ID A0A250WRK6_9CHLO Unreviewed; 511 AA.
AC A0A250WRK6;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 29.
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=CEUSTIGMA_g633.t1 {ECO:0000313|EMBL:GAX73180.1};
OS Chlamydomonas eustigma.
OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC CS clade; Chlamydomonadales; Chlamydomonadaceae; Chlamydomonas.
OX NCBI_TaxID=1157962 {ECO:0000313|EMBL:GAX73180.1, ECO:0000313|Proteomes:UP000232323};
RN [1] {ECO:0000313|EMBL:GAX73180.1, ECO:0000313|Proteomes:UP000232323}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIES-2499 {ECO:0000313|EMBL:GAX73180.1,
RC ECO:0000313|Proteomes:UP000232323};
RA Hirooka S., Hirose Y., Kanesaki Y., Higuchi S., Fujiwara T., Onuma R.,
RA Era A., Ohbayashi R., Uzuka A., Nozaki H., Yoshikawa H., Miyagishima S.Y.;
RT "Acidophilic green algal genome provides insights into adaptation to an
RT acidic environment.";
RL Submitted (AUG-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 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}.
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:GAX73180.1}.
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DR EMBL; BEGY01000002; GAX73180.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A250WRK6; -.
DR STRING; 1157962.A0A250WRK6; -.
DR OrthoDB; 314307at2759; -.
DR Proteomes; UP000232323; 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; 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 PANTHER; PTHR18929:SF246; 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:UP000232323};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|RuleBase:RU361130}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|RuleBase:RU361130"
FT CHAIN 22..511
FT /note="Protein disulfide-isomerase"
FT /evidence="ECO:0000256|RuleBase:RU361130"
FT /id="PRO_5011833855"
FT DOMAIN 14..147
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT DOMAIN 366..490
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT REGION 492..511
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 68..71
FT /note="Redox-active"
FT /evidence="ECO:0000256|PIRSR:PIRSR605792-51"
FT DISULFID 412..415
FT /note="Redox-active"
FT /evidence="ECO:0000256|PIRSR:PIRSR605792-51"
SQ SEQUENCE 511 AA; 55367 MW; ED6FC0B897D70AAF CRC64;
MSKFQLVALL MGCLLVAVPF SRNSASAAAD EGDDDDDADD VVVLTTKNFD SVIAGSKFAL
VEFYAPWCGH CKSLAPHYSK AATILKASDP SVVIAKVDAT VESELGTKFD VKGYPTLKWF
IDGELASDYN GGRDTDGIVS WIKKKTGPFA ITVETTESLE ELEDDHPVLM VAYFKSLEGA
EYEEFKSVAL KTEDVPFVQT TDAAVAAAAG LEKPGISAVK NFVGEAREVV AFTGSLTAVE
IKTFVTAEKL PLTIEFTQGN SDKIFNSGIK KQIIFWGSAA DLSAESTSFA SVRAVAKALK
GQLVFVTANN EGESHEPITN YFGLKGAASP VIMGFHMEKN KKFRYTGELT EAALSAFANS
VLDDTAKADY KSAPIPEEPE DGGVTVVVGK NFDDIVMDPS KDVLLEVYAP WCGHCKKLEP
IYKKLAKRFS SVDTVVIAKM DGTENEHPEV EAKGYPTILF YPAGKKTPIP FDGGDRSLKA
LTKFIKKHAE SEYELPKKGD KDDESNDKDE L
//
