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Database: UniProt
Entry: M1WC42_CLAP2
LinkDB: M1WC42_CLAP2
Original site: M1WC42_CLAP2 
ID   M1WC42_CLAP2            Unreviewed;       372 AA.
AC   M1WC42;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2013, sequence version 1.
DT   27-MAR-2024, entry version 48.
DE   RecName: Full=protein disulfide-isomerase {ECO:0000256|ARBA:ARBA00012723};
DE            EC=5.3.4.1 {ECO:0000256|ARBA:ARBA00012723};
GN   ORFNames=CPUR_02306 {ECO:0000313|EMBL:CCE28619.1};
OS   Claviceps purpurea (strain 20.1) (Ergot fungus) (Sphacelia segetum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Clavicipitaceae; Claviceps.
OX   NCBI_TaxID=1111077 {ECO:0000313|EMBL:CCE28619.1, ECO:0000313|Proteomes:UP000016801};
RN   [1] {ECO:0000313|EMBL:CCE28619.1, ECO:0000313|Proteomes:UP000016801}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=20.1 {ECO:0000313|EMBL:CCE28619.1,
RC   ECO:0000313|Proteomes:UP000016801};
RX   PubMed=23468653; DOI=10.1371/journal.pgen.1003323;
RA   Schardl C.L., Young C.A., Hesse U., Amyotte S.G., Andreeva K., Calie P.J.,
RA   Fleetwood D.J., Haws D.C., Moore N., Oeser B., Panaccione D.G.,
RA   Schweri K.K., Voisey C.R., Farman M.L., Jaromczyk J.W., Roe B.A.,
RA   O'Sullivan D.M., Scott B., Tudzynski P., An Z., Arnaoudova E.G.,
RA   Bullock C.T., Charlton N.D., Chen L., Cox M., Dinkins R.D., Florea S.,
RA   Glenn A.E., Gordon A., Gueldener U., Harris D.R., Hollin W., Jaromczyk J.,
RA   Johnson R.D., Khan A.K., Leistner E., Leuchtmann A., Li C., Liu J., Liu J.,
RA   Liu M., Mace W., Machado C., Nagabhyru P., Pan J., Schmid J., Sugawara K.,
RA   Steiner U., Takach J.E., Tanaka E., Webb J.S., Wilson E.V., Wiseman J.L.,
RA   Yoshida R., Zeng Z.;
RT   "Plant-symbiotic fungi as chemical engineers: Multi-genome analysis of the
RT   Clavicipitaceae reveals dynamics of alkaloid loci.";
RL   PLoS Genet. 9:E1003323-E1003323(2013).
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};
CC   -!- SIMILARITY: Belongs to the protein disulfide isomerase family.
CC       {ECO:0000256|ARBA:ARBA00006347, ECO:0000256|RuleBase:RU004208}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:CCE28619.1}.
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DR   EMBL; CAGA01000009; CCE28619.1; -; Genomic_DNA.
DR   AlphaFoldDB; M1WC42; -.
DR   STRING; 1111077.M1WC42; -.
DR   VEuPathDB; FungiDB:CPUR_02306; -.
DR   eggNOG; KOG0191; Eukaryota.
DR   HOGENOM; CLU_038617_1_1_1; -.
DR   OrthoDB; 52245at2759; -.
DR   PhylomeDB; M1WC42; -.
DR   Proteomes; UP000016801; Unassembled WGS sequence.
DR   GO; GO:0005783; C:endoplasmic reticulum; IEA:InterPro.
DR   GO; GO:0003756; F:protein disulfide isomerase activity; IEA:InterPro.
DR   CDD; cd00238; ERp29c; 1.
DR   CDD; cd02998; PDI_a_ERp38; 2.
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; IPR005788; PDI_thioredoxin-like_dom.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   InterPro; IPR017937; Thioredoxin_CS.
DR   InterPro; IPR013766; Thioredoxin_domain.
DR   NCBIfam; TIGR01126; pdi_dom; 2.
DR   PANTHER; PTHR45672:SF11; PROTEIN DISULFIDE-ISOMERASE C17H9.14C; 1.
DR   PANTHER; PTHR45672; PROTEIN DISULFIDE-ISOMERASE C17H9.14C-RELATED; 1.
DR   Pfam; PF07749; ERp29; 1.
DR   Pfam; PF00085; Thioredoxin; 2.
DR   PRINTS; PR00421; THIOREDOXIN.
DR   SUPFAM; SSF47933; ERP29 C domain-like; 1.
DR   SUPFAM; SSF52833; Thioredoxin-like; 2.
DR   PROSITE; PS00194; THIOREDOXIN_1; 2.
DR   PROSITE; PS51352; THIOREDOXIN_2; 2.
PE   3: Inferred from homology;
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000313|EMBL:CCE28619.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000016801};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           19..372
FT                   /note="protein disulfide-isomerase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5005688770"
FT   DOMAIN          3..130
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
FT   DOMAIN          133..251
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
SQ   SEQUENCE   372 AA;  40206 MW;  7A4E481DC652CD9D CRC64;
     MVMLKSFVLA TLTAVAAAGS AVIDLTPANF DQVVLKSGKP TLVEFFAPWC GHCKTLAPVY
     EELASAFEHA KSKVQIAKVD ADAERALGKR FGVQGFPTLK YFDGKTDKPE DYKSGRDLES
     LSAFIAKKTG VKPKKQLEMP SEIVMLTDET FAETIGSDKN VLVAFTAPWC GHCKTLAPVF
     ESVALDFSGD KNVVIAKVDA EAANSKAVAK ENGVSSYPTI KWFPAGSKEG EAYSGERTEE
     SFLEFVNKKA GTHRVVGGGL DAIAGTIDAL DSLVARFTGG AKMEDIAAEV KKAAGEYSEE
     AKYQYAKYYV RVFDKLSASD NYAAKELARL EGILAQGGLA PSKRDEIHSK TNILRRFAQK
     AAEKAEELKD EL
//
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