ID   A0A1X6MZR2_9APHY        Unreviewed;       597 AA.
AC   A0A1X6MZR2;
DT   05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2017, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   RecName: Full=Cytochrome P450 {ECO:0008006|Google:ProtNLM};
GN   ORFNames=POSPLADRAFT_1034368 {ECO:0000313|EMBL:OSX61869.1};
OS   Postia placenta MAD-698-R-SB12.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Polyporales; Postiaceae; Postia.
OX   NCBI_TaxID=670580 {ECO:0000313|EMBL:OSX61869.1, ECO:0000313|Proteomes:UP000194127};
RN   [1] {ECO:0000313|EMBL:OSX61869.1, ECO:0000313|Proteomes:UP000194127}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MAD-698-R-SB12 {ECO:0000313|EMBL:OSX61869.1,
RC   ECO:0000313|Proteomes:UP000194127};
RG   DOE Joint Genome Institute;
RA   Gaskell J., Kersten P., Larrondo L.F., Canessa P., Martinez D., Hibbett D.,
RA   Schmoll M., Kubicek C.P., Martinez A.T., Yadav J., Master E.,
RA   Magnuson J.K., James T., Yaver D., Berka R., Labutti K., Lipzen A.,
RA   Aerts A., Barry K., Henrissat B., Blanchette R., Grigoriev I., Cullen D.;
RT   "Genome Sequence of the Model Brown-Rot Fungus Postia placenta SB12.";
RL   Submitted (APR-2017) to the EMBL/GenBank/DDBJ databases.
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   ---------------------------------------------------------------------------
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; KZ110598; OSX61869.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1X6MZR2; -.
DR   STRING; 670580.A0A1X6MZR2; -.
DR   OrthoDB; 3640568at2759; -.
DR   Proteomes; UP000194127; 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:InterPro.
DR   GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
DR   CDD; cd11069; CYP_FUM15-like; 1.
DR   Gene3D; 1.10.630.10; Cytochrome P450; 1.
DR   InterPro; IPR001128; Cyt_P450.
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; 1.
DR   PRINTS; PR00463; EP450I.
DR   SUPFAM; SSF48264; Cytochrome P450; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000194127};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..30
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           31..597
FT                   /note="Cytochrome P450"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5010884923"
SQ   SEQUENCE   597 AA;  66879 MW;  57827303BF1B79E3 CRC64;
     MSVAHAGASV LLALVLWALV KRLTATKARA IDIAGPEKDH WLKGTRVDRN YHRIFQDGLE
     YNLQLTEKYG GAVRIHALLG VRTLIVAAEE QLYVSDPRAL HHIVVKEQDV YEETDMFIMG
     NKLIFGEGLI STLGEQHRKQ RKMLNPVFSL ANMRDLLPTI QPIADQLCDL LVSKITAGEQ
     EIDIVPWTSR GALEYICQAA LGYTFDALNP EKTSEYAEAL RRFSPTALRL ILIRPFVPFF
     DHGLVPIKPL KEFRRIVEVM HRTCKGIYAD KKSAIEGTLV DGSLKLNEPQ GATGFRSRGR
     DIMSILLRAN RPSNVRDMLT ESELLGQMNT IIFAGFETTA IATSRLLYLL ASRPDAQARL
     CREVRAAKMA HVGDSARWQD VNLSYDVLMG LPYLDALVRE TLRVYPPTSI LSRTTRKSTV
     LPLEFPVRSA SGQEVTSVPL PENTTVIISI LAANHNKEIW GEDASDWRPE RWLTSTGERI
     RLGDGDNLPD GYVIVERSEE EDKVPGNRDG IKYPGVYASM MTFLGGGRAC IGFKFAEMEM
     NQVLTTLLST LHFSLPAEKE IYWKMNGLQV PVVRPPAGDG QTPQVPLKIR LVRDDDY
//