| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| ADU47849.1 | ADU49780.1 | Intca_1333 | Intca_3297 | Chaperonin Cpn10; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter; Belongs to the GroES chaperonin family. | COGs: COG0484 DnaJ-class molecular chaperone with C-terminal Zn finger domain; InterProIPR018260: IPR018253: IPR001623: IPR003095: IPR 002939; KEGG: kra:Krad_4231 chaperone DnaJ domain protein; PFAM: chaperone DnaJ domain protein; heat shock protein DnaJ domain protein; SMART: heat shock protein DnaJ domain protein; SPTR: DnaJ protein; PFAM: DnaJ C terminal region; DnaJ domain. | 0.581 |
| ADU47849.1 | dnaJ | Intca_1333 | Intca_2143 | Chaperonin Cpn10; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter; Belongs to the GroES chaperonin family. | Chaperone DnaJ domain protein; 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 [...] | 0.581 |
| ADU47849.1 | dnaK | Intca_1333 | Intca_3299 | Chaperonin Cpn10; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter; Belongs to the GroES chaperonin family. | Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.902 |
| ADU47849.1 | groL | Intca_1333 | Intca_1017 | Chaperonin Cpn10; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter; Belongs to the GroES chaperonin family. | Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.947 |
| ADU47849.1 | groL-2 | Intca_1333 | Intca_2857 | Chaperonin Cpn10; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter; Belongs to the GroES chaperonin family. | Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.947 |
| ADU47849.1 | grpE | Intca_1333 | Intca_3298 | Chaperonin Cpn10; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter; Belongs to the GroES chaperonin 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 [...] | 0.863 |
| ADU48984.1 | dnaK | Intca_2477 | Intca_3299 | COGs: COG0567 2-oxoglutarate dehydrogenase complex dehydrogenase (E1); InterProIPR011603: IPR001078: IPR001017: IPR005475: IPR 000897; KEGG: kra:Krad_1228 alpha-ketoglutarate decarboxylase; PFAM: Transketolase central region; dehydrogenase E1 component; catalytic domain-containing protein of components of various dehydrogenase complexes; SPTR: Alpha-ketoglutarate decarboxylase; TIGRFAM: 2-oxoglutarate dehydrogenase, E1 subunit; PFAM: 2-oxoacid dehydrogenases acyltransferase (catalytic domain); Dehydrogenase E1 component; Transketolase, pyrimidine binding domain; TIGRFAM: 2-oxoglutarate [...] | Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.853 |
| ADU48984.1 | groL | Intca_2477 | Intca_1017 | COGs: COG0567 2-oxoglutarate dehydrogenase complex dehydrogenase (E1); InterProIPR011603: IPR001078: IPR001017: IPR005475: IPR 000897; KEGG: kra:Krad_1228 alpha-ketoglutarate decarboxylase; PFAM: Transketolase central region; dehydrogenase E1 component; catalytic domain-containing protein of components of various dehydrogenase complexes; SPTR: Alpha-ketoglutarate decarboxylase; TIGRFAM: 2-oxoglutarate dehydrogenase, E1 subunit; PFAM: 2-oxoacid dehydrogenases acyltransferase (catalytic domain); Dehydrogenase E1 component; Transketolase, pyrimidine binding domain; TIGRFAM: 2-oxoglutarate [...] | Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.779 |
| ADU48984.1 | groL-2 | Intca_2477 | Intca_2857 | COGs: COG0567 2-oxoglutarate dehydrogenase complex dehydrogenase (E1); InterProIPR011603: IPR001078: IPR001017: IPR005475: IPR 000897; KEGG: kra:Krad_1228 alpha-ketoglutarate decarboxylase; PFAM: Transketolase central region; dehydrogenase E1 component; catalytic domain-containing protein of components of various dehydrogenase complexes; SPTR: Alpha-ketoglutarate decarboxylase; TIGRFAM: 2-oxoglutarate dehydrogenase, E1 subunit; PFAM: 2-oxoacid dehydrogenases acyltransferase (catalytic domain); Dehydrogenase E1 component; Transketolase, pyrimidine binding domain; TIGRFAM: 2-oxoglutarate [...] | Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.779 |
| ADU49506.1 | dnaK | Intca_3016 | Intca_3299 | COGs: COG3261 Ni Fe-hydrogenase III large subunit; InterPro IPR001268: IPR020396; KEGG: tcu:Tcur_4707 NADH dehydrogenase (ubiquinone) 30 kDa subunit; PFAM: NADH dehydrogenase (ubiquinone) 30 kDa subunit; SPTR: NADH dehydrogenase (Ubiquinone) 30 kDa subunit; PFAM: Respiratory-chain NADH dehydrogenase, 30 Kd subunit; Respiratory-chain NADH dehydrogenase, 49 Kd subunit; Nickel-dependent hydrogenase. | Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.443 |
