| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| ADQ04756.1 | ADQ04921.1 | Calow_1198 | Calow_1369 | KEGG: ate:Athe_1420 heat shock protein DnaJ domain protein; PFAM: heat shock protein DnaJ domain protein; SMART: heat shock protein DnaJ domain protein. | Thioredoxin; KEGG: csc:Csac_1727 thioredoxin; TIGRFAM: thioredoxin; PFAM: Thioredoxin domain-containing protein; Belongs to the thioredoxin family. | 0.435 |
| ADQ04756.1 | dnaK | Calow_1198 | Calow_1329 | KEGG: ate:Athe_1420 heat shock protein DnaJ domain protein; PFAM: heat shock protein DnaJ domain protein; SMART: heat shock protein DnaJ domain protein. | Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.992 |
| ADQ04756.1 | groL | Calow_1198 | Calow_1827 | KEGG: ate:Athe_1420 heat shock protein DnaJ domain protein; PFAM: heat shock protein DnaJ domain protein; SMART: heat shock protein DnaJ domain protein. | Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.869 |
| ADQ04756.1 | groS | Calow_1198 | Calow_1828 | KEGG: ate:Athe_1420 heat shock protein DnaJ domain protein; PFAM: heat shock protein DnaJ domain protein; SMART: heat shock protein DnaJ domain protein. | Chaperonin Cpn10; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.744 |
| ADQ04756.1 | grpE | Calow_1198 | Calow_1330 | KEGG: ate:Athe_1420 heat shock protein DnaJ domain protein; PFAM: heat shock protein DnaJ domain protein; SMART: heat shock protein DnaJ domain 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 [...] | 0.954 |
| ADQ04756.1 | hslU | Calow_1198 | Calow_1868 | KEGG: ate:Athe_1420 heat shock protein DnaJ domain protein; PFAM: heat shock protein DnaJ domain protein; SMART: heat shock protein DnaJ domain protein. | 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. | 0.651 |
| ADQ04756.1 | ldh | Calow_1198 | Calow_1634 | KEGG: ate:Athe_1420 heat shock protein DnaJ domain protein; PFAM: heat shock protein DnaJ domain protein; SMART: heat shock protein DnaJ domain protein. | L-lactate dehydrogenase; Catalyzes the conversion of lactate to pyruvate. Belongs to the LDH/MDH superfamily. LDH family. | 0.526 |
| ADQ04756.1 | lon | Calow_1198 | Calow_0742 | KEGG: ate:Athe_1420 heat shock protein DnaJ domain protein; PFAM: heat shock protein DnaJ domain protein; SMART: heat shock protein DnaJ domain protein. | ATP-dependent protease La; ATP-dependent serine protease that mediates the selective degradation of mutant and abnormal proteins as well as certain short- lived regulatory proteins. Required for cellular homeostasis and for survival from DNA damage and developmental changes induced by stress. Degrades polypeptides processively to yield small peptide fragments that are 5 to 10 amino acids long. Binds to DNA in a double-stranded, site-specific manner. | 0.673 |
| ADQ04921.1 | ADQ04756.1 | Calow_1369 | Calow_1198 | Thioredoxin; KEGG: csc:Csac_1727 thioredoxin; TIGRFAM: thioredoxin; PFAM: Thioredoxin domain-containing protein; Belongs to the thioredoxin family. | KEGG: ate:Athe_1420 heat shock protein DnaJ domain protein; PFAM: heat shock protein DnaJ domain protein; SMART: heat shock protein DnaJ domain protein. | 0.435 |
| ADQ04921.1 | dnaJ | Calow_1369 | Calow_1328 | Thioredoxin; KEGG: csc:Csac_1727 thioredoxin; TIGRFAM: thioredoxin; PFAM: Thioredoxin domain-containing protein; Belongs to the thioredoxin 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 [...] | 0.484 |
| ADQ04921.1 | dnaK | Calow_1369 | Calow_1329 | Thioredoxin; KEGG: csc:Csac_1727 thioredoxin; TIGRFAM: thioredoxin; PFAM: Thioredoxin domain-containing protein; Belongs to the thioredoxin family. | Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.642 |
| ADQ04921.1 | groL | Calow_1369 | Calow_1827 | Thioredoxin; KEGG: csc:Csac_1727 thioredoxin; TIGRFAM: thioredoxin; PFAM: Thioredoxin domain-containing protein; Belongs to the thioredoxin family. | Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.910 |
| ADQ04921.1 | groS | Calow_1369 | Calow_1828 | Thioredoxin; KEGG: csc:Csac_1727 thioredoxin; TIGRFAM: thioredoxin; PFAM: Thioredoxin domain-containing protein; Belongs to the thioredoxin family. | Chaperonin Cpn10; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.531 |
| ADQ04921.1 | grpE | Calow_1369 | Calow_1330 | Thioredoxin; KEGG: csc:Csac_1727 thioredoxin; TIGRFAM: thioredoxin; PFAM: Thioredoxin domain-containing protein; Belongs to the thioredoxin 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 [...] | 0.613 |
| ADQ04921.1 | hslU | Calow_1369 | Calow_1868 | Thioredoxin; KEGG: csc:Csac_1727 thioredoxin; TIGRFAM: thioredoxin; PFAM: Thioredoxin domain-containing protein; Belongs to the thioredoxin 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. | 0.592 |
| ADQ05379.1 | dnaK | Calow_1850 | Calow_1329 | KEGG: ate:Athe_2160 CheC, inhibitor of MCP methylation / FliN fusion protein; TIGRFAM: flagellar motor switch protein FliN; PFAM: surface presentation of antigens (SPOA) protein; CheC domain protein. | Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.425 |
| ADQ05379.1 | groL | Calow_1850 | Calow_1827 | KEGG: ate:Athe_2160 CheC, inhibitor of MCP methylation / FliN fusion protein; TIGRFAM: flagellar motor switch protein FliN; PFAM: surface presentation of antigens (SPOA) protein; CheC domain protein. | Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.877 |
| ADQ05379.1 | grpE | Calow_1850 | Calow_1330 | KEGG: ate:Athe_2160 CheC, inhibitor of MCP methylation / FliN fusion protein; TIGRFAM: flagellar motor switch protein FliN; PFAM: surface presentation of antigens (SPOA) protein; CheC domain 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 [...] | 0.413 |
| ADQ05379.1 | hslU | Calow_1850 | Calow_1868 | KEGG: ate:Athe_2160 CheC, inhibitor of MCP methylation / FliN fusion protein; TIGRFAM: flagellar motor switch protein FliN; PFAM: surface presentation of antigens (SPOA) protein; CheC domain protein. | 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. | 0.430 |
| dnaJ | ADQ04921.1 | Calow_1328 | Calow_1369 | 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 [...] | Thioredoxin; KEGG: csc:Csac_1727 thioredoxin; TIGRFAM: thioredoxin; PFAM: Thioredoxin domain-containing protein; Belongs to the thioredoxin family. | 0.484 |