ID A0A0D2BRH8_9EURO Unreviewed; 513 AA.
AC A0A0D2BRH8;
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=PV06_08602 {ECO:0000313|EMBL:KIW40047.1};
OS Exophiala oligosperma.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX NCBI_TaxID=215243 {ECO:0000313|EMBL:KIW40047.1, ECO:0000313|Proteomes:UP000053342};
RN [1] {ECO:0000313|EMBL:KIW40047.1, ECO:0000313|Proteomes:UP000053342}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 72588 {ECO:0000313|EMBL:KIW40047.1,
RC ECO:0000313|Proteomes:UP000053342};
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 oligosperma CBS72588.";
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|RuleBase:RU000461}.
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DR EMBL; KN847339; KIW40047.1; -; Genomic_DNA.
DR RefSeq; XP_016260263.1; XM_016409955.1.
DR AlphaFoldDB; A0A0D2BRH8; -.
DR STRING; 215243.A0A0D2BRH8; -.
DR GeneID; 27360676; -.
DR VEuPathDB; FungiDB:PV06_08602; -.
DR HOGENOM; CLU_001570_14_0_1; -.
DR OrthoDB; 408598at2759; -.
DR Proteomes; UP000053342; 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; cd11060; CYP57A1-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:SF236; 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 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:UP000053342}.
SQ SEQUENCE 513 AA; 58636 MW; 6C8C4E234CD82215 CRC64;
MFFGLFSKDS GIVGDRSNPM DLLSSTSLRY LIALFVGSLI VRSIKRRYLT ALRTVPGPFA
ASVTRAWRIK EVYYGHIEQT ELKLHELHGP LVRTGPNEVI TNDLNAVDLL YSIGSKFPKT
DFYRLFGFPD VYGVHQFSAL PNMLHKKLVR YTAGAFSMTS IVELEPFVDS SVEFFIHRIK
DIGSNSTPMN MAEWFQWYAF DVIGELTFSS RYGFMEQARD VADSTKIIDK FQAYVSFVGQ
AFSYHWMLLG NPILSLFMKP PSGIIGDMAI REIQARQGRS TDRRDMLSRF LKEHEKHPND
FTMSDVYRAG AMTIGGGSDT TGIALTATFY HLLRYPEAYK RLRAEIDQAI LDNKLSKPAK
LRETQSLTYL QAVIKEGMRI HPSVAFILPR HVPEGGCTIA GKYLPAGTRV GMNPYVVHRN
KEIFGEDADI FRPERWFERE EKTMNRYMLQ FGQGSRICAG RHISIMEMNK ALVELIRNFD
IELADPNFEL NTMTRWFLKP DALPCIFKPR SLL
//
