ID A0A0D0C497_9AGAR Unreviewed; 544 AA.
AC A0A0D0C497;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Unplaced genomic scaffold GYMLUscaffold_17, whole genome shotgun sequence {ECO:0000313|EMBL:KIK62961.1};
GN ORFNames=GYMLUDRAFT_41250 {ECO:0000313|EMBL:KIK62961.1};
OS Collybiopsis luxurians FD-317 M1.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Marasmiineae; Omphalotaceae; Collybiopsis;
OC Collybiopsis luxurians.
OX NCBI_TaxID=944289 {ECO:0000313|EMBL:KIK62961.1, ECO:0000313|Proteomes:UP000053593};
RN [1] {ECO:0000313|EMBL:KIK62961.1, ECO:0000313|Proteomes:UP000053593}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FD-317 M1 {ECO:0000313|EMBL:KIK62961.1,
RC ECO:0000313|Proteomes:UP000053593};
RG DOE Joint Genome Institute;
RG Mycorrhizal Genomics Consortium;
RA Kohler A., Kuo A., Nagy L.G., Floudas D., Copeland A., Barry K.W.,
RA Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A., Lipzen A.,
RA Lundell T., Morin E., Murat C., Riley R., Ohm R., Sun H., Tunlid A.,
RA Henrissat B., Grigoriev I.V., Hibbett D.S., Martin F.;
RT "Evolutionary Origins and Diversification of the Mycorrhizal Mutualists.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000256|ARBA:ARBA00001971};
CC -!- PATHWAY: Secondary metabolite biosynthesis.
CC {ECO:0000256|ARBA:ARBA00005179}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family.
CC {ECO:0000256|RuleBase:RU000461}.
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DR EMBL; KN834765; KIK62961.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0D0C497; -.
DR HOGENOM; CLU_001570_5_11_1; -.
DR OrthoDB; 3640568at2759; -.
DR Proteomes; UP000053593; 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; cd11069; CYP_FUM15-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:SF242; CYTOCHROME P450 MONOOXYGENASE ATNE-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 Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|RuleBase:RU000461};
KW Monooxygenase {ECO:0000256|RuleBase:RU000461};
KW Oxidoreductase {ECO:0000256|RuleBase:RU000461};
KW Reference proteome {ECO:0000313|Proteomes:UP000053593};
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"
SQ SEQUENCE 544 AA; 61936 MW; C091410113FFF954 CRC64;
MSIFVAKAAL ALMLIPVTYV LYCGILYRHN RKSLKYLRGP PKTSFFMGAE YELMLQEEAY
QLESKWFKEY GTAFRASTYF SEDLLMVADP GALQYILHTS GYRFPKPQDV TQSSRFLNGC
GIINAEGEVH NRHRKALNPA FSAKQLRQFL ELFQQSTAKL ASKWQQQLDD ATDGELVVNV
CHWLPKTTLD IIGESAFNYK FGSLDGKETE LGNIFENLFV DSRIHLPKLQ LLYRSFRRDL
PTPIADFLLN FPTKEEKRFL GFLTASKKIG KPILEKGTKE KIPEEEGKDI LSILVRANQE
VDEKKSMNED EVLSQITTFL VAGHETTASA TTWILYSLAK HPKIQARVYQ EIQDLRELIG
ANEPTVQDLD SMPYLNAVIK ETLRCFPIVP HITREAHSDD VIPLEFPVAG VSGDPVSRIP
VSKGQRILID IAVYNKLPQI WGEDAEEWRP ERFLESFKMA ATTVGVYSNL LTFSAGIRAC
IGWRFAVMEL QALVFGLLEK FEFCPPPSGE LDEIQAVSFA LIMPMKRNRW REGKQMPLFV
KARN
//
