entry stringlengths 6 10 | 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 | FOLC_MYCTU | Dihydrofolate synthase/folylpolyglutamate synthase (DHFS / FPGS) (EC 6.3.2.12) (EC 6.3.2.17) (Folylpoly-gamma-glutamate synthetase) (Tetrahydrofolylpolyglutamate synthase) | MNSTNSGPPDSGSATGVVPTPDEIASLLQVEHLLDQRWPETRIDPSLTRISALMDLLGSPQRSYPSIHIAGTNGKTSVARMVDALVTALHRRTGRTTSPHLQSPVERISIDGKPISPAQYVATYREIEPLVALIDQQSQASAGKGGPAMSKFEVLTAMAFAAFADAPVDVAVVEVGMGGRWDATNVINAPVAVITPISIDHVDYLGADIAGIAGEKAGIITRAPDGSPDTVAVIGRQVPKVMEVLLAESVRADASVAREDSEFAVLRRQIAVGGQVLQLQGLGGVYSDIYLPLHGEHQAHNAVLALASVEAFFGAGAQRQ... | 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 bio... |
I6Y2J4 | LIPY_MYCTU | Triacylglycerol lipase (EC 3.1.1.3) (Esterase/lipase) (Triolein hydrolase) [Cleaved into: Cytosolic triacylglycerol lipase; Extracellular triacylglycerol lipase] | MVSYVVALPEVMSAAATDVASIGSVVATASQGVAGATTTVLAAAEDEVSAAIAALFSGHGQDYQALSAQLAVFHERFVQALTGAAKGYAAAELANASLLQSEFASGIGNGFATIHQEIQRAPTALAAGFTQVPPFAAAQAGIFTGTPSGAAGFDIASLWPVKPLLSLSALETHFAIPNNPLLALIASDIPPLSWFLGNSPPPLLNSLLGQTVQYTTYDGMSVVQITPAHPTGEYVVAIHGGAFILPPSIFHWLNYSVTAYQTGATVQVPIYPLVQEGGTAGTVVPAMAGLISTQIAQHGVSNVSVVGDSAGGNLALAAAQ... | 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) an... |
I6Y3Q0 | CHSE5_MYCTU | Acyl-CoA dehydrogenase FadE27 (ACAD) (EC 1.3.99.-) (3-oxocholest-4-en-26-oyl-CoA dehydrogenase beta subunit) | MDFTTTEAAQDLGGLVDTIVDAVCTPEHQRELDKLEQRFDRELWRKLIDAGILSSAAPESLGGDGFGVLEQVAVLVALGHQLAAVPYLESVVLAAGALARFGSPELQQGWGVSAVSGDRILTVALDGEMGEGPVQAAGTGHGYRLTGTRTQVGYGPVADAFLVPAETDSGAAVFLVAAGDPGVAVTALATTGLGSVGHLELNGAKVDAARRVGGTDVAVWLGTLSTLSRTAFQLGVLERGLQMTAEYARTREQFDRPIGSFQAVGQRLADGYIDVKGLRLTLTQAAWRVAEDSLASRECPQPADIDVATAGFWAAEAGHR... | 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)-... |
I6Y4D2 | PEPAM_MYCTU | N-acetylmuramoyl-L-alanine amidase Rv3717 (EC 3.5.1.28) (Zinc-dependent peptidoglycan amidase) | MIVGVLVAAATPIISSASATPANIAGMVVFIDPGHNGANDASIGRQVPTGRGGTKNCQASGTSTNSGYPEHTFTWETGLRLRAALNALGVRTALSRGNDNALGPCVDERANMANALRPNAIVSLHADGGPASGRGFHVNYSAPPLNAIQAGPSVQFARIMRDQLQASGIPKANYIGQDGLYGRSDLAGLNLAQYPSILVELGNMKNPADSALMESAEGRQKYANALVRGVAGFLATQGQAR | 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 W311... |
I6Y4U9 | DYP_MYCTU | Dye-decolorizing peroxidase (DyP) (EC 1.11.1.7) | MAVPAVSPQPILAPLTPAAIFLVATIGADGEATVHDALSKISGLVRAIGFRDPTKHLSVVVSIGSDAWDRLFAGPRPTELHPFVELTGPRHTAPATPGDLLFHIRAETMDVCFELAGRILKSMGDAVTVVDEVHGFRFFDNRDLLGFVDGTENPSGPIAIKATTIGDEDRNFAGSCYVHVQKYVHDMASWESLSVTEQERVIGRTKLDDIELDDNAKPANSHVALNVITDDDGTERKIVRHNMPFGEVGKGEYGTYFIGYSRTPTVTEQMLRNMFLGDPAGNTDRVLDFSTAVTGGLFFSPTIDFLDHPPPLPQAATPTL... | 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 oxidati... |
I6Y778 | FABG4_MYCTU | 3-oxoacyl-[acyl-carrier-protein] reductase [NADH] (EC 1.1.1.212) (Beta-ketoacyl CoA reductase) (FASII-like 3-oxoacyl-thioester reductase) (HMwFabG) | MAPKRSSDLFSQVVNSGPGSFLARQLGVPQPETLRRYRAGEPPLTGSLLIGGAGRVVEPLRAALEKDYDLVGNNLGGRWADSFGGLVFDATGITEPAGLKGLHEFFTPVLRNLGRCGRVVVVGGTPEAAASTNERIAQRALEGFTRSLGKELRRGATTALVYLSPDAKPAATGLESTMRFLLSAKSAYVDGQVFSVGADDSTPPADWEKPLDGKVAIVTGAARGIGATIAEVFARDGAHVVAIDVESAAENLAETASKVGGTALWLDVTADDAVDKISEHLRDHHGGKADILVNNAGITRDKLLANMDDARWDAVLAVNL... | 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). |
I6Y9J2 | LDT2_MYCTU | L,D-transpeptidase 2 (LDT 2) (EC 2.3.2.-) (Ldt(Mt2)) | MPKVGIAAQAGRTRVRRAWLTALMMTAVMIGAVACGSGRGPAPIKVIADKGTPFADLLVPKLTASVTDGAVGVTVDAPVSVTAADGVLAAVTMVNDNGRPVAGRLSPDGLRWSTTEQLGYNRRYTLNATALGLGGAATRQLTFQTSSPAHLTMPYVMPGDGEVVGVGEPVAIRFDENIADRGAAEKAIKITTNPPVEGAFYWLNNREVRWRPEHFWKPGTAVDVAVNTYGVDLGEGMFGEDNVQTHFTIGDEVIATADDNTKILTVRVNGEVVKSMPTSMGKDSTPTANGIYIVGSRYKHIIMDSSTYGVPVNSPNGYRT... | 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... |
I6Y9Q3 | PRPC_MYCTU | 2-methylcitrate synthase (2-MCS) (MCS) (EC 2.3.3.5) (Citrate synthase) (EC 2.3.3.16) | MTGPLAAARSVAATKSMTAPTVDERPDIKKGLAGVVVDTTAISKVVPQTNSLTYRGYPVQDLAARCSFEQVAFLLWRGELPTDAELALFSQRERASRRVDRSMLSLLAKLPDNCHPMDVVRTAISYLGAEDPDEDDAAANRAKAMRMMAVLPTIVAIDMRRRRGLPPIAPHSGLGYAQNFLHMCFGEVPETAVVSAFEQSMILYAEHGFNASTFAARVVTSTQSDIYSAVTGAIGALKGRLHGGANEAVMHDMIEIGDPANAREWLRAKLARKEKIMGFGHRVYRHGDSRVPTMKRALERVGTVRDGQRWLDIYQVLAAE... | 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 t... |
I6YCA3 | CHSE4_MYCTU | Acyl-CoA dehydrogenase FadE26 (ACAD) (EC 1.3.99.-) (3-oxocholest-4-en-26-oyl-CoA dehydrogenase alpha subunit) | MRISYTPQQEELRRELRSYFATLMTPERREALSSVQGEYGVGNVYRETIAQMGRDGWLALGWPKEYGGQGRSAMDQLIFTDEAAIAGAPVPFLTINSVAPTIMAYGTDEQKRFFLPRIAAGDLHFSIGYSEPGAGTDLANLRTTAVRDGDDYVVNGQKMWTSLIQYADYVWLAVRTNPESSGAKKHRGISVLIVPTTAEGFSWTPVHTMAGPDTSATYYSDVRVPVANRVGEENAGWKLVTNQLNHERVALVSPAPIFGCLREVREWAQNTKDAGGTRLIDSEWVQLNLARVHAKAEVLKLINWELASSQSGPKDAGPSP... | 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)-... |
I6YFP0 | BIRA_MYCTU | 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) | MTDRDRLRPPLDERSLRDQLIGAGSGWRQLDVVAQTGSTNADLLARAASGADIDGVVLIAEHQTAGRGRHGRGWAATARAQIILSVGVRVVDVPVQAWGWLSLAAGLAVLDSVAPLIAVPPAETGLKWPNDVLARGGKLAGILAEVAQPFVVLGVGLNVTQAPEEVDPDATSLLDLGVAAPDRNRIASRLLRELEARIIQWRNANPQLAADYRARSLTIGSRVRVELPGGQDVVGIARDIDDQGRLCLDVGGRTVVVSAGDVVHLR | 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. |
I6YG32 | RIMI_MYCTU | N-alpha-acetyltransferase RimI (EC 2.3.1.255) (EC 2.3.1.258) | MTADTEPVTIGALTRADAQRCAELEAQLFVGDDPWPPAAFNRELASPHNHYVGARSGGTLVGYAGISRLGRTPPFEYEVHTIGVDPAYQGRGIGRRLLRELLDFARGGVVYLEVRTDNDAALALYRSVGFQRVGLRRRYYRVSGADAYTMRRDSGDPS | 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 acetyl... |
