ID A0A161Y7S7_9PEZI Unreviewed; 461 AA.
AC A0A161Y7S7;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE SubName: Full=Cytochrome P450 oxidoreductase {ECO:0000313|EMBL:KZL67897.1};
GN ORFNames=CT0861_12297 {ECO:0000313|EMBL:KZL67897.1};
OS Colletotrichum tofieldiae.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum spaethianum species complex.
OX NCBI_TaxID=708197 {ECO:0000313|EMBL:KZL67897.1, ECO:0000313|Proteomes:UP000076552};
RN [1] {ECO:0000313|EMBL:KZL67897.1, ECO:0000313|Proteomes:UP000076552}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=0861 {ECO:0000313|EMBL:KZL67897.1,
RC ECO:0000313|Proteomes:UP000076552};
RA Hacquard S., Kracher B., Hiruma K., Weinman A., Muench P., Garrido Oter R.,
RA Ver Loren van Themaat E., Dallerey J.-F., Damm U., Henrissat B.,
RA Lespinet O., Thon M., Kemen E., McHardy A.C., Schulze-Lefert P.,
RA O'Connell R.J.;
RT "Survival trade-offs in plant roots during colonization by closely related
RT pathogenic and mutualistic fungi.";
RL Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
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:KZL67897.1}.
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DR EMBL; LFIV01000135; KZL67897.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A161Y7S7; -.
DR STRING; 708197.A0A161Y7S7; -.
DR OrthoDB; 408598at2759; -.
DR Proteomes; UP000076552; 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:InterPro.
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; IPR002401; Cyt_P450_E_grp-I.
DR InterPro; IPR036396; Cyt_P450_sf.
DR PANTHER; PTHR24305; CYTOCHROME P450; 1.
DR PANTHER; PTHR24305:SF188; 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 Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022617};
KW Reference proteome {ECO:0000313|Proteomes:UP000076552};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 15..34
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 461 AA; 52561 MW; 0B30AA9B84DD3D60 CRC64;
MESPVLFKSI TSNLLGFQTA VYVLAGLVCA FYVVRPFLSP LRPVPGPFLA RYTDAWFLWR
VHRGHVEQDF ISLHREHGSI VRYGPNRYSI KDLEAPKIIY GHGHSFVKSS LYRSYSSPEL
QDWNPFAVEN PQVHSQLRRH LQSTYTLSAL VSYEPYVDEC ARILKQRLEE ISVAGLPIDF
GHWLQCYAFD VIGLITYGSR FGFLDRGEDV HGVISAIDIS LQDSSRLSMY PSFHVPAVLL
RSWLSGGKSG FAYVNNFAQL NIDRFRANSK TATLESDEEA GGKMQSFLEK FLQKHEADPT
NFTIMHIFTG CGANVGAGSD TTGISLSAIL YYLMKRPDCY QKLREEADAV QPSQNKEFTF
HETRDMPYLQ AVIKEALRVH PAFGMPLERV VPEGGATIAG RFFPPGDAQN KVSVHCWVEN
RNELIFEDPD DFRPERWLIE DENKLMLMNR HWIPHSEQRT L
//
