ID A3K3S8_9RHOB Unreviewed; 304 AA.
AC A3K3S8;
DT 03-APR-2007, integrated into UniProtKB/TrEMBL.
DT 03-APR-2007, sequence version 1.
DT 24-JAN-2024, entry version 74.
DE SubName: Full=Thioredoxin {ECO:0000313|EMBL:EBA08192.1};
GN ORFNames=SSE37_11629 {ECO:0000313|EMBL:EBA08192.1};
OS Sagittula stellata E-37.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Sagittula.
OX NCBI_TaxID=388399 {ECO:0000313|EMBL:EBA08192.1, ECO:0000313|Proteomes:UP000005713};
RN [1] {ECO:0000313|EMBL:EBA08192.1, ECO:0000313|Proteomes:UP000005713}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=E-37 {ECO:0000313|EMBL:EBA08192.1,
RC ECO:0000313|Proteomes:UP000005713};
RA Moran M.A., Ferriera S., Johnson J., Kravitz S., Beeson K., Sutton G.,
RA Rogers Y.-H., Friedman R., Frazier M., Venter J.C.;
RL Submitted (JUN-2006) 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:EBA08192.1}.
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DR EMBL; AAYA01000006; EBA08192.1; -; Genomic_DNA.
DR RefSeq; WP_005859070.1; NZ_AAYA01000006.1.
DR AlphaFoldDB; A3K3S8; -.
DR eggNOG; COG3118; Bacteria.
DR OrthoDB; 9790390at2; -.
DR Proteomes; UP000005713; 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; 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:UP000005713};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 10..122
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
SQ SEQUENCE 304 AA; 32132 MW; E82A3F96ACA33BAE CRC64;
MELNLQPQGQ TAGDLVKDIT EADFMAEVVD ASMKTPIIVD FWAPWCGPCK QLGPALEKVV
TAAKGAVKMV KVNVDQAQAI AGQLRIQSIP TVYAFWQGQP VDGFQGALPE SELKAFVDRV
VQAAGGDAGG GLDDALAAAE EMLEQGAAAD AVEVFAAVLE EDPVNAKAYG GMVRAHIATG
DLDTAEAVLN GAPVEISKAP ELEAAHAQIE LAKQAAQAGP VAELTAQVEA EPDNLQARFD
LAKAKYAHGD SEGAVTELLE VFRRDREWND GAAKAQLFTI FEALKPNDPV VLNGRRKLSS
MIFA
//
