| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| CF15_02790 | CF15_02795 | CF15_02790 | CF15_02795 | tRNA-Leu; Derived by automated computational analysis using gene prediction method: Protein Homology. | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.658 |
| CF15_02790 | CF15_02805 | CF15_02790 | CF15_02805 | tRNA-Leu; Derived by automated computational analysis using gene prediction method: Protein Homology. | Phosphohydrolase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.406 |
| CF15_02790 | cca | CF15_02790 | CF15_02800 | tRNA-Leu; Derived by automated computational analysis using gene prediction method: Protein Homology. | Hypothetical protein; Catalyzes the addition and repair of the essential 3'- terminal CCA sequence in tRNAs without using a nucleic acid template. Adds these three nucleotides in the order of C, C, and A to the tRNA nucleotide-73, using CTP and ATP as substrates and producing inorganic pyrophosphate. | 0.658 |
| CF15_02795 | CF15_02790 | CF15_02795 | CF15_02790 | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | tRNA-Leu; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.658 |
| CF15_02795 | CF15_02805 | CF15_02795 | CF15_02805 | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | Phosphohydrolase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.465 |
| CF15_02795 | cca | CF15_02795 | CF15_02800 | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | Hypothetical protein; Catalyzes the addition and repair of the essential 3'- terminal CCA sequence in tRNAs without using a nucleic acid template. Adds these three nucleotides in the order of C, C, and A to the tRNA nucleotide-73, using CTP and ATP as substrates and producing inorganic pyrophosphate. | 0.873 |
| CF15_02805 | CF15_02790 | CF15_02805 | CF15_02790 | Phosphohydrolase; Derived by automated computational analysis using gene prediction method: Protein Homology. | tRNA-Leu; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.406 |
| CF15_02805 | CF15_02795 | CF15_02805 | CF15_02795 | Phosphohydrolase; Derived by automated computational analysis using gene prediction method: Protein Homology. | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.465 |
| CF15_02805 | cca | CF15_02805 | CF15_02800 | Phosphohydrolase; Derived by automated computational analysis using gene prediction method: Protein Homology. | Hypothetical protein; Catalyzes the addition and repair of the essential 3'- terminal CCA sequence in tRNAs without using a nucleic acid template. Adds these three nucleotides in the order of C, C, and A to the tRNA nucleotide-73, using CTP and ATP as substrates and producing inorganic pyrophosphate. | 0.465 |
| CF15_02805 | purS | CF15_02805 | CF15_04880 | Phosphohydrolase; Derived by automated computational analysis using gene prediction method: Protein Homology. | Hypothetical protein; Part of the phosphoribosylformylglycinamidine synthase complex involved in the purines biosynthetic pathway. Catalyzes the ATP-dependent conversion of formylglycinamide ribonucleotide (FGAR) and glutamine to yield formylglycinamidine ribonucleotide (FGAM) and glutamate. The FGAM synthase complex is composed of three subunits. PurQ produces an ammonia molecule by converting glutamine to glutamate. PurL transfers the ammonia molecule to FGAR to form FGAM in an ATP- dependent manner. PurS interacts with PurQ and PurL and is thought to assist in the transfer of the am [...] | 0.428 |
| cca | CF15_02790 | CF15_02800 | CF15_02790 | Hypothetical protein; Catalyzes the addition and repair of the essential 3'- terminal CCA sequence in tRNAs without using a nucleic acid template. Adds these three nucleotides in the order of C, C, and A to the tRNA nucleotide-73, using CTP and ATP as substrates and producing inorganic pyrophosphate. | tRNA-Leu; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.658 |
| cca | CF15_02795 | CF15_02800 | CF15_02795 | Hypothetical protein; Catalyzes the addition and repair of the essential 3'- terminal CCA sequence in tRNAs without using a nucleic acid template. Adds these three nucleotides in the order of C, C, and A to the tRNA nucleotide-73, using CTP and ATP as substrates and producing inorganic pyrophosphate. | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.873 |
| cca | CF15_02805 | CF15_02800 | CF15_02805 | Hypothetical protein; Catalyzes the addition and repair of the essential 3'- terminal CCA sequence in tRNAs without using a nucleic acid template. Adds these three nucleotides in the order of C, C, and A to the tRNA nucleotide-73, using CTP and ATP as substrates and producing inorganic pyrophosphate. | Phosphohydrolase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.465 |
| purS | CF15_02805 | CF15_04880 | CF15_02805 | Hypothetical protein; Part of the phosphoribosylformylglycinamidine synthase complex involved in the purines biosynthetic pathway. Catalyzes the ATP-dependent conversion of formylglycinamide ribonucleotide (FGAR) and glutamine to yield formylglycinamidine ribonucleotide (FGAM) and glutamate. The FGAM synthase complex is composed of three subunits. PurQ produces an ammonia molecule by converting glutamine to glutamate. PurL transfers the ammonia molecule to FGAR to form FGAM in an ATP- dependent manner. PurS interacts with PurQ and PurL and is thought to assist in the transfer of the am [...] | Phosphohydrolase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.428 |