| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| XF_1196 | XF_2174 | XF_1196 | XF_2174 | Ribonucleoside-diphosphate reductase alpha chain; Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides. | Thioredoxin; Similar to SP|P77395 (percent identity: 31 %/query alignment coverage: 82.5 %/subject alignment coverage: 94.3 %); identified by sequence similarity; putative; ORF located using Glimmer/RBSfinder. | 0.670 |
| XF_1196 | XF_2710 | XF_1196 | XF_2710 | Ribonucleoside-diphosphate reductase alpha chain; Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides. | Glutamate synthase, alpha subunit; Similar to SP|P09831 (percent identity: 53 %/query alignment coverage: 99.7 %/subject alignment coverage: 97.9 %); identified by sequence similarity; putative; ORF located using Glimmer/RBSfinder/Start codon shift: -117. | 0.482 |
| XF_1448 | XF_2174 | XF_1448 | XF_2174 | Thioredoxin reductase; Similar to SP|P09625 (percent identity: 70 %/query alignment coverage: 97.5 %/subject alignment coverage: 97.5 %); identified by sequence similarity; putative; ORF located using Glimmer/RBSfinder/Start codon shift: -144. | Thioredoxin; Similar to SP|P77395 (percent identity: 31 %/query alignment coverage: 82.5 %/subject alignment coverage: 94.3 %); identified by sequence similarity; putative; ORF located using Glimmer/RBSfinder. | 0.851 |
| XF_2174 | XF_1196 | XF_2174 | XF_1196 | Thioredoxin; Similar to SP|P77395 (percent identity: 31 %/query alignment coverage: 82.5 %/subject alignment coverage: 94.3 %); identified by sequence similarity; putative; ORF located using Glimmer/RBSfinder. | Ribonucleoside-diphosphate reductase alpha chain; Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides. | 0.670 |
| XF_2174 | XF_1448 | XF_2174 | XF_1448 | Thioredoxin; Similar to SP|P77395 (percent identity: 31 %/query alignment coverage: 82.5 %/subject alignment coverage: 94.3 %); identified by sequence similarity; putative; ORF located using Glimmer/RBSfinder. | Thioredoxin reductase; Similar to SP|P09625 (percent identity: 70 %/query alignment coverage: 97.5 %/subject alignment coverage: 97.5 %); identified by sequence similarity; putative; ORF located using Glimmer/RBSfinder/Start codon shift: -144. | 0.851 |
| XF_2174 | XF_2298 | XF_2174 | XF_2298 | Thioredoxin; Similar to SP|P77395 (percent identity: 31 %/query alignment coverage: 82.5 %/subject alignment coverage: 94.3 %); identified by sequence similarity; putative; ORF located using Glimmer/RBSfinder. | Low molecular weight phosphotyrosine protein phosphatase; Similar to GI|257210 (percent identity: 40 %/query alignment coverage: 89.0 %/subject alignment coverage: 86.2 %); identified by sequence similarity; putative; ORF located using Glimmer/RBSfinder; Belongs to the low molecular weight phosphotyrosine protein phosphatase family. | 0.635 |
| XF_2174 | XF_2710 | XF_2174 | XF_2710 | Thioredoxin; Similar to SP|P77395 (percent identity: 31 %/query alignment coverage: 82.5 %/subject alignment coverage: 94.3 %); identified by sequence similarity; putative; ORF located using Glimmer/RBSfinder. | Glutamate synthase, alpha subunit; Similar to SP|P09831 (percent identity: 53 %/query alignment coverage: 99.7 %/subject alignment coverage: 97.9 %); identified by sequence similarity; putative; ORF located using Glimmer/RBSfinder/Start codon shift: -117. | 0.619 |
| XF_2174 | dnaJ | XF_2174 | XF_2339 | Thioredoxin; Similar to SP|P77395 (percent identity: 31 %/query alignment coverage: 82.5 %/subject alignment coverage: 94.3 %); identified by sequence similarity; putative; ORF located using Glimmer/RBSfinder. | DnaJ protein; 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, DnaK and Gr [...] | 0.709 |
| XF_2174 | groL | XF_2174 | XF_0615 | Thioredoxin; Similar to SP|P77395 (percent identity: 31 %/query alignment coverage: 82.5 %/subject alignment coverage: 94.3 %); identified by sequence similarity; putative; ORF located using Glimmer/RBSfinder. | 60kDa chaperonin; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.906 |
| XF_2174 | grpE | XF_2174 | XF_2341 | Thioredoxin; Similar to SP|P77395 (percent identity: 31 %/query alignment coverage: 82.5 %/subject alignment coverage: 94.3 %); identified by sequence similarity; putative; ORF located using Glimmer/RBSfinder. | Heat shock protein 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- [...] | 0.882 |
