ID A0A0M8MXE1_9HYPO Unreviewed; 537 AA.
AC A0A0M8MXE1;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=p450 monooxygenase {ECO:0000313|EMBL:KOS20668.1};
GN ORFNames=ESCO_006834 {ECO:0000313|EMBL:KOS20668.1};
OS Escovopsis weberi.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Hypocreaceae; Escovopsis.
OX NCBI_TaxID=150374 {ECO:0000313|EMBL:KOS20668.1, ECO:0000313|Proteomes:UP000053831};
RN [1] {ECO:0000313|EMBL:KOS20668.1, ECO:0000313|Proteomes:UP000053831}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA de Man T.J., Stajich J.E., Kubicek C.P., Chenthamara K., Atanasova L.,
RA Druzhinina I.S., Birnbaum S., Barribeau S.M., Teiling C., Suen G.,
RA Currie C., Gerardo N.M.;
RT "The genome of the fungus Escovopsis weberi, a specialized disease agent of
RT ant agriculture.";
RL Submitted (JUL-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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KOS20668.1}.
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DR EMBL; LGSR01000015; KOS20668.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0M8MXE1; -.
DR STRING; 150374.A0A0M8MXE1; -.
DR OrthoDB; 2727850at2759; -.
DR Proteomes; UP000053831; 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 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:SF164; 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|ARBA:ARBA00022617, ECO:0000256|RuleBase:RU000461};
KW Iron {ECO:0000256|RuleBase:RU000461}; Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|RuleBase:RU000461};
KW Monooxygenase {ECO:0000256|RuleBase:RU000461, ECO:0000313|EMBL:KOS20668.1};
KW Oxidoreductase {ECO:0000256|RuleBase:RU000461};
KW Reference proteome {ECO:0000313|Proteomes:UP000053831};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 6..24
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 537 AA; 60650 MW; 3B51D13B13A54039 CRC64;
MGFFSDSIGV IAGYAVFLGS VAFVHRMYKV RMMVRRVHAQ HGVPILPHSF LLGHLFTMAK
IIIKHKLPPD VFPHHHYFAI QKDYPEIFEA GVLYLDPWPI SWPIMIVFKP EMIAQFVSSP
SLPKFYYMRT IEFGPLTGGR DVFTAEGQMW KEQHALFMPG FSSKNALAMT PWFVNEVLVF
RDRMLKASKT GETVKLEQWA ADLTLDVIAR ATLSQEQASP HWLVALKEQV KLMVFKLDVV
KALNLLSPLQ HWRYNRIFKK AIEPMIIEAF NKPTEPDGPQ SIMGLAIGRL VRSGQAIPQQ
LLDDLVVNIK MFLYAGHVTT AMALSMLYWQ LSQNPDKLAL VREEHDRVLG PDPARAAEAI
LADVNILNKL TYTGAAIKEA MRLWPPTGGS LREANAPGYM ITNPETGMSF PTHGFMISSG
SVYLARDPKY WHRSDEYLPE RFLVRDPNDP LHPTKNAWQP FSTGPRACIA QDLVQAEVRL
AAALTLREFD IEPQYAADAP EFHGSKAYQT EDPYDVSGMR VKDGLPVKVI ARKRPVG
//