I7CA98 | TODT_PSEPT | Response regulator protein TodT | MPARWGCLFPGKYPCQTGLRHMSDRASVIYILDDDNAVLEALSSLVRSIGLSVECFSSASVFLNDVNRSACGCLILDVRMPEMSGLDVQRQLKELGEQIPIIFISGHGDIPMAVKAIKAGAVDFFTKPFREEELLGAIRAALKLAPQQRSNAPRVSELKENYESLSKREQQVLKFVLRGYLNKQTALELDISEATVKVHRHNIMRKMKVSSIQDLVRVTERLKDSLE | 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-... |
I7H727 | TPS2_TOOSI | 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.-) | MSVPVSQIPSLKAKGVIMRRNANYHPNIWGDRFINYVPVDKMNHTCHLQAIEELKDAVRRELLTATGLSQLNLIDAIQRLGVGYHFERELEEALQHVYHKNHYHDDTEDNLYSISLRFRLLRQHGYYVSCDILNKFKDEKDNFKESLTTDVPGMLSLYEAAHPGVHGEDILDEAIAFTTTHLKSLAIDHLRNPSLASQVIHALRQPLHRGVPRLENRRYISIYQDEVSHNKALVKLFKLDFNLVQSLHKKELSEISRWWKELDLANKLPFARDRLVECYFWIIGVYYEPQYSLARKILTKTIAMGSIIDDIYDVYGTPEE... | 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. |
I7HJS4 | ZN683_MOUSE | Tissue-resident T-cell transcription regulator protein ZNF683 (Homolog of Blimp-1 in T-cell) (Hobit) (Zinc finger protein 683) | MKALDGLRESLYPSLDFQLYQDDQVCSADASQPLADSVGAHDLAWSERMCPLPLAPAKSPLLACPESPDLCLCALQKTPLGRAPQDLGEDASNMRHQPPSLYKASTDSEKLTIKDSLNREEMGNEPERGAYPHLPPRTSSFPDAGLDRKSLSPLTFWPWLPPTLISKEPPIHIYPIFPGYPLLPLPYLFTYGALPSAQHPYLFMLPPHSTYPTVAGPSLLMTASGSGPRIPQEKTLLLHSGAFQSAGHTLHSQVESRSSRDTRTPGQAGVAAPTRRAVPGSRAGVIALPYPLKKENGKILYECNVCGKNFGQLSNLKVHL... | 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... |
J3KML8 | GFY_MOUSE | Golgi-associated olfactory signaling regulator (Golgi protein in olfactory neurons) (Goofy) | MQPFSPIFFHLLFLLNGLSSRAAPSPGQPVVADLQGMLQPSGMPTGTLENLTRDQPTPGSSASHPPEHSETPPSASPHISTKILRETPSPSPFLSLETPIPDQLTSVAESQGTSQMSPSRATLGKPSETPKPDPTGISPSDSPETPKPNPSNTSPPESPESVYTDPTPTLHHESPEISKRDTPKLSPGEESKIPSPRPTQFLSSKSLETYDPSATRHLNSALEPTTHPDPTESPQSVFLTTHNSNPTVVPQTQFPTSPSQNVTETARTSDLEPSSSLPTQPTTFREEATTPSEPGLSPSPEAPAVTRVATPGLSTSDSPG... | Required for proper function of the olfactory system. May be involved in establishing the acuity of olfactory sensory signaling. |
J3QMI4 | CAHM3_MOUSE | Calcium homeostasis modulator protein 3 | MDRFRMLFQHLQSSSESVMNGICLLLAAVTVKIYSSLDFNCPCLERYNALYGLGLLLTPPLALFLCGLLVNRQSVLMVEEWRRPAGHRRKDLGIIRYMCSSVLQRALAAPLVWILLALLDGKCFVCAFSNSVDPEKFLDFANMTPRQVQLFLAKVPCKEDELVKNSPARKAVSRYLRCLSQAIGWSITLLVIVVAFLARCLRPCFDQTVFLQRRYWSNYMDLEQKLFDETCCEHARDFAHRCVLHFFANMQSELRALGLRRDPAGGIPESQESSEPPELREDRDSGNGKAHLRAISSREQVDQLLSTWYSSKPPLDLAAS... | 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 GPC... |
J3QMK6 | AL3B3_MOUSE | Aldehyde dehydrogenase family 3 member B3 (EC 1.2.1.3) | MSTKGKHPRADQGTDPFEEKLQRLKEAFNTGKTKTAKFRAEQLQSLGRFLQDNSKQLHDALDGDLGKSGFESDMSEIILCENEVDLALKNLQTWMKDEPVSTNLLTKLSTAFIRKEPFGLVLIIAPWNYPVNLMIIPLVGAIAAGNCVVLKPSEISKNTEKVLAELLPQYLDQSCFAVMLGGPEETGQLLEHKFDYIFFTGSPRVGKIVMTAAAKHLTPITLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVAPDYILCSQEMQEQLVPALQNAITRFYGDNPQTSPNLGRIINQKHFKRLQGLLGCGRVAIGG... | Oxidizes medium and long chain aldehydes into non-toxic fatty acids. |
J3QMY9 | TO6BL_MOUSE | 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) | MERTALAVCEILRYLIIHWKCEAGTAKGTLLDGQLVISIEALRSKHLPDSLHCIITIASTRSVYGGLNFKKFLQEIQPALPRLSAKLALASEEGGRSQDASGIAPCQVTFEVDENSQSLMTDCLVIKHFLRKIIIVHHKLKFSFSVAVNGTLSAETFGAENEPTLRLDNGVTLVVGFQRYVSKPKLNWSEAHCSRIHPVLGHPAPLFIPDAKADTGLLGELTLTPAAALCPSPKGFSSQLCRISSVSIFLYGPLGLPLLSSDQDQPSTAVFRDTSYFIDWKKYNLFMVPNLDLNLDTQSVLPDVNYKAESPEGNQSQNMN... | 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... |
J3QPC3 | ACTMP_MOUSE | Actin maturation protease (EC 3.4.11.-) (Actin aminopeptidase ACTMAP) | MTSPCSFPLKPTISPIIHETPDTNIPPPLPLNPPDLALPSPPCSLHTSISSPLPPPPPPPAPPPPPPPPPLPSAVEPVLPHVYGLKNSQLLKEALEKAGPAPKGKEDVKRLLKLHKDRFRSDLQWILFCADLPSCIQEGPQCGLVALWMAEALLSTPDSVSLERLVQVAKERGYTAQGEMFSVADMAKLAQETLDCQAELLCGGLGGPNRERVLQHLITGHPLLIPYDEDFNHEPCQKKGHKAHWAVSAGVLIGVQNVPSPGYIEDSELPGLFHPVPGAPHQPPSFPEESSPGALFLLSKQGKSWHYQLWDYSQVRESNL... | 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 ... |
J3S6Y1 | TSEAR_MOUSE | Thrombospondin-type laminin G domain and EAR repeat-containing protein (TSP-EAR) | MSALLMLCAVLLLLGTPSRGARPWEPCTDLRPLDILAEVVPLNGATSGIRMVQVEGVRGLQFSATEPRTTSFPASRIFSSCDFFPEEFSIIVTLRVPNLPPKKNEYLLSLLAEERDTLLLGLRYSPTQLHFLFLSEDLAGAWQTRVSFWSPGLMDSRWHTLILAVSQGSFSLTTDCGLPVDIMADVSFPPTLSVRGARFFIGSRKRTKGLFTGVIRQLVLLPGSDATPQLCPSRNARLAELSIPQVLKRLTGKPDDNEVLNYPYEADMKVTLGSRPPCTKAEGAQFWFDAAQKGLYLCAGSEWVSVLAAKTKLDYVEEHQ... | 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. |
J3TRD1 | L_HTRV | RNA-directed RNA polymerase L (Protein L) (EC 2.7.7.48) (Large structural protein) (Replicase) (Transcriptase) [Includes: cap-snatching endonuclease (EC 3.1.-.-)] | MNLEALCSRVLSERGLSTGEPGVYDQIFERPGLPNLEVTVDSTGVVVDVGAIPDSASQLGSSINAGVLTIPLSEAYKINHDFTFSGLTKTTDRKLSEVFPLVHDGSDSMTPDVIHTRLDGTVVVIEFTTTRSTNMGGLEAAYRSKLEKYRDPLNRRTDIMPDASIYFGIIVVSASGVLTNMPLTQDEAEELMFRFCVANEIYSQARAMDAEVELQKSEEEYEAISRARAFFTLFDYDDGKLSEAFPNSDIEMLRRFLSQPVDTSFVTTTLKEKEQEAYKRMCEEHYLKSGMSTKERLEANRSDAIDKTRALMERLHNMSS... | 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 cl... |
J3WAX0 | GP_HTRV | Envelopment polyprotein (M polyprotein) [Cleaved into: Glycoprotein N (Gn) (Glycoprotein G1); Glycoprotein C (Gc) (Glycoprotein G2)] | MIVPIVLFLTLCPSELSAWGSPGDPIVCGVRTETNKSIQIEWKEGRSEKLCQIDRLGHVTSWLRNHSSFQGLIGQVKGRPSVSYFPEGASYPRWSGLLSPCDAEWLGLIAVSKAGDTDMIVPGPTYKGKIFVERPTYNGYKGWGCADGKSLSHSGTYCETDSSVSSGLIQGDRVLWVGEVVCQRGTPVPEDVFSELVSLSQSEFPDVCKIDGVALNQCEQESIPQPLDVAWIDVGRSHKVLMREHKTKWVQESSAKDFVCFKVGQGPCSKQEEDDCMSKGNCHGDEVFCRMAGCSARMQDNQEGCRCELLQKPGEIIVNY... | [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... |
