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Database: UniProt
Entry: A0A5J9STJ5_9POAL
LinkDB: A0A5J9STJ5_9POAL
Original site: A0A5J9STJ5_9POAL 
ID   A0A5J9STJ5_9POAL        Unreviewed;       314 AA.
AC   A0A5J9STJ5;
DT   11-DEC-2019, integrated into UniProtKB/TrEMBL.
DT   11-DEC-2019, sequence version 1.
DT   24-JAN-2024, entry version 13.
DE   RecName: Full=Fe2OG dioxygenase domain-containing protein {ECO:0000259|PROSITE:PS51471};
DE   Flags: Fragment;
GN   ORFNames=EJB05_52240 {ECO:0000313|EMBL:TVU02268.1};
OS   Eragrostis curvula (weeping love grass).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC   Chloridoideae; Eragrostideae; Eragrostidinae; Eragrostis.
OX   NCBI_TaxID=38414 {ECO:0000313|EMBL:TVU02268.1, ECO:0000313|Proteomes:UP000324897};
RN   [1] {ECO:0000313|EMBL:TVU02268.1, ECO:0000313|Proteomes:UP000324897}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Victoria {ECO:0000313|Proteomes:UP000324897};
RC   TISSUE=Leaf {ECO:0000313|EMBL:TVU02268.1};
RX   PubMed=31308395; DOI=.1038/s41598-019-46610-0;
RA   Carballo J., Santos B.A.C.M., Zappacosta D., Garbus I., Selva J.P.,
RA   Gallo C.A., Diaz A., Albertini E., Caccamo M., Echenique V.;
RT   "A high-quality genome of Eragrostis curvula grass provides insights into
RT   Poaceae evolution and supports new strategies to enhance forage quality.";
RL   Sci. Rep. 9:10250-10250(2019).
CC   -!- COFACTOR:
CC       Name=L-ascorbate; Xref=ChEBI:CHEBI:38290;
CC         Evidence={ECO:0000256|ARBA:ARBA00001961};
CC   -!- SIMILARITY: Belongs to the iron/ascorbate-dependent oxidoreductase
CC       family. {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:TVU02268.1}.
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DR   EMBL; RWGY01000343; TVU02268.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A5J9STJ5; -.
DR   Proteomes; UP000324897; 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   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:SF128; 2-OXOGLUTARATE (2OG) AND FE(II)-DEPENDENT OXYGENASE SUPERFAMILY PROTEIN; 1.
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; 1.
DR   SUPFAM; SSF51197; Clavaminate synthase-like; 1.
DR   PROSITE; PS51471; FE2OG_OXY; 1.
PE   3: Inferred from homology;
KW   Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|RuleBase:RU003682};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU003682};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU003682};
KW   Reference proteome {ECO:0000313|Proteomes:UP000324897}.
FT   DOMAIN          154..257
FT                   /note="Fe2OG dioxygenase"
FT                   /evidence="ECO:0000259|PROSITE:PS51471"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:TVU02268.1"
SQ   SEQUENCE   314 AA;  35217 MW;  E75C22FBD339F4E9 CRC64;
     MDIGKVNLSG VESGKPGWDE ARSAVTASLV AHGCVVVAHD ALSPELMRSL FDRAMPELFA
     LPRETRLRNV SAKGNFRGYM GFDNWESVSV DEPTEEGNVN DFVSLFWPQG NPESRDVMLQ
     FGRNLLKLKE TVEKMVLEGL GVRKENIESH LRSLSHTLRL THYGALPDDA DNSLSMGVHT
     DFNFSTMVVQ HEVEGLEVQT KDGSWLAVRP EPGTVTFQAG EIFRVVTNGR VPACVHRVRT
     PSNRERFAVV FGCWYREGTE VSAMDELVDE DHPRMYNPCK PDEFVEFLYS EEGRKCDDDP
     LKAFCGVDVG RTMN
//
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