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Database: UniProt
Entry: A0A2B7Z9M1_9EURO
LinkDB: A0A2B7Z9M1_9EURO
Original site: A0A2B7Z9M1_9EURO 
ID   A0A2B7Z9M1_9EURO        Unreviewed;       356 AA.
AC   A0A2B7Z9M1;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   RecName: Full=Fe2OG dioxygenase domain-containing protein {ECO:0000259|PROSITE:PS51471};
GN   ORFNames=GX50_07335 {ECO:0000313|EMBL:PGH29893.1};
OS   Emmonsia crescens.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Ajellomycetaceae; Emmonsia.
OX   NCBI_TaxID=73230 {ECO:0000313|EMBL:PGH29893.1, ECO:0000313|Proteomes:UP000226031};
RN   [1] {ECO:0000313|EMBL:PGH29893.1, ECO:0000313|Proteomes:UP000226031}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UAMH4076 {ECO:0000313|EMBL:PGH29893.1,
RC   ECO:0000313|Proteomes:UP000226031};
RA   Munoz J.F., Mcewen J.G., Clay O.K., Cuomo C.A.;
RT   "Comparative genomics in systemic dimorphic fungi from Ajellomycetaceae.";
RL   Submitted (OCT-2017) 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:PGH29893.1}.
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DR   EMBL; PDND01000204; PGH29893.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2B7Z9M1; -.
DR   STRING; 73230.A0A2B7Z9M1; -.
DR   VEuPathDB; FungiDB:EMCG_02028; -.
DR   OrthoDB; 1057251at2759; -.
DR   Proteomes; UP000226031; 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:0044249; P:cellular biosynthetic process; IEA:UniProt.
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:SF35; 2OG-FE(II) OXYGENASE FAMILY, PUTATIVE (AFU_ORTHOLOGUE AFUA_5G11160)-RELATED; 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:UP000226031}.
FT   DOMAIN          182..287
FT                   /note="Fe2OG dioxygenase"
FT                   /evidence="ECO:0000259|PROSITE:PS51471"
SQ   SEQUENCE   356 AA;  40099 MW;  227E513C98B074BF CRC64;
     MSYEKNFDGI PPFADDVPCA PLLRLSLEKL LSHEEAEVQR FYSACKDLGF FYLDLRGNDI
     LADADQLFGI GEQLFELDLD EKRRYDLSKK NSYFGYKETG AAVVDREGNP DRNEFYNVSK
     DDILGISEPL PAPDILKKSR PLFKSFMTNA HNIVTTVLNL LNENLHLPPS TLANLHRLHA
     VSGDQVRMIK APPQPADDRR TALGQHTDFG SVTVLFNRVG GLQILPPGQD AEWCYVRPLP
     GHAIINLGDA MVKFTNGLLR SNIHRVVSPP GPQAETTRYS LVYFSRPEDD IILKRLEGSD
     CIPPLALRDE TGAVVEEEDI KSKDWIIRRA LGNRPALHKE IDYENTLGTE MMSRRI
//
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