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Database: UniProt
Entry: A0A5N5PFR8_9PEZI
LinkDB: A0A5N5PFR8_9PEZI
Original site: A0A5N5PFR8_9PEZI 
ID   A0A5N5PFR8_9PEZI        Unreviewed;       423 AA.
AC   A0A5N5PFR8;
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_546975 {ECO:0000313|EMBL:KAB5578372.1};
OS   Coniochaeta sp. 2T2.1.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Coniochaetales; Coniochaetaceae; Coniochaeta.
OX   NCBI_TaxID=1571157 {ECO:0000313|EMBL:KAB5578372.1, ECO:0000313|Proteomes:UP000325492};
RN   [1] {ECO:0000313|EMBL:KAB5578372.1, ECO:0000313|Proteomes:UP000325492}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2T2.1 {ECO:0000313|EMBL:KAB5578372.1,
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:KAB5578372.1}.
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DR   EMBL; VSMA01000004; KAB5578372.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A5N5PFR8; -.
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   Pfam; PF03171; 2OG-FeII_Oxy; 1.
DR   Pfam; PF14226; DIOX_N; 2.
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          198..308
FT                   /note="Fe2OG dioxygenase"
FT                   /evidence="ECO:0000259|PROSITE:PS51471"
FT   REGION          392..423
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   423 AA;  46185 MW;  2A26BE56B1BF0B1D CRC64;
     MSFTSIPILD MALANDPATK AAFLSDLRHA LLEVGFLYLK NVGIPDELFK RTIEEGKGFF
     DIPEEEKSVP SPPLLNPHLY SSSPSPTNPL HVRLKIEMKN APSFLGYSRL SAEVTAGAAD
     HREQIDLSTP HPVPPPTAPR YHNLLAPNQW PSPSVLPRFR PTFEEYMSHM GSVSLRFTSL
     IAEAIGLPPN AFDRYFDQPP STQQHKLKIV KYPDAPGDGS RDNQGVGPHK DSMLTSYLLQ
     ASQHKGLQVQ NVRGEWIDCP PIDGTLVVAI GQGMEALTRG VCVSTTHRVL SPPAGQGARY
     SIPFFQGVRG DAEFEELETV GVGSVPEEVR ELRRKVVERN GGGRLDDVEF TFRTGGRART
     LGEATLRNRV KSHPDVGERW YPDILAEIRE EQAAAAGKKS PAAGEGEGGE GAPVVEAKAV
     EAH
//
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