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Database: UniProt
Entry: A8Y1E0_CAEBR
LinkDB: A8Y1E0_CAEBR
Original site: A8Y1E0_CAEBR 
ID   A8Y1E0_CAEBR            Unreviewed;       105 AA.
AC   A8Y1E0;
DT   15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT   15-JAN-2008, sequence version 1.
DT   27-MAR-2024, entry version 89.
DE   RecName: Full=Glutaredoxin-1 {ECO:0000256|ARBA:ARBA00013662};
GN   Name=glrx-10 {ECO:0000313|WormBase:CBG22036};
GN   Synonyms=Cbr-glrx-10 {ECO:0000313|EMBL:CAP38709.1};
GN   ORFNames=CBG22036 {ECO:0000313|WormBase:CBG22036}, CBG_22036
GN   {ECO:0000313|EMBL:CAP38709.1};
OS   Caenorhabditis briggsae.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6238 {ECO:0000313|EMBL:CAP38709.1, ECO:0000313|Proteomes:UP000008549};
RN   [1] {ECO:0000313|EMBL:CAP38709.1, ECO:0000313|Proteomes:UP000008549}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AF16 {ECO:0000313|EMBL:CAP38709.1,
RC   ECO:0000313|Proteomes:UP000008549};
RX   PubMed=14624247; DOI=10.1371/journal.pbio.0000045;
RA   Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N.,
RA   Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P.,
RA   Fitch D.H., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W.,
RA   Hillier L.W., Kamath R., Kuwabara P.E., Mardis E.R., Marra M.A.,
RA   Miner T.L., Minx P., Mullikin J.C., Plumb R.W., Rogers J., Schein J.E.,
RA   Sohrmann M., Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K.,
RA   Durbin R., Waterston R.H.;
RT   "The genome sequence of Caenorhabditis briggsae: a platform for comparative
RT   genomics.";
RL   PLoS Biol. 1:166-192(2003).
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.
CC       {ECO:0000256|ARBA:ARBA00007787}.
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DR   EMBL; HE601428; CAP38709.1; -; Genomic_DNA.
DR   RefSeq; XP_002638831.1; XM_002638785.1.
DR   AlphaFoldDB; A8Y1E0; -.
DR   STRING; 6238.A8Y1E0; -.
DR   EnsemblMetazoa; CBG22036.1; CBG22036.1; WBGene00040679.
DR   GeneID; 8580826; -.
DR   KEGG; cbr:CBG_22036; -.
DR   CTD; 8580826; -.
DR   WormBase; CBG22036; CBP12076; WBGene00040679; Cbr-glrx-10.
DR   eggNOG; KOG1752; Eukaryota.
DR   HOGENOM; CLU_026126_7_2_1; -.
DR   InParanoid; A8Y1E0; -.
DR   OMA; YCHKARA; -.
DR   OrthoDB; 203654at2759; -.
DR   Proteomes; UP000008549; Unassembled WGS sequence.
DR   GO; GO:0015038; F:glutathione disulfide oxidoreductase activity; IBA:GO_Central.
DR   CDD; cd03419; GRX_GRXh_1_2_like; 1.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR   InterPro; IPR011767; GLR_AS.
DR   InterPro; IPR047185; GLRX1.
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; PTHR46185; GLUTAREDOXIN-1; 1.
DR   PANTHER; PTHR46185:SF1; GLUTAREDOXIN-1; 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   Redox-active center {ECO:0000256|ARBA:ARBA00023284};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008549};
KW   Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   DOMAIN          15..79
FT                   /note="Glutaredoxin"
FT                   /evidence="ECO:0000259|Pfam:PF00462"
SQ   SEQUENCE   105 AA;  11361 MW;  DF5D8C5202F721B9 CRC64;
     MSKAFVDGLL QSHKVVVFSK SYCPYCHKAR AALDSVNVKP DALQWIEIDD RKDCDEIQNY
     LGSLTGARSV PRVFINGKFF GGGDDTAAAA KNGKLAKLLQ EAGAI
//
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