| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| EAR52606.1 | EAR52623.1 | OG2516_05843 | OG2516_05928 | Heat shock protein, Hsp70 family protein; COG0443 Molecular chaperone. | DnaJ domain protein; COG2214 DnaJ-class molecular chaperone. | 0.996 |
| EAR52606.1 | dnaJ | OG2516_05843 | OG2516_11106 | Heat shock protein, Hsp70 family protein; COG0443 Molecular chaperone. | Chaperone, 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, DnaK and [...] | 0.997 |
| EAR52606.1 | groEL | OG2516_05843 | OG2516_17146 | Heat shock protein, Hsp70 family protein; COG0443 Molecular chaperone. | Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.974 |
| EAR52606.1 | groS | OG2516_05843 | OG2516_17151 | Heat shock protein, Hsp70 family protein; COG0443 Molecular chaperone. | Chaperonin Cpn10 (GroES); Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.943 |
| EAR52606.1 | grpE | OG2516_05843 | OG2516_11351 | Heat shock protein, Hsp70 family protein; COG0443 Molecular chaperone. | Co-chaperone GrpE; 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-depend [...] | 0.993 |
| EAR52606.1 | hslU | OG2516_05843 | OG2516_11241 | Heat shock protein, Hsp70 family protein; COG0443 Molecular chaperone. | ATP-dependent protease ATP-binding subunit; 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. | 0.776 |
| EAR52606.1 | hslV | OG2516_05843 | OG2516_11206 | Heat shock protein, Hsp70 family protein; COG0443 Molecular chaperone. | ATP-dependent protease peptidase subunit; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.661 |
| EAR52606.1 | lon | OG2516_05843 | OG2516_03810 | Heat shock protein, Hsp70 family protein; COG0443 Molecular chaperone. | 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. | 0.800 |
| EAR52623.1 | EAR52606.1 | OG2516_05928 | OG2516_05843 | DnaJ domain protein; COG2214 DnaJ-class molecular chaperone. | Heat shock protein, Hsp70 family protein; COG0443 Molecular chaperone. | 0.996 |
| EAR52623.1 | dnaK | OG2516_05928 | OG2516_11101 | DnaJ domain protein; COG2214 DnaJ-class molecular chaperone. | Heat shock protein (Hsp70, DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.997 |
| EAR52623.1 | groEL | OG2516_05928 | OG2516_17146 | DnaJ domain protein; COG2214 DnaJ-class molecular chaperone. | Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.936 |
| EAR52623.1 | groS | OG2516_05928 | OG2516_17151 | DnaJ domain protein; COG2214 DnaJ-class molecular chaperone. | Chaperonin Cpn10 (GroES); Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.836 |
| EAR52623.1 | grpE | OG2516_05928 | OG2516_11351 | DnaJ domain protein; COG2214 DnaJ-class molecular chaperone. | Co-chaperone GrpE; 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-depend [...] | 0.968 |
| EAR52623.1 | hslU | OG2516_05928 | OG2516_11241 | DnaJ domain protein; COG2214 DnaJ-class molecular chaperone. | ATP-dependent protease ATP-binding subunit; 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. | 0.845 |
| EAR52623.1 | hslV | OG2516_05928 | OG2516_11206 | DnaJ domain protein; COG2214 DnaJ-class molecular chaperone. | ATP-dependent protease peptidase subunit; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.768 |
| EAR52623.1 | lon | OG2516_05928 | OG2516_03810 | DnaJ domain protein; COG2214 DnaJ-class molecular chaperone. | 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. | 0.809 |
| dnaJ | EAR52606.1 | OG2516_11106 | OG2516_05843 | Chaperone, 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, DnaK and [...] | Heat shock protein, Hsp70 family protein; COG0443 Molecular chaperone. | 0.997 |
| dnaJ | dnaK | OG2516_11106 | OG2516_11101 | Chaperone, 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, DnaK and [...] | Heat shock protein (Hsp70, DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.999 |
| dnaJ | groEL | OG2516_11106 | OG2516_17146 | Chaperone, 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, DnaK and [...] | Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.970 |
| dnaJ | groS | OG2516_11106 | OG2516_17151 | Chaperone, 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, DnaK and [...] | Chaperonin Cpn10 (GroES); Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.930 |