node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
ADK80717.1 | ADK81230.1 | Spirs_1590 | Spirs_2110 | Heat shock protein 70; COGs: COG0443 Molecular chaperone; InterPro IPR001023:IPR013126:IPR018181; KEGG: tit:Thit_0894 chaperone protein DnaK; PFAM: Heat shock protein 70; SPTR: Chaperone protein DnaK; PFAM: Hsp70 protein. | Heat shock protein DnaJ domain protein; COGs: COG0484 DnaJ-class molecular chaperone with C-terminal Zn finger domain; InterPro IPR001623; KEGG: ere:EUBREC_2351 chaperone protein DnaJ; PFAM: heat shock protein DnaJ domain protein; SMART: heat shock protein DnaJ domain protein; SPTR: Putative uncharacterized protein; PFAM: DnaJ domain. | 0.938 |
ADK80717.1 | dnaJ | Spirs_1590 | Spirs_3197 | Heat shock protein 70; COGs: COG0443 Molecular chaperone; InterPro IPR001023:IPR013126:IPR018181; KEGG: tit:Thit_0894 chaperone protein DnaK; PFAM: Heat shock protein 70; SPTR: Chaperone protein DnaK; 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 [...] | 0.961 |
ADK80717.1 | dnaK | Spirs_1590 | Spirs_2108 | Heat shock protein 70; COGs: COG0443 Molecular chaperone; InterPro IPR001023:IPR013126:IPR018181; KEGG: tit:Thit_0894 chaperone protein DnaK; PFAM: Heat shock protein 70; SPTR: Chaperone protein DnaK; PFAM: Hsp70 protein. | Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.909 |
ADK80717.1 | dnaK-2 | Spirs_1590 | Spirs_3198 | Heat shock protein 70; COGs: COG0443 Molecular chaperone; InterPro IPR001023:IPR013126:IPR018181; KEGG: tit:Thit_0894 chaperone protein DnaK; PFAM: Heat shock protein 70; SPTR: Chaperone protein DnaK; PFAM: Hsp70 protein. | Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.910 |
ADK80717.1 | groL | Spirs_1590 | Spirs_3240 | Heat shock protein 70; COGs: COG0443 Molecular chaperone; InterPro IPR001023:IPR013126:IPR018181; KEGG: tit:Thit_0894 chaperone protein DnaK; PFAM: Heat shock protein 70; SPTR: Chaperone protein DnaK; PFAM: Hsp70 protein. | Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.943 |
ADK80717.1 | groS | Spirs_1590 | Spirs_1713 | Heat shock protein 70; COGs: COG0443 Molecular chaperone; InterPro IPR001023:IPR013126:IPR018181; KEGG: tit:Thit_0894 chaperone protein DnaK; PFAM: Heat shock protein 70; SPTR: Chaperone protein DnaK; PFAM: Hsp70 protein. | Chaperonin Cpn10; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.888 |
ADK80717.1 | grpE | Spirs_1590 | Spirs_3199 | Heat shock protein 70; COGs: COG0443 Molecular chaperone; InterPro IPR001023:IPR013126:IPR018181; KEGG: tit:Thit_0894 chaperone protein DnaK; PFAM: Heat shock protein 70; SPTR: Chaperone protein DnaK; PFAM: Hsp70 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 [...] | 0.988 |
ADK80717.1 | hslU | Spirs_1590 | Spirs_1558 | Heat shock protein 70; COGs: COG0443 Molecular chaperone; InterPro IPR001023:IPR013126:IPR018181; KEGG: tit:Thit_0894 chaperone protein DnaK; PFAM: Heat shock protein 70; SPTR: Chaperone protein DnaK; PFAM: Hsp70 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. | 0.635 |
ADK80717.1 | hslV | Spirs_1590 | Spirs_1557 | Heat shock protein 70; COGs: COG0443 Molecular chaperone; InterPro IPR001023:IPR013126:IPR018181; KEGG: tit:Thit_0894 chaperone protein DnaK; PFAM: Heat shock protein 70; SPTR: Chaperone protein DnaK; PFAM: Hsp70 protein. | 20S proteasome A and B subunits; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.523 |
ADK81230.1 | ADK80717.1 | Spirs_2110 | Spirs_1590 | Heat shock protein DnaJ domain protein; COGs: COG0484 DnaJ-class molecular chaperone with C-terminal Zn finger domain; InterPro IPR001623; KEGG: ere:EUBREC_2351 chaperone protein DnaJ; PFAM: heat shock protein DnaJ domain protein; SMART: heat shock protein DnaJ domain protein; SPTR: Putative uncharacterized protein; PFAM: DnaJ domain. | Heat shock protein 70; COGs: COG0443 Molecular chaperone; InterPro IPR001023:IPR013126:IPR018181; KEGG: tit:Thit_0894 chaperone protein DnaK; PFAM: Heat shock protein 70; SPTR: Chaperone protein DnaK; PFAM: Hsp70 protein. | 0.938 |
ADK81230.1 | ADK82912.1 | Spirs_2110 | Spirs_3826 | Heat shock protein DnaJ domain protein; COGs: COG0484 DnaJ-class molecular chaperone with C-terminal Zn finger domain; InterPro IPR001623; KEGG: ere:EUBREC_2351 chaperone protein DnaJ; PFAM: heat shock protein DnaJ domain protein; SMART: heat shock protein DnaJ domain protein; SPTR: Putative uncharacterized protein; PFAM: DnaJ domain. | InterPro IPR002482:IPR018392; KEGG: tde:TDE2281 LysM domain-containing protein; PFAM: Peptidoglycan-binding lysin domain; SMART: Peptidoglycan-binding LysM; SPTR: LysM domain protein; PFAM: Hsp70 protein; LysM domain. | 0.832 |
