ID A0A1M6ZK06_9RHOB Unreviewed; 305 AA.
AC A0A1M6ZK06;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE SubName: Full=Thioredoxin {ECO:0000313|EMBL:SHL30797.1};
GN ORFNames=SAMN05444414_11075 {ECO:0000313|EMBL:SHL30797.1};
OS Roseovarius marisflavi.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Roseovarius.
OX NCBI_TaxID=1054996 {ECO:0000313|EMBL:SHL30797.1, ECO:0000313|Proteomes:UP000184191};
RN [1] {ECO:0000313|EMBL:SHL30797.1, ECO:0000313|Proteomes:UP000184191}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 29327 {ECO:0000313|EMBL:SHL30797.1,
RC ECO:0000313|Proteomes:UP000184191};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-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; FRBN01000010; SHL30797.1; -; Genomic_DNA.
DR RefSeq; WP_073197962.1; NZ_FRBN01000010.1.
DR AlphaFoldDB; A0A1M6ZK06; -.
DR STRING; 1054996.SAMN05444414_11075; -.
DR OrthoDB; 9790390at2; -.
DR Proteomes; UP000184191; 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 Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 11..123
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
SQ SEQUENCE 305 AA; 32123 MW; F5A6A2FFF634C122 CRC64;
MIELGQTQNA PAAGDLIKDV SEADFMTEVV EMSQTVPVIV DFWAPWCGPC KTLGPVLEAA
VTRANGAVKM AKVNVDENQM IAGQLRVQSI PTVYAFWQGQ PVDGFQGAVP PSEIDAFVAR
VVEAGGGAPD GGLDEALDAA DEMLEEGAVA DAAQTYAAIA QEDPNNVRAY AGMARAEIAL
GELDQAEAIL NGAPAEIATA PEIEAIHAQI ALARQAADAG PVAELRAAVD ADPSDHQARF
DLAQALYANG QAEEAVDELL AIFRADREWN DGAAKAQLFT IFEALKPNDP VVLNGRRKLS
SMIFA
//
