node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
AFY55239.1 | AFY55283.1 | Riv7116_2737 | Riv7116_2784 | Hypothetical protein. | PFAM: CO2 hydration protein (ChpXY); TIGRFAM: CO2 hydration protein. | 0.461 |
AFY55239.1 | AFY55782.1 | Riv7116_2737 | Riv7116_3319 | Hypothetical protein. | Secreted/surface protein with fasciclin-like repeats; PFAM: Fasciclin domain. | 0.520 |
AFY55239.1 | AFY57706.1 | Riv7116_2737 | Riv7116_5324 | Hypothetical protein. | PFAM: CO2 hydration protein (ChpXY); TIGRFAM: CO2 hydration protein. | 0.461 |
AFY55239.1 | ndhH | Riv7116_2737 | Riv7116_2365 | Hypothetical protein. | NADH dehydrogenase subunit D; NDH-1 shuttles electrons from an unknown electron donor, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory and/or the photosynthetic chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient. Cyanobacterial NDH-1 also plays a role in inorganic carbon-concentration. | 0.461 |
AFY55239.1 | ndhH-2 | Riv7116_2737 | Riv7116_5355 | Hypothetical protein. | NADH:ubiquinone oxidoreductase 49 kD subunit 7; NDH-1 shuttles electrons from an unknown electron donor, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory and/or the photosynthetic chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient. Cyanobacterial NDH-1 also plays a role in inorganic carbon-concentration. | 0.461 |
AFY55283.1 | AFY55239.1 | Riv7116_2784 | Riv7116_2737 | PFAM: CO2 hydration protein (ChpXY); TIGRFAM: CO2 hydration protein. | Hypothetical protein. | 0.461 |
AFY55283.1 | AFY55782.1 | Riv7116_2784 | Riv7116_3319 | PFAM: CO2 hydration protein (ChpXY); TIGRFAM: CO2 hydration protein. | Secreted/surface protein with fasciclin-like repeats; PFAM: Fasciclin domain. | 0.482 |
AFY55283.1 | ndhC | Riv7116_2784 | Riv7116_0949 | PFAM: CO2 hydration protein (ChpXY); TIGRFAM: CO2 hydration protein. | NADH:ubiquinone oxidoreductase subunit 3 (chain A); NDH-1 shuttles electrons from an unknown electron donor, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory and/or the photosynthetic chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient. Cyanobacterial NDH-1 also plays a role in inorganic carbon-concentration. | 0.497 |
AFY55283.1 | ndhH | Riv7116_2784 | Riv7116_2365 | PFAM: CO2 hydration protein (ChpXY); TIGRFAM: CO2 hydration protein. | NADH dehydrogenase subunit D; NDH-1 shuttles electrons from an unknown electron donor, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory and/or the photosynthetic chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient. Cyanobacterial NDH-1 also plays a role in inorganic carbon-concentration. | 0.749 |
AFY55283.1 | ndhH-2 | Riv7116_2784 | Riv7116_5355 | PFAM: CO2 hydration protein (ChpXY); TIGRFAM: CO2 hydration protein. | NADH:ubiquinone oxidoreductase 49 kD subunit 7; NDH-1 shuttles electrons from an unknown electron donor, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory and/or the photosynthetic chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient. Cyanobacterial NDH-1 also plays a role in inorganic carbon-concentration. | 0.749 |
AFY55283.1 | ndhJ | Riv7116_2784 | Riv7116_0947 | PFAM: CO2 hydration protein (ChpXY); TIGRFAM: CO2 hydration protein. | NADH/F420H2 dehydrogenase, subunit C; NDH-1 shuttles electrons from an unknown electron donor, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory and/or the photosynthetic chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient. Cyanobacterial NDH-1 also plays a role in inorganic carbon-concentration. | 0.504 |
AFY55283.1 | ndhK | Riv7116_2784 | Riv7116_0948 | PFAM: CO2 hydration protein (ChpXY); TIGRFAM: CO2 hydration protein. | NADH-quinone oxidoreductase, B subunit; NDH-1 shuttles electrons from an unknown electron donor, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory and/or the photosynthetic chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient. Cyanobacterial NDH-1 also plays a role in inorganic carbon-concentration; Belongs to the complex I 20 kDa subunit family. | 0.499 |
AFY55283.1 | ndhL | Riv7116_2784 | Riv7116_4663 | PFAM: CO2 hydration protein (ChpXY); TIGRFAM: CO2 hydration protein. | NADH dehydrogenase transmembrane subunit; NDH-1 shuttles electrons from an unknown electron donor, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory and/or the photosynthetic chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient. Cyanobacterial NDH-1 also plays a role in inorganic carbon-concentration. | 0.741 |
AFY55283.1 | ndhM | Riv7116_2784 | Riv7116_1098 | PFAM: CO2 hydration protein (ChpXY); TIGRFAM: CO2 hydration protein. | Cyanobacterial and plastid NDH-1 subunit M; NDH-1 shuttles electrons from an unknown electron donor, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory and/or the photosynthetic chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient. Cyanobacterial NDH-1 also plays a role in inorganic carbon-concentration. | 0.746 |
AFY55782.1 | AFY55239.1 | Riv7116_3319 | Riv7116_2737 | Secreted/surface protein with fasciclin-like repeats; PFAM: Fasciclin domain. | Hypothetical protein. | 0.520 |
AFY55782.1 | AFY55283.1 | Riv7116_3319 | Riv7116_2784 | Secreted/surface protein with fasciclin-like repeats; PFAM: Fasciclin domain. | PFAM: CO2 hydration protein (ChpXY); TIGRFAM: CO2 hydration protein. | 0.482 |
AFY55782.1 | AFY57706.1 | Riv7116_3319 | Riv7116_5324 | Secreted/surface protein with fasciclin-like repeats; PFAM: Fasciclin domain. | PFAM: CO2 hydration protein (ChpXY); TIGRFAM: CO2 hydration protein. | 0.817 |
AFY55782.1 | ndhC | Riv7116_3319 | Riv7116_0949 | Secreted/surface protein with fasciclin-like repeats; PFAM: Fasciclin domain. | NADH:ubiquinone oxidoreductase subunit 3 (chain A); NDH-1 shuttles electrons from an unknown electron donor, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory and/or the photosynthetic chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient. Cyanobacterial NDH-1 also plays a role in inorganic carbon-concentration. | 0.414 |
AFY55782.1 | ndhH | Riv7116_3319 | Riv7116_2365 | Secreted/surface protein with fasciclin-like repeats; PFAM: Fasciclin domain. | NADH dehydrogenase subunit D; NDH-1 shuttles electrons from an unknown electron donor, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory and/or the photosynthetic chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient. Cyanobacterial NDH-1 also plays a role in inorganic carbon-concentration. | 0.707 |
AFY55782.1 | ndhH-2 | Riv7116_3319 | Riv7116_5355 | Secreted/surface protein with fasciclin-like repeats; PFAM: Fasciclin domain. | NADH:ubiquinone oxidoreductase 49 kD subunit 7; NDH-1 shuttles electrons from an unknown electron donor, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory and/or the photosynthetic chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient. Cyanobacterial NDH-1 also plays a role in inorganic carbon-concentration. | 0.707 |