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Database: UniProt
Entry: A0A5N5NSE0_9PEZI
LinkDB: A0A5N5NSE0_9PEZI
Original site: A0A5N5NSE0_9PEZI 
ID   A0A5N5NSE0_9PEZI        Unreviewed;       334 AA.
AC   A0A5N5NSE0;
DT   17-JUN-2020, integrated into UniProtKB/TrEMBL.
DT   17-JUN-2020, sequence version 1.
DT   27-MAR-2024, entry version 11.
DE   RecName: Full=Fe2OG dioxygenase domain-containing protein {ECO:0000259|PROSITE:PS51471};
GN   ORFNames=GE09DRAFT_1102645 {ECO:0000313|EMBL:KAB5570304.1};
OS   Coniochaeta sp. 2T2.1.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Coniochaetales; Coniochaetaceae; Coniochaeta.
OX   NCBI_TaxID=1571157 {ECO:0000313|EMBL:KAB5570304.1, ECO:0000313|Proteomes:UP000325492};
RN   [1] {ECO:0000313|EMBL:KAB5570304.1, ECO:0000313|Proteomes:UP000325492}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2T2.1 {ECO:0000313|EMBL:KAB5570304.1,
RC   ECO:0000313|Proteomes:UP000325492};
RX   PubMed=31572496;
RA   Mondo S.J., Jimenez D.J., Hector R.E., Lipzen A., Yan M., LaButti K.,
RA   Barry K., van Elsas J.D., Grigoriev I.V., Nichols N.N.;
RT   "Genome expansion by allopolyploidization in the fungal strain Coniochaeta
RT   2T2.1 and its exceptional lignocellulolytic machinery.";
RL   Biotechnol. Biofuels 12:229-229(2019).
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:KAB5570304.1}.
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DR   EMBL; VSMA01000007; KAB5570304.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A5N5NSE0; -.
DR   Proteomes; UP000325492; 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:SF62; IRON_ASCORBATE OXIDOREDUCTASE DDB_G0283291-RELATED; 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:UP000325492}.
FT   DOMAIN          185..296
FT                   /note="Fe2OG dioxygenase"
FT                   /evidence="ECO:0000259|PROSITE:PS51471"
SQ   SEQUENCE   334 AA;  37045 MW;  2EC821DFE1BAECAB CRC64;
     MEKAAVKGDG LLIPLIDFSK FLNGDDAQKQ EVAKAILHGF QTAGFIYLSN IPITEETRTH
     VFGTSAKFFD QPLEDKMAKC WTTPEANRGY SAPGREKVSQ LTDPAEVERM RSAAPDIKES
     FEIGREGEKD HPNQWPEEKD ALAGFKSTML DFFEQCKALH VEVMRAIAVG MDLDPGFFDG
     FVDVGDNTLR LLHYPAVDKK VFQVNPGQVR AGEHSDYGSI TLLFQDNRGG LQVKSPNGKF
     IDATPIPGTC VVNAGDLLAR WSNDTIKSTI HRVVEPPTVE GDIHPARYSI AYFCNPNFKS
     HIEVLPGTYA AEEEKKYPGI NSGQYLVQRL ATTY
//
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