ID A0A0B4RBV9_9BACL Unreviewed; 104 AA.
AC A0A0B4RBV9;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE RecName: Full=Thioredoxin {ECO:0000256|PIRNR:PIRNR000077};
GN ORFNames=Plano_1669 {ECO:0000313|EMBL:AIY05634.1};
OS Planococcus sp. PAMC 21323.
OC Bacteria; Bacillota; Bacilli; Bacillales; Planococcaceae; Planococcus.
OX NCBI_TaxID=1526927 {ECO:0000313|EMBL:AIY05634.1, ECO:0000313|Proteomes:UP000031496};
RN [1] {ECO:0000313|EMBL:AIY05634.1, ECO:0000313|Proteomes:UP000031496}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PAMC 21323 {ECO:0000313|EMBL:AIY05634.1,
RC ECO:0000313|Proteomes:UP000031496};
RA Jung J.-H., Joe M.-H., Cho Y.-J., Lee S.G., Han S.J., Lim S., Choi J.-i.;
RT "Complete genome sequence of Planococcus sp. PAMC21323 isolated from the
RT Antarctica.";
RL Submitted (AUG-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the thioredoxin family.
CC {ECO:0000256|ARBA:ARBA00008987, ECO:0000256|PIRNR:PIRNR000077}.
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; CP009129; AIY05634.1; -; Genomic_DNA.
DR RefSeq; WP_038704052.1; NZ_CP009129.1.
DR AlphaFoldDB; A0A0B4RBV9; -.
DR STRING; 1526927.Plano_1669; -.
DR KEGG; pln:Plano_1669; -.
DR eggNOG; COG3118; Bacteria.
DR HOGENOM; CLU_090389_10_4_9; -.
DR OrthoDB; 9790390at2; -.
DR Proteomes; UP000031496; Chromosome.
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 InterPro; IPR005746; Thioredoxin.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR013766; Thioredoxin_domain.
DR NCBIfam; TIGR01068; thioredoxin; 1.
DR PANTHER; PTHR45663; GEO12009P1; 1.
DR PANTHER; PTHR45663:SF11; GEO12009P1; 1.
DR Pfam; PF00085; Thioredoxin; 1.
DR PIRSF; PIRSF000077; Thioredoxin; 1.
DR PRINTS; PR00421; THIOREDOXIN.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157,
KW ECO:0000256|PIRSR:PIRSR000077-4};
KW Electron transport {ECO:0000256|ARBA:ARBA00022982};
KW Redox-active center {ECO:0000256|ARBA:ARBA00023284,
KW ECO:0000256|PIRSR:PIRSR000077-4};
KW Reference proteome {ECO:0000313|Proteomes:UP000031496};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 1..104
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT DISULFID 29..32
FT /note="Redox-active"
FT /evidence="ECO:0000256|PIRSR:PIRSR000077-4"
SQ SEQUENCE 104 AA; 11576 MW; 9DAB927A86FBA61C CRC64;
MSIKDVTDST FVDETKEGFV IAELGAAWCA PCKMIAPALE EINEDQQNNI SVVQVDIDNN
QEIAQKYGVM SIPTLLFFKN GELMEQSVGF QQKDEILAIA QKHI
//