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Database: UniProt
Entry: A0A372Q3U9_9GLOM
LinkDB: A0A372Q3U9_9GLOM
Original site: A0A372Q3U9_9GLOM 
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
//
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