ID   A0A0G4F631_VITBC        Unreviewed;       549 AA.
AC   A0A0G4F631;
DT   16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT   16-SEP-2015, sequence version 1.
DT   27-MAR-2024, entry version 46.
DE   RecName: Full=Protein disulfide-isomerase {ECO:0000256|ARBA:ARBA00012723, ECO:0000256|RuleBase:RU361130};
DE            EC=5.3.4.1 {ECO:0000256|ARBA:ARBA00012723, ECO:0000256|RuleBase:RU361130};
GN   ORFNames=Vbra_14444 {ECO:0000313|EMBL:CEM07350.1};
OS   Vitrella brassicaformis (strain CCMP3155).
OC   Eukaryota; Sar; Alveolata; Colpodellida; Vitrellaceae; Vitrella.
OX   NCBI_TaxID=1169540 {ECO:0000313|EMBL:CEM07350.1, ECO:0000313|Proteomes:UP000041254};
RN   [1] {ECO:0000313|EMBL:CEM07350.1, ECO:0000313|Proteomes:UP000041254}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Zhu J., Qi W., Song R.;
RL   Submitted (NOV-2014) 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         ECO:0000256|RuleBase:RU361130};
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, ECO:0000256|RuleBase:RU004208}.
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DR   EMBL; CDMY01000376; CEM07350.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G4F631; -.
DR   STRING; 1169540.A0A0G4F631; -.
DR   VEuPathDB; CryptoDB:Vbra_14444; -.
DR   InParanoid; A0A0G4F631; -.
DR   OMA; HRTQDSV; -.
DR   OrthoDB; 5399045at2759; -.
DR   PhylomeDB; A0A0G4F631; -.
DR   Proteomes; UP000041254; 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; 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; IPR005788; PDI_thioredoxin-like_dom.
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   NCBIfam; TIGR01126; pdi_dom; 2.
DR   PANTHER; PTHR18929; PROTEIN DISULFIDE ISOMERASE; 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; 2.
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, ECO:0000256|RuleBase:RU361130};
KW   Redox-active center {ECO:0000256|ARBA:ARBA00023284,
KW   ECO:0000256|PIRSR:PIRSR605792-51};
KW   Reference proteome {ECO:0000313|Proteomes:UP000041254};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Signal {ECO:0000256|ARBA:ARBA00022729}.
FT   DOMAIN          34..147
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
FT   DOMAIN          349..478
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
FT   DISULFID        72..75
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR605792-51"
FT   DISULFID        399..402
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR605792-51"
SQ   SEQUENCE   549 AA;  61965 MW;  64127686A5CAFEE8 CRC64;
     MPPCSLQVLS EIAVEQTTNV MLVRVGVCGL VASLALLAAA ADEAVVSLTQ DTFKPFIDEN
     PISLVEFYAP WCGHCKQLAP EYEKAAKELK GKIPLAKVDA TVEEKLAQEF DVQGFPTIKF
     FKKGKPQEYD GGRTSSDIVE WLEKQTGPAV TNMTKDEFKT MIDTETVVVS AKFTDKSHSL
     YKVFEEVADL MRMAAKFVQI DDNQNKIVIH RKGEDAPIVY SGAADAEELG AWVEEERFHL
     FGEINAENFQ SYDERKREGI AWVCVKMEKS NQANVTAVTP IFRAMAKEYP QYSFVWLDTQ
     QFGEHVESFL GISDDDYPAM VITTKEDKKY RWTGPAIEKS AIKQFIEDVR AGKVEPFLKS
     QPIPETNDEP VKVVVGKNFD EMVFHADKDV MLEVYAPWCG HCKKLEPQYN AVAEMLAKNE
     HIMLAKLDGT ANEVAHSDFQ YEGFPTIFYV KAGEKKPIPY EGDRTKKGII KFIKKNASKP
     VEITETKAAA TKEPQLPFVD TAGWREWMQD TTEKIEELGA LLDSYDELKR IHEEKKGKKA
     KKTSTKDEL
//