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Database: UniProt
Entry: A0A0D2I206_9EURO
LinkDB: A0A0D2I206_9EURO
Original site: A0A0D2I206_9EURO 
ID   A0A0D2I206_9EURO        Unreviewed;       317 AA.
AC   A0A0D2I206;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   RecName: Full=Fe2OG dioxygenase domain-containing protein {ECO:0000259|PROSITE:PS51471};
GN   ORFNames=Z518_10706 {ECO:0000313|EMBL:KIW99778.1};
OS   Rhinocladiella mackenziei CBS 650.93.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae;
OC   Rhinocladiella.
OX   NCBI_TaxID=1442369 {ECO:0000313|EMBL:KIW99778.1, ECO:0000313|Proteomes:UP000053617};
RN   [1] {ECO:0000313|EMBL:KIW99778.1, ECO:0000313|Proteomes:UP000053617}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 650.93 {ECO:0000313|EMBL:KIW99778.1,
RC   ECO:0000313|Proteomes:UP000053617};
RG   The Broad Institute Genomics Platform;
RA   Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA   Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Rhinocladiella mackenzie CBS 650.93.";
RL   Submitted (JAN-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}.
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DR   EMBL; KN847484; KIW99778.1; -; Genomic_DNA.
DR   RefSeq; XP_013266991.1; XM_013411537.1.
DR   AlphaFoldDB; A0A0D2I206; -.
DR   STRING; 1442369.A0A0D2I206; -.
DR   GeneID; 25298777; -.
DR   VEuPathDB; FungiDB:Z518_10706; -.
DR   HOGENOM; CLU_010119_6_3_1; -.
DR   OrthoDB; 1380829at2759; -.
DR   Proteomes; UP000053617; 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:SF272; SEXUAL DIFFERENTIATION PROCESS PROTEIN ISP7; 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:UP000053617}.
FT   DOMAIN          175..279
FT                   /note="Fe2OG dioxygenase"
FT                   /evidence="ECO:0000259|PROSITE:PS51471"
SQ   SEQUENCE   317 AA;  35564 MW;  E0BB27498644B972 CRC64;
     MGSISDAPAL EIPLINISGY LRGDQEQASQ IAKALHSACQ SPGFFQITGH GVPSELRAKL
     LAKLAEFFAL PMAIKQGLHR GQSKCLRGYE TVGEQRLEEA FSDQKEGFMI GPELPADGRF
     LQGPNQWPDE EIIPGFRDTF MAYFNEVHSL SKVMFRLMAL SLDLDEHYFD EFVSTIAMCR
     AHRYPPTTPE MATKSRGIGA HTDFGALTLL LQDDIGGLEV FHKTTGTWHG VPPVQDAYVV
     NIGDMMERWT NNSYTSTLHR VISPVCNRDR YSVAFFNEGL LDQVIECIPT CLKPSDKPLY
     EPIRAEDHLR TRYGKSY
//
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