| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| Meso_0741 | Meso_0746 | Meso_0741 | Meso_0746 | 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: mlo:mlr7496 cytochrome c oxidase subunit III. | 0.998 |
| Meso_0741 | Meso_2165 | Meso_0741 | Meso_2165 | 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 b/b6-like protein; Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex), which is a respiratory chain that generates an electrochemical potential coupled to ATP synthesis. | 0.985 |
| Meso_0741 | Meso_2477 | Meso_0741 | Meso_2477 | 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: mlo:mlr1043 cytochrome c oxidase subunit III. | 0.960 |
| Meso_0741 | Meso_2792 | Meso_0741 | Meso_2792 | 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 II cytochrome c, class I; KEGG: sme:SMb21368 putative cytochrome c oxidase chain II protein. | 0.981 |
| Meso_0741 | Meso_3533 | Meso_0741 | Meso_3533 | 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 IV; KEGG: psp:PSPPH_1213 cytochrome o ubiquinol oxidase, subunit IV. | 0.930 |
| Meso_0741 | Meso_3534 | Meso_0741 | Meso_3534 | 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: sgl:SG0665 cytochrome o ubiquinol oxidase subunit III. | 0.931 |
| Meso_0741 | Meso_3535 | Meso_0741 | Meso_3535 | 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 I; KEGG: bbr:BB1284 ubiquinol oxidase polypeptide I; Belongs to the heme-copper respiratory oxidase family. | 0.970 |
| Meso_0741 | ctaB | Meso_0741 | Meso_0743 | 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). | Protoheme IX farnesyltransferase; Converts heme B (protoheme IX) to heme O by substitution of the vinyl group on carbon 2 of heme B porphyrin ring with a hydroxyethyl farnesyl side group. | 0.976 |
| Meso_0741 | nuoA | Meso_0741 | Meso_1022 | 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). | NADH dehydrogenase subunit A; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient; Belongs to the complex I subunit 3 family. | 0.915 |
| Meso_0746 | Meso_0741 | Meso_0746 | Meso_0741 | PFAM: cytochrome c oxidase, subunit III; KEGG: mlo:mlr7496 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). | 0.998 |
| Meso_0746 | Meso_2165 | Meso_0746 | Meso_2165 | PFAM: cytochrome c oxidase, subunit III; KEGG: mlo:mlr7496 cytochrome c oxidase subunit III. | Cytochrome b/b6-like protein; Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex), which is a respiratory chain that generates an electrochemical potential coupled to ATP synthesis. | 0.994 |
| Meso_0746 | Meso_2477 | Meso_0746 | Meso_2477 | PFAM: cytochrome c oxidase, subunit III; KEGG: mlo:mlr7496 cytochrome c oxidase subunit III. | PFAM: cytochrome c oxidase, subunit III; KEGG: mlo:mlr1043 cytochrome c oxidase subunit III. | 0.916 |
| Meso_0746 | Meso_2792 | Meso_0746 | Meso_2792 | PFAM: cytochrome c oxidase, subunit III; KEGG: mlo:mlr7496 cytochrome c oxidase subunit III. | PFAM: cytochrome c oxidase, subunit II cytochrome c, class I; KEGG: sme:SMb21368 putative cytochrome c oxidase chain II protein. | 0.996 |
| Meso_0746 | Meso_3533 | Meso_0746 | Meso_3533 | PFAM: cytochrome c oxidase, subunit III; KEGG: mlo:mlr7496 cytochrome c oxidase subunit III. | PFAM: cytochrome C oxidase subunit IV; KEGG: psp:PSPPH_1213 cytochrome o ubiquinol oxidase, subunit IV. | 0.976 |
| Meso_0746 | Meso_3535 | Meso_0746 | Meso_3535 | PFAM: cytochrome c oxidase, subunit III; KEGG: mlo:mlr7496 cytochrome c oxidase subunit III. | PFAM: cytochrome c oxidase, subunit I; KEGG: bbr:BB1284 ubiquinol oxidase polypeptide I; Belongs to the heme-copper respiratory oxidase family. | 0.980 |
| Meso_0746 | Meso_3536 | Meso_0746 | Meso_3536 | PFAM: cytochrome c oxidase, subunit III; KEGG: mlo:mlr7496 cytochrome c oxidase subunit III. | TIGRFAM: ubiquinol oxidase, subunit II; PFAM: cytochrome c oxidase, subunit II COX aromatic rich; KEGG: pfl:PFL_4735 cytochrome o ubiquinol oxidase, subunit II. | 0.952 |
| Meso_0746 | ctaB | Meso_0746 | Meso_0743 | PFAM: cytochrome c oxidase, subunit III; KEGG: mlo:mlr7496 cytochrome c oxidase subunit III. | Protoheme IX farnesyltransferase; Converts heme B (protoheme IX) to heme O by substitution of the vinyl group on carbon 2 of heme B porphyrin ring with a hydroxyethyl farnesyl side group. | 0.990 |
| Meso_0746 | nuoA | Meso_0746 | Meso_1022 | PFAM: cytochrome c oxidase, subunit III; KEGG: mlo:mlr7496 cytochrome c oxidase subunit III. | NADH dehydrogenase subunit A; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient; Belongs to the complex I subunit 3 family. | 0.921 |
| Meso_2165 | Meso_0741 | Meso_2165 | Meso_0741 | Cytochrome b/b6-like protein; Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex), which is a respiratory chain that generates an electrochemical potential coupled to ATP synthesis. | 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). | 0.985 |
| Meso_2165 | Meso_0746 | Meso_2165 | Meso_0746 | Cytochrome b/b6-like protein; Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex), which is a respiratory chain that generates an electrochemical potential coupled to ATP synthesis. | PFAM: cytochrome c oxidase, subunit III; KEGG: mlo:mlr7496 cytochrome c oxidase subunit III. | 0.994 |