ID A0A1R3FWT9_COCAP Unreviewed; 430 AA.
AC A0A1R3FWT9;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE SubName: Full=Thioredoxin {ECO:0000313|EMBL:OMO50317.1};
GN ORFNames=CCACVL1_30513 {ECO:0000313|EMBL:OMO50317.1};
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:OMO50317.1, ECO:0000313|Proteomes:UP000188268};
RN [1] {ECO:0000313|EMBL:OMO50317.1, 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:OMO50317.1};
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 -!- 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:OMO50317.1}.
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DR EMBL; AWWV01016196; OMO50317.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1R3FWT9; -.
DR STRING; 210143.A0A1R3FWT9; -.
DR EnsemblPlants; OMO50317; OMO50317; CCACVL1_30513.
DR Gramene; OMO50317; OMO50317; CCACVL1_30513.
DR OMA; NSTTQHH; -.
DR OrthoDB; 1053050at2759; -.
DR Proteomes; UP000188268; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR CDD; cd02961; PDI_a_family; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 2.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR017937; Thioredoxin_CS.
DR InterPro; IPR013766; Thioredoxin_domain.
DR PANTHER; PTHR18929; PROTEIN DISULFIDE ISOMERASE; 1.
DR PANTHER; PTHR18929:SF215; PROTEIN DISULFIDE-ISOMERASE 5-2-LIKE; 1.
DR Pfam; PF00085; Thioredoxin; 1.
DR Pfam; PF13848; Thioredoxin_6; 1.
DR PRINTS; PR00421; THIOREDOXIN.
DR SUPFAM; SSF52833; Thioredoxin-like; 3.
DR PROSITE; PS00194; THIOREDOXIN_1; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000188268};
KW Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..430
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012074002"
FT TRANSMEM 370..393
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 11..137
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT REGION 399..430
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 430 AA; 48536 MW; F3A027BCD23EED0D CRC64;
MRLLLILALL LLSILKTGNF ATANQLKADG KVLELDESNF DSAISSFDYI LVDFYAPWCG
HCKRLSPQLD EAAPVLAGLK EPIVIAKVNA DKHTRLARKY DIDAYPTLML FMHGVYTEYY
GPRKADLLVQ YLKKFVAPDV SILSSDAAIN DFIEAAGSFF PIYIGFGLNE TVISNLAVKY
KKKAWFSVAK DFSEDAMVLY DFDKVPALVA LHQSYKQQSI FYGPFEDEYL GDFIKQNLLP
LVVPLNHETL KLLKDEKRKV VLAITADENE EQSQNLIKFL KAAASANRDL VFGHVGVKQW
EDFADKFGVN EKTKLPKMIV WDGEEEYFSV VGIESLDNED QGSQISHFLE GYKAGRTERK
KVKGPSFMEF IHSLIGIRTI YIIVFIVAMM MLIQSVGKDD EPVRDGRRDE IHHAESSVSS
EAESSQKKED
//
