| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| Ping_1112 | Ping_3190 | Ping_1112 | Ping_3190 | Ribonucleoside-diphosphate reductase class Ia alpha subunit; Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides. | TIGRFAM: thioredoxin; PFAM: Thioredoxin domain; KEGG: ppr:PBPRA3541 putative thioredoxin; Belongs to the thioredoxin family. | 0.597 |
| Ping_2209 | Ping_2448 | Ping_2209 | Ping_2448 | TIGRFAM: thioredoxin reductase; PFAM: FAD-dependent pyridine nucleotide-disulphide oxidoreductase; KEGG: vfi:VF0902 thioredoxin reductase. | Superoxide dismutase; Destroys radicals which are normally produced within the cells and which are toxic to biological systems. Belongs to the iron/manganese superoxide dismutase family. | 0.466 |
| Ping_2209 | Ping_3190 | Ping_2209 | Ping_3190 | TIGRFAM: thioredoxin reductase; PFAM: FAD-dependent pyridine nucleotide-disulphide oxidoreductase; KEGG: vfi:VF0902 thioredoxin reductase. | TIGRFAM: thioredoxin; PFAM: Thioredoxin domain; KEGG: ppr:PBPRA3541 putative thioredoxin; Belongs to the thioredoxin family. | 0.997 |
| Ping_2209 | dnaJ | Ping_2209 | Ping_0918 | TIGRFAM: thioredoxin reductase; PFAM: FAD-dependent pyridine nucleotide-disulphide oxidoreductase; KEGG: vfi:VF0902 thioredoxin reductase. | 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 [...] | 0.404 |
| Ping_2448 | Ping_2209 | Ping_2448 | Ping_2209 | Superoxide dismutase; Destroys radicals which are normally produced within the cells and which are toxic to biological systems. Belongs to the iron/manganese superoxide dismutase family. | TIGRFAM: thioredoxin reductase; PFAM: FAD-dependent pyridine nucleotide-disulphide oxidoreductase; KEGG: vfi:VF0902 thioredoxin reductase. | 0.466 |
| Ping_2448 | Ping_2449 | Ping_2448 | Ping_2449 | Superoxide dismutase; Destroys radicals which are normally produced within the cells and which are toxic to biological systems. Belongs to the iron/manganese superoxide dismutase family. | TIGRFAM: glutaredoxin-like protein; PFAM: glutaredoxin; KEGG: vpa:VP2117 putative glutaredoxin protein; Belongs to the glutaredoxin family. Monothiol subfamily. | 0.726 |
| Ping_2448 | Ping_2621 | Ping_2448 | Ping_2621 | Superoxide dismutase; Destroys radicals which are normally produced within the cells and which are toxic to biological systems. Belongs to the iron/manganese superoxide dismutase family. | PFAM: heat shock protein DnaJ domain protein; chaperone DnaJ domain protein; KEGG: vfi:VF1108 chaperone protein DnaJ. | 0.483 |
| Ping_2448 | Ping_3190 | Ping_2448 | Ping_3190 | Superoxide dismutase; Destroys radicals which are normally produced within the cells and which are toxic to biological systems. Belongs to the iron/manganese superoxide dismutase family. | TIGRFAM: thioredoxin; PFAM: Thioredoxin domain; KEGG: ppr:PBPRA3541 putative thioredoxin; Belongs to the thioredoxin family. | 0.565 |
| Ping_2448 | dnaJ | Ping_2448 | Ping_0918 | Superoxide dismutase; Destroys radicals which are normally produced within the cells and which are toxic to biological systems. Belongs to the iron/manganese superoxide dismutase family. | 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 [...] | 0.449 |
| Ping_2449 | Ping_2448 | Ping_2449 | Ping_2448 | TIGRFAM: glutaredoxin-like protein; PFAM: glutaredoxin; KEGG: vpa:VP2117 putative glutaredoxin protein; Belongs to the glutaredoxin family. Monothiol subfamily. | Superoxide dismutase; Destroys radicals which are normally produced within the cells and which are toxic to biological systems. Belongs to the iron/manganese superoxide dismutase family. | 0.726 |
