node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
Dde_2116 | dnaJ | Dde_2116 | Dde_0248 | Putative RNA polymerase, sigma 70 family subunit; Sigma factors are initiation factors that promote the attachment of RNA polymerase to specific initiation sites and are then released. | 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 [...] | 0.853 |
Dde_2116 | dnaK | Dde_2116 | Dde_1023 | Putative RNA polymerase, sigma 70 family subunit; Sigma factors are initiation factors that promote the attachment of RNA polymerase to specific initiation sites and are then released. | Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.857 |
Dde_2116 | groL | Dde_2116 | Dde_2473 | Putative RNA polymerase, sigma 70 family subunit; Sigma factors are initiation factors that promote the attachment of RNA polymerase to specific initiation sites and are then released. | Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.856 |
Dde_2116 | groS | Dde_2116 | Dde_2474 | Putative RNA polymerase, sigma 70 family subunit; Sigma factors are initiation factors that promote the attachment of RNA polymerase to specific initiation sites and are then released. | Chaperonin Cpn10; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.499 |
Dde_2116 | grpE | Dde_2116 | Dde_1025 | Putative RNA polymerase, sigma 70 family subunit; Sigma factors are initiation factors that promote the attachment of RNA polymerase to specific initiation sites and are then released. | 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 [...] | 0.534 |
Dde_2116 | hslU | Dde_2116 | Dde_2014 | Putative RNA polymerase, sigma 70 family subunit; Sigma factors are initiation factors that promote the attachment of RNA polymerase to specific initiation sites and are then released. | Heat shock protein HslVU, ATPase subunit HslU; ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. The binding of ATP and its subsequent hydrolysis by HslU are essential for unfolding of protein substrates subsequently hydrolyzed by HslV. HslU recognizes the N-terminal part of its protein substrates and unfolds these before they are guided to HslV for hydrolysis. | 0.447 |
Dde_2116 | hslV | Dde_2116 | Dde_2124 | Putative RNA polymerase, sigma 70 family subunit; Sigma factors are initiation factors that promote the attachment of RNA polymerase to specific initiation sites and are then released. | 20S proteasome A and B subunits; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.610 |
Dde_2116 | htpG | Dde_2116 | Dde_1147 | Putative RNA polymerase, sigma 70 family subunit; Sigma factors are initiation factors that promote the attachment of RNA polymerase to specific initiation sites and are then released. | ATP-binding region ATPase domain protein; Molecular chaperone. Has ATPase activity. | 0.414 |
Dde_3237 | dnaJ | Dde_3237 | Dde_0248 | SMART: Pyruvate-flavodoxin oxidoreductase, EKR domain; TIGRFAM: Pyruvate-flavodoxin oxidoreductase; KEGG: dvl:Dvul_0348 pyruvate flavodoxin/ferredoxin oxidoreductase domain-containing protein; PFAM: Pyruvate flavodoxin/ferredoxin oxidoreductase, N-terminal; Pyruvate-flavodoxin oxidoreductase, EKR domain; 4Fe-4S ferredoxin, iron-sulphur binding, subgroup; Thiamine pyrophosphate enzyme, C-terminal TPP-binding; Pyruvate/ketoisovalerate oxidoreductase; Belongs to the pyruvate:ferredoxin/flavodoxin oxidoreductase 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 [...] | 0.886 |
Dde_3237 | dnaK | Dde_3237 | Dde_1023 | SMART: Pyruvate-flavodoxin oxidoreductase, EKR domain; TIGRFAM: Pyruvate-flavodoxin oxidoreductase; KEGG: dvl:Dvul_0348 pyruvate flavodoxin/ferredoxin oxidoreductase domain-containing protein; PFAM: Pyruvate flavodoxin/ferredoxin oxidoreductase, N-terminal; Pyruvate-flavodoxin oxidoreductase, EKR domain; 4Fe-4S ferredoxin, iron-sulphur binding, subgroup; Thiamine pyrophosphate enzyme, C-terminal TPP-binding; Pyruvate/ketoisovalerate oxidoreductase; Belongs to the pyruvate:ferredoxin/flavodoxin oxidoreductase family. | Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.576 |