J4KMC1 | TENS_BEAB2 | Tenellin synthetase (TENS) (EC 2.3.1.-) (EC 6.3.2.-) (Hybrid PKS-NRPS synthetase tenS) (Tenellin biosynthesis protein S) | MSPMKQNESESHSVSEPIAIVGSAYRFPGGCNTPSKLWDLLQQPRDILKELDPERLNLRRYYHPDGETHGSTDVSNKAYTLEEDISRFDASFFGISPLEAASMDPQQRTLLEVVYESTETAGIPLDKLRGSLTSVHVGVMTTDWAQVQRRDPETMPQYTATGIASSIISNRISYIFDLKGASETIDTACSSSLVALHNAARALQSGDCEKAIVAGVNLILDPDPFIYESKLHMLSPDARSRMWDAAANGYARGEGAAAVVLKTLGHALRDGDRIEGVIRSTFVNSDGLSSGLTMPSSAAQTALIRQTYRKAGLDPVRDRP... | 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-amin... |
J4W0G2 | ATG1_BEAB2 | Serine/threonine-protein kinase ATG1 (EC 2.7.11.1) (Autophagy-related protein 1) | MTSRQEGASSHGSRRSSRHVGSFIIDREIGKGSFAQVYMGWHKESKAAVAIKSVELERLNKKLKENLYGEIQILKTLRHPHIVALHDCVESSTHINLIMEYCELGDLSLFIKKRDKLITHPATHDMARKYPSAPNSGLHEVVIRHFLKQLSSALEFLRAKNYVHRDVKPQNLLLLPSQAFREERALPIMEASQDSLIPISGLASLPMLKLADFGFARVLPSTSLADTLCGSPLYMAPEILRYERYDAKADLWSVGTVLYEMITGRPPFRARNHVELLRKIEAAEDVIKFPREVSVTPDLKALVRSLLKRSPVERLSFENF... | 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 selec... |
J5JV76 | BSLS_BEAB2 | Bassianolide nonribosomal cyclodepsipeptide synthetase (BSLS) [Includes: Nonribosomal peptide synthetase (EC 6.1.2.-); S-adenosyl-L-methionine-dependent N-methyltransferase (EC 2.1.1.-)] | MEPPNNANTGQLGPTLPNGTVDLPTDLSREITRHFGLEQDEIEEILPCTPFQRDVIECASDDKRRAVGHVVYEIPEDVDTERLAAAWKATVRYTPALRTCIFTSETGNAFQVVLRDCFIFARMYCPSAHLKSAIVKDEATAAVAGPRCNRYVLTGEPNSKRRVLVWTFSHSFVDSAFQGRILQQVLAAYKDEHGRVFSLQPTTDLVESENGDCLSTPASERTVGIERATQFWQEKLHGLDASVFPHLPSHKRVPAIDARADHYLPCPPFIQHEWSSTTVCRTALAILLARYTHSSEALFGVVTEQSHEEHPLLLDGPTST... | 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... |
J7FIX8 | IDTG_CLAPA | 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) (... | MAPSPIMPRYHVGPMASTRRAISKKGFPRTRSFPVLTAPLDYLRDSPGKDIRSGLTDAFNEFLCVPEDKVVTIKRIIDLLHNASLLIDDIQDDSKLRRGVPVAHSIFGIAQTINSANLAYFLAQQELKKLSNPDAFAIYTDELINLHRGQGMELHWRESLHCPTEEEYMRMVQNKTGGLFRLAIRLLQGESRSDRDYVPLVDTLGTLFQIRDDYQNLQSDVYSKNKGFCEDISEGKFSYPVIHSIRARPGDLRLLNILKQRSEDLMVKQYAVSYINSTGSFEFCRGKIDCLAQWANLQLAALEEAEGAGRGDKLRAVLRL... | 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... |
J7GQ11 | TYRDC_LEVBR | L-tyrosine decarboxylase (TDC) (EC 4.1.1.25) | MEKSNRSLKDLDLNALFIGDKAENGQLYKDLLNKLVDEHLGWRKNYIPSDPNMIGPEDQNSPAFKKTVGHMKTVLDQLSERIRTESVPWHSAGRYWGHMNSETLMPALLAYNYAMLWNGNNVAYESSPATSQMEEEVGQEFARLMGYDYGWGHIVADGSLANLEGLWYARNIKSLPFAMKEVNPELVAGKSDWELLNMPTKEIMDLLENAGSQIDEVKKRSARSGKNLQRLGKWLVPQTKHYSWMKAADIIGIGLDQVVPVPIDSNYRMDIQALESIIRKYAAEKTPILGVVGVAGSTEEGAVDGIDKIVALRQKLQKEG... | 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. |
J7H670 | OXLA_LACMT | L-amino acid oxidase Lm29 (LmLAAO) (LAO) (EC 1.4.3.2) | MNVFFMFSLLFLAALGSCADDRNPLGECFRETDYEEFLEIAKNGLRATSNPKHVVIVGAGMSGLSAAYVLAEAGHQVTVLEASERAGGRVRTYRNDKEGWYANLGPMRLPEKHRIVREYIRKFGLQLNEFHQENDNAWHFIKNIRKRVGEVKEDPGLLQYPVKPSEEGKSAGQLYEESLGKVAEELKRTNCSYILNKYDTYSTKEYLLKEGNLSPGAVDMIGDLLNEDSGYYVSFIESLKHDDIFGYEKRFDEIVDGMDKLPTSMYQAIKEKVRFNARVIKIQQNDREVTVTYQTSANEMSPVTADYVIVCTTSRATRRI... | 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, an... |
J7I4B7 | WBDD_ECOLX | 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)] | MTKDLNTLVSELPEIYQTIFGHPEWDGDAARDCNQRLDLITEQYDNLSRALGRPLNVLDLGCAQGFFSLSLASKGATIVGIDFQQENINVCRALAEENPDFAAEFRVGRIEEVIAALEEGEFDLAIGLSVFHHIVHLHGIDEVKRLLSRLADVTQAVILELAVKEEPFYWGVSQPDDPRELIEQCAFYRLIGEFDTHLSPVPRPMYLVSNHRVLINDFNQPFQHWQNQPYAGAGLAHKRSRRYFFGEDYVCKFFYYDMPHGILTAEESQRNKYELHNEIKFLTQPPAGFDAPAVLAHGENAQSGWLVMEKLPGRLLSDML... | 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... |
J7QLC0 | CYAA_BORP1 | 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] | MQQSHQAGYANAADRESGIPAAVLDGIKAVAKEKNATLMFRLVNPHSTSLIAEGVATKGLGVHAKSSDWGLQAGYIPVNPNLSKLFGRAPEVIARADNDVNSSLAHGHTAVDLTLSKERLDYLRQAGLVTGMADGVVASNHAGYEQFEFRVKETSDGRYAVQYRRKGGDDFEAVKVIGNAAGIPLTADIDMFAIMPHLSNFRDSARSSVTSGDSVTDYLARTRRAASEATGGLDRERIDLLWKIARAGARSAVGTEARRQFRYDGDMNIGVITDFELEVRNALNRRAHAVGAQDVVQHGTEQNNPFPEADEKIFVVSATG... | 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 intracellula... |
J7RUA5 | CAS9_STAAU | CRISPR-associated endonuclease Cas9 (EC 3.1.-.-) (SaCas9) | MKRNYILGLDIGITSVGYGIIDYETRDVIDAGVRLFKEANVENNEGRRSKRGARRLKRRRRHRIQRVKKLLFDYNLLTDHSELSGINPYEARVKGLSQKLSEEEFSAALLHLAKRRGVHNVNEVEEDTGNELSTKEQISRNSKALEEKYVAELQLERLKKDGEVRGSINRFKTSDYVKEAKQLLKVQKAYHQLDQSFIDTYIDLLETRRTYYEGPGEGSPFGWKDIKEWYEMLMGHCTYFPEELRSVKYAYNADLYNALNDLNNLVITRDENEKLEYYEKFQIIENVFKQKKKPTLKQIAKEILVNEEDIKGYRVTSTGK... | 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 n... |
J7SHB8 | FLDH_CLOS1 | Aromatic 2-oxoacid reductase (EC 1.1.1.110) (Indolelactate dehydrogenase) | MKILAYCVRPDEIDSFKNFSEKYGHTVDLIPDSFGPNVAHLAKGYDGISILGNDTCNREALEKIKDCGIKYLATRTAGVNNIDFDAAKEFGINVANVPAYSPNSVSEFTVGLALSLTRKIPFALKRVELNNFALGGLIGVELRNLTLGVIGTGRIGLKVIEGFSGFGMKKMIGYDIFENEKAKEYIEYKSLDEVYKEADIITLHAPLTDDNYHMIGKESIAKMKDGVFIINAARGALIDSEALIEGLKSGKIAGAALDSYEYEQGVFHNNKMNEIMKDDTLERLKSFPNVVITPHLGFYTDEAVSNMVEITLMNLQEFEL... | 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. |
