ID B2W830_PYRTR Unreviewed; 363 AA.
AC B2W830;
DT 01-JUL-2008, integrated into UniProtKB/TrEMBL.
DT 01-JUL-2008, sequence version 1.
DT 27-MAR-2024, entry version 79.
DE RecName: Full=protein disulfide-isomerase {ECO:0000256|ARBA:ARBA00012723};
DE EC=5.3.4.1 {ECO:0000256|ARBA:ARBA00012723};
GN ORFNames=PTRG_05968 {ECO:0000313|EMBL:EDU48888.1};
OS Pyrenophora tritici-repentis (strain Pt-1C-BFP) (Wheat tan spot fungus)
OS (Drechslera tritici-repentis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae;
OC Pyrenophora.
OX NCBI_TaxID=426418 {ECO:0000313|EMBL:EDU48888.1, ECO:0000313|Proteomes:UP000001471};
RN [1] {ECO:0000313|Proteomes:UP000001471}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Pt-1C-BFP {ECO:0000313|Proteomes:UP000001471};
RX PubMed=23316438; DOI=10.1534/g3.112.004044;
RA Manning V.A., Pandelova I., Dhillon B., Wilhelm L.J., Goodwin S.B.,
RA Berlin A.M., Figueroa M., Freitag M., Hane J.K., Henrissat B., Holman W.H.,
RA Kodira C.D., Martin J., Oliver R.P., Robbertse B., Schackwitz W.,
RA Schwartz D.C., Spatafora J.W., Turgeon B.G., Yandava C., Young S., Zhou S.,
RA Zeng Q., Grigoriev I.V., Ma L.-J., Ciuffetti L.M.;
RT "Comparative genomics of a plant-pathogenic fungus, Pyrenophora tritici-
RT repentis, reveals transduplication and the impact of repeat elements on
RT pathogenicity and population divergence.";
RL G3 (Bethesda) 3:41-63(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}.
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DR EMBL; DS231619; EDU48888.1; -; Genomic_DNA.
DR RefSeq; XP_001936301.1; XM_001936266.1.
DR AlphaFoldDB; B2W830; -.
DR STRING; 426418.B2W830; -.
DR EnsemblFungi; EDU48888; EDU48888; PTRG_05968.
DR GeneID; 6344223; -.
DR eggNOG; KOG0191; Eukaryota.
DR HOGENOM; CLU_038617_1_1_1; -.
DR InParanoid; B2W830; -.
DR OMA; WEDLANT; -.
DR OrthoDB; 52245at2759; -.
DR Proteomes; UP000001471; 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:EDU48888.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001471};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..363
FT /note="protein disulfide-isomerase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002784594"
FT DOMAIN 8..131
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT DOMAIN 134..252
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
SQ SEQUENCE 363 AA; 39458 MW; 317675BBD13FF08B CRC64;
MLFRNLIPAA IALLPALAAA SSVIDLEPSN FDKVVLKSGK PALVEFFAPW CGHCKNLAPV
WEELATVFQH AGDKVTVAKV DADNHKSLGK RFGVSGFPTL KWFDGKSDKP TDYTGGRDLE
SLSKFIQEKT SIKPKVKGKL PSQVVYLDDK TFKEKVGKDQ NVLVAFTAPW CGHCKTLAPV
WETLANDFVN EPSVLIAKVD AEAENAKALA TEQGVSSYPT IKYFPKGSTE PLPYEGARDE
KAFIDFLNTN AGTHRAVGGS LDATGGTIEA FNSIISKFQG KWADGATEAK TLAGTLQDKY
AEYYVKVFNK IGANSGYAAK ELKRLQGLIA KGNLAPEKMD DLVSRSNILS KFIADDSEEK
NEL
//
