node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
AFZ06248.1 | AFZ06522.1 | Osc7112_1755 | Osc7112_2051 | KEGG: ava:Ava_4792 hypothetical protein; SPTR: Putative uncharacterized protein. | PFAM: CO2 hydration protein (ChpXY); TIGRFAM: CO2 hydration protein; InterPro IPR010220; KEGG: naz:Aazo_4081 CO2 hydration protein; PFAM: CO2 hydration; SPTR: CO2 hydration protein; TIGRFAM: CO2 hydration. | 0.459 |
AFZ06248.1 | AFZ06931.1 | Osc7112_1755 | Osc7112_2500 | KEGG: ava:Ava_4792 hypothetical protein; SPTR: Putative uncharacterized protein. | beta-Ig-H3/fasciclin; PFAM: Fasciclin domain; COGs: COG2335 Secreted and surface protein containing fasciclin-like repeats; InterPro IPR000782; KEGG: ava:Ava_2167 beta-Ig-H3/fasciclin; PFAM: FAS1 domain; SMART: FAS1 domain; SPTR: Beta-Ig-H3/fasciclin. | 0.429 |
AFZ06248.1 | AFZ09417.1 | Osc7112_1755 | Osc7112_5163 | KEGG: ava:Ava_4792 hypothetical protein; SPTR: Putative uncharacterized protein. | PFAM: CO2 hydration protein (ChpXY); TIGRFAM: CO2 hydration protein; InterPro IPR010220; KEGG: cyj:Cyan7822_2890 CO2 hydration protein; PFAM: CO2 hydration; SPTR: CO2 hydration protein; TIGRFAM: CO2 hydration. | 0.459 |
AFZ06248.1 | ndhH | Osc7112_1755 | Osc7112_3389 | KEGG: ava:Ava_4792 hypothetical protein; SPTR: Putative uncharacterized 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. | 0.701 |
AFZ06522.1 | AFZ06248.1 | Osc7112_2051 | Osc7112_1755 | PFAM: CO2 hydration protein (ChpXY); TIGRFAM: CO2 hydration protein; InterPro IPR010220; KEGG: naz:Aazo_4081 CO2 hydration protein; PFAM: CO2 hydration; SPTR: CO2 hydration protein; TIGRFAM: CO2 hydration. | KEGG: ava:Ava_4792 hypothetical protein; SPTR: Putative uncharacterized protein. | 0.459 |
AFZ06522.1 | AFZ06931.1 | Osc7112_2051 | Osc7112_2500 | PFAM: CO2 hydration protein (ChpXY); TIGRFAM: CO2 hydration protein; InterPro IPR010220; KEGG: naz:Aazo_4081 CO2 hydration protein; PFAM: CO2 hydration; SPTR: CO2 hydration protein; TIGRFAM: CO2 hydration. | beta-Ig-H3/fasciclin; PFAM: Fasciclin domain; COGs: COG2335 Secreted and surface protein containing fasciclin-like repeats; InterPro IPR000782; KEGG: ava:Ava_2167 beta-Ig-H3/fasciclin; PFAM: FAS1 domain; SMART: FAS1 domain; SPTR: Beta-Ig-H3/fasciclin. | 0.750 |
AFZ06522.1 | ndhH | Osc7112_2051 | Osc7112_3389 | PFAM: CO2 hydration protein (ChpXY); TIGRFAM: CO2 hydration protein; InterPro IPR010220; KEGG: naz:Aazo_4081 CO2 hydration protein; PFAM: CO2 hydration; SPTR: CO2 hydration protein; TIGRFAM: CO2 hydration. | 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. | 0.942 |
AFZ06931.1 | AFZ06248.1 | Osc7112_2500 | Osc7112_1755 | beta-Ig-H3/fasciclin; PFAM: Fasciclin domain; COGs: COG2335 Secreted and surface protein containing fasciclin-like repeats; InterPro IPR000782; KEGG: ava:Ava_2167 beta-Ig-H3/fasciclin; PFAM: FAS1 domain; SMART: FAS1 domain; SPTR: Beta-Ig-H3/fasciclin. | KEGG: ava:Ava_4792 hypothetical protein; SPTR: Putative uncharacterized protein. | 0.429 |
AFZ06931.1 | AFZ06522.1 | Osc7112_2500 | Osc7112_2051 | beta-Ig-H3/fasciclin; PFAM: Fasciclin domain; COGs: COG2335 Secreted and surface protein containing fasciclin-like repeats; InterPro IPR000782; KEGG: ava:Ava_2167 beta-Ig-H3/fasciclin; PFAM: FAS1 domain; SMART: FAS1 domain; SPTR: Beta-Ig-H3/fasciclin. | PFAM: CO2 hydration protein (ChpXY); TIGRFAM: CO2 hydration protein; InterPro IPR010220; KEGG: naz:Aazo_4081 CO2 hydration protein; PFAM: CO2 hydration; SPTR: CO2 hydration protein; TIGRFAM: CO2 hydration. | 0.750 |
AFZ06931.1 | AFZ06932.1 | Osc7112_2500 | Osc7112_2501 | beta-Ig-H3/fasciclin; PFAM: Fasciclin domain; COGs: COG2335 Secreted and surface protein containing fasciclin-like repeats; InterPro IPR000782; KEGG: ava:Ava_2167 beta-Ig-H3/fasciclin; PFAM: FAS1 domain; SMART: FAS1 domain; SPTR: Beta-Ig-H3/fasciclin. | Protein of unknown function DUF2358; PFAM: Uncharacterized conserved protein (DUF2358); InterPro IPR018790; KEGG: ter:Tery_4691 hypothetical protein; PFAM: Protein of unknown function DUF2358; SPTR: Putative uncharacterized protein. | 0.465 |