J8G6Z1 | THSA_BACCS | NAD(+) hydrolase ThsA (BcThsA) (NADase ThsA) (EC 3.2.2.5) (Thoeris protein ThsA) | MKMNPIVELFIKDFTKEVMEENAAIFAGAGLSMSVGYVSWAKLLEPIAQEIGLDVNKENDLVSLAQYYCNENQGNRGRINQIILDEFSRKVDLTENHKILARLPIHTYWTTNYDRLIEKALEEENKIADVKYTVKQLATTKVKRDAVVYKMHGDVEHPSEAVLIKDDYEKYSIKMDPYIKALSGDLVSKTFLFVGFSFTDPNLDYILSRVRSAYERDQRRHYCLIKKEERRPDELEADFEYRVRKQELFISDLSRFNIKTIVLNNYNEITEILQRIENNIKTKTVFLSGSAVEYNHWETEHAEQFIHQLSKELIRKDFNI... | 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 ac... |
J8H9C1 | GAJA_BACC6 | Endonuclease GajA (EC 3.1.-.-) (Gabija protein GajA) (Nicking endonuclease GajA) | MKFSNITIKNFRNFEKVNINLDNKNVIFGMNDIGKTNFLYALRFLLDKEIRKFGFNKSDYHKHDTSKKIEIILTLDLSNYEKDEDTKKLISVVKGARTSANADVFYIALESKYDDKELYGNIILKWGSELDNLIDIPGRGNINALDNVFKVIYINPLVDLDKLFAQNKKYIFEESQGNESDEGILNNIKSLTDQVNQQIGEMTIIKGFQQEITSEYRSLKKEEVSIELKSEMAIKGFFSDIIPYIKKDGDSNYYPTSGDGRRKMLSYSIYNYLAKKKYEDKIVIYLIEEPEISLHRSMQIALSKQLFEQSTYKYFFLSTH... | 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 nucleo... |
J9VE33 | CRZ1_CRYNH | Transcriptional regulator CRZ1 | MADPASPPSFDAIFAQQPVRRSSSTSTSSFANYTYSALQQHQQFNSDAPLVDEPQSLSEQARKQQRDPSKDGNNKRYLDMMSGLADGYGVINGRRQESLRKESLPFNPQEDSTLIATAPKRGERNGLGRNGYSSPIGDIMFGPEQTIPNQPQQPSQQPPWGEGRMSEQSVHYASVQQPQYSSFQSSGPGAGSAGIDYLPRGTTSSMNDSMLSSQISPYLNHDVASEGQPPQQQQQQQQQQQGEWGQEFIGVEQQQQYAQGEGQSNGMEDMLTMGDESPFESELQRVISNTSHPSQYPSRTSSPFPQQSQSNMVPASTVNQ... | 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... |
J9VHN6 | 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.-) | 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... |
J9VI03 | DMT5_CRYNH | DNA (cytosine-5-)-methyltransferase DMT5 (EC 3.6.4.-) | MTTALTFGGGLFKDNTKFDIDMRGTADGAVNGGNIPNSQSQKRKRASPSPEIESEEDGDDWYEIDYIADSRVIRRKGRQILQYLIHWAGYAVHERTWEDEDGIGGEDCALVQEFYRKNPGKPRLSPSSVRKEVKLARMVEVVITTRRIDGKSRAASSTDQPSPHRLGITSPQANNIGGEDPNPSLTRRPVRSTVSEIAKRPTSKKVHPNKKCKASSDDESDFVFEEGEWDEDEDDDNDVDFRSSEDDEDDEQERSAEEPESDEEIIKPAKKTKSSLPKAKLRPKPANLGGFVTGVRPLNQGLDIKAAVRNMSDDLPPISD... | 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) | MAARNWSRVWVGGTVILISFIAFSSQIFVIWPWYGREISLDLLMLLVPLNLAAFMIFWNYRLCVITSPGTVPEGWRPNIGAMDGMEVKKGTHTPRYCKNCAHYKPPRAHHCRQCKTCWLKLDHHCPWIGNCVGFYNQGHFIRFLLWVDIGTTFHLIIMVRRVLYIAEYYHEPTLADVLFLVFNFATCVPVWLCVGMFSIYHVYLACGNSTTIEGWEKDKVATLIRRGKIKEVKYPYNIGIYKNIKSVLGPNPLLWLWPQKMQGDGLSFPVNPSAGDHMTQYFWPPQDPSRLPNPPPIPAHASPFVYGNNGFNPNLRPTNS... | 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 memb... |
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) (Ino... | MSSEAPIALLSVYDKTGLLPFAKSLKELGFRLLGSGGTAKMIREAGMEIEDVSNITKAPEMLGGRVKTLHPAVHGGILSRDIPSDLADLATNKISPITLVVCNLYPFVLQTAKPDCTLAGAIEEIDIGGVTLLRAAAKNHGRVSIISSPSDYETIVAELRAKGEVSAETRRGLAIKAFEDTKSYDEAISDYFRKVYATPGVEEEMKAGAGVGYQRLGLRYGANPHQKPAQAFVEQGEMPIKVLSGSPGYINLLDALNSWALVKELAAGLDLPAAASFKHVSPAGAAVGLPLDERAAKVFGVEDLKELSPLACAYARARGA... | 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... |
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) | MIPSTAAALLTLTAGAAFAHTGCGGHEIGRRNVGGPMLYRRAVTDEASAAVSTDINTECTAYSYAPVTELISSFPTIWQTASIPSNDTEAQQLFGKINSTLNTKIPNDVPHGTPTGDWTGVNYSNSDPDCWWTHNKCTTPSNDTGLQADISIAPEPMTWGLGFDDGPNCSHNALYDLLLENNQKATMFFIGSNVLDWPLQAMRAHDEGHEICVHTWSHQYMTALSNEVVFAELYYTQKAIKAVLGVTPQCWRPPYGDVDNRVRMIAEGLNLTTIIWSDDTDDWAAGTNGVTEQDVTNNYQSVIDKAGNGTYTTHGPVVLN... | 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 chit... |
J9VNT4 | CHS5_CRYNH | Chitin synthase 5 (EC 2.4.1.16) | MAQQPPPSRFLGVTDLSSLAVTEDTVLVTLQERYISHKPYTSLSPAALVFLSPYSHLPIDDEESLLHYVEEYYQCNNEEGGSRNEQGWWKKKMEQPHVFQLALSAYYNMRRTGQDQVIIASGPTGSGKSELKRLAIEAITQVSLANPGKKGSKIGLQVSSAEFILKCFGNAHTLSNDEASRFGTYTELQFNERGRLEGLKTIVYYFERSRVSQAPINGERNFHAFYYLVSGAPEEERNFLKLGDVSDYRYLNCRVRRVGVDDRHRYSQLRQAFKLMGISSRLIAQIFQLLASILHIGNLRFSPSDGIQEGASVINVETLD... | 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) | MFTFAAFSALLISLAGVVAQTTGTSVDSSILTKTADSTGPSGFSIPALSELTSGAPTDSTVALYSTFAAGATPTVSGAPVLPTSALTIADYPALDVTPPTNSSLVKDWMAKIDLSKVPSYNVTTGDCSTDAAAISDGRCWWTCGGCTRETDIVECPDKNVWGLSYDDGPSPFTPLLIDYLQEKNIKTTFFVVGSRVLSRPEMLQTEYMSGHQISIHTWSHPALTTLTNEEIVAELGWTMKVIKDTLGVTPNTFRPPYGDIDDRVRAIAAQMGLTPVIWTSYTDGSTTVNFDTNDWHISGGTATGASSYETFEKILTEYAP... | 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 o... |
J9VWU3 | ATM1_CRYNH | Iron-sulfur clusters transporter ATM1, mitochondrial (EC 7.-.-.-) | MGFGSCSRHALFTPAAFSGSFTTMTTSCFKRVYTAQIHGGDALGKRLPSVSSFSGQLPRHGLHRQSLAFFSTSHRRQTSPPPSPRTTSQSPTVPSKASTTPPTSLNTSKPIATESQDKTDWSIIVKLAGNIWPKNNPNVKFRVIGALTLLVAGKVLNVQVPFFFKTIVDSLNVPITESTTVWVLAGASIAGYGAARILTTLFGELRNAVFASVAQNAIRKVARETFEHLLNMDMKFHLERQTGGLTRAIDRGTKGISFILSSIVFHVIPTALEISMVCGILSWKFGWDFAAVTAITMLLYTWFTIKTTAWRTTFRKQANA... | 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-conju... |
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) | MSRPHLQQNVSFQDTKPPSRRAGRDDIPPRPPTKSDPSKASLTTTTTVQSVGGYNNHQLDFDDNAYVDAGSSNPQGFSDYNGVRRKKSMVRPERERIDPNHRLWHYREHAAEDQVDIQPSSTGNQPYNQYNNQRPGANLRRGKSLLARETDDVDDSSGLNIFKRGATIRRKASRATPRQAPTGAQSNRVSAGQKEDEECCCLGNFAPGPKNCWMIYCYLLTICIPGFVIAKVFGKKTPDAQRAWREKIGIVSIVLYLMGAVGFITFGFTQTVCGDTQLRLPGGSANTGSLVINGYDYDFSTWRHPVAGDTFNGTTSPLYM... | 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 chi... |
