(data stored in SCRATCH zone)

SWISSPROT: C1AT33_RHOOB

ID   C1AT33_RHOOB            Unreviewed;       122 AA.
AC   C1AT33;
DT   26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   26-MAY-2009, sequence version 1.
DT   07-JUN-2017, entry version 53.
DE   RecName: Full=Thioredoxin {ECO:0000256|PIRNR:PIRNR000077};
GN   Name=trxA {ECO:0000313|EMBL:BAH48965.1};
GN   OrderedLocusNames=ROP_07180 {ECO:0000313|EMBL:BAH48965.1};
OS   Rhodococcus opacus (strain B4).
OC   Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae;
OC   Rhodococcus.
OX   NCBI_TaxID=632772 {ECO:0000313|EMBL:BAH48965.1, ECO:0000313|Proteomes:UP000002212};
RN   [1] {ECO:0000313|EMBL:BAH48965.1, ECO:0000313|Proteomes:UP000002212}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B4 {ECO:0000313|EMBL:BAH48965.1,
RC   ECO:0000313|Proteomes:UP000002212};
RA   Takarada H., Sekine M., Hosoyama A., Yamada R., Fujisawa T., Omata S.,
RA   Shimizu A., Tsukatani N., Tanikawa S., Fujita N., Harayama S.;
RT   "Comparison of the complete genome sequences of Rhodococcus
RT   erythropolis PR4 and Rhodococcus opacus B4.";
RL   Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the thioredoxin family.
CC       {ECO:0000256|PIRNR:PIRNR000077}.
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DR   EMBL; AP011115; BAH48965.1; -; Genomic_DNA.
DR   RefSeq; WP_005247443.1; NC_012522.1.
DR   ProteinModelPortal; C1AT33; -.
DR   STRING; 632772.ROP_07180; -.
DR   EnsemblBacteria; BAH48965; BAH48965; ROP_07180.
DR   KEGG; rop:ROP_07180; -.
DR   PATRIC; fig|632772.20.peg.781; -.
DR   eggNOG; ENOG41080RH; Bacteria.
DR   eggNOG; COG0526; LUCA.
DR   HOGENOM; HOG000292977; -.
DR   KO; K03671; -.
DR   OMA; QRVDMIN; -.
DR   OrthoDB; POG091H03UW; -.
DR   Proteomes; UP000002212; 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; IPR012336; Thioredoxin-like_fold.
DR   InterPro; IPR017937; Thioredoxin_CS.
DR   InterPro; IPR013766; Thioredoxin_domain.
DR   PANTHER; PTHR10438; PTHR10438; 1.
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; C1AT33.
DR   SWISS-2DPAGE; C1AT33.
KW   Complete proteome {ECO:0000313|Proteomes:UP000002212}.
FT   DOMAIN        1    105       Thioredoxin. {ECO:0000259|PROSITE:
FT                                PS51352}.
FT   DISULFID     30     33       Redox-active. {ECO:0000256|PIRSR:
FT                                PIRSR000077-4}.
SQ   SEQUENCE   122 AA;  13186 MW;  2ADDC319309EFF05 CRC64;
     MATKTLTQQN FDETVTGNDV VLVDFWASWC GPCRSFAPTF EASSEQHPDV VHAKVDTEAE
     QGIAAAANIR SIPTIMAFRE GVLVFSQPGA LPPAALEDLV TQVKALDMDE VRKQIAEQAP
     AE
//

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