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Database: UniProt
Entry: A0A1J9RPU6_9PEZI
LinkDB: A0A1J9RPU6_9PEZI
Original site: A0A1J9RPU6_9PEZI 
ID   A0A1J9RPU6_9PEZI        Unreviewed;       357 AA.
AC   A0A1J9RPU6;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   SubName: Full=2og-fe oxygenase family {ECO:0000313|EMBL:OJD30487.1};
GN   ORFNames=BKCO1_6000047 {ECO:0000313|EMBL:OJD30487.1};
OS   Diplodia corticola.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetes incertae sedis; Botryosphaeriales; Botryosphaeriaceae;
OC   Diplodia.
OX   NCBI_TaxID=236234 {ECO:0000313|EMBL:OJD30487.1, ECO:0000313|Proteomes:UP000183809};
RN   [1] {ECO:0000313|EMBL:OJD30487.1, ECO:0000313|Proteomes:UP000183809}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 112549 {ECO:0000313|EMBL:OJD30487.1,
RC   ECO:0000313|Proteomes:UP000183809};
RA   Fernandes I., De Jonge R., Van De Peer Y., Devreese B., Alves A.,
RA   Esteves A.C.;
RT   "Proteomics and genomics reveal pathogen-plant mechanisms compatible with a
RT   hemibiotrophic lifestyle of Diplodia corticola.";
RL   Submitted (OCT-2016) 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:OJD30487.1}.
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DR   EMBL; MNUE01000060; OJD30487.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1J9RPU6; -.
DR   STRING; 236234.A0A1J9RPU6; -.
DR   OrthoDB; 1332763at2759; -.
DR   Proteomes; UP000183809; 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   PRINTS; PR00682; IPNSYNTHASE.
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:UP000183809}.
FT   DOMAIN          193..310
FT                   /note="Fe2OG dioxygenase"
FT                   /evidence="ECO:0000259|PROSITE:PS51471"
SQ   SEQUENCE   357 AA;  39670 MW;  4FC2F3A25B400DCF CRC64;
     MASIQVDSAV EKDDLFIPLI DFSHFASPTS TPSTRLATAR ALLSGFQRAG FVYLRNHGIP
     AADVRAVFAH SAGFFARPQP QKDALAWYSP RANRGYVAHG REKVTRADYA GDVAQLRAAV
     PDLKESMEIG REGEDGCPNM WPSAEEEAGA AFREVMEAFH GMCKELHRGV MRAVALGMGL
     EDEGWFDEYT RRGDNTLRLL HYPEVEKSVF EREDGQVQVR AGEHSDYGSL TLLFQDDRGG
     LQVLSPKGTF VDATPIPDTI VVNAGDLLER WANDTIKSTK HRVVEPPPKP GQESLEKYPA
     RYSVAYFCNP DFDKLIEAIP GTYEEGKQKY PGVLSGDYLA KRLSETYGDL DKYDLKV
//
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