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) (Phospho... | MPEITAFPQPKSDLSILLLGAGGREHALAFKLAQSSRVARIVVCPGNGGTALMGGKVSNLALPWGAPPAFRSIVEWAQKENIDLVVPGPEQPLVDGVEGAFKKVGIPVFGPSPAAAMLEGSKSLSKEFMARHNIPTAAFRSFTSTQYEDAVAYIKSKPFTSGRSVIKASGLAAGKGVLIPETDEEAFAALKSVMVDKEFGDAGDEVVVEEYLSGPEISVLAFSDGYTIVPMPAAQDHKRIGEGDTGLNTGGMGAYAPAPIATKEIMERCVKDVLEPTIKGMREDGYPFVGMLFTGFMITADGPRVLEYNVRFGDPETQAL... | 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) | MMSWKFGKKFKEGGFLSGKHHSSNNNSPSDTSRSTTPTPGNPHPEDAVKPPVPRSGMLKIRVTAAKGLSLPQGVSVPAPVQEALTTHPTLASRIATSPPTAIVKAAGANRDSLQRRQVWWLPYLVLEFDKNEVLVDALGGDLASPVWMYSATFDVSRISEISATVYLRTREPHAEGREKSNGEGEGEDMGNSDLCLGSIRFTPNLDSLRVTDDWVTVQGGGGSGSINVQVSFKPASGQILTIDSFELLKVIGKGSFGKVMQVRKRDTLRIYALKTIRKAHIVSRSEVTHTLAERTVLAQVNCPFIVPLKFSFQSKEKLYL... | 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.-) | MAVDKEVELHAQAWDHALSYITPTALSAAVELEIPDILEDHGGLMSLSELSAASGCPREPLYRLMRFLIFHGIFTKSNDCYAQSPLSRVFTRENLGPYMLMQATPVTRSPAGLSGEALKTGTPLYLKSIRGEDSWNDPAYGFHMRAFTNGMAAHARLTAAAIVTNYPTAFNGVRSVVDVGGRHGMAIGKLVEAFPWVRGIAFDLPEVVADAPPRKGVDFVGGDMFESLPKADAVMLMWVLHDWSDDKCIEILKKCKEAIPTSTGKVMIVDAIINEEGEGDEFSGARLSLDMTMMAMTTQGKERSYKEWVHLLNEAGFSKH... | 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-proliferat... |
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.-) | MAVDKEVQLHAQAWEHALSYINSTALSAAVELEIPDILEDHGGLMSLSELSAASGCPREPLYRLMRFLIFHGIFTKSDDCYAQSPLSRLFTRENLGPYMLMQATPVTRSPAGLSGEALKTGTSLYLKSIRGEDSWSDPAYGYHMKAFTNAMIAHARLTAAAIVSNYPAAFDGLRSVVDVGGRHGTAIGRLVEAFPWVRGIAFDLPEIVADAPPRKGVDFVGGDMFESVPKADAVMLMWILHDWSDDKCIEILKKCKEAIPASTGKVMIVDAIINEDGEGDEFSGARLSLDMIMLAVMAQGKERTYKEWVHLLNEAGFSKH... | 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, a... |
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-me... | MGRDEEAAAQAEAWNHGFGFIKTSVIKTAIELEIPDILHNQGGPLSLSALSSAVGVPPDRLHRIMRFLAHHGVSKKTASPPGESDYYYAETAVSRSLTKDNLGPFVLLQGAQRGPSACITAQGLKSRERPGVEELGSDPLYEDPIFTEKVFRDAMTCHARVTTSAVIENYGEGFRGVGSLVDVGGSYGMTLGMLVEAFPWIRGICYDLPPVVAKAKPLHGVEFVAGSMFESVPKADVIMLMFVLHNWSDNECIDILKRCKEAIPAETGRLMIIDAIIDEDGEGDEFAGARLGLDVTMMAVTYEGKERTHREWAYILTEAG... | 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, an... |
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.-) | MVADEEAQLHAQAWDHALSYIKPTALSAAVELEIPDILENHGGPMTLSELSAASGCPREPLYRLMRFLIFHGIFTKSDDCYAQSPLSRLFTTENLGPYMLMQATPVTRCPTGLSGEALKTGTSLYLKSIRGEDSWSDPAYGYHMKAFTNAMTAHARLTAAAIVRNYPAAFDGVQSVVDVGSRHGTAIGKLVEAFPWVRGIAFDLPEIVADAPPRKGVDFVGGDMFESVPKADAVMLMWILHDWSDDKCIEILKKCKEAIPANIGKVMIVDAIINEDGEGDEFSGTRLSLDMIMLAVMAQGKERTYKEWVHLLNEAGFSKH... | 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, a... |
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-me... | MGRDEEAAARAEAWNHGFGFIKTSVIKTAIELEIPDILHNHGAPLSLSALSSAVGVPPDRLHRIMRFLTHHGVSKKTASPPGESDYYYAETAVSRSLTKDNLGAFVLLQGAQRGPSACITAQGLKSRERPGVEELGSDPLYEDPIFTKMVFRDAMACHARLTTSAVIENYGEGFRGVGSLVDVGGSYGMTLGMLVEAFPWIRGICYDLPQVVAKAKPLHGVEFVAGSMFESVPEADVVMLMFVLHNWSDNECIDILKRCKEAIPRETGKVMIIDAIIEEDGEGDEFAEARLGLDVTMMAVTFEGKERTHREWAFILKEAG... | 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, an... |
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 prote... |
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 (... |
K4C9E2 | NSY_SOLLC | Neoxanthin synthase, chloroplastic (EC 5.3.99.9) (Lycopene beta-cyclase) (EC 5.5.1.19) | METLLKPFPSLLLSSPTPYRSIVQQNPSFLSPTTKKKSRKCLLRNKSSKLFCSFLDLAPTSKPESLDVNISWVDPNSNRAQFDVIIIGAGPAGLRLAEQVSKYGIKVCCVDPSPLSMWPNNYGVWVDEFENLGLEDCLDHKWPMTCVHINDNKTKYLGRPYGRVSRKKLKLKLLNSCVENRVKFYKAKVWKVEHEEFESSIVCDDGKKIRGSLVVDASGFASDFIEYDRPRNHGYQIAHGVLVEVDNHPFDLDKMVLMDWRDSHLGNEPYLRVNNAKEPTFLYAMPFDRDLVFLEETSLVSRPVLSYMEVKRRMVARLRH... | Involved in the synthesis of neoxanthin, the last product of carotenoid synthesis and a precursor of abscisic acid. Involved in the beta-carotene biosynthesis. |
K4CI52 | ABAH2_SOLLC | Abscisic acid 8'-hydroxylase CYP707A2 (ABA 8'-hydroxylase CYP707A2) (SlCYP707A2) (EC 1.14.14.137) (Cytochrome P450 707A2) | MEFVSMLCLFTFISLTLLLIHSIFKFLAFASKKLPLPPGTLGLPYIGETFQLYSQNPNVFFASKVKKYGSIFKTYILGCPCVMISSPEAAKQVLVTKANLFKPTFPASKERMLGKQAIFFHQGDYHAKLRKLVLQAFKPDSIRNIIPDIESIAITSLESFQGRLINTYQEMKTYTFNVALISIFGKDEFLYREELKKCYYILEKGYNSMPINLPGTLFNKAMKARKELAKIVAKIISTRREMKIDHGDLLGSFMGDKEGLTDEQIADNVIGVIFAARDTTASVLTWILKYLGENPSVLQAVTEEQENIMRKKEVNGEEKV... | Negative regulator of fruit ripening involved in the oxidative degradation of abscisic acid (ABA). |
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) | MVQPHVLLVTFPAQGHINPSLQFAKRLIEMGIEVTFTTSVFAHRRMAKIAASTAPKGLNLAAFSDGFDDGFKSNVDDSKRYMSEIRSRGSQTLRDVILKSSDEGRPVTSLVYTLLLPWAAEVARELHIPSALLWIQPATVLDIYYYYFNGYEDEMKCSSSNDPNWSIQLPRLPLLKSQDLPSFLVSSSSKDDKYSFALPTFKEQLDTLDGEENPKVLVNTFDALELEPLKAIEKYNLIGIGPLIPSSFLGGKDSLESSFGGDLFQKSNDDYMEWLNTKPKSSIVYISFGSLLNLSRNQKEEIAKGLIEIQRPFLWVIRDQ... | 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) | MYELTPEQRTLQTQARELAQSVFASTAVQTDLTEQYPWDNVAQLRDAGFMGMMLPTSVGGRGLSTLDTVIVIEEMAKACATMGRITVDSNLGAIGAITKYGSEEQIKLAADLVLAGDKPAICISEPNAGSAASEMTTRADKNGDHYILNGEKYWITGGGVSKLHLIFARVFDDGVEQGIGAFITVLDDHGPEGLKVGRRLYAMGVRGIPETHLEFHDLKIHKSMMITFPDGLKRGFAALMSAYNAQRVGAGAVALGIAQCAFEEGVAYLKRREQFGRPLAEFQGLQWMVADMSVQLEAARLMLRSAAVSGETFPDINKAA... | 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). |
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 a... |
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 ... |
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 precurs... |
