node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
APT57309.1 | APT58062.1 | RGI145_09535 | RGI145_14005 | ATPase; Derived by automated computational analysis using gene prediction method: Protein Homology. | ATPase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.543 |
APT57309.1 | APT58907.1 | RGI145_09535 | RGI145_19135 | ATPase; Derived by automated computational analysis using gene prediction method: Protein Homology. | Transcriptional regulator; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.419 |
APT58062.1 | APT57309.1 | RGI145_14005 | RGI145_09535 | ATPase; Derived by automated computational analysis using gene prediction method: Protein Homology. | ATPase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.543 |
APT58062.1 | APT58907.1 | RGI145_14005 | RGI145_19135 | ATPase; Derived by automated computational analysis using gene prediction method: Protein Homology. | Transcriptional regulator; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.506 |
APT58062.1 | APT59506.1 | RGI145_14005 | RGI145_19130 | ATPase; Derived by automated computational analysis using gene prediction method: Protein Homology. | Thioredoxin; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the thioredoxin family. | 0.435 |
APT58906.1 | APT58907.1 | RGI145_19125 | RGI145_19135 | Hypothetical protein; Derived by automated computational analysis using gene prediction method: GeneMarkS+. | Transcriptional regulator; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.447 |
APT58906.1 | APT59506.1 | RGI145_19125 | RGI145_19130 | Hypothetical protein; Derived by automated computational analysis using gene prediction method: GeneMarkS+. | Thioredoxin; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the thioredoxin family. | 0.693 |
APT58907.1 | APT57309.1 | RGI145_19135 | RGI145_09535 | Transcriptional regulator; Derived by automated computational analysis using gene prediction method: Protein Homology. | ATPase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.419 |
APT58907.1 | APT58062.1 | RGI145_19135 | RGI145_14005 | Transcriptional regulator; Derived by automated computational analysis using gene prediction method: Protein Homology. | ATPase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.506 |
APT58907.1 | APT58906.1 | RGI145_19135 | RGI145_19125 | Transcriptional regulator; Derived by automated computational analysis using gene prediction method: Protein Homology. | Hypothetical protein; Derived by automated computational analysis using gene prediction method: GeneMarkS+. | 0.447 |
APT58907.1 | APT58908.1 | RGI145_19135 | RGI145_19140 | Transcriptional regulator; Derived by automated computational analysis using gene prediction method: Protein Homology. | 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). | 0.461 |
APT58907.1 | APT58909.1 | RGI145_19135 | RGI145_19145 | Transcriptional regulator; Derived by automated computational analysis using gene prediction method: Protein Homology. | 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. | 0.455 |
APT58907.1 | APT59506.1 | RGI145_19135 | RGI145_19130 | Transcriptional regulator; Derived by automated computational analysis using gene prediction method: Protein Homology. | Thioredoxin; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the thioredoxin family. | 0.540 |
APT58907.1 | ctaB | RGI145_19135 | RGI145_19150 | Transcriptional regulator; Derived by automated computational analysis using gene prediction method: Protein Homology. | 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. | 0.428 |
APT58908.1 | APT58907.1 | RGI145_19140 | RGI145_19135 | 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). | Transcriptional regulator; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.461 |
APT58908.1 | APT58909.1 | RGI145_19140 | RGI145_19145 | 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 |
APT58908.1 | ctaB | RGI145_19140 | RGI145_19150 | 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. | 0.993 |
APT58909.1 | APT58907.1 | RGI145_19145 | RGI145_19135 | 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. | Transcriptional regulator; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.455 |
APT58909.1 | APT58908.1 | RGI145_19145 | RGI145_19140 | 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 |
APT58909.1 | ctaB | RGI145_19145 | RGI145_19150 | 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. | 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 |