ID A0A0G2I2F0_9PEZI Unreviewed; 555 AA.
AC A0A0G2I2F0;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Putative cytochrome p450 monooxygenase {ECO:0000313|EMBL:KKY34235.1};
GN ORFNames=UCDDA912_g05793 {ECO:0000313|EMBL:KKY34235.1};
OS Diaporthe ampelina.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Diaporthales; Diaporthaceae; Diaporthe.
OX NCBI_TaxID=1214573 {ECO:0000313|EMBL:KKY34235.1, ECO:0000313|Proteomes:UP000034680};
RN [1] {ECO:0000313|EMBL:KKY34235.1, ECO:0000313|Proteomes:UP000034680}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DA912 {ECO:0000313|EMBL:KKY34235.1};
RA Lawrence D.P., Travadon R., Rolshausen P.E., Baumgartner K.;
RT "Distinctive expansion of gene families associated with plant cell wall
RT degradation and secondary metabolism in the genomes of grapevine trunk
RT pathogens.";
RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KKY34235.1, ECO:0000313|Proteomes:UP000034680}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DA912 {ECO:0000313|EMBL:KKY34235.1};
RA Morales-Cruz A., Amrine K.C., Cantu D.;
RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000256|ARBA:ARBA00001971,
CC ECO:0000256|PIRSR:PIRSR602403-1};
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:KKY34235.1}.
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DR EMBL; LCUC01000212; KKY34235.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G2I2F0; -.
DR STRING; 1214573.A0A0G2I2F0; -.
DR OrthoDB; 1611592at2759; -.
DR Proteomes; UP000034680; 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:UniProtKB-KW.
DR GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
DR CDD; cd00302; cytochrome_P450; 1.
DR Gene3D; 1.10.630.10; Cytochrome P450; 1.
DR InterPro; IPR001128; Cyt_P450.
DR InterPro; IPR002403; Cyt_P450_E_grp-IV.
DR InterPro; IPR036396; Cyt_P450_sf.
DR PANTHER; PTHR24305; CYTOCHROME P450; 1.
DR PANTHER; PTHR24305:SF87; CYTOCHROME P450 MONOOXYGENASE ALND-RELATED; 1.
DR Pfam; PF00067; p450; 1.
DR PRINTS; PR00465; EP450IV.
DR PRINTS; PR00385; P450.
DR SUPFAM; SSF48264; Cytochrome P450; 1.
PE 3: Inferred from homology;
KW Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|PIRSR:PIRSR602403-1};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRSR:PIRSR602403-1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR602403-1};
KW Monooxygenase {ECO:0000256|ARBA:ARBA00023033, ECO:0000313|EMBL:KKY34235.1};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023033,
KW ECO:0000313|EMBL:KKY34235.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000034680}.
FT BINDING 494
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000256|PIRSR:PIRSR602403-1"
SQ SEQUENCE 555 AA; 62387 MW; 637D543BD8F5DA3E CRC64;
MRPDFATKQF YLLGEHVSTA REIDVPSTID EDELRQLIAS NFAIVGAKGI GFVNDREAFS
SVAEVLDAQG PVAITIDGRG VREVQGPKGL PYVGNYFEIY PDHLGNHQRL FEKYGPLFKT
NNMGSATYLT NDPTLAGIFF SENDFFTKDI IPGHPLYPIK NNEAGVFLGD TDTEEWKVAH
KFLPPFFGPK AVRHYAPTMN QTVEDAFKVF DELADRDEAW NVYSYMLKLG SQAVGKLILG
MDFNHFSSVD APPHEMVILM ATSLELNKKI TSMGSWYAHL PFGDPKRLHD ARERMRVMIE
EVIAGASRGV EDLDLQEAAL KANNMVDYVL RATDSKGNKI PTNRVLEPLV VATGAGFTTT
SSLLSWLLYG MVNYPGMQAR LLQELVDAGF ADGTEVTPDL TAKMPFLDHF IKETQRRHNP
SYQPARTARR DLVLPGGYKV PRDAIVIPAL HHIHNNPAIW GNPAAFDPDR WDSGRVRNRP
NNSYIPFATG PRGCIGFNFA LQEVRIFLTK LVWRYEFSLA TEGAVDYDPM FQLIRPTNLY
VRAERRVKWP PRTEA
//