ID A0A0F8WRE8_9EURO Unreviewed; 522 AA.
AC A0A0F8WRE8;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=Cytochrome P450 {ECO:0008006|Google:ProtNLM};
GN ORFNames=ARAM_001605 {ECO:0000313|EMBL:KKK13822.1};
OS Aspergillus rambellii.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=308745 {ECO:0000313|EMBL:KKK13822.1, ECO:0000313|Proteomes:UP000034291};
RN [1] {ECO:0000313|EMBL:KKK13822.1, ECO:0000313|Proteomes:UP000034291}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SRRC1468 {ECO:0000313|EMBL:KKK13822.1,
RC ECO:0000313|Proteomes:UP000034291};
RA Moore G.G., Beltz S.B., Mack B.M.;
RT "Draft Genome Sequences of Two Closely-Related Aflatoxigenic Aspergillus
RT Species Obtained from the Cote d'Ivoire.";
RL Submitted (FEB-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}.
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:KKK13822.1}.
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DR EMBL; JZBS01003737; KKK13822.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0F8WRE8; -.
DR STRING; 308745.A0A0F8WRE8; -.
DR OrthoDB; 1351063at2759; -.
DR Proteomes; UP000034291; 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:InterPro.
DR GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
DR CDD; cd11041; CYP503A1-like; 1.
DR Gene3D; 1.10.630.10; Cytochrome P450; 1.
DR InterPro; IPR001128; Cyt_P450.
DR InterPro; IPR002403; Cyt_P450_E_grp-IV.
DR InterPro; IPR036396; Cyt_P450_sf.
DR PANTHER; PTHR46206; CYTOCHROME P450; 1.
DR PANTHER; PTHR46206:SF3; P450, PUTATIVE (EUROFUNG)-RELATED; 1.
DR Pfam; PF00067; p450; 1.
DR PRINTS; PR00465; EP450IV.
DR SUPFAM; SSF48264; Cytochrome P450; 1.
PE 3: Inferred from homology;
KW Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|PIRSR:PIRSR602403-1};
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 Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000034291};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 14..31
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT BINDING 456
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 522 AA; 58438 MW; 87F4F2A893848B6C CRC64;
MLLDYFRILR PTDLAPLVGI LLSTLVLYLA FPITRRAKLP LINGKRPGEI WATDAINRFL
SDSESLLKEG FEKSENGFYL GTDNGTMLIL PMRYATSIRD TNGLSFSLFA RDLFHWHIGG
LEAFQPNHVV HETVNKKLTR KLESLVDPLS AVTAATLREH WADCSDWSKI TLSDSILAIF
TKVSSRVFLG EDLYQTPEWI QLLQDYMVDS YVAVGSLRRW PVPFRPLVAN FLPSVHKARK
LIQGARDIIN PVVEERRAAP ETTTETCGLD WIDETASALG VPYDPAVAQL GLSLGSVNTG
ADMVTQLLFD ICGQEKLVRD LRQEIIAVLR HEEEEVAAAM SEDSGSRKTS RKALLYKLKL
LDSVMKESQR LKPLASVMVT RTAQREVTLP EGIVLPRGSY VGISNYEMRR AGSPMGAEFD
GYRYYNLRES TGDETWTQFV STGPKVMGFG YGQYACPGRF FASDQIKIFM CHLLLKFDFK
LPPGEGRPPV YTSGFSLIAN PTAQILIRKR EAEVDLDAIL GL
//
