ID M7TW14_BOTF1 Unreviewed; 523 AA.
AC M7TW14;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE SubName: Full=Putative cytochrome p450 protein {ECO:0000313|EMBL:EMR85429.1};
GN ORFNames=BcDW1_5932 {ECO:0000313|EMBL:EMR85429.1};
OS Botryotinia fuckeliana (strain BcDW1) (Noble rot fungus) (Botrytis
OS cinerea).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Sclerotiniaceae; Botrytis.
OX NCBI_TaxID=1290391 {ECO:0000313|EMBL:EMR85429.1, ECO:0000313|Proteomes:UP000012045};
RN [1] {ECO:0000313|Proteomes:UP000012045}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BcDW1 {ECO:0000313|Proteomes:UP000012045};
RX PubMed=23704180; DOI=10.1128/genomea.00252-13;
RA Blanco-Ulate B., Allen G., Powell A.L., Cantu D.;
RT "Draft genome sequence of Botrytis cinerea BcDW1, inoculum for noble rot of
RT grape berries.";
RL Genome Announc. 1:E0025213-E0025213(2013).
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000256|ARBA:ARBA00001971,
CC ECO:0000256|PIRSR:PIRSR602403-1};
CC -!- SIMILARITY: Belongs to the cytochrome P450 family.
CC {ECO:0000256|ARBA:ARBA00010617}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KB707903; EMR85429.1; -; Genomic_DNA.
DR AlphaFoldDB; M7TW14; -.
DR STRING; 1290391.M7TW14; -.
DR HOGENOM; CLU_022195_9_1_1; -.
DR Proteomes; UP000012045; 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:InterPro.
DR GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
DR CDD; cd11041; CYP503A1-like; 1.
DR Gene3D; 1.10.630.10; Cytochrome P450; 1.
DR InterPro; IPR001128; Cyt_P450.
DR InterPro; IPR002403; Cyt_P450_E_grp-IV.
DR InterPro; IPR036396; Cyt_P450_sf.
DR PANTHER; PTHR46206; CYTOCHROME P450; 1.
DR PANTHER; PTHR46206:SF1; P450, PUTATIVE (EUROFUNG)-RELATED; 1.
DR Pfam; PF00067; p450; 1.
DR PRINTS; PR00465; EP450IV.
DR SUPFAM; SSF48264; Cytochrome P450; 1.
PE 3: Inferred from homology;
KW Heme {ECO:0000256|PIRSR:PIRSR602403-1};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRSR:PIRSR602403-1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR602403-1}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Virulence {ECO:0000256|ARBA:ARBA00023026}.
FT TRANSMEM 305..325
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT BINDING 469
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000256|PIRSR:PIRSR602403-1"
SQ SEQUENCE 523 AA; 59698 MW; E57756673B9B9FA1 CRC64;
MGTQLLLLVL LITVIILSRL LFQTFFQNKD EVDVWTKVEP IGVSSGGIFS WTRAVIGSAF
SYQQNTQDGY DKFCKAQNRP FILPTMWTGG SVVVLPPSLL HLTQKVYPSM ARHQAKMDHL
QLPYMISDRD VIDNLIQFDI ARKKLRQAEV VSSLAAITEE EIDVAFRKYW GTSETWTSIN
AWDNCTRVIT QAGFRILIGL PLCRDESLLE NARMYANYLF KGTSIINCLP PFSRPVLARI
ISWPSKYYQA RCRRILRPLI EQRIRGFKDH KAGSEKPDDF LQWLIEHCSK LDAKEMEPDK
ISDRILVLCI AFVFAMGYIF CSSVLDLYKS PEKTSFVAGL VAECKCVSAE HGGLSTKQAV
DSLFRVDSAL RESMRVSDVG ATSIPIDVVS GKVDLGNGIQ IPSGMRMVFA TQPMHLDPDS
YPNPLRYDAF RFSRKYEEIE KCEQELGERE LCTTITESFL PFGYGKFQCP GRWFATQTIK
QALAYVAMNY DIEFDGRQYK RQALLNMMLP PEYVEMSVRR RRA
//
