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Database: UniProt
Entry: Q59NQ2_CANAL
LinkDB: Q59NQ2_CANAL
Original site: Q59NQ2_CANAL 
ID   Q59NQ2_CANAL            Unreviewed;       229 AA.
AC   Q59NQ2;
DT   26-APR-2005, integrated into UniProtKB/TrEMBL.
DT   26-APR-2005, sequence version 1.
DT   27-MAR-2024, entry version 122.
DE   SubName: Full=Glutathione-disulfide reductase {ECO:0000313|EMBL:AOW29589.1};
GN   OrderedLocusNames=CAALFM_C501560CA {ECO:0000313|EMBL:AOW29589.1},
GN   orf19.11626 {ECO:0000313|CGD:CAL0000192543};
OS   Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX   NCBI_TaxID=237561 {ECO:0000313|EMBL:AOW29589.1, ECO:0000313|Proteomes:UP000000559};
RN   [1] {ECO:0000313|EMBL:AOW29589.1, ECO:0000313|Proteomes:UP000000559}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SC5314 / ATCC MYA-2876 {ECO:0000313|Proteomes:UP000000559};
RX   PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA   Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA   Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA   Scherer S.;
RT   "The diploid genome sequence of Candida albicans.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN   [2] {ECO:0000313|EMBL:AOW29589.1, ECO:0000313|Proteomes:UP000000559}
RP   GENOME REANNOTATION.
RC   STRAIN=SC5314 / ATCC MYA-2876 {ECO:0000313|Proteomes:UP000000559};
RX   PubMed=17419877; DOI=.1186/gb-2007-8-4-r52;
RA   van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA   Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA   Chibana H., Nantel A., Magee P.T.;
RT   "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT   on the eight chromosomes.";
RL   Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN   [3] {ECO:0000313|EMBL:AOW29589.1, ECO:0000313|Proteomes:UP000000559}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SC5314 / ATCC MYA-2876 {ECO:0000313|Proteomes:UP000000559};
RX   PubMed=24025428; DOI=.1186/gb-2013-14-9-r97;
RA   Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT   "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT   specific measurements and provides a simple model for repeat and indel
RT   structure.";
RL   Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
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DR   EMBL; CP017627; AOW29589.1; -; Genomic_DNA.
DR   RefSeq; XP_711354.1; XM_706262.2.
DR   AlphaFoldDB; Q59NQ2; -.
DR   SMR; Q59NQ2; -.
DR   STRING; 237561.Q59NQ2; -.
DR   EnsemblFungi; C5_01560C_A-T; C5_01560C_A-T-p1; C5_01560C_A.
DR   GeneID; 3647064; -.
DR   KEGG; cal:CAALFM_C501560CA; -.
DR   CGD; CAL0000192543; orf19.11626.
DR   VEuPathDB; FungiDB:C5_01560C_A; -.
DR   eggNOG; KOG1752; Eukaryota.
DR   HOGENOM; CLU_026126_0_1_1; -.
DR   InParanoid; Q59NQ2; -.
DR   OMA; VAQNANF; -.
DR   OrthoDB; 1333222at2759; -.
DR   Proteomes; UP000000559; Chromosome 5.
DR   GO; GO:0005801; C:cis-Golgi network; IBA:GO_Central.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0000324; C:fungal-type vacuole; IBA:GO_Central.
DR   GO; GO:0005796; C:Golgi lumen; IBA:GO_Central.
DR   GO; GO:0015038; F:glutathione disulfide oxidoreductase activity; IBA:GO_Central.
DR   GO; GO:0034599; P:cellular response to oxidative stress; IBA:GO_Central.
DR   CDD; cd03419; GRX_GRXh_1_2_like; 1.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 1.
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:SF30; GLUTAREDOXIN 2; 1.
DR   Pfam; PF00462; Glutaredoxin; 1.
DR   PRINTS; PR00160; GLUTAREDOXIN.
DR   SUPFAM; SSF52833; Thioredoxin-like; 1.
DR   PROSITE; PS51354; GLUTAREDOXIN_2; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000000559};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..30
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           31..229
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5009971193"
FT   DOMAIN          125..187
FT                   /note="Glutaredoxin"
FT                   /evidence="ECO:0000259|Pfam:PF00462"
FT   REGION          37..106
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        37..68
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        90..106
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   229 AA;  25489 MW;  EBF522577F7152C4 CRC64;
     MAGVRQLRII ALTAFVLGLI FTLHKVGSNA ASLVHAQASD QQPNKHNTKS TTYTATNDES
     VANLIDSKND PQTDDKINQK ISQDQDEAIN GNKDTNKDTT KVKPDNGEYD PISDLIKIRS
     LSPMTIFSKS YCPYSKKIKQ LLLEKYDITP APNVVELDRY EYGAELQSYL TEKSGRRTVP
     NVLVGKSFES RGGCDEFEKL HKDNDLIKLL VEWGSGRLQV AKKNTPSNA
//
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