ID T0LXI2_COLGC Unreviewed; 483 AA.
AC T0LXI2;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Cytochrome P450 {ECO:0000313|EMBL:EQB53115.1};
GN ORFNames=CGLO_07199 {ECO:0000313|EMBL:EQB53115.1};
OS Colletotrichum gloeosporioides (strain Cg-14) (Anthracnose fungus)
OS (Glomerella cingulata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum gloeosporioides species complex.
OX NCBI_TaxID=1237896 {ECO:0000313|EMBL:EQB53115.1, ECO:0000313|Proteomes:UP000015530};
RN [1] {ECO:0000313|Proteomes:UP000015530}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Cg-14 {ECO:0000313|Proteomes:UP000015530};
RX PubMed=23902260; DOI=10.1094/MPMI-03-13-0080-R;
RA Alkan N., Meng X., Friedlander G., Reuveni E., Sukno S., Sherman A.,
RA Thon M., Fluhr R., Prusky D.;
RT "Global aspects of pacC regulation of pathogenicity genes in Colletotrichum
RT gloeosporioides as revealed by transcriptome analysis.";
RL Mol. Plant Microbe Interact. 26:1345-1358(2013).
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000256|ARBA:ARBA00001971};
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:EQB53115.1}.
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DR EMBL; AMYD01001449; EQB53115.1; -; Genomic_DNA.
DR AlphaFoldDB; T0LXI2; -.
DR STRING; 1237896.T0LXI2; -.
DR eggNOG; KOG0157; Eukaryota.
DR HOGENOM; CLU_001570_14_2_1; -.
DR OMA; NRLISHY; -.
DR OrthoDB; 509202at2759; -.
DR Proteomes; UP000015530; 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:InterPro.
DR GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
DR CDD; cd11059; CYP_fungal; 1.
DR Gene3D; 1.10.630.10; Cytochrome P450; 1.
DR InterPro; IPR001128; Cyt_P450.
DR InterPro; IPR002401; Cyt_P450_E_grp-I.
DR InterPro; IPR036396; Cyt_P450_sf.
DR PANTHER; PTHR24305; CYTOCHROME P450; 1.
DR PANTHER; PTHR24305:SF164; P450, PUTATIVE (EUROFUNG)-RELATED; 1.
DR Pfam; PF00067; p450; 1.
DR PRINTS; PR00463; EP450I.
DR PRINTS; PR00385; P450.
DR SUPFAM; SSF48264; Cytochrome P450; 1.
PE 3: Inferred from homology;
KW Heme {ECO:0000256|ARBA:ARBA00022617}; Iron {ECO:0000256|ARBA:ARBA00022617};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022617};
KW Reference proteome {ECO:0000313|Proteomes:UP000015530}.
SQ SEQUENCE 483 AA; 54601 MW; 801760AEF662A3A7 CRC64;
MLLLSPVVLG AASIVLTLVY LARCVSSPLW RLPGPRASAF TSVLLKWHEW HAQRTKYIHR
LHEEYGPVVR IAPNEVAFTS YDAVKEIYCS GGSGYDKTEF YNLFRVYGRR TMFTTLNKED
HAKRKRIIAD RYANSNVLRP APLSGIQERS LNFIKRCEAS VGKSHDIFMS LHSYACDCVT
YHLFHPYGTN CLQDTADEEM MHQVAADDSL QNRLIQHYSP ALHKALSGVL YAFAKPRETP
LADNFVMESS RQPDPAPFTL LSRLHEKSSD LDQTDKAGEN LDHMAAGIDT TGDGLCFLMW
ELSQPRSMQF QERLQWELRE NPGVSFDKLP FLDAVVQEGL RVFPAIPMSL PRYVPQGGRT
IDGHFIPEKT IVSCQAYSVH RVNSDVFPRP DLFDPGRWMG PTGDAERKRL MFAFANGGRG
CVGKHLALAE MKILLSDIYS RYTTLPETSM TAESMAMSDQ LISSRPLGQR CLLQFVPIAE
KRE
//
