node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
ARC33007.1 | ARC33881.1 | A6J79_00285 | A6J79_05485 | Tetracycline resistance ribosomal protection protein Tet(M); Derived by automated computational analysis using gene prediction method: Protein Homology. | Peptidyl-prolyl cis-trans isomerase; 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. | 0.844 |
ARC33007.1 | cshA | A6J79_00285 | A6J79_00490 | Tetracycline resistance ribosomal protection protein Tet(M); Derived by automated computational analysis using gene prediction method: Protein Homology. | ATP-dependent RNA helicase; DEAD-box RNA helicase possibly involved in RNA degradation. Unwinds dsRNA in both 5'- and 3'-directions, has RNA-dependent ATPase activity; Belongs to the DEAD box helicase family. CshA subfamily. | 0.766 |
ARC33007.1 | cshB | A6J79_00285 | A6J79_01270 | Tetracycline resistance ribosomal protection protein Tet(M); Derived by automated computational analysis using gene prediction method: Protein Homology. | DEAD/DEAH box helicase; Probable DEAD-box RNA helicase. May work in conjunction with the cold shock proteins to ensure proper initiation of transcription at low and optimal temperatures. | 0.766 |
ARC33007.1 | dnaJ | A6J79_00285 | A6J79_03645 | Tetracycline resistance ribosomal protection protein Tet(M); 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, [...] | 0.633 |
ARC33007.1 | rplC | A6J79_00285 | A6J79_02505 | Tetracycline resistance ribosomal protection protein Tet(M); Derived by automated computational analysis using gene prediction method: Protein Homology. | 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. | 0.938 |
ARC33007.1 | rplM | A6J79_00285 | A6J79_03490 | Tetracycline resistance ribosomal protection protein Tet(M); Derived by automated computational analysis using gene prediction method: Protein Homology. | 50S ribosomal protein L13; This protein is one of the early assembly proteins of the 50S ribosomal subunit, although it is not seen to bind rRNA by itself. It is important during the early stages of 50S assembly. | 0.938 |
ARC33007.1 | rplU | A6J79_00285 | A6J79_04950 | Tetracycline resistance ribosomal protection protein Tet(M); Derived by automated computational analysis using gene prediction method: Protein Homology. | 50S ribosomal protein L21; This protein binds to 23S rRNA in the presence of protein L20; Belongs to the bacterial ribosomal protein bL21 family. | 0.930 |
ARC33007.1 | rpsQ | A6J79_00285 | A6J79_02460 | Tetracycline resistance ribosomal protection protein Tet(M); Derived by automated computational analysis using gene prediction method: Protein Homology. | 30S ribosomal protein S17; One of the primary rRNA binding proteins, it binds specifically to the 5'-end of 16S ribosomal RNA. | 0.939 |
ARC33881.1 | ARC33007.1 | A6J79_05485 | A6J79_00285 | Peptidyl-prolyl cis-trans isomerase; 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. | Tetracycline resistance ribosomal protection protein Tet(M); Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.844 |
ARC33881.1 | ARC34113.1 | A6J79_05485 | A6J79_06750 | Peptidyl-prolyl cis-trans isomerase; 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. | 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. | 0.822 |
ARC33881.1 | cshA | A6J79_05485 | A6J79_00490 | Peptidyl-prolyl cis-trans isomerase; 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. | ATP-dependent RNA helicase; DEAD-box RNA helicase possibly involved in RNA degradation. Unwinds dsRNA in both 5'- and 3'-directions, has RNA-dependent ATPase activity; Belongs to the DEAD box helicase family. CshA subfamily. | 0.865 |
ARC33881.1 | cshB | A6J79_05485 | A6J79_01270 | Peptidyl-prolyl cis-trans isomerase; 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. | DEAD/DEAH box helicase; Probable DEAD-box RNA helicase. May work in conjunction with the cold shock proteins to ensure proper initiation of transcription at low and optimal temperatures. | 0.871 |
ARC33881.1 | dnaJ | A6J79_05485 | A6J79_03645 | Peptidyl-prolyl cis-trans isomerase; 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. | 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, [...] | 0.985 |
ARC33881.1 | fusA | A6J79_05485 | A6J79_01750 | Peptidyl-prolyl cis-trans isomerase; 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. | Elongation factor G; Catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome; Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. EF-G/EF-2 subfamily. | 0.817 |
ARC33881.1 | rplC | A6J79_05485 | A6J79_02505 | Peptidyl-prolyl cis-trans isomerase; 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. | 0.813 |
ARC33881.1 | rplM | A6J79_05485 | A6J79_03490 | Peptidyl-prolyl cis-trans isomerase; 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 L13; This protein is one of the early assembly proteins of the 50S ribosomal subunit, although it is not seen to bind rRNA by itself. It is important during the early stages of 50S assembly. | 0.847 |
ARC33881.1 | rplU | A6J79_05485 | A6J79_04950 | Peptidyl-prolyl cis-trans isomerase; 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 L21; This protein binds to 23S rRNA in the presence of protein L20; Belongs to the bacterial ribosomal protein bL21 family. | 0.818 |
ARC33881.1 | rpsQ | A6J79_05485 | A6J79_02460 | Peptidyl-prolyl cis-trans isomerase; 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. | 30S ribosomal protein S17; One of the primary rRNA binding proteins, it binds specifically to the 5'-end of 16S ribosomal RNA. | 0.870 |
ARC34113.1 | ARC33881.1 | A6J79_06750 | A6J79_05485 | 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. | Peptidyl-prolyl cis-trans isomerase; 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. | 0.822 |
ARC34113.1 | dnaJ | A6J79_06750 | A6J79_03645 | 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, [...] | 0.912 |