ID   A0A395HI36_ASPHC        Unreviewed;       527 AA.
AC   A0A395HI36;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   SubName: Full=Putative cytochrome P450 {ECO:0000313|EMBL:RAL07410.1};
GN   ORFNames=BO97DRAFT_481326 {ECO:0000313|EMBL:RAL07410.1};
OS   Aspergillus homomorphus (strain CBS 101889).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=1450537 {ECO:0000313|EMBL:RAL07410.1, ECO:0000313|Proteomes:UP000248961};
RN   [1] {ECO:0000313|EMBL:RAL07410.1, ECO:0000313|Proteomes:UP000248961}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 101889 {ECO:0000313|EMBL:RAL07410.1,
RC   ECO:0000313|Proteomes:UP000248961};
RG   DOE Joint Genome Institute;
RA   Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA   Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA   Salamov A., Henrissat B., Wiebenga A., De vries R.P., Grigoriev I.V.,
RA   Mortensen U.H., Andersen M.R., Baker S.E.;
RT   "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT   speciation.";
RL   Submitted (FEB-2018) 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; KZ824333; RAL07410.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A395HI36; -.
DR   STRING; 1450537.A0A395HI36; -.
DR   VEuPathDB; FungiDB:BO97DRAFT_481326; -.
DR   OrthoDB; 1351063at2759; -.
DR   Proteomes; UP000248961; 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; cd11041; CYP503A1-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; PTHR46206; CYTOCHROME P450; 1.
DR   PANTHER; PTHR46206:SF8; 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   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR602403-1};
KW   Monooxygenase {ECO:0000256|RuleBase:RU000461};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU000461};
KW   Reference proteome {ECO:0000313|Proteomes:UP000248961}.
FT   BINDING         467
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   527 AA;  58941 MW;  9C1AC4FD4CA7827E CRC64;
     MMLTNINPSI LLGVGMVIFF TCLIAKLFET SPVPEGIPWV LSKKGFFGRA TERFIGVNPI
     VFIKDGYEKY SKNNKPFVMP SVNEGDEVLL PIKESNTILF AKETDLSFKA HIIDFFQLAY
     TSWPLAFAEK YDFYVKLISK DLSETLKTPS IAESLAEEAR ACLSDIWGED TENWVQVPLY
     SFMEKTAGQM INVLAIGPGN SDDKALLAAL THCSNAIVFG ANVIKAFPAF LHPIVGPIVG
     LVNRYFERVF HARLKPIIEK KIQDQKNATD SEVMKETLKS KGSLLDLLIQ AGMRSKWPME
     LTTMWLAYRI FMINFPGVHT SGVSATSVLL DILSYSDVNL VDLLREEVLS ISSDGSWTAQ
     DLAKAALLES AIKESLRLNG INAVSPTRKV VATSGVDLGN GLHLPFGTKV GVPQYALHRD
     SDIYPSPDQY NPFRFYVPDV PVEERRNDLI TATSDTYVVF GHGRRQCPGR WIFAHVFKVL
     VAEMLLKYDI QPMETRPKIH RWGRFQLPPL ATKLSVRRKK DATAVVA
//