| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| map | rplS | sync_2170 | sync_2168 | Methionine aminopeptidase, type I; Removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val). Requires deformylation of the N(alpha)-formylated initiator methionine before it can be hydrolyzed; Belongs to the peptidase M24A family. Methionine aminopeptidase type 1 subfamily. | Ribosomal protein L19; This protein is located at the 30S-50S ribosomal subunit interface and may play a role in the structure and function of the aminoacyl-tRNA binding site. | 0.681 |
| map | sync_2169 | sync_2170 | sync_2169 | Methionine aminopeptidase, type I; Removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val). Requires deformylation of the N(alpha)-formylated initiator methionine before it can be hydrolyzed; Belongs to the peptidase M24A family. Methionine aminopeptidase type 1 subfamily. | Conserved hypothetical protein; Identified by match to protein family HMM PF03929. | 0.568 |
| ndhL | sync_0287 | sync_1912 | sync_0287 | Possible inorganic carbon transport protein; 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. | Uncharacterized protein. | 0.734 |
| ndhL | sync_0598 | sync_1912 | sync_0598 | Possible inorganic carbon transport protein; 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. | Uncharacterized protein. | 0.727 |
| ndhL | sync_1146 | sync_1912 | sync_1146 | Possible inorganic carbon transport protein; 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. | Uncharacterized protein. | 0.522 |
| ndhL | sync_1881 | sync_1912 | sync_1881 | Possible inorganic carbon transport protein; 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. | Conserved hypothetical protein. | 0.741 |
| ndhL | sync_2124 | sync_1912 | sync_2124 | Possible inorganic carbon transport protein; 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. | AbrB family transciptional regulator. | 0.751 |
| ndhL | sync_2169 | sync_1912 | sync_2169 | Possible inorganic carbon transport protein; 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. | Conserved hypothetical protein; Identified by match to protein family HMM PF03929. | 0.642 |
| ndhL | sync_2587 | sync_1912 | sync_2587 | Possible inorganic carbon transport protein; 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. | Conserved hypothetical protein; Identified by similarity to GB:CAE22160.1; Belongs to the UPF0367 family. | 0.584 |
| rplS | map | sync_2168 | sync_2170 | Ribosomal protein L19; This protein is located at the 30S-50S ribosomal subunit interface and may play a role in the structure and function of the aminoacyl-tRNA binding site. | Methionine aminopeptidase, type I; Removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val). Requires deformylation of the N(alpha)-formylated initiator methionine before it can be hydrolyzed; Belongs to the peptidase M24A family. Methionine aminopeptidase type 1 subfamily. | 0.681 |
| rplS | sync_2169 | sync_2168 | sync_2169 | Ribosomal protein L19; This protein is located at the 30S-50S ribosomal subunit interface and may play a role in the structure and function of the aminoacyl-tRNA binding site. | Conserved hypothetical protein; Identified by match to protein family HMM PF03929. | 0.691 |
| sodX | sync_2169 | sync_0754 | sync_2169 | Nickel-type superoxide dismutase maturation protease; Identified by match to protein family HMM PF00717; match to protein family HMM TIGR02754. | Conserved hypothetical protein; Identified by match to protein family HMM PF03929. | 0.547 |
| sync_0287 | ndhL | sync_0287 | sync_1912 | Uncharacterized protein. | Possible inorganic carbon transport protein; 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. | 0.734 |
| sync_0287 | sync_0598 | sync_0287 | sync_0598 | Uncharacterized protein. | Uncharacterized protein. | 0.774 |
| sync_0287 | sync_1146 | sync_0287 | sync_1146 | Uncharacterized protein. | Uncharacterized protein. | 0.702 |
| sync_0287 | sync_1881 | sync_0287 | sync_1881 | Uncharacterized protein. | Conserved hypothetical protein. | 0.772 |
| sync_0287 | sync_2124 | sync_0287 | sync_2124 | Uncharacterized protein. | AbrB family transciptional regulator. | 0.774 |
| sync_0287 | sync_2169 | sync_0287 | sync_2169 | Uncharacterized protein. | Conserved hypothetical protein; Identified by match to protein family HMM PF03929. | 0.533 |
| sync_0287 | sync_2587 | sync_0287 | sync_2587 | Uncharacterized protein. | Conserved hypothetical protein; Identified by similarity to GB:CAE22160.1; Belongs to the UPF0367 family. | 0.746 |
| sync_0598 | ndhL | sync_0598 | sync_1912 | Uncharacterized protein. | Possible inorganic carbon transport protein; 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. | 0.727 |