AFZ06931.1 | AFZ09417.1 | Osc7112_2500 | Osc7112_5163 | beta-Ig-H3/fasciclin; PFAM: Fasciclin domain; COGs: COG2335 Secreted and surface protein containing fasciclin-like repeats; InterPro IPR000782; KEGG: ava:Ava_2167 beta-Ig-H3/fasciclin; PFAM: FAS1 domain; SMART: FAS1 domain; SPTR: Beta-Ig-H3/fasciclin. | PFAM: CO2 hydration protein (ChpXY); TIGRFAM: CO2 hydration protein; InterPro IPR010220; KEGG: cyj:Cyan7822_2890 CO2 hydration protein; PFAM: CO2 hydration; SPTR: CO2 hydration protein; TIGRFAM: CO2 hydration. | 0.471 |
AFZ06931.1 | ndhH | Osc7112_2500 | Osc7112_3389 | beta-Ig-H3/fasciclin; PFAM: Fasciclin domain; COGs: COG2335 Secreted and surface protein containing fasciclin-like repeats; InterPro IPR000782; KEGG: ava:Ava_2167 beta-Ig-H3/fasciclin; PFAM: FAS1 domain; SMART: FAS1 domain; SPTR: Beta-Ig-H3/fasciclin. | 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. | 0.745 |
AFZ06932.1 | AFZ06931.1 | Osc7112_2501 | Osc7112_2500 | Protein of unknown function DUF2358; PFAM: Uncharacterized conserved protein (DUF2358); InterPro IPR018790; KEGG: ter:Tery_4691 hypothetical protein; PFAM: Protein of unknown function DUF2358; SPTR: Putative uncharacterized protein. | beta-Ig-H3/fasciclin; PFAM: Fasciclin domain; COGs: COG2335 Secreted and surface protein containing fasciclin-like repeats; InterPro IPR000782; KEGG: ava:Ava_2167 beta-Ig-H3/fasciclin; PFAM: FAS1 domain; SMART: FAS1 domain; SPTR: Beta-Ig-H3/fasciclin. | 0.465 |
AFZ09417.1 | AFZ06248.1 | Osc7112_5163 | Osc7112_1755 | PFAM: CO2 hydration protein (ChpXY); TIGRFAM: CO2 hydration protein; InterPro IPR010220; KEGG: cyj:Cyan7822_2890 CO2 hydration protein; PFAM: CO2 hydration; SPTR: CO2 hydration protein; TIGRFAM: CO2 hydration. | KEGG: ava:Ava_4792 hypothetical protein; SPTR: Putative uncharacterized protein. | 0.459 |
AFZ09417.1 | AFZ06931.1 | Osc7112_5163 | Osc7112_2500 | PFAM: CO2 hydration protein (ChpXY); TIGRFAM: CO2 hydration protein; InterPro IPR010220; KEGG: cyj:Cyan7822_2890 CO2 hydration protein; PFAM: CO2 hydration; SPTR: CO2 hydration protein; TIGRFAM: CO2 hydration. | beta-Ig-H3/fasciclin; PFAM: Fasciclin domain; COGs: COG2335 Secreted and surface protein containing fasciclin-like repeats; InterPro IPR000782; KEGG: ava:Ava_2167 beta-Ig-H3/fasciclin; PFAM: FAS1 domain; SMART: FAS1 domain; SPTR: Beta-Ig-H3/fasciclin. | 0.471 |
AFZ09417.1 | ndhH | Osc7112_5163 | Osc7112_3389 | PFAM: CO2 hydration protein (ChpXY); TIGRFAM: CO2 hydration protein; InterPro IPR010220; KEGG: cyj:Cyan7822_2890 CO2 hydration protein; PFAM: CO2 hydration; SPTR: CO2 hydration protein; TIGRFAM: CO2 hydration. | 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. | 0.859 |
ndhH | AFZ06248.1 | Osc7112_3389 | Osc7112_1755 | 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. | KEGG: ava:Ava_4792 hypothetical protein; SPTR: Putative uncharacterized protein. | 0.701 |
ndhH | AFZ06522.1 | Osc7112_3389 | Osc7112_2051 | 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. | PFAM: CO2 hydration protein (ChpXY); TIGRFAM: CO2 hydration protein; InterPro IPR010220; KEGG: naz:Aazo_4081 CO2 hydration protein; PFAM: CO2 hydration; SPTR: CO2 hydration protein; TIGRFAM: CO2 hydration. | 0.942 |
ndhH | AFZ06931.1 | Osc7112_3389 | Osc7112_2500 | 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. | beta-Ig-H3/fasciclin; PFAM: Fasciclin domain; COGs: COG2335 Secreted and surface protein containing fasciclin-like repeats; InterPro IPR000782; KEGG: ava:Ava_2167 beta-Ig-H3/fasciclin; PFAM: FAS1 domain; SMART: FAS1 domain; SPTR: Beta-Ig-H3/fasciclin. | 0.745 |
ndhH | AFZ09417.1 | Osc7112_3389 | Osc7112_5163 | 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. | PFAM: CO2 hydration protein (ChpXY); TIGRFAM: CO2 hydration protein; InterPro IPR010220; KEGG: cyj:Cyan7822_2890 CO2 hydration protein; PFAM: CO2 hydration; SPTR: CO2 hydration protein; TIGRFAM: CO2 hydration. | 0.859 |