node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
OAZ12622.1 | OAZ12664.1 | TH15_16840 | TH15_14650 | Peptidylprolyl 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 Hsp70; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.777 |
OAZ12622.1 | dnaJ | TH15_16840 | TH15_04095 | Peptidylprolyl 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, [...] | 0.954 |
OAZ12622.1 | dnaK | TH15_16840 | TH15_04100 | Peptidylprolyl 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 DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.833 |
OAZ12622.1 | groEL | TH15_16840 | TH15_22135 | Peptidylprolyl 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 GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.439 |
OAZ12622.1 | hscA | TH15_16840 | TH15_16530 | Peptidylprolyl 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. | Hypothetical protein; Chaperone involved in the maturation of iron-sulfur cluster- containing proteins. Has a low intrinsic ATPase activity which is markedly stimulated by HscB. | 0.777 |
OAZ12622.1 | htpG | TH15_16840 | TH15_11020 | Peptidylprolyl 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. | Heat shock protein 90; Molecular chaperone. Has ATPase activity. | 0.993 |
OAZ12622.1 | rplM | TH15_16840 | TH15_14535 | Peptidylprolyl 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. | 0.960 |
OAZ12622.1 | rplN | TH15_16840 | TH15_21620 | Peptidylprolyl 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 L14; Binds to 23S rRNA. Forms part of two intersubunit bridges in the 70S ribosome; Belongs to the universal ribosomal protein uL14 family. | 0.958 |
OAZ12622.1 | rplQ | TH15_16840 | TH15_21695 | Peptidylprolyl 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 L17; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.954 |
OAZ12664.1 | OAZ12622.1 | TH15_14650 | TH15_16840 | Molecular chaperone Hsp70; Derived by automated computational analysis using gene prediction method: Protein Homology. | Peptidylprolyl 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. | 0.777 |
OAZ12664.1 | OAZ15010.1 | TH15_14650 | TH15_04255 | Molecular chaperone Hsp70; Derived by automated computational analysis using gene prediction method: Protein Homology. | Heat shock protein GrpE; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.993 |
OAZ12664.1 | dnaJ | TH15_14650 | TH15_04095 | Molecular chaperone Hsp70; 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, [...] | 0.964 |
OAZ12664.1 | groEL | TH15_14650 | TH15_22135 | Molecular chaperone Hsp70; Derived by automated computational analysis using gene prediction method: Protein Homology. | Molecular chaperone GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.932 |
OAZ12664.1 | htpG | TH15_14650 | TH15_11020 | Molecular chaperone Hsp70; Derived by automated computational analysis using gene prediction method: Protein Homology. | Heat shock protein 90; Molecular chaperone. Has ATPase activity. | 0.997 |
OAZ12664.1 | rplM | TH15_14650 | TH15_14535 | Molecular chaperone Hsp70; 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. | 0.630 |
OAZ12664.1 | rplN | TH15_14650 | TH15_21620 | Molecular chaperone Hsp70; Derived by automated computational analysis using gene prediction method: Protein Homology. | 50S ribosomal protein L14; Binds to 23S rRNA. Forms part of two intersubunit bridges in the 70S ribosome; Belongs to the universal ribosomal protein uL14 family. | 0.693 |
OAZ15010.1 | OAZ12664.1 | TH15_04255 | TH15_14650 | Heat shock protein GrpE; Derived by automated computational analysis using gene prediction method: Protein Homology. | Molecular chaperone Hsp70; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.993 |
OAZ15010.1 | dnaJ | TH15_04255 | TH15_04095 | Heat shock protein GrpE; 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, [...] | 0.968 |
OAZ15010.1 | dnaK | TH15_04255 | TH15_04100 | Heat shock protein GrpE; 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. | 0.998 |
OAZ15010.1 | groEL | TH15_04255 | TH15_22135 | Heat shock protein GrpE; Derived by automated computational analysis using gene prediction method: Protein Homology. | Molecular chaperone GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.993 |