| XF_2174 | hslU | XF_2174 | XF_1485 | Thioredoxin; Similar to SP|P77395 (percent identity: 31 %/query alignment coverage: 82.5 %/subject alignment coverage: 94.3 %); identified by sequence similarity; putative; ORF located using Glimmer/RBSfinder. | Heat shock protein; ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. The binding of ATP and its subsequent hydrolysis by HslU are essential for unfolding of protein substrates subsequently hydrolyzed by HslV. HslU recognizes the N-terminal part of its protein substrates and unfolds these before they are guided to HslV for hydrolysis. | 0.896 |
| XF_2174 | hslV | XF_2174 | XF_1484 | Thioredoxin; Similar to SP|P77395 (percent identity: 31 %/query alignment coverage: 82.5 %/subject alignment coverage: 94.3 %); identified by sequence similarity; putative; ORF located using Glimmer/RBSfinder. | Heat shock protein; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.912 |
| XF_2174 | htpG | XF_2174 | XF_0978 | Thioredoxin; Similar to SP|P77395 (percent identity: 31 %/query alignment coverage: 82.5 %/subject alignment coverage: 94.3 %); identified by sequence similarity; putative; ORF located using Glimmer/RBSfinder. | Heat shock protein G; Molecular chaperone. Has ATPase activity. | 0.731 |
| XF_2298 | XF_2174 | XF_2298 | XF_2174 | Low molecular weight phosphotyrosine protein phosphatase; Similar to GI|257210 (percent identity: 40 %/query alignment coverage: 89.0 %/subject alignment coverage: 86.2 %); identified by sequence similarity; putative; ORF located using Glimmer/RBSfinder; Belongs to the low molecular weight phosphotyrosine protein phosphatase family. | Thioredoxin; Similar to SP|P77395 (percent identity: 31 %/query alignment coverage: 82.5 %/subject alignment coverage: 94.3 %); identified by sequence similarity; putative; ORF located using Glimmer/RBSfinder. | 0.635 |
| XF_2710 | XF_1196 | XF_2710 | XF_1196 | Glutamate synthase, alpha subunit; Similar to SP|P09831 (percent identity: 53 %/query alignment coverage: 99.7 %/subject alignment coverage: 97.9 %); identified by sequence similarity; putative; ORF located using Glimmer/RBSfinder/Start codon shift: -117. | Ribonucleoside-diphosphate reductase alpha chain; Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides. | 0.482 |
| XF_2710 | XF_2174 | XF_2710 | XF_2174 | Glutamate synthase, alpha subunit; Similar to SP|P09831 (percent identity: 53 %/query alignment coverage: 99.7 %/subject alignment coverage: 97.9 %); identified by sequence similarity; putative; ORF located using Glimmer/RBSfinder/Start codon shift: -117. | Thioredoxin; Similar to SP|P77395 (percent identity: 31 %/query alignment coverage: 82.5 %/subject alignment coverage: 94.3 %); identified by sequence similarity; putative; ORF located using Glimmer/RBSfinder. | 0.619 |
| dnaJ | XF_2174 | XF_2339 | XF_2174 | DnaJ protein; 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, DnaK and Gr [...] | Thioredoxin; Similar to SP|P77395 (percent identity: 31 %/query alignment coverage: 82.5 %/subject alignment coverage: 94.3 %); identified by sequence similarity; putative; ORF located using Glimmer/RBSfinder. | 0.709 |
| dnaJ | groL | XF_2339 | XF_0615 | DnaJ protein; 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, DnaK and Gr [...] | 60kDa chaperonin; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.964 |
| dnaJ | grpE | XF_2339 | XF_2341 | DnaJ protein; 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, DnaK and Gr [...] | Heat shock protein 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- [...] | 0.991 |
| dnaJ | hslU | XF_2339 | XF_1485 | DnaJ protein; 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, DnaK and Gr [...] | Heat shock protein; ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. The binding of ATP and its subsequent hydrolysis by HslU are essential for unfolding of protein substrates subsequently hydrolyzed by HslV. HslU recognizes the N-terminal part of its protein substrates and unfolds these before they are guided to HslV for hydrolysis. | 0.964 |
