| node1 | node2 | node1 annotation | node2 annotation | score |
| Tter_1510 | Tter_1588 | KEGG: aba:Acid345_3204 hypothetical 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). | 0.996 |
| Tter_1510 | Tter_2153 | KEGG: aba:Acid345_3204 hypothetical protein. | KEGG: smd:Smed_6282 hypothetical protein. | 0.853 |
| Tter_1588 | Tter_1510 | 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). | KEGG: aba:Acid345_3204 hypothetical protein. | 0.996 |
| Tter_1588 | Tter_1592 | 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). | Quinol:cytochrome c oxidoreductase monoheme cytochrome subunit; KEGG: sus:Acid_0493 hypothetical protein. | 0.999 |
| Tter_1588 | Tter_1593 | 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). | KEGG: sus:Acid_0492 transmembrane prediction. | 0.999 |
| Tter_1588 | Tter_2153 | 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). | KEGG: smd:Smed_6282 hypothetical protein. | 0.733 |
| Tter_1592 | Tter_1588 | Quinol:cytochrome c oxidoreductase monoheme cytochrome subunit; KEGG: sus:Acid_0493 hypothetical 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). | 0.999 |
| Tter_1592 | Tter_1593 | Quinol:cytochrome c oxidoreductase monoheme cytochrome subunit; KEGG: sus:Acid_0493 hypothetical protein. | KEGG: sus:Acid_0492 transmembrane prediction. | 0.994 |
| Tter_1592 | Tter_2153 | Quinol:cytochrome c oxidoreductase monoheme cytochrome subunit; KEGG: sus:Acid_0493 hypothetical protein. | KEGG: smd:Smed_6282 hypothetical protein. | 0.853 |
| Tter_1593 | Tter_1588 | KEGG: sus:Acid_0492 transmembrane prediction. | 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 |
| Tter_1593 | Tter_1592 | KEGG: sus:Acid_0492 transmembrane prediction. | Quinol:cytochrome c oxidoreductase monoheme cytochrome subunit; KEGG: sus:Acid_0493 hypothetical protein. | 0.994 |
| Tter_1593 | Tter_2153 | KEGG: sus:Acid_0492 transmembrane prediction. | KEGG: smd:Smed_6282 hypothetical protein. | 0.853 |
| Tter_2149 | Tter_2150 | KEGG: oca:OCAR_7249 copper-containing nitrite reductase; TIGRFAM: nitrite reductase, copper-containing; PFAM: multicopper oxidase type 3; blue (type 1) copper domain protein; multicopper oxidase type 2. | 4Fe-4S ferredoxin iron-sulfur binding domain protein; Ferredoxins are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions. | 0.447 |
| Tter_2149 | Tter_2151 | KEGG: oca:OCAR_7249 copper-containing nitrite reductase; TIGRFAM: nitrite reductase, copper-containing; PFAM: multicopper oxidase type 3; blue (type 1) copper domain protein; multicopper oxidase type 2. | PFAM: protein of unknown function DUF59; KEGG: noc:Noc_1484 hypothetical protein. | 0.469 |
| Tter_2149 | Tter_2152 | KEGG: oca:OCAR_7249 copper-containing nitrite reductase; TIGRFAM: nitrite reductase, copper-containing; PFAM: multicopper oxidase type 3; blue (type 1) copper domain protein; multicopper oxidase type 2. | PFAM: Domain of unknown function DUF1858; KEGG: sme:SMa1256 hypothetical protein. | 0.655 |
| Tter_2149 | Tter_2153 | KEGG: oca:OCAR_7249 copper-containing nitrite reductase; TIGRFAM: nitrite reductase, copper-containing; PFAM: multicopper oxidase type 3; blue (type 1) copper domain protein; multicopper oxidase type 2. | KEGG: smd:Smed_6282 hypothetical protein. | 0.735 |
| Tter_2149 | Tter_2154 | KEGG: oca:OCAR_7249 copper-containing nitrite reductase; TIGRFAM: nitrite reductase, copper-containing; PFAM: multicopper oxidase type 3; blue (type 1) copper domain protein; multicopper oxidase type 2. | KEGG: mag:amb3531 hypothetical protein. | 0.786 |
| Tter_2149 | Tter_2155 | KEGG: oca:OCAR_7249 copper-containing nitrite reductase; TIGRFAM: nitrite reductase, copper-containing; PFAM: multicopper oxidase type 3; blue (type 1) copper domain protein; multicopper oxidase type 2. | KEGG: rpd:RPD_4272 copper resistance D. | 0.680 |
| Tter_2150 | Tter_2149 | 4Fe-4S ferredoxin iron-sulfur binding domain protein; Ferredoxins are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions. | KEGG: oca:OCAR_7249 copper-containing nitrite reductase; TIGRFAM: nitrite reductase, copper-containing; PFAM: multicopper oxidase type 3; blue (type 1) copper domain protein; multicopper oxidase type 2. | 0.447 |
| Tter_2150 | Tter_2151 | 4Fe-4S ferredoxin iron-sulfur binding domain protein; Ferredoxins are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions. | PFAM: protein of unknown function DUF59; KEGG: noc:Noc_1484 hypothetical protein. | 0.774 |