ID A0A0D2F2H3_9EURO Unreviewed; 534 AA.
AC A0A0D2F2H3;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=Cytochrome P450 {ECO:0008006|Google:ProtNLM};
GN ORFNames=PV05_02182 {ECO:0000313|EMBL:KIW62138.1};
OS Exophiala xenobiotica.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX NCBI_TaxID=348802 {ECO:0000313|EMBL:KIW62138.1, ECO:0000313|Proteomes:UP000054342};
RN [1] {ECO:0000313|EMBL:KIW62138.1, ECO:0000313|Proteomes:UP000054342}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 118157 {ECO:0000313|EMBL:KIW62138.1,
RC ECO:0000313|Proteomes:UP000054342};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Exophiala xenobiotica CBS118157.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family.
CC {ECO:0000256|RuleBase:RU000461}.
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DR EMBL; KN847317; KIW62138.1; -; Genomic_DNA.
DR RefSeq; XP_013322722.1; XM_013467268.1.
DR AlphaFoldDB; A0A0D2F2H3; -.
DR STRING; 348802.A0A0D2F2H3; -.
DR GeneID; 25324090; -.
DR HOGENOM; CLU_001570_2_1_1; -.
DR OrthoDB; 2900138at2759; -.
DR Proteomes; UP000054342; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; P450, PUTATIVE (EUROFUNG)-RELATED-RELATED; 1.
DR PANTHER; PTHR46300:SF11; P450, PUTATIVE-RELATED; 1.
DR Pfam; PF00067; p450; 1.
DR PRINTS; PR00463; EP450I.
DR PRINTS; PR00385; P450.
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 Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|RuleBase:RU000461};
KW Monooxygenase {ECO:0000256|RuleBase:RU000461};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU000461};
KW Reference proteome {ECO:0000313|Proteomes:UP000054342};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..33
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 534 AA; 60858 MW; 9E3383DA65E9A864 CRC64;
MPISISAVAS HSYIFLGATA FVAFAALVAW NIISIRGPPT PKGLRRPPSP PGARFFSGHA
HLWSGRVTNN PSQSQLVKWA REYGEIYEFR LGVERWVIVS SPEAVKEIFD KNGALTGSRP
AFRVMNILSG GYRMLFMPYG KKWRSLRAIA HRCLSIKSAE AIKPSSSLES HRYLLDILRD
PDNFLDHVKR YTSSVIMYSI YGRRVLDLDE AVLKAIYEET SHFSEAMAQV HTVDQYPILE
RLPKSLQWWR PKWEAYHQKE VELWMGLWND LKKRLNAGVR TGCFAEKFQE EDYLAMGISE
TQAAYAAGSM IEAGSDTTQL TMNSMILAMV AFPEVVSKAQ KELDAVVGDR MPEFTDMPNL
PYIRAMVKEV LRWRSVSNDH ERHVSSGDVV YKDYFIPAGS SVVINQWAMH FDPDLFPEPE
RFNPDRYLGT PVNDLTAGEC IHTNDVNLRD HWSFGAGRRV CAGYNLAENS LLILTARLLW
AFDVRPTIDQ QTGQGTKYDV WNYYPTRLFG PKPFPVDFRV RSEEKRQAIL KAEI
//
