| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| Dbac_0306 | Dbac_1908 | Dbac_0306 | Dbac_1908 | TIGRFAM: thioredoxin; PFAM: Thioredoxin domain; KEGG: mfa:Mfla_1161 thioredoxin. | PFAM: Thioredoxin domain; KEGG: sfu:Sfum_3604 thioredoxin domain. | 0.653 |
| Dbac_1538 | Dbac_1542 | Dbac_1538 | Dbac_1542 | 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). | KEGG: dde:Dde_1822 uncharacterized protein SCO1/SenC/PrrC. | 0.997 |
| Dbac_1538 | Dbac_1907 | Dbac_1538 | Dbac_1907 | 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). | TIGRFAM: redox-active disulfide protein 2; KEGG: dde:Dde_2778 redox-active disulfide protein 2. | 0.850 |
| Dbac_1538 | Dbac_1908 | Dbac_1538 | Dbac_1908 | 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). | PFAM: Thioredoxin domain; KEGG: sfu:Sfum_3604 thioredoxin domain. | 0.864 |
| Dbac_1538 | rpoB | Dbac_1538 | Dbac_2781 | 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). | DNA-directed RNA polymerase, beta subunit; DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. | 0.412 |
| Dbac_1542 | Dbac_1538 | Dbac_1542 | Dbac_1538 | KEGG: dde:Dde_1822 uncharacterized protein SCO1/SenC/PrrC. | 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). | 0.997 |
| Dbac_1542 | Dbac_1907 | Dbac_1542 | Dbac_1907 | KEGG: dde:Dde_1822 uncharacterized protein SCO1/SenC/PrrC. | TIGRFAM: redox-active disulfide protein 2; KEGG: dde:Dde_2778 redox-active disulfide protein 2. | 0.686 |
| Dbac_1542 | Dbac_1908 | Dbac_1542 | Dbac_1908 | KEGG: dde:Dde_1822 uncharacterized protein SCO1/SenC/PrrC. | PFAM: Thioredoxin domain; KEGG: sfu:Sfum_3604 thioredoxin domain. | 0.822 |
| Dbac_1730 | Dbac_1907 | Dbac_1730 | Dbac_1907 | PFAM: cytochrome c biogenesis protein transmembrane region; KEGG: dde:Dde_1301 thiol:disulfide interchange protein-like. | TIGRFAM: redox-active disulfide protein 2; KEGG: dde:Dde_2778 redox-active disulfide protein 2. | 0.644 |
| Dbac_1730 | Dbac_1908 | Dbac_1730 | Dbac_1908 | PFAM: cytochrome c biogenesis protein transmembrane region; KEGG: dde:Dde_1301 thiol:disulfide interchange protein-like. | PFAM: Thioredoxin domain; KEGG: sfu:Sfum_3604 thioredoxin domain. | 0.844 |
| Dbac_1730 | msrA | Dbac_1730 | Dbac_3441 | PFAM: cytochrome c biogenesis protein transmembrane region; KEGG: dde:Dde_1301 thiol:disulfide interchange protein-like. | Peptide methionine sulfoxide 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. | 0.831 |
| Dbac_1907 | Dbac_1538 | Dbac_1907 | Dbac_1538 | TIGRFAM: redox-active disulfide protein 2; KEGG: dde:Dde_2778 redox-active disulfide protein 2. | 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). | 0.850 |
| Dbac_1907 | Dbac_1542 | Dbac_1907 | Dbac_1542 | TIGRFAM: redox-active disulfide protein 2; KEGG: dde:Dde_2778 redox-active disulfide protein 2. | KEGG: dde:Dde_1822 uncharacterized protein SCO1/SenC/PrrC. | 0.686 |
| Dbac_1907 | Dbac_1730 | Dbac_1907 | Dbac_1730 | TIGRFAM: redox-active disulfide protein 2; KEGG: dde:Dde_2778 redox-active disulfide protein 2. | PFAM: cytochrome c biogenesis protein transmembrane region; KEGG: dde:Dde_1301 thiol:disulfide interchange protein-like. | 0.644 |
| Dbac_1907 | Dbac_1908 | Dbac_1907 | Dbac_1908 | TIGRFAM: redox-active disulfide protein 2; KEGG: dde:Dde_2778 redox-active disulfide protein 2. | PFAM: Thioredoxin domain; KEGG: sfu:Sfum_3604 thioredoxin domain. | 0.560 |
| Dbac_1907 | Dbac_1909 | Dbac_1907 | Dbac_1909 | TIGRFAM: redox-active disulfide protein 2; KEGG: dde:Dde_2778 redox-active disulfide protein 2. | PFAM: cytochrome c biogenesis protein transmembrane region; KEGG: dde:Dde_2782 hypothetical protein. | 0.849 |
| Dbac_1907 | Dbac_1910 | Dbac_1907 | Dbac_1910 | TIGRFAM: redox-active disulfide protein 2; KEGG: dde:Dde_2778 redox-active disulfide protein 2. | TIGRFAM: arsenical-resistance protein; PFAM: Bile acid:sodium symporter; KEGG: dsy:DSY4672 hypothetical protein. | 0.458 |
| Dbac_1907 | Dbac_2508 | Dbac_1907 | Dbac_2508 | TIGRFAM: redox-active disulfide protein 2; KEGG: dde:Dde_2778 redox-active disulfide protein 2. | PFAM: cytochrome c assembly protein; KEGG: dde:Dde_1477 cytochrome c-type biogenesis protein CcmF. | 0.402 |
| Dbac_1907 | msrA | Dbac_1907 | Dbac_3441 | TIGRFAM: redox-active disulfide protein 2; KEGG: dde:Dde_2778 redox-active disulfide protein 2. | Peptide methionine sulfoxide 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. | 0.803 |
| Dbac_1907 | rpoB | Dbac_1907 | Dbac_2781 | TIGRFAM: redox-active disulfide protein 2; KEGG: dde:Dde_2778 redox-active disulfide protein 2. | DNA-directed RNA polymerase, beta subunit; DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. | 0.584 |