node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
EET46396.1 | EET49443.1 | TR2A62_3274 | TR2A62_2349 | AAA ATPase, central domain protein. | Thioredoxin; Identified by match to protein family HMM PF00085. | 0.468 |
EET46396.1 | dnaJ | TR2A62_3274 | TR2A62_2538 | AAA ATPase, central domain 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 [...] | 0.804 |
EET46396.1 | dnaK | TR2A62_3274 | TR2A62_2537 | AAA ATPase, central domain protein. | Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.716 |
EET46396.1 | groL | TR2A62_3274 | TR2A62_3328 | AAA ATPase, central domain protein. | Chaperonin GroL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.707 |
EET46396.1 | groS | TR2A62_3274 | TR2A62_3327 | AAA ATPase, central domain protein. | Chaperonin GroS; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.414 |
EET46396.1 | grpE | TR2A62_3274 | TR2A62_2589 | AAA ATPase, central domain protein. | Co-chaperone GrpE; 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-depend [...] | 0.770 |
EET46396.1 | hslU | TR2A62_3274 | TR2A62_2611 | AAA ATPase, central 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. | 0.800 |
EET46396.1 | hslV | TR2A62_3274 | TR2A62_2612 | AAA ATPase, central domain protein. | ATP-dependent protease HslV; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.762 |
EET46396.1 | htpG | TR2A62_3274 | TR2A62_0262 | AAA ATPase, central domain protein. | Chaperone protein HtpG; Molecular chaperone. Has ATPase activity. | 0.755 |
EET49443.1 | EET46396.1 | TR2A62_2349 | TR2A62_3274 | Thioredoxin; Identified by match to protein family HMM PF00085. | AAA ATPase, central domain protein. | 0.468 |
EET49443.1 | dnaJ | TR2A62_2349 | TR2A62_2538 | Thioredoxin; Identified by match to protein family HMM PF00085. | 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 [...] | 0.721 |
EET49443.1 | dnaK | TR2A62_2349 | TR2A62_2537 | Thioredoxin; Identified by match to protein family HMM PF00085. | Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.634 |
EET49443.1 | groL | TR2A62_2349 | TR2A62_3328 | Thioredoxin; Identified by match to protein family HMM PF00085. | Chaperonin GroL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.763 |
EET49443.1 | groS | TR2A62_2349 | TR2A62_3327 | Thioredoxin; Identified by match to protein family HMM PF00085. | Chaperonin GroS; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.594 |
EET49443.1 | grpE | TR2A62_2349 | TR2A62_2589 | Thioredoxin; Identified by match to protein family HMM PF00085. | Co-chaperone GrpE; 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-depend [...] | 0.856 |
EET49443.1 | hslU | TR2A62_2349 | TR2A62_2611 | Thioredoxin; Identified by match to protein family HMM PF00085. | 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. | 0.871 |
EET49443.1 | hslV | TR2A62_2349 | TR2A62_2612 | Thioredoxin; Identified by match to protein family HMM PF00085. | ATP-dependent protease HslV; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.854 |
EET49443.1 | htpG | TR2A62_2349 | TR2A62_0262 | Thioredoxin; Identified by match to protein family HMM PF00085. | Chaperone protein HtpG; Molecular chaperone. Has ATPase activity. | 0.810 |
EET49443.1 | lon | TR2A62_2349 | TR2A62_1091 | Thioredoxin; Identified by match to protein family HMM PF00085. | 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. | 0.468 |
dnaJ | EET46396.1 | TR2A62_2538 | TR2A62_3274 | 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 [...] | AAA ATPase, central domain protein. | 0.804 |