| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| EDR45496.1 | EDR45946.1 | DORFOR_03280 | DORFOR_02548 | Peptidyl-prolyl cis-trans isomerase, cyclophilin-type; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides; Belongs to the cyclophilin-type PPIase family. | Hsp90 protein; KEGG: hpa:HPAG1_0211 4.8e-61 chaperone and heat shock protein 90; COG: COG0326 Molecular chaperone, HSP90 family; Psort location: Cytoplasmic, score: 9.98. | 0.994 |
| EDR45496.1 | EDR46654.1 | DORFOR_03280 | DORFOR_01877 | Peptidyl-prolyl cis-trans isomerase, cyclophilin-type; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides; Belongs to the cyclophilin-type PPIase family. | Hypothetical protein; Psort location: Cytoplasmic, score: 8.87. | 0.643 |
| EDR45496.1 | EDR46849.1 | DORFOR_03280 | DORFOR_02072 | Peptidyl-prolyl cis-trans isomerase, cyclophilin-type; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides; Belongs to the cyclophilin-type PPIase family. | Hypothetical protein; Psort location: Cytoplasmic, score: 8.87. | 0.643 |
| EDR45496.1 | EDR48434.1 | DORFOR_03280 | DORFOR_00176 | Peptidyl-prolyl cis-trans isomerase, cyclophilin-type; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides; Belongs to the cyclophilin-type PPIase family. | Pyridine nucleotide-disulfide oxidoreductase; KEGG: btl:BALH_0703 2.0e-140 ndh; NADH dehydrogenase K00356; COG: COG0607 Rhodanese-related sulfurtransferase; Psort location: Cytoplasmic, score: 9.98. | 0.934 |
| EDR45496.1 | dnaJ | DORFOR_03280 | DORFOR_00805 | Peptidyl-prolyl cis-trans isomerase, cyclophilin-type; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides; Belongs to the cyclophilin-type PPIase 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 [...] | 0.887 |
| EDR45496.1 | dnaK | DORFOR_03280 | DORFOR_00806 | Peptidyl-prolyl cis-trans isomerase, cyclophilin-type; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides; Belongs to the cyclophilin-type PPIase family. | Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.689 |
| EDR45496.1 | nifJ | DORFOR_03280 | DORFOR_02415 | Peptidyl-prolyl cis-trans isomerase, cyclophilin-type; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides; Belongs to the cyclophilin-type PPIase family. | KEGG: ctc:CTC01741 0. pyruvate-flavodoxin oxidoreductase K03737; COG: COG1013 Pyruvate:ferredoxin oxidoreductase and related 2-oxoacid:ferredoxin oxidoreductases, beta subunit; Psort location: Cytoplasmic, score: 8.87. | 0.925 |
| EDR45496.1 | rplC | DORFOR_03280 | DORFOR_01359 | Peptidyl-prolyl cis-trans isomerase, cyclophilin-type; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides; Belongs to the cyclophilin-type PPIase family. | 50S ribosomal protein L3; One of the primary rRNA binding proteins, it binds directly near the 3'-end of the 23S rRNA, where it nucleates assembly of the 50S subunit; Belongs to the universal ribosomal protein uL3 family. | 0.903 |
| EDR45496.1 | rplK | DORFOR_03280 | DORFOR_01208 | Peptidyl-prolyl cis-trans isomerase, cyclophilin-type; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides; Belongs to the cyclophilin-type PPIase family. | Ribosomal protein L11; Forms part of the ribosomal stalk which helps the ribosome interact with GTP-bound translation factors. | 0.915 |
