ID A0A1R3H0S6_COCAP Unreviewed; 581 AA.
AC A0A1R3H0S6;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=protein disulfide-isomerase {ECO:0000256|ARBA:ARBA00012723};
DE EC=5.3.4.1 {ECO:0000256|ARBA:ARBA00012723};
GN ORFNames=CCACVL1_22155 {ECO:0000313|EMBL:OMO63954.1};
OS Corchorus capsularis (Jute).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Malvales; Malvaceae; Grewioideae; Apeibeae; Corchorus.
OX NCBI_TaxID=210143 {ECO:0000313|EMBL:OMO63954.1, ECO:0000313|Proteomes:UP000188268};
RN [1] {ECO:0000313|EMBL:OMO63954.1, ECO:0000313|Proteomes:UP000188268}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. CVL-1 {ECO:0000313|Proteomes:UP000188268};
RC TISSUE=Whole seedling {ECO:0000313|EMBL:OMO63954.1};
RA Alam M., Haque M.S., Islam M.S., Emdad E.M., Islam M.M., Ahmed B.,
RA Halim A., Hossen Q.M.M., Hossain M.Z., Ahmed R., Khan M.M., Islam R.,
RA Rashid M.M., Khan S.A., Rahman M.S., Alam M.;
RT "Corchorus capsularis genome sequencing.";
RL Submitted (SEP-2013) 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 -!- 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:OMO63954.1}.
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DR EMBL; AWWV01012856; OMO63954.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1R3H0S6; -.
DR STRING; 210143.A0A1R3H0S6; -.
DR EnsemblPlants; OMO63954; OMO63954; CCACVL1_22155.
DR Gramene; OMO63954; OMO63954; CCACVL1_22155.
DR OMA; APIVEMT; -.
DR OrthoDB; 52245at2759; -.
DR Proteomes; UP000188268; Unassembled WGS sequence.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:InterPro.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0003756; F:protein disulfide isomerase activity; IEA:UniProtKB-EC.
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; IPR035979; RBD_domain_sf.
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; PROTEIN DISULFIDE-ISOMERASE C17H9.14C-RELATED; 1.
DR PANTHER; PTHR45672:SF17; PROTEIN DISULFIDE-ISOMERASE LIKE 2-1; 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; SSF54928; RNA-binding domain, RBD; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000188268};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 215..354
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT DOMAIN 360..473
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT REGION 1..66
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 41..66
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 581 AA; 63553 MW; DE7FEF45F6F47231 CRC64;
MENGGGILLQ TEKRDPLRIG GTKKKNQGSP CKDSCPNKKD VSPKLGNSTT SRDLENNNDK
SSNFRTSSSV TIKNVPSIID LPQLEEAISV FGKVSKAFKR SVPNGLDCCD IEFKTIKSCK
TALSSGCLTI KNFNLAICPL HSSETVTIRI SNISSATAYS AIHSTCASCG PLEGLVRTKE
DVVVALFSVK GEEDTKSIIK RLNSTVMDES NWSADLHHSE APIVEMTDNA DPEDDLGLKI
SEPFADDVVV LTEENFEKEV GQDRGALVEF YAPWCGHCKK LAPEYEKLGA SFKKAKSVLI
GKVDCDEHKS VCSKYGVQGY PTIQWFPKGS LEPKKYEGPR TAESLAEFVN TEGGTNVKIA
TVPSNAVVLS ADNFDEVVLD ETKDVLVEFY APWCGHCKNL APTYEKVATA FKLEEEVVIA
NLDADKHKDL AEKYGVSGYP TLKFFPKGNK AGEDYDGGRD LDDFVTFINE KCGTSRDGKG
QLTSKAGILE SLNALVKEFV AASNDEKKAV FSKIEEEVEK LKGSTARYGK IYLKAAKSCI
EKGAEYPKKE IERLQRMLDK SISPAKADEF TLKKNILSAF A
//
