ID Q6FSC0_CANGA Unreviewed; 533 AA.
AC Q6FSC0;
DT 19-JUL-2004, integrated into UniProtKB/TrEMBL.
DT 19-JUL-2004, sequence version 1.
DT 27-MAR-2024, entry version 113.
DE RecName: Full=protein disulfide-isomerase {ECO:0000256|ARBA:ARBA00012723};
DE EC=5.3.4.1 {ECO:0000256|ARBA:ARBA00012723};
GN Name=EUG1 {ECO:0000313|CGD:CAL0131586};
GN OrderedLocusNames=CAGL0H01727g {ECO:0000313|CGD:CAL0131586,
GN ECO:0000313|EMBL:CAG59807.1};
OS Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 /
OS NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Nakaseomyces.
OX NCBI_TaxID=284593 {ECO:0000313|EMBL:CAG59807.1, ECO:0000313|Proteomes:UP000002428};
RN [1] {ECO:0000313|EMBL:CAG59807.1, 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., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.F., Straub M.L.,
RA Suleau A., Swennene D., Tekaia F., Wesolowski-Louvel M., Westhof E.,
RA Wirth B., 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 protein disulfide isomerase family.
CC {ECO:0000256|ARBA:ARBA00006347}.
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DR EMBL; CR380954; CAG59807.1; -; Genomic_DNA.
DR RefSeq; XP_446874.1; XM_446874.1.
DR AlphaFoldDB; Q6FSC0; -.
DR STRING; 284593.Q6FSC0; -.
DR EnsemblFungi; CAGL0H01727g-T; CAGL0H01727g-T-p1; CAGL0H01727g.
DR GeneID; 2888494; -.
DR KEGG; cgr:CAGL0H01727g; -.
DR CGD; CAL0131586; EUG1.
DR VEuPathDB; FungiDB:CAGL0H01727g; -.
DR eggNOG; KOG0190; Eukaryota.
DR HOGENOM; CLU_025879_5_0_1; -.
DR InParanoid; Q6FSC0; -.
DR OMA; FRSKHEP; -.
DR Proteomes; UP000002428; Chromosome H.
DR GO; GO:0003756; F:protein disulfide isomerase activity; IEA:EnsemblFungi.
DR GO; GO:0019153; F:protein-disulfide reductase (glutathione) activity; IEA:EnsemblFungi.
DR GO; GO:0051082; F:unfolded protein binding; IEA:EnsemblFungi.
DR GO; GO:0006457; P:protein folding; IEA:EnsemblFungi.
DR CDD; cd02961; PDI_a_family; 1.
DR CDD; cd02995; PDI_a_PDI_a'_C; 1.
DR CDD; cd02982; PDI_b'_family; 1.
DR CDD; cd02981; PDI_b_family; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 3.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR013766; Thioredoxin_domain.
DR PANTHER; PTHR18929; PROTEIN DISULFIDE ISOMERASE; 1.
DR PANTHER; PTHR18929:SF132; PROTEIN DISULFIDE-ISOMERASE A3; 1.
DR Pfam; PF00085; Thioredoxin; 2.
DR Pfam; PF13848; Thioredoxin_6; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 2.
DR PROSITE; PS51352; THIOREDOXIN_2; 2.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Reference proteome {ECO:0000313|Proteomes:UP000002428};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..16
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 17..533
FT /note="protein disulfide-isomerase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004274167"
FT DOMAIN 13..136
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT DOMAIN 345..479
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT COILED 485..528
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 533 AA; 59991 MW; 08727D1813E2F4B2 CRC64;
MVSVKSLALA IGVASAIQLP DAIAPDSSNI IKANISQFAT HVKENPIVMV EFFTPWCTHS
KMLQPRLSEA ATIVKGVKIP ILQVDCTQYG VLCDQQMIDF YPTLKVYKNH RLVGAENYKG
SQAGNEIANY LLNLKNNPVT NITSAQEVEK MKSETDMPIV HNRGNLEIDE ILRSVALDMS
EKFAFIRDTV ASENGTLEMY FPGTNRTAVY DGPQPPTEES ISIWMHMENL PFFADIEAAD
FKNYMATKLP IAYFYYSTPQ ELNDFTGLFN ELGEKYRGKL NFVGMNPHKF QEHLKLLNLK
QRFPLFVIHN VNNNLKYTLD QFTDESDKVM KKLESEDIKK LVEDFVEGKA QPIIKSEPIP
KTQDSVLYKL VAKTHNDFVY NNDKDVFVKY YAPWCQHSKA FRPVLEEIAE LFGSNPETKE
KIVFAEVDST ANDIIDFPVA GYPTLVLYRA GSKPGSQPII FEGKRSLENV LDFIKSHSTS
NLDGQALLEK QKQDEAKAIE DAQAAEAAEA VNAQAQAANA DQKAFNNEIK DEL
//
