ID A0A0D1VLL9_9EURO Unreviewed; 508 AA.
AC A0A0D1VLL9;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=Cytochrome P450 {ECO:0008006|Google:ProtNLM};
GN ORFNames=PV11_08730 {ECO:0000313|EMBL:KIV76880.1};
OS Exophiala sideris.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX NCBI_TaxID=1016849 {ECO:0000313|EMBL:KIV76880.1, ECO:0000313|Proteomes:UP000053599};
RN [1] {ECO:0000313|EMBL:KIV76880.1, ECO:0000313|Proteomes:UP000053599}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 121828 {ECO:0000313|EMBL:KIV76880.1,
RC ECO:0000313|Proteomes:UP000053599};
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 sideris CBS121828.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000256|ARBA:ARBA00001971};
CC -!- SIMILARITY: Belongs to the cytochrome P450 family.
CC {ECO:0000256|ARBA:ARBA00010617, ECO:0000256|RuleBase:RU000461}.
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DR EMBL; KN846954; KIV76880.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0D1VLL9; -.
DR STRING; 1016849.A0A0D1VLL9; -.
DR HOGENOM; CLU_001570_14_4_1; -.
DR OrthoDB; 3184603at2759; -.
DR Proteomes; UP000053599; 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; cd11062; CYP58-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; PTHR24305; CYTOCHROME P450; 1.
DR PANTHER; PTHR24305:SF152; P450, PUTATIVE (EUROFUNG)-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:UP000053599};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 6..27
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 508 AA; 57715 MW; 400AD874D4CA9BBF CRC64;
MAMHVFIKVG LQLFSTWIIY LLLQVIYRLK YHPLAKFPGP RLAAVTMMYA GWYDLPFASS
FCKQLPRLHD DYGPIVRIRP NELHIRDMDS FRQVYRLGTP FKKYPGFYNA YVIDGSFFNI
HETKAVKPIK DMYSPHFSRA AIQKLEGVIH AKITKLLNAL HMASQESKVV DLTLAFKCLT
ADVVMEYCYQ RNFGALDATD FHFKIIEDME GLFGTASYTW YFPNTFNLLC RILEHAPVSV
TKVVAKPLAA SFEIYKGCQE RIATLQRTTL DPSVPSIFQT ALLPEPKKGR STPALKELTA
DALVFFGAGT DTTAHALATG TWYLLQNPAI LTRLRQELCN AIVDADSSTM LSWVELEKLP
FLRAVIKESL RLSFGVPGRL PRVVPENGAV FCGQEIPPNT VISHSAYAYH MSDQYFPEAK
AFKPDRWLGP GSVERERYML SFSAGSRGCL GINLAYAELF TTFAYLFRKF DLEVFNTTEH
DINWHDCYTP ATFGHLKVRL NRVVGEKQ
//
