| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| DM82_2498 | DM82_831 | DM82_2498 | DM82_831 | Thioredoxin-like domain protein. | dnaJ domain protein. | 0.549 |
| DM82_2498 | ahpC | DM82_2498 | DM82_4593 | Thioredoxin-like domain protein. | Peroxiredoxin; Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides; Belongs to the peroxiredoxin family. AhpC/Prx1 subfamily. | 0.612 |
| DM82_2498 | ahpC_1 | DM82_2498 | DM82_1646 | Thioredoxin-like domain protein. | Redoxin family protein. | 0.612 |
| DM82_2498 | coxB | DM82_2498 | DM82_3668 | Thioredoxin-like domain protein. | Cytochrome c oxidase, subunit II; 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). | 0.565 |
| DM82_2498 | dnaJ | DM82_2498 | DM82_2496 | Thioredoxin-like domain 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 [...] | 0.666 |
| DM82_2498 | dnaK | DM82_2498 | DM82_2497 | Thioredoxin-like domain protein. | Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.711 |
| DM82_2498 | grpE | DM82_2498 | DM82_2499 | Thioredoxin-like domain protein. | grpE family 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-depe [...] | 0.848 |
| DM82_2498 | hflB-2 | DM82_2498 | DM82_5919 | Thioredoxin-like domain protein. | ftsH_fam: ATP-dependent metallopeptidase HflB family protein; Belongs to the AAA ATPase family. | 0.585 |
| DM82_2498 | msrA | DM82_2498 | DM82_240 | Thioredoxin-like domain protein. | Peptide-methionine (S)-S-oxide reductase; Has an important function as a repair enzyme for proteins that have been inactivated by oxidation. Catalyzes the reversible oxidation-reduction of methionine sulfoxide in proteins to methionine. | 0.761 |
| DM82_2498 | tsaA | DM82_2498 | DM82_2416 | Thioredoxin-like domain protein. | Hypothetical protein; C-terminal domain of 1-Cys peroxiredoxin family protein. | 0.612 |
| DM82_831 | DM82_2498 | DM82_831 | DM82_2498 | dnaJ domain protein. | Thioredoxin-like domain protein. | 0.549 |
| DM82_831 | dnaK | DM82_831 | DM82_2497 | dnaJ domain protein. | Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.970 |
| DM82_831 | grpE | DM82_831 | DM82_2499 | dnaJ domain protein. | grpE family 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-depe [...] | 0.965 |
| DM82_831 | hflB-2 | DM82_831 | DM82_5919 | dnaJ domain protein. | ftsH_fam: ATP-dependent metallopeptidase HflB family protein; Belongs to the AAA ATPase family. | 0.839 |
| ahpC | DM82_2498 | DM82_4593 | DM82_2498 | Peroxiredoxin; Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides; Belongs to the peroxiredoxin family. AhpC/Prx1 subfamily. | Thioredoxin-like domain protein. | 0.612 |
| ahpC | dnaK | DM82_4593 | DM82_2497 | Peroxiredoxin; Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides; Belongs to the peroxiredoxin family. AhpC/Prx1 subfamily. | Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.469 |
| ahpC_1 | DM82_2498 | DM82_1646 | DM82_2498 | Redoxin family protein. | Thioredoxin-like domain protein. | 0.612 |
| ahpC_1 | dnaK | DM82_1646 | DM82_2497 | Redoxin family protein. | Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.469 |
| coxB | DM82_2498 | DM82_3668 | DM82_2498 | Cytochrome c oxidase, subunit II; 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). | Thioredoxin-like domain protein. | 0.565 |
| dnaJ | DM82_2498 | DM82_2496 | DM82_2498 | 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 [...] | Thioredoxin-like domain protein. | 0.666 |