ID A0A161WH45_9PEZI Unreviewed; 492 AA.
AC A0A161WH45;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Cytochrome p450 {ECO:0000313|EMBL:KZL83868.1};
GN ORFNames=CI238_06990 {ECO:0000313|EMBL:KZL83868.1};
OS Colletotrichum incanum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum spaethianum species complex.
OX NCBI_TaxID=1573173 {ECO:0000313|EMBL:KZL83868.1, ECO:0000313|Proteomes:UP000076584};
RN [1] {ECO:0000313|EMBL:KZL83868.1, ECO:0000313|Proteomes:UP000076584}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MAFF 238704 {ECO:0000313|EMBL:KZL83868.1,
RC ECO:0000313|Proteomes:UP000076584};
RA Hacquard S., Kracher B., Hiruma K., Weinman A., Muench P., Garrido Oter R.,
RA Ver Loren van Themaat E., Dallerey J.-F., Damm U., Henrissat B.,
RA Lespinet O., Thon M., Kemen E., McHardy A.C., Schulze-Lefert P.,
RA O'Connell R.J.;
RT "Survival trade-offs in plant roots during colonization by closely related
RT pathogenic and mutualistic fungi.";
RL Submitted (JUN-2015) 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:KZL83868.1}.
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DR EMBL; LFIW01001039; KZL83868.1; -; Genomic_DNA.
DR STRING; 1573173.A0A161WH45; -.
DR OrthoDB; 928042at2759; -.
DR Proteomes; UP000076584; 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; 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:SF240; CYTOCHROME P450 MONOOXYGENASE STCF-RELATED; 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};
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:UP000076584}.
SQ SEQUENCE 492 AA; 55834 MW; E4C29F760CE63070 CRC64;
MSIFEFIVLV AVLGVVAKGV YNAFLHPLRH YPGPKLAGVT RAYYLFFDVR GVSHWKVKEW
HEKYGEVVRI APGELSYTSS QAWQNIYGFP NKDGMGNFEK DAQWWNKNVN GVENILTADH
IGHKRMRRLQ NPAFSDKALK AQESVITGYI KLLIHKLHGQ ASSSADATVD MNSWYNFTTF
DIIGDLAFGE PFYCLRDAKW HWWLHAVFDI FQAGTYLRAA RRFPSPLSEM LLLLIPRRLI
KTRVAQFNFG VERVNRRLEQ DTDRPDFMSY ILQGSDEKAM SVDEMYTAAQ VLIVAGSETT
ATGLTAATYL LCENPHTLEK LTAEIRDTFE NEDDITIQST AGLSYLNAVV EEALRLGPPG
PGTFPRVVPD GGRTVCGKFV PAGYSVGVHH LSVNRSPINF RAHDEFHPER WLGNPEFESD
KKSAAQPFSF GPRNCIGKNL AYAEIRTIIA RVVWNFDMKL HPDSAGWLGR QKMFTTWHKT
EMKVHLSARE KQ
//
