node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
KMK67064.1 | KMK67065.1 | IMCC21224_111927 | IMCC21224_111928 | NADH dehydrogenase subunit E; PFAM: Thioredoxin-like [2Fe-2S] ferredoxin; Helix-hairpin-helix domain; TIGRFAM: NADH-quinone oxidoreductase, E subunit. | Hypothetical protein; PFAM: Helix-hairpin-helix domain. | 0.951 |
KMK67064.1 | KMK67066.1 | IMCC21224_111927 | IMCC21224_111929 | NADH dehydrogenase subunit E; PFAM: Thioredoxin-like [2Fe-2S] ferredoxin; Helix-hairpin-helix domain; TIGRFAM: NADH-quinone oxidoreductase, E subunit. | Hypothetical protein. | 0.762 |
KMK67064.1 | KMK67067.1 | IMCC21224_111927 | IMCC21224_111930 | NADH dehydrogenase subunit E; PFAM: Thioredoxin-like [2Fe-2S] ferredoxin; Helix-hairpin-helix domain; TIGRFAM: NADH-quinone oxidoreductase, E subunit. | NADH dehydrogenase subunit F; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. Belongs to the complex I 51 kDa subunit family. | 0.999 |
KMK67064.1 | KMK67068.1 | IMCC21224_111927 | IMCC21224_111931 | NADH dehydrogenase subunit E; PFAM: Thioredoxin-like [2Fe-2S] ferredoxin; Helix-hairpin-helix domain; TIGRFAM: NADH-quinone oxidoreductase, E subunit. | Hypothetical protein; PFAM: MAPEG family. | 0.617 |
KMK67064.1 | KMK67069.1 | IMCC21224_111927 | IMCC21224_111932 | NADH dehydrogenase subunit E; PFAM: Thioredoxin-like [2Fe-2S] ferredoxin; Helix-hairpin-helix domain; TIGRFAM: NADH-quinone oxidoreductase, E subunit. | PFAM: Domain of unknown function (DUF3291). | 0.681 |
KMK67064.1 | KMK67070.1 | IMCC21224_111927 | IMCC21224_111933 | NADH dehydrogenase subunit E; PFAM: Thioredoxin-like [2Fe-2S] ferredoxin; Helix-hairpin-helix domain; TIGRFAM: NADH-quinone oxidoreductase, E subunit. | Hypothetical protein. | 0.719 |
KMK67064.1 | nuoB | IMCC21224_111927 | IMCC21224_111922 | NADH dehydrogenase subunit E; PFAM: Thioredoxin-like [2Fe-2S] ferredoxin; Helix-hairpin-helix domain; TIGRFAM: NADH-quinone oxidoreductase, E subunit. | NADH dehydrogenase subunit B; 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. | 0.999 |
KMK67064.1 | nuoC | IMCC21224_111927 | IMCC21224_111923 | NADH dehydrogenase subunit E; PFAM: Thioredoxin-like [2Fe-2S] ferredoxin; Helix-hairpin-helix domain; TIGRFAM: NADH-quinone oxidoreductase, E subunit. | NADH dehydrogenase subunit C; 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 30 kDa subunit family. | 0.999 |
KMK67064.1 | nuoD | IMCC21224_111927 | IMCC21224_111925 | NADH dehydrogenase subunit E; PFAM: Thioredoxin-like [2Fe-2S] ferredoxin; Helix-hairpin-helix domain; TIGRFAM: NADH-quinone oxidoreductase, E subunit. | NADH dehydrogenase subunit D; 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 49 kDa subunit family. | 0.999 |
KMK67064.1 | nuoI | IMCC21224_111927 | IMCC21224_111939 | NADH dehydrogenase subunit E; PFAM: Thioredoxin-like [2Fe-2S] ferredoxin; Helix-hairpin-helix domain; TIGRFAM: NADH-quinone oxidoreductase, E subunit. | NADH dehydrogenase subunit I; 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. | 0.999 |
KMK67065.1 | KMK67064.1 | IMCC21224_111928 | IMCC21224_111927 | Hypothetical protein; PFAM: Helix-hairpin-helix domain. | NADH dehydrogenase subunit E; PFAM: Thioredoxin-like [2Fe-2S] ferredoxin; Helix-hairpin-helix domain; TIGRFAM: NADH-quinone oxidoreductase, E subunit. | 0.951 |
KMK67065.1 | KMK67066.1 | IMCC21224_111928 | IMCC21224_111929 | Hypothetical protein; PFAM: Helix-hairpin-helix domain. | Hypothetical protein. | 0.810 |
KMK67065.1 | KMK67067.1 | IMCC21224_111928 | IMCC21224_111930 | Hypothetical protein; PFAM: Helix-hairpin-helix domain. | NADH dehydrogenase subunit F; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. Belongs to the complex I 51 kDa subunit family. | 0.823 |
KMK67065.1 | KMK67068.1 | IMCC21224_111928 | IMCC21224_111931 | Hypothetical protein; PFAM: Helix-hairpin-helix domain. | Hypothetical protein; PFAM: MAPEG family. | 0.701 |
KMK67065.1 | KMK67069.1 | IMCC21224_111928 | IMCC21224_111932 | Hypothetical protein; PFAM: Helix-hairpin-helix domain. | PFAM: Domain of unknown function (DUF3291). | 0.750 |
KMK67065.1 | KMK67070.1 | IMCC21224_111928 | IMCC21224_111933 | Hypothetical protein; PFAM: Helix-hairpin-helix domain. | Hypothetical protein. | 0.747 |
KMK67065.1 | nuoB | IMCC21224_111928 | IMCC21224_111922 | Hypothetical protein; PFAM: Helix-hairpin-helix domain. | NADH dehydrogenase subunit B; 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. | 0.908 |
KMK67065.1 | nuoC | IMCC21224_111928 | IMCC21224_111923 | Hypothetical protein; PFAM: Helix-hairpin-helix domain. | NADH dehydrogenase subunit C; 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 30 kDa subunit family. | 0.830 |
KMK67065.1 | nuoD | IMCC21224_111928 | IMCC21224_111925 | Hypothetical protein; PFAM: Helix-hairpin-helix domain. | NADH dehydrogenase subunit D; 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 49 kDa subunit family. | 0.799 |
KMK67065.1 | nuoI | IMCC21224_111928 | IMCC21224_111939 | Hypothetical protein; PFAM: Helix-hairpin-helix domain. | NADH dehydrogenase subunit I; 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. | 0.574 |