ID A0A316BZ49_PSESE Unreviewed; 326 AA.
AC A0A316BZ49;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE SubName: Full=Thioredoxin {ECO:0000313|EMBL:PWJ80133.1};
GN ORFNames=C7441_11359 {ECO:0000313|EMBL:PWJ80133.1};
OS Pseudaminobacter salicylatoxidans.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Phyllobacteriaceae; Pseudaminobacter.
OX NCBI_TaxID=93369 {ECO:0000313|EMBL:PWJ80133.1, ECO:0000313|Proteomes:UP000245396};
RN [1] {ECO:0000313|EMBL:PWJ80133.1, ECO:0000313|Proteomes:UP000245396}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 6986 {ECO:0000313|EMBL:PWJ80133.1,
RC ECO:0000313|Proteomes:UP000245396};
RA Goeker M.;
RT "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT most valuable type-strain genomes for metagenomic binning, comparative
RT biology and taxonomic classification.";
RL Submitted (MAY-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the thioredoxin family.
CC {ECO:0000256|ARBA:ARBA00008987}.
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:PWJ80133.1}.
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DR EMBL; QGGG01000013; PWJ80133.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A316BZ49; -.
DR STRING; 1192868.GCA_000304395_01182; -.
DR OrthoDB; 9790390at2; -.
DR Proteomes; UP000245396; 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:UP000245396};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 28..147
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT REGION 1..39
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..25
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 326 AA; 34154 MW; D7B221C987B9D3FA CRC64;
MSNQDNSFGG ADNSYTTTMT FGSQPAPAGN GAAAPDDASL IKDTTTSGFA ADVLQESRRQ
PVLVDFWAPW CGPCKQLAPA LEKTVQQAGG RVKLVKMNID DHPSVAGQLG IQSIPAVIAF
KDGQPVDGFM GAVPESQIRE FIDRIAGKDA GPQLEEALAA AAQARDAGDA NTAAAIFDSV
LQQAPDNVEA LAGLADLLFD AGDAAGAEEV LARAPADKAD APALAGVRAK IALATQAASL
GDPKEFEARL AANPKDHQAR FDLAMIQNAL GQRAEAADNL LTIVRTDRGW NDDAARTQLL
QLFEAWGMTD EVTLASRRKL SSLLFS
//
