| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| PSHAa2342 | dnaJ | PSHAa2342 | PSHAb0358 | Putative thioredoxin-like protein; Function proposed based on presence of conserved amino acid motif, structural feature or limited homolgy. | Chaperone protein dnaJ (Heat shock protein J) (HSP40), co-chaperone with DnaK; 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. Sever [...] | 0.702 |
| PSHAa2342 | gor | PSHAa2342 | PSHAa0360 | Putative thioredoxin-like protein; Function proposed based on presence of conserved amino acid motif, structural feature or limited homolgy. | Glutathione reductase; Function of homologous gene experimentally demonstrated in an other organism; enzyme. | 0.981 |
| PSHAa2342 | htpG | PSHAa2342 | PSHAa1207 | Putative thioredoxin-like protein; Function proposed based on presence of conserved amino acid motif, structural feature or limited homolgy. | Chaperone protein htpG; Molecular chaperone. Has ATPase activity. | 0.785 |
| PSHAa2342 | prlC | PSHAa2342 | PSHAa0361 | Putative thioredoxin-like protein; Function proposed based on presence of conserved amino acid motif, structural feature or limited homolgy. | Function of homologous gene experimentally demonstrated in an other organism; enzyme. | 0.421 |
| dnaJ | PSHAa2342 | PSHAb0358 | PSHAa2342 | Chaperone protein dnaJ (Heat shock protein J) (HSP40), co-chaperone with DnaK; 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. Sever [...] | Putative thioredoxin-like protein; Function proposed based on presence of conserved amino acid motif, structural feature or limited homolgy. | 0.702 |
| dnaJ | htpG | PSHAb0358 | PSHAa1207 | Chaperone protein dnaJ (Heat shock protein J) (HSP40), co-chaperone with DnaK; 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. Sever [...] | Chaperone protein htpG; Molecular chaperone. Has ATPase activity. | 0.988 |
| dnaJ | prlC | PSHAb0358 | PSHAa0361 | Chaperone protein dnaJ (Heat shock protein J) (HSP40), co-chaperone with DnaK; 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. Sever [...] | Function of homologous gene experimentally demonstrated in an other organism; enzyme. | 0.453 |
| gor | PSHAa2342 | PSHAa0360 | PSHAa2342 | Glutathione reductase; Function of homologous gene experimentally demonstrated in an other organism; enzyme. | Putative thioredoxin-like protein; Function proposed based on presence of conserved amino acid motif, structural feature or limited homolgy. | 0.981 |
| gor | prlC | PSHAa0360 | PSHAa0361 | Glutathione reductase; Function of homologous gene experimentally demonstrated in an other organism; enzyme. | Function of homologous gene experimentally demonstrated in an other organism; enzyme. | 0.771 |
| htpG | PSHAa2342 | PSHAa1207 | PSHAa2342 | Chaperone protein htpG; Molecular chaperone. Has ATPase activity. | Putative thioredoxin-like protein; Function proposed based on presence of conserved amino acid motif, structural feature or limited homolgy. | 0.785 |
| htpG | dnaJ | PSHAa1207 | PSHAb0358 | Chaperone protein htpG; Molecular chaperone. Has ATPase activity. | Chaperone protein dnaJ (Heat shock protein J) (HSP40), co-chaperone with DnaK; 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. Sever [...] | 0.988 |
| htpG | prlC | PSHAa1207 | PSHAa0361 | Chaperone protein htpG; Molecular chaperone. Has ATPase activity. | Function of homologous gene experimentally demonstrated in an other organism; enzyme. | 0.438 |
| prlC | PSHAa2342 | PSHAa0361 | PSHAa2342 | Function of homologous gene experimentally demonstrated in an other organism; enzyme. | Putative thioredoxin-like protein; Function proposed based on presence of conserved amino acid motif, structural feature or limited homolgy. | 0.421 |
| prlC | dnaJ | PSHAa0361 | PSHAb0358 | Function of homologous gene experimentally demonstrated in an other organism; enzyme. | Chaperone protein dnaJ (Heat shock protein J) (HSP40), co-chaperone with DnaK; 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. Sever [...] | 0.453 |
| prlC | gor | PSHAa0361 | PSHAa0360 | Function of homologous gene experimentally demonstrated in an other organism; enzyme. | Glutathione reductase; Function of homologous gene experimentally demonstrated in an other organism; enzyme. | 0.771 |
| prlC | htpG | PSHAa0361 | PSHAa1207 | Function of homologous gene experimentally demonstrated in an other organism; enzyme. | Chaperone protein htpG; Molecular chaperone. Has ATPase activity. | 0.438 |
| prlC | rsmJ | PSHAa0361 | PSHAa0362 | Function of homologous gene experimentally demonstrated in an other organism; enzyme. | Conserved protein of unknown function; Specifically methylates the guanosine in position 1516 of 16S rRNA. | 0.747 |
| rsmJ | prlC | PSHAa0362 | PSHAa0361 | Conserved protein of unknown function; Specifically methylates the guanosine in position 1516 of 16S rRNA. | Function of homologous gene experimentally demonstrated in an other organism; enzyme. | 0.747 |
