| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| AJC20353.1 | AJC23033.1 | RO07_07500 | RO07_03675 | Derived by automated computational analysis using gene prediction method: Protein Homology. | Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.910 |
| AJC20353.1 | yedY_2 | RO07_07500 | RO07_06720 | Derived by automated computational analysis using gene prediction method: Protein Homology. | Mononuclear molybdenum enzyme YedY; Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine generated by the host defense mechanisms. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated periplasmic proteins from methionine oxidation. The catalytic subunit MsrP is non-stereospecific, being able to reduce bot [...] | 0.445 |
| AJC21699.1 | ctaC_1 | RO07_16615 | RO07_11010 | 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). | 0.797 |
| AJC21699.1 | yedY_2 | RO07_16615 | RO07_06720 | Hypothetical protein; Derived by automated computational analysis using gene prediction method: GeneMarkS+. | Mononuclear molybdenum enzyme YedY; Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine generated by the host defense mechanisms. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated periplasmic proteins from methionine oxidation. The catalytic subunit MsrP is non-stereospecific, being able to reduce bot [...] | 0.520 |
| AJC23033.1 | AJC20353.1 | RO07_03675 | RO07_07500 | Derived by automated computational analysis using gene prediction method: Protein Homology. | Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.910 |
| AJC23033.1 | ctaC_1 | RO07_03675 | RO07_11010 | 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). | 0.914 |
| AJC23033.1 | ctaC_2 | RO07_03675 | RO07_07395 | Derived by automated computational analysis using gene prediction method: Protein Homology. | Cytochrome c oxidase subunit I; Incomplete; partial on complete genome; missing stop; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.616 |
| AJC23033.1 | yedY_2 | RO07_03675 | RO07_06720 | Derived by automated computational analysis using gene prediction method: Protein Homology. | Mononuclear molybdenum enzyme YedY; Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine generated by the host defense mechanisms. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated periplasmic proteins from methionine oxidation. The catalytic subunit MsrP is non-stereospecific, being able to reduce bot [...] | 0.521 |
| AJC23129.1 | ccsB | RO07_06725 | RO07_06730 | C-type cytochrome biogenesis protein CcsB; Derived by automated computational analysis using gene prediction method: Protein Homology. | Cytochrome C biogenesis protein ResB; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.994 |
| AJC23129.1 | ctaC_1 | RO07_06725 | RO07_11010 | C-type cytochrome biogenesis protein CcsB; 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). | 0.428 |
| AJC23129.1 | ctaC_2 | RO07_06725 | RO07_07395 | C-type cytochrome biogenesis protein CcsB; Derived by automated computational analysis using gene prediction method: Protein Homology. | Cytochrome c oxidase subunit I; Incomplete; partial on complete genome; missing stop; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.438 |
| AJC23129.1 | yedY_2 | RO07_06725 | RO07_06720 | C-type cytochrome biogenesis protein CcsB; Derived by automated computational analysis using gene prediction method: Protein Homology. | Mononuclear molybdenum enzyme YedY; Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine generated by the host defense mechanisms. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated periplasmic proteins from methionine oxidation. The catalytic subunit MsrP is non-stereospecific, being able to reduce bot [...] | 0.511 |
| AJC23129.1 | yedZ | RO07_06725 | RO07_06715 | C-type cytochrome biogenesis protein CcsB; Derived by automated computational analysis using gene prediction method: Protein Homology. | Sulfoxide reductase heme-binding subunit YedZ; Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine generated by the host defense mechanisms. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated periplasmic proteins from methionine oxidation. MsrQ provides electrons for reduction to the reductase catalyti [...] | 0.446 |
| AJC23144.1 | ctaC_1 | RO07_07485 | RO07_11010 | Sulfur oxidation c-type cytochrome SoxA; 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). | 0.797 |
| AJC23144.1 | yedY_2 | RO07_07485 | RO07_06720 | Sulfur oxidation c-type cytochrome SoxA; Derived by automated computational analysis using gene prediction method: Protein Homology. | Mononuclear molybdenum enzyme YedY; Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine generated by the host defense mechanisms. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated periplasmic proteins from methionine oxidation. The catalytic subunit MsrP is non-stereospecific, being able to reduce bot [...] | 0.520 |
| ccsB | AJC23129.1 | RO07_06730 | RO07_06725 | Cytochrome C biogenesis protein ResB; Derived by automated computational analysis using gene prediction method: Protein Homology. | C-type cytochrome biogenesis protein CcsB; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.994 |
| ccsB | yedY_2 | RO07_06730 | RO07_06720 | Cytochrome C biogenesis protein ResB; Derived by automated computational analysis using gene prediction method: Protein Homology. | Mononuclear molybdenum enzyme YedY; Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine generated by the host defense mechanisms. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated periplasmic proteins from methionine oxidation. The catalytic subunit MsrP is non-stereospecific, being able to reduce bot [...] | 0.506 |
| ccsB | yedZ | RO07_06730 | RO07_06715 | Cytochrome C biogenesis protein ResB; Derived by automated computational analysis using gene prediction method: Protein Homology. | Sulfoxide reductase heme-binding subunit YedZ; Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine generated by the host defense mechanisms. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated periplasmic proteins from methionine oxidation. MsrQ provides electrons for reduction to the reductase catalyti [...] | 0.426 |
| ctaC_1 | AJC21699.1 | RO07_11010 | RO07_16615 | 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+. | 0.797 |
| ctaC_1 | AJC23033.1 | RO07_11010 | RO07_03675 | 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). | Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.914 |
