| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| CCH87930.1 | CCH88231.1 | MODMU_2501 | MODMU_2802 | Protein of unknown function; No homology to any previously reported sequences. | Major intrinsic protein; Belongs to the MIP/aquaporin (TC 1.A.8) family. | 0.627 |
| CCH87930.1 | dnaJ | MODMU_2501 | MODMU_1760 | Protein of unknown function; No homology to any previously reported sequences. | Chaperone Hsp40, co-chaperone with DnaK; 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 interaction [...] | 0.727 |
| CCH87930.1 | dnaJ-2 | MODMU_2501 | MODMU_5177 | Protein of unknown function; No homology to any previously reported sequences. | Chaperone protein dnaJ, heat shock protein (Hsp40), co-chaperone with dnaK; 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 [...] | 0.727 |
| CCH88230.1 | CCH88231.1 | MODMU_2801 | MODMU_2802 | Protein of unknown function; No homology to any previously reported sequences. | Major intrinsic protein; Belongs to the MIP/aquaporin (TC 1.A.8) family. | 0.773 |
| CCH88231.1 | CCH87930.1 | MODMU_2802 | MODMU_2501 | Major intrinsic protein; Belongs to the MIP/aquaporin (TC 1.A.8) family. | Protein of unknown function; No homology to any previously reported sequences. | 0.627 |
| CCH88231.1 | CCH88230.1 | MODMU_2802 | MODMU_2801 | Major intrinsic protein; Belongs to the MIP/aquaporin (TC 1.A.8) family. | Protein of unknown function; No homology to any previously reported sequences. | 0.773 |
| CCH88231.1 | arsC-2 | MODMU_2802 | MODMU_1927 | Major intrinsic protein; Belongs to the MIP/aquaporin (TC 1.A.8) family. | Protein-tyrosine phosphatase ArsC; Function of strongly homologous gene; enzyme; Belongs to the low molecular weight phosphotyrosine protein phosphatase family. | 0.607 |
| CCH88231.1 | dnaJ | MODMU_2802 | MODMU_1760 | Major intrinsic protein; Belongs to the MIP/aquaporin (TC 1.A.8) family. | Chaperone Hsp40, co-chaperone with DnaK; 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 interaction [...] | 0.668 |
| CCH88231.1 | dnaJ-2 | MODMU_2802 | MODMU_5177 | Major intrinsic protein; Belongs to the MIP/aquaporin (TC 1.A.8) family. | Chaperone protein dnaJ, heat shock protein (Hsp40), co-chaperone with dnaK; 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 [...] | 0.668 |
| CCH88231.1 | glpK | MODMU_2802 | MODMU_5537 | Major intrinsic protein; Belongs to the MIP/aquaporin (TC 1.A.8) family. | Glycerol kinase; Key enzyme in the regulation of glycerol uptake and metabolism. Catalyzes the phosphorylation of glycerol to yield sn- glycerol 3-phosphate; Belongs to the FGGY kinase family. | 0.622 |
| CCH88231.1 | glpK-2 | MODMU_2802 | MODMU_5539 | Major intrinsic protein; Belongs to the MIP/aquaporin (TC 1.A.8) family. | Glycerol kinase; Key enzyme in the regulation of glycerol uptake and metabolism. Catalyzes the phosphorylation of glycerol to yield sn- glycerol 3-phosphate; Belongs to the FGGY kinase family. | 0.622 |
| CCH88231.1 | grpE | MODMU_2802 | MODMU_5178 | Major intrinsic protein; Belongs to the MIP/aquaporin (TC 1.A.8) family. | Molecular chaperone GrpE (Heat shock protein); 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. [...] | 0.658 |
| CCH88231.1 | trpA | MODMU_2802 | MODMU_3405 | Major intrinsic protein; Belongs to the MIP/aquaporin (TC 1.A.8) family. | Tryptophan synthase alpha chain; The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate. Belongs to the TrpA family. | 0.755 |
| CCH88231.1 | trpD | MODMU_2802 | MODMU_3527 | Major intrinsic protein; Belongs to the MIP/aquaporin (TC 1.A.8) family. | Anthranilate phosphoribosyltransferase; Catalyzes the transfer of the phosphoribosyl group of 5- phosphorylribose-1-pyrophosphate (PRPP) to anthranilate to yield N-(5'- phosphoribosyl)-anthranilate (PRA). | 0.749 |
| arsC-2 | CCH88231.1 | MODMU_1927 | MODMU_2802 | Protein-tyrosine phosphatase ArsC; Function of strongly homologous gene; enzyme; Belongs to the low molecular weight phosphotyrosine protein phosphatase family. | Major intrinsic protein; Belongs to the MIP/aquaporin (TC 1.A.8) family. | 0.607 |
| dnaJ | CCH87930.1 | MODMU_1760 | MODMU_2501 | Chaperone Hsp40, co-chaperone with DnaK; 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 interaction [...] | Protein of unknown function; No homology to any previously reported sequences. | 0.727 |
| dnaJ | CCH88231.1 | MODMU_1760 | MODMU_2802 | Chaperone Hsp40, co-chaperone with DnaK; 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 interaction [...] | Major intrinsic protein; Belongs to the MIP/aquaporin (TC 1.A.8) family. | 0.668 |
| dnaJ | grpE | MODMU_1760 | MODMU_5178 | Chaperone Hsp40, co-chaperone with DnaK; 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 interaction [...] | Molecular chaperone GrpE (Heat shock protein); 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. [...] | 0.980 |
| dnaJ-2 | CCH87930.1 | MODMU_5177 | MODMU_2501 | Chaperone protein dnaJ, heat shock protein (Hsp40), co-chaperone with dnaK; 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 [...] | Protein of unknown function; No homology to any previously reported sequences. | 0.727 |
| dnaJ-2 | CCH88231.1 | MODMU_5177 | MODMU_2802 | Chaperone protein dnaJ, heat shock protein (Hsp40), co-chaperone with dnaK; 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 [...] | Major intrinsic protein; Belongs to the MIP/aquaporin (TC 1.A.8) family. | 0.668 |