node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
ALM06568.1 | ALM06613.1 | SB49_01145 | SB49_01390 | Molecular chaperone Hsp90; Molecular chaperone. Has ATPase activity. | Molecular chaperone DnaJ; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.830 |
ALM06568.1 | ALM06870.1 | SB49_01145 | SB49_02920 | Molecular chaperone Hsp90; Molecular chaperone. Has ATPase activity. | Molecular chaperone DnaJ; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.830 |
ALM06568.1 | ALM08332.1 | SB49_01145 | SB49_11340 | Molecular chaperone Hsp90; Molecular chaperone. Has ATPase activity. | Molecular chaperone DnaJ; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.840 |
ALM06568.1 | dnaJ | SB49_01145 | SB49_07335 | Molecular chaperone Hsp90; Molecular chaperone. Has ATPase activity. | 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, [...] | 0.830 |
ALM06568.1 | dnaK | SB49_01145 | SB49_05100 | Molecular chaperone Hsp90; Molecular chaperone. Has ATPase activity. | Molecular chaperone DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.997 |
ALM06568.1 | groEL | SB49_01145 | SB49_09615 | Molecular chaperone Hsp90; Molecular chaperone. Has ATPase activity. | Molecular chaperone GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.887 |
ALM06568.1 | groS | SB49_01145 | SB49_09610 | Molecular chaperone Hsp90; Molecular chaperone. Has ATPase activity. | Molecular chaperone GroES; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.776 |
ALM06568.1 | grpE | SB49_01145 | SB49_07340 | Molecular chaperone Hsp90; Molecular chaperone. Has ATPase activity. | 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 [...] | 0.752 |
ALM06568.1 | lon | SB49_01145 | SB49_01910 | Molecular chaperone Hsp90; Molecular chaperone. Has ATPase activity. | Lon protease; 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. | 0.706 |
ALM06613.1 | ALM06568.1 | SB49_01390 | SB49_01145 | Molecular chaperone DnaJ; Derived by automated computational analysis using gene prediction method: Protein Homology. | Molecular chaperone Hsp90; Molecular chaperone. Has ATPase activity. | 0.830 |
ALM06613.1 | dnaK | SB49_01390 | SB49_05100 | Molecular chaperone DnaJ; Derived by automated computational analysis using gene prediction method: Protein Homology. | Molecular chaperone DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.885 |
ALM06613.1 | groEL | SB49_01390 | SB49_09615 | Molecular chaperone DnaJ; Derived by automated computational analysis using gene prediction method: Protein Homology. | Molecular chaperone GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.682 |
ALM06613.1 | groS | SB49_01390 | SB49_09610 | Molecular chaperone DnaJ; Derived by automated computational analysis using gene prediction method: Protein Homology. | Molecular chaperone GroES; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.578 |
ALM06613.1 | grpE | SB49_01390 | SB49_07340 | Molecular chaperone DnaJ; Derived by automated computational analysis using gene prediction method: Protein Homology. | 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 [...] | 0.761 |
ALM06613.1 | lon | SB49_01390 | SB49_01910 | Molecular chaperone DnaJ; Derived by automated computational analysis using gene prediction method: Protein Homology. | Lon protease; 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. | 0.532 |
ALM06870.1 | ALM06568.1 | SB49_02920 | SB49_01145 | Molecular chaperone DnaJ; Derived by automated computational analysis using gene prediction method: Protein Homology. | Molecular chaperone Hsp90; Molecular chaperone. Has ATPase activity. | 0.830 |
ALM06870.1 | dnaK | SB49_02920 | SB49_05100 | Molecular chaperone DnaJ; Derived by automated computational analysis using gene prediction method: Protein Homology. | Molecular chaperone DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.979 |
ALM06870.1 | groEL | SB49_02920 | SB49_09615 | Molecular chaperone DnaJ; Derived by automated computational analysis using gene prediction method: Protein Homology. | Molecular chaperone GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.719 |
ALM06870.1 | groS | SB49_02920 | SB49_09610 | Molecular chaperone DnaJ; Derived by automated computational analysis using gene prediction method: Protein Homology. | Molecular chaperone GroES; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.578 |
ALM06870.1 | grpE | SB49_02920 | SB49_07340 | Molecular chaperone DnaJ; Derived by automated computational analysis using gene prediction method: Protein Homology. | 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 [...] | 0.799 |