GenomeNet

Database: UniProt
Entry: A0A1N7S3B0_9BURK
LinkDB: A0A1N7S3B0_9BURK
Original site: A0A1N7S3B0_9BURK 
ID   A0A1N7S3B0_9BURK        Unreviewed;       282 AA.
AC   A0A1N7S3B0;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   SubName: Full=Thioredoxin {ECO:0000313|EMBL:SIT41894.1};
GN   ORFNames=BN2475_320083 {ECO:0000313|EMBL:SIT41894.1};
OS   Paraburkholderia ribeironis.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Paraburkholderia.
OX   NCBI_TaxID=1247936 {ECO:0000313|EMBL:SIT41894.1, ECO:0000313|Proteomes:UP000187012};
RN   [1] {ECO:0000313|EMBL:SIT41894.1, ECO:0000313|Proteomes:UP000187012}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=STM7296 {ECO:0000313|EMBL:SIT41894.1,
RC   ECO:0000313|Proteomes:UP000187012};
RA   Song W.-J., Kurnit D.M.;
RL   Submitted (DEC-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the thioredoxin family.
CC       {ECO:0000256|ARBA:ARBA00008987}.
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; CYGX02000032; SIT41894.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1N7S3B0; -.
DR   STRING; 1247936.BN2475_320083; -.
DR   OrthoDB; 9790390at2; -.
DR   Proteomes; UP000187012; Unassembled WGS sequence.
DR   GO; GO:0015035; F:protein-disulfide reductase activity; IEA:InterPro.
DR   CDD; cd02947; TRX_family; 1.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR   Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 2.
DR   InterPro; IPR005746; Thioredoxin.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   InterPro; IPR017937; Thioredoxin_CS.
DR   InterPro; IPR013766; Thioredoxin_domain.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   NCBIfam; TIGR01068; thioredoxin; 1.
DR   PANTHER; PTHR45663; GEO12009P1; 1.
DR   PANTHER; PTHR45663:SF11; GEO12009P1; 1.
DR   Pfam; PF00085; Thioredoxin; 1.
DR   Pfam; PF14559; TPR_19; 1.
DR   Pfam; PF14561; TPR_20; 1.
DR   PRINTS; PR00421; THIOREDOXIN.
DR   SUPFAM; SSF52833; Thioredoxin-like; 1.
DR   SUPFAM; SSF48452; TPR-like; 1.
DR   PROSITE; PS00194; THIOREDOXIN_1; 1.
DR   PROSITE; PS51352; THIOREDOXIN_2; 1.
PE   3: Inferred from homology;
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Electron transport {ECO:0000256|ARBA:ARBA00022982};
KW   Redox-active center {ECO:0000256|ARBA:ARBA00023284};
KW   Reference proteome {ECO:0000313|Proteomes:UP000187012};
KW   Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   DOMAIN          1..106
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
SQ   SEQUENCE   282 AA;  31339 MW;  195FEE7E78EA22DD CRC64;
     MDTTLATFEQ DVITASTLAP VLVDFWAPWC GPCKSLGPML EKLEAEAAGK WKLVKVNVDE
     NQELAGHFQV RSIPHVIAFA DGRPVDQFVG VLPEGQLREF IERLVPQGAD GARIEAQTAL
     AEGRRDDAYD ALQAALAYDP GFDEARMDRI EMLLEDNRID EARNEVDLLS PKTTQGIDAR
     FNKIKTRLDA VDAAADLPPT DALEARVAAN PDDLDARFDL ASALIARHKY AQALEHLLAI
     VQRDRAFRDD IGRKMMLSVF DLAAHQPELV SHWRRKLSAS LF
//
DBGET integrated database retrieval system