| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| LHA_1129 | LHA_2505 | LHA_1129 | LHA_2505 | Lycopene cyclase; Function of strongly homologous gene; enzyme. | Conserved protein of unknown function [Beta-Ig-H3/Fasciclin domain]; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology. | 0.467 |
| LHA_2498 | LHA_2502 | LHA_2498 | LHA_2502 | Homologs of previously reported genes of unknown function. | Homologs of previously reported genes of unknown function. | 0.622 |
| LHA_2498 | LHA_2505 | LHA_2498 | LHA_2505 | Homologs of previously reported genes of unknown function. | Conserved protein of unknown function [Beta-Ig-H3/Fasciclin domain]; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology. | 0.472 |
| LHA_2502 | LHA_2498 | LHA_2502 | LHA_2498 | Homologs of previously reported genes of unknown function. | Homologs of previously reported genes of unknown function. | 0.622 |
| LHA_2502 | LHA_2505 | LHA_2502 | LHA_2505 | Homologs of previously reported genes of unknown function. | Conserved protein of unknown function [Beta-Ig-H3/Fasciclin domain]; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology. | 0.530 |
| LHA_2505 | LHA_1129 | LHA_2505 | LHA_1129 | Conserved protein of unknown function [Beta-Ig-H3/Fasciclin domain]; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology. | Lycopene cyclase; Function of strongly homologous gene; enzyme. | 0.467 |
| LHA_2505 | LHA_2498 | LHA_2505 | LHA_2498 | Conserved protein of unknown function [Beta-Ig-H3/Fasciclin domain]; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology. | Homologs of previously reported genes of unknown function. | 0.472 |
| LHA_2505 | LHA_2502 | LHA_2505 | LHA_2502 | Conserved protein of unknown function [Beta-Ig-H3/Fasciclin domain]; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology. | Homologs of previously reported genes of unknown function. | 0.530 |
| LHA_2505 | LHA_2506 | LHA_2505 | LHA_2506 | Conserved protein of unknown function [Beta-Ig-H3/Fasciclin domain]; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology. | Protein of unknown function; No homology to any previously reported sequences. | 0.686 |
| LHA_2505 | nuoD | LHA_2505 | LHA_2991 | Conserved protein of unknown function [Beta-Ig-H3/Fasciclin domain]; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology. | NADH-quinone oxidoreductase 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. | 0.939 |
| LHA_2505 | nuoH | LHA_2505 | LHA_2987 | Conserved protein of unknown function [Beta-Ig-H3/Fasciclin domain]; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology. | NADH-quinone oxidoreductase subunit H; 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. | 0.467 |
| LHA_2505 | nuoI | LHA_2505 | LHA_2986 | Conserved protein of unknown function [Beta-Ig-H3/Fasciclin domain]; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology. | NADH-quinone oxidoreductase 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. | 0.511 |
| LHA_2505 | nuoJ | LHA_2505 | LHA_2985 | Conserved protein of unknown function [Beta-Ig-H3/Fasciclin domain]; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology. | NADH dehydrogenase I, J subunit; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. 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. | 0.467 |
| LHA_2505 | nuoK | LHA_2505 | LHA_2984 | Conserved protein of unknown function [Beta-Ig-H3/Fasciclin domain]; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology. | NADH-quinone oxidoreductase subunit K; 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 4L family. | 0.467 |
| LHA_2505 | nuoN | LHA_2505 | LHA_2981 | Conserved protein of unknown function [Beta-Ig-H3/Fasciclin domain]; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology. | NADH-quinone oxidoreductase subunit 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. | 0.473 |
| LHA_2506 | LHA_2505 | LHA_2506 | LHA_2505 | Protein of unknown function; No homology to any previously reported sequences. | Conserved protein of unknown function [Beta-Ig-H3/Fasciclin domain]; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology. | 0.686 |
| nuoD | LHA_2505 | LHA_2991 | LHA_2505 | NADH-quinone oxidoreductase 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. | Conserved protein of unknown function [Beta-Ig-H3/Fasciclin domain]; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology. | 0.939 |
| nuoD | nuoH | LHA_2991 | LHA_2987 | NADH-quinone oxidoreductase 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. | NADH-quinone oxidoreductase subunit H; 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 |
| nuoD | nuoI | LHA_2991 | LHA_2986 | NADH-quinone oxidoreductase 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. | NADH-quinone oxidoreductase 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 |
| nuoD | nuoJ | LHA_2991 | LHA_2985 | NADH-quinone oxidoreductase 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. | NADH dehydrogenase I, J subunit; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. 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 |