAILNTVKFCDHMVKAGLVGVLTLDNQDLNGKWYDFGDFVITQPGSGVAIVDSYYSYLMPVLSMTDCLAAETHRDCDFNKPLIEWPLTEYDFTDYKVQLFEKYFKYWDQTYHANCVNCTDDRCVLHCANFNVLFAMTMPKTCFGPIVRKIFVDGVPFVVSCGYHYKELGLVMNMDVSLHRHRLSLKELMMYAADPAMHIASSNAFLDLRTSCFSVAALTTGLTFQTVRPGNFNQDFYDFVVSKGFFKEGSSVTLKHFFFAQDGNAAITDYNYYSYNLPTMCDIKQMLFCMEVVNKYFEIYDGGCLNASEVVVNNLDKSAGHPFNKFGKARVYYESMSYQEQDELFAMTKRNVIPTMTQMNLKYAISAKNRARTVAGVSILSTMTNRQYHQKMLKSMAATRGATCVIGTTKFYGGWDFMLKTLYKDVDNPHLMGWDYPKCDRAMPNMCRIFASLILARKHGTCCTTRDRFYRLANECAQVLSEYVLCGGGYYVKPGGTSSGDATTAYANSVFNILQATTANVSALMGANGNKIVDKEVKDMQFDLYVNVYRSTSPDPKFVDKYYAFLNKHFSMMILSDDGVVCYNSDYAAKGYIAGIQNFKETLYYQNNVFMSEAKCWVETDLKKGPHEFCSQHTLYIKDGDDGYFLPYPDPSRILSAGCFVDDIVKTDGTLMVERFVSLAIDAYPLTKHEDIEYQNVFWVYLQYIEKLYKDLTGHMLDSYSVMLCGDNSAKFWEEAFYRDLYSSPTTLQAVGSCVVCHSQTSLRCGTCIRRPFLCCKCCYDHVIATPHKMVLSVSPYVCNAPGCGVSDVTKLYLGGMSYFCVDHRPVCSFPLCANGLVFGLYKNMCTGSPSIVEFNRLATCDWTESGDYTLANTTTEPLKLFAAETLRATEEASKQSYAIATIKEIVGERQLLLVWEAGKSKPPLNRNYVFTGYHITKNSKVQLGEYIFERIDYSDAVSYKSSTTYKLTVGDIFVLTSHSVATLTAPTIVNQERYVKITGLYPTITVPEEFASHVANFQKSGYSKYVTVQGPPGTGKSHFAIGLAIYYPTARVVYTACSHAAVDALCEKAFKYLNIAKCSRIIPAKARVECYDRFKVNETNSQYLFSTINALPETSADILVVDEVSMCTNYDLSIINARIKAKHIVYVGDPAQLPAPRTLLTRGTLEPENFNSVTRLMCNLGPDIFLSMCYRCPKEIVSTVSALVYNNKLLAKKELSGQCFKILYKGNVTHDASSAINRPQLTFVKNFITANPAWSKAVFISPYNSQNAVARSMLGLTTQTVDSSQGSEYQYVIFCQTADTAHANNINRFNVAITRAQKGILCVMTSQALFESLEFTELSFTNYKLQSQIVTGLFKDCSRETSGLSPAYAPTYVSVDDKYKTSDELCVNLNLPANVPYSRVISRMGFKLDATVPGYPKLFITREEAVRQVRSWIGFDVEGAHASRNACGTNVPLQLGFSTGVNFVVQPVGVVDTEWGNMLTGIAARPPPGEQFKHLVPLMHKGAAWPIVRRRIVQMLSDTLDKLSDYCTFVCWAHGFELTSASYFCKIGKEQKCCMCNRRAAAYSSPLQSYACWTHSCGYDYVYNPFFVDVQQWGYVGNLATNHDRYCSVHQGAHVASNDAIMTRCLAIHSCFIERVDWDIEYPYISHEKKLNSCCRIVERNVVRAALLAGSFDKVYDIGNPKGIPIVDDPVVDWHYFDAQPLTRKVQQLFYTEDMASRFADGLCLFWNCNVPKYPNNAIVCRFDTRVHSEFNLPGCDGGSLYVNKHAFHTPAYDVSAFRDLKPLPFFYYSTTPCEVHGNGSMIEDIDYVPLKSAVCITACNLGGAVCRKHATEYREYMEAYNLVSASGFRLWCYKTFDIYNLWSTFTKVQGLENIAFNFVKQGHFIGVEGELPVAVVNDKIFTKSGVNDICMFENKTTLPTNIAFELYAKRAVRSHPDFKLLHNLQADICYKFVLWDYERSNIYGTATIGVCKYTDIDVNSALNICFDIRDNGSLEKFMSTPNAIFISDRKIKKYPCMVGPDYAYFNGAIIRDSDVVKQPVKFYLYKKVNNEFIDPTECIYTQSRSCSDFLPLSDMEKDFLSFDSDVFIKKYGLENYAFEHVVYGDFSHTTLGGLHLLIGLYKKQQEGHIIMEEMLKGSSTIHNYFITETNTAAFKAVCSVIDLKLDDFVMILKSQDLGVVSKVVKVPIDLTMIEFMLWCKDGQVQTFYPRLQASADWKPGHAMPSLFKVQNVNLERCELANYKQSIPMPRGVHMNIAKYMQLCQYLNTCTLAVPANMRVIHFGAGSDKGIAPGTSVLRQWLPTDAIIIDNDLNEFVSDADITLFGDCVTVRVGQQVDLVISDMYDPTTKNVTGSNESKALFFTYLCNLINNNLALGGSVAIKITEHSWSVELYELMGKFAWWTVFCTNANASSSEGFLLGINYLGTIKENIDGGAMHANYIFWRNSTPMNLSTYSLFDLSKFQLKLKGTPVLQLKESQINELVISLLSQGKLLIRDNDTLSVSTDVLVNTYRKLR
