ID A0A2P6Q5C5_ROSCH Unreviewed; 112 AA.
AC A0A2P6Q5C5;
DT 23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT 23-MAY-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Putative thioredoxin-disulfide reductase {ECO:0000313|EMBL:PRQ29376.1};
DE EC=1.8.1.9 {ECO:0000313|EMBL:PRQ29376.1};
GN ORFNames=RchiOBHm_Chr5g0013221 {ECO:0000313|EMBL:PRQ29376.1};
OS Rosa chinensis (China rose).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Rosales; Rosaceae; Rosoideae; Rosoideae incertae sedis;
OC Rosa.
OX NCBI_TaxID=74649 {ECO:0000313|EMBL:PRQ29376.1, ECO:0000313|Proteomes:UP000238479};
RN [1] {ECO:0000313|EMBL:PRQ29376.1, ECO:0000313|Proteomes:UP000238479}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Old Blush {ECO:0000313|Proteomes:UP000238479};
RA Bendahmane M.;
RT "The Rosa genome provides new insights in the design of modern roses.";
RL Nat. Genet. 0:0-0(2018).
CC -!- FUNCTION: Has a glutathione-disulfide oxidoreductase activity in the
CC presence of NADPH and glutathione reductase. Reduces low molecular
CC weight disulfides and proteins. {ECO:0000256|ARBA:ARBA00002549}.
CC -!- SIMILARITY: Belongs to the glutaredoxin family. CPYC subfamily.
CC {ECO:0000256|ARBA:ARBA00007190}.
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:PRQ29376.1}.
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DR EMBL; PDCK01000043; PRQ29376.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2P6Q5C5; -.
DR STRING; 74649.A0A2P6Q5C5; -.
DR EnsemblPlants; PRQ29376; PRQ29376; RchiOBHm_Chr5g0013221.
DR Gramene; PRQ29376; PRQ29376; RchiOBHm_Chr5g0013221.
DR OMA; KPGHLEC; -.
DR OrthoDB; 903at2759; -.
DR Proteomes; UP000238479; Chromosome 5.
DR GO; GO:0004791; F:thioredoxin-disulfide reductase (NADP) activity; IEA:UniProtKB-EC.
DR CDD; cd03419; GRX_GRXh_1_2_like; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR InterPro; IPR011767; GLR_AS.
DR InterPro; IPR002109; Glutaredoxin.
DR InterPro; IPR011899; Glutaredoxin_euk/vir.
DR InterPro; IPR014025; Glutaredoxin_subgr.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR NCBIfam; TIGR02180; GRX_euk; 1.
DR PANTHER; PTHR45694; GLUTAREDOXIN 2; 1.
DR PANTHER; PTHR45694:SF14; GLUTAREDOXIN-C2; 1.
DR Pfam; PF00462; Glutaredoxin; 1.
DR PRINTS; PR00160; GLUTAREDOXIN.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
DR PROSITE; PS00195; GLUTAREDOXIN_1; 1.
DR PROSITE; PS51354; GLUTAREDOXIN_2; 1.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Electron transport {ECO:0000256|ARBA:ARBA00022982};
KW Oxidoreductase {ECO:0000313|EMBL:PRQ29376.1};
KW Redox-active center {ECO:0000256|ARBA:ARBA00023284};
KW Reference proteome {ECO:0000313|Proteomes:UP000238479};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 15..78
FT /note="Glutaredoxin"
FT /evidence="ECO:0000259|Pfam:PF00462"
SQ SEQUENCE 112 AA; 12225 MW; 6BD006381B6729BB CRC64;
MALGKVKELV SSNPVVIFSN KLCPYCVCVK QLFVLKLEVQ YKAIELDQES DGSEIQSALA
EWTGQHTLPN VFVGGNHIGD CDTTWDLHKE GKLVPLLTGA GVVAKLQELE IS
//
