| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| ADD66829.1 | ADD67781.1 | Dacet_0022 | Dacet_1005 | KEGG: gur:Gura_4232 proton-translocating NADH- quinone oxidoreductase, chain M; TIGRFAM: proton-translocating NADH-quinone oxidoreductase, chain M; PFAM: NADH/Ubiquinone/plastoquinone (complex I). | 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 |
| ADD66829.1 | ADD67783.1 | Dacet_0022 | Dacet_1007 | KEGG: gur:Gura_4232 proton-translocating NADH- quinone oxidoreductase, chain M; TIGRFAM: proton-translocating NADH-quinone oxidoreductase, chain M; PFAM: NADH/Ubiquinone/plastoquinone (complex I). | PFAM: cytochrome c oxidase subunit III; KEGG: dde:Dde_1824 cytochrome c oxidase, subunit III. | 0.983 |
| ADD66829.1 | ADD67784.1 | Dacet_0022 | Dacet_1008 | KEGG: gur:Gura_4232 proton-translocating NADH- quinone oxidoreductase, chain M; TIGRFAM: proton-translocating NADH-quinone oxidoreductase, chain M; PFAM: NADH/Ubiquinone/plastoquinone (complex I). | 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. | 0.984 |
| ADD66829.1 | ADD68308.1 | Dacet_0022 | Dacet_1539 | KEGG: gur:Gura_4232 proton-translocating NADH- quinone oxidoreductase, chain M; TIGRFAM: proton-translocating NADH-quinone oxidoreductase, chain M; PFAM: NADH/Ubiquinone/plastoquinone (complex I). | KEGG: gbm:Gbem_1236 cytochrome c oxidase, cbb3- type, subunit II; TIGRFAM: cytochrome c oxidase, cbb3-type, subunit II; PFAM: cytochrome C oxidase mono-heme subunit/FixO; cytochrome c class I. | 0.954 |
| ADD66829.1 | ADD68560.1 | Dacet_0022 | Dacet_1796 | KEGG: gur:Gura_4232 proton-translocating NADH- quinone oxidoreductase, chain M; TIGRFAM: proton-translocating NADH-quinone oxidoreductase, chain M; PFAM: NADH/Ubiquinone/plastoquinone (complex I). | PFAM: Rieske [2Fe-2S] iron-sulphur domain; KEGG: geo:Geob_1345 Rieske (2Fe-2S) domain protein. | 0.913 |
| ADD66829.1 | ADD68561.1 | Dacet_0022 | Dacet_1797 | KEGG: gur:Gura_4232 proton-translocating NADH- quinone oxidoreductase, chain M; TIGRFAM: proton-translocating NADH-quinone oxidoreductase, chain M; PFAM: NADH/Ubiquinone/plastoquinone (complex I). | PFAM: Cytochrome b/b6 domain; KEGG: glo:Glov_1196 cytochrome b/b6 domain. | 0.983 |
| ADD66829.1 | ADD68562.1 | Dacet_0022 | Dacet_1798 | KEGG: gur:Gura_4232 proton-translocating NADH- quinone oxidoreductase, chain M; TIGRFAM: proton-translocating NADH-quinone oxidoreductase, chain M; PFAM: NADH/Ubiquinone/plastoquinone (complex I). | KEGG: gur:Gura_0460 hypothetical protein. | 0.710 |
| ADD66829.1 | nuoA | Dacet_0022 | Dacet_0010 | KEGG: gur:Gura_4232 proton-translocating NADH- quinone oxidoreductase, chain M; TIGRFAM: proton-translocating NADH-quinone oxidoreductase, chain M; PFAM: NADH/Ubiquinone/plastoquinone (complex I). | NADH-ubiquinone/plastoquinone oxidoreductase chain 3; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient; Belongs to the complex I subunit 3 family. | 0.999 |
| ADD66829.1 | nuoH | Dacet_0022 | Dacet_0017 | KEGG: gur:Gura_4232 proton-translocating NADH- quinone oxidoreductase, chain M; TIGRFAM: proton-translocating NADH-quinone oxidoreductase, chain M; PFAM: NADH/Ubiquinone/plastoquinone (complex I). | NADH dehydrogenase (quinone); NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient. This subunit may bind ubiquinone. | 0.999 |
| ADD66829.1 | nuoN | Dacet_0022 | Dacet_0023 | KEGG: gur:Gura_4232 proton-translocating NADH- quinone oxidoreductase, chain M; TIGRFAM: proton-translocating NADH-quinone oxidoreductase, chain M; PFAM: NADH/Ubiquinone/plastoquinone (complex I). | Proton-translocating NADH-quinone oxidoreductase, chain N; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient; Belongs to the complex I subunit 2 family. | 0.999 |
| ADD67781.1 | ADD66829.1 | Dacet_1005 | Dacet_0022 | 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: gur:Gura_4232 proton-translocating NADH- quinone oxidoreductase, chain M; TIGRFAM: proton-translocating NADH-quinone oxidoreductase, chain M; PFAM: NADH/Ubiquinone/plastoquinone (complex I). | 0.981 |
| ADD67781.1 | ADD67783.1 | Dacet_1005 | Dacet_1007 | 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 III; KEGG: dde:Dde_1824 cytochrome c oxidase, subunit III. | 0.999 |
| ADD67781.1 | ADD67784.1 | Dacet_1005 | Dacet_1008 | 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 |
| ADD67781.1 | ADD68308.1 | Dacet_1005 | Dacet_1539 | 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: gbm:Gbem_1236 cytochrome c oxidase, cbb3- type, subunit II; TIGRFAM: cytochrome c oxidase, cbb3-type, subunit II; PFAM: cytochrome C oxidase mono-heme subunit/FixO; cytochrome c class I. | 0.998 |
| ADD67781.1 | ADD68560.1 | Dacet_1005 | Dacet_1796 | 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: Rieske [2Fe-2S] iron-sulphur domain; KEGG: geo:Geob_1345 Rieske (2Fe-2S) domain protein. | 0.980 |
| ADD67781.1 | ADD68561.1 | Dacet_1005 | Dacet_1797 | 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 b/b6 domain; KEGG: glo:Glov_1196 cytochrome b/b6 domain. | 0.994 |
| ADD67781.1 | ADD68562.1 | Dacet_1005 | Dacet_1798 | 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: gur:Gura_0460 hypothetical protein. | 0.939 |
| ADD67781.1 | nuoA | Dacet_1005 | Dacet_0010 | 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). | NADH-ubiquinone/plastoquinone oxidoreductase chain 3; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient; Belongs to the complex I subunit 3 family. | 0.982 |
| ADD67781.1 | nuoH | Dacet_1005 | Dacet_0017 | 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). | NADH dehydrogenase (quinone); NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient. This subunit may bind ubiquinone. | 0.987 |
| ADD67781.1 | nuoN | Dacet_1005 | Dacet_0023 | 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). | Proton-translocating NADH-quinone oxidoreductase, chain N; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient; Belongs to the complex I subunit 2 family. | 0.967 |
