GenomeNet

Database: UniProt
Entry: A0A0P1GRY7_9RHOB
LinkDB: A0A0P1GRY7_9RHOB
Original site: A0A0P1GRY7_9RHOB 
ID   A0A0P1GRY7_9RHOB        Unreviewed;       233 AA.
AC   A0A0P1GRY7;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   SubName: Full=Thiol-disulfide oxidoreductase D {ECO:0000313|EMBL:CUH78450.1};
GN   Name=bdbD_1 {ECO:0000313|EMBL:CUH78450.1};
GN   ORFNames=TRN7648_01983 {ECO:0000313|EMBL:CUH78450.1};
OS   Tropicibacter naphthalenivorans.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Tropicibacter.
OX   NCBI_TaxID=441103 {ECO:0000313|EMBL:CUH78450.1, ECO:0000313|Proteomes:UP000054935};
RN   [1] {ECO:0000313|EMBL:CUH78450.1, ECO:0000313|Proteomes:UP000054935}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CECT 7648 {ECO:0000313|EMBL:CUH78450.1,
RC   ECO:0000313|Proteomes:UP000054935};
RG   Swine Surveillance;
RL   Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: May be required for disulfide bond formation in some
CC       proteins. {ECO:0000256|ARBA:ARBA00003565}.
CC   -!- SIMILARITY: Belongs to the thioredoxin family. DsbA subfamily.
CC       {ECO:0000256|ARBA:ARBA00005791}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CYSE01000003; CUH78450.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0P1GRY7; -.
DR   STRING; 441103.TRN7648_01983; -.
DR   OrthoDB; 8478320at2; -.
DR   Proteomes; UP000054935; Unassembled WGS sequence.
DR   CDD; cd02972; DsbA_family; 1.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR   InterPro; IPR012336; Thioredoxin-like_fold.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   InterPro; IPR013766; Thioredoxin_domain.
DR   PANTHER; PTHR13887; GLUTATHIONE S-TRANSFERASE KAPPA; 1.
DR   PANTHER; PTHR13887:SF14; THIOREDOXIN-LIKE REDUCTASE RV2466C; 1.
DR   Pfam; PF13462; Thioredoxin_4; 1.
DR   SUPFAM; SSF52833; Thioredoxin-like; 1.
DR   PROSITE; PS51352; THIOREDOXIN_2; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000054935}.
FT   DOMAIN          36..230
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
SQ   SEQUENCE   233 AA;  25296 MW;  75F42E6DB88AB73A CRC64;
     MKMTSTAGAL ALAVIAGGAW FYGQEQGQVA GPEFTLPMAA NAQEASAPAA EEAEEYVVQD
     MVLGAEDAPV TVIEYASYTC PHCATFHENV FKDVKANYID TGKVKFVYRE VYFDKFGMWG
     SMIARCGDDT NRFFGITDML FKTQGTWARA GSEAAIADEL RKVGRLAGLG NEQLDACLTD
     GGKLRALVGW YKENAEEHGI DSTPSFIING EKVSNMNYAD FSAYLDEQLA AAE
//
DBGET integrated database retrieval system