K5BDL0 | GGH_MYCHD | Glucosylglycerate hydrolase (GG hydrolase) (EC 3.2.1.208) | MPHDPSFTPTQLAARAAYLLRGNDLGTMTTAAPLLYPHMWSWDAAFVAIGLAPLSVERAVVELDTLLSAQWRNGMIPHIVFANGVDGYFPGPARWATATLADNAPRNRLTSGITQPPVHAIAVQRILEHARTRGRSTRAVAEAFLDRRWGDLMRWHRWLAECRDRNERGRITLYHGWESGMDNSPRWDSAYANVVPGKLPEYQRADNVIITDPSQRPSDGEYDRYLWLLEEMKAVRYDDERLPSVMSFQVEDVFFSAIFSVACQVLAEIGEDYKRPHADVKDLYLWAERFRAGVVETTDQRTGAARDFDVLAEKWLVTET... | 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 | Amiloride-sensitive sodium channel subunit beta (Beta-NaCH) (Epithelial Na(+) channel subunit beta) (Beta-ENaC) (Nonvoltage-gated sodium channel 1 subunit beta) (SCNEB) | MNLKKYFIRVLHRLQKGPGYTYKELLVWYCDNTNTHGPKRIIREGPKKKFIWFFLTLLFASLVFWQWGILITTYLSYSVSSSLSIGFKTMKFPAVTVCNASPFKYSKVRHLLRELDELTEAALERILQSKNRDATSALPLNSSETPSQTLNLRLWNQIPLVLIDESDPERPVIIDLFETDESGSGAQPNNSSPALVNVTSEAKKQKVAMKLCSRKALPNCIYRNFTSAAQAVTEWYILQSTSIFAKIPRNETVEMGYQPEDMILACLYGAEPCSYRNFTPIYHPDHGNCYIFNWGKDEEALFSSNPGAEFGLKLILDISQ... | 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 su... |
K7MTW9 | TAP1_SOYBN | Histone acetyltransferase TAP1 (GmTAP1) (EC 2.3.1.48) | MSMLSLLRSQLFNFMPIIHCLLKLNSTRKFKSFQLKAGFWESIKSGLMKNNSMQVIDPPSTDEENVEPLSQDFVLVEKTEPDGTIEQIIFSSGGDVDVYDLQALCDKVGWPRRPLSKLAAALKNSYIVASLHSIRKSHGSEGNEQKRLIGMARATSDHAFNATIWDVLVDPGYQGQGLGKALIEKLIRTLLQRDIGNITLFADSQVVEFYRNLGFEADPEGIKGMFWYPNH | 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 du... |
K7N5M8 | DYP2_AMYS7 | 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) | MPVDLSTTLSWKSATGEAATMLDELQPNILKAHVRDRLTVLFLGFGDAAEARTFLNGLSGLMKSARTHLQEVEAHKLTKAVGTPYLGVGLTAHGYATLGVTAPADPSFTAGAKAAVEKLADPAVTEWEGHYQQTIDAVLLLGDATAGPVRTLRRQVEALRPASVTVVGEESGLGLANANGDGIEHFGYVDGRSQPLFLTEDVDAERDTTDGVNDWDPSAPLEQVLVPDPAAPDPTVHFGSYFVFRKLEQNVRLFKEAERDLAHDLGLRGEDRERAGAMLVGRFEDGTPLTAQSAPGSHHPVGNDFSYDSDKLGQKCPFHA... | 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. |
K7N6K2 | TR34B_MOUSE | E3 ubiquitin-protein ligase TRIM34B (EC 2.3.2.27) (Tripartite motif-containing protein 34B) | MASTGPTNIQEKTTCPVCQELLTKALSLGCGHLVCQACLISNKNAVINPRGKSSCPVCGTRFSLENLQANKHLANVVERLGEVKLKPDIGTKRDLCVHHGEKLLLFCKEDKKVICWVCERSQEHRGHHTFLWEEAVRECQENLQKALTRLRKEQEKVETLEADIKEDRLSWKRQVQTERQRIQTGFNQLRRILDKEEQRELKRLREEEQMILDSLAGAEAELAQQSQLVEELISDLELRREWSDTELLQDMSGILKWSQIWTLKKPKAVSKKLSMVFQAPDLSGMLQKFRELSAVRAYWDNFTFNPENLNLNLILSEDHR... | 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... |
K7NBW3 | 74AC1_SIRGR | Mogroside IE synthase (EC 2.4.1.350) (UDP-glycosyltransferase 74AC1) | MEKGDTHILVFPFPSQGHINPLLQLSKRLIAKGIKVSLVTTLHVSNHLQLQGAYSNSVKIEVISDGSEDRLETDTMRQTLDRFRQKMTKNLEDFLQKAMVSSNPPKFILYDSTMPWVLEVAKEFGLDRAPFYTQSCALNSINYHVLHGQLKLPPETPTISLPSMPLLRPSDLPAYDFDPASTDTIIDLLTSQYSNIQDANLLFCNTFDKLEGEIIQWMETLGRPVKTVGPTVPSAYLDKRVENDKHYGLSLFKPNEDVCLKWLDSKPSGSVLYVSYGSLVEMGEEQLKELALGIKETGKFFLWVVRDTEAEKLPPNFVES... | 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. |
K7QHS5 | BCAT2_HUMLU | Branched-chain amino acid aminotransferase 2, chloroplastic (HlBCAT2) (EC 2.6.1.42) | MDCAAALLPGFHPNYLLCPSRHFSSLLPKTDLSSPLKFQLQNKQLSLASSHGFSPVICNATLSDTYSETVELADIDWDNLGFGFLPTDYMYNMKCAQGESFSNGELQRFGNIELSPSAGVLNYGQGLFEGLKAYRKEDGNILLFRPEENALRMRLGAERMCMPSPTVDQFVDAVKATVLANKRWIPPVGKGSLYIRPLLMGSGAVLGLAPAPEYTFLIYVSPVGNYFKEGVAPIHLIVEDNLHRATPGGTGGVKTIGNYAAVLKAQSAAKEQGYSDVLYLDCVHKKYLEEVSSCNIFVVKGNLIFTPAIKGTILPGITRK... | 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. |
K7QKH1 | BCAT1_HUMLU | Branched-chain amino acid aminotransferase 1, mitochondrial (HlBCAT1) (EC 2.6.1.42) | MIHRGLWLHNLVQSYRVGSSSSSSTLFKLVYRYNSSTSLAKSSLKQSCELSCKSNTEPSNMDWDKLGFKLMPTDYVYSMKCSNEGNFEQGRLELHGNIELSPAAAVLNYGQGIFEGTKAYRKEDGSLLLFRPDQNGVRMRIGAERMCMPSPSVDQFVDAVKQTAIANRRWVPPSGKGSLYIRPLLMGTGAVLGVAPAPQYTFLAYASPVGNYFKEGLAPLRLYVEDEFDRASPGGTGFVKTIGNYSRCLAALSRAKNKGFSDVLFLDSVHKKYVEELSSCNIFIVQGNQISTPAANGTILSGVTRSSIIEIARDHGFKVE... | 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. |
K7QRJ5 | PYRE3_STRRG | Dialkyldecalin synthase (EC 5.5.1.-) (FAD-dependent [4+2] cyclase) | MSDTVIIAGGGPVGLMLACELGLAGVDTVVLERHDAPREPSRGGAINATVVELFTQRGIMESLRDDGFEFRMAHFAHIPLAPERVPGDRAFSFAVPHAQVERRLEERARSLGVRVRRSTEITSVRQTPDGVQVTTGDGEVVEGAYLVGCDGSASLVREQAGIPFPGVDPDFHGLWGDIKVEPGAPVLERIGARQYELGLCMVAPIGPDTVRVITGEFDVPSPPADQEVGFDELRAAVARIAGVELDGVPGWLSRWTATSRQAERYREGRILLAGDAAHTLFPLGGQALGTGIEDAVNLGWKLAATVQGWAPPSLLDSYHE... | 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. |
K7QVW7 | PYRI4_STRRG | Spiro-conjugate synthase (EC 5.-.-.-) ([4+2] cyclase PyrI4) | MTTPQIDERAMEAGAAALQETIVDPGPLDVTALAVAAALAAGLHSAADDPAAALDKCIVLDELTEFAEKLVVHDRPGGIGTTVEYVEVYEDASGVRLGTATGNAVVLKMEPHMWQFHQSVSELADGSFEAVGVIDCTAMLRRMTQVLRVTGRSGRYAGKSGFMTLAISDPNQRPPHYSVQVVLC | 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. |
K7TLS0 | MYB69_MAIZE | MYB transcription factor 69 (ZmMYB69) (Myb-related protein 306) | MGRPPCCDKAGVKKGPWTPEEDIVLVSYVQEHGPGNWRAVPVSTGLMRCSKSCRLRWTNYLRPGIRRGNFTPHEEGIIVHLQALLGNRWAAIASYLPQRTDNDIKNYWNTHLKKKLRKQQAIGAIFAPPRPSEPTAGHADCRRHDMTRSSKDSHAACPADSTPAADEVVTQLIAQQFAATDGDTSSSSSYSYASSTDNISKLLNGFMMKSASPARDDATDTIKTSSAIDIDPFDHKSGGAALPPPKKRQQQQHLSSIENWLFDDATEQLVVQLMEEISGGSCSVPMLLY | Transcription factor that binds to the promoter of MYB31 and MYB42 and activates directly their expression, thus repressing lignin biosynthesis. |
K7U9N8 | OP1_MAIZE | Protein OPAQUE1 (Myosin XI motor protein) | MSYRKGLKVWVEEKGEGWVEAEVVEAKERAVVVFSSQRKKITVSPEKLLPRDTDEDLGGGHVDDMTKLTYLNEPGVLYNLKKRYALNEIYTYTGSILIAVNPFTRLPHLYNEYMMEQYKGIRLGELSPHVFAVADASYSRAMVNDSRSQSILVSGESGAGKTETTKLIMQYLTFVGGRAALDDRTVEQQVLESNPLLEAFGNAKTVRNDNSSRFGKFVEIQFDSSGRISGAAIRTYLLERSRVVQITDPERNFHCFYQLCASGKDAELYKLGHISSFHYLNQSNTHDLEGTNNEDEYWKTKRAMDIVGISREDQDAIFRT... | 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 simi... |
