node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
SFT36819.1 | SFT65769.1 | SAMN04515657_0122 | SAMN04515657_1549 | Peptidyl-prolyl cis-trans isomerase B (cyclophilin B); 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 Zn proteases. | 0.868 |
SFT36819.1 | dnaJ | SAMN04515657_0122 | SAMN04515657_0174 | Peptidyl-prolyl cis-trans isomerase B (cyclophilin B); 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, [...] | 0.952 |
SFT36819.1 | dnaK | SAMN04515657_0122 | SAMN04515657_0173 | Peptidyl-prolyl cis-trans isomerase B (cyclophilin B); 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 DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.844 |
SFT36819.1 | groL | SAMN04515657_0122 | SAMN04515657_1926 | Peptidyl-prolyl cis-trans isomerase B (cyclophilin B); 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. | Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.823 |
SFT36819.1 | htpG | SAMN04515657_0122 | SAMN04515657_1059 | Peptidyl-prolyl cis-trans isomerase B (cyclophilin B); 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 HtpG; Molecular chaperone. Has ATPase activity. | 0.954 |
SFT36819.1 | rpsE | SAMN04515657_0122 | SAMN04515657_2272 | Peptidyl-prolyl cis-trans isomerase B (cyclophilin B); 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. | SSU ribosomal protein S5P; 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. | 0.750 |
SFT36819.1 | rpsG | SAMN04515657_0122 | SAMN04515657_2614 | Peptidyl-prolyl cis-trans isomerase B (cyclophilin B); 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. | SSU ribosomal protein S7P; One of the primary rRNA binding proteins, it binds directly to 16S rRNA where it nucleates assembly of the head domain of the 30S subunit. Is located at the subunit interface close to the decoding center, probably blocks exit of the E-site tRNA; Belongs to the universal ribosomal protein uS7 family. | 0.729 |
SFT36819.1 | rpsQ | SAMN04515657_0122 | SAMN04515657_2257 | Peptidyl-prolyl cis-trans isomerase B (cyclophilin B); 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. | SSU ribosomal protein S17P; One of the primary rRNA binding proteins, it binds specifically to the 5'-end of 16S ribosomal RNA. | 0.933 |
SFT65769.1 | SFT36819.1 | SAMN04515657_1549 | SAMN04515657_0122 | ATP-dependent Zn proteases. | Peptidyl-prolyl cis-trans isomerase B (cyclophilin B); 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. | 0.868 |
SFT65769.1 | dnaJ | SAMN04515657_1549 | SAMN04515657_0174 | ATP-dependent Zn proteases. | 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, [...] | 0.991 |
SFT65769.1 | dnaK | SAMN04515657_1549 | SAMN04515657_0173 | ATP-dependent Zn proteases. | Molecular chaperone DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.997 |
SFT65769.1 | groL | SAMN04515657_1549 | SAMN04515657_1926 | ATP-dependent Zn proteases. | Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.969 |
SFT65769.1 | grpE | SAMN04515657_1549 | SAMN04515657_0172 | ATP-dependent Zn proteases. | 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 [...] | 0.972 |
SFT65769.1 | htpG | SAMN04515657_1549 | SAMN04515657_1059 | ATP-dependent Zn proteases. | Molecular chaperone HtpG; Molecular chaperone. Has ATPase activity. | 0.862 |
SFT65769.1 | rpsE | SAMN04515657_1549 | SAMN04515657_2272 | ATP-dependent Zn proteases. | SSU ribosomal protein S5P; 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. | 0.951 |
SFT65769.1 | rpsG | SAMN04515657_1549 | SAMN04515657_2614 | ATP-dependent Zn proteases. | SSU ribosomal protein S7P; One of the primary rRNA binding proteins, it binds directly to 16S rRNA where it nucleates assembly of the head domain of the 30S subunit. Is located at the subunit interface close to the decoding center, probably blocks exit of the E-site tRNA; Belongs to the universal ribosomal protein uS7 family. | 0.879 |
SFT65769.1 | rpsJ | SAMN04515657_1549 | SAMN04515657_2247 | ATP-dependent Zn proteases. | SSU ribosomal protein S10P; Involved in the binding of tRNA to the ribosomes. Belongs to the universal ribosomal protein uS10 family. | 0.974 |
SFT65769.1 | rpsQ | SAMN04515657_1549 | SAMN04515657_2257 | ATP-dependent Zn proteases. | SSU ribosomal protein S17P; One of the primary rRNA binding proteins, it binds specifically to the 5'-end of 16S ribosomal RNA. | 0.828 |
dnaJ | SFT36819.1 | SAMN04515657_0174 | SAMN04515657_0122 | 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, [...] | Peptidyl-prolyl cis-trans isomerase B (cyclophilin B); 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. | 0.952 |
dnaJ | SFT65769.1 | SAMN04515657_0174 | SAMN04515657_1549 | 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, [...] | ATP-dependent Zn proteases. | 0.991 |