node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
MCRY_09165 | MCRY_17500 | MCRY_09165 | MCRY_17500 | NADH-quinone oxidoreductase subunit F; Bacteria available from JCM 15447. Source DNA available from JCM 15447; Derived by automated computational analysis using gene prediction method: Protein Homology. | 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. | 0.697 |
MCRY_09165 | MCRY_22055 | MCRY_09165 | MCRY_22055 | NADH-quinone oxidoreductase subunit F; Bacteria available from JCM 15447. Source DNA available from JCM 15447; Derived by automated computational analysis using gene prediction method: Protein Homology. | Heat shock protein Hsp70; Bacteria available from JCM 15447. Source DNA available from JCM 15447; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.460 |
MCRY_09165 | dnaJ | MCRY_09165 | MCRY_01900 | NADH-quinone oxidoreductase subunit F; Bacteria available from JCM 15447. Source DNA available from JCM 15447; Derived by automated computational analysis using gene prediction method: Protein Homology. | 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, [...] | 0.975 |
MCRY_09165 | dnaK | MCRY_09165 | MCRY_01895 | NADH-quinone oxidoreductase subunit F; Bacteria available from JCM 15447. Source DNA available from JCM 15447; Derived by automated computational analysis using gene prediction method: Protein Homology. | Molecular chaperone DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.460 |
MCRY_17500 | MCRY_09165 | MCRY_17500 | MCRY_09165 | 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. | NADH-quinone oxidoreductase subunit F; Bacteria available from JCM 15447. Source DNA available from JCM 15447; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.697 |
MCRY_17500 | dnaJ | MCRY_17500 | MCRY_01900 | 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. | 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, [...] | 0.957 |
MCRY_17500 | grpE | MCRY_17500 | MCRY_00500 | 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. | 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 [...] | 0.651 |
MCRY_17500 | rplK | MCRY_17500 | MCRY_07345 | 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. | 50S ribosomal protein L11; Forms part of the ribosomal stalk which helps the ribosome interact with GTP-bound translation factors. | 0.957 |
MCRY_17500 | rplQ | MCRY_17500 | MCRY_07560 | 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. | 50S ribosomal protein L17; Bacteria available from JCM 15447. Source DNA available from JCM 15447; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.966 |
MCRY_17500 | rpsE | MCRY_17500 | MCRY_07515 | 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. | 30S ribosomal protein S5; Located at the back of the 30S subunit body where it stabilizes the conformation of the head with respect to the body. Belongs to the universal ribosomal protein uS5 family. | 0.953 |
MCRY_17500 | rpsI | MCRY_17500 | MCRY_15985 | 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. | 30S ribosomal protein S9; Bacteria available from JCM 15447. Source DNA available from JCM 15447; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the universal ribosomal protein uS9 family. | 0.956 |
MCRY_22055 | MCRY_09165 | MCRY_22055 | MCRY_09165 | Heat shock protein Hsp70; Bacteria available from JCM 15447. Source DNA available from JCM 15447; Derived by automated computational analysis using gene prediction method: Protein Homology. | NADH-quinone oxidoreductase subunit F; Bacteria available from JCM 15447. Source DNA available from JCM 15447; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.460 |
MCRY_22055 | dnaJ | MCRY_22055 | MCRY_01900 | Heat shock protein Hsp70; Bacteria available from JCM 15447. Source DNA available from JCM 15447; Derived by automated computational analysis using gene prediction method: Protein Homology. | 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, [...] | 0.999 |
MCRY_22055 | grpE | MCRY_22055 | MCRY_00500 | Heat shock protein Hsp70; Bacteria available from JCM 15447. Source DNA available from JCM 15447; Derived by automated computational analysis using gene prediction method: Protein Homology. | 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 [...] | 0.997 |
MCRY_22055 | rplK | MCRY_22055 | MCRY_07345 | Heat shock protein Hsp70; Bacteria available from JCM 15447. Source DNA available from JCM 15447; Derived by automated computational analysis using gene prediction method: Protein Homology. | 50S ribosomal protein L11; Forms part of the ribosomal stalk which helps the ribosome interact with GTP-bound translation factors. | 0.687 |
MCRY_22055 | rpsE | MCRY_22055 | MCRY_07515 | Heat shock protein Hsp70; Bacteria available from JCM 15447. Source DNA available from JCM 15447; Derived by automated computational analysis using gene prediction method: Protein Homology. | 30S ribosomal protein S5; Located at the back of the 30S subunit body where it stabilizes the conformation of the head with respect to the body. Belongs to the universal ribosomal protein uS5 family. | 0.843 |
dnaJ | MCRY_09165 | MCRY_01900 | MCRY_09165 | 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, [...] | NADH-quinone oxidoreductase subunit F; Bacteria available from JCM 15447. Source DNA available from JCM 15447; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.975 |
dnaJ | MCRY_17500 | MCRY_01900 | MCRY_17500 | 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, [...] | 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. | 0.957 |
dnaJ | MCRY_22055 | MCRY_01900 | MCRY_22055 | 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, [...] | Heat shock protein Hsp70; Bacteria available from JCM 15447. Source DNA available from JCM 15447; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.999 |
dnaJ | dnaK | MCRY_01900 | MCRY_01895 | 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 DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.999 |