ID L8X765_THACA Unreviewed; 641 AA.
AC L8X765;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=Cytochrome P450 {ECO:0000313|EMBL:ELU44942.1};
GN ORFNames=AG1IA_01023 {ECO:0000313|EMBL:ELU44942.1};
OS Thanatephorus cucumeris (strain AG1-IA) (Rice sheath blight fungus)
OS (Rhizoctonia solani).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Cantharellales; Ceratobasidiaceae; Rhizoctonia; Rhizoctonia solani AG-1.
OX NCBI_TaxID=983506 {ECO:0000313|EMBL:ELU44942.1, ECO:0000313|Proteomes:UP000011668};
RN [1] {ECO:0000313|EMBL:ELU44942.1, ECO:0000313|Proteomes:UP000011668}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AG-1 IA {ECO:0000313|Proteomes:UP000011668};
RX PubMed=23361014; DOI=10.1038/ncomms2427;
RA Zheng A., Lin R., Xu L., Qin P., Tang C., Ai P., Zhang D., Liu Y., Sun Z.,
RA Feng H., Wang Y., Chen Y., Liang X., Fu R., Li Q., Zhang J., Yu X., Xie Z.,
RA Ding L., Guan P., Tang J., Liang Y., Wang S., Deng Q., Li S., Zhu J.,
RA Wang L., Liu H., Li P.;
RT "The evolution and pathogenic mechanisms of the rice sheath blight
RT pathogen.";
RL Nat. Commun. 4:1424-1424(2013).
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000256|ARBA:ARBA00001971};
CC -!- PATHWAY: Secondary metabolite biosynthesis.
CC {ECO:0000256|ARBA:ARBA00005179}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family.
CC {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:ELU44942.1}.
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DR EMBL; AFRT01000239; ELU44942.1; -; Genomic_DNA.
DR AlphaFoldDB; L8X765; -.
DR STRING; 983506.L8X765; -.
DR HOGENOM; CLU_001570_5_11_1; -.
DR OMA; HASEDIT; -.
DR Proteomes; UP000011668; 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; IPR002401; Cyt_P450_E_grp-I.
DR InterPro; IPR036396; Cyt_P450_sf.
DR PANTHER; PTHR24305; CYTOCHROME P450; 1.
DR PANTHER; PTHR24305:SF242; CYTOCHROME P450 MONOOXYGENASE ATNE-RELATED; 1.
DR Pfam; PF00067; p450; 2.
DR PRINTS; PR00463; EP450I.
DR PRINTS; PR00385; P450.
DR SUPFAM; SSF48264; Cytochrome P450; 2.
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:UP000011668}.
SQ SEQUENCE 641 AA; 71577 MW; 34194C4646852D5A CRC64;
MVHQMVILIV STDHPPRPRI YGPLDLLVSN TNNPPPPTRC AGRITIPLLF LNHGRCYLLR
PHYSYTLRAC RMPSCLYGGR SSLHSISVRE HDCEQIINYY KSYVKHLPGP KRRGAFISDL
NIICETETSK EFNERLVQKY GRNIRAQGFG YMDQRLVTYD PVTINYILGS AADRFPKPWQ
MRRFVSKLTG GDIKQKAVNV AEGPYHHRLR KIIAPAFAPS TIRGHAPTFI RKANELCDHW
RSVLSEPAAP AVPGVETDAK GNTILDVHNW FGRAAFDVIG LAAFGYSFDS LRDDTNELFG
AYMRLHHVTR EGPSMRGNLC LAYPWLERYL RDETSDAIAQ SAQVVQKTSQ MLLKEMRDAN
PEGDGKSILG LLLRSNANAA PEDRLTDEEL LAQIDSFLFA GSDSTSIATI WALYELACNP
EIQQALRAEL RPLGLNEHAG EQDFASDSGI DIDIATPDHA AQFAAIDTLP LLDRVVRESL
RLHPPVHSTL RIAEEDDIVP FSIDSPPKMQ DGSISRAVVT GLGADGVERT GIRVRKVKMD
TSSSKWNPDR WIDLPAAAKN NPGVVPGLMS FSVGPHSCPA FRFAMAEMKT MLAYVVSSFA
VEDTPKKILP HNMMMTRPYV ENQWSKGQLP GFRLPLQVRA L
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