ID   A0A1I5YMG4_9RHOB        Unreviewed;       306 AA.
AC   A0A1I5YMG4;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   24-JAN-2024, entry version 17.
DE   SubName: Full=Putative thioredoxin {ECO:0000313|EMBL:SFQ45418.1};
GN   ORFNames=SAMN05421853_10690 {ECO:0000313|EMBL:SFQ45418.1};
OS   Roseivivax halotolerans.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Roseivivax.
OX   NCBI_TaxID=93684 {ECO:0000313|EMBL:SFQ45418.1, ECO:0000313|Proteomes:UP000243106};
RN   [1] {ECO:0000313|Proteomes:UP000243106}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 10271 {ECO:0000313|Proteomes:UP000243106};
RA   Varghese N., Submissions S.;
RL   Submitted (OCT-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; FOXV01000006; SFQ45418.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I5YMG4; -.
DR   STRING; 93684.SAMN05421853_10690; -.
DR   Proteomes; UP000243106; 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:UP000243106};
KW   Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   DOMAIN          2..124
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
SQ   SEQUENCE   306 AA;  32817 MW;  17D0135C3114FE85 CRC64;
     MIELGTSTQN AAATDDVIKD VAEQDFMKEV IEASQDVPVI VDFWAPWCGP CKTLGPQLEA
     AVRAQRGAVK MAKVNVDEAQ AIAGQLRIQS IPTVYAFHKG QPVDGFQGAV PESQLKQFVE
     QIAKMGGGDT SGGLDDALAA AEEMLEAGQL EDAAQIFQAV MAEDSTNAKA YGGFARVAIA
     AGDVEQAEAI LNGAPAEIAD HAELEAARAQ IELARQAEQA GPIAELQEKV DAEPDNHQAR
     FDLAQALYAG GRTEDAVNQL LELFRRDREW NDGAAKQQLF TIFDALKPND PIVLNGRRKL
     SSMIFA
//