node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
AGA85883.1 | AGA87532.1 | Psest_1325 | Psest_3034 | Molecular chaperone; PFAM: Hsp70 protein. | DnaJ-class molecular chaperone with C-terminal Zn finger domain; PFAM: DnaJ domain; DNA-J related protein. | 0.931 |
AGA85883.1 | dnaJ | Psest_1325 | Psest_0965 | Molecular chaperone; PFAM: Hsp70 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 [...] | 0.949 |
AGA85883.1 | groL | Psest_1325 | Psest_1151 | Molecular chaperone; PFAM: Hsp70 protein. | Chaperonin GroL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.932 |
AGA85883.1 | groS | Psest_1325 | Psest_1150 | Molecular chaperone; PFAM: Hsp70 protein. | Co-chaperonin GroES; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.887 |
AGA85883.1 | grpE | Psest_1325 | Psest_0963 | Molecular chaperone; PFAM: Hsp70 protein. | Molecular chaperone GrpE (heat shock 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. [...] | 0.959 |
AGA85883.1 | hslU | Psest_1325 | Psest_3937 | Molecular chaperone; PFAM: Hsp70 protein. | ATP-dependent protease HslVU, ATPase subunit; 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. | 0.622 |
AGA85883.1 | hslV | Psest_1325 | Psest_3936 | Molecular chaperone; PFAM: Hsp70 protein. | HslV component of HslUV peptidase; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.508 |
AGA85883.1 | htpG | Psest_1325 | Psest_2484 | Molecular chaperone; PFAM: Hsp70 protein. | Molecular chaperone of HSP90 family; Molecular chaperone. Has ATPase activity. | 0.972 |
AGA87532.1 | AGA85883.1 | Psest_3034 | Psest_1325 | DnaJ-class molecular chaperone with C-terminal Zn finger domain; PFAM: DnaJ domain; DNA-J related protein. | Molecular chaperone; PFAM: Hsp70 protein. | 0.931 |
AGA87532.1 | dnaK | Psest_3034 | Psest_0964 | DnaJ-class molecular chaperone with C-terminal Zn finger domain; PFAM: DnaJ domain; DNA-J related protein. | Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.931 |
AGA87532.1 | groL | Psest_3034 | Psest_1151 | DnaJ-class molecular chaperone with C-terminal Zn finger domain; PFAM: DnaJ domain; DNA-J related protein. | Chaperonin GroL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.874 |
AGA87532.1 | groS | Psest_3034 | Psest_1150 | DnaJ-class molecular chaperone with C-terminal Zn finger domain; PFAM: DnaJ domain; DNA-J related protein. | Co-chaperonin GroES; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.763 |
AGA87532.1 | grpE | Psest_3034 | Psest_0963 | DnaJ-class molecular chaperone with C-terminal Zn finger domain; PFAM: DnaJ domain; DNA-J related protein. | Molecular chaperone GrpE (heat shock 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. [...] | 0.938 |
AGA87532.1 | hscA | Psest_3034 | Psest_1255 | DnaJ-class molecular chaperone with C-terminal Zn finger domain; PFAM: DnaJ domain; DNA-J related protein. | Fe-S protein assembly chaperone HscA; Chaperone involved in the maturation of iron-sulfur cluster- containing proteins. Has a low intrinsic ATPase activity which is markedly stimulated by HscB. | 0.931 |
AGA87532.1 | hslU | Psest_3034 | Psest_3937 | DnaJ-class molecular chaperone with C-terminal Zn finger domain; PFAM: DnaJ domain; DNA-J related protein. | ATP-dependent protease HslVU, ATPase subunit; 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. | 0.805 |
AGA87532.1 | hslV | Psest_3034 | Psest_3936 | DnaJ-class molecular chaperone with C-terminal Zn finger domain; PFAM: DnaJ domain; DNA-J related protein. | HslV component of HslUV peptidase; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.667 |
AGA87532.1 | htpG | Psest_3034 | Psest_2484 | DnaJ-class molecular chaperone with C-terminal Zn finger domain; PFAM: DnaJ domain; DNA-J related protein. | Molecular chaperone of HSP90 family; Molecular chaperone. Has ATPase activity. | 0.968 |
dnaJ | AGA85883.1 | Psest_0965 | Psest_1325 | 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 [...] | Molecular chaperone; PFAM: Hsp70 protein. | 0.949 |
dnaJ | dnaK | Psest_0965 | Psest_0964 | 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. | 0.997 |
dnaJ | groL | Psest_0965 | Psest_1151 | 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 GroL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.935 |