node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
SFR30287.1 | SFR35429.1 | SAMN04487937_0104 | SAMN04487937_1434 | Thermosome; Belongs to the TCP-1 chaperonin family. | Molecular chaperone DnaK; Belongs to the heat shock protein 70 family. | 0.801 |
SFR30287.1 | SFR35437.1 | SAMN04487937_0104 | SAMN04487937_1435 | Thermosome; Belongs to the TCP-1 chaperonin family. | Molecular chaperone GrpE (heat shock protein). | 0.784 |
SFR30287.1 | SFR40337.1 | SAMN04487937_0104 | SAMN04487937_1915 | Thermosome; Belongs to the TCP-1 chaperonin family. | Lon-like ATP-dependent protease; Belongs to the peptidase S16 family. | 0.744 |
SFR30287.1 | SFR58737.1 | SAMN04487937_0104 | SAMN04487937_2928 | Thermosome; Belongs to the TCP-1 chaperonin family. | PDZ domain-containing protein. | 0.669 |
SFR30287.1 | dnaJ | SAMN04487937_0104 | SAMN04487937_1750 | Thermosome; Belongs to the TCP-1 chaperonin family. | 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, [...] | 0.779 |
SFR30287.1 | dnaK | SAMN04487937_0104 | SAMN04487937_1749 | Thermosome; Belongs to the TCP-1 chaperonin family. | Molecular chaperone DnaK; Acts as a chaperone. | 0.801 |
SFR30287.1 | grpE | SAMN04487937_0104 | SAMN04487937_2550 | Thermosome; Belongs to the TCP-1 chaperonin family. | Molecular 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 [...] | 0.784 |
SFR35429.1 | SFR30287.1 | SAMN04487937_1434 | SAMN04487937_0104 | Molecular chaperone DnaK; Belongs to the heat shock protein 70 family. | Thermosome; Belongs to the TCP-1 chaperonin family. | 0.801 |
SFR35429.1 | SFR35437.1 | SAMN04487937_1434 | SAMN04487937_1435 | Molecular chaperone DnaK; Belongs to the heat shock protein 70 family. | Molecular chaperone GrpE (heat shock protein). | 0.917 |
SFR35429.1 | SFR35559.1 | SAMN04487937_1434 | SAMN04487937_1450 | Molecular chaperone DnaK; Belongs to the heat shock protein 70 family. | Thermosome; Belongs to the TCP-1 chaperonin family. | 0.788 |
SFR35429.1 | SFR40337.1 | SAMN04487937_1434 | SAMN04487937_1915 | Molecular chaperone DnaK; Belongs to the heat shock protein 70 family. | Lon-like ATP-dependent protease; Belongs to the peptidase S16 family. | 0.683 |
SFR35429.1 | SFR58737.1 | SAMN04487937_1434 | SAMN04487937_2928 | Molecular chaperone DnaK; Belongs to the heat shock protein 70 family. | PDZ domain-containing protein. | 0.588 |
SFR35429.1 | dnaJ | SAMN04487937_1434 | SAMN04487937_1750 | Molecular chaperone DnaK; Belongs to the heat shock protein 70 family. | 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, [...] | 0.998 |
SFR35429.1 | grpE | SAMN04487937_1434 | SAMN04487937_2550 | Molecular chaperone DnaK; Belongs to the heat shock protein 70 family. | Molecular 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 [...] | 0.937 |
SFR35429.1 | rpl40e | SAMN04487937_1434 | SAMN04487937_1263 | Molecular chaperone DnaK; Belongs to the heat shock protein 70 family. | Large subunit ribosomal protein L40e; Belongs to the eukaryotic ribosomal protein eL40 family. | 0.701 |
SFR35437.1 | SFR30287.1 | SAMN04487937_1435 | SAMN04487937_0104 | Molecular chaperone GrpE (heat shock protein). | Thermosome; Belongs to the TCP-1 chaperonin family. | 0.784 |
SFR35437.1 | SFR35429.1 | SAMN04487937_1435 | SAMN04487937_1434 | Molecular chaperone GrpE (heat shock protein). | Molecular chaperone DnaK; Belongs to the heat shock protein 70 family. | 0.917 |
SFR35437.1 | SFR35559.1 | SAMN04487937_1435 | SAMN04487937_1450 | Molecular chaperone GrpE (heat shock protein). | Thermosome; Belongs to the TCP-1 chaperonin family. | 0.784 |
SFR35437.1 | SFR40337.1 | SAMN04487937_1435 | SAMN04487937_1915 | Molecular chaperone GrpE (heat shock protein). | Lon-like ATP-dependent protease; Belongs to the peptidase S16 family. | 0.714 |
SFR35437.1 | dnaJ | SAMN04487937_1435 | SAMN04487937_1750 | Molecular chaperone GrpE (heat shock protein). | 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, [...] | 0.916 |