ID I1R4N4_ORYGL Unreviewed; 172 AA.
AC I1R4N4;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE RecName: Full=Thioredoxin domain-containing protein {ECO:0000259|PROSITE:PS51352};
OS Oryza glaberrima (African rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX NCBI_TaxID=4538 {ECO:0000313|EnsemblPlants:ORGLA12G0049000.1, ECO:0000313|Proteomes:UP000007306};
RN [1] {ECO:0000313|Proteomes:UP000007306}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IRGC 96717 {ECO:0000313|Proteomes:UP000007306};
RA Wing R.A., Yu Y., Rounsley S., Reddy-Marri P., Goicoechea J.L.,
RA Sisneros N., Lee S., Song X., Angelova A., Kudrna D.P., de Baynast K.,
RA Zuccolo A.;
RT "The complete genome of Oryza glaberrima.";
RL Submitted (JUN-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblPlants:ORGLA12G0049000.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (JUN-2015) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000256|ARBA:ARBA00004229}.
CC -!- SIMILARITY: Belongs to the thioredoxin family. Plant M-type subfamily.
CC {ECO:0000256|ARBA:ARBA00038056}.
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DR AlphaFoldDB; I1R4N4; -.
DR STRING; 4538.I1R4N4; -.
DR EnsemblPlants; ORGLA12G0049000.1; ORGLA12G0049000.1; ORGLA12G0049000.
DR Gramene; ORGLA12G0049000.1; ORGLA12G0049000.1; ORGLA12G0049000.
DR eggNOG; KOG0910; Eukaryota.
DR HOGENOM; CLU_090389_0_2_1; -.
DR OMA; CSIGAKS; -.
DR Proteomes; UP000007306; Unassembled WGS sequence.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0015035; F:protein-disulfide reductase activity; IEA:EnsemblPlants.
DR GO; GO:0042744; P:hydrogen peroxide catabolic process; IEA:EnsemblPlants.
DR GO; GO:0009657; P:plastid organization; IEA:EnsemblPlants.
DR CDD; cd02947; TRX_family; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR InterPro; IPR005746; Thioredoxin.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR017937; Thioredoxin_CS.
DR InterPro; IPR013766; Thioredoxin_domain.
DR NCBIfam; TIGR01068; thioredoxin; 1.
DR PANTHER; PTHR45663; GEO12009P1; 1.
DR PANTHER; PTHR45663:SF42; THIOREDOXIN M5, CHLOROPLASTIC; 1.
DR Pfam; PF00085; Thioredoxin; 1.
DR PRINTS; PR00421; THIOREDOXIN.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
DR PROSITE; PS00194; THIOREDOXIN_1; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Electron transport {ECO:0000256|ARBA:ARBA00022982};
KW Redox-active center {ECO:0000256|ARBA:ARBA00023284};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 47..171
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT REGION 17..44
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 30..44
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 172 AA; 18532 MW; 5996783BB6E01B12 CRC64;
MALETCFRAW ATLHAPQPPS SGGSRDRLLL SGAGSSQSKP RLSVASPSQL RPASRFACQC
SNAVDEVVVA DEKNWDSMVL GSEAPVLVEF WAPWCGPCRM IAPVIDELAK EYVGKIKCCK
VNTDDSPNIA TNYGIRSIPT VLMFKNGEKK ESVIGAVPKT TLATIIDKYV SS
//