| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| Swoo_0121 | Swoo_1797 | Swoo_0121 | Swoo_1797 | TIGRFAM: glutathione-disulfide reductase; PFAM: FAD-dependent pyridine nucleotide-disulphide oxidoreductase; pyridine nucleotide-disulphide oxidoreductase dimerisation region; KEGG: sse:Ssed_0142 glutathione-disulfide reductase. | PFAM: Thioredoxin domain; KEGG: sse:Ssed_2848 thioredoxin domain protein. | 0.975 |
| Swoo_0121 | Swoo_2486 | Swoo_0121 | Swoo_2486 | TIGRFAM: glutathione-disulfide reductase; PFAM: FAD-dependent pyridine nucleotide-disulphide oxidoreductase; pyridine nucleotide-disulphide oxidoreductase dimerisation region; KEGG: sse:Ssed_0142 glutathione-disulfide reductase. | TIGRFAM: thioredoxin reductase; PFAM: FAD-dependent pyridine nucleotide-disulphide oxidoreductase; KEGG: sse:Ssed_2124 thioredoxin reductase. | 0.591 |
| Swoo_0121 | groL | Swoo_0121 | Swoo_4308 | TIGRFAM: glutathione-disulfide reductase; PFAM: FAD-dependent pyridine nucleotide-disulphide oxidoreductase; pyridine nucleotide-disulphide oxidoreductase dimerisation region; KEGG: sse:Ssed_0142 glutathione-disulfide reductase. | Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.444 |
| Swoo_0121 | hslU | Swoo_0121 | Swoo_4430 | TIGRFAM: glutathione-disulfide reductase; PFAM: FAD-dependent pyridine nucleotide-disulphide oxidoreductase; pyridine nucleotide-disulphide oxidoreductase dimerisation region; KEGG: sse:Ssed_0142 glutathione-disulfide reductase. | Heat shock protein HslVU, ATPase subunit HslU; ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. The binding of ATP and its subsequent hydrolysis by HslU are essential for unfolding of protein substrates subsequently hydrolyzed by HslV. HslU recognizes the N-terminal part of its protein substrates and unfolds these before they are guided to HslV for hydrolysis. | 0.443 |
| Swoo_1797 | Swoo_0121 | Swoo_1797 | Swoo_0121 | PFAM: Thioredoxin domain; KEGG: sse:Ssed_2848 thioredoxin domain protein. | TIGRFAM: glutathione-disulfide reductase; PFAM: FAD-dependent pyridine nucleotide-disulphide oxidoreductase; pyridine nucleotide-disulphide oxidoreductase dimerisation region; KEGG: sse:Ssed_0142 glutathione-disulfide reductase. | 0.975 |
| Swoo_1797 | Swoo_2303 | Swoo_1797 | Swoo_2303 | PFAM: Thioredoxin domain; KEGG: sse:Ssed_2848 thioredoxin domain protein. | Ribonucleoside-diphosphate reductase, alpha subunit; Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides. | 0.744 |
| Swoo_1797 | Swoo_2486 | Swoo_1797 | Swoo_2486 | PFAM: Thioredoxin domain; KEGG: sse:Ssed_2848 thioredoxin domain protein. | TIGRFAM: thioredoxin reductase; PFAM: FAD-dependent pyridine nucleotide-disulphide oxidoreductase; KEGG: sse:Ssed_2124 thioredoxin reductase. | 0.838 |
| Swoo_1797 | Swoo_4156 | Swoo_1797 | Swoo_4156 | PFAM: Thioredoxin domain; KEGG: sse:Ssed_2848 thioredoxin domain protein. | PFAM: FxsA cytoplasmic membrane protein; KEGG: sse:Ssed_4013 FxsA cytoplasmic membrane protein. | 0.817 |
| Swoo_1797 | dnaJ | Swoo_1797 | Swoo_3582 | PFAM: Thioredoxin domain; KEGG: sse:Ssed_2848 thioredoxin domain protein. | Chaperone protein DnaJ; Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, D [...] | 0.744 |
