| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| Acid_0976 | Acid_0977 | Acid_0976 | Acid_0977 | KEGG: reu:Reut_A1751 hypothetical protein. | KEGG: reu:Reut_A1752 putative heat-shock chaperone protein; Belongs to the heat shock protein 70 family. | 0.934 |
| Acid_0977 | Acid_0976 | Acid_0977 | Acid_0976 | KEGG: reu:Reut_A1752 putative heat-shock chaperone protein; Belongs to the heat shock protein 70 family. | KEGG: reu:Reut_A1751 hypothetical protein. | 0.934 |
| Acid_0977 | Acid_2034 | Acid_0977 | Acid_2034 | KEGG: reu:Reut_A1752 putative heat-shock chaperone protein; Belongs to the heat shock protein 70 family. | PFAM: heat shock protein DnaJ domain protein; KEGG: mlo:mlr0945 probable heat shock protein. | 0.836 |
| Acid_0977 | Acid_4826 | Acid_0977 | Acid_4826 | KEGG: reu:Reut_A1752 putative heat-shock chaperone protein; Belongs to the heat shock protein 70 family. | KEGG: pcu:pc1032 hypothetical protein. | 0.849 |
| Acid_0977 | Acid_5307 | Acid_0977 | Acid_5307 | KEGG: reu:Reut_A1752 putative heat-shock chaperone protein; Belongs to the heat shock protein 70 family. | TIGRFAM: 2-oxoglutarate dehydrogenase, E1 subunit; PFAM: dehydrogenase, E1 component; catalytic domain of components of various dehydrogenase complexes; Transketolase, central region; KEGG: sru:SRU_1173 2-oxoglutarate dehydrogenase, E1 component. | 0.820 |
| Acid_0977 | Acid_6318 | Acid_0977 | Acid_6318 | KEGG: reu:Reut_A1752 putative heat-shock chaperone protein; Belongs to the heat shock protein 70 family. | PFAM: heat shock protein DnaJ domain protein; KEGG: mma:MM1381 chaperone protein. | 0.870 |
| Acid_0977 | Acid_6319 | Acid_0977 | Acid_6319 | KEGG: reu:Reut_A1752 putative heat-shock chaperone protein; Belongs to the heat shock protein 70 family. | GrpE protein; 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-dependent i [...] | 0.974 |
| Acid_0977 | dnaJ | Acid_0977 | Acid_0734 | KEGG: reu:Reut_A1752 putative heat-shock chaperone protein; Belongs to the heat shock protein 70 family. | Chaperone protein 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, D [...] | 0.836 |
| Acid_0977 | dnaJ-2 | Acid_0977 | Acid_7483 | KEGG: reu:Reut_A1752 putative heat-shock chaperone protein; Belongs to the heat shock protein 70 family. | Chaperone DnaJ domain protein; 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 [...] | 0.836 |
| Acid_0977 | groL | Acid_0977 | Acid_6747 | KEGG: reu:Reut_A1752 putative heat-shock chaperone protein; 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. | 0.974 |
| Acid_0977 | grpE | Acid_0977 | Acid_0733 | KEGG: reu:Reut_A1752 putative heat-shock chaperone protein; Belongs to the heat shock protein 70 family. | GrpE protein; 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-dependent i [...] | 0.964 |
| Acid_2034 | Acid_0977 | Acid_2034 | Acid_0977 | PFAM: heat shock protein DnaJ domain protein; KEGG: mlo:mlr0945 probable heat shock protein. | KEGG: reu:Reut_A1752 putative heat-shock chaperone protein; Belongs to the heat shock protein 70 family. | 0.836 |
| Acid_2034 | Acid_4826 | Acid_2034 | Acid_4826 | PFAM: heat shock protein DnaJ domain protein; KEGG: mlo:mlr0945 probable heat shock protein. | KEGG: pcu:pc1032 hypothetical protein. | 0.884 |
| Acid_2034 | Acid_6319 | Acid_2034 | Acid_6319 | PFAM: heat shock protein DnaJ domain protein; KEGG: mlo:mlr0945 probable heat shock protein. | GrpE protein; 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-dependent i [...] | 0.827 |
| Acid_2034 | groL | Acid_2034 | Acid_6747 | PFAM: heat shock protein DnaJ domain protein; KEGG: mlo:mlr0945 probable heat shock protein. | Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.946 |
| Acid_2034 | grpE | Acid_2034 | Acid_0733 | PFAM: heat shock protein DnaJ domain protein; KEGG: mlo:mlr0945 probable heat shock protein. | GrpE protein; 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-dependent i [...] | 0.866 |
| Acid_4826 | Acid_0977 | Acid_4826 | Acid_0977 | KEGG: pcu:pc1032 hypothetical protein. | KEGG: reu:Reut_A1752 putative heat-shock chaperone protein; Belongs to the heat shock protein 70 family. | 0.849 |
| Acid_4826 | Acid_2034 | Acid_4826 | Acid_2034 | KEGG: pcu:pc1032 hypothetical protein. | PFAM: heat shock protein DnaJ domain protein; KEGG: mlo:mlr0945 probable heat shock protein. | 0.884 |
| Acid_4826 | Acid_6318 | Acid_4826 | Acid_6318 | KEGG: pcu:pc1032 hypothetical protein. | PFAM: heat shock protein DnaJ domain protein; KEGG: mma:MM1381 chaperone protein. | 0.884 |
| Acid_4826 | dnaJ | Acid_4826 | Acid_0734 | KEGG: pcu:pc1032 hypothetical protein. | Chaperone protein 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, D [...] | 0.884 |