node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
SDO14352.1 | trxA | SAMN04489756_101106 | SAMN04489756_11431 | Arsenate reductase. | Thioredoxin; Belongs to the thioredoxin family. | 0.508 |
SDO18751.1 | SDO79800.1 | SAMN04489756_10280 | SAMN04489756_11915 | Glutamate synthase (NADPH/NADH) large chain. | Thioredoxin reductase (NADPH). | 0.455 |
SDO18751.1 | gap | SAMN04489756_10280 | SAMN04489756_12017 | Glutamate synthase (NADPH/NADH) large chain. | Glyceraldehyde-3-phosphate dehydrogenase (NAD+); Belongs to the glyceraldehyde-3-phosphate dehydrogenase family. | 0.452 |
SDO18751.1 | trxA | SAMN04489756_10280 | SAMN04489756_11431 | Glutamate synthase (NADPH/NADH) large chain. | Thioredoxin; Belongs to the thioredoxin family. | 0.561 |
SDO18751.1 | trxB | SAMN04489756_10280 | SAMN04489756_11114 | Glutamate synthase (NADPH/NADH) large chain. | Thioredoxin reductase (NADPH). | 0.455 |
SDO69449.1 | dnaJ | SAMN04489756_11432 | SAMN04489756_12136 | Cysteine desulfurase. | Molecular chaperone 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, [...] | 0.671 |
SDO69449.1 | grpE | SAMN04489756_11432 | SAMN04489756_12135 | Cysteine desulfurase. | Molecular chaperone GrpE; 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 [...] | 0.443 |
SDO69449.1 | trxA | SAMN04489756_11432 | SAMN04489756_11431 | Cysteine desulfurase. | Thioredoxin; Belongs to the thioredoxin family. | 0.542 |
SDO79800.1 | SDO18751.1 | SAMN04489756_11915 | SAMN04489756_10280 | Thioredoxin reductase (NADPH). | Glutamate synthase (NADPH/NADH) large chain. | 0.455 |
SDO79800.1 | trxA | SAMN04489756_11915 | SAMN04489756_11431 | Thioredoxin reductase (NADPH). | Thioredoxin; Belongs to the thioredoxin family. | 0.554 |
SDO79800.1 | trxB | SAMN04489756_11915 | SAMN04489756_11114 | Thioredoxin reductase (NADPH). | Thioredoxin reductase (NADPH). | 0.911 |
dnaJ | SDO69449.1 | SAMN04489756_12136 | SAMN04489756_11432 | Molecular chaperone 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, [...] | Cysteine desulfurase. | 0.671 |
dnaJ | groL | SAMN04489756_12136 | SAMN04489756_10321 | Molecular chaperone 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, [...] | Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.780 |
dnaJ | grpE | SAMN04489756_12136 | SAMN04489756_12135 | Molecular chaperone 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, [...] | Molecular chaperone GrpE; 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 [...] | 0.987 |
dnaJ | trxA | SAMN04489756_12136 | SAMN04489756_11431 | Molecular chaperone 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, [...] | Thioredoxin; Belongs to the thioredoxin family. | 0.513 |
gap | SDO18751.1 | SAMN04489756_12017 | SAMN04489756_10280 | Glyceraldehyde-3-phosphate dehydrogenase (NAD+); Belongs to the glyceraldehyde-3-phosphate dehydrogenase family. | Glutamate synthase (NADPH/NADH) large chain. | 0.452 |
gap | groL | SAMN04489756_12017 | SAMN04489756_10321 | Glyceraldehyde-3-phosphate dehydrogenase (NAD+); Belongs to the glyceraldehyde-3-phosphate dehydrogenase family. | Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.606 |
gap | trxA | SAMN04489756_12017 | SAMN04489756_11431 | Glyceraldehyde-3-phosphate dehydrogenase (NAD+); Belongs to the glyceraldehyde-3-phosphate dehydrogenase family. | Thioredoxin; Belongs to the thioredoxin family. | 0.542 |
groL | dnaJ | SAMN04489756_10321 | SAMN04489756_12136 | Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | Molecular chaperone 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, [...] | 0.780 |
groL | gap | SAMN04489756_10321 | SAMN04489756_12017 | Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | Glyceraldehyde-3-phosphate dehydrogenase (NAD+); Belongs to the glyceraldehyde-3-phosphate dehydrogenase family. | 0.606 |