| 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 | fxsA | AWOD_I_0753 | AWOD_I_0249 | Thioredoxin. | Protein FxsA. | 0.806 |
| CED70847.1 | gor | AWOD_I_0753 | AWOD_I_2573 | Thioredoxin. | Glutathione reductase. | 0.962 |
| 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 | 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 | 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 |
| CED70847.1 | trxA | AWOD_I_0753 | AWOD_I_0059 | Thioredoxin. | Thioredoxin 1; Belongs to the thioredoxin family. | 0.637 |
| CED70847.1 | trxB | AWOD_I_0753 | AWOD_I_0884 | Thioredoxin. | Thioredoxin reductase. | 0.757 |
| 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 | 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 |
| dnaJ-2 | grpE | AWOD_I_2106 | AWOD_I_2108 | 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 [...] | 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 [...] | 0.994 |
| dnaJ-2 | hslU | AWOD_I_2106 | AWOD_I_0322 | 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 [...] | 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. | 0.963 |
| dnaJ-2 | hslV | AWOD_I_2106 | AWOD_I_0323 | 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 [...] | ATP-dependent protease HslV (heat shock protein HslV); Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.958 |
| dnaJ-2 | htpG | AWOD_I_2106 | AWOD_I_0759 | 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 HtpG (heat shock protein HtpG); Molecular chaperone. Has ATPase activity. | 0.989 |
| dnaJ-2 | trxA | AWOD_I_2106 | AWOD_I_0059 | 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 1; Belongs to the thioredoxin family. | 0.593 |
| dnaJ-2 | trxB | AWOD_I_2106 | AWOD_I_0884 | 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 reductase. | 0.476 |
| fxsA | CED70847.1 | AWOD_I_0249 | AWOD_I_0753 | Protein FxsA. | Thioredoxin. | 0.806 |
| fxsA | grpE | AWOD_I_0249 | AWOD_I_2108 | Protein FxsA. | 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 [...] | 0.464 |