ADK81230.1 | dnaK | Spirs_2110 | Spirs_2108 | Heat shock protein DnaJ domain protein; COGs: COG0484 DnaJ-class molecular chaperone with C-terminal Zn finger domain; InterPro IPR001623; KEGG: ere:EUBREC_2351 chaperone protein DnaJ; PFAM: heat shock protein DnaJ domain protein; SMART: heat shock protein DnaJ domain protein; SPTR: Putative uncharacterized protein; PFAM: DnaJ domain. | Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.984 |
ADK81230.1 | dnaK-2 | Spirs_2110 | Spirs_3198 | Heat shock protein DnaJ domain protein; COGs: COG0484 DnaJ-class molecular chaperone with C-terminal Zn finger domain; InterPro IPR001623; KEGG: ere:EUBREC_2351 chaperone protein DnaJ; PFAM: heat shock protein DnaJ domain protein; SMART: heat shock protein DnaJ domain protein; SPTR: Putative uncharacterized protein; PFAM: DnaJ domain. | Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.933 |
ADK81230.1 | groL | Spirs_2110 | Spirs_3240 | Heat shock protein DnaJ domain protein; COGs: COG0484 DnaJ-class molecular chaperone with C-terminal Zn finger domain; InterPro IPR001623; KEGG: ere:EUBREC_2351 chaperone protein DnaJ; PFAM: heat shock protein DnaJ domain protein; SMART: heat shock protein DnaJ domain protein; SPTR: Putative uncharacterized protein; PFAM: DnaJ domain. | Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.700 |
ADK81230.1 | groS | Spirs_2110 | Spirs_1713 | Heat shock protein DnaJ domain protein; COGs: COG0484 DnaJ-class molecular chaperone with C-terminal Zn finger domain; InterPro IPR001623; KEGG: ere:EUBREC_2351 chaperone protein DnaJ; PFAM: heat shock protein DnaJ domain protein; SMART: heat shock protein DnaJ domain protein; SPTR: Putative uncharacterized protein; PFAM: DnaJ domain. | Chaperonin Cpn10; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.635 |
ADK81230.1 | grpE | Spirs_2110 | Spirs_3199 | Heat shock protein DnaJ domain protein; COGs: COG0484 DnaJ-class molecular chaperone with C-terminal Zn finger domain; InterPro IPR001623; KEGG: ere:EUBREC_2351 chaperone protein DnaJ; PFAM: heat shock protein DnaJ domain protein; SMART: heat shock protein DnaJ domain protein; SPTR: Putative uncharacterized protein; PFAM: DnaJ 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 [...] | 0.904 |
ADK81230.1 | hslU | Spirs_2110 | Spirs_1558 | Heat shock protein DnaJ domain protein; COGs: COG0484 DnaJ-class molecular chaperone with C-terminal Zn finger domain; InterPro IPR001623; KEGG: ere:EUBREC_2351 chaperone protein DnaJ; PFAM: heat shock protein DnaJ domain protein; SMART: heat shock protein DnaJ domain protein; SPTR: Putative uncharacterized protein; PFAM: DnaJ 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. | 0.639 |
ADK81230.1 | hslV | Spirs_2110 | Spirs_1557 | Heat shock protein DnaJ domain protein; COGs: COG0484 DnaJ-class molecular chaperone with C-terminal Zn finger domain; InterPro IPR001623; KEGG: ere:EUBREC_2351 chaperone protein DnaJ; PFAM: heat shock protein DnaJ domain protein; SMART: heat shock protein DnaJ domain protein; SPTR: Putative uncharacterized protein; PFAM: DnaJ domain. | 20S proteasome A and B subunits; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.457 |
ADK82912.1 | ADK81230.1 | Spirs_3826 | Spirs_2110 | InterPro IPR002482:IPR018392; KEGG: tde:TDE2281 LysM domain-containing protein; PFAM: Peptidoglycan-binding lysin domain; SMART: Peptidoglycan-binding LysM; SPTR: LysM domain protein; PFAM: Hsp70 protein; LysM domain. | Heat shock protein DnaJ domain protein; COGs: COG0484 DnaJ-class molecular chaperone with C-terminal Zn finger domain; InterPro IPR001623; KEGG: ere:EUBREC_2351 chaperone protein DnaJ; PFAM: heat shock protein DnaJ domain protein; SMART: heat shock protein DnaJ domain protein; SPTR: Putative uncharacterized protein; PFAM: DnaJ domain. | 0.832 |
ADK82912.1 | dnaJ | Spirs_3826 | Spirs_3197 | InterPro IPR002482:IPR018392; KEGG: tde:TDE2281 LysM domain-containing protein; PFAM: Peptidoglycan-binding lysin domain; SMART: Peptidoglycan-binding LysM; SPTR: LysM domain protein; PFAM: Hsp70 protein; LysM 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 [...] | 0.857 |