| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| Smed_1571 | Smed_3045 | Smed_1571 | Smed_3045 | Glutathione-disulfide reductase; Maintains high levels of reduced glutathione. | TIGRFAM: thioredoxin; PFAM: Thioredoxin domain; KEGG: sme:SMc03801 putative thioredoxin protein. | 0.908 |
| Smed_1619 | Smed_3045 | Smed_1619 | Smed_3045 | PFAM: heat shock protein DnaJ domain protein; KEGG: sme:SMc04233 hypothetical DnaJ domain protein. | TIGRFAM: thioredoxin; PFAM: Thioredoxin domain; KEGG: sme:SMc03801 putative thioredoxin protein. | 0.603 |
| Smed_1619 | grpE | Smed_1619 | Smed_0012 | PFAM: heat shock protein DnaJ domain protein; KEGG: sme:SMc04233 hypothetical DnaJ domain protein. | Ribulose-phosphate 3-epimerase; 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 [...] | 0.823 |
| Smed_1619 | hslU | Smed_1619 | Smed_3266 | PFAM: heat shock protein DnaJ domain protein; KEGG: sme:SMc04233 hypothetical DnaJ 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. | 0.774 |
| Smed_1619 | hslV | Smed_1619 | Smed_3264 | PFAM: heat shock protein DnaJ domain protein; KEGG: sme:SMc04233 hypothetical DnaJ domain protein. | 20S proteasome A and B subunits; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.737 |
| Smed_1619 | lon | Smed_1619 | Smed_0874 | PFAM: heat shock protein DnaJ domain protein; KEGG: sme:SMc04233 hypothetical DnaJ domain protein. | ATP-dependent protease La; ATP-dependent serine protease that mediates the selective degradation of mutant and abnormal proteins as well as certain short- lived regulatory proteins. Required for cellular homeostasis and for survival from DNA damage and developmental changes induced by stress. Degrades polypeptides processively to yield small peptide fragments that are 5 to 10 amino acids long. Binds to DNA in a double-stranded, site-specific manner. | 0.742 |
| Smed_3044 | Smed_3045 | Smed_3044 | Smed_3045 | PFAM: YbaK/prolyl-tRNA synthetase associated region; KEGG: sme:SMc03800 hypothetical protein. | TIGRFAM: thioredoxin; PFAM: Thioredoxin domain; KEGG: sme:SMc03801 putative thioredoxin protein. | 0.638 |
| Smed_3044 | Smed_3046 | Smed_3044 | Smed_3046 | PFAM: YbaK/prolyl-tRNA synthetase associated region; KEGG: sme:SMc03800 hypothetical protein. | PFAM: peptidase S16 lon domain protein; KEGG: sme:SMc03802 hypothetical protein. | 0.455 |
| Smed_3045 | Smed_1571 | Smed_3045 | Smed_1571 | TIGRFAM: thioredoxin; PFAM: Thioredoxin domain; KEGG: sme:SMc03801 putative thioredoxin protein. | Glutathione-disulfide reductase; Maintains high levels of reduced glutathione. | 0.908 |
| Smed_3045 | Smed_1619 | Smed_3045 | Smed_1619 | TIGRFAM: thioredoxin; PFAM: Thioredoxin domain; KEGG: sme:SMc03801 putative thioredoxin protein. | PFAM: heat shock protein DnaJ domain protein; KEGG: sme:SMc04233 hypothetical DnaJ domain protein. | 0.603 |
| Smed_3045 | Smed_3044 | Smed_3045 | Smed_3044 | TIGRFAM: thioredoxin; PFAM: Thioredoxin domain; KEGG: sme:SMc03801 putative thioredoxin protein. | PFAM: YbaK/prolyl-tRNA synthetase associated region; KEGG: sme:SMc03800 hypothetical protein. | 0.638 |
| Smed_3045 | Smed_3046 | Smed_3045 | Smed_3046 | TIGRFAM: thioredoxin; PFAM: Thioredoxin domain; KEGG: sme:SMc03801 putative thioredoxin protein. | PFAM: peptidase S16 lon domain protein; KEGG: sme:SMc03802 hypothetical protein. | 0.639 |
| Smed_3045 | Smed_3215 | Smed_3045 | Smed_3215 | TIGRFAM: thioredoxin; PFAM: Thioredoxin domain; KEGG: sme:SMc03801 putative thioredoxin protein. | PFAM: FxsA cytoplasmic membrane protein; KEGG: sme:SMc02787 hypothetical transmembrane protein. | 0.701 |
| Smed_3045 | dnaJ | Smed_3045 | Smed_3390 | TIGRFAM: thioredoxin; PFAM: Thioredoxin domain; KEGG: sme:SMc03801 putative thioredoxin 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 [...] | 0.603 |
| Smed_3045 | grpE | Smed_3045 | Smed_0012 | TIGRFAM: thioredoxin; PFAM: Thioredoxin domain; KEGG: sme:SMc03801 putative thioredoxin protein. | Ribulose-phosphate 3-epimerase; 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 [...] | 0.769 |
| Smed_3045 | hslU | Smed_3045 | Smed_3266 | TIGRFAM: thioredoxin; PFAM: Thioredoxin domain; KEGG: sme:SMc03801 putative thioredoxin 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. | 0.793 |
| Smed_3045 | hslV | Smed_3045 | Smed_3264 | TIGRFAM: thioredoxin; PFAM: Thioredoxin domain; KEGG: sme:SMc03801 putative thioredoxin protein. | 20S proteasome A and B subunits; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.792 |
| Smed_3045 | lon | Smed_3045 | Smed_0874 | TIGRFAM: thioredoxin; PFAM: Thioredoxin domain; KEGG: sme:SMc03801 putative thioredoxin protein. | ATP-dependent protease La; ATP-dependent serine protease that mediates the selective degradation of mutant and abnormal proteins as well as certain short- lived regulatory proteins. Required for cellular homeostasis and for survival from DNA damage and developmental changes induced by stress. Degrades polypeptides processively to yield small peptide fragments that are 5 to 10 amino acids long. Binds to DNA in a double-stranded, site-specific manner. | 0.581 |
| Smed_3046 | Smed_3044 | Smed_3046 | Smed_3044 | PFAM: peptidase S16 lon domain protein; KEGG: sme:SMc03802 hypothetical protein. | PFAM: YbaK/prolyl-tRNA synthetase associated region; KEGG: sme:SMc03800 hypothetical protein. | 0.455 |
| Smed_3046 | Smed_3045 | Smed_3046 | Smed_3045 | PFAM: peptidase S16 lon domain protein; KEGG: sme:SMc03802 hypothetical protein. | TIGRFAM: thioredoxin; PFAM: Thioredoxin domain; KEGG: sme:SMc03801 putative thioredoxin protein. | 0.639 |