| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| DvMF_0458 | dnaJ | DvMF_0458 | DvMF_2295 | KEGG: dde:Dde_2099 ATPase; TIGRFAM: ATP-dependent Clp protease, ATP-binding subunit clpA; PFAM: AAA ATPase central domain protein; Clp domain protein; ATPase associated with various cellular activities AAA_5; ATPase AAA-2 domain protein; ATP-dependent Clp protease ATP-binding subunit clpA; SMART: AAA ATPase; Belongs to the ClpA/ClpB 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 [...] | 0.805 |
| DvMF_0458 | dnaK | DvMF_0458 | DvMF_2835 | KEGG: dde:Dde_2099 ATPase; TIGRFAM: ATP-dependent Clp protease, ATP-binding subunit clpA; PFAM: AAA ATPase central domain protein; Clp domain protein; ATPase associated with various cellular activities AAA_5; ATPase AAA-2 domain protein; ATP-dependent Clp protease ATP-binding subunit clpA; SMART: AAA ATPase; Belongs to the ClpA/ClpB family. | Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.957 |
| DvMF_0458 | groL | DvMF_0458 | DvMF_3064 | KEGG: dde:Dde_2099 ATPase; TIGRFAM: ATP-dependent Clp protease, ATP-binding subunit clpA; PFAM: AAA ATPase central domain protein; Clp domain protein; ATPase associated with various cellular activities AAA_5; ATPase AAA-2 domain protein; ATP-dependent Clp protease ATP-binding subunit clpA; SMART: AAA ATPase; Belongs to the ClpA/ClpB family. | Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.702 |
| DvMF_0458 | groS | DvMF_0458 | DvMF_3063 | KEGG: dde:Dde_2099 ATPase; TIGRFAM: ATP-dependent Clp protease, ATP-binding subunit clpA; PFAM: AAA ATPase central domain protein; Clp domain protein; ATPase associated with various cellular activities AAA_5; ATPase AAA-2 domain protein; ATP-dependent Clp protease ATP-binding subunit clpA; SMART: AAA ATPase; Belongs to the ClpA/ClpB family. | Chaperonin Cpn10; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.718 |
| DvMF_0458 | grpE | DvMF_0458 | DvMF_1194 | KEGG: dde:Dde_2099 ATPase; TIGRFAM: ATP-dependent Clp protease, ATP-binding subunit clpA; PFAM: AAA ATPase central domain protein; Clp domain protein; ATPase associated with various cellular activities AAA_5; ATPase AAA-2 domain protein; ATP-dependent Clp protease ATP-binding subunit clpA; SMART: AAA ATPase; Belongs to the ClpA/ClpB 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 [...] | 0.826 |
| DvMF_0458 | hslU | DvMF_0458 | DvMF_0307 | KEGG: dde:Dde_2099 ATPase; TIGRFAM: ATP-dependent Clp protease, ATP-binding subunit clpA; PFAM: AAA ATPase central domain protein; Clp domain protein; ATPase associated with various cellular activities AAA_5; ATPase AAA-2 domain protein; ATP-dependent Clp protease ATP-binding subunit clpA; SMART: AAA ATPase; Belongs to the ClpA/ClpB family. | 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. | 0.654 |
| DvMF_0458 | hslV | DvMF_0458 | DvMF_0485 | KEGG: dde:Dde_2099 ATPase; TIGRFAM: ATP-dependent Clp protease, ATP-binding subunit clpA; PFAM: AAA ATPase central domain protein; Clp domain protein; ATPase associated with various cellular activities AAA_5; ATPase AAA-2 domain protein; ATP-dependent Clp protease ATP-binding subunit clpA; SMART: AAA ATPase; Belongs to the ClpA/ClpB family. | 20S proteasome A and B subunits; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.512 |
| DvMF_0458 | htpG | DvMF_0458 | DvMF_1117 | KEGG: dde:Dde_2099 ATPase; TIGRFAM: ATP-dependent Clp protease, ATP-binding subunit clpA; PFAM: AAA ATPase central domain protein; Clp domain protein; ATPase associated with various cellular activities AAA_5; ATPase AAA-2 domain protein; ATP-dependent Clp protease ATP-binding subunit clpA; SMART: AAA ATPase; Belongs to the ClpA/ClpB family. | Heat shock protein Hsp90; Molecular chaperone. Has ATPase activity. | 0.742 |
