| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| DM40_101 | DM40_4431 | DM40_101 | DM40_4431 | Cytochrome c-551 domain protein. | Cytochrome c family protein. | 0.917 |
| DM40_101 | msrP | DM40_101 | DM40_1102 | Cytochrome c-551 domain protein. | Oxidoreductase molybdopterin binding domain protein; 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 a [...] | 0.651 |
| DM40_101 | ph | DM40_101 | DM40_996 | Cytochrome c-551 domain protein. | Cytochrome c domain protein. | 0.908 |
| DM40_1100 | msrP | DM40_1100 | DM40_1102 | resB-like family protein. | Oxidoreductase molybdopterin binding domain protein; 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 a [...] | 0.521 |
| DM40_1100 | msrQ | DM40_1100 | DM40_1103 | resB-like family protein. | Ferric reductase like transmembrane component family protein; 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 red [...] | 0.561 |
| DM40_4431 | DM40_101 | DM40_4431 | DM40_101 | Cytochrome c family protein. | Cytochrome c-551 domain protein. | 0.917 |
| DM40_4431 | msrP | DM40_4431 | DM40_1102 | Cytochrome c family protein. | Oxidoreductase molybdopterin binding domain protein; 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 a [...] | 0.651 |
| DM40_4431 | ph | DM40_4431 | DM40_996 | Cytochrome c family protein. | Cytochrome c domain protein. | 0.913 |
| DM40_5852 | coxB | DM40_5852 | DM40_449 | Cytochrome c family protein. | 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). | 0.666 |
| DM40_5852 | coxB-2 | DM40_5852 | DM40_5107 | Cytochrome c family protein. | coxB: cytochrome c oxidase, subunit II. | 0.900 |
| DM40_5852 | coxB-3 | DM40_5852 | DM40_5123 | Cytochrome c family protein. | coxB: cytochrome c oxidase, subunit II. | 0.900 |
| DM40_5852 | msrP | DM40_5852 | DM40_1102 | Cytochrome c family protein. | Oxidoreductase molybdopterin binding domain protein; 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 a [...] | 0.549 |
| coxB | DM40_5852 | DM40_449 | DM40_5852 | 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). | Cytochrome c family protein. | 0.666 |
| coxB | coxB-2 | DM40_449 | DM40_5107 | 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). | coxB: cytochrome c oxidase, subunit II. | 0.998 |
| coxB | coxB-3 | DM40_449 | DM40_5123 | 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). | coxB: cytochrome c oxidase, subunit II. | 0.998 |
| coxB | msrP | DM40_449 | DM40_1102 | 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). | Oxidoreductase molybdopterin binding domain protein; 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 a [...] | 0.574 |
| coxB-2 | DM40_5852 | DM40_5107 | DM40_5852 | coxB: cytochrome c oxidase, subunit II. | Cytochrome c family protein. | 0.900 |
| coxB-2 | coxB | DM40_5107 | DM40_449 | coxB: cytochrome c oxidase, subunit II. | 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). | 0.998 |
| coxB-2 | coxB-3 | DM40_5107 | DM40_5123 | coxB: cytochrome c oxidase, subunit II. | coxB: cytochrome c oxidase, subunit II. | 0.998 |
| coxB-2 | msrP | DM40_5107 | DM40_1102 | coxB: cytochrome c oxidase, subunit II. | Oxidoreductase molybdopterin binding domain protein; 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 a [...] | 0.755 |