K7W9N9 | CPT6_SOLLC | (2Z,6Z)-farnesyl diphosphate synthase CPT6, chloroplastic (EC 2.5.1.92) (Cis-prenyltransferase 6) (SlCPT6) | MNSLFVGRPIVKSSYNVYTLPSSICGGHFFKVSNSLSLYDDHRRTRIEIIRNSELIPKHVAIIMDGNRRWAKARGLPVQEGHKFLAPNLKNICNISSKLGIQVITAFAFSTENWNRSSEEVDFLMRLFEEFFEEFMRLGVRVSLIGGKSKLPTKLQQVIELTEEVTKSNEGLHLMMALNYGGQYDMLQATKNIASKVKDGLIKLEDIDYTLFEQELTTKCAKFPKPDLLIRTGGEQRISNFLLWQLAYSELYFTNTLFPDFGEEALMDAIFSFQRRHRRFGGHTY | Uses neryl diphosphate to catalyze the cis-prenyl chain elongation and produce the 15 carbon product (2Z,6Z)-farnesyl diphosphate. |
K7WDL7 | IRIS_CATRO | (S)-8-oxocitronellyl enol synthase (EC 1.3.1.122) (Iridoid synthase) (ISY) | MSWWWKRSIGAGKNLPNQNKENGVCKSYKSVALVVGVTGIVGSSLAEVLKLPDTPGGPWKVYGVARRPCPVWLAKKPVEYIQCDVSDNQETISKLSPLKDITHIFYVSWIGSEDCQTNATMFKNILNSVIPNASNLQHVCLQTGIKHYFGIFEEGSKVVPHDSPFTEDLPRLNVPNFYHDLEDILYEETGKNNLTWSVHRPALVFGFSPCSMMNIVSTLCVYATICKHENKALVYPGSKNSWNCYADAVDADLVAEHEIWAAVDPKAKNQVLNCNNGDVFKWKHIWKKLAEEFGIEMVGYVEGKEQVSLAELMKDKDQVW... | 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, ... |
K7WIZ6 | RIBRX_MAIZE | 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.... | MPLPQPLLGGASPAPARAASSFLHPLLHTRHRVSTAPAAASSFVPASHSSHANDAMLLRRAADVADRSAGLTSPHPNFGCVIARPQLNTDSADSWVVGEGFLYAQGTPCAELLASQEAGEHARGGTAYLNLEPGDCFGDNTAVGSLVQAGITRVVVGLRHPLKHLRGKAIQALRNEGIQVDVVGEDLQSKLFKEALKSCLTVNAPLLYRAAFHVPFSVLKYAMTADGKIAASSGHASWISGKASRGRVFELRGRSDAVIVGGNTVRFDDPRLTARHVKGHVPVRIVMSQSLNLPEEANLWNLNDAYTIVATQRGARRDFQ... | 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 hydro... |
K7WQ45 | CPT2_SOLLC | Nerylneryl diphosphate synthase CPT2, chloroplastic (EC 2.5.1.142) (Cis-prenyltransferase 2) (SlCPT2) | MNSSIVSQHFFISLKSSLDLQCWKSSSPSSISMGEFKGIHDKLQILKLPLTMSDRGLSKISCSLSLQTEKLRYDNDDNDDLELHEELIPKHIALIMDGNRRWAKAKGLEVYEGHKLIIPKLKEICDISSKLGIQVITAFAFSTENWKRSKEEVDFLMQLFEEFFNEFLRFGVRVSVIGCKSNLPMTLQKCIALTEETTKGNKGLHLVIALNYGGYYDILQATKSIVNKAMNGLLDVEDINKNLFEQELESKCPNPDLLIRTGGEQRVSNFLLWQLAYTEFYFTNTLFPDFGEKDLKKAILNFQQRHRRFGGHTY | Uses dimethylallyl diphosphate and isopentenyl diphosphate to catalyze the cis-prenyl chain elongation and produce the 20 carbon product nerylneryl diphosphate. |
K7ZP88 | ATAA_ACIS5 | Trimeric autotransporter adhesin AtaA (TAA AtaA) (Type 5 secretion system autotransporter AtaA) | MNKIYKVIWNATLLAWVAVSELAKGKTKSTTSKSKAKSLSSSVIVGGIILTTPLSLIAATVQVGGGTNSGTTATASTNCADLYNYQNPENSGSGAAGNYNAGNPSVCSIAIGENAQGGTSGTGGSPGIAIGGNSKATGGLSVAIGGYAQATNVGSIALGTAALSSGFNSLAISRQAAATNNYSIAIGTTSVSKGVGSIAMGHSTNASGDQSIAIGSSDAVNSATATTTYDGTTNTQASGSKSIAIGASAKASTNNSIALGAGSVTSAQSGNSYLTGVGASATNGVVSVGTSTATRRIQNVADGSAASDAVTVAQLDKAYD... | 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 b... |
K8DWB5 | CA1D_CONTE | Alpha-conotoxin TxID (Alpha-conotoxin TxIC) | FDGRNAAGNDKMSALMALTTRGCCSHPVCSAMSPICG | 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)=4... |
K8ERR8 | LSY12_CAEEL | Histone acetyltransferase lsy-12 (EC 2.3.1.48) | MGKKRKPSPERSSDEDEVSTPSPKDRTARPTAAARRENVALSQAVALSLEDASNFCSLAFSLERIKREPVDTDYDDPNQPGPSSVPVSARTDHVLPIRFKIKAEPQEYDSDEYGKDHGAVQIANKEVPAISPIEEVSQKRRGRPRKTDAAQHLFFPHVSIKQEPDDGFINFHESRCVGIAQDPEMQHLHDVNESHSSEIAIFRETKKITERKKKKTEAEKLWDNMSLTEKEVFQSHTRRRRTTRLPIIQNFEETEEGCIVEVPIPLIDLDNDAVESVTGPQHENVTVSENVLSTESTDQEVTETKRLHDSSRDFNPPRIQ... | 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. |
K8ESC5 | ATG41_CAEEL | Cysteine protease atg-4.1 (EC 3.4.22.-) (Autophagy-related protein 4 homolog 1) | MLSILPLAYSNFSRILQYFEQLPVVDKMTEEILKQGVGIVETSLTFEPPFCESFERISIDNFPIFALGKEISKEDGIEAMKKYVTSRFWFTYRRDFSPIGGTGPSTDQGWGCMLRCAQMLLGEVLLRRHIGRHFEWDIEKTSEIYEKILQMFFDEKDALYSIHQIAQMGVTEGKEVSKWFGPNTAAQVMKKLTIFDDWSNIAVHVALDNILVKEDAITMATSYPSEDAVKLIMENGLVDKNRLSLSPGNIIPEWRPLLLMIPLRLGLTTINPCYLSAIQEFFKIPQCVGIIGGRPNHALYFVGMSGSKLFYLDPHYCRPK... | 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 (P... |
K8FE10 | SYT2_CAEEL | Synaptotagmin 2 | MWATGAIVCSPVFRILSTCCPIRRGVPTSNGYHPRPKHVDIGNGAVPILSSKPITVQPTNSDYYEPVNNGTLPLSSSGALIKQYGNIHFRVEYDFEQSKLSVTIVSASDLPAMDRNGMSDPYVKVYVLPERKQKFETRIIRNTLNPTYNETFQFSIPFNELHSKTLMLVVYDYDRLSKDDKMGQLSVPLESIDFGITTDIERPLQKPEKDDEKECRLGDICFSTRYRPATGTVTLTIMEARNLKKMDVGGSSDPYVKIYLHHGRKLLSKKKTSRKYKTLNPYYNESFQFKIEPHMIEKVHLIVSVWDYDKMSKNDFIGEV... | 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. |
K9IMD0 | TRLF_DESRO | Lactotransferrin (Lactoferrin) (EC 3.4.21.-) (Draculin) (Draculin-1) | MKLLFLALLSLLALGPSLAARRRGVRWCTISKPEAAKCSKLQQNLKRVRGPSLSCISRKSYLECIQAIAAKRADAMSLDAGLVYEAGQDPYRLRPVAAEVYGTEGAPRTHYYAVALVKKDSNLQLNQLQGVRSCHTGLNRSAGWKIPVGTLRPYLGWAGPPAPLQEAVANFFSASCVPCADGNQYPNLCRLCAGTGADKCACSSKEPYFGYSGAFKCLKDGAGDVAFVKDSTVFENLPNKAERDQYELLCPDNTRKPVDEFEQCHLARVPSHAVVARSVGGKEDSIWRLLSKAQEKFGKGTSGSFQLFSSPPGQKDLLFK... | 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. Antimicro... |
K9JHZ4 | TET3B_XENLA | Methylcytosine dioxygenase tet3-B (EC 1.14.11.80) | METQPASVPCVLPQDVYEFSEDRESLGRLRVSEMPSELNGGGDGSKGDGAAVVATEVSQQSNKKRKRCGVCVPCLRKEPCGTCYNCVNRSTSHQICKMRKCEQLKKKRVVPMKGVEAVDKDDAKNQAKEQVPSVKNCSESILVDGPKTDQMEAGPVNHVQEGRLKQECDSTLPSKGSEDLANQLLMEANSWLSNTAAPQDPCNKLNWDKPIIPNHIAANNNSNLEDAKNLVAFSAVAEAMSNYGMPASGTPSSISMQLYEKFNYETNQDNSGHSEGNAPSCPEDLNTLKEALALAKHGVKPPNCNCDGPECPDYLEWLEN... | 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. Selectivel... |