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The replicase polyprotein of coronaviruses is a multifunctional protein: it contains the activities necessary for the transcription of negative stranded RNA, leader RNA, subgenomic mRNAs and progeny virion RNA as well as proteinases responsible for the cleavage of the polyprotein into functional products. [Host translation inhibitor nsp1]: Promotes the degradation of host mRNAs by inducing an endonucleolytic RNA cleavage in template mRNAs, and inhibits of host mRNA translation, a function that is separable from its RNA cleavage activity. By suppressing host gene expression, nsp1 facilitates efficient viral gene expression in infected cells and evasion from host immune response. [Non-structural protein 2]: May play a role in the modulation of host cell survival signaling pathway by interacting with host PHB and PHB2. Indeed, these two proteins play a role in maintaining the functional integrity of the mitochondria and protecting cells from various stresses. [Papain-like proteinase nsp3]: Responsible for the cleavages located at the N-terminus of the replicase polyprotein. In addition, PL-PRO possesses a deubiquitinating/deISGylating activity and processes both 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains from cellular substrates. Participates, together with nsp4, in the assembly of virally induced cytoplasmic double-membrane vesicles necessary for viral replication. Antagonizes innate immune induction of type I interferon by blocking the phosphorylation, dimerization and subsequent nuclear translocation of host IRF3. Prevents also host NF-kappa-B. signaling. [3C-like proteinase nsp5]: Cleaves the C-terminus of replicase polyprotein at 11 sites. Recognizes substrates containing the core sequence [ILMVF]-Q-|-[SGACN] (By similarity). May cleave human NLRP1 in lung epithelial cells, thereby activating the NLRP1 inflammasome pathway. Also able to bind an ADP-ribose-1''-phosphate (ADRP) (By similarity). [Non-structural protein 6]: Plays a role in the initial induction of autophagosomes from host reticulum endoplasmic. Later, limits the expansion of these phagosomes that are no longer able to deliver viral components to lysosomes. [Non-structural protein 7]: Forms a hexadecamer with nsp8 (8 subunits of each) that may participate in viral replication by acting as a primase. Alternatively, may synthesize substantially longer products than oligonucleotide primers. [Non-structural protein 8]: Forms a hexadecamer with nsp7 (8 subunits of each) that may participate in viral replication by acting as a primase. Alternatively, may synthesize substantially longer products than oligonucleotide primers. [RNA-capping enzyme subunit nsp9]: Catalytic subunit of viral RNA capping enzyme which catalyzes the RNA guanylyltransferase reaction for genomic and sub-genomic RNAs. The kinase-like NiRAN domain of NSP12 transfers RNA to the amino terminus of NSP9, forming a covalent RNA-protein intermediate. Subsequently, the NiRAN domain transfers RNA to GDP, forming the core cap structure GpppA-RNA. The NSP14 and NSP16 methyltransferases then add methyl groups to form functional cap structures. [RNA-directed RNA polymerase nsp12]: RNA-directed RNA polymerase that catalyzes the