ID A0A165J4H6_EXIGL Unreviewed; 514 AA.
AC A0A165J4H6;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Cytochrome P450 {ECO:0000313|EMBL:KZV94320.1};
GN ORFNames=EXIGLDRAFT_767274 {ECO:0000313|EMBL:KZV94320.1};
OS Exidia glandulosa HHB12029.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Auriculariales; Exidiaceae; Exidia.
OX NCBI_TaxID=1314781 {ECO:0000313|EMBL:KZV94320.1, ECO:0000313|Proteomes:UP000077266};
RN [1] {ECO:0000313|EMBL:KZV94320.1, ECO:0000313|Proteomes:UP000077266}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HHB12029 {ECO:0000313|EMBL:KZV94320.1,
RC ECO:0000313|Proteomes:UP000077266};
RX PubMed=26659563; DOI=10.1093/molbev/msv337;
RA Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT Insights into the Origins of Lignocellulose Decay Capabilities.";
RL Mol. Biol. Evol. 33:959-970(2016).
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|ARBA:ARBA00010617, ECO:0000256|RuleBase:RU000461}.
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DR EMBL; KV425975; KZV94320.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A165J4H6; -.
DR STRING; 1314781.A0A165J4H6; -.
DR InParanoid; A0A165J4H6; -.
DR OrthoDB; 2900138at2759; -.
DR Proteomes; UP000077266; 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; cd11065; CYP64-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; PTHR46300:SF7; P450, PUTATIVE (EUROFUNG)-RELATED; 1.
DR PANTHER; PTHR46300; P450, PUTATIVE (EUROFUNG)-RELATED-RELATED; 1.
DR Pfam; PF00067; p450; 1.
DR PRINTS; PR00463; EP450I.
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|ARBA:ARBA00023033,
KW ECO:0000256|RuleBase:RU000461};
KW Oxidoreductase {ECO:0000256|RuleBase:RU000461};
KW Reference proteome {ECO:0000313|Proteomes:UP000077266}.
SQ SEQUENCE 514 AA; 57458 MW; A9A6D5EB3C6B5C5C CRC64;
MLQSNISPAL GLTVCAGVWL AARLLRPSRA SVPPGPPGRP LLGNLLDFPK EKEWLKYAEW
AKQYGDIISV NVLGQTVVVL HSAKDVKELF VNRASSYSAR IRMTMVQLAG WEVGTATVSP
GEQFRAMRRF MSQILSGQAV KGYIDVEEQE ITTFLRLAIR NGSGADMKAQ IQRMAAAIDL
RLTYGYNIKT DADEFKDLAE HALRIFNAAA QPGWVVDAFP FLRFIPTWFP FASFKRKAVE
WRKVVEASRQ RTLDWTRSQV ETGTAVPCFA TQLLADPERM EQERMFQVVL ADLFMAGVDT
VTVAAAKLFL ALATHPEAQA RAQGEIDALT KGERLPTYED KQHLPYLDAL LKEVHRWDTP
IAPLALPHCA SEEDMYKGYR IPKDAIVFAN VWAIFRNPEK YPDPDTFKPE RFLEKGERQT
ASRDIINEDP YKFAFGFGAR ICPGRHLADS AQFLLAAKLL ATCTVSNAVD MQGQRLSSRT
IEFSPGVVSQ PPRFTCTVEP RSPQAEGLLF EGAN
//
