| node1 | node2 | node1 annotation | node2 annotation | score |
| Meso_0741 | Meso_0742 | 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, subunit I; Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Subunits 1-3 form the functional core of the enzyme complex. CO I is the catalytic subunit of the enzyme. Electrons originating in cytochrome c are transferred via the copper A center of subunit 2 and heme A of subunit 1 to the bimetallic center formed by heme A3 and copper B. | 0.999 |
| 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_2474 | 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; KEGG: mlo:mlr1039 cytochrome c oxidase subunit II. | 0.923 |
| Meso_0741 | Meso_2475 | 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: sme:SMc01983 cytochrome c oxidase subunit I; Belongs to the heme-copper respiratory oxidase family. | 0.977 |
| Meso_0741 | Meso_2476 | 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:mlr1042 cytochrome c oxidase subunit III. | 0.846 |
| 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_2791 | 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: sme:SMb21370 putative cytochrome c oxidase chain I protein; Belongs to the heme-copper respiratory oxidase family. | 0.977 |
| 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 | 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_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_0742 | Meso_0741 | Cytochrome c oxidase, subunit I; Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Subunits 1-3 form the functional core of the enzyme complex. CO I is the catalytic subunit of the enzyme. Electrons originating in cytochrome c are transferred via the copper A center of subunit 2 and heme A of subunit 1 to the bimetallic center formed by heme A3 and copper B. | 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 |
| Meso_0742 | Meso_2165 | Cytochrome c oxidase, subunit I; Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Subunits 1-3 form the functional core of the enzyme complex. CO I is the catalytic subunit of the enzyme. Electrons originating in cytochrome c are transferred via the copper A center of subunit 2 and heme A of subunit 1 to the bimetallic center formed by heme A3 and copper 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. | 0.993 |
| Meso_0742 | Meso_2474 | Cytochrome c oxidase, subunit I; Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Subunits 1-3 form the functional core of the enzyme complex. CO I is the catalytic subunit of the enzyme. Electrons originating in cytochrome c are transferred via the copper A center of subunit 2 and heme A of subunit 1 to the bimetallic center formed by heme A3 and copper B. | PFAM: cytochrome c oxidase, subunit II; KEGG: mlo:mlr1039 cytochrome c oxidase subunit II. | 0.969 |
| Meso_0742 | Meso_2475 | Cytochrome c oxidase, subunit I; Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Subunits 1-3 form the functional core of the enzyme complex. CO I is the catalytic subunit of the enzyme. Electrons originating in cytochrome c are transferred via the copper A center of subunit 2 and heme A of subunit 1 to the bimetallic center formed by heme A3 and copper B. | PFAM: cytochrome c oxidase, subunit I; KEGG: sme:SMc01983 cytochrome c oxidase subunit I; Belongs to the heme-copper respiratory oxidase family. | 0.909 |
| Meso_0742 | Meso_2476 | Cytochrome c oxidase, subunit I; Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Subunits 1-3 form the functional core of the enzyme complex. CO I is the catalytic subunit of the enzyme. Electrons originating in cytochrome c are transferred via the copper A center of subunit 2 and heme A of subunit 1 to the bimetallic center formed by heme A3 and copper B. | PFAM: cytochrome c oxidase, subunit III; KEGG: mlo:mlr1042 cytochrome c oxidase subunit III. | 0.876 |
| Meso_0742 | Meso_2477 | Cytochrome c oxidase, subunit I; Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Subunits 1-3 form the functional core of the enzyme complex. CO I is the catalytic subunit of the enzyme. Electrons originating in cytochrome c are transferred via the copper A center of subunit 2 and heme A of subunit 1 to the bimetallic center formed by heme A3 and copper B. | PFAM: cytochrome c oxidase, subunit III; KEGG: mlo:mlr1043 cytochrome c oxidase subunit III. | 0.993 |
| Meso_0742 | Meso_2791 | Cytochrome c oxidase, subunit I; Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Subunits 1-3 form the functional core of the enzyme complex. CO I is the catalytic subunit of the enzyme. Electrons originating in cytochrome c are transferred via the copper A center of subunit 2 and heme A of subunit 1 to the bimetallic center formed by heme A3 and copper B. | PFAM: cytochrome c oxidase, subunit I; KEGG: sme:SMb21370 putative cytochrome c oxidase chain I protein; Belongs to the heme-copper respiratory oxidase family. | 0.912 |
| Meso_0742 | Meso_2792 | Cytochrome c oxidase, subunit I; Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Subunits 1-3 form the functional core of the enzyme complex. CO I is the catalytic subunit of the enzyme. Electrons originating in cytochrome c are transferred via the copper A center of subunit 2 and heme A of subunit 1 to the bimetallic center formed by heme A3 and copper B. | PFAM: cytochrome c oxidase, subunit II cytochrome c, class I; KEGG: sme:SMb21368 putative cytochrome c oxidase chain II protein. | 0.997 |
| Meso_0742 | Meso_3533 | Cytochrome c oxidase, subunit I; Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Subunits 1-3 form the functional core of the enzyme complex. CO I is the catalytic subunit of the enzyme. Electrons originating in cytochrome c are transferred via the copper A center of subunit 2 and heme A of subunit 1 to the bimetallic center formed by heme A3 and copper B. | PFAM: cytochrome C oxidase subunit IV; KEGG: psp:PSPPH_1213 cytochrome o ubiquinol oxidase, subunit IV. | 0.970 |
| 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 |
