| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| Meso_0741 | Meso_1992 | Meso_0741 | Meso_1992 | 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: electron transport protein SCO1/SenC; KEGG: mlo:mlr1532 inner mitochondrial membrane protein Sco1p. | 0.818 |
| Meso_0741 | Meso_2474 | 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_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_3037 | Meso_0741 | Meso_3037 | 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: Redoxin; KEGG: mlo:mll3505 thioredoxin-like protein. | 0.789 |
| Meso_1403 | Meso_1404 | Meso_1403 | Meso_1404 | Peptidyl-prolyl cis-trans isomerase, cyclophilin type; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides; Belongs to the cyclophilin-type PPIase family. | Peptidyl-prolyl cis-trans isomerase, cyclophilin type; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides; Belongs to the cyclophilin-type PPIase family. | 0.793 |
| Meso_1403 | Meso_3037 | Meso_1403 | Meso_3037 | Peptidyl-prolyl cis-trans isomerase, cyclophilin type; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides; Belongs to the cyclophilin-type PPIase family. | PFAM: Redoxin; KEGG: mlo:mll3505 thioredoxin-like protein. | 0.821 |
| Meso_1403 | dnaK | Meso_1403 | Meso_0679 | Peptidyl-prolyl cis-trans isomerase, cyclophilin type; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides; Belongs to the cyclophilin-type PPIase family. | Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.917 |
| Meso_1404 | Meso_1403 | Meso_1404 | Meso_1403 | Peptidyl-prolyl cis-trans isomerase, cyclophilin type; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides; Belongs to the cyclophilin-type PPIase family. | Peptidyl-prolyl cis-trans isomerase, cyclophilin type; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides; Belongs to the cyclophilin-type PPIase family. | 0.793 |
| Meso_1404 | Meso_3037 | Meso_1404 | Meso_3037 | Peptidyl-prolyl cis-trans isomerase, cyclophilin type; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides; Belongs to the cyclophilin-type PPIase family. | PFAM: Redoxin; KEGG: mlo:mll3505 thioredoxin-like protein. | 0.820 |
| Meso_1404 | dnaK | Meso_1404 | Meso_0679 | Peptidyl-prolyl cis-trans isomerase, cyclophilin type; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides; Belongs to the cyclophilin-type PPIase family. | Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.915 |
| Meso_1992 | Meso_0741 | Meso_1992 | Meso_0741 | PFAM: electron transport protein SCO1/SenC; KEGG: mlo:mlr1532 inner mitochondrial membrane protein Sco1p. | 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). | 0.818 |
| Meso_1992 | Meso_2474 | Meso_1992 | Meso_2474 | PFAM: electron transport protein SCO1/SenC; KEGG: mlo:mlr1532 inner mitochondrial membrane protein Sco1p. | PFAM: cytochrome c oxidase, subunit II; KEGG: mlo:mlr1039 cytochrome c oxidase subunit II. | 0.784 |
| Meso_1992 | Meso_2792 | Meso_1992 | Meso_2792 | PFAM: electron transport protein SCO1/SenC; KEGG: mlo:mlr1532 inner mitochondrial membrane protein Sco1p. | PFAM: cytochrome c oxidase, subunit II cytochrome c, class I; KEGG: sme:SMb21368 putative cytochrome c oxidase chain II protein. | 0.874 |
| Meso_1992 | Meso_3037 | Meso_1992 | Meso_3037 | PFAM: electron transport protein SCO1/SenC; KEGG: mlo:mlr1532 inner mitochondrial membrane protein Sco1p. | PFAM: Redoxin; KEGG: mlo:mll3505 thioredoxin-like protein. | 0.916 |
| Meso_2474 | Meso_0741 | Meso_2474 | Meso_0741 | PFAM: cytochrome c oxidase, subunit II; KEGG: mlo:mlr1039 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). | 0.923 |
| Meso_2474 | Meso_1992 | Meso_2474 | Meso_1992 | PFAM: cytochrome c oxidase, subunit II; KEGG: mlo:mlr1039 cytochrome c oxidase subunit II. | PFAM: electron transport protein SCO1/SenC; KEGG: mlo:mlr1532 inner mitochondrial membrane protein Sco1p. | 0.784 |
| Meso_2474 | Meso_2792 | Meso_2474 | Meso_2792 | PFAM: cytochrome c oxidase, subunit II; KEGG: mlo:mlr1039 cytochrome c oxidase subunit II. | PFAM: cytochrome c oxidase, subunit II cytochrome c, class I; KEGG: sme:SMb21368 putative cytochrome c oxidase chain II protein. | 0.980 |
| Meso_2474 | Meso_3037 | Meso_2474 | Meso_3037 | PFAM: cytochrome c oxidase, subunit II; KEGG: mlo:mlr1039 cytochrome c oxidase subunit II. | PFAM: Redoxin; KEGG: mlo:mll3505 thioredoxin-like protein. | 0.789 |
| Meso_2792 | Meso_0741 | Meso_2792 | Meso_0741 | PFAM: cytochrome c oxidase, subunit II cytochrome c, class I; KEGG: sme:SMb21368 putative cytochrome c oxidase chain II 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). | 0.981 |
| Meso_2792 | Meso_1992 | Meso_2792 | Meso_1992 | PFAM: cytochrome c oxidase, subunit II cytochrome c, class I; KEGG: sme:SMb21368 putative cytochrome c oxidase chain II protein. | PFAM: electron transport protein SCO1/SenC; KEGG: mlo:mlr1532 inner mitochondrial membrane protein Sco1p. | 0.874 |