| ADU49506.1 | groL | Intca_3016 | Intca_1017 | COGs: COG3261 Ni Fe-hydrogenase III large subunit; InterPro IPR001268: IPR020396; KEGG: tcu:Tcur_4707 NADH dehydrogenase (ubiquinone) 30 kDa subunit; PFAM: NADH dehydrogenase (ubiquinone) 30 kDa subunit; SPTR: NADH dehydrogenase (Ubiquinone) 30 kDa subunit; PFAM: Respiratory-chain NADH dehydrogenase, 30 Kd subunit; Respiratory-chain NADH dehydrogenase, 49 Kd subunit; Nickel-dependent hydrogenase. | Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.883 |
| ADU49506.1 | groL-2 | Intca_3016 | Intca_2857 | COGs: COG3261 Ni Fe-hydrogenase III large subunit; InterPro IPR001268: IPR020396; KEGG: tcu:Tcur_4707 NADH dehydrogenase (ubiquinone) 30 kDa subunit; PFAM: NADH dehydrogenase (ubiquinone) 30 kDa subunit; SPTR: NADH dehydrogenase (Ubiquinone) 30 kDa subunit; PFAM: Respiratory-chain NADH dehydrogenase, 30 Kd subunit; Respiratory-chain NADH dehydrogenase, 49 Kd subunit; Nickel-dependent hydrogenase. | Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.883 |
| ADU49780.1 | ADU47849.1 | Intca_3297 | Intca_1333 | COGs: COG0484 DnaJ-class molecular chaperone with C-terminal Zn finger domain; InterProIPR018260: IPR018253: IPR001623: IPR003095: IPR 002939; KEGG: kra:Krad_4231 chaperone DnaJ domain protein; PFAM: chaperone DnaJ domain protein; heat shock protein DnaJ domain protein; SMART: heat shock protein DnaJ domain protein; SPTR: DnaJ protein; PFAM: DnaJ C terminal region; DnaJ domain. | Chaperonin Cpn10; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter; Belongs to the GroES chaperonin family. | 0.581 |
| ADU49780.1 | dnaK | Intca_3297 | Intca_3299 | COGs: COG0484 DnaJ-class molecular chaperone with C-terminal Zn finger domain; InterProIPR018260: IPR018253: IPR001623: IPR003095: IPR 002939; KEGG: kra:Krad_4231 chaperone DnaJ domain protein; PFAM: chaperone DnaJ domain protein; heat shock protein DnaJ domain protein; SMART: heat shock protein DnaJ domain protein; SPTR: DnaJ protein; PFAM: DnaJ C terminal region; DnaJ domain. | Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.999 |
| ADU49780.1 | groL | Intca_3297 | Intca_1017 | COGs: COG0484 DnaJ-class molecular chaperone with C-terminal Zn finger domain; InterProIPR018260: IPR018253: IPR001623: IPR003095: IPR 002939; KEGG: kra:Krad_4231 chaperone DnaJ domain protein; PFAM: chaperone DnaJ domain protein; heat shock protein DnaJ domain protein; SMART: heat shock protein DnaJ domain protein; SPTR: DnaJ protein; PFAM: DnaJ C terminal region; DnaJ domain. | Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.831 |
| ADU49780.1 | groL-2 | Intca_3297 | Intca_2857 | COGs: COG0484 DnaJ-class molecular chaperone with C-terminal Zn finger domain; InterProIPR018260: IPR018253: IPR001623: IPR003095: IPR 002939; KEGG: kra:Krad_4231 chaperone DnaJ domain protein; PFAM: chaperone DnaJ domain protein; heat shock protein DnaJ domain protein; SMART: heat shock protein DnaJ domain protein; SPTR: DnaJ protein; PFAM: DnaJ C terminal region; DnaJ domain. | Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.833 |
| ADU49780.1 | groS | Intca_3297 | Intca_1016 | COGs: COG0484 DnaJ-class molecular chaperone with C-terminal Zn finger domain; InterProIPR018260: IPR018253: IPR001623: IPR003095: IPR 002939; KEGG: kra:Krad_4231 chaperone DnaJ domain protein; PFAM: chaperone DnaJ domain protein; heat shock protein DnaJ domain protein; SMART: heat shock protein DnaJ domain protein; SPTR: DnaJ protein; PFAM: DnaJ C terminal region; DnaJ domain. | Chaperonin Cpn10; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.684 |
| ADU49780.1 | grpE | Intca_3297 | Intca_3298 | COGs: COG0484 DnaJ-class molecular chaperone with C-terminal Zn finger domain; InterProIPR018260: IPR018253: IPR001623: IPR003095: IPR 002939; KEGG: kra:Krad_4231 chaperone DnaJ domain protein; PFAM: chaperone DnaJ domain protein; heat shock protein DnaJ domain protein; SMART: heat shock protein DnaJ domain protein; SPTR: DnaJ protein; PFAM: DnaJ C terminal region; 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 [...] | 0.983 |
| dnaJ | ADU47849.1 | Intca_2143 | Intca_1333 | Chaperone DnaJ domain protein; 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 [...] | Chaperonin Cpn10; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter; Belongs to the GroES chaperonin family. | 0.581 |
| dnaJ | dnaK | Intca_2143 | Intca_3299 | Chaperone DnaJ domain protein; 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 [...] | Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.996 |