(data stored in SCRATCH zone)

SWISSPROT: Q13EP8_RHOPS

ID   Q13EP8_RHOPS            Unreviewed;       106 AA.
AC   Q13EP8;
DT   31-OCT-2006, integrated into UniProtKB/TrEMBL.
DT   31-OCT-2006, sequence version 1.
DT   08-MAY-2019, entry version 80.
DE   RecName: Full=Thioredoxin {ECO:0000256|PIRNR:PIRNR000077};
GN   OrderedLocusNames=RPD_0201 {ECO:0000313|EMBL:ABE37441.1};
OS   Rhodopseudomonas palustris (strain BisB5).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Bradyrhizobiaceae; Rhodopseudomonas.
OX   NCBI_TaxID=316057 {ECO:0000313|EMBL:ABE37441.1, ECO:0000313|Proteomes:UP000001818};
RN   [1] {ECO:0000313|EMBL:ABE37441.1, ECO:0000313|Proteomes:UP000001818}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BisB5 {ECO:0000313|EMBL:ABE37441.1,
RC   ECO:0000313|Proteomes:UP000001818};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H.,
RA   Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Pelletier D.A., Kyrpides N.,
RA   Lykidis A., Oda Y., Harwood C.S., Richardson P.;
RT   "Complete sequence of Rhodopseudomonas palustris BisB5.";
RL   Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the thioredoxin family.
CC       {ECO:0000256|PIRNR:PIRNR000077}.
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DR   EMBL; CP000283; ABE37441.1; -; Genomic_DNA.
DR   RefSeq; WP_011500633.1; NC_007958.1.
DR   STRING; 316057.RPD_0201; -.
DR   EnsemblBacteria; ABE37441; ABE37441; RPD_0201.
DR   KEGG; rpd:RPD_0201; -.
DR   eggNOG; ENOG4105K63; Bacteria.
DR   eggNOG; COG0526; LUCA.
DR   HOGENOM; HOG000292977; -.
DR   KO; K03671; -.
DR   OMA; DANQEFA; -.
DR   OrthoDB; 1630944at2; -.
DR   BioCyc; RPAL316057:RPD_RS01020-MONOMER; -.
DR   Proteomes; UP000001818; Chromosome.
DR   GO; GO:0005623; C:cell; IEA:GOC.
DR   GO; GO:0015035; F:protein disulfide oxidoreductase activity; IEA:InterPro.
DR   GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro.
DR   GO; GO:0006662; P:glycerol ether metabolic process; IEA:InterPro.
DR   InterPro; IPR005746; Thioredoxin.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   InterPro; IPR017937; Thioredoxin_CS.
DR   InterPro; IPR013766; Thioredoxin_domain.
DR   Pfam; PF00085; Thioredoxin; 1.
DR   PIRSF; PIRSF000077; Thioredoxin; 1.
DR   SUPFAM; SSF52833; SSF52833; 1.
DR   TIGRFAMs; TIGR01068; thioredoxin; 1.
DR   PROSITE; PS00194; THIOREDOXIN_1; 1.
DR   PROSITE; PS51352; THIOREDOXIN_2; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q13EP8.
DR   SWISS-2DPAGE; Q13EP8.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001818};
KW   Disulfide bond {ECO:0000256|PIRSR:PIRSR000077-4};
KW   Redox-active center {ECO:0000256|PIRSR:PIRSR000077-4}.
FT   DOMAIN        1    106       Thioredoxin. {ECO:0000259|PROSITE:
FT                                PS51352}.
FT   DISULFID     31     34       Redox-active. {ECO:0000256|PIRSR:
FT                                PIRSR000077-4}.
SQ   SEQUENCE   106 AA;  11302 MW;  7529B1198F8229EA CRC64;
     MSVGKVSDAD FETEVLKAQG PVVVDFWAEW CGPCRMIAPA LDEISGAMGD KVKIVKLNVD
     ESPVTASKYG VMSIPTLMIF KGGEMASRQV GAAPKAKLQQ WISSAV
//

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