node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
OJV39536.1 | OJV39537.1 | BGO25_01660 | BGO25_01665 | Hypothetical protein; Derived by automated computational analysis using gene prediction method: GeneMarkS+. | Nitric-oxide reductase large subunit; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.779 |
OJV39537.1 | OJV39536.1 | BGO25_01665 | BGO25_01660 | Nitric-oxide reductase large subunit; Derived by automated computational analysis using gene prediction method: Protein Homology. | Hypothetical protein; Derived by automated computational analysis using gene prediction method: GeneMarkS+. | 0.779 |
OJV39537.1 | OJV39702.1 | BGO25_01665 | BGO25_00230 | Nitric-oxide reductase large subunit; Derived by automated computational analysis using gene prediction method: Protein Homology. | Pyrroloquinoline quinone-dependent dehydrogenase; Derived by automated computational analysis using gene prediction method: GeneMarkS+. | 0.593 |
OJV39537.1 | OJV39915.1 | BGO25_01665 | BGO25_08875 | Nitric-oxide reductase large subunit; 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). | 0.746 |
OJV39537.1 | OJV39920.1 | BGO25_01665 | BGO25_08905 | Nitric-oxide reductase large subunit; Derived by automated computational analysis using gene prediction method: Protein Homology. | Cytochrome B6; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.633 |
OJV39537.1 | OJV40267.1 | BGO25_01665 | BGO25_03740 | Nitric-oxide reductase large subunit; Derived by automated computational analysis using gene prediction method: Protein Homology. | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.593 |
OJV39537.1 | OJV40336.1 | BGO25_01665 | BGO25_04145 | Nitric-oxide reductase large subunit; Derived by automated computational analysis using gene prediction method: Protein Homology. | Copper oxidase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.645 |
OJV39537.1 | OJV41269.1 | BGO25_01665 | BGO25_16120 | Nitric-oxide reductase large subunit; Derived by automated computational analysis using gene prediction method: Protein Homology. | Phosphoesterase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.590 |
OJV39537.1 | OJV41357.1 | BGO25_01665 | BGO25_16670 | Nitric-oxide reductase large subunit; Derived by automated computational analysis using gene prediction method: Protein Homology. | Hypothetical protein; Derived by automated computational analysis using gene prediction method: GeneMarkS+. | 0.569 |
OJV39537.1 | OJV44262.1 | BGO25_01665 | BGO25_12935 | Nitric-oxide reductase large subunit; Derived by automated computational analysis using gene prediction method: Protein Homology. | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.593 |
OJV39537.1 | OJV44474.1 | BGO25_01665 | BGO25_05125 | Nitric-oxide reductase large subunit; 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). | 0.717 |
OJV39702.1 | OJV39537.1 | BGO25_00230 | BGO25_01665 | Pyrroloquinoline quinone-dependent dehydrogenase; Derived by automated computational analysis using gene prediction method: GeneMarkS+. | Nitric-oxide reductase large subunit; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.593 |
OJV39702.1 | OJV39915.1 | BGO25_00230 | BGO25_08875 | Pyrroloquinoline quinone-dependent dehydrogenase; Derived by automated computational analysis using gene prediction method: GeneMarkS+. | 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). | 0.967 |
OJV39702.1 | OJV39920.1 | BGO25_00230 | BGO25_08905 | Pyrroloquinoline quinone-dependent dehydrogenase; Derived by automated computational analysis using gene prediction method: GeneMarkS+. | Cytochrome B6; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.867 |
OJV39702.1 | OJV40267.1 | BGO25_00230 | BGO25_03740 | Pyrroloquinoline quinone-dependent dehydrogenase; Derived by automated computational analysis using gene prediction method: GeneMarkS+. | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.443 |
OJV39702.1 | OJV41269.1 | BGO25_00230 | BGO25_16120 | Pyrroloquinoline quinone-dependent dehydrogenase; Derived by automated computational analysis using gene prediction method: GeneMarkS+. | Phosphoesterase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.667 |
OJV39702.1 | OJV41357.1 | BGO25_00230 | BGO25_16670 | Pyrroloquinoline quinone-dependent dehydrogenase; Derived by automated computational analysis using gene prediction method: GeneMarkS+. | Hypothetical protein; Derived by automated computational analysis using gene prediction method: GeneMarkS+. | 0.667 |
OJV39702.1 | OJV44262.1 | BGO25_00230 | BGO25_12935 | Pyrroloquinoline quinone-dependent dehydrogenase; Derived by automated computational analysis using gene prediction method: GeneMarkS+. | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.433 |
OJV39702.1 | OJV44474.1 | BGO25_00230 | BGO25_05125 | Pyrroloquinoline quinone-dependent dehydrogenase; Derived by automated computational analysis using gene prediction method: GeneMarkS+. | 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). | 0.967 |
OJV39915.1 | OJV39537.1 | BGO25_08875 | BGO25_01665 | 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). | Nitric-oxide reductase large subunit; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.746 |