node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
SHM31909.1 | SHM31948.1 | SAMN05192549_101282 | SAMN05192549_101283 | Molecular chaperone DnaK (HSP70); Belongs to the heat shock protein 70 family. | Hsp70 protein. | 0.822 |
SHM31909.1 | SHN39004.1 | SAMN05192549_101282 | SAMN05192549_109233 | Molecular chaperone DnaK (HSP70); Belongs to the heat shock protein 70 family. | Molecular chaperone DnaJ. | 0.985 |
SHM31909.1 | dnaJ | SAMN05192549_101282 | SAMN05192549_106188 | Molecular chaperone DnaK (HSP70); 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, [...] | 0.985 |
SHM31909.1 | groL | SAMN05192549_101282 | SAMN05192549_111125 | Molecular chaperone DnaK (HSP70); Belongs to the heat shock protein 70 family. | Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.956 |
SHM31909.1 | groL-2 | SAMN05192549_101282 | SAMN05192549_11213 | Molecular chaperone DnaK (HSP70); Belongs to the heat shock protein 70 family. | Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.956 |
SHM31909.1 | grpE | SAMN05192549_101282 | SAMN05192549_106186 | Molecular chaperone DnaK (HSP70); 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 [...] | 0.990 |
SHM31948.1 | SHM31909.1 | SAMN05192549_101283 | SAMN05192549_101282 | Hsp70 protein. | Molecular chaperone DnaK (HSP70); Belongs to the heat shock protein 70 family. | 0.822 |
SHM31948.1 | SHN39004.1 | SAMN05192549_101283 | SAMN05192549_109233 | Hsp70 protein. | Molecular chaperone DnaJ. | 0.985 |
SHM31948.1 | dnaJ | SAMN05192549_101283 | SAMN05192549_106188 | Hsp70 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, [...] | 0.985 |
SHM31948.1 | groL | SAMN05192549_101283 | SAMN05192549_111125 | Hsp70 protein. | Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.956 |
SHM31948.1 | groL-2 | SAMN05192549_101283 | SAMN05192549_11213 | Hsp70 protein. | Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.956 |
SHM31948.1 | grpE | SAMN05192549_101283 | SAMN05192549_106186 | Hsp70 protein. | 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 [...] | 0.990 |
SHM63060.1 | SHN39004.1 | SAMN05192549_10252 | SAMN05192549_109233 | Hypothetical chaperone protein. | Molecular chaperone DnaJ. | 0.980 |
SHM63060.1 | dnaJ | SAMN05192549_10252 | SAMN05192549_106188 | Hypothetical chaperone 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, [...] | 0.977 |
SHM63060.1 | groL | SAMN05192549_10252 | SAMN05192549_111125 | Hypothetical chaperone protein. | Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.960 |
SHM63060.1 | groL-2 | SAMN05192549_10252 | SAMN05192549_11213 | Hypothetical chaperone protein. | Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.960 |
SHM63060.1 | grpE | SAMN05192549_10252 | SAMN05192549_106186 | Hypothetical chaperone protein. | 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 [...] | 0.990 |
SHM98729.1 | SHN39004.1 | SAMN05192549_103481 | SAMN05192549_109233 | Molecular chaperone HscC; Belongs to the heat shock protein 70 family. | Molecular chaperone DnaJ. | 0.996 |
SHM98729.1 | dnaJ | SAMN05192549_103481 | SAMN05192549_106188 | Molecular chaperone HscC; 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, [...] | 0.996 |
SHM98729.1 | groL | SAMN05192549_103481 | SAMN05192549_111125 | Molecular chaperone HscC; Belongs to the heat shock protein 70 family. | Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.964 |