node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
SFN87165.1 | SFO29911.1 | SAMN04489757_103104 | SAMN04489757_1173 | Molecular chaperone 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. | 0.754 |
SFN87165.1 | SFO34761.1 | SAMN04489757_103104 | SAMN04489757_11941 | Molecular chaperone DnaJ. | Molecular chaperone HtpG. | 0.964 |
SFN87165.1 | SFO46874.1 | SAMN04489757_103104 | SAMN04489757_12917 | Molecular chaperone DnaJ. | PglZ domain-containing protein. | 0.754 |
SFN87165.1 | dnaK | SAMN04489757_103104 | SAMN04489757_104126 | Molecular chaperone DnaJ. | Molecular chaperone DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.999 |
SFN87165.1 | groL | SAMN04489757_103104 | SAMN04489757_10746 | Molecular chaperone DnaJ. | Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.863 |
SFN87165.1 | groS | SAMN04489757_103104 | SAMN04489757_10745 | Molecular chaperone DnaJ. | Chaperonin GroES; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.836 |
SFN87165.1 | guaB | SAMN04489757_103104 | SAMN04489757_10748 | Molecular chaperone DnaJ. | IMP dehydrogenase; Catalyzes the conversion of inosine 5'-phosphate (IMP) to xanthosine 5'-phosphate (XMP), the first committed and rate-limiting step in the de novo synthesis of guanine nucleotides, and therefore plays an important role in the regulation of cell growth. Belongs to the IMPDH/GMPR family. | 0.407 |
SFO29911.1 | SFN87165.1 | SAMN04489757_1173 | SAMN04489757_103104 | 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. | 0.754 |
SFO29911.1 | SFO34761.1 | SAMN04489757_1173 | SAMN04489757_11941 | 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. | 0.954 |
SFO29911.1 | SFO42495.1 | SAMN04489757_1173 | SAMN04489757_12510 | 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. | Hypothetical protein. | 0.754 |
SFO29911.1 | dnaJ | SAMN04489757_1173 | SAMN04489757_104127 | 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, [...] | 0.754 |
SFO29911.1 | dnaK | SAMN04489757_1173 | SAMN04489757_104126 | 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. | 0.693 |
SFO29911.1 | groS | SAMN04489757_1173 | SAMN04489757_10745 | 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 GroES; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.484 |
SFO34761.1 | SFN87165.1 | SAMN04489757_11941 | SAMN04489757_103104 | Molecular chaperone HtpG. | Molecular chaperone DnaJ. | 0.964 |
SFO34761.1 | SFO29911.1 | SAMN04489757_11941 | SAMN04489757_1173 | Molecular chaperone HtpG. | 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. | 0.954 |
SFO34761.1 | SFO40808.1 | SAMN04489757_11941 | SAMN04489757_12357 | Molecular chaperone HtpG. | Tetratricopeptide repeat-containing protein. | 0.958 |
SFO34761.1 | SFO42495.1 | SAMN04489757_11941 | SAMN04489757_12510 | Molecular chaperone HtpG. | Hypothetical protein. | 0.948 |
SFO34761.1 | SFO46874.1 | SAMN04489757_11941 | SAMN04489757_12917 | Molecular chaperone HtpG. | PglZ domain-containing protein. | 0.948 |
SFO34761.1 | dnaJ | SAMN04489757_11941 | SAMN04489757_104127 | Molecular chaperone HtpG. | 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, [...] | 0.964 |
SFO34761.1 | dnaK | SAMN04489757_11941 | SAMN04489757_104126 | Molecular chaperone HtpG. | Molecular chaperone DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.999 |