| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| HtpG_2 | PpiB | CLOSCI_00176 | CLOSCI_01597 | Ser/Thr phosphatase family protein; KEGG: hpa:HPAG1_0211 1.2e-08 chaperone and heat shock protein 90; COG: COG0326 Molecular chaperone, HSP90 family; Psort location: Cytoplasmic, score: 9.65. | Peptidyl-prolyl cis-trans isomerase, cyclophilin-type; 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. | 0.891 |
| HtpG_2 | dnaJ | CLOSCI_00176 | CLOSCI_01191 | Ser/Thr phosphatase family protein; KEGG: hpa:HPAG1_0211 1.2e-08 chaperone and heat shock protein 90; COG: COG0326 Molecular chaperone, HSP90 family; Psort location: Cytoplasmic, score: 9.65. | Chaperone protein 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, D [...] | 0.726 |
| HtpG_2 | dnaJ_1 | CLOSCI_00176 | CLOSCI_00879 | Ser/Thr phosphatase family protein; KEGG: hpa:HPAG1_0211 1.2e-08 chaperone and heat shock protein 90; COG: COG0326 Molecular chaperone, HSP90 family; Psort location: Cytoplasmic, score: 9.65. | Putative chaperone protein DnaJ; KEGG: cme:CMJ043C 5.2e-07 phycocyanobilin lyase alpha subunit K02288; COG: COG0484 DnaJ-class molecular chaperone with C-terminal Zn finger domain; Psort location: Cytoplasmic, score: 9.65. | 0.726 |
| HtpG_2 | dnaJ_2 | CLOSCI_00176 | CLOSCI_03204 | Ser/Thr phosphatase family protein; KEGG: hpa:HPAG1_0211 1.2e-08 chaperone and heat shock protein 90; COG: COG0326 Molecular chaperone, HSP90 family; Psort location: Cytoplasmic, score: 9.65. | DnaJ domain protein; KEGG: cya:CYA_0373 0.00021 serine/threonine protein kinase K00924; COG: COG0484 DnaJ-class molecular chaperone with C-terminal Zn finger domain; Psort location: Cytoplasmic, score: 9.65. | 0.726 |
| HtpG_2 | dnaJ_3 | CLOSCI_00176 | CLOSCI_01311 | Ser/Thr phosphatase family protein; KEGG: hpa:HPAG1_0211 1.2e-08 chaperone and heat shock protein 90; COG: COG0326 Molecular chaperone, HSP90 family; Psort location: Cytoplasmic, score: 9.65. | DnaJ domain protein; COG: COG0484 DnaJ-class molecular chaperone with C-terminal Zn finger domain; Psort location: Cytoplasmic, score: 8.87. | 0.726 |
| HtpG_2 | dnaK | CLOSCI_00176 | CLOSCI_01190 | Ser/Thr phosphatase family protein; KEGG: hpa:HPAG1_0211 1.2e-08 chaperone and heat shock protein 90; COG: COG0326 Molecular chaperone, HSP90 family; Psort location: Cytoplasmic, score: 9.65. | Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.980 |
| HtpG_2 | groL | CLOSCI_00176 | CLOSCI_00050 | Ser/Thr phosphatase family protein; KEGG: hpa:HPAG1_0211 1.2e-08 chaperone and heat shock protein 90; COG: COG0326 Molecular chaperone, HSP90 family; Psort location: Cytoplasmic, score: 9.65. | Chaperonin GroL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.924 |
| HtpG_2 | groS | CLOSCI_00176 | CLOSCI_00049 | Ser/Thr phosphatase family protein; KEGG: hpa:HPAG1_0211 1.2e-08 chaperone and heat shock protein 90; COG: COG0326 Molecular chaperone, HSP90 family; Psort location: Cytoplasmic, score: 9.65. | Chaperonin GroS; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.797 |
| HtpG_2 | grpE | CLOSCI_00176 | CLOSCI_01189 | Ser/Thr phosphatase family protein; KEGG: hpa:HPAG1_0211 1.2e-08 chaperone and heat shock protein 90; COG: COG0326 Molecular chaperone, HSP90 family; Psort location: Cytoplasmic, score: 9.65. | Co-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-depend [...] | 0.717 |
