node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
Dde_1659 | clpP | Dde_1659 | Dde_2220 | KEGG: dvm:DvMF_0569 chaperone DnaJ domain protein; PFAM: Chaperone DnaJ, C-terminal; Heat shock protein DnaJ, N-terminal; SMART: Heat shock protein DnaJ, N-terminal. | ATP-dependent Clp protease, proteolytic subunit ClpP; Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins. Belongs to the peptidase S14 family. | 0.489 |
Dde_1659 | dnaK | Dde_1659 | Dde_1023 | KEGG: dvm:DvMF_0569 chaperone DnaJ domain protein; PFAM: Chaperone DnaJ, C-terminal; Heat shock protein DnaJ, N-terminal; SMART: Heat shock protein DnaJ, N-terminal. | Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.993 |
Dde_1659 | groL | Dde_1659 | Dde_2473 | KEGG: dvm:DvMF_0569 chaperone DnaJ domain protein; PFAM: Chaperone DnaJ, C-terminal; Heat shock protein DnaJ, N-terminal; SMART: Heat shock protein DnaJ, N-terminal. | Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.788 |
Dde_1659 | groS | Dde_1659 | Dde_2474 | KEGG: dvm:DvMF_0569 chaperone DnaJ domain protein; PFAM: Chaperone DnaJ, C-terminal; Heat shock protein DnaJ, N-terminal; SMART: Heat shock protein DnaJ, N-terminal. | Chaperonin Cpn10; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.716 |
Dde_1659 | grpE | Dde_1659 | Dde_1025 | KEGG: dvm:DvMF_0569 chaperone DnaJ domain protein; PFAM: Chaperone DnaJ, C-terminal; Heat shock protein DnaJ, N-terminal; SMART: Heat shock protein DnaJ, N-terminal. | 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 [...] | 0.947 |
Dde_1659 | hrcA | Dde_1659 | Dde_1026 | KEGG: dvm:DvMF_0569 chaperone DnaJ domain protein; PFAM: Chaperone DnaJ, C-terminal; Heat shock protein DnaJ, N-terminal; SMART: Heat shock protein DnaJ, N-terminal. | Heat-inducible transcription repressor HrcA; Negative regulator of class I heat shock genes (grpE-dnaK- dnaJ and groELS operons). Prevents heat-shock induction of these operons. | 0.691 |
Dde_1659 | hslU | Dde_1659 | Dde_2014 | KEGG: dvm:DvMF_0569 chaperone DnaJ domain protein; PFAM: Chaperone DnaJ, C-terminal; Heat shock protein DnaJ, N-terminal; SMART: Heat shock protein DnaJ, N-terminal. | 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. | 0.639 |
Dde_1659 | hslV | Dde_1659 | Dde_2124 | KEGG: dvm:DvMF_0569 chaperone DnaJ domain protein; PFAM: Chaperone DnaJ, C-terminal; Heat shock protein DnaJ, N-terminal; SMART: Heat shock protein DnaJ, N-terminal. | 20S proteasome A and B subunits; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.547 |
Dde_1659 | htpG | Dde_1659 | Dde_1147 | KEGG: dvm:DvMF_0569 chaperone DnaJ domain protein; PFAM: Chaperone DnaJ, C-terminal; Heat shock protein DnaJ, N-terminal; SMART: Heat shock protein DnaJ, N-terminal. | ATP-binding region ATPase domain protein; Molecular chaperone. Has ATPase activity. | 0.874 |
clpP | Dde_1659 | Dde_2220 | Dde_1659 | ATP-dependent Clp protease, proteolytic subunit ClpP; Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins. Belongs to the peptidase S14 family. | KEGG: dvm:DvMF_0569 chaperone DnaJ domain protein; PFAM: Chaperone DnaJ, C-terminal; Heat shock protein DnaJ, N-terminal; SMART: Heat shock protein DnaJ, N-terminal. | 0.489 |
clpP | dnaJ | Dde_2220 | Dde_0248 | ATP-dependent Clp protease, proteolytic subunit ClpP; Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins. Belongs to the peptidase S14 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 [...] | 0.618 |
clpP | dnaK | Dde_2220 | Dde_1023 | ATP-dependent Clp protease, proteolytic subunit ClpP; Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins. Belongs to the peptidase S14 family. | Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.884 |
clpP | groL | Dde_2220 | Dde_2473 | ATP-dependent Clp protease, proteolytic subunit ClpP; Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins. Belongs to the peptidase S14 family. | Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.811 |
clpP | groS | Dde_2220 | Dde_2474 | ATP-dependent Clp protease, proteolytic subunit ClpP; Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins. Belongs to the peptidase S14 family. | Chaperonin Cpn10; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.880 |
clpP | grpE | Dde_2220 | Dde_1025 | ATP-dependent Clp protease, proteolytic subunit ClpP; Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins. Belongs to the peptidase S14 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 [...] | 0.854 |
clpP | hrcA | Dde_2220 | Dde_1026 | ATP-dependent Clp protease, proteolytic subunit ClpP; Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins. Belongs to the peptidase S14 family. | Heat-inducible transcription repressor HrcA; Negative regulator of class I heat shock genes (grpE-dnaK- dnaJ and groELS operons). Prevents heat-shock induction of these operons. | 0.914 |
clpP | hslU | Dde_2220 | Dde_2014 | ATP-dependent Clp protease, proteolytic subunit ClpP; Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins. Belongs to the peptidase S14 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. | 0.495 |
clpP | hslV | Dde_2220 | Dde_2124 | ATP-dependent Clp protease, proteolytic subunit ClpP; Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins. Belongs to the peptidase S14 family. | 20S proteasome A and B subunits; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.731 |
clpP | htpG | Dde_2220 | Dde_1147 | ATP-dependent Clp protease, proteolytic subunit ClpP; Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins. Belongs to the peptidase S14 family. | ATP-binding region ATPase domain protein; Molecular chaperone. Has ATPase activity. | 0.533 |
dnaJ | clpP | Dde_0248 | Dde_2220 | 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 [...] | ATP-dependent Clp protease, proteolytic subunit ClpP; Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins. Belongs to the peptidase S14 family. | 0.618 |