transcription of viral genomic and subgenomic RNAs. Acts in complex with nsp7 and nsp8 to transcribe both the minus and positive strands of genomic RNA. Subgenomic RNAs (sgRNAs) are formed by discontinuous transcription: The polymerase has the ability to pause at transcription-regulating sequences (TRS) and jump to the leader TRS, resulting in a major deletion. This creates a series of subgenomic RNAs that are replicated, transcribed and translated. In addition, Nsp12 is a subunit of the viral RNA capping enzyme that catalyzes the RNA guanylyltransferase reaction for genomic and sub-genomic RNAs. The kinase-like NiRAN domain of NSP12 transfers RNA to the amino terminus of NSP9, forming a covalent RNA-protein intermediate. Subsequently, the NiRAN domain transfers RNA to GDP, and forms the core cap structure GpppA-RNA. [Uridylate-specific endoribonuclease nsp15]: Plays a role in viral transcription/replication and prevents the simultaneous activation of host cell dsRNA sensors, such as MDA5/IFIH1, OAS, and PKR (By similarity). Acts by degrading the 5'-polyuridines generated during replication of the poly(A) region of viral genomic and subgenomic RNAs. Catalyzes a two-step reaction in which a 2'3'-cyclic phosphate (2'3'-cP) is first generated by 2'-O transesterification, which is then hydrolyzed to a 3'-phosphate (3'-P) (By similarity). If not degraded, poly(U) RNA would hybridize with poly(A) RNA tails and activate host dsRNA sensors (By similarity).
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K9NBS6
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AAM_RHOER
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Acylamidase (EC 3.5.1.13) (EC 3.5.1.14) (EC 3.5.1.4)
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MTEQNLHWLSATEMAASVASNNLSPNEIAEAMIQRVDAVNPSINAIVQFDREQVTRDAAELSRQQEAGEKLGPLHGVPFTIKDLTAVDGLPTTFGMKPMADNIATGNAVVVDRLRGAGGLFLGKTNTPESGYYGGTDNHLYGPTHNPWKLGNSAGGSSGGASAAVAAGLGPLAEGSDGAGSVRIPSALCGVVGLKPTTGVIPQTILAGRFYNWAYHGPITRTVADNALMLDIMAGPDNADPLSIERAETSYVEASKGDVKGLRVAWSPNLGLGHVDPEVLAVCLDALAAFEELGAQITEATPQWGNPSESMWSGIWVPGFASEYDLLDWENQRGEVDDYLIEIMHEAERLTGVDVGRADAFRGDMWDTWTTFMNDYDVLVSPTLASATFPLRQFAPSWLEGASLREQLLDWLFTYPYNMLNNPAITVPAGFTADGRPVGLQIAARHRRDALVLRTAANFEAVRPWADKKPADSLVVA
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Amidase with broad substrate specificity, catalyzing the hydrolysis of a wide range of N-substituted amides, and, to a lesser extent, the hydrolysis of non-substituted amides. Acid para-nitroanilides (4'-nitroacetanilide, Gly-pNA, Ala-pNA, Leu-pNA) are the best substrates for this enzyme. N-substituted acrylamides (isopropyl acrylamide, N,N-dimethyl-aminopropyl acrylamide, and methylene-bis-acrylamide), N-acetyl derivatives of glycine, alanine and leucine, and aliphatic amides (acetamide, acrylamide, isobutyramide, n-butyramide, and valeramide) can also be used as substrates but with less efficiency.
