| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| JNB_01430 | JNB_01435 | JNB_01430 | JNB_01435 | COG1622 Heme/copper-type cytochrome/quinol oxidases, subunit 2. | 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 |
| JNB_01430 | JNB_01440 | JNB_01430 | JNB_01440 | COG1622 Heme/copper-type cytochrome/quinol oxidases, subunit 2. | Putative membrane protein; Part of cytochrome c oxidase, its function is unknown. Belongs to the cytochrome c oxidase bacterial subunit CtaF family. | 0.999 |
| JNB_01430 | JNB_01465 | JNB_01430 | JNB_01465 | COG1622 Heme/copper-type cytochrome/quinol oxidases, subunit 2. | COG1290 Cytochrome b subunit of the bc complex. | 0.999 |
| JNB_01430 | JNB_01470 | JNB_01430 | JNB_01470 | COG1622 Heme/copper-type cytochrome/quinol oxidases, subunit 2. | Rieske iron-sulphur component of ubiQ-cytB reductase; COG0723 Rieske Fe-S protein. | 0.999 |
| JNB_01430 | JNB_01475 | JNB_01430 | JNB_01475 | COG1622 Heme/copper-type cytochrome/quinol oxidases, subunit 2. | COG2010 Cytochrome c, mono- and diheme variants. | 0.999 |
| JNB_01430 | JNB_01480 | JNB_01430 | JNB_01480 | COG1622 Heme/copper-type cytochrome/quinol oxidases, subunit 2. | COG1845 Heme/copper-type cytochrome/quinol oxidase, subunit 3. | 0.999 |
| JNB_01430 | JNB_03535 | JNB_01430 | JNB_03535 | COG1622 Heme/copper-type cytochrome/quinol oxidases, subunit 2. | Putative iron sulphur protein; COG2146 Ferredoxin subunits of nitrite reductase and ring-hydroxylating dioxygenases. | 0.978 |
| JNB_01430 | JNB_08804 | JNB_01430 | JNB_08804 | COG1622 Heme/copper-type cytochrome/quinol oxidases, subunit 2. | COG1008 NADH:ubiquinone oxidoreductase subunit 4 (chain M). | 0.961 |
| JNB_01430 | JNB_08969 | JNB_01430 | JNB_08969 | COG1622 Heme/copper-type cytochrome/quinol oxidases, subunit 2. | COG1008 NADH:ubiquinone oxidoreductase subunit 4 (chain M). | 0.961 |
| JNB_01430 | ctaB | JNB_01430 | JNB_03440 | COG1622 Heme/copper-type cytochrome/quinol oxidases, subunit 2. | Putative cytochrome oxidase assembly factor; 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. | 0.998 |
| JNB_01435 | JNB_01430 | JNB_01435 | JNB_01430 | 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. | COG1622 Heme/copper-type cytochrome/quinol oxidases, subunit 2. | 0.999 |
| JNB_01435 | JNB_01440 | JNB_01435 | JNB_01440 | 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. | Putative membrane protein; Part of cytochrome c oxidase, its function is unknown. Belongs to the cytochrome c oxidase bacterial subunit CtaF family. | 0.999 |
| JNB_01435 | JNB_01465 | JNB_01435 | JNB_01465 | 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. | COG1290 Cytochrome b subunit of the bc complex. | 0.999 |
| JNB_01435 | JNB_01470 | JNB_01435 | JNB_01470 | 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. | Rieske iron-sulphur component of ubiQ-cytB reductase; COG0723 Rieske Fe-S protein. | 0.999 |
| JNB_01435 | JNB_01475 | JNB_01435 | JNB_01475 | 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. | COG2010 Cytochrome c, mono- and diheme variants. | 0.999 |
| JNB_01435 | JNB_01480 | JNB_01435 | JNB_01480 | 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. | COG1845 Heme/copper-type cytochrome/quinol oxidase, subunit 3. | 0.999 |
| JNB_01435 | JNB_03535 | JNB_01435 | JNB_03535 | 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. | Putative iron sulphur protein; COG2146 Ferredoxin subunits of nitrite reductase and ring-hydroxylating dioxygenases. | 0.983 |
| JNB_01435 | JNB_08804 | JNB_01435 | JNB_08804 | 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. | COG1008 NADH:ubiquinone oxidoreductase subunit 4 (chain M). | 0.977 |
| JNB_01435 | JNB_08969 | JNB_01435 | JNB_08969 | 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. | COG1008 NADH:ubiquinone oxidoreductase subunit 4 (chain M). | 0.978 |
| JNB_01435 | ctaB | JNB_01435 | JNB_03440 | 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. | Putative cytochrome oxidase assembly factor; 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. | 0.999 |