node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
AKT35978.1 | dnaJ-2 | CMC5_000900 | CMC5_022060 | Heat-shock protein Hsp70. | Molecular chaperone DnaJ. | 0.911 |
AKT35978.1 | dnaJ-4 | CMC5_000900 | CMC5_065320 | Heat-shock protein Hsp70. | Molecular 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, [...] | 0.943 |
AKT35978.1 | dnaJ-5 | CMC5_000900 | CMC5_073530 | Heat-shock protein Hsp70. | Molecular 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, [...] | 0.943 |
AKT35978.1 | groEL | CMC5_000900 | CMC5_037170 | Heat-shock protein Hsp70. | Molecular chaperone GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.692 |
AKT35978.1 | grpE | CMC5_000900 | CMC5_000040 | Heat-shock protein Hsp70. | 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 [...] | 0.930 |
AKT36845.1 | dnaJ-2 | CMC5_009660 | CMC5_022060 | Heat-shock protein Hsp70. | Molecular chaperone DnaJ. | 0.903 |
AKT36845.1 | dnaJ-4 | CMC5_009660 | CMC5_065320 | Heat-shock protein Hsp70. | Molecular 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, [...] | 0.939 |
AKT36845.1 | dnaJ-5 | CMC5_009660 | CMC5_073530 | Heat-shock protein Hsp70. | Molecular 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, [...] | 0.938 |
AKT36845.1 | groEL | CMC5_009660 | CMC5_037170 | Heat-shock protein Hsp70. | Molecular chaperone GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.719 |
AKT36845.1 | grpE | CMC5_009660 | CMC5_000040 | Heat-shock protein Hsp70. | 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 [...] | 0.903 |
dnaJ-2 | AKT35978.1 | CMC5_022060 | CMC5_000900 | Molecular chaperone DnaJ. | Heat-shock protein Hsp70. | 0.911 |
dnaJ-2 | AKT36845.1 | CMC5_022060 | CMC5_009660 | Molecular chaperone DnaJ. | Heat-shock protein Hsp70. | 0.903 |
dnaJ-2 | dnaK | CMC5_022060 | CMC5_000030 | Molecular chaperone DnaJ. | Molecular chaperone DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.917 |
dnaJ-2 | dnaK-3 | CMC5_022060 | CMC5_016550 | Molecular chaperone DnaJ. | Molecular chaperone DnaK; Chaperone involved in the maturation of iron-sulfur cluster- containing proteins. Has a low intrinsic ATPase activity which is markedly stimulated by HscB. | 0.913 |
dnaJ-2 | dnaK-4 | CMC5_022060 | CMC5_038870 | Molecular chaperone DnaJ. | Molecular chaperone DnaK; Belongs to the heat shock protein 70 family. | 0.915 |
dnaJ-2 | dnaK-7 | CMC5_022060 | CMC5_082630 | Molecular chaperone DnaJ. | Molecular chaperone DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.919 |
dnaJ-2 | groEL | CMC5_022060 | CMC5_037170 | Molecular chaperone DnaJ. | Molecular chaperone GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.737 |
dnaJ-2 | grpE | CMC5_022060 | CMC5_000040 | Molecular chaperone DnaJ. | 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 [...] | 0.905 |
dnaJ-4 | AKT35978.1 | CMC5_065320 | CMC5_000900 | Molecular 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, [...] | Heat-shock protein Hsp70. | 0.943 |
dnaJ-4 | AKT36845.1 | CMC5_065320 | CMC5_009660 | Molecular 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, [...] | Heat-shock protein Hsp70. | 0.939 |