ID   A0A1J4MFX7_9CRYT        Unreviewed;       481 AA.
AC   A0A1J4MFX7;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   13-SEP-2023, entry version 22.
DE   RecName: Full=protein disulfide-isomerase {ECO:0000256|ARBA:ARBA00012723};
DE            EC=5.3.4.1 {ECO:0000256|ARBA:ARBA00012723};
GN   ORFNames=cubi_02142 {ECO:0000313|EMBL:OII72911.1};
OS   Cryptosporidium ubiquitum.
OC   Eukaryota; Sar; Alveolata; Apicomplexa; Conoidasida; Coccidia;
OC   Eucoccidiorida; Eimeriorina; Cryptosporidiidae; Cryptosporidium.
OX   NCBI_TaxID=857276 {ECO:0000313|EMBL:OII72911.1, ECO:0000313|Proteomes:UP000186176};
RN   [1] {ECO:0000313|EMBL:OII72911.1, ECO:0000313|Proteomes:UP000186176}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=39726 {ECO:0000313|EMBL:OII72911.1};
RA   Liu S., Roellig D.M., Guo Y., Li N., Frace M.A., Tang K., Zhang L.,
RA   Feng Y., Xiao L.;
RT   "Reductive evolution of mitochondrial metabolism and differential evolution
RT   of invasion-related proteins in Cryptosporidium.";
RL   Submitted (OCT-2016) 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}.
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:OII72911.1}.
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DR   EMBL; LRBP01000017; OII72911.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1J4MFX7; -.
DR   VEuPathDB; CryptoDB:cubi_02142; -.
DR   OrthoDB; 5399045at2759; -.
DR   Proteomes; UP000186176; 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; 3.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
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};
KW   Redox-active center {ECO:0000256|ARBA:ARBA00023284,
KW   ECO:0000256|PIRSR:PIRSR605792-51}; Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           25..481
FT                   /note="protein disulfide-isomerase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5012520644"
FT   DOMAIN          22..141
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
FT   DOMAIN          328..470
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
FT   DISULFID        62..65
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR605792-51"
FT   DISULFID        391..394
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR605792-51"
SQ   SEQUENCE   481 AA;  53696 MW;  620C722E3EFD8210 CRC64;
     MIGVKSLISA AFLGFSCLSK VVLGGDEAHF ISEHITSLTS SNFEDFVKSK SHVLITFFAP
     WCGHCTALEP EFKATCAEIS KLSPPVFCGS VDATENMELA QQHGVSGYPT IKFFTGIDNV
     QNYSGARSKD AFIKYIKKLT GPAVQIAESE DAIKTIFASS SSAFVGRFTS KDSAEYAVFE
     KVANGHREHN YAFIAFFQAG DQKLEVLHKD EDPVSLPMPK TVEELEAKIS IMNVPLFSAI
     SAENYSLYMS REGYTAWFCG TNEDFAKYAA NIRKVAADYR EKYAFVFLDT EQFGSHATQH
     LLIENFPGLV IQSVNVPSIR YMYGPAKFDS VEPLKEFMKQ VSEGKHELSI KSEPIPAEQS
     GPVTVVVGKT FEEIVFRSDK DVLLEIYAQW CGHCKNLEPI YNQLGEEYKD NDKVVIAKIN
     GPQNDIPYEG FSPRAFPTIL FVKAGTRTPI PYDGKRTVEA FKEFIKEHSS FPQEKESRDE
     L
//