node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
OES43457.1 | OES43725.1 | BA724_13625 | BA724_11530 | Hypothetical protein; Derived by automated computational analysis using gene prediction method: GeneMarkS+. | Cytochrome c oxidase subunit II; Subunits I and II form the functional core of the enzyme complex. Electrons originating in cytochrome c are transferred via heme a and Cu(A) to the binuclear center formed by heme a3 and Cu(B). | 0.509 |
OES43457.1 | OES43753.1 | BA724_13625 | BA724_11690 | Hypothetical protein; Derived by automated computational analysis using gene prediction method: GeneMarkS+. | Thioredoxin; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.547 |
OES43457.1 | OES45292.1 | BA724_13625 | BA724_04600 | Hypothetical protein; Derived by automated computational analysis using gene prediction method: GeneMarkS+. | Thioredoxin; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.713 |
OES43457.1 | msrA-2 | BA724_13625 | BA724_09785 | Hypothetical protein; Derived by automated computational analysis using gene prediction method: GeneMarkS+. | Peptide-methionine (S)-S-oxide reductase; 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. | 0.540 |
OES43457.1 | msrB | BA724_13625 | BA724_09790 | Hypothetical protein; Derived by automated computational analysis using gene prediction method: GeneMarkS+. | Peptide-methionine (R)-S-oxide reductase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the MsrB Met sulfoxide reductase family. | 0.540 |
OES43725.1 | OES43457.1 | BA724_11530 | BA724_13625 | Cytochrome c oxidase subunit II; Subunits I and II form the functional core of the enzyme complex. Electrons originating in cytochrome c are transferred via heme a and Cu(A) to the binuclear center formed by heme a3 and Cu(B). | Hypothetical protein; Derived by automated computational analysis using gene prediction method: GeneMarkS+. | 0.509 |
OES43725.1 | OES43742.1 | BA724_11530 | BA724_11630 | Cytochrome c oxidase subunit II; Subunits I and II form the functional core of the enzyme complex. Electrons originating in cytochrome c are transferred via heme a and Cu(A) to the binuclear center formed by heme a3 and Cu(B). | Dihydrolipoyl dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.509 |
OES43725.1 | OES44415.1 | BA724_11530 | BA724_09045 | Cytochrome c oxidase subunit II; Subunits I and II form the functional core of the enzyme complex. Electrons originating in cytochrome c are transferred via heme a and Cu(A) to the binuclear center formed by heme a3 and Cu(B). | Dihydrolipoyl dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.509 |
OES43725.1 | OES45292.1 | BA724_11530 | BA724_04600 | Cytochrome c oxidase subunit II; Subunits I and II form the functional core of the enzyme complex. Electrons originating in cytochrome c are transferred via heme a and Cu(A) to the binuclear center formed by heme a3 and Cu(B). | Thioredoxin; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.922 |
OES43725.1 | dnaJ | BA724_11530 | BA724_08520 | Cytochrome c oxidase subunit II; Subunits I and II form the functional core of the enzyme complex. Electrons originating in cytochrome c are transferred via heme a and Cu(A) to the binuclear center formed by heme a3 and Cu(B). | 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, [...] | 0.672 |
OES43742.1 | OES43725.1 | BA724_11630 | BA724_11530 | Dihydrolipoyl dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology. | Cytochrome c oxidase subunit II; Subunits I and II form the functional core of the enzyme complex. Electrons originating in cytochrome c are transferred via heme a and Cu(A) to the binuclear center formed by heme a3 and Cu(B). | 0.509 |
OES43742.1 | OES43753.1 | BA724_11630 | BA724_11690 | Dihydrolipoyl dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology. | Thioredoxin; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.547 |
OES43742.1 | OES44415.1 | BA724_11630 | BA724_09045 | Dihydrolipoyl dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology. | Dihydrolipoyl dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.615 |
OES43742.1 | OES45292.1 | BA724_11630 | BA724_04600 | Dihydrolipoyl dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology. | Thioredoxin; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.713 |
OES43742.1 | msrA-2 | BA724_11630 | BA724_09785 | Dihydrolipoyl dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology. | Peptide-methionine (S)-S-oxide reductase; 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. | 0.540 |
OES43742.1 | msrB | BA724_11630 | BA724_09790 | Dihydrolipoyl dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology. | Peptide-methionine (R)-S-oxide reductase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the MsrB Met sulfoxide reductase family. | 0.540 |
OES43753.1 | OES43457.1 | BA724_11690 | BA724_13625 | Thioredoxin; Derived by automated computational analysis using gene prediction method: Protein Homology. | Hypothetical protein; Derived by automated computational analysis using gene prediction method: GeneMarkS+. | 0.547 |
OES43753.1 | OES43742.1 | BA724_11690 | BA724_11630 | Thioredoxin; Derived by automated computational analysis using gene prediction method: Protein Homology. | Dihydrolipoyl dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.547 |
OES43753.1 | OES44415.1 | BA724_11690 | BA724_09045 | Thioredoxin; Derived by automated computational analysis using gene prediction method: Protein Homology. | Dihydrolipoyl dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.547 |
OES43753.1 | OES45292.1 | BA724_11690 | BA724_04600 | Thioredoxin; Derived by automated computational analysis using gene prediction method: Protein Homology. | Thioredoxin; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.862 |