node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
Acry_1376 | Acry_2127 | Acry_1376 | Acry_2127 | Chaperonin Cpn60/TCP-1; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. Belongs to the chaperonin (HSP60) family. | PFAM: Thioredoxin domain. | 0.601 |
Acry_1376 | dnaJ | Acry_1376 | Acry_1645 | Chaperonin Cpn60/TCP-1; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. Belongs to the chaperonin (HSP60) 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 [...] | 0.868 |
Acry_1376 | dnaK | Acry_1376 | Acry_1646 | Chaperonin Cpn60/TCP-1; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. Belongs to the chaperonin (HSP60) family. | Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.927 |
Acry_1376 | groL | Acry_1376 | Acry_2503 | Chaperonin Cpn60/TCP-1; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. Belongs to the chaperonin (HSP60) family. | Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.910 |
Acry_1376 | groS | Acry_1376 | Acry_2504 | Chaperonin Cpn60/TCP-1; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. Belongs to the chaperonin (HSP60) family. | Chaperonin Cpn10; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.991 |
Acry_1376 | grpE | Acry_1376 | Acry_1647 | Chaperonin Cpn60/TCP-1; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. Belongs to the chaperonin (HSP60) 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 [...] | 0.878 |
Acry_1376 | hslU | Acry_1376 | Acry_1409 | Chaperonin Cpn60/TCP-1; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. Belongs to the chaperonin (HSP60) 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. | 0.778 |
Acry_1376 | hslV | Acry_1376 | Acry_1410 | Chaperonin Cpn60/TCP-1; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. Belongs to the chaperonin (HSP60) family. | HslV component of HslUV peptidase, Threonine peptidase, MEROPS family T01B; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.723 |
Acry_1376 | htpG | Acry_1376 | Acry_3087 | Chaperonin Cpn60/TCP-1; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. Belongs to the chaperonin (HSP60) family. | Heat shock protein Hsp90; Molecular chaperone. Has ATPase activity. | 0.826 |
Acry_1376 | lon | Acry_1376 | Acry_0919 | Chaperonin Cpn60/TCP-1; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. Belongs to the chaperonin (HSP60) family. | ATP-dependent proteinase, Serine peptidase, MEROPS family S16; 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. | 0.765 |
Acry_2127 | Acry_1376 | Acry_2127 | Acry_1376 | PFAM: Thioredoxin domain. | Chaperonin Cpn60/TCP-1; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. Belongs to the chaperonin (HSP60) family. | 0.601 |
Acry_2127 | dnaJ | Acry_2127 | Acry_1645 | PFAM: Thioredoxin domain. | 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 [...] | 0.754 |
Acry_2127 | dnaK | Acry_2127 | Acry_1646 | PFAM: Thioredoxin domain. | Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.501 |
Acry_2127 | groL | Acry_2127 | Acry_2503 | PFAM: Thioredoxin domain. | Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.619 |
Acry_2127 | groS | Acry_2127 | Acry_2504 | PFAM: Thioredoxin domain. | Chaperonin Cpn10; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.596 |
Acry_2127 | grpE | Acry_2127 | Acry_1647 | PFAM: Thioredoxin domain. | 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 [...] | 0.799 |
Acry_2127 | hslU | Acry_2127 | Acry_1409 | PFAM: Thioredoxin domain. | 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. | 0.809 |
Acry_2127 | hslV | Acry_2127 | Acry_1410 | PFAM: Thioredoxin domain. | HslV component of HslUV peptidase, Threonine peptidase, MEROPS family T01B; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.802 |
Acry_2127 | htpG | Acry_2127 | Acry_3087 | PFAM: Thioredoxin domain. | Heat shock protein Hsp90; Molecular chaperone. Has ATPase activity. | 0.765 |
Acry_2127 | lon | Acry_2127 | Acry_0919 | PFAM: Thioredoxin domain. | ATP-dependent proteinase, Serine peptidase, MEROPS family S16; 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. | 0.514 |