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K9UJK2
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TM175_CHAP6
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Potassium channel Cha6605_3372 (Transmembrane protein 175) (CmTMEM175)
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MVEAPEQSETGRIEAFSDGVFAIAITLLVLEIKVPQHKIVETVGLVSSLLSLWPSYLAFLTSFASILVMWVNHHRIFSLVARTDHAFFYWNGLLLMLVTFVPFPTALLAEYLIHPQARVAASVYAGIFLAIAIVFNRLWKHAATADRLLAQKADRHEVDAITKQYRFGPGLYLVAFALSFISVWLSVGVCFVLAIYFALRSNA
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Potassium channel. The channel is permeable for K(+), Rb(+) and Cs(+), while it is unable to conduct Na(+).
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K9USW8
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A1O_LOXGA
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Dermonecrotic toxin LgSicTox-alphaIC1 (EC 4.6.1.-) (Phospholipase D) (PLD) (Phospholipase D LgRec1) (Sphingomyelin phosphodiesterase D) (SMD) (SMase D) (Sphingomyelinase D) [Cleaved into: U1-sicaritoxin-Lg1a (U1-SCRTX-Lg1a) (Anionic antimicrobial peptide) (AAMP) (Lg-AMP1)]
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ADNRRPIWVMGHMVNSLAQIDEFVGLGSNSIETDVSFDKQANPEYTYHGIPCDCGRACLHSTKFNDFLKGLRKVTTPGDSKYLEKLILVVFDLKTGSLYDNQAYDAGTKLAKNLLQHYWNNGNNGGRAYIILSIPNLNHYKLITGFKETLKNEGHEELLEKVGTDFSGNDDISDVQKTYNKAGVTGHVWQSDGITNCLLRGLTRVKAAVANRDSGSGIINKVYYWTVDKRQSTRDTLDANVDGIMTNYPDITVEILNEAAYKKKFRIATYEDNPWETFKG
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[Dermonecrotic toxin LgSicTox-alphaIC1]: Dermonecrotic toxins cleave the phosphodiester linkage between the phosphate and headgroup of certain phospholipids (sphingolipid and lysolipid substrates), forming an alcohol (often choline) and a cyclic phosphate (By similarity). This toxin acts on sphingomyelin (SM) with high activity. It may also act on ceramide phosphoethanolamine (CPE), lysophosphatidylcholine (LPC) and lysophosphatidylethanolamine (LPE), but not on lysophosphatidylserine (LPS), and lysophosphatidylglycerol (LPG) (By similarity). It acts by transphosphatidylation, releasing exclusively cyclic phosphate products as second products (By similarity). Induces platelet aggregation in platelet rich plasma, but not in washed platelet, indicating that this activity is dependent on plasma components. Also induces hemolysis. In vivo, the recombinant protein evokes an intense inflammatory reaction and dermonecrosis, similar to those induced by L.gaucho total venom. Is a good immunogen, capable of inducing immunoprotection in test animals. [U1-sicaritoxin-Lg1a]: Anionic antimicrobial peptide that shows antimicrobial activity against Gram-negative bacteria (MIC=1.15-4.6 uM) (tested on E.coli, P.aeruginosa, and E.cloacae), but not on Gram-negative bacteria (M.luteus, S.aureus, and B.subtilis), neither on fungi and yeasts (A.niger, C.albicans and C.krusei). Does not show hemolytic effects against human erythrocytes, and has no cytotoxic effects against human cervical carcinoma cells (HeLa).
