ID A0A2J5HCS0_9EURO Unreviewed; 254 AA.
AC A0A2J5HCS0;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=Fe2OG dioxygenase domain-containing protein {ECO:0000259|PROSITE:PS51471};
GN ORFNames=BDW42DRAFT_182020 {ECO:0000313|EMBL:PLN74529.1};
OS Aspergillus taichungensis.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=482145 {ECO:0000313|EMBL:PLN74529.1, ECO:0000313|Proteomes:UP000235023};
RN [1] {ECO:0000313|Proteomes:UP000235023}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBT 19404 {ECO:0000313|Proteomes:UP000235023};
RG DOE Joint Genome Institute;
RA Mondo S.J., Kjaerbolling I., Vesth T.C., Frisvad J.C., Nybo J.L.,
RA Theobald S., Kuo A., Bowyer P., Matsuda Y., Lyhne E.K., Kogle M.E.,
RA Clum A., Lipzen A., Salamov A., Ngan C.Y., Daum C., Chiniquy J., Barry K.,
RA LaButti K., Haridas S., Simmons B.A., Magnuson J.K., Mortensen U.H.,
RA Larsen T.O., Grigoriev I.V., Baker S.E., Andersen M.R., Nordberg H.P.,
RA Cantor M.N., Hua S.X.;
RL Submitted (DEC-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=L-ascorbate; Xref=ChEBI:CHEBI:38290;
CC Evidence={ECO:0000256|ARBA:ARBA00001961};
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DR EMBL; KZ559710; PLN74529.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2J5HCS0; -.
DR OrthoDB; 5473532at2759; -.
DR Proteomes; UP000235023; Unassembled WGS sequence.
DR GO; GO:0051213; F:dioxygenase activity; IEA:UniProtKB-KW.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0031418; F:L-ascorbic acid binding; IEA:InterPro.
DR GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
DR GO; GO:0044249; P:cellular biosynthetic process; IEA:UniProt.
DR GO; GO:1901576; P:organic substance biosynthetic process; IEA:UniProt.
DR Gene3D; 2.60.120.620; q2cbj1_9rhob like domain; 1.
DR InterPro; IPR005123; Oxoglu/Fe-dep_dioxygenase.
DR InterPro; IPR045054; P4HA-like.
DR InterPro; IPR006620; Pro_4_hyd_alph.
DR InterPro; IPR044862; Pro_4_hyd_alph_FE2OG_OXY.
DR PANTHER; PTHR10869:SF207; P4HA_N DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR PANTHER; PTHR10869; PROLYL 4-HYDROXYLASE ALPHA SUBUNIT; 1.
DR Pfam; PF13640; 2OG-FeII_Oxy_3; 1.
DR SMART; SM00702; P4Hc; 1.
DR PROSITE; PS51471; FE2OG_OXY; 1.
PE 4: Predicted;
KW Dioxygenase {ECO:0000256|ARBA:ARBA00022964};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT DOMAIN 143..254
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000259|PROSITE:PS51471"
FT REGION 1..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 9..25
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 254 AA; 28384 MW; AF92A42B7B7EC73C CRC64;
MGKPKPPKPS KNQPKEPKEP EQEIPKWPPL RPSPPKAHTL SLTPLLPSHI YTTTGLLPAP
LCKAYVSFLS SLQLSTTPVQ RGKDYAARVN DRFQVWDPGF ARVLWEGTAL RELVLSFLSE
DGKEEGEGGE DGEGNMWDGV PIGLNPNIRV YRYSKGQFFA KHYDDSNTLT LPPSSQKFHT
TWTLLIYLST CTGGETVFYP EPTRENRSPE PISVAPRVGM ALLHRHGESC LLHEGREVTG
GEKWVLRSDL VVSR
//
