| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| Cagg_0631 | Cagg_3530 | Cagg_0631 | Cagg_3530 | TIGRFAM: LPXTG-motif cell wall anchor domain protein; PFAM: metallophosphoesterase; 5'-Nucleotidase domain protein; KEGG: cau:Caur_3261 5'-nucleotidase domain-containing protein; Belongs to the 5'-nucleotidase family. | KEGG: cau:Caur_3002 hypothetical protein. | 0.400 |
| Cagg_1452 | Cagg_1522 | Cagg_1452 | Cagg_1522 | PFAM: oxidoreductase molybdopterin binding; KEGG: cau:Caur_2488 oxidoreductase molybdopterin binding. | 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). | 0.456 |
| Cagg_1452 | Cagg_1526 | Cagg_1452 | Cagg_1526 | PFAM: oxidoreductase molybdopterin binding; KEGG: cau:Caur_2488 oxidoreductase molybdopterin binding. | KEGG: cau:Caur_2137 hypothetical protein. | 0.456 |
| Cagg_1452 | Cagg_3045 | Cagg_1452 | Cagg_3045 | PFAM: oxidoreductase molybdopterin binding; KEGG: cau:Caur_2488 oxidoreductase molybdopterin binding. | PFAM: oxidoreductase molybdopterin binding; KEGG: cau:Caur_2348 oxidoreductase molybdopterin binding. | 0.665 |
| Cagg_1452 | Cagg_3383 | Cagg_1452 | Cagg_3383 | PFAM: oxidoreductase molybdopterin binding; KEGG: cau:Caur_2488 oxidoreductase molybdopterin binding. | KEGG: cau:Caur_0625 hypothetical protein. | 0.456 |
| Cagg_1452 | Cagg_3384 | Cagg_1452 | Cagg_3384 | PFAM: oxidoreductase molybdopterin binding; KEGG: cau:Caur_2488 oxidoreductase molybdopterin binding. | KEGG: cau:Caur_0624 transmembrane prediction. | 0.456 |
| Cagg_1452 | Cagg_3530 | Cagg_1452 | Cagg_3530 | PFAM: oxidoreductase molybdopterin binding; KEGG: cau:Caur_2488 oxidoreductase molybdopterin binding. | KEGG: cau:Caur_3002 hypothetical protein. | 0.631 |
| Cagg_1520 | Cagg_1522 | Cagg_1520 | Cagg_1522 | PFAM: cytochrome c oxidase subunit III; KEGG: cau:Caur_2143 cytochrome c oxidase subunit III. | 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). | 0.999 |
| Cagg_1520 | Cagg_1526 | Cagg_1520 | Cagg_1526 | PFAM: cytochrome c oxidase subunit III; KEGG: cau:Caur_2143 cytochrome c oxidase subunit III. | KEGG: cau:Caur_2137 hypothetical protein. | 0.987 |
| Cagg_1520 | Cagg_3383 | Cagg_1520 | Cagg_3383 | PFAM: cytochrome c oxidase subunit III; KEGG: cau:Caur_2143 cytochrome c oxidase subunit III. | KEGG: cau:Caur_0625 hypothetical protein. | 0.984 |
| Cagg_1520 | Cagg_3384 | Cagg_1520 | Cagg_3384 | PFAM: cytochrome c oxidase subunit III; KEGG: cau:Caur_2143 cytochrome c oxidase subunit III. | KEGG: cau:Caur_0624 transmembrane prediction. | 0.985 |
| Cagg_1520 | Cagg_3530 | Cagg_1520 | Cagg_3530 | PFAM: cytochrome c oxidase subunit III; KEGG: cau:Caur_2143 cytochrome c oxidase subunit III. | KEGG: cau:Caur_3002 hypothetical protein. | 0.404 |
| Cagg_1522 | Cagg_1452 | Cagg_1522 | Cagg_1452 | 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: oxidoreductase molybdopterin binding; KEGG: cau:Caur_2488 oxidoreductase molybdopterin binding. | 0.456 |
| Cagg_1522 | Cagg_1520 | Cagg_1522 | Cagg_1520 | 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 oxidase subunit III; KEGG: cau:Caur_2143 cytochrome c oxidase subunit III. | 0.999 |
| Cagg_1522 | Cagg_1526 | Cagg_1522 | Cagg_1526 | 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: cau:Caur_2137 hypothetical protein. | 0.991 |
| Cagg_1522 | Cagg_3045 | Cagg_1522 | Cagg_3045 | 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: oxidoreductase molybdopterin binding; KEGG: cau:Caur_2348 oxidoreductase molybdopterin binding. | 0.456 |
| Cagg_1522 | Cagg_3383 | Cagg_1522 | Cagg_3383 | 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: cau:Caur_0625 hypothetical protein. | 0.985 |
| Cagg_1522 | Cagg_3384 | Cagg_1522 | Cagg_3384 | 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: cau:Caur_0624 transmembrane prediction. | 0.986 |
| Cagg_1522 | Cagg_3530 | Cagg_1522 | Cagg_3530 | 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: cau:Caur_3002 hypothetical protein. | 0.493 |
| Cagg_1522 | msrP | Cagg_1522 | Cagg_2049 | 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; Part of the MsrPQ system that repairs oxidized cell envelope 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. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated cell envelope proteins from methionine oxidation. The catalytic subunit MsrP is non-stereospecific, being able to reduce both (R-) and (S-) diastereoisomers of [...] | 0.456 |