ID A0A372Q3U9_9GLOM Unreviewed; 480 AA.
AC A0A372Q3U9;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 24-JAN-2024, entry version 13.
DE SubName: Full=Cytochrome P450 {ECO:0000313|EMBL:RGB22412.1};
GN ORFNames=C1646_647517 {ECO:0000313|EMBL:RGB22412.1};
OS Rhizophagus sp. MUCL 43196.
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Glomeromycotina;
OC Glomeromycetes; Glomerales; Glomeraceae; Rhizophagus.
OX NCBI_TaxID=1803374 {ECO:0000313|EMBL:RGB22412.1, ECO:0000313|Proteomes:UP000263633};
RN [1] {ECO:0000313|EMBL:RGB22412.1, ECO:0000313|Proteomes:UP000263633}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MUCL 43196 {ECO:0000313|EMBL:RGB22412.1,
RC ECO:0000313|Proteomes:UP000263633};
RA Morin E., San Clemente H., Chen E.C.H., De La Providencia I., Hainaut M.,
RA Kuo A., Kohler A., Murat C., Tang N., Roy S., Loubradou J., Henrissat B.,
RA Grigoriev I.V., Corradi N., Roux C., Martin F.M.;
RT "Comparative genomics reveals the genomic features of Rhizophagus
RT irregularis, R. cerebriforme, R. diaphanum and Gigaspora rosea, and their
RT symbiotic lifestyle signature.";
RL Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family.
CC {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:RGB22412.1}.
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DR EMBL; QKKE01001266; RGB22412.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A372Q3U9; -.
DR STRING; 1803374.A0A372Q3U9; -.
DR InParanoid; A0A372Q3U9; -.
DR Proteomes; UP000263633; 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; 2.
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; PTHR46300:SF5; -; 1.
DR PANTHER; PTHR46300; P450, PUTATIVE (EUROFUNG)-RELATED-RELATED; 1.
DR Pfam; PF00067; p450; 2.
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 Coiled coil {ECO:0000256|SAM:Coils}; Heme {ECO:0000256|RuleBase:RU000461};
KW Iron {ECO:0000256|RuleBase:RU000461}; Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU000461};
KW Monooxygenase {ECO:0000256|RuleBase:RU000461};
KW Oxidoreductase {ECO:0000256|RuleBase:RU000461};
KW Reference proteome {ECO:0000313|Proteomes:UP000263633};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 6..22
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT COILED 248..275
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 480 AA; 56150 MW; 90E9FD8145C43D79 CRC64;
MELPTFLFTL FFAAIIYVFF NNQRKKSKIP NGCIPLPGPT PLPIIGNLHQ INNVPIQDFI
DKFSNEYGPI FQVHYGAETW VILNDYEIVK DVLVKRSAIY SSRPYNDATT RVYFDGGKSI
GFSPYGKYWR AMRAVSHQAL TQKMVNINYR DIIHTEVKNL MIKFYNRSSE SYNPTNDLRF
FLINLFTTIL FGQKSEKLSL QIEQMISEIA HILRPENGTI DKFPWLKYIP FVEKRLNRHA
YKARDLAREL FKHLLEDLRQ KLKENENENS FAAHVLKNMN ISSDIALLAN YPEVQRKIQK
ELDECLQGNR FQTPQDDLKL PYLWATIKES LRCRTGSSTL MKHSTTKDDV YRGYYIPAKA
TIMMSYKSAH TSEKLFERPN EFYPEHYLDE NGQLKKYDDL RDPWTFGRGR RACVGQHLAE
RNLITTVGYA LTLFNVENDY DSITGNPIKL DLKRVDKRQP YKVRFVPRPG VTLEKIMQMN
//