| DvMF_1860 | dnaJ | DvMF_1860 | DvMF_2295 | PFAM: 4Fe-4S ferredoxin iron-sulfur binding domain protein; pyruvate ferredoxin/flavodoxin oxidoreductase; pyruvate flavodoxin/ferredoxin oxidoreductase domain protein; pyruvate:ferredoxin (flavodoxin) oxidoreductase; KEGG: dde:Dde_3237 pyruvate:ferredoxin (flavodoxin) 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 [...] | 0.850 |
| DvMF_1860 | dnaK | DvMF_1860 | DvMF_2835 | PFAM: 4Fe-4S ferredoxin iron-sulfur binding domain protein; pyruvate ferredoxin/flavodoxin oxidoreductase; pyruvate flavodoxin/ferredoxin oxidoreductase domain protein; pyruvate:ferredoxin (flavodoxin) oxidoreductase; KEGG: dde:Dde_3237 pyruvate:ferredoxin (flavodoxin) oxidoreductase; Belongs to the pyruvate:ferredoxin/flavodoxin oxidoreductase family. | Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.616 |
| DvMF_1860 | groL | DvMF_1860 | DvMF_3064 | PFAM: 4Fe-4S ferredoxin iron-sulfur binding domain protein; pyruvate ferredoxin/flavodoxin oxidoreductase; pyruvate flavodoxin/ferredoxin oxidoreductase domain protein; pyruvate:ferredoxin (flavodoxin) oxidoreductase; KEGG: dde:Dde_3237 pyruvate:ferredoxin (flavodoxin) 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. | 0.767 |
| DvMF_1860 | grpE | DvMF_1860 | DvMF_1194 | PFAM: 4Fe-4S ferredoxin iron-sulfur binding domain protein; pyruvate ferredoxin/flavodoxin oxidoreductase; pyruvate flavodoxin/ferredoxin oxidoreductase domain protein; pyruvate:ferredoxin (flavodoxin) oxidoreductase; KEGG: dde:Dde_3237 pyruvate:ferredoxin (flavodoxin) 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 [...] | 0.565 |
| DvMF_1860 | htpG | DvMF_1860 | DvMF_1117 | PFAM: 4Fe-4S ferredoxin iron-sulfur binding domain protein; pyruvate ferredoxin/flavodoxin oxidoreductase; pyruvate flavodoxin/ferredoxin oxidoreductase domain protein; pyruvate:ferredoxin (flavodoxin) oxidoreductase; KEGG: dde:Dde_3237 pyruvate:ferredoxin (flavodoxin) oxidoreductase; Belongs to the pyruvate:ferredoxin/flavodoxin oxidoreductase family. | Heat shock protein Hsp90; Molecular chaperone. Has ATPase activity. | 0.458 |
| dnaJ | DvMF_0458 | DvMF_2295 | DvMF_0458 | 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 [...] | KEGG: dde:Dde_2099 ATPase; TIGRFAM: ATP-dependent Clp protease, ATP-binding subunit clpA; PFAM: AAA ATPase central domain protein; Clp domain protein; ATPase associated with various cellular activities AAA_5; ATPase AAA-2 domain protein; ATP-dependent Clp protease ATP-binding subunit clpA; SMART: AAA ATPase; Belongs to the ClpA/ClpB family. | 0.805 |
| dnaJ | DvMF_1860 | DvMF_2295 | DvMF_1860 | 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 [...] | PFAM: 4Fe-4S ferredoxin iron-sulfur binding domain protein; pyruvate ferredoxin/flavodoxin oxidoreductase; pyruvate flavodoxin/ferredoxin oxidoreductase domain protein; pyruvate:ferredoxin (flavodoxin) oxidoreductase; KEGG: dde:Dde_3237 pyruvate:ferredoxin (flavodoxin) oxidoreductase; Belongs to the pyruvate:ferredoxin/flavodoxin oxidoreductase family. | 0.850 |
| dnaJ | dnaK | DvMF_2295 | DvMF_2835 | 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. | 0.994 |
| dnaJ | groL | DvMF_2295 | DvMF_3064 | 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. | 0.894 |
| dnaJ | groS | DvMF_2295 | DvMF_3063 | 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. | 0.806 |
| dnaJ | grpE | DvMF_2295 | DvMF_1194 | 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 | DvMF_2295 | DvMF_0307 | 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. | 0.885 |