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Database: UniProt
Entry: A0A1Y2DTL6_9PEZI
LinkDB: A0A1Y2DTL6_9PEZI
Original site: A0A1Y2DTL6_9PEZI 
ID   A0A1Y2DTL6_9PEZI        Unreviewed;       332 AA.
AC   A0A1Y2DTL6;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   SubName: Full=2og-Fe oxygenase family protein {ECO:0000313|EMBL:ORY62623.1};
GN   ORFNames=BCR38DRAFT_346820 {ECO:0000313|EMBL:ORY62623.1};
OS   Pseudomassariella vexata.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Xylariomycetidae; Xylariales; Pseudomassariaceae; Pseudomassariella.
OX   NCBI_TaxID=1141098 {ECO:0000313|EMBL:ORY62623.1, ECO:0000313|Proteomes:UP000193689};
RN   [1] {ECO:0000313|EMBL:ORY62623.1, ECO:0000313|Proteomes:UP000193689}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 129021 {ECO:0000313|EMBL:ORY62623.1,
RC   ECO:0000313|Proteomes:UP000193689};
RG   DOE Joint Genome Institute;
RA   Mondo S.J., Dannebaum R.O., Kuo R.C., Labutti K., Haridas S., Kuo A.,
RA   Salamov A., Ahrendt S.R., Lipzen A., Sullivan W., Andreopoulos W.B.,
RA   Clum A., Lindquist E., Daum C., Ramamoorthy G.K., Gryganskyi A., Culley D.,
RA   Magnuson J.K., James T.Y., O'Malley M.A., Stajich J.E., Spatafora J.W.,
RA   Visel A., Grigoriev I.V.;
RT   "Pervasive Adenine N6-methylation of Active Genes in Fungi.";
RL   Submitted (JUL-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:ORY62623.1}.
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DR   EMBL; MCFJ01000009; ORY62623.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y2DTL6; -.
DR   STRING; 1141098.A0A1Y2DTL6; -.
DR   InParanoid; A0A1Y2DTL6; -.
DR   OrthoDB; 1380829at2759; -.
DR   Proteomes; UP000193689; 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:UP000193689}.
FT   DOMAIN          183..285
FT                   /note="Fe2OG dioxygenase"
FT                   /evidence="ECO:0000259|PROSITE:PS51471"
SQ   SEQUENCE   332 AA;  36559 MW;  84D2A3284027AF7F CRC64;
     MTIDKPTPFV IPTVDLAPYL EDPSSAASAN IIEQVRQACI TSGFFQIENH GISRDLQQSV
     LNAAEAFFAL PLEAKKQVVH PTLKNRGYEL IGSQALQEGA LPDLKEGFYV GQHIPNTDER
     VKDHPHLMGP NIFPPNIPED VLKNPTETYY RDLLSLSGKI MEILAKGLPY GNEVFVPFMS
     NDPVCSIRLL HYPPQKTKDV RQLGAGAHTD FGAITLLMQD MSGGLEVLND TTGQWIPVDP
     NPDAYVVNIG DMLSMWTKNK YKSATHRVIN TSNKDRYSVP FFVDGNTDVK LTPFDGSEPV
     GGKVLTAEEH MLERFGTTYG RAEKLVAASS GS
//
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