ID A0A0D2AQX1_9PEZI Unreviewed; 509 AA.
AC A0A0D2AQX1;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE RecName: Full=Cytochrome P450 {ECO:0008006|Google:ProtNLM};
GN ORFNames=PV09_00026 {ECO:0000313|EMBL:KIW09078.1};
OS Verruconis gallopava.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Venturiales; Sympoventuriaceae; Verruconis.
OX NCBI_TaxID=253628 {ECO:0000313|EMBL:KIW09078.1, ECO:0000313|Proteomes:UP000053259};
RN [1] {ECO:0000313|EMBL:KIW09078.1, ECO:0000313|Proteomes:UP000053259}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 43764 {ECO:0000313|EMBL:KIW09078.1,
RC ECO:0000313|Proteomes:UP000053259};
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 Ochroconis gallopava CBS43764.";
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 ECO:0000256|PIRSR:PIRSR602403-1};
CC -!- SIMILARITY: Belongs to the cytochrome P450 family.
CC {ECO:0000256|ARBA:ARBA00010617, ECO:0000256|RuleBase:RU000461}.
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DR EMBL; KN847529; KIW09078.1; -; Genomic_DNA.
DR RefSeq; XP_016218947.1; XM_016352690.1.
DR AlphaFoldDB; A0A0D2AQX1; -.
DR STRING; 253628.A0A0D2AQX1; -.
DR GeneID; 27307999; -.
DR VEuPathDB; FungiDB:PV09_00026; -.
DR HOGENOM; CLU_018012_4_2_1; -.
DR InParanoid; A0A0D2AQX1; -.
DR OrthoDB; 1761436at2759; -.
DR Proteomes; UP000053259; 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; cd11040; CYP7_CYP8-like; 1.
DR Gene3D; 1.10.630.10; Cytochrome P450; 1.
DR InterPro; IPR001128; Cyt_P450.
DR InterPro; IPR017972; Cyt_P450_CS.
DR InterPro; IPR002403; Cyt_P450_E_grp-IV.
DR InterPro; IPR036396; Cyt_P450_sf.
DR PANTHER; PTHR47582; P450, PUTATIVE (EUROFUNG)-RELATED; 1.
DR PANTHER; PTHR47582:SF1; P450, PUTATIVE (EUROFUNG)-RELATED; 1.
DR Pfam; PF00067; p450; 1.
DR PRINTS; PR00465; EP450IV.
DR SUPFAM; SSF48264; Cytochrome P450; 1.
DR PROSITE; PS00086; CYTOCHROME_P450; 1.
PE 3: Inferred from homology;
KW Heme {ECO:0000256|PIRSR:PIRSR602403-1, ECO:0000256|RuleBase:RU000461};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRSR:PIRSR602403-1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR602403-1};
KW Monooxygenase {ECO:0000256|RuleBase:RU000461};
KW Oxidoreductase {ECO:0000256|RuleBase:RU000461};
KW Reference proteome {ECO:0000313|Proteomes:UP000053259};
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"
FT TRANSMEM 294..317
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT BINDING 447
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000256|PIRSR:PIRSR602403-1"
SQ SEQUENCE 509 AA; 57217 MW; 6223F2BE39F04CFB CRC64;
MEVLGLQLDL IVLLSITFIS FISLQSLSCR KVDPREPSVV KLGVPYFGAL IGMVTQGGKW
LRDLAIRTQD PIFTIAMPWS RMYVVTDPAL AASVQRNKNL SFSPLIPEAT QRILGLDQET
VKIVRKNLNR EDNVRGFIPE IHDMVYAYMA PGDSLDELSA SASKELADLI YDYAGGLQNA
ANSSNKEHLL KFCQHFVTVA TARFLYGPEN PIDTDIGNEQ AFWDFDHGIG LLLVNVAPSI
TARKAFRGRE KLVKALETYL REDHTKTASK LIQNRVEISV RHGWKVDMLA RAELSFLFAG
IVNTAITSFW LILHIFARPR LLDEVREELQ AAFGTLSINK KRQALDATKI RNECPIFMSV
FRETLRVGSE NSSTRIVMAD TVLADKYFLK KDSVLQISGG AMHVDRRIWG SDADAFDPYR
FTEERVKKQD KIHPAAYRAF GGGATLCPGR HFATNEITSF VALVIMLFDL EPVHGADFSI
PRKRDNVLPV HILEPVADVQ CFFKLRTRS
//
