ID T0JTJ1_COLGC Unreviewed; 505 AA.
AC T0JTJ1;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE RecName: Full=Cytochrome P450 {ECO:0008006|Google:ProtNLM};
GN ORFNames=CGLO_17513 {ECO:0000313|EMBL:EQB43808.1};
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:EQB43808.1, 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|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:EQB43808.1}.
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DR EMBL; AMYD01004165; EQB43808.1; -; Genomic_DNA.
DR AlphaFoldDB; T0JTJ1; -.
DR STRING; 1237896.T0JTJ1; -.
DR eggNOG; KOG0158; Eukaryota.
DR HOGENOM; CLU_001570_14_0_1; -.
DR OMA; IVNPVYT; -.
DR OrthoDB; 408598at2759; -.
DR Proteomes; UP000015530; 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; cd11060; CYP57A1-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:SF229; P450, PUTATIVE (EUROFUNG)-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|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:UP000015530};
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 505 AA; 57629 MW; D094EB55167EAEBF CRC64;
MFLELSLPRV GVLIALPVIY WIGWVVYART FHPLSRIPGP FLATVSRLWY MLKIWTEDVE
KDERALHEKY GPLVRLAPDE ISCSDPEAFA DIYRFSNALD KAQFYEPYNT TGFSPHGDVF
SCKSDKKHGQ RRRITSSVYS MSNVSKSEQY IDTCSDLLTE RLGQYADSGK PCDIGEWLHW
YTFDIIGELF YGRAFGFVDE GKDQNDWIKS LDKMIPFVCL MGVAPPILRP FVGIGCMLTS
AGKEIAKGVK NIGESSARLM KDAYESRLEA PRTDMAQQVF SIYEKSGEKF DYRWGDVEQE
SYGALFAGSD TTAIAFRSLF YHLMHNPEAY RKLEAEVDQA VNEGRLSMPP TYKETSQLPY
LCACIKEALR IHPGAQLSLP RIVPPQGMTL CGQFIPGGYV VGINAAVLHF DKKVFGADAE
SFNPDRWMDQ SRANYMDKFM MAFGSGTRTC LGKNIALIEL HKLTPQLVWN YRFEFYDQAK
TQWHTRNTFF ARQEGVIARV KRRNH
//