ID   A0A2T6AJ60_9RHOB        Unreviewed;       308 AA.
AC   A0A2T6AJ60;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   SubName: Full=Thioredoxin {ECO:0000313|EMBL:PTX43837.1};
GN   ORFNames=C8N44_12449 {ECO:0000313|EMBL:PTX43837.1};
OS   Allosediminivita pacifica.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Allosediminivita.
OX   NCBI_TaxID=1267769 {ECO:0000313|EMBL:PTX43837.1, ECO:0000313|Proteomes:UP000244069};
RN   [1] {ECO:0000313|EMBL:PTX43837.1, ECO:0000313|Proteomes:UP000244069}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 29329 {ECO:0000313|EMBL:PTX43837.1,
RC   ECO:0000313|Proteomes:UP000244069};
RA   Goeker M.;
RT   "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT   (KMG-II): from individual species to whole genera.";
RL   Submitted (APR-2018) to the EMBL/GenBank/DDBJ databases.
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:PTX43837.1}.
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DR   EMBL; QBKN01000024; PTX43837.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2T6AJ60; -.
DR   OrthoDB; 9790390at2; -.
DR   Proteomes; UP000244069; Unassembled WGS sequence.
DR   GO; GO:0015035; F:protein-disulfide reductase activity; IEA:InterPro.
DR   CDD; cd02956; ybbN; 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; PTHR43601; THIOREDOXIN, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR43601:SF3; THIOREDOXIN, MITOCHONDRIAL; 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   4: Predicted;
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Redox-active center {ECO:0000256|ARBA:ARBA00023284};
KW   Reference proteome {ECO:0000313|Proteomes:UP000244069};
KW   Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT   DOMAIN          4..123
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
SQ   SEQUENCE   308 AA;  32345 MW;  E819090A14F1B440 CRC64;
     MIELGGGAAA PAQDANIKDV SEQDFMAEVV DASMQVPVIV DFWAPWCGPC KTLGPMLEEA
     VKAAGGAVKM AKVNVDEAQM VASQLRIQSI PTVYAFWQGQ PVDGFQGAVP QSEIKAFVDR
     LVQQGGGAGA DQGNGLEDAL TAAEEMLEQG AASDAAQTFS AILGEDEKNA AAYGGLVRAH
     IALGELEQAE AILNGAPAEI SKAPELEAAH AQLELAKQAA GVGPVAELTA KVEANPDDHQ
     ARYDLAQALY AQGDGEGAVD HLLELFRRDR EWNDGAAKAQ LTTIFDALKP NDPVALKGRR
     RLSSMIFA
//