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Database: UniProt
Entry: R7QGT1_CHOCR
LinkDB: R7QGT1_CHOCR
Original site: R7QGT1_CHOCR 
ID   R7QGT1_CHOCR            Unreviewed;       157 AA.
AC   R7QGT1;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   27-MAR-2024, entry version 46.
DE   RecName: Full=Thioredoxin domain-containing protein {ECO:0000259|Pfam:PF00085};
GN   ORFNames=CHC_T00005936001 {ECO:0000313|EMBL:CDF37727.1};
OS   Chondrus crispus (Carrageen Irish moss) (Polymorpha crispa).
OC   Eukaryota; Rhodophyta; Florideophyceae; Rhodymeniophycidae; Gigartinales;
OC   Gigartinaceae; Chondrus.
OX   NCBI_TaxID=2769 {ECO:0000313|EMBL:CDF37727.1, ECO:0000313|Proteomes:UP000012073};
RN   [1] {ECO:0000313|Proteomes:UP000012073}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Stackhouse {ECO:0000313|Proteomes:UP000012073};
RX   PubMed=23503846; DOI=10.1073/pnas.1221259110;
RA   Collen J., Porcel B., Carre W., Ball S.G., Chaparro C., Tonon T.,
RA   Barbeyron T., Michel G., Noel B., Valentin K., Elias M., Artiguenave F.,
RA   Arun A., Aury J.M., Barbosa-Neto J.F., Bothwell J.H., Bouget F.Y.,
RA   Brillet L., Cabello-Hurtado F., Capella-Gutierrez S., Charrier B.,
RA   Cladiere L., Cock J.M., Coelho S.M., Colleoni C., Czjzek M., Da Silva C.,
RA   Delage L., Denoeud F., Deschamps P., Dittami S.M., Gabaldon T.,
RA   Gachon C.M., Groisillier A., Herve C., Jabbari K., Katinka M., Kloareg B.,
RA   Kowalczyk N., Labadie K., Leblanc C., Lopez P.J., McLachlan D.H.,
RA   Meslet-Cladiere L., Moustafa A., Nehr Z., Nyvall Collen P., Panaud O.,
RA   Partensky F., Poulain J., Rensing S.A., Rousvoal S., Samson G.,
RA   Symeonidi A., Weissenbach J., Zambounis A., Wincker P., Boyen C.;
RT   "Genome structure and metabolic features in the red seaweed Chondrus
RT   crispus shed light on evolution of the Archaeplastida.";
RL   Proc. Natl. Acad. Sci. U.S.A. 110:5247-5252(2013).
CC   -!- FUNCTION: Participates in various redox reactions through the
CC       reversible oxidation of its active center dithiol to a disulfide and
CC       catalyzes dithiol-disulfide exchange reactions.
CC       {ECO:0000256|ARBA:ARBA00003318}.
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DR   EMBL; HG001864; CDF37727.1; -; Genomic_DNA.
DR   RefSeq; XP_005717598.1; XM_005717541.1.
DR   AlphaFoldDB; R7QGT1; -.
DR   STRING; 2769.R7QGT1; -.
DR   EnsemblPlants; CDF37727; CDF37727; CHC_T00005936001.
DR   GeneID; 17325311; -.
DR   Gramene; CDF37727; CDF37727; CHC_T00005936001.
DR   KEGG; ccp:CHC_T00005936001; -.
DR   OMA; DADECPE; -.
DR   OrthoDB; 45858at2759; -.
DR   PhylomeDB; R7QGT1; -.
DR   Proteomes; UP000012073; Unassembled WGS sequence.
DR   CDD; cd02947; TRX_family; 1.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 2.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   InterPro; IPR017937; Thioredoxin_CS.
DR   InterPro; IPR013766; Thioredoxin_domain.
DR   PANTHER; PTHR46115:SF5; THIOREDOXIN DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR46115; THIOREDOXIN-LIKE PROTEIN 1; 1.
DR   Pfam; PF00085; Thioredoxin; 2.
DR   PRINTS; PR00421; THIOREDOXIN.
DR   SUPFAM; SSF52833; Thioredoxin-like; 1.
DR   PROSITE; PS00194; THIOREDOXIN_1; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000012073}.
FT   DOMAIN          7..49
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|Pfam:PF00085"
FT   DOMAIN          94..141
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|Pfam:PF00085"
FT   REGION          51..89
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   157 AA;  17079 MW;  496E38C038B281BF CRC64;
     MVYQLKAADE FDSILEKNHV VVADFFAEWC GPCRAIAPKV ESMEKDYTEL PAENSTTAPV
     TNLETGDAGV PPPDTLQPPA NSEVLTAEAT VSSPKKEKIK FVKVDVDSLS ELSARMDVTA
     MPTFLIFVNG RLHKTIIGAN APLLKNSVQD ALVEYVK
//
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