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L0DSL2
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NIR_THIND
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Cytochrome c-552 (EC 1.7.2.2) (Cytochrome c nitrite reductase) (TvNiR)
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MNDLNRLGRVGRWIAGAACLFLASAAHAEPGENLKPVDAMQCFDCHTQIEDMHTVGKHATVNCVHCHDATEHVETASSRRMGERPVTRMDLEACATCHTAQFNSFVEVRHESHPRLEKATPTSRSPMFDKLIAGHGFAFEHAEPRSHAFMLVDHFVVDRAYGGRFQFKNWQKVTDGMGAVRGAWTVLTDADPESSDQRRFLSQTATAANPVCLNCKTQDHILDWAYMGDEHEAAKWSRTSEVVEFARDLNHPLNCFMCHDPHSAGPRVVRDGLINAVVDRGLGTYPHDPVKSEQQGMTKVTFQRGREDFRAIGLLDTADSNVMCAQCHVEYNCNPGYQLSDGSRVGMDDRRANHFFWANVFDYKEAAQEIDFFDFRHATTGAALPKLQHPEAETFWGSVHERNGVACADCHMPKVQLENGKVYTSHSQRTPRDMMGQACLNCHAEWTEDQALYAIDYIKNYTHGKIVKSEYWLAKMIDLFPVAKRAGVSEDVLNQARELHYDAHLYWEWWTAENSVGFHNPDQARESLMTSISKSKEAVSLLNDAIDAQVASR
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Catalyzes the reduction of nitrite to ammonia, consuming six electrons in the process. Has very low activity toward hydroxylamine. Has even lower activity toward sulfite. Sulfite reductase activity is maximal at neutral pH.
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L0E155
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MALA_MALAU
|
Flavin-dependent halogenase malA (EC 1.14.-.-) (Malbrancheamide biosynthesis cluster protein A)
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MAPTPKYTFTERAAAGNLSDAEILNSNNPTGSELPDESDVVVGGAGIHGLIYALHASKYKPNNLKISVIEKNTRPGYKIGESTLPIFYTWCKLHGISAAYLLRLFGLKDGLCFYFLDRENQGQYTDFCSVGAPGLVLASLQIERPMSELLFTILAQRNGVNVYHGREVDFKSTVVQGGGQGNKIAVSRGKYDSTPKTIDSALFVDATGRFRQFCSKKAPRHRFDGWNCNAFWGYFTAPKDESKIPFDLYEGDHTNHLCFPEGWVWVIRLPSWEGSLIANLMDMVTYILECADAGVPGDELPSSEELARMFGLKFQWVTSIGFAVRNDVKYPEDLSAYGTREAEQKFNYFVQKYELLQQFMSNFELIENLYGPGTTWFIRKTLAYQSPVVSGPGWLAIGDACGFTNPLYSPGINVGMSTSTWAAQLSHRIVEIGKSAPADAAESSIRKLLVPYDDYCKSLVPALEQMNRFNYVCYRDTRLGPQVACLWQFFAGIERYLSDVNIETFAHYAIKWVWGAMVPEYQQVAQKCIEHIETVPLDERLPDAMVDELLAFSNRIKSAAVAADDFSLRWDAILRSFDRSLNFVEGKTSRDIYTRQCSGCGAWLQLRPDWKKCHSCGLLGTEPQTAVTFDPPLTAEEEALLYAAWNTAPKYDPSKELKLPTPTRPAA
|
Flavin-dependent halogenase part of the gene cluster that mediates the biosynthesis of malbrancheamide, a dichlorinated fungal indole alkaloid that belongs to a family of natural products containing a characteristic bicyclo[2.2.2]diazaoctane core. The first step of malbrancheamide biosynthesis involves coupling of L-proline and L-tryptophan by malG, a bimodular NRPS, to produce L-Pro-L-Trp aldehyde through reductive offloading. This compound undergoes spontaneous cyclization and dehydration to give a dienamine which is reverse prenylated at C-2 by malE. The other prenyltransferase present in the cluster, malB, displays modest activity, suggesting that may be a redundant gene in the pathway. Subsequently, a [4+2] Diels-Alder cyclo-addition catalyzed by the bifunctional enzyme malC forms the characteristic bicyclo[2.2.2]diazaoctane ring of premalbrancheamid. Finally, the flavin-dependent halogenase malA catalyzes the iterative dichlorination of the indole ring of premalbrancheamide to yield C-9 monochlorinated malbrancheamide B, C-8 monochlorinated isomalbrancheamide B, and dichlorinated malbrancheamide. MalA is also able to brominate premalbrancheamide at C-9 to yield malbrancheamide C, and, to a lesser extend, at C-8 to yield isomalbrancheamide C. Finally, malA can brominate C-9 monochlorinated malbrancheamide B at C-8 to yield malbrancheamide D, or C-8 monochlorinated isomalbrancheamide B at C-9 to produce isomalbrancheamide D.
