ID W7I613_9PEZI Unreviewed; 555 AA.
AC W7I613;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE RecName: Full=Cytochrome P450 {ECO:0008006|Google:ProtNLM};
GN ORFNames=DRE_07000 {ECO:0000313|EMBL:EWC44175.1};
OS Drechslerella stenobrocha 248.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Orbiliomycetes;
OC Orbiliales; Orbiliaceae; Drechslerella.
OX NCBI_TaxID=1043628 {ECO:0000313|EMBL:EWC44175.1, ECO:0000313|Proteomes:UP000024837};
RN [1] {ECO:0000313|EMBL:EWC44175.1, ECO:0000313|Proteomes:UP000024837}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=248 {ECO:0000313|EMBL:EWC44175.1,
RC ECO:0000313|Proteomes:UP000024837};
RA Liu X., Zhang W., Liu K.;
RT "Drechslerella stenobrocha genome reveals carnivorous origination and
RT mechanical trapping mechanism of predatory fungi.";
RL Submitted (MAY-2013) 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}.
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DR EMBL; KI966445; EWC44175.1; -; Genomic_DNA.
DR AlphaFoldDB; W7I613; -.
DR HOGENOM; CLU_022195_0_2_1; -.
DR Proteomes; UP000024837; 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; cd11041; CYP503A1-like; 1.
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; PTHR46206; CYTOCHROME P450; 1.
DR PANTHER; PTHR46206:SF1; P450, PUTATIVE (EUROFUNG)-RELATED; 1.
DR Pfam; PF00067; p450; 1.
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};
KW Oxidoreductase {ECO:0000256|RuleBase:RU000461};
KW Reference proteome {ECO:0000313|Proteomes:UP000024837}.
SQ SEQUENCE 555 AA; 62696 MW; 7E2B30EE76D10856 CRC64;
MIVHTIFESL AGHATEAILC CLALYTVYSV ITSYTRPRPL DIYTKEPPAV VGLPKTYTWF
FPKLRSRLAS TKHAFGWVQE GYAKYHKIGK PFMVHSIDGD MIILPQDMMP ETKNLPVNVA
NIRSLQSLAV RYTFDKYIES DLFHVGMIRK DLTARLAAFT PAIVEELDLA FKHYTPKIAG
QPGEKGWQKV VMYDLILKIV ARTSHRVFIG EELCREEEYL DLSIKYAITI LPTAMLLNCF
PKFLWPIIGP LFCIPLQLIR RKASKFLEPV ILKRIAGIRA NLPESERPND LMQWVIDASL
ARGGGFATTD AIVNRVLTVA FAAIHTTSLS ATNAIYDLAY LPSQVPSDAY PRPPADILRD
EVMAVFPPPH TFNRRYMQRL YNMDAFLKET ARMSLIGALH SERLVTAPAG FTTSSGLHMP
HGTAFAFIGS PRVLDPEIFE RAGEHRYTRF YRGDVAGAGD EEVEEAVVSG KGATDRKLDR
YMVTVTDDFP VFGMGTHACP GRFFAASELR ILISWFLLNY DVKTVAERPP SWQFIYLDIM
NTTAELEIRR RDLVN
//
