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Database: UniProt
Entry: A0A423X8R4_9PEZI
LinkDB: A0A423X8R4_9PEZI
Original site: A0A423X8R4_9PEZI 
ID   A0A423X8R4_9PEZI        Unreviewed;       336 AA.
AC   A0A423X8R4;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   27-MAR-2024, entry version 15.
DE   RecName: Full=Fe2OG dioxygenase domain-containing protein {ECO:0000259|PROSITE:PS51471};
GN   ORFNames=VMCG_00594 {ECO:0000313|EMBL:ROW12213.1};
OS   Valsa malicola.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Diaporthales; Valsaceae; Valsa.
OX   NCBI_TaxID=356882 {ECO:0000313|EMBL:ROW12213.1, ECO:0000313|Proteomes:UP000283895};
RN   [1] {ECO:0000313|EMBL:ROW12213.1, ECO:0000313|Proteomes:UP000283895}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=03-1 {ECO:0000313|EMBL:ROW12213.1,
RC   ECO:0000313|Proteomes:UP000283895};
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   -!- SIMILARITY: Belongs to the iron/ascorbate-dependent oxidoreductase
CC       family. {ECO:0000256|ARBA:ARBA00008056, ECO:0000256|RuleBase:RU003682}.
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:ROW12213.1}.
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DR   EMBL; LKEA01000001; ROW12213.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A423X8R4; -.
DR   STRING; 356882.A0A423X8R4; -.
DR   Proteomes; UP000283895; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:1901362; P:organic cyclic compound biosynthetic process; IEA:UniProt.
DR   GO; GO:0044283; P:small molecule biosynthetic process; IEA:UniProt.
DR   InterPro; IPR026992; DIOX_N.
DR   InterPro; IPR044861; IPNS-like_FE2OG_OXY.
DR   InterPro; IPR027443; IPNS-like_sf.
DR   InterPro; IPR005123; Oxoglu/Fe-dep_dioxygenase.
DR   PANTHER; PTHR47990; 2-OXOGLUTARATE (2OG) AND FE(II)-DEPENDENT OXYGENASE SUPERFAMILY PROTEIN-RELATED; 1.
DR   PANTHER; PTHR47990:SF27; FE2OG DIOXYGENASE DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF03171; 2OG-FeII_Oxy; 1.
DR   Pfam; PF14226; DIOX_N; 1.
DR   SUPFAM; SSF51197; Clavaminate synthase-like; 1.
DR   PROSITE; PS51471; FE2OG_OXY; 1.
PE   3: Inferred from homology;
KW   Iron {ECO:0000256|RuleBase:RU003682};
KW   Metal-binding {ECO:0000256|RuleBase:RU003682};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU003682};
KW   Reference proteome {ECO:0000313|Proteomes:UP000283895}.
FT   DOMAIN          188..298
FT                   /note="Fe2OG dioxygenase"
FT                   /evidence="ECO:0000259|PROSITE:PS51471"
SQ   SEQUENCE   336 AA;  37067 MW;  94360B505A5CBAB6 CRC64;
     MEKAAVDEQG LMIPLIDLSR FLNGDAAQRK ETADAILNGF QNAGFIYLKG LPITPSTRKH
     VFDTSAKFFN GLSKDEKMAL GWTTPEANRG YSAPGREKVT QLTDITEVAK LKAGNPDIKE
     SFEIGRDSDP AWPNQWPVEE PGTAVDGFKK TMLDFFDQCK TIHVEVMRAV AVGMGLDEDY
     FDGFTDAGDN TLRLLHYPAV KSEVFKINPG QVRAGSHSDY GSITLLFQDS AGGLQVRSPN
     GTFVDAAPIE DTCVVNAGDL LARWSNETIK STVHRVVEPR RKADEHPARY SIAYFCNPNF
     KSHIEAIPGT YSTEADKKYE GINSGQYLVQ RLAATY
//
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