ID R1E766_BOTPV Unreviewed; 505 AA.
AC R1E766;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE SubName: Full=Putative pisatin demethylase protein {ECO:0000313|EMBL:EOD43272.1};
GN ORFNames=UCRNP2_10020 {ECO:0000313|EMBL:EOD43272.1};
OS Botryosphaeria parva (strain UCR-NP2) (Grapevine canker fungus)
OS (Neofusicoccum parvum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetes incertae sedis; Botryosphaeriales; Botryosphaeriaceae;
OC Neofusicoccum.
OX NCBI_TaxID=1287680 {ECO:0000313|EMBL:EOD43272.1, ECO:0000313|Proteomes:UP000013521};
RN [1] {ECO:0000313|Proteomes:UP000013521}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UCR-NP2 {ECO:0000313|Proteomes:UP000013521};
RX PubMed=23766404; DOI=10.1128/genomea.00339-13;
RA Blanco-Ulate B., Rolshausen P., Cantu D.;
RT "Draft genome sequence of Neofusicoccum parvum isolate UCR-NP2, a fungal
RT vascular pathogen associated with grapevine cankers.";
RL Genome Announc. 1:E0033913-E0033913(2013).
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, ECO:0000256|RuleBase:RU000461}.
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DR EMBL; KB916876; EOD43272.1; -; Genomic_DNA.
DR RefSeq; XP_007589253.1; XM_007589191.1.
DR AlphaFoldDB; R1E766; -.
DR KEGG; npa:UCRNP2_10020; -.
DR eggNOG; KOG0158; Eukaryota.
DR HOGENOM; CLU_001570_14_0_1; -.
DR OMA; EPFVDTC; -.
DR OrthoDB; 408598at2759; -.
DR Proteomes; UP000013521; 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:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
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 GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
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; IPR002403; Cyt_P450_E_grp-IV.
DR InterPro; IPR036396; Cyt_P450_sf.
DR PANTHER; PTHR24305:SF190; -; 1.
DR PANTHER; PTHR24305; CYTOCHROME P450; 1.
DR Pfam; PF00067; p450; 1.
DR PRINTS; PR00465; EP450IV.
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|PIRSR:PIRSR602403-1, ECO:0000256|RuleBase:RU000461};
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 Methyltransferase {ECO:0000313|EMBL:EOD43272.1};
KW Monooxygenase {ECO:0000256|RuleBase:RU000461};
KW Oxidoreductase {ECO:0000256|RuleBase:RU000461};
KW Reference proteome {ECO:0000313|Proteomes:UP000013521};
KW Transferase {ECO:0000313|EMBL:EOD43272.1}.
FT BINDING 452
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 505 AA; 56158 MW; 1A004784DF136FE0 CRC64;
MGLISSLPSA DLQSTAIYIA CLPAGIILFT LIQRIYTSFF GPLRGVKGPW LARYTRLWEM
FALYQGDFEK QNIALHKRYG KIVRIAPNKY TIDDPDAVRT IYGHGTKFTK TRFYEAFRMP
DRSNLFAELD VKEHAMQRRR IASLYSLTNL LSYESFIDKC TAVLDDKFTK FAHEGRAVEM
VEFLQFYAFD VIGAITAGNP FGLMTSERDS AGIITAIHHA MQYGGFTGLI PEAHPWIVRA
AALFSRSGVS NNAVGAYIQA QISLRRAGVT PADKHDFLTK LLQLEAAGAN TAFDTFNSCG
SNIAAGSDTT AITLSAVLYH LLRAPRALAA LRREIDAAAA DGRVADPVTY AQAQDQLPYL
QAVLKEALRV HPAVGQPLLR RVPPGGAVVA GRWFPEGAEV GVNPWVAHSN EEVFGADAAA
FRPERWLERG EGEEAKRMEG YFLAFGHGSR TCIGKHISLL EISKVIPQLV RKFDFELVEP
GKEWETATAW FTKQRFHCYI KRRAE
//