| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| CED70847.1 | dnaJ-2 | AWOD_I_0753 | AWOD_I_2106 | Thioredoxin. | 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 [...] | 0.720 |
| CED70847.1 | dnaK | AWOD_I_0753 | AWOD_I_2107 | Thioredoxin. | Chaperone protein DnaK (heat shock protein 70); Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.517 |
| CED70847.1 | groL1 | AWOD_I_0753 | AWOD_I_2470 | Thioredoxin. | 60 kda chaperonin 1; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.913 |
| CED70847.1 | groS1 | AWOD_I_0753 | AWOD_I_2471 | Thioredoxin. | 10 kDa chaperonin 1; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.570 |
| CED70847.1 | grpE | AWOD_I_0753 | AWOD_I_2108 | Thioredoxin. | Protein GrpE (heat shock 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 roun [...] | 0.914 |
| CED70847.1 | hscA | AWOD_I_0753 | AWOD_I_0596 | Thioredoxin. | Chaperone protein HscA; Chaperone involved in the maturation of iron-sulfur cluster- containing proteins. Has a low intrinsic ATPase activity which is markedly stimulated by HscB. | 0.510 |
| CED70847.1 | hslU | AWOD_I_0753 | AWOD_I_0322 | Thioredoxin. | ATP-dependent hsl protease ATP-binding subunit HslU (heat shock protein 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. | 0.913 |
| CED70847.1 | hslV | AWOD_I_0753 | AWOD_I_0323 | Thioredoxin. | ATP-dependent protease HslV (heat shock protein HslV); Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.922 |
| CED70847.1 | htpG | AWOD_I_0753 | AWOD_I_0759 | Thioredoxin. | Chaperone protein HtpG (heat shock protein HtpG); Molecular chaperone. Has ATPase activity. | 0.806 |
| dnaJ | dnaK | AWOD_I_1103 | AWOD_I_2107 | Chaperone protein DnaJ. | Chaperone protein DnaK (heat shock protein 70); Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.966 |
| dnaJ | groL1 | AWOD_I_1103 | AWOD_I_2470 | Chaperone protein DnaJ. | 60 kda chaperonin 1; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.875 |
| dnaJ | groS1 | AWOD_I_1103 | AWOD_I_2471 | Chaperone protein DnaJ. | 10 kDa chaperonin 1; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.641 |
| dnaJ | grpE | AWOD_I_1103 | AWOD_I_2108 | Chaperone protein DnaJ. | Protein GrpE (heat shock 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 roun [...] | 0.965 |
| dnaJ | hscA | AWOD_I_1103 | AWOD_I_0596 | Chaperone protein DnaJ. | Chaperone protein HscA; Chaperone involved in the maturation of iron-sulfur cluster- containing proteins. Has a low intrinsic ATPase activity which is markedly stimulated by HscB. | 0.920 |
| dnaJ | hslU | AWOD_I_1103 | AWOD_I_0322 | Chaperone protein DnaJ. | ATP-dependent hsl protease ATP-binding subunit HslU (heat shock protein 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. | 0.630 |
| dnaJ | hslV | AWOD_I_1103 | AWOD_I_0323 | Chaperone protein DnaJ. | ATP-dependent protease HslV (heat shock protein HslV); Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.509 |
| dnaJ | htpG | AWOD_I_1103 | AWOD_I_0759 | Chaperone protein DnaJ. | Chaperone protein HtpG (heat shock protein HtpG); Molecular chaperone. Has ATPase activity. | 0.918 |
| dnaJ-2 | CED70847.1 | AWOD_I_2106 | AWOD_I_0753 | 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 [...] | Thioredoxin. | 0.720 |
| dnaJ-2 | dnaK | AWOD_I_2106 | AWOD_I_2107 | 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 [...] | Chaperone protein DnaK (heat shock protein 70); Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.992 |
| dnaJ-2 | groL1 | AWOD_I_2106 | AWOD_I_2470 | 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 [...] | 60 kda chaperonin 1; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.981 |
