ID C4Y7P8_CLAL4 Unreviewed; 385 AA.
AC C4Y7P8;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE RecName: Full=protein disulfide-isomerase {ECO:0000256|ARBA:ARBA00012723};
DE EC=5.3.4.1 {ECO:0000256|ARBA:ARBA00012723};
GN ORFNames=CLUG_04226 {ECO:0000313|EMBL:EEQ40098.1};
OS Clavispora lusitaniae (strain ATCC 42720) (Yeast) (Candida lusitaniae).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Metschnikowiaceae; Clavispora.
OX NCBI_TaxID=306902 {ECO:0000313|EMBL:EEQ40098.1, ECO:0000313|Proteomes:UP000007703};
RN [1] {ECO:0000313|EMBL:EEQ40098.1, ECO:0000313|Proteomes:UP000007703}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 42720 {ECO:0000313|EMBL:EEQ40098.1,
RC ECO:0000313|Proteomes:UP000007703};
RX PubMed=19465905; DOI=10.1038/nature08064;
RA Butler G., Rasmussen M.D., Lin M.F., Santos M.A., Sakthikumar S.,
RA Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA Arnaud M.B., Bates S., Brown A.J., Brunke S., Costanzo M.C.,
RA Fitzpatrick D.A., de Groot P.W., Harris D., Hoyer L.L., Hube B., Klis F.M.,
RA Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M., Nikolaou E.,
RA Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F., Sherlock G.,
RA Shah P., Silverstein K.A., Skrzypek M.S., Soll D., Staggs R.,
RA Stansfield I., Stumpf M.P., Sudbery P.E., Srikantha T., Zeng Q., Berman J.,
RA Berriman M., Heitman J., Gow N.A., Lorenz M.C., Birren B.W., Kellis M.,
RA Cuomo C.A.;
RT "Evolution of pathogenicity and sexual reproduction in eight Candida
RT genomes.";
RL Nature 459:657-662(2009).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Catalyzes the rearrangement of -S-S- bonds in proteins.;
CC EC=5.3.4.1; Evidence={ECO:0000256|ARBA:ARBA00001182};
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DR EMBL; CH408080; EEQ40098.1; -; Genomic_DNA.
DR RefSeq; XP_002615344.1; XM_002615298.1.
DR AlphaFoldDB; C4Y7P8; -.
DR STRING; 306902.C4Y7P8; -.
DR GeneID; 8496354; -.
DR KEGG; clu:CLUG_04226; -.
DR VEuPathDB; FungiDB:CLUG_04226; -.
DR HOGENOM; CLU_038617_1_1_1; -.
DR InParanoid; C4Y7P8; -.
DR OMA; WEDLANT; -.
DR OrthoDB; 52245at2759; -.
DR Proteomes; UP000007703; Unassembled WGS sequence.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:InterPro.
DR GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
DR CDD; cd02961; PDI_a_family; 1.
DR Gene3D; 1.20.1150.12; Endoplasmic reticulum resident protein 29, C-terminal domain; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 2.
DR InterPro; IPR011679; ERp29_C.
DR InterPro; IPR036356; ERp29_C_sf.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR013766; Thioredoxin_domain.
DR PANTHER; PTHR45672; PROTEIN DISULFIDE-ISOMERASE C17H9.14C-RELATED; 1.
DR PANTHER; PTHR45672:SF3; THIOREDOXIN DOMAIN-CONTAINING PROTEIN 5; 1.
DR Pfam; PF07749; ERp29; 1.
DR Pfam; PF00085; Thioredoxin; 2.
DR SUPFAM; SSF47933; ERP29 C domain-like; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 2.
DR PROSITE; PS51352; THIOREDOXIN_2; 2.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235};
KW Reference proteome {ECO:0000313|Proteomes:UP000007703}.
FT DOMAIN 8..124
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT DOMAIN 126..261
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
SQ SEQUENCE 385 AA; 44035 MW; BC3D777AB85485E2 CRC64;
MNILFLLFAL GVFASELVRI NDKNFKEVAV ESGKWTLVDF YADWCRHCSN LMPTIEQLAE
VYKDEPDIQI VKLNGDEDGK KTTRKYNVPG FPTLLMFHGS DDPIEYEGMR DLDAISNFVQ
SVSGIRLGAK PAPEVVEPTN ILSLNDDNFQ DTVLRANHKT VVAVTAPWCR FCKELEPIFN
KLANEIYIHD GEVVQFGKVD LSDENKQKCE MITKQFGVEK LPTIFLFDPS RVDKDGLRRP
VIFNDDRDLE SLIAFVNDET GLCRNEEGRL HSNAGRIMAI DQALKTKSPE AILEELETLE
EEVKIYGRDA LVNDDVLFFK DDVSMIPYYK KLLKKIQEGD REFFSREFAR LERLLATEEK
NIEKGAYDHM QKRASVLQSF LSAKA
//
