| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| Ping_0936 | Ping_1387 | Ping_0936 | Ping_1387 | Cytochrome c oxidase, cbb3-type, subunit III; C-type cytochrome. Part of the cbb3-type cytochrome c oxidase complex. | PFAM: cytochrome c, class I; KEGG: sit:TM1040_1744 cytochrome c, class I. | 0.640 |
| Ping_0936 | Ping_1830 | Ping_0936 | Ping_1830 | Cytochrome c oxidase, cbb3-type, subunit III; C-type cytochrome. Part of the cbb3-type cytochrome c oxidase complex. | PFAM: cytochrome c, class I; KEGG: gox:GOX0585 cytochrome c subunit of aldehyde dehydrogenase. | 0.893 |
| Ping_0936 | Ping_2717 | Ping_0936 | Ping_2717 | Cytochrome c oxidase, cbb3-type, subunit III; C-type cytochrome. Part of the cbb3-type cytochrome c oxidase complex. | 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). | 0.983 |
| Ping_0936 | msrP | Ping_0936 | Ping_0576 | Cytochrome c oxidase, cbb3-type, subunit III; C-type cytochrome. Part of the cbb3-type cytochrome c oxidase complex. | Oxidoreductase, molybdopterin binding 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 able to [...] | 0.586 |
| Ping_1387 | Ping_0936 | Ping_1387 | Ping_0936 | PFAM: cytochrome c, class I; KEGG: sit:TM1040_1744 cytochrome c, class I. | Cytochrome c oxidase, cbb3-type, subunit III; C-type cytochrome. Part of the cbb3-type cytochrome c oxidase complex. | 0.640 |
| Ping_1387 | Ping_1830 | Ping_1387 | Ping_1830 | PFAM: cytochrome c, class I; KEGG: sit:TM1040_1744 cytochrome c, class I. | PFAM: cytochrome c, class I; KEGG: gox:GOX0585 cytochrome c subunit of aldehyde dehydrogenase. | 0.688 |
| Ping_1387 | Ping_2717 | Ping_1387 | Ping_2717 | PFAM: cytochrome c, class I; KEGG: sit:TM1040_1744 cytochrome c, class I. | 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). | 0.773 |
| Ping_1387 | Ping_2734 | Ping_1387 | Ping_2734 | PFAM: cytochrome c, class I; KEGG: sit:TM1040_1744 cytochrome c, class I. | PFAM: UspA domain protein; KEGG: eci:UTI89_C0610 universal stress protein UspG. | 0.501 |
| Ping_1387 | Ping_3097 | Ping_1387 | Ping_3097 | PFAM: cytochrome c, class I; KEGG: sit:TM1040_1744 cytochrome c, class I. | PFAM: major facilitator superfamily MFS_1; KEGG: sit:TM1040_1598 twin-arginine translocation pathway signal. | 0.413 |
| Ping_1387 | Ping_3674 | Ping_1387 | Ping_3674 | PFAM: cytochrome c, class I; KEGG: sit:TM1040_1744 cytochrome c, class I. | PFAM: Tripartite ATP-independent periplasmic transporter, DctQ component; KEGG: rde:RD1_1477 hypothetical protein. | 0.599 |
| Ping_1387 | Ping_3675 | Ping_1387 | Ping_3675 | PFAM: cytochrome c, class I; KEGG: sit:TM1040_1744 cytochrome c, class I. | PFAM: TRAP dicarboxylate transporter- DctP subunit; KEGG: rde:RD1_1478 C4-dicarboxylate transport system C4-dicarboxylate-binding protein, putative. | 0.567 |
| Ping_1387 | msrP | Ping_1387 | Ping_0576 | PFAM: cytochrome c, class I; KEGG: sit:TM1040_1744 cytochrome c, class I. | Oxidoreductase, molybdopterin binding 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 able to [...] | 0.591 |
| Ping_1830 | Ping_0936 | Ping_1830 | Ping_0936 | PFAM: cytochrome c, class I; KEGG: gox:GOX0585 cytochrome c subunit of aldehyde dehydrogenase. | Cytochrome c oxidase, cbb3-type, subunit III; C-type cytochrome. Part of the cbb3-type cytochrome c oxidase complex. | 0.893 |
| Ping_1830 | Ping_1387 | Ping_1830 | Ping_1387 | PFAM: cytochrome c, class I; KEGG: gox:GOX0585 cytochrome c subunit of aldehyde dehydrogenase. | PFAM: cytochrome c, class I; KEGG: sit:TM1040_1744 cytochrome c, class I. | 0.688 |
| Ping_1830 | Ping_2717 | Ping_1830 | Ping_2717 | PFAM: cytochrome c, class I; KEGG: gox:GOX0585 cytochrome c subunit of aldehyde dehydrogenase. | 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). | 0.858 |
| Ping_1830 | msrP | Ping_1830 | Ping_0576 | PFAM: cytochrome c, class I; KEGG: gox:GOX0585 cytochrome c subunit of aldehyde dehydrogenase. | Oxidoreductase, molybdopterin binding 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 able to [...] | 0.586 |
| Ping_2717 | Ping_0936 | Ping_2717 | Ping_0936 | 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 oxidase, cbb3-type, subunit III; C-type cytochrome. Part of the cbb3-type cytochrome c oxidase complex. | 0.983 |
| Ping_2717 | Ping_1387 | Ping_2717 | Ping_1387 | 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: cytochrome c, class I; KEGG: sit:TM1040_1744 cytochrome c, class I. | 0.773 |
| Ping_2717 | Ping_1830 | Ping_2717 | Ping_1830 | 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: cytochrome c, class I; KEGG: gox:GOX0585 cytochrome c subunit of aldehyde dehydrogenase. | 0.858 |
| Ping_2717 | msrP | Ping_2717 | Ping_0576 | 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 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 able to [...] | 0.700 |