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L0E4H0
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PHQK_PENFE
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FAD-dependent monooxygenase phqK (EC 1.-.-.-) (Paraherquamide biosynthesis cluster protein K)
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MGSLGEEVQVIIVGLGIVGLAAAIECREKGHSVHAFEKSNILKSIGDCIGLQSNATRIIKRWGDGAVHEALRPWIVSSKEIRIHNSSGRLIIRQDLSEVCEQPNYLLPRSELIRVMYEHALKIGVEISLGVEVCEPSEDEEGASVVALTRDGERQIVRGDFIICSDGVHSKMRKAIMPQPVEPRPSGYAAFRALVDTETLKGDPEASWVFEGVEENDRFDVFFLSGAQIALQSCNKGKVFSWFCIHQDTRNLLDVWTSPADPNEMLDLIKVWPIGQRLWSVIRHTQPQKFINYPLLNHKPLDHWVSSHGRLILIGDAAHPLSPAAGQGASQGIEDANVLATSLSLAGRQRVSLALHVAERIRYARASAVQLISHRVNEGWRNQDWDAYEPNEQNIASLPLETWIYGHDSQAYTEQEFEMVVRAVQEGEEYHATNLPDKLRVQLGIRNVDVKEPLQNKSP
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FAD-dependent monooxygenase part of the gene cluster that mediates the biosynthesis of paraherquamide, a fungal indole alkaloid that belongs to a family of natural products containing a characteristic bicyclo[2.2.2]diazaoctane core. Within the pathway, phqK catalyzes spirocycle formation through two parallel pathways in the biosynthesis of paraherquamides A and G, using as substrates paraherquamides K and L, with paraherquamide L, bearing the dioxepin, being likely the favored substrate. The first steps in the biosynthesis of paraherquamide is the production of the beta-methyl-proline precursor from L-isoleucine. They require oxidation of a terminally hydroxylated L-isoleucine to the corresponding aldehyde by enzymes which have still to be identified. Spontaneous cyclization and dehydration would yield the 4-methyl pyrolline-5-carboxylic acid, which is then reduced by the pyrroline-5-carboxylate reductase phqD leading to the beta-methyl-proline precursor. The next step of paraherquamide biosynthesis involves coupling of beta-methyl-proline and L-tryptophan by the bimodular NRPS phqB, to produce a monooxopiperazine intermediate. The reductase (R) domain of phqB utilizes NADPH for hydride transfer to reduce the thioester bond of the T domain-tethered linear dipeptide to a hemithioaminal intermediate, which spontaneously cleaves the C-S bond to release the aldehyde product. This compound undergoes spontaneous cyclization and dehydration to give a dienamine which is reverse prenylated at C-2 by the reverse prenyltransferase phqJ. The other prenyltransferase present in the cluster, phqI may be a redundant gene in the pathway. During biosynthetic assembly, the key step to produce the polycyclic core is catalyzed by the bifunctional reductase and intramolecular [4+2] Diels-Alderase, phqE, resulting in formation of the [2.2.2] diazaoctane intermediate preparaherquamide. Following formation of preparaherquamide, an indole 2,3-epoxidation-initiated pinacol-like rearrangement is catalyzed by the phqK FAD-dependent monooxygenase. The prenyltransferase phqA, the cytochrome P450 monooxygenase phqL, and the FAD-linked oxidoreductase phqH (or the cytochrome P450 monooxygenase phqM), are