ID K3VZ95_FUSPC Unreviewed; 489 AA.
AC K3VZ95;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=Cytochrome P450 {ECO:0008006|Google:ProtNLM};
GN ORFNames=FPSE_07864 {ECO:0000313|EMBL:EKJ72010.1};
OS Fusarium pseudograminearum (strain CS3096) (Wheat and barley crown-rot
OS fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX NCBI_TaxID=1028729 {ECO:0000313|EMBL:EKJ72010.1, ECO:0000313|Proteomes:UP000007978};
RN [1] {ECO:0000313|EMBL:EKJ72010.1, ECO:0000313|Proteomes:UP000007978}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CS3096 {ECO:0000313|EMBL:EKJ72010.1,
RC ECO:0000313|Proteomes:UP000007978};
RX PubMed=23028337; DOI=10.1371/journal.ppat.1002952;
RA Gardiner D.M., McDonald M.C., Covarelli L., Solomon P.S., Rusu A.G.,
RA Marshall M., Kazan K., Chakraborty S., McDonald B.A., Manners J.M.;
RT "Comparative pathogenomics reveals horizontally acquired novel virulence
RT genes in fungi infecting cereal hosts.";
RL PLoS Pathog. 8:E1002952-E1002952(2012).
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, 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:EKJ72010.1}.
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DR EMBL; AFNW01000277; EKJ72010.1; -; Genomic_DNA.
DR RefSeq; XP_009259257.1; XM_009260982.1.
DR AlphaFoldDB; K3VZ95; -.
DR EnsemblFungi; EKJ72010; EKJ72010; FPSE_07864.
DR GeneID; 20366482; -.
DR KEGG; fpu:FPSE_07864; -.
DR eggNOG; KOG0156; Eukaryota.
DR HOGENOM; CLU_001570_2_3_1; -.
DR OrthoDB; 2900138at2759; -.
DR Proteomes; UP000007978; Chromosome 1.
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; cd11065; CYP64-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; PTHR46300:SF7; P450, PUTATIVE (EUROFUNG)-RELATED; 1.
DR PANTHER; PTHR46300; P450, PUTATIVE (EUROFUNG)-RELATED-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 Metal-binding {ECO:0000256|RuleBase:RU000461};
KW Monooxygenase {ECO:0000256|RuleBase:RU000461};
KW Oxidoreductase {ECO:0000256|RuleBase:RU000461};
KW Reference proteome {ECO:0000313|Proteomes:UP000007978}.
SQ SEQUENCE 489 AA; 55441 MW; 959898B049036BA2 CRC64;
MPPTGVPAFR HWLKHKDTYG PVSSVSVLGQ PLIIIHDREA AHYLFDKSSG KSSGRPSANF
GGRLCGFDKI LSLQQYGDTF KRHRKLVHRQ MGTRAGAAKF RQIQDVESHR FLLRSLDNPG
NLMEHIRKEA GGVILKATYG YSIEPHKPDP LVHLVEFMVE GISIVVVPMK FVVDFLPWLE
YLPECLPGMS FKGRARQWRN ILNNTIEAPY QFVRQQMAKG IQCESYVSSL LTQEKLKGSG
NDILDETYEA DIKRTAAIMY AGGADTTVST IQSFILAMMV YPEVLKKAQA EIDNVIGPDR
LPGFEDRENL PYINGMVKES LRWMPAVPMG AAHKADDDIY YGDLCIPKGS FLLPNVWWFL
HNPETYRDPE RYDPDRYLEP RNEPDPDSNC WGYGRRICPG RLLADESIFI VIARVVAAFD
IEKDVDEQGN TIEPKVEFTT EGALSRPVDY PYRIKPRNAK CVDLIRAVEK EHPWDKGDAS
LLPQDMVVV
//
