(data stored in ACNUC8465 zone)

SWISSPROT: Q6FJD0_CANGA

ID   Q6FJD0_CANGA            Unreviewed;       149 AA.
AC   Q6FJD0;
DT   19-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   19-JUL-2004, sequence version 1.
DT   30-AUG-2017, entry version 98.
DE   RecName: Full=Glutaredoxin {ECO:0000256|PIRNR:PIRNR005894};
GN   OrderedLocusNames=CAGL0M07271g {ECO:0000313|CGD:CAL0136633,
GN   ECO:0000313|EMBL:CAG62640.1};
OS   Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 /
OS   NRRL Y-65) (Yeast) (Torulopsis glabrata).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC   Nakaseomyces/Candida clade.
OX   NCBI_TaxID=284593 {ECO:0000313|Proteomes:UP000002428};
RN   [1] {ECO:0000313|EMBL:CAG62640.1, ECO:0000313|Proteomes:UP000002428}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65
RC   {ECO:0000313|Proteomes:UP000002428};
RX   PubMed=15229592; DOI=10.1038/nature02579;
RG   Genolevures;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S.,
RA   Lafontaine I., de Montigny J., Marck C., Neuveglise C., Talla E.,
RA   Goffard N., Frangeul L., Aigle M., Anthouard V., Babour A., Barbe V.,
RA   Barnay S., Blanchin S., Beckerich J.M., Beyne E., Bleykasten C.,
RA   Boisrame A., Boyer J., Cattolico L., Confanioleri F., de Daruvar A.,
RA   Despons L., Fabre E., Fairhead C., Ferry-Dumazet H., Groppi A.,
RA   Hantraye F., Hennequin C., Jauniaux N., Joyet P., Kachouri R.,
RA   Kerrest A., Koszul R., Lemaire M., Lesur I., Ma L., Muller H.,
RA   Nicaud J.M., Nikolski M., Oztas S., Ozier-Kalogeropoulos O.,
RA   Pellenz S., Potier S., Richard G.F., Straub M.L., Suleau A.,
RA   Swennene D., Tekaia F., Wesolowski-Louvel M., Westhof E., Wirth B.,
RA   Zeniou-Meyer M., Zivanovic I., Bolotin-Fukuhara M., Thierry A.,
RA   Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J.,
RA   Wincker P., Souciet J.L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
CC   -!- SIMILARITY: Belongs to the glutaredoxin family. Monothiol
CC       subfamily. {ECO:0000256|PIRNR:PIRNR005894}.
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DR   EMBL; CR380959; CAG62640.1; -; Genomic_DNA.
DR   RefSeq; XP_449664.1; XM_449664.1.
DR   ProteinModelPortal; Q6FJD0; -.
DR   STRING; 284593.XP_449664.1; -.
DR   EnsemblFungi; CAG62640; CAG62640; CAGL0M07271g.
DR   KEGG; cgr:CAGL0M07271g; -.
DR   CGD; CAL0136633; CAGL0M07271g.
DR   EuPathDB; FungiDB:CAGL0M07271g; -.
DR   eggNOG; KOG0911; Eukaryota.
DR   eggNOG; COG0278; LUCA.
DR   HOGENOM; HOG000095211; -.
DR   InParanoid; Q6FJD0; -.
DR   KO; K07390; -.
DR   OMA; KGTKLMP; -.
DR   OrthoDB; EOG092C3TIP; -.
DR   Proteomes; UP000002428; Chromosome M.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:EnsemblFungi.
DR   GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0009055; F:electron carrier activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0015035; F:protein disulfide oxidoreductase activity; IEA:InterPro.
DR   GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro.
DR   GO; GO:0034599; P:cellular response to oxidative stress; IEA:EnsemblFungi.
DR   GO; GO:0016226; P:iron-sulfur cluster assembly; IEA:EnsemblFungi.
DR   GO; GO:0006970; P:response to osmotic stress; IEA:EnsemblFungi.
DR   CDD; cd03028; GRX_PICOT_like; 1.
DR   InterPro; IPR002109; Glutaredoxin.
DR   InterPro; IPR033658; GRX_PICOT-like.
DR   InterPro; IPR014434; Monothiol_GRX.
DR   InterPro; IPR004480; Monothiol_GRX-rel.
DR   InterPro; IPR012336; Thioredoxin-like_fold.
DR   PANTHER; PTHR10293; PTHR10293; 1.
DR   Pfam; PF00462; Glutaredoxin; 1.
DR   PIRSF; PIRSF005894; Monothiol_GRX; 1.
DR   SUPFAM; SSF52833; SSF52833; 1.
DR   TIGRFAMs; TIGR00365; TIGR00365; 1.
DR   PROSITE; PS51354; GLUTAREDOXIN_2; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q6FJD0.
DR   SWISS-2DPAGE; Q6FJD0.
KW   2Fe-2S {ECO:0000256|PIRSR:PIRSR005894-2};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002428};
KW   Iron {ECO:0000256|PIRSR:PIRSR005894-2};
KW   Iron-sulfur {ECO:0000256|PIRSR:PIRSR005894-2};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR005894-2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002428}.
FT   DOMAIN       35    140       Glutaredoxin. {ECO:0000259|PROSITE:
FT                                PS51354}.
FT   METAL        60     60       Iron-sulfur (2Fe-2S); shared with dimeric
FT                                partner. {ECO:0000256|PIRSR:PIRSR005894-
FT                                2}.
SQ   SEQUENCE   149 AA;  16335 MW;  FA4D36B0696B9A8C CRC64;
     MFATRLLGKS ALLGTTSTRM VFRSQMARYM STETKKAIEG AIASAPVVLF MKGTPEFPQC
     GFSRATISML GQQGVDPEKF AAYNVLEDPE LREGIKEFSN WPTIPQLYVN KEFIGGCDVI
     TSMARSGELA DVLEEANALV PEEKEEGTD
//

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