ID A0A135RXS8_9PEZI Unreviewed; 504 AA.
AC A0A135RXS8;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=Cytochrome P450 {ECO:0000313|EMBL:KXH28471.1};
GN ORFNames=CNYM01_10582 {ECO:0000313|EMBL:KXH28471.1};
OS Colletotrichum nymphaeae SA-01.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum acutatum species complex.
OX NCBI_TaxID=1460502 {ECO:0000313|EMBL:KXH28471.1, ECO:0000313|Proteomes:UP000070054};
RN [1] {ECO:0000313|EMBL:KXH28471.1, ECO:0000313|Proteomes:UP000070054}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SA-01 {ECO:0000313|EMBL:KXH28471.1,
RC ECO:0000313|Proteomes:UP000070054};
RA Baroncelli R., Thon M.R.;
RT "The genome sequence of Colletotrichum nymphaeae SA-01.";
RL Submitted (FEB-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000256|ARBA:ARBA00001971};
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:KXH28471.1}.
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DR EMBL; JEMN01001720; KXH28471.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A135RXS8; -.
DR Proteomes; UP000070054; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; cd11058; CYP60B-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; PTHR24305; CYTOCHROME P450; 1.
DR PANTHER; PTHR24305:SF230; CYTOCHROME P450 MONOOXYGENASE STHF; 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|ARBA:ARBA00022617, ECO:0000256|RuleBase:RU000461};
KW Iron {ECO:0000256|RuleBase:RU000461}; Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|RuleBase:RU000461};
KW Monooxygenase {ECO:0000256|RuleBase:RU000461};
KW Oxidoreductase {ECO:0000256|RuleBase:RU000461};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 21..42
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 504 AA; 57319 MW; CEE00FEFFEE5111E CRC64;
MSDHSTGFTA QILNIHTLCS AFALIITLGV AYLFGTIIYN VFFHPLRVYP GPKLWAASRI
PFTRATLSGQ VHRKILALHQ EYGPIVRVAP NELAYNSPDA WKDLHGHLKN GTGDHGRDPV
ATQDSRHGII GANREDHSRF RRALSHGFSA QSMLEQEPIV KKYVDLLFQR LHEKCAGGAE
ALNMVAWYNW TTFDVIGDLA FGEPFHCLDD SGYHPWVKLI FDGIKGNSFK NCMRRFPPIE
KLLMHLIPAD LRNKRDQHIA LTKEKVSKRL AMETDRPDFM DSMLRTKGPQ KLTFEELKSN
SSVLIIAGSE TTATALSAIT YYLCTNRQAL DKLTHEVRTA FSSEEEIEMV SAQQLQYMQA
VMNEGLRMYP PVPTGIVRRV TDDGGVFLGQ YVPSGTLVQV WHWPAFHSPE NFTLPDSFIP
ERWLDDARFS GDKKEAFQPF SVGPRNCIGR NLAYAEMRLI LARMIWNFDM KLSEESRGWD
DKSQVYLLWE KGPVNVYLTP REKA
//