| HtpG_2 | lon | CLOSCI_00176 | CLOSCI_03704 | Ser/Thr phosphatase family protein; KEGG: hpa:HPAG1_0211 1.2e-08 chaperone and heat shock protein 90; COG: COG0326 Molecular chaperone, HSP90 family; Psort location: Cytoplasmic, score: 9.65. | Endopeptidase La; ATP-dependent serine protease that mediates the selective degradation of mutant and abnormal proteins as well as certain short- lived regulatory proteins. Required for cellular homeostasis and for survival from DNA damage and developmental changes induced by stress. Degrades polypeptides processively to yield small peptide fragments that are 5 to 10 amino acids long. Binds to DNA in a double-stranded, site-specific manner. | 0.746 |
| PpiB | HtpG_2 | CLOSCI_01597 | CLOSCI_00176 | Peptidyl-prolyl cis-trans isomerase, cyclophilin-type; 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. | Ser/Thr phosphatase family protein; KEGG: hpa:HPAG1_0211 1.2e-08 chaperone and heat shock protein 90; COG: COG0326 Molecular chaperone, HSP90 family; Psort location: Cytoplasmic, score: 9.65. | 0.891 |
| PpiB | dnaJ | CLOSCI_01597 | CLOSCI_01191 | Peptidyl-prolyl cis-trans isomerase, cyclophilin-type; 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. | Chaperone protein 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, D [...] | 0.631 |
| PpiB | dnaJ_1 | CLOSCI_01597 | CLOSCI_00879 | Peptidyl-prolyl cis-trans isomerase, cyclophilin-type; 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. | Putative chaperone protein DnaJ; KEGG: cme:CMJ043C 5.2e-07 phycocyanobilin lyase alpha subunit K02288; COG: COG0484 DnaJ-class molecular chaperone with C-terminal Zn finger domain; Psort location: Cytoplasmic, score: 9.65. | 0.631 |
| PpiB | dnaJ_2 | CLOSCI_01597 | CLOSCI_03204 | Peptidyl-prolyl cis-trans isomerase, cyclophilin-type; 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. | DnaJ domain protein; KEGG: cya:CYA_0373 0.00021 serine/threonine protein kinase K00924; COG: COG0484 DnaJ-class molecular chaperone with C-terminal Zn finger domain; Psort location: Cytoplasmic, score: 9.65. | 0.631 |
| PpiB | dnaJ_3 | CLOSCI_01597 | CLOSCI_01311 | Peptidyl-prolyl cis-trans isomerase, cyclophilin-type; 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. | DnaJ domain protein; COG: COG0484 DnaJ-class molecular chaperone with C-terminal Zn finger domain; Psort location: Cytoplasmic, score: 8.87. | 0.631 |
| PpiB | dnaK | CLOSCI_01597 | CLOSCI_01190 | Peptidyl-prolyl cis-trans isomerase, cyclophilin-type; 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. | Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.882 |
| PpiB | groS | CLOSCI_01597 | CLOSCI_00049 | Peptidyl-prolyl cis-trans isomerase, cyclophilin-type; 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 GroS; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.773 |
| dnaJ | HtpG_2 | CLOSCI_01191 | CLOSCI_00176 | Chaperone protein 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, D [...] | Ser/Thr phosphatase family protein; KEGG: hpa:HPAG1_0211 1.2e-08 chaperone and heat shock protein 90; COG: COG0326 Molecular chaperone, HSP90 family; Psort location: Cytoplasmic, score: 9.65. | 0.726 |
| dnaJ | PpiB | CLOSCI_01191 | CLOSCI_01597 | Chaperone protein 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, D [...] | Peptidyl-prolyl cis-trans isomerase, cyclophilin-type; 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. | 0.631 |
| dnaJ | dnaK | CLOSCI_01191 | CLOSCI_01190 | Chaperone protein 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, D [...] | Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.995 |