ID V2XTM2_MONRO Unreviewed; 485 AA.
AC V2XTM2;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE SubName: Full=Cytochrome p450 {ECO:0000313|EMBL:ESK95890.1};
GN ORFNames=Moror_12298 {ECO:0000313|EMBL:ESK95890.1};
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:ESK95890.1, ECO:0000313|Proteomes:UP000017559};
RN [1] {ECO:0000313|EMBL:ESK95890.1, ECO:0000313|Proteomes:UP000017559}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MCA 2997 {ECO:0000313|EMBL:ESK95890.1,
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}.
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:ESK95890.1}.
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DR EMBL; AWSO01000058; ESK95890.1; -; Genomic_DNA.
DR RefSeq; XP_007844773.1; XM_007846582.1.
DR AlphaFoldDB; V2XTM2; -.
DR KEGG; mrr:Moror_12298; -.
DR HOGENOM; CLU_001570_2_3_1; -.
DR OrthoDB; 1611696at2759; -.
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:InterPro.
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; 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.
PE 3: Inferred from homology;
KW Monooxygenase {ECO:0000256|ARBA:ARBA00023033};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023033};
KW Reference proteome {ECO:0000313|Proteomes:UP000017559};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..485
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004711874"
SQ SEQUENCE 485 AA; 55403 MW; 1D4F83F453D68472 CRC64;
MPLLALCIYS VSILLIAAIW KKSLSRQSDQ KYPPGPPGRL IVGNLHDIPG KKPWVVYAEW
AKKYGDIMHL QVMNDHILVL SSVKVVNDLL EKRSRTYSGR PFADIAEITG WGFSLAGQNY
SEMWRKNRRV YQQILRPDAV VELRPVIQQC ISKFSRNLLS NPKDFMSHID VLSGGLALKT
MYGINVTAGD DPMISVAKIA THTADKIFEP FFIAILQYCP FIMSVPRWIP VLGPIRRYVE
ITRKHLEEFR ELPIQHIQRN TESGFENDGV VPRFLKRLDT EDASSMDEIH RIKDVASTIY
AAAADTTLSS IGTFFLAMVR NAQSQRTAQQ EIDTVVGRNR LPDLGDREKL PFIEAVYREV
MRWHPAVPIG VPHLTTDHDE YCGYFIPQDT IIFANIWAMT HDEKVYPEPY DFRPERFLNM
KVNINDVLAY GFGRRICVGR HLADAELWLT FASVLACFNI DKERDEQGKD IDVPERYSDG
PGLFS
//
