ID A0A423W056_9PEZI Unreviewed; 247 AA.
AC A0A423W056;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 13.
DE RecName: Full=Fe2OG dioxygenase domain-containing protein {ECO:0000259|PROSITE:PS51471};
GN ORFNames=VSDG_05607 {ECO:0000313|EMBL:ROV96720.1};
OS Valsa sordida.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Diaporthales; Valsaceae; Valsa.
OX NCBI_TaxID=252740 {ECO:0000313|EMBL:ROV96720.1, ECO:0000313|Proteomes:UP000284375};
RN [1] {ECO:0000313|EMBL:ROV96720.1, ECO:0000313|Proteomes:UP000284375}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YSFL {ECO:0000313|EMBL:ROV96720.1,
RC ECO:0000313|Proteomes:UP000284375};
RA Yin Z., Huang L.;
RT "Host preference determinants of Valsa canker pathogens revealed by
RT comparative genomics.";
RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=L-ascorbate; Xref=ChEBI:CHEBI:38290;
CC Evidence={ECO:0000256|ARBA:ARBA00001961};
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:ROV96720.1}.
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DR EMBL; LJZO01000019; ROV96720.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A423W056; -.
DR Proteomes; UP000284375; Unassembled WGS sequence.
DR GO; GO:0051213; F:dioxygenase activity; IEA:UniProtKB-KW.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0031418; F:L-ascorbic acid binding; IEA:InterPro.
DR GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
DR Gene3D; 2.60.120.620; q2cbj1_9rhob like domain; 1.
DR InterPro; IPR005123; Oxoglu/Fe-dep_dioxygenase.
DR InterPro; IPR045054; P4HA-like.
DR InterPro; IPR006620; Pro_4_hyd_alph.
DR InterPro; IPR044862; Pro_4_hyd_alph_FE2OG_OXY.
DR PANTHER; PTHR10869:SF207; P4HA_N DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR PANTHER; PTHR10869; PROLYL 4-HYDROXYLASE ALPHA SUBUNIT; 1.
DR Pfam; PF13640; 2OG-FeII_Oxy_3; 1.
DR SMART; SM00702; P4Hc; 1.
DR PROSITE; PS51471; FE2OG_OXY; 1.
PE 4: Predicted;
KW Dioxygenase {ECO:0000256|ARBA:ARBA00022964};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000284375}.
FT DOMAIN 131..245
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000259|PROSITE:PS51471"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 247 AA; 27825 MW; 5B304CBF54494862 CRC64;
MPKAKGKPTA KAKTSNAATT TRPAAAPPSW PVFRPPLPLT DLQPEPLLDS RVLLIRNFWP
RSLCRDYISF LRSLPLTTTP GKPKRGDAVR VNDRFQVQDQ GFANRLWLET GLKQLLMSEE
WKGLWGGDVV GLSPNIRIYR YSAGQFFDAH YDDSNAITSD FDQGTPIQTK TTWTVLLYLT
SEADGCRGGE TVFFPHDRRV AREEVAVPPE TGMVLLHKHG DDCMMHEGRE VMAGEKWVIR
SDICVRK
//