Dde_3237 | groL | Dde_3237 | Dde_2473 | SMART: Pyruvate-flavodoxin oxidoreductase, EKR domain; TIGRFAM: Pyruvate-flavodoxin oxidoreductase; KEGG: dvl:Dvul_0348 pyruvate flavodoxin/ferredoxin oxidoreductase domain-containing protein; PFAM: Pyruvate flavodoxin/ferredoxin oxidoreductase, N-terminal; Pyruvate-flavodoxin oxidoreductase, EKR domain; 4Fe-4S ferredoxin, iron-sulphur binding, subgroup; Thiamine pyrophosphate enzyme, C-terminal TPP-binding; Pyruvate/ketoisovalerate oxidoreductase; Belongs to the pyruvate:ferredoxin/flavodoxin oxidoreductase family. | Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.788 |
Dde_3237 | grpE | Dde_3237 | Dde_1025 | SMART: Pyruvate-flavodoxin oxidoreductase, EKR domain; TIGRFAM: Pyruvate-flavodoxin oxidoreductase; KEGG: dvl:Dvul_0348 pyruvate flavodoxin/ferredoxin oxidoreductase domain-containing protein; PFAM: Pyruvate flavodoxin/ferredoxin oxidoreductase, N-terminal; Pyruvate-flavodoxin oxidoreductase, EKR domain; 4Fe-4S ferredoxin, iron-sulphur binding, subgroup; Thiamine pyrophosphate enzyme, C-terminal TPP-binding; Pyruvate/ketoisovalerate oxidoreductase; Belongs to the pyruvate:ferredoxin/flavodoxin oxidoreductase 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 [...] | 0.598 |
Dde_3237 | htpG | Dde_3237 | Dde_1147 | SMART: Pyruvate-flavodoxin oxidoreductase, EKR domain; TIGRFAM: Pyruvate-flavodoxin oxidoreductase; KEGG: dvl:Dvul_0348 pyruvate flavodoxin/ferredoxin oxidoreductase domain-containing protein; PFAM: Pyruvate flavodoxin/ferredoxin oxidoreductase, N-terminal; Pyruvate-flavodoxin oxidoreductase, EKR domain; 4Fe-4S ferredoxin, iron-sulphur binding, subgroup; Thiamine pyrophosphate enzyme, C-terminal TPP-binding; Pyruvate/ketoisovalerate oxidoreductase; Belongs to the pyruvate:ferredoxin/flavodoxin oxidoreductase family. | ATP-binding region ATPase domain protein; Molecular chaperone. Has ATPase activity. | 0.480 |
dnaJ | Dde_2116 | Dde_0248 | Dde_2116 | 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 [...] | Putative RNA polymerase, sigma 70 family subunit; Sigma factors are initiation factors that promote the attachment of RNA polymerase to specific initiation sites and are then released. | 0.853 |
dnaJ | Dde_3237 | Dde_0248 | Dde_3237 | 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 [...] | SMART: Pyruvate-flavodoxin oxidoreductase, EKR domain; TIGRFAM: Pyruvate-flavodoxin oxidoreductase; KEGG: dvl:Dvul_0348 pyruvate flavodoxin/ferredoxin oxidoreductase domain-containing protein; PFAM: Pyruvate flavodoxin/ferredoxin oxidoreductase, N-terminal; Pyruvate-flavodoxin oxidoreductase, EKR domain; 4Fe-4S ferredoxin, iron-sulphur binding, subgroup; Thiamine pyrophosphate enzyme, C-terminal TPP-binding; Pyruvate/ketoisovalerate oxidoreductase; Belongs to the pyruvate:ferredoxin/flavodoxin oxidoreductase family. | 0.886 |
dnaJ | dnaK | Dde_0248 | Dde_1023 | 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 [...] | Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.996 |
dnaJ | groL | Dde_0248 | Dde_2473 | 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 [...] | Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.910 |
dnaJ | groS | Dde_0248 | Dde_2474 | 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 [...] | Chaperonin Cpn10; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.824 |
dnaJ | grpE | Dde_0248 | Dde_1025 | 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 [...] | 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 [...] | 0.972 |
dnaJ | hslU | Dde_0248 | Dde_2014 | 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 [...] | Heat shock protein HslVU, ATPase subunit HslU; ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. The binding of ATP and its subsequent hydrolysis by HslU are essential for unfolding of protein substrates subsequently hydrolyzed by HslV. HslU recognizes the N-terminal part of its protein substrates and unfolds these before they are guided to HslV for hydrolysis. | 0.900 |