K9M1U5 | IFNL4_HUMAN | Interferon lambda-4 (IFN-lambda-4) | MRPSVWAAVAAGLWVLCTVIAAAPRRCLLSHYRSLEPRTLAAAKALRDRYEEEALSWGQRNCSFRPRRDPPRPSSCARLRHVARGIADAQAVLSGLHRSELLPGAGPILELLAAAGRDVAACLELARPGSSRKVPGAQKRRHKPRRADSPRCRKASVVFNLLRLLTWELRLAAHSGPCL | Cytokine that may trigger an antiviral response activating the JAK-STAT pathway and up-regulating specifically some interferon-stimulated genes. |
K9N4V7 | NCAP_MERS1 | Nucleoprotein (Nucleocapsid protein) (NC) (Protein N) | MASPAAPRAVSFADNNDITNTNLSRGRGRNPKPRAAPNNTVSWYTGLTQHGKVPLTFPPGQGVPLNANSTPAQNAGYWRRQDRKINTGNGIKQLAPRWYFYYTGTGPEAALPFRAVKDGIVWVHEDGATDAPSTFGTRNPNNDSAIVTQFAPGTKLPKNFHIEGTGGNSQSSSRASSVSRNSSRSSSQGSRSGNSTRGTSPGPSGIGAVGGDLLYLDLLNRLQALESGKVKQSQPKVITKKDAAAAKNKMRHKRTSTKSFNMVQAFGLRGPGDLQGNFGDLQLNKLGTEDPRWPQIAELAPTASAFMGMSQFKLTHQNND... | 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 replic... |
K9N5Q8 | SPIKE_MERS1 | Spike glycoprotein (S glycoprotein) (E2) (Peplomer protein) [Cleaved into: Spike protein S1; Spike protein S2; Spike protein S2'] | MIHSVFLLMFLLTPTESYVDVGPDSVKSACIEVDIQQTFFDKTWPRPIDVSKADGIIYPQGRTYSNITITYQGLFPYQGDHGDMYVYSAGHATGTTPQKLFVANYSQDVKQFANGFVVRIGAAANSTGTVIISPSTSATIRKIYPAFMLGSSVGNFSDGKMGRFFNHTLVLLPDGCGTLLRAFYCILEPRSGNHCPAGNSYTSFATYHTPATDCSDGNYNRNASLNSFKEYFNLRNCTFMYTYNITEDEILEWFGITQTAQGVHLFSSRYVDLYGGNMFQFATLPVYDTIKYYSIIPHSIRSIQSDRKAWAAFYVYKLQP... | [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 membra... |
K9N638 | R1A_MERS1 | 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... | MSFVAGVTAQGARGTYRAALNSEKHQDHVSLTVPLCGSGNLVEKLSPWFMDGENAYEVVKAMLLKKEPLLYVPIRLAGHTRHLPGPRVYLVERLIACENPFMVNQLAYSSSANGSLVGTTLQGKPIGMFFPYDIELVTGKQNILLRKYGRGGYHYTPFHYERDNTSCPEWMDDFEADPKGKYAQNLLKKLIGGDVTPVDQYMCGVDGKPISAYAFLMAKDGITKLADVEADVAARADDEGFITLKNNLYRLVWHVERKDVPYPKQSIFTINSVVQKDGVENTPPHYFTLGCKILTLTPRNKWSGVSDLSLKQKLLYTFYG... | 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 transl... |
K9N7C7 | R1AB_MERS1 | 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 prot... | MSFVAGVTAQGARGTYRAALNSEKHQDHVSLTVPLCGSGNLVEKLSPWFMDGENAYEVVKAMLLKKEPLLYVPIRLAGHTRHLPGPRVYLVERLIACENPFMVNQLAYSSSANGSLVGTTLQGKPIGMFFPYDIELVTGKQNILLRKYGRGGYHYTPFHYERDNTSCPEWMDDFEADPKGKYAQNLLKKLIGGDVTPVDQYMCGVDGKPISAYAFLMAKDGITKLADVEADVAARADDEGFITLKNNLYRLVWHVERKDVPYPKQSIFTINSVVQKDGVENTPPHYFTLGCKILTLTPRNKWSGVSDLSLKQKLLYTFYG... | 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 transl... |
K9NBS6 | AAM_RHOER | Acylamidase (EC 3.5.1.13) (EC 3.5.1.14) (EC 3.5.1.4) | MTEQNLHWLSATEMAASVASNNLSPNEIAEAMIQRVDAVNPSINAIVQFDREQVTRDAAELSRQQEAGEKLGPLHGVPFTIKDLTAVDGLPTTFGMKPMADNIATGNAVVVDRLRGAGGLFLGKTNTPESGYYGGTDNHLYGPTHNPWKLGNSAGGSSGGASAAVAAGLGPLAEGSDGAGSVRIPSALCGVVGLKPTTGVIPQTILAGRFYNWAYHGPITRTVADNALMLDIMAGPDNADPLSIERAETSYVEASKGDVKGLRVAWSPNLGLGHVDPEVLAVCLDALAAFEELGAQITEATPQWGNPSESMWSGIWVPGF... | 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 (iso... |
K9UJK2 | TM175_CHAP6 | Potassium channel Cha6605_3372 (Transmembrane protein 175) (CmTMEM175) | MVEAPEQSETGRIEAFSDGVFAIAITLLVLEIKVPQHKIVETVGLVSSLLSLWPSYLAFLTSFASILVMWVNHHRIFSLVARTDHAFFYWNGLLLMLVTFVPFPTALLAEYLIHPQARVAASVYAGIFLAIAIVFNRLWKHAATADRLLAQKADRHEVDAITKQYRFGPGLYLVAFALSFISVWLSVGVCFVLAIYFALRSNA | Potassium channel. The channel is permeable for K(+), Rb(+) and Cs(+), while it is unable to conduct Na(+). |
K9USW8 | A1O_LOXGA | 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)] | ADNRRPIWVMGHMVNSLAQIDEFVGLGSNSIETDVSFDKQANPEYTYHGIPCDCGRACLHSTKFNDFLKGLRKVTTPGDSKYLEKLILVVFDLKTGSLYDNQAYDAGTKLAKNLLQHYWNNGNNGGRAYIILSIPNLNHYKLITGFKETLKNEGHEELLEKVGTDFSGNDDISDVQKTYNKAGVTGHVWQSDGITNCLLRGLTRVKAAVANRDSGSGIINKVYYWTVDKRQSTRDTLDANVDGIMTNYPDITVEILNEAAYKKKFRIATYEDNPWETFKG | [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... |
L0DSL2 | NIR_THIND | Cytochrome c-552 (EC 1.7.2.2) (Cytochrome c nitrite reductase) (TvNiR) | MNDLNRLGRVGRWIAGAACLFLASAAHAEPGENLKPVDAMQCFDCHTQIEDMHTVGKHATVNCVHCHDATEHVETASSRRMGERPVTRMDLEACATCHTAQFNSFVEVRHESHPRLEKATPTSRSPMFDKLIAGHGFAFEHAEPRSHAFMLVDHFVVDRAYGGRFQFKNWQKVTDGMGAVRGAWTVLTDADPESSDQRRFLSQTATAANPVCLNCKTQDHILDWAYMGDEHEAAKWSRTSEVVEFARDLNHPLNCFMCHDPHSAGPRVVRDGLINAVVDRGLGTYPHDPVKSEQQGMTKVTFQRGREDFRAIGLLDTADS... | 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. |
L0E155 | MALA_MALAU | Flavin-dependent halogenase malA (EC 1.14.-.-) (Malbrancheamide biosynthesis cluster protein A) | MAPTPKYTFTERAAAGNLSDAEILNSNNPTGSELPDESDVVVGGAGIHGLIYALHASKYKPNNLKISVIEKNTRPGYKIGESTLPIFYTWCKLHGISAAYLLRLFGLKDGLCFYFLDRENQGQYTDFCSVGAPGLVLASLQIERPMSELLFTILAQRNGVNVYHGREVDFKSTVVQGGGQGNKIAVSRGKYDSTPKTIDSALFVDATGRFRQFCSKKAPRHRFDGWNCNAFWGYFTAPKDESKIPFDLYEGDHTNHLCFPEGWVWVIRLPSWEGSLIANLMDMVTYILECADAGVPGDELPSSEELARMFGLKFQWVTSI... | 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-pr... |
L0E4H0 | PHQK_PENFE | FAD-dependent monooxygenase phqK (EC 1.-.-.-) (Paraherquamide biosynthesis cluster protein K) | MGSLGEEVQVIIVGLGIVGLAAAIECREKGHSVHAFEKSNILKSIGDCIGLQSNATRIIKRWGDGAVHEALRPWIVSSKEIRIHNSSGRLIIRQDLSEVCEQPNYLLPRSELIRVMYEHALKIGVEISLGVEVCEPSEDEEGASVVALTRDGERQIVRGDFIICSDGVHSKMRKAIMPQPVEPRPSGYAAFRALVDTETLKGDPEASWVFEGVEENDRFDVFFLSGAQIALQSCNKGKVFSWFCIHQDTRNLLDVWTSPADPNEMLDLIKVWPIGQRLWSVIRHTQPQKFINYPLLNHKPLDHWVSSHGRLILIGDAAHP... | 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 i... |
L0L3V3 | FRE21_SPHLA | Frenatin 2.3S (F2.3S) [Cleaved into: Frenatin 2.1S (F2.1S)] | 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 do... |
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