| Ping_2449 | Ping_3190 | Ping_2449 | Ping_3190 | TIGRFAM: glutaredoxin-like protein; PFAM: glutaredoxin; KEGG: vpa:VP2117 putative glutaredoxin protein; Belongs to the glutaredoxin family. Monothiol subfamily. | TIGRFAM: thioredoxin; PFAM: Thioredoxin domain; KEGG: ppr:PBPRA3541 putative thioredoxin; Belongs to the thioredoxin family. | 0.567 |
| Ping_2621 | Ping_2448 | Ping_2621 | Ping_2448 | PFAM: heat shock protein DnaJ domain protein; chaperone DnaJ domain protein; KEGG: vfi:VF1108 chaperone protein DnaJ. | Superoxide dismutase; Destroys radicals which are normally produced within the cells and which are toxic to biological systems. Belongs to the iron/manganese superoxide dismutase family. | 0.483 |
| Ping_2621 | Ping_3190 | Ping_2621 | Ping_3190 | PFAM: heat shock protein DnaJ domain protein; chaperone DnaJ domain protein; KEGG: vfi:VF1108 chaperone protein DnaJ. | TIGRFAM: thioredoxin; PFAM: Thioredoxin domain; KEGG: ppr:PBPRA3541 putative thioredoxin; Belongs to the thioredoxin family. | 0.631 |
| Ping_3190 | Ping_1112 | Ping_3190 | Ping_1112 | TIGRFAM: thioredoxin; PFAM: Thioredoxin domain; KEGG: ppr:PBPRA3541 putative thioredoxin; Belongs to the thioredoxin family. | Ribonucleoside-diphosphate reductase class Ia alpha subunit; Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides. | 0.597 |
| Ping_3190 | Ping_2209 | Ping_3190 | Ping_2209 | TIGRFAM: thioredoxin; PFAM: Thioredoxin domain; KEGG: ppr:PBPRA3541 putative thioredoxin; Belongs to the thioredoxin family. | TIGRFAM: thioredoxin reductase; PFAM: FAD-dependent pyridine nucleotide-disulphide oxidoreductase; KEGG: vfi:VF0902 thioredoxin reductase. | 0.997 |
| Ping_3190 | Ping_2448 | Ping_3190 | Ping_2448 | TIGRFAM: thioredoxin; PFAM: Thioredoxin domain; KEGG: ppr:PBPRA3541 putative thioredoxin; Belongs to the thioredoxin family. | Superoxide dismutase; Destroys radicals which are normally produced within the cells and which are toxic to biological systems. Belongs to the iron/manganese superoxide dismutase family. | 0.565 |
| Ping_3190 | Ping_2449 | Ping_3190 | Ping_2449 | TIGRFAM: thioredoxin; PFAM: Thioredoxin domain; KEGG: ppr:PBPRA3541 putative thioredoxin; Belongs to the thioredoxin family. | TIGRFAM: glutaredoxin-like protein; PFAM: glutaredoxin; KEGG: vpa:VP2117 putative glutaredoxin protein; Belongs to the glutaredoxin family. Monothiol subfamily. | 0.567 |
| Ping_3190 | Ping_2621 | Ping_3190 | Ping_2621 | TIGRFAM: thioredoxin; PFAM: Thioredoxin domain; KEGG: ppr:PBPRA3541 putative thioredoxin; Belongs to the thioredoxin family. | PFAM: heat shock protein DnaJ domain protein; chaperone DnaJ domain protein; KEGG: vfi:VF1108 chaperone protein DnaJ. | 0.631 |
| Ping_3190 | cysH | Ping_3190 | Ping_3436 | TIGRFAM: thioredoxin; PFAM: Thioredoxin domain; KEGG: ppr:PBPRA3541 putative thioredoxin; Belongs to the thioredoxin family. | Phosphoadenylylsulfate reductase (thioredoxin); Reduction of activated sulfate into sulfite. Belongs to the PAPS reductase family. CysH subfamily. | 0.851 |
| Ping_3190 | dnaJ | Ping_3190 | Ping_0918 | TIGRFAM: thioredoxin; PFAM: Thioredoxin domain; KEGG: ppr:PBPRA3541 putative thioredoxin; Belongs to the thioredoxin family. | 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 [...] | 0.537 |