| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| MCP_0070 | MCP_2698 | MCP_0070 | MCP_2698 | Peroxiredoxin. | Protein kinase; Contains at least one Tetratricopeptide region domain (IPR013026); Contains at least three Tetratricopeptide TPR_1 repeats (IPR001440).; Contains at least five Tetratricopeptide TPR_2repeats (IPR013105). | 0.599 |
| MCP_0070 | dnaK | MCP_0070 | MCP_2019 | Peroxiredoxin. | Heat shock protein 70; Acts as a chaperone. | 0.713 |
| MCP_0070 | trxA | MCP_0070 | MCP_0039 | Peroxiredoxin. | Thioredoxin. | 0.689 |
| MCP_0070 | trxB-2 | MCP_0070 | MCP_0680 | Peroxiredoxin. | Putative thioredoxin reductase. | 0.702 |
| MCP_0070 | trxB-3 | MCP_0070 | MCP_1904 | Peroxiredoxin. | Putative thioredoxin reductase. | 0.702 |
| MCP_0970 | dnaK | MCP_0970 | MCP_2019 | Putative FAD-dependent pyridine nucleotide-disulphide oxidoreductase; Belongs to the class-I pyridine nucleotide-disulfide oxidoreductase family. | Heat shock protein 70; Acts as a chaperone. | 0.514 |
| MCP_0970 | trxA | MCP_0970 | MCP_0039 | Putative FAD-dependent pyridine nucleotide-disulphide oxidoreductase; Belongs to the class-I pyridine nucleotide-disulfide oxidoreductase family. | Thioredoxin. | 0.708 |
| MCP_0970 | trxB-2 | MCP_0970 | MCP_0680 | Putative FAD-dependent pyridine nucleotide-disulphide oxidoreductase; Belongs to the class-I pyridine nucleotide-disulfide oxidoreductase family. | Putative thioredoxin reductase. | 0.551 |
| MCP_0970 | trxB-3 | MCP_0970 | MCP_1904 | Putative FAD-dependent pyridine nucleotide-disulphide oxidoreductase; Belongs to the class-I pyridine nucleotide-disulfide oxidoreductase family. | Putative thioredoxin reductase. | 0.551 |
| MCP_2009 | MCP_2698 | MCP_2009 | MCP_2698 | Conserved hypothetical protein; Contains one Heat shock protein DnaJ, N-terminal domain (IPR001623). | Protein kinase; Contains at least one Tetratricopeptide region domain (IPR013026); Contains at least three Tetratricopeptide TPR_1 repeats (IPR001440).; Contains at least five Tetratricopeptide TPR_2repeats (IPR013105). | 0.969 |
| MCP_2009 | dnaK | MCP_2009 | MCP_2019 | Conserved hypothetical protein; Contains one Heat shock protein DnaJ, N-terminal domain (IPR001623). | Heat shock protein 70; Acts as a chaperone. | 0.998 |
| MCP_2009 | trxA | MCP_2009 | MCP_0039 | Conserved hypothetical protein; Contains one Heat shock protein DnaJ, N-terminal domain (IPR001623). | Thioredoxin. | 0.710 |
| MCP_2698 | MCP_0070 | MCP_2698 | MCP_0070 | Protein kinase; Contains at least one Tetratricopeptide region domain (IPR013026); Contains at least three Tetratricopeptide TPR_1 repeats (IPR001440).; Contains at least five Tetratricopeptide TPR_2repeats (IPR013105). | Peroxiredoxin. | 0.599 |
| MCP_2698 | MCP_2009 | MCP_2698 | MCP_2009 | Protein kinase; Contains at least one Tetratricopeptide region domain (IPR013026); Contains at least three Tetratricopeptide TPR_1 repeats (IPR001440).; Contains at least five Tetratricopeptide TPR_2repeats (IPR013105). | Conserved hypothetical protein; Contains one Heat shock protein DnaJ, N-terminal domain (IPR001623). | 0.969 |
| MCP_2698 | dnaJ | MCP_2698 | MCP_2018 | Protein kinase; Contains at least one Tetratricopeptide region domain (IPR013026); Contains at least three Tetratricopeptide TPR_1 repeats (IPR001440).; Contains at least five Tetratricopeptide TPR_2repeats (IPR013105). | Heat shock protein 40; 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, Dn [...] | 0.968 |
| MCP_2698 | dnaK | MCP_2698 | MCP_2019 | Protein kinase; Contains at least one Tetratricopeptide region domain (IPR013026); Contains at least three Tetratricopeptide TPR_1 repeats (IPR001440).; Contains at least five Tetratricopeptide TPR_2repeats (IPR013105). | Heat shock protein 70; Acts as a chaperone. | 0.989 |
| MCP_2698 | msrA | MCP_2698 | MCP_1211 | Protein kinase; Contains at least one Tetratricopeptide region domain (IPR013026); Contains at least three Tetratricopeptide TPR_1 repeats (IPR001440).; Contains at least five Tetratricopeptide TPR_2repeats (IPR013105). | Peptide methionine sulfoxide reductase MsrA; Has an important function as a repair enzyme for proteins that have been inactivated by oxidation. Catalyzes the reversible oxidation-reduction of methionine sulfoxide in proteins to methionine. | 0.432 |
| MCP_2698 | trxA | MCP_2698 | MCP_0039 | Protein kinase; Contains at least one Tetratricopeptide region domain (IPR013026); Contains at least three Tetratricopeptide TPR_1 repeats (IPR001440).; Contains at least five Tetratricopeptide TPR_2repeats (IPR013105). | Thioredoxin. | 0.824 |
| dnaJ | MCP_2698 | MCP_2018 | MCP_2698 | Heat shock protein 40; 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, Dn [...] | Protein kinase; Contains at least one Tetratricopeptide region domain (IPR013026); Contains at least three Tetratricopeptide TPR_1 repeats (IPR001440).; Contains at least five Tetratricopeptide TPR_2repeats (IPR013105). | 0.968 |
| dnaJ | dnaK | MCP_2018 | MCP_2019 | Heat shock protein 40; 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, Dn [...] | Heat shock protein 70; Acts as a chaperone. | 0.999 |