ID V2XNW8_MONRO Unreviewed; 515 AA.
AC V2XNW8;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Cytochrome p450 {ECO:0000313|EMBL:ESK95447.1};
GN ORFNames=Moror_1001 {ECO:0000313|EMBL:ESK95447.1};
OS Moniliophthora roreri (strain MCA 2997) (Cocoa frosty pod rot fungus)
OS (Crinipellis roreri).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Marasmiineae; Marasmiaceae; Moniliophthora.
OX NCBI_TaxID=1381753 {ECO:0000313|EMBL:ESK95447.1, ECO:0000313|Proteomes:UP000017559};
RN [1] {ECO:0000313|EMBL:ESK95447.1, ECO:0000313|Proteomes:UP000017559}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MCA 2997 {ECO:0000313|EMBL:ESK95447.1,
RC ECO:0000313|Proteomes:UP000017559};
RX PubMed=24571091; DOI=10.1186/1471-2164-15-164;
RA Meinhardt L.W., Costa G.G.L., Thomazella D.P.T., Teixeira P.J.P.L.,
RA Carazzolle M.F., Schuster S.C., Carlson J.E., Guiltinan M.J.,
RA Mieczkowski P., Farmer A., Ramaraj T., Crozier J., Davis R.E., Shao J.,
RA Melnick R.L., Pereira G.A.G., Bailey B.A.;
RT "Genome and secretome analysis of the hemibiotrophic fungal pathogen,
RT Moniliophthora roreri, which causes frosty pod rot disease of cacao:
RT mechanisms of the biotrophic and necrotrophic phases.";
RL BMC Genomics 15:164-164(2014).
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000256|ARBA:ARBA00001971};
CC -!- PATHWAY: Secondary metabolite biosynthesis.
CC {ECO:0000256|ARBA:ARBA00005179}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family.
CC {ECO:0000256|RuleBase:RU000461}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ESK95447.1}.
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DR EMBL; AWSO01000082; ESK95447.1; -; Genomic_DNA.
DR RefSeq; XP_007845261.1; XM_007847070.1.
DR AlphaFoldDB; V2XNW8; -.
DR STRING; 1381753.V2XNW8; -.
DR KEGG; mrr:Moror_1001; -.
DR HOGENOM; CLU_001570_5_11_1; -.
DR OrthoDB; 1609276at2759; -.
DR Proteomes; UP000017559; Unassembled WGS sequence.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
DR Gene3D; 1.10.630.10; Cytochrome P450; 1.
DR InterPro; IPR001128; Cyt_P450.
DR InterPro; IPR017972; Cyt_P450_CS.
DR InterPro; IPR002401; Cyt_P450_E_grp-I.
DR InterPro; IPR036396; Cyt_P450_sf.
DR PANTHER; PTHR24305; CYTOCHROME P450; 1.
DR PANTHER; PTHR24305:SF242; CYTOCHROME P450 MONOOXYGENASE ATNE-RELATED; 1.
DR Pfam; PF00067; p450; 1.
DR PRINTS; PR00463; EP450I.
DR PRINTS; PR00385; P450.
DR SUPFAM; SSF48264; Cytochrome P450; 1.
DR PROSITE; PS00086; CYTOCHROME_P450; 1.
PE 3: Inferred from homology;
KW Heme {ECO:0000256|RuleBase:RU000461}; Iron {ECO:0000256|RuleBase:RU000461};
KW Metal-binding {ECO:0000256|RuleBase:RU000461};
KW Monooxygenase {ECO:0000256|RuleBase:RU000461};
KW Oxidoreductase {ECO:0000256|RuleBase:RU000461};
KW Reference proteome {ECO:0000313|Proteomes:UP000017559}.
SQ SEQUENCE 515 AA; 57071 MW; A6CC5381DE741C4A CRC64;
MDTVLLAILL GLSGWIISYL WSSSRAIPDV DGPPSPSVIF GHSSQVAKAP VGTLYKRWQE
LYGPTFLLKG RFRQSRLIIN DPKGLNYVLQ GRNFERNPGK KAALELFFGR GVFSAEGDEH
RKMRKTLNRP FSNQSIQEIS HVFFDLTNRL VRTWEEKLES NPNATFDVTI DVNRLALDAI
TMTMLSHDLN AENSDVGPLL ARMMHSPPGG GIELLLRGLG ALFPAVLKMP SSMKSYTDNL
RSALGAIARD AWSGREVTGT HAKLLHALAE DNVSEDETIA QIITVIFAGS ETTANVITEC
LWELAKNQSI QKKLRTELLD FEATSGRKPT YEDLNGSTTL PYLDAVTRET LRTKAVLRSV
TRVVVQDDVI PLYNPIKRKS TGVEVYEVVV KAGTTLEIPL RDGINVSKAI WGEDAASFRP
ERWLDPTGLP ETVKLVRAQG HVLSFGDGPK VCLGRSFAIA EFKIVLSHII RSFSFEEVVG
VQFDFYHVGQ TTIKPVIRGR EDEGTQLPLK VSLAS
//
