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Database: UniProt
Entry: V2YCL3_MONRO
LinkDB: V2YCL3_MONRO
Original site: V2YCL3_MONRO 
ID   V2YCL3_MONRO            Unreviewed;       522 AA.
AC   V2YCL3;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   SubName: Full=Cytochrome p450 {ECO:0000313|EMBL:ESK89434.1};
GN   ORFNames=Moror_16153 {ECO:0000313|EMBL:ESK89434.1};
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:ESK89434.1, ECO:0000313|Proteomes:UP000017559};
RN   [1] {ECO:0000313|EMBL:ESK89434.1, ECO:0000313|Proteomes:UP000017559}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MCA 2997 {ECO:0000313|EMBL:ESK89434.1,
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|ARBA:ARBA00010617, 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:ESK89434.1}.
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DR   EMBL; AWSO01000561; ESK89434.1; -; Genomic_DNA.
DR   RefSeq; XP_007851259.1; XM_007853068.1.
DR   AlphaFoldDB; V2YCL3; -.
DR   KEGG; mrr:Moror_16153; -.
DR   HOGENOM; CLU_001570_2_3_1; -.
DR   OrthoDB; 1563065at2759; -.
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   CDD; cd11065; CYP64-like; 1.
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; PTHR46300:SF7; P450, PUTATIVE (EUROFUNG)-RELATED; 1.
DR   PANTHER; PTHR46300; P450, PUTATIVE (EUROFUNG)-RELATED-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|ARBA:ARBA00023033,
KW   ECO:0000256|RuleBase:RU000461};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000461};
KW   Reference proteome {ECO:0000313|Proteomes:UP000017559};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           24..522
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004712752"
SQ   SEQUENCE   522 AA;  58575 MW;  9B5DEB703E1EE9B3 CRC64;
     MPSQLHLISL CLLLLVALLL VRSRSQKARN LLPPGPKPLP LIGNLLDVPQ SFEWKTYAEW
     SQLYQSDILS INVFGSPMII LNSPQLASDL LEKRSSVYSS RPTGFAVMLT ELIGWKNIFI
     FKPYGKEVTE SRKLVHQELS AKDTSRYRPQ IQKSVRMLLF NLLKTNGGTI SGELVDLLKY
     LLGTICLSTI YGITAEGTED PFIAAANRAT IGFTAAVIPG KFAVDWIPLL RYIPSWLPGA
     GFQRKAQTWK QDLMRMVDGP FEAVQRKIIS GEHVSPSFLS RCLEKLSGDT SAEKLHFLKF
     VAGSLFAGGT DTVVTALHTF FLAMVCYPDV QKKAHCELDR VVGSERLPDY EDVEALLYVR
     AVVYETLRWQ PVTPLGPLRA TTEEDVYKGY RIPKGATVVT NAWAFLHDSD VYGSDCEIFN
     PDRWLTDEGN LKSEKDMPRP FAQFGYGRRQ CPGQHLAMAT LYLGIASVLH TFSVRKAIDE
     DGKEITPPQA YISSFQNRPA EFPCRIEVRS PVHERLVREI AE
//
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