| EDR45946.1 | EDR45496.1 | DORFOR_02548 | DORFOR_03280 | Hsp90 protein; KEGG: hpa:HPAG1_0211 4.8e-61 chaperone and heat shock protein 90; COG: COG0326 Molecular chaperone, HSP90 family; Psort location: Cytoplasmic, score: 9.98. | Peptidyl-prolyl cis-trans isomerase, cyclophilin-type; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides; Belongs to the cyclophilin-type PPIase family. | 0.994 |
| EDR45946.1 | EDR46654.1 | DORFOR_02548 | DORFOR_01877 | Hsp90 protein; KEGG: hpa:HPAG1_0211 4.8e-61 chaperone and heat shock protein 90; COG: COG0326 Molecular chaperone, HSP90 family; Psort location: Cytoplasmic, score: 9.98. | Hypothetical protein; Psort location: Cytoplasmic, score: 8.87. | 0.997 |
| EDR45946.1 | EDR46849.1 | DORFOR_02548 | DORFOR_02072 | Hsp90 protein; KEGG: hpa:HPAG1_0211 4.8e-61 chaperone and heat shock protein 90; COG: COG0326 Molecular chaperone, HSP90 family; Psort location: Cytoplasmic, score: 9.98. | Hypothetical protein; Psort location: Cytoplasmic, score: 8.87. | 0.997 |
| EDR45946.1 | dnaJ | DORFOR_02548 | DORFOR_00805 | Hsp90 protein; KEGG: hpa:HPAG1_0211 4.8e-61 chaperone and heat shock protein 90; COG: COG0326 Molecular chaperone, HSP90 family; Psort location: Cytoplasmic, score: 9.98. | 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 [...] | 0.978 |
| EDR45946.1 | dnaK | DORFOR_02548 | DORFOR_00806 | Hsp90 protein; KEGG: hpa:HPAG1_0211 4.8e-61 chaperone and heat shock protein 90; COG: COG0326 Molecular chaperone, HSP90 family; Psort location: Cytoplasmic, score: 9.98. | Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.998 |
| EDR45946.1 | grpE | DORFOR_02548 | DORFOR_00807 | Hsp90 protein; KEGG: hpa:HPAG1_0211 4.8e-61 chaperone and heat shock protein 90; COG: COG0326 Molecular chaperone, HSP90 family; Psort location: Cytoplasmic, score: 9.98. | Co-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-depend [...] | 0.877 |
| EDR45946.1 | nifJ | DORFOR_02548 | DORFOR_02415 | Hsp90 protein; KEGG: hpa:HPAG1_0211 4.8e-61 chaperone and heat shock protein 90; COG: COG0326 Molecular chaperone, HSP90 family; Psort location: Cytoplasmic, score: 9.98. | KEGG: ctc:CTC01741 0. pyruvate-flavodoxin oxidoreductase K03737; COG: COG1013 Pyruvate:ferredoxin oxidoreductase and related 2-oxoacid:ferredoxin oxidoreductases, beta subunit; Psort location: Cytoplasmic, score: 8.87. | 0.446 |
| EDR46654.1 | EDR45496.1 | DORFOR_01877 | DORFOR_03280 | Hypothetical protein; Psort location: Cytoplasmic, score: 8.87. | Peptidyl-prolyl cis-trans isomerase, cyclophilin-type; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides; Belongs to the cyclophilin-type PPIase family. | 0.643 |
| EDR46654.1 | EDR45946.1 | DORFOR_01877 | DORFOR_02548 | Hypothetical protein; Psort location: Cytoplasmic, score: 8.87. | Hsp90 protein; KEGG: hpa:HPAG1_0211 4.8e-61 chaperone and heat shock protein 90; COG: COG0326 Molecular chaperone, HSP90 family; Psort location: Cytoplasmic, score: 9.98. | 0.997 |
| EDR46654.1 | EDR48434.1 | DORFOR_01877 | DORFOR_00176 | Hypothetical protein; Psort location: Cytoplasmic, score: 8.87. | Pyridine nucleotide-disulfide oxidoreductase; KEGG: btl:BALH_0703 2.0e-140 ndh; NADH dehydrogenase K00356; COG: COG0607 Rhodanese-related sulfurtransferase; Psort location: Cytoplasmic, score: 9.98. | 0.416 |
| EDR46654.1 | dnaJ | DORFOR_01877 | DORFOR_00805 | Hypothetical protein; Psort location: Cytoplasmic, score: 8.87. | 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 [...] | 0.915 |