proposed to be involved in the formation of the pyran ring. The FAD-dependent monooxygenase phqK is likely responsible for generation of the spiro-oxindole, and the N-methylation is likely mediated by the phqN methyltransferase leading to the isolable natural product paraherquamide F. However, the order of these biosynthetic steps has still to be determined. In late-stage paraherquamide biosynthesis, the third P450 monooxygenase, phqO, is probably responsible for the C-14 hydroxylation, transforming paraherquamide F to paraherquamide G, and paraherquamide E to the final product paraherquamide A. The expansion from the 6-membered ring pyran (in paraherquamides F and G) to the 7-membered dioxepin ring (in paraherquamides A and E) represents a poorly understood but intriguing process that probably involves the 2-oxoglutarate-dependent dioxygenase phqC. Finally, the remaining members of the paraherquamide cluster, including phqI as well as phqM (or phqH), do not have a clearly prescribed role and appear to be redundant (Probable).
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L0L3V3
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FRE21_SPHLA
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Frenatin 2.3S (F2.3S) [Cleaved into: Frenatin 2.1S (F2.1S)]
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MAFLKKSLFLVLFLGLVSLSMGEREKREEEEEEEEENKEEEANEEGKGESEEKRGLVGTLLGHIGKAILGG
|
[Frenatin 2.1S]: Antimicrobial peptide with potent activity against Gram-negative bacteria. Shows immunostimulatory actions both in vitro and in vivo. In vitro, is cytotoxic to non-small cell lung adenocarcinoma A549 cells. Also, stimulates production of pro-inflammatory cytokines by mouse peritoneal macrophages and down-regulates production of the anti-inflammatory cytokine IL-10 by lipopolysaccharide (LPS)-stimulated cells. In vivo, intraperitoneal injection in mice enhances the activation state and homing capacity of Th1 type lymphocytes and promotes the recruitment, activation and tumoricidal capacities of peritoneal NK cells. Has a very weak activity in stimulation of insulin release and a weak hemolytic activity. [Frenatin 2.3S]: Antimicrobial peptide with potent activity against some Gram-positive and Gram-negative bacteria. Has a multifunctional mode of action. It displays depolarization and bacterial cell leakage, and can also internalize into bacterial cells and alter specific gene expression involved in bacterial resistance mechanisms. Does not agglutinate bacteria and lipid vesicles, even a high concentrations. Also displays moderate cellular protection against yellow fever virus (YFV)-infected Vero cells without causing significant cytotoxicity. Shows a weak hemolytic activity, and is not cytotoxic to monocytes. Frenatin 2.3S (version without Gly-71) shows no or very weak antibacterial activity, shows no or very weak cytotoxicity to lung adenocarcinoma A549 cells and shows very weak hemolysis. It only stimulates production of pro-inflammatory cytokines IL-23 (but not IL-1beta and TNF-alpha) by mouse peritoneal macrophages and has no effect on the production of the anti-inflammatory cytokine IL-10. Frenatin 2.3S (version without Gly-71) very weakly stimulates insulin release.
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