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Database: UniProt
Entry: A0A164Y6V9_9AGAM
LinkDB: A0A164Y6V9_9AGAM
Original site: A0A164Y6V9_9AGAM 
ID   A0A164Y6V9_9AGAM        Unreviewed;       548 AA.
AC   A0A164Y6V9;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=Cytochrome P450 {ECO:0000313|EMBL:KZS96639.1};
GN   ORFNames=SISNIDRAFT_406676 {ECO:0000313|EMBL:KZS96639.1};
OS   Sistotremastrum niveocremeum HHB9708.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Trechisporales; Trechisporales incertae sedis; Sistotremastrum.
OX   NCBI_TaxID=1314777 {ECO:0000313|EMBL:KZS96639.1, ECO:0000313|Proteomes:UP000076722};
RN   [1] {ECO:0000313|EMBL:KZS96639.1, ECO:0000313|Proteomes:UP000076722}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HHB9708 {ECO:0000313|EMBL:KZS96639.1,
RC   ECO:0000313|Proteomes:UP000076722};
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}.
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DR   EMBL; KV419398; KZS96639.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A164Y6V9; -.
DR   STRING; 1314777.A0A164Y6V9; -.
DR   OrthoDB; 3640568at2759; -.
DR   Proteomes; UP000076722; 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   PRINTS; PR00385; P450.
DR   SUPFAM; SSF48264; Cytochrome P450; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000076722}.
SQ   SEQUENCE   548 AA;  61910 MW;  B7E8DE4F030DE76D CRC64;
     MSLRVIIFGT LAFIAIQIIR LVDRLFIKPR LSNLRVLPGP KSKSLLYGNF KEVKHSKPGE
     LHAKWIEEYG PTMSYTGVFN SGRLYTHDTR ALSFVLSHPD IFRKPDQFQF VLARVLGKGL
     IFADGDPHRK QRRLLNPAFS NLHIRQMTPI FFSKAFELRD AWIALASEKE SPFDTTACEI
     DAMSWLSRVT LDIIGLAGFD HAFKATNPQG PADDFQKAFE TAFNGAMKFS LMSLLTARFS
     ILRKLPSKRE RDIQEAQTTM RRLGKKLIAD KKKTILESLS DKDEKITKTT VEGKDILSLL
     IRANMSSEVP ESARLSDEDI LAQIPTFILA GHETTAAALA WCLYAMTRHT DIQCKLRDEV
     GSVDTDGPTM DVLNSLPYLD AVVRETLRFF PIVPMVMRIA SEDVNVPFKT PVTDKRGRSL
     SEIRIRKGEG VDIPIIALNR SKDIWGDDAD QYRPERWENV PEIAHEVPGV WSDLMTFLGG
     PRSCIGYKFS IIEMKVLIFT LIRAFSFEPP EKDVEILPKT TFITKPVVVG EEEKGSQLPL
     KIRLLPTA
//
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