| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| CEO16776.1 | ctaC | RMONA_01835 | RMONA_05015 | SCO1/SenC protein precursor. | Cytochrome c oxidase subunit 2 precursor; Subunits I and II form the functional core of the enzyme complex. Electrons originating in cytochrome c are transferred via heme a and Cu(A) to the binuclear center formed by heme a3 and Cu(B). | 0.872 |
| CEO16776.1 | tlpA | RMONA_01835 | RMONA_06300 | SCO1/SenC protein precursor. | Thiol:disulfide interchange protein TlpA. | 0.831 |
| CEO17154.1 | dnaK | RMONA_03835 | RMONA_03615 | Hypothetical protein. | Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.982 |
| CEO17154.1 | hscA | RMONA_03835 | RMONA_00860 | Hypothetical protein. | Chaperone protein HscA; Chaperone involved in the maturation of iron-sulfur cluster- containing proteins. Has a low intrinsic ATPase activity which is markedly stimulated by HscB. | 0.982 |
| CEO17154.1 | tlpA | RMONA_03835 | RMONA_06300 | Hypothetical protein. | Thiol:disulfide interchange protein TlpA. | 0.807 |
| CEO17154.1 | tsaA | RMONA_03835 | RMONA_07595 | Hypothetical protein. | Putative peroxiredoxin. | 0.423 |
| CEO17759.1 | ctaC | RMONA_07035 | RMONA_05015 | SCO1 protein homolog precursor. | Cytochrome c oxidase subunit 2 precursor; Subunits I and II form the functional core of the enzyme complex. Electrons originating in cytochrome c are transferred via heme a and Cu(A) to the binuclear center formed by heme a3 and Cu(B). | 0.872 |
| CEO17759.1 | tlpA | RMONA_07035 | RMONA_06300 | SCO1 protein homolog precursor. | Thiol:disulfide interchange protein TlpA. | 0.875 |
| ctaC | CEO16776.1 | RMONA_05015 | RMONA_01835 | Cytochrome c oxidase subunit 2 precursor; Subunits I and II form the functional core of the enzyme complex. Electrons originating in cytochrome c are transferred via heme a and Cu(A) to the binuclear center formed by heme a3 and Cu(B). | SCO1/SenC protein precursor. | 0.872 |
| ctaC | CEO17759.1 | RMONA_05015 | RMONA_07035 | Cytochrome c oxidase subunit 2 precursor; Subunits I and II form the functional core of the enzyme complex. Electrons originating in cytochrome c are transferred via heme a and Cu(A) to the binuclear center formed by heme a3 and Cu(B). | SCO1 protein homolog precursor. | 0.872 |
| ctaC | tlpA | RMONA_05015 | RMONA_06300 | Cytochrome c oxidase subunit 2 precursor; Subunits I and II form the functional core of the enzyme complex. Electrons originating in cytochrome c are transferred via heme a and Cu(A) to the binuclear center formed by heme a3 and Cu(B). | Thiol:disulfide interchange protein TlpA. | 0.833 |
| dnaJ | dnaK | RMONA_03620 | RMONA_03615 | 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. | 0.998 |
| dnaJ | hscA | RMONA_03620 | RMONA_00860 | 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 HscA; Chaperone involved in the maturation of iron-sulfur cluster- containing proteins. Has a low intrinsic ATPase activity which is markedly stimulated by HscB. | 0.993 |
| dnaJ | tlpA | RMONA_03620 | RMONA_06300 | 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 [...] | Thiol:disulfide interchange protein TlpA. | 0.806 |
| dnaJ | tsaA | RMONA_03620 | RMONA_07595 | 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 [...] | Putative peroxiredoxin. | 0.422 |
| dnaK | CEO17154.1 | RMONA_03615 | RMONA_03835 | Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | Hypothetical protein. | 0.982 |
| dnaK | dnaJ | RMONA_03615 | RMONA_03620 | Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 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 [...] | 0.998 |
| dnaK | lpd | RMONA_03615 | RMONA_01070 | Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | Dihydrolipoyl dehydrogenase. | 0.473 |
| dnaK | lpd3 | RMONA_03615 | RMONA_04915 | Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | Dihydrolipoyl dehydrogenase 3. | 0.473 |
| dnaK | tlpA | RMONA_03615 | RMONA_06300 | Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | Thiol:disulfide interchange protein TlpA. | 0.842 |
