| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| AGB48626.1 | AGB50054.1 | Metho_0353 | Metho_1877 | NADH:flavin oxidoreductase. | TIGRFAM: PAS domain S-box. | 0.532 |
| AGB48626.1 | msrA | Metho_0353 | Metho_0352 | NADH:flavin oxidoreductase. | Peptide methionine sulfoxide 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. | 0.659 |
| AGB49156.1 | AGB50054.1 | Metho_0914 | Metho_1877 | Small redox-active disulfide protein 2; Does not function as a glutathione-disulfide oxidoreductase in the presence of glutathione and glutathione reductase. Has low thioredoxin activity in vitro. | TIGRFAM: PAS domain S-box. | 0.424 |
| AGB49156.1 | dnaJ | Metho_0914 | Metho_0944 | Small redox-active disulfide protein 2; Does not function as a glutathione-disulfide oxidoreductase in the presence of glutathione and glutathione reductase. Has low thioredoxin activity in vitro. | 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 [...] | 0.538 |
| AGB49156.1 | msrA | Metho_0914 | Metho_0352 | Small redox-active disulfide protein 2; Does not function as a glutathione-disulfide oxidoreductase in the presence of glutathione and glutathione reductase. Has low thioredoxin activity in vitro. | Peptide methionine sulfoxide 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. | 0.451 |
| AGB49156.1 | msrB | Metho_0914 | Metho_0079 | Small redox-active disulfide protein 2; Does not function as a glutathione-disulfide oxidoreductase in the presence of glutathione and glutathione reductase. Has low thioredoxin activity in vitro. | TIGRFAM: methionine-R-sulfoxide reductase; Belongs to the MsrB Met sulfoxide reductase family. | 0.407 |
| AGB49171.1 | AGB50054.1 | Metho_0929 | Metho_1877 | Glutaredoxin-like protein. | TIGRFAM: PAS domain S-box. | 0.424 |
| AGB49171.1 | dnaJ | Metho_0929 | Metho_0944 | Glutaredoxin-like 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 [...] | 0.538 |
| AGB49171.1 | msrA | Metho_0929 | Metho_0352 | Glutaredoxin-like protein. | Peptide methionine sulfoxide 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. | 0.451 |
| AGB49171.1 | msrB | Metho_0929 | Metho_0079 | Glutaredoxin-like protein. | TIGRFAM: methionine-R-sulfoxide reductase; Belongs to the MsrB Met sulfoxide reductase family. | 0.407 |
| AGB49751.1 | AGB50054.1 | Metho_1552 | Metho_1877 | Cytochrome c biogenesis protein. | TIGRFAM: PAS domain S-box. | 0.693 |
| AGB49751.1 | AGB50359.1 | Metho_1552 | Metho_2196 | Cytochrome c biogenesis protein. | Thioredoxin domain-containing protein. | 0.404 |
| AGB49751.1 | dnaJ | Metho_1552 | Metho_0944 | Cytochrome c biogenesis 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 [...] | 0.546 |
| AGB49751.1 | msrA | Metho_1552 | Metho_0352 | Cytochrome c biogenesis protein. | Peptide methionine sulfoxide 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. | 0.632 |
| AGB49751.1 | msrB | Metho_1552 | Metho_0079 | Cytochrome c biogenesis protein. | TIGRFAM: methionine-R-sulfoxide reductase; Belongs to the MsrB Met sulfoxide reductase family. | 0.853 |
| AGB49794.1 | AGB50054.1 | Metho_1598 | Metho_1877 | TIGRFAM: PAS domain S-box. | TIGRFAM: PAS domain S-box. | 0.839 |
| AGB49794.1 | msrA | Metho_1598 | Metho_0352 | TIGRFAM: PAS domain S-box. | Peptide methionine sulfoxide 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. | 0.461 |
| AGB49794.1 | msrB | Metho_1598 | Metho_0079 | TIGRFAM: PAS domain S-box. | TIGRFAM: methionine-R-sulfoxide reductase; Belongs to the MsrB Met sulfoxide reductase family. | 0.610 |
| AGB49904.1 | AGB50054.1 | Metho_1715 | Metho_1877 | TIGRFAM: thioredoxin. | TIGRFAM: PAS domain S-box. | 0.492 |
| AGB49904.1 | dnaJ | Metho_1715 | Metho_0944 | TIGRFAM: thioredoxin. | 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 [...] | 0.610 |
