ID A0A167RG51_CALVF Unreviewed; 519 AA.
AC A0A167RG51;
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:KZP00871.1};
GN ORFNames=CALVIDRAFT_524596 {ECO:0000313|EMBL:KZP00871.1};
OS Calocera viscosa (strain TUFC12733).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Dacrymycetes;
OC Dacrymycetales; Dacrymycetaceae; Calocera.
OX NCBI_TaxID=1330018 {ECO:0000313|EMBL:KZP00871.1, ECO:0000313|Proteomes:UP000076738};
RN [1] {ECO:0000313|EMBL:KZP00871.1, ECO:0000313|Proteomes:UP000076738}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TUFC12733 {ECO:0000313|EMBL:KZP00871.1,
RC ECO:0000313|Proteomes:UP000076738};
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; KV417268; KZP00871.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A167RG51; -.
DR STRING; 1330018.A0A167RG51; -.
DR OrthoDB; 2900138at2759; -.
DR Proteomes; UP000076738; 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:UP000076738}.
SQ SEQUENCE 519 AA; 57482 MW; BB98C3F97B49B164 CRC64;
MPLLFLDYLF AALLLALIIS LWRRRAPALP LPPGPRGIPL LGNALQIPKE RPWLVYADWA
KTYGELTHLN AFGQHLIILN TRQAARDLLE KRNAVYSGRV HMTFAGELVG WEKSVAMLEG
PRHVQTRRMG QVMMSLAAVQ AQYGEGMTAE AHRLLRNLLE TPERWMDHYR SSAGAFIMLT
TYGTVPGKER DALIEQAKHV VEHFSVAATP GNWIVDFVPF LKYLPAWVPG CGFNATGKAW
RAELEHLVNS PFDGVKDMMP DRWQAKHIAP PSIVSDLLEK NPEPASEVLI RWLAGSLFAA
GADTTVGALA SFTLAMTKFP AAQRAAQAKL DSLVGRDRLP TFTDIDPERA PYLHALVKEV
LRWGIIVPMG FPHRLSSPGE DEYLGWRIPP NTLLMPNAWA MSRDRDVYGE DVEVFRPERF
LAMSKEQQTA LGYGSPTFGF GGRVCLGQHV AYATLLVQIA SILATFDIAR PVGADGREVV
PGEVGFSSGV VSHPDHFETV IRPRSKEAAE LVQAANAFE
//