| Swoo_1797 | groL | Swoo_1797 | Swoo_4308 | PFAM: Thioredoxin domain; KEGG: sse:Ssed_2848 thioredoxin domain protein. | Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.914 |
| Swoo_1797 | grpE | Swoo_1797 | Swoo_3479 | PFAM: Thioredoxin domain; KEGG: sse:Ssed_2848 thioredoxin domain protein. | GrpE protein; Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent i [...] | 0.896 |
| Swoo_1797 | hslU | Swoo_1797 | Swoo_4430 | PFAM: Thioredoxin domain; KEGG: sse:Ssed_2848 thioredoxin domain protein. | Heat shock protein HslVU, ATPase subunit HslU; ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. The binding of ATP and its subsequent hydrolysis by HslU are essential for unfolding of protein substrates subsequently hydrolyzed by HslV. HslU recognizes the N-terminal part of its protein substrates and unfolds these before they are guided to HslV for hydrolysis. | 0.890 |
| Swoo_1797 | hslV | Swoo_1797 | Swoo_4429 | PFAM: Thioredoxin domain; KEGG: sse:Ssed_2848 thioredoxin domain protein. | 20S proteasome A and B subunits; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.914 |
| Swoo_1797 | htpG | Swoo_1797 | Swoo_1796 | PFAM: Thioredoxin domain; KEGG: sse:Ssed_2848 thioredoxin domain protein. | Heat shock protein Hsp90; Molecular chaperone. Has ATPase activity. | 0.893 |
| Swoo_2303 | Swoo_1797 | Swoo_2303 | Swoo_1797 | Ribonucleoside-diphosphate reductase, alpha subunit; Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides. | PFAM: Thioredoxin domain; KEGG: sse:Ssed_2848 thioredoxin domain protein. | 0.744 |
| Swoo_2486 | Swoo_0121 | Swoo_2486 | Swoo_0121 | TIGRFAM: thioredoxin reductase; PFAM: FAD-dependent pyridine nucleotide-disulphide oxidoreductase; KEGG: sse:Ssed_2124 thioredoxin reductase. | TIGRFAM: glutathione-disulfide reductase; PFAM: FAD-dependent pyridine nucleotide-disulphide oxidoreductase; pyridine nucleotide-disulphide oxidoreductase dimerisation region; KEGG: sse:Ssed_0142 glutathione-disulfide reductase. | 0.591 |
| Swoo_2486 | Swoo_1797 | Swoo_2486 | Swoo_1797 | TIGRFAM: thioredoxin reductase; PFAM: FAD-dependent pyridine nucleotide-disulphide oxidoreductase; KEGG: sse:Ssed_2124 thioredoxin reductase. | PFAM: Thioredoxin domain; KEGG: sse:Ssed_2848 thioredoxin domain protein. | 0.838 |
| Swoo_2486 | dnaJ | Swoo_2486 | Swoo_3582 | TIGRFAM: thioredoxin reductase; PFAM: FAD-dependent pyridine nucleotide-disulphide oxidoreductase; KEGG: sse:Ssed_2124 thioredoxin reductase. | Chaperone protein DnaJ; Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, D [...] | 0.492 |
| Swoo_2486 | grpE | Swoo_2486 | Swoo_3479 | TIGRFAM: thioredoxin reductase; PFAM: FAD-dependent pyridine nucleotide-disulphide oxidoreductase; KEGG: sse:Ssed_2124 thioredoxin reductase. | GrpE protein; Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent i [...] | 0.421 |
| Swoo_4156 | Swoo_1797 | Swoo_4156 | Swoo_1797 | PFAM: FxsA cytoplasmic membrane protein; KEGG: sse:Ssed_4013 FxsA cytoplasmic membrane protein. | PFAM: Thioredoxin domain; KEGG: sse:Ssed_2848 thioredoxin domain protein. | 0.817 |