ID M7UBT9_BOTF1 Unreviewed; 501 AA.
AC M7UBT9;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Putative cytochrome p450 monooxygenase protein {ECO:0000313|EMBL:EMR84118.1};
GN ORFNames=BcDW1_7266 {ECO:0000313|EMBL:EMR84118.1};
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:EMR84118.1, 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 -!- SIMILARITY: Belongs to the cytochrome P450 family.
CC {ECO:0000256|RuleBase:RU000461}.
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; KB707965; EMR84118.1; -; Genomic_DNA.
DR AlphaFoldDB; M7UBT9; -.
DR STRING; 1290391.M7UBT9; -.
DR HOGENOM; CLU_001570_25_2_1; -.
DR Proteomes; UP000012045; 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; IPR036396; Cyt_P450_sf.
DR PANTHER; PTHR24305; CYTOCHROME P450; 1.
DR PANTHER; PTHR24305:SF166; CYTOCHROME P450 12A4, MITOCHONDRIAL-RELATED; 1.
DR Pfam; PF00067; p450; 1.
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, ECO:0000313|EMBL:EMR84118.1};
KW Oxidoreductase {ECO:0000256|RuleBase:RU000461};
KW Virulence {ECO:0000256|ARBA:ARBA00023026}.
SQ SEQUENCE 501 AA; 56724 MW; D8E747903AF5AD17 CRC64;
MSVRRNHFQK PTEVYAIIDL YGKNILTTER DEWKRHKKVV APAFSEKSYA VVWKETMKQA
HGMLRHWSGA KNSNEDSLEV KDTAPDTAVL GLHVISGAAY GISQGWEGDD EELGDNIVPG
FNTTKLEGSH RLMFKEALST LVDEIIWAAL APMWVYSISP FHKKWYRSFV ECGDYFNELF
DHNLKAIESG QNKDSGATGI IGSLVEATQL DSTDDSKKML TKQEAIANSF IFLFAGHETT
SNAIHFIILF LSISLTAQDQ LQSTLDAILA DKSQEYWNYE TYFPALHNSF VGAVMNESLR
IMSPVIAIPK VSMGLQQINV DGKIVTVPAN TFLHFDVLGV HRNPRYWPCQ KSRISDKSHD
LDDFVPERWL AGYEENSKDK ASPDASSDSL LFVPRRGALI PWSEGAHVCM GKRFSQVEMM
AALAVIFKVW SVELDVRKWA SDEEIEKMNF GDRRVVYEKA MDSARQLIKK SETIITLKML
GESVPLRFVK RGKERFRGCF L
//
