ID A0A1Y2DHG7_9PEZI Unreviewed; 385 AA.
AC A0A1Y2DHG7;
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(II) oxygenase {ECO:0000313|EMBL:ORY58701.1};
GN ORFNames=BCR38DRAFT_413024 {ECO:0000313|EMBL:ORY58701.1};
OS Pseudomassariella vexata.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Xylariomycetidae; Xylariales; Pseudomassariaceae; Pseudomassariella.
OX NCBI_TaxID=1141098 {ECO:0000313|EMBL:ORY58701.1, ECO:0000313|Proteomes:UP000193689};
RN [1] {ECO:0000313|EMBL:ORY58701.1, ECO:0000313|Proteomes:UP000193689}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 129021 {ECO:0000313|EMBL:ORY58701.1,
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:ORY58701.1}.
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DR EMBL; MCFJ01000015; ORY58701.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y2DHG7; -.
DR STRING; 1141098.A0A1Y2DHG7; -.
DR InParanoid; A0A1Y2DHG7; -.
DR OrthoDB; 2908779at2759; -.
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: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:UP000193689}.
FT DOMAIN 221..333
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000259|PROSITE:PS51471"
SQ SEQUENCE 385 AA; 43248 MW; B15BA83F3CFC8537 CRC64;
MTKISPAEAT QYSTTKLRIS SGNGPVSRDV LCTPLRNADP SEIPIIDVSG IFSPSLHERT
AVAKQIHDAA ANNGFFYIKN TGISAEITSA AHTSCLDFFR QPPDLKERAN SNQSKCYNGY
KPPKTQRINP FESIDNRESF SWRYDPEYDP CIGDISSIPP EIAECLHSED FIWTATANLP
NFKPSLITYW RACLALARAL VRSFALSLDL AEDFFDAKFS HPDASLSLNY YPPIPKPDSS
SVAAADVAHT PVSIGSHTDF QLFTILWQDR NGGLQVLNRQ GQWINASPVE GTFVVNIADY
LQRITNDRYV STVHRAQNWS GRERVSMPFF FGFNLNESCA VLDCCVEPGE QSRYEEVSCK
EWVRRRVKDM HRTEGDEEEK VLLTS
//