ID   A0A2N1J9Q2_9BASI        Unreviewed;       497 AA.
AC   A0A2N1J9Q2;
DT   25-APR-2018, integrated into UniProtKB/TrEMBL.
DT   25-APR-2018, sequence version 1.
DT   13-SEP-2023, entry version 17.
DE   RecName: Full=protein disulfide-isomerase {ECO:0000256|ARBA:ARBA00012723};
DE            EC=5.3.4.1 {ECO:0000256|ARBA:ARBA00012723};
GN   Name=PDI1 {ECO:0000313|EMBL:PKI83283.1};
GN   ORFNames=MVES_003049 {ECO:0000313|EMBL:PKI83283.1};
OS   Malassezia vespertilionis.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC   Malasseziomycetes; Malasseziales; Malasseziaceae; Malassezia.
OX   NCBI_TaxID=2020962 {ECO:0000313|EMBL:PKI83283.1, ECO:0000313|Proteomes:UP000232875};
RN   [1] {ECO:0000313|EMBL:PKI83283.1, ECO:0000313|Proteomes:UP000232875}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NWHC:44797-103 {ECO:0000313|EMBL:PKI83283.1,
RC   ECO:0000313|Proteomes:UP000232875};
RA   Lorch J.M., Palmer J.M., Vanderwolf K.J., Schmidt K.Z., Verant M.L.,
RA   Weller T.J., Blehert D.S.;
RT   "A novel species of cold-tolerant Malassezia isolated from bats.";
RL   Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
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   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen
CC       {ECO:0000256|ARBA:ARBA00004319}.
CC   -!- SIMILARITY: Belongs to the protein disulfide isomerase family.
CC       {ECO:0000256|ARBA:ARBA00006347}.
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DR   EMBL; KZ454992; PKI83283.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2N1J9Q2; -.
DR   STRING; 2020962.A0A2N1J9Q2; -.
DR   OrthoDB; 5399045at2759; -.
DR   Proteomes; UP000232875; Unassembled WGS sequence.
DR   GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
DR   GO; GO:0003756; F:protein disulfide isomerase activity; IEA:UniProtKB-EC.
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; 4.
DR   InterPro; IPR005792; Prot_disulphide_isomerase.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   InterPro; IPR017937; Thioredoxin_CS.
DR   InterPro; IPR013766; Thioredoxin_domain.
DR   NCBIfam; TIGR01130; ER_PDI_fam; 1.
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   PRINTS; PR00421; THIOREDOXIN.
DR   SUPFAM; SSF52833; Thioredoxin-like; 4.
DR   PROSITE; PS00194; THIOREDOXIN_1; 1.
DR   PROSITE; PS51352; THIOREDOXIN_2; 2.
PE   3: Inferred from homology;
KW   Disulfide bond {ECO:0000256|PIRSR:PIRSR605792-51};
KW   Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW   Isomerase {ECO:0000256|ARBA:ARBA00023235};
KW   Redox-active center {ECO:0000256|ARBA:ARBA00023284,
KW   ECO:0000256|PIRSR:PIRSR605792-51};
KW   Reference proteome {ECO:0000313|Proteomes:UP000232875};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           21..497
FT                   /note="protein disulfide-isomerase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5014638380"
FT   DOMAIN          4..129
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
FT   DOMAIN          341..476
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
FT   DISULFID        53..56
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR605792-51"
FT   DISULFID        390..393
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR605792-51"
SQ   SEQUENCE   497 AA;  54534 MW;  B36C15638E22B537 CRC64;
     MRFLVGILFA AVFAVLSVHA EEKSDVVDLD KTTFAKFTAE EPLALIEFFA PWCGHCQALA
     PHYEEAATEL LPQNIKLAKV DCTKEEALCS ELEISGFPTL KVFRHGNAAA YGGPRKKDGI
     VSYMRKQQLP AVSSISAAGL DEFRAKDRFV VVAFVDEGDK ASMDAINQLA EKHRETYVVG
     VSHDKDLAAK HNASLPGLVA FRTFDEPEVS LDVKSKSLNI AEMEAFVNVQ SVSLMDEVNP
     DNFARYIQSG LPLAYYFVSA DTPTHAEDVK KLTEVAKEFR DKVNLVWIDA IKFGGHAKAL
     NLKGDSWPAL AIQDMESGAK YPLTDLDKDV KSSVHDFISK FVSGKLKPSI KSAPVPSQNS
     TVVEVVADVF DKYVFDDAKD VLLEVYAPWC GFCKHLAPTY QKLADLYAAH PQGSSQVSIV
     KMDGTENDIP PHADITLTAF PTILLKPAGK GKKDMVTYEG DRTLESLIDF IAKHGTHKVS
     VEPSDPVAGA EQRHDEL
//