| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| AEB85335.1 | AEB85336.1 | Alide2_2988 | Alide2_2989 | PFAM: Deoxyribodipyrimidine photolyase-related protein; KEGG: ctt:CtCNB1_1993 deoxyribodipyrimidine photolyase-related protein. | beta-Ig-H3/fasciclin; KEGG: reu:Reut_C6236 beta-Ig-H3/fasciclin; PFAM: FAS1 domain; SMART: FAS1 domain. | 0.663 |
| AEB85335.1 | AEB85337.1 | Alide2_2988 | Alide2_2990 | PFAM: Deoxyribodipyrimidine photolyase-related protein; KEGG: ctt:CtCNB1_1993 deoxyribodipyrimidine photolyase-related protein. | PFAM: DNA photolyase, FAD-binding/Cryptochrome, C-terminal; DNA photolyase, N-terminal; KEGG: tmz:Tmz1t_3951 deoxyribodipyrimidine photo-lyase. | 0.854 |
| AEB85336.1 | AEB85335.1 | Alide2_2989 | Alide2_2988 | beta-Ig-H3/fasciclin; KEGG: reu:Reut_C6236 beta-Ig-H3/fasciclin; PFAM: FAS1 domain; SMART: FAS1 domain. | PFAM: Deoxyribodipyrimidine photolyase-related protein; KEGG: ctt:CtCNB1_1993 deoxyribodipyrimidine photolyase-related protein. | 0.663 |
| AEB85336.1 | AEB85337.1 | Alide2_2989 | Alide2_2990 | beta-Ig-H3/fasciclin; KEGG: reu:Reut_C6236 beta-Ig-H3/fasciclin; PFAM: FAS1 domain; SMART: FAS1 domain. | PFAM: DNA photolyase, FAD-binding/Cryptochrome, C-terminal; DNA photolyase, N-terminal; KEGG: tmz:Tmz1t_3951 deoxyribodipyrimidine photo-lyase. | 0.757 |
| AEB85336.1 | AEB86338.1 | Alide2_2989 | Alide2_4019 | beta-Ig-H3/fasciclin; KEGG: reu:Reut_C6236 beta-Ig-H3/fasciclin; PFAM: FAS1 domain; SMART: FAS1 domain. | NADH-ubiquinone/plastoquinone oxidoreductase chain 6; 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. | 0.650 |
| AEB85336.1 | nuoA | Alide2_2989 | Alide2_4010 | beta-Ig-H3/fasciclin; KEGG: reu:Reut_C6236 beta-Ig-H3/fasciclin; PFAM: FAS1 domain; SMART: FAS1 domain. | NAD(P)H-quinone oxidoreductase subunit 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. | 0.650 |
| AEB85336.1 | nuoB | Alide2_2989 | Alide2_4011 | beta-Ig-H3/fasciclin; KEGG: reu:Reut_C6236 beta-Ig-H3/fasciclin; PFAM: FAS1 domain; SMART: FAS1 domain. | NADH-quinone oxidoreductase, B subunit; 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. | 0.650 |
| AEB85336.1 | nuoC | Alide2_2989 | Alide2_4012 | beta-Ig-H3/fasciclin; KEGG: reu:Reut_C6236 beta-Ig-H3/fasciclin; PFAM: FAS1 domain; SMART: FAS1 domain. | NADH (or F420H2) 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. | 0.650 |
| AEB85336.1 | nuoD | Alide2_2989 | Alide2_4013 | beta-Ig-H3/fasciclin; KEGG: reu:Reut_C6236 beta-Ig-H3/fasciclin; PFAM: FAS1 domain; SMART: FAS1 domain. | NADH dehydrogenase I, D subunit; 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. | 0.792 |
| AEB85336.1 | nuoH | Alide2_2989 | Alide2_4017 | beta-Ig-H3/fasciclin; KEGG: reu:Reut_C6236 beta-Ig-H3/fasciclin; PFAM: FAS1 domain; SMART: FAS1 domain. | 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. | 0.654 |
| AEB85336.1 | nuoK | Alide2_2989 | Alide2_4020 | beta-Ig-H3/fasciclin; KEGG: reu:Reut_C6236 beta-Ig-H3/fasciclin; PFAM: FAS1 domain; SMART: FAS1 domain. | NADH-ubiquinone oxidoreductase chain 4L; 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. | 0.650 |
| AEB85336.1 | nuoN | Alide2_2989 | Alide2_4023 | beta-Ig-H3/fasciclin; KEGG: reu:Reut_C6236 beta-Ig-H3/fasciclin; PFAM: FAS1 domain; SMART: FAS1 domain. | 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. | 0.665 |
| AEB85337.1 | AEB85335.1 | Alide2_2990 | Alide2_2988 | PFAM: DNA photolyase, FAD-binding/Cryptochrome, C-terminal; DNA photolyase, N-terminal; KEGG: tmz:Tmz1t_3951 deoxyribodipyrimidine photo-lyase. | PFAM: Deoxyribodipyrimidine photolyase-related protein; KEGG: ctt:CtCNB1_1993 deoxyribodipyrimidine photolyase-related protein. | 0.854 |
| AEB85337.1 | AEB85336.1 | Alide2_2990 | Alide2_2989 | PFAM: DNA photolyase, FAD-binding/Cryptochrome, C-terminal; DNA photolyase, N-terminal; KEGG: tmz:Tmz1t_3951 deoxyribodipyrimidine photo-lyase. | beta-Ig-H3/fasciclin; KEGG: reu:Reut_C6236 beta-Ig-H3/fasciclin; PFAM: FAS1 domain; SMART: FAS1 domain. | 0.757 |
| AEB86338.1 | AEB85336.1 | Alide2_4019 | Alide2_2989 | NADH-ubiquinone/plastoquinone oxidoreductase chain 6; 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. | beta-Ig-H3/fasciclin; KEGG: reu:Reut_C6236 beta-Ig-H3/fasciclin; PFAM: FAS1 domain; SMART: FAS1 domain. | 0.650 |
| AEB86338.1 | nuoA | Alide2_4019 | Alide2_4010 | NADH-ubiquinone/plastoquinone oxidoreductase chain 6; 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. | NAD(P)H-quinone oxidoreductase subunit 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 |
| AEB86338.1 | nuoB | Alide2_4019 | Alide2_4011 | NADH-ubiquinone/plastoquinone oxidoreductase chain 6; 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. | NADH-quinone oxidoreductase, B subunit; 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 |
| AEB86338.1 | nuoC | Alide2_4019 | Alide2_4012 | NADH-ubiquinone/plastoquinone oxidoreductase chain 6; 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. | NADH (or F420H2) 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 |
| AEB86338.1 | nuoD | Alide2_4019 | Alide2_4013 | NADH-ubiquinone/plastoquinone oxidoreductase chain 6; 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. | NADH dehydrogenase I, D subunit; 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 |
| AEB86338.1 | nuoH | Alide2_4019 | Alide2_4017 | NADH-ubiquinone/plastoquinone oxidoreductase chain 6; 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. | 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 |