| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| RPC_0804 | def | RPC_0804 | RPC_0803 | Hypothetical protein. | Peptide deformylase; Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions. | 0.601 |
| RPC_0804 | fmt | RPC_0804 | RPC_0806 | Hypothetical protein. | methionyl-tRNA formyltransferase; Attaches a formyl group to the free amino group of methionyl- tRNA(fMet). The formyl group appears to play a dual role in the initiator identity of N-formylmethionyl-tRNA by promoting its recognition by IF2 and preventing the misappropriation of this tRNA by the elongation apparatus; Belongs to the Fmt family. | 0.701 |
| RPC_0804 | truA | RPC_0804 | RPC_0807 | Hypothetical protein. | tRNA pseudouridine synthase A; Formation of pseudouridine at positions 38, 39 and 40 in the anticodon stem and loop of transfer RNAs. | 0.428 |
| RPC_0804 | vapC | RPC_0804 | RPC_0805 | Hypothetical protein. | PilT protein-like; Toxic component of a toxin-antitoxin (TA) system. An RNase. Belongs to the PINc/VapC protein family. | 0.773 |
| def | RPC_0804 | RPC_0803 | RPC_0804 | Peptide deformylase; Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions. | Hypothetical protein. | 0.601 |
| def | fmt | RPC_0803 | RPC_0806 | Peptide deformylase; Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions. | methionyl-tRNA formyltransferase; Attaches a formyl group to the free amino group of methionyl- tRNA(fMet). The formyl group appears to play a dual role in the initiator identity of N-formylmethionyl-tRNA by promoting its recognition by IF2 and preventing the misappropriation of this tRNA by the elongation apparatus; Belongs to the Fmt family. | 0.970 |
| def | truA | RPC_0803 | RPC_0807 | Peptide deformylase; Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions. | tRNA pseudouridine synthase A; Formation of pseudouridine at positions 38, 39 and 40 in the anticodon stem and loop of transfer RNAs. | 0.644 |
| def | vapC | RPC_0803 | RPC_0805 | Peptide deformylase; Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions. | PilT protein-like; Toxic component of a toxin-antitoxin (TA) system. An RNase. Belongs to the PINc/VapC protein family. | 0.601 |
| fmt | RPC_0804 | RPC_0806 | RPC_0804 | methionyl-tRNA formyltransferase; Attaches a formyl group to the free amino group of methionyl- tRNA(fMet). The formyl group appears to play a dual role in the initiator identity of N-formylmethionyl-tRNA by promoting its recognition by IF2 and preventing the misappropriation of this tRNA by the elongation apparatus; Belongs to the Fmt family. | Hypothetical protein. | 0.701 |
| fmt | def | RPC_0806 | RPC_0803 | methionyl-tRNA formyltransferase; Attaches a formyl group to the free amino group of methionyl- tRNA(fMet). The formyl group appears to play a dual role in the initiator identity of N-formylmethionyl-tRNA by promoting its recognition by IF2 and preventing the misappropriation of this tRNA by the elongation apparatus; Belongs to the Fmt family. | Peptide deformylase; Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions. | 0.970 |
| fmt | truA | RPC_0806 | RPC_0807 | methionyl-tRNA formyltransferase; Attaches a formyl group to the free amino group of methionyl- tRNA(fMet). The formyl group appears to play a dual role in the initiator identity of N-formylmethionyl-tRNA by promoting its recognition by IF2 and preventing the misappropriation of this tRNA by the elongation apparatus; Belongs to the Fmt family. | tRNA pseudouridine synthase A; Formation of pseudouridine at positions 38, 39 and 40 in the anticodon stem and loop of transfer RNAs. | 0.764 |
| fmt | vapC | RPC_0806 | RPC_0805 | methionyl-tRNA formyltransferase; Attaches a formyl group to the free amino group of methionyl- tRNA(fMet). The formyl group appears to play a dual role in the initiator identity of N-formylmethionyl-tRNA by promoting its recognition by IF2 and preventing the misappropriation of this tRNA by the elongation apparatus; Belongs to the Fmt family. | PilT protein-like; Toxic component of a toxin-antitoxin (TA) system. An RNase. Belongs to the PINc/VapC protein family. | 0.701 |
| truA | RPC_0804 | RPC_0807 | RPC_0804 | tRNA pseudouridine synthase A; Formation of pseudouridine at positions 38, 39 and 40 in the anticodon stem and loop of transfer RNAs. | Hypothetical protein. | 0.428 |
| truA | def | RPC_0807 | RPC_0803 | tRNA pseudouridine synthase A; Formation of pseudouridine at positions 38, 39 and 40 in the anticodon stem and loop of transfer RNAs. | Peptide deformylase; Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions. | 0.644 |
| truA | fmt | RPC_0807 | RPC_0806 | tRNA pseudouridine synthase A; Formation of pseudouridine at positions 38, 39 and 40 in the anticodon stem and loop of transfer RNAs. | methionyl-tRNA formyltransferase; Attaches a formyl group to the free amino group of methionyl- tRNA(fMet). The formyl group appears to play a dual role in the initiator identity of N-formylmethionyl-tRNA by promoting its recognition by IF2 and preventing the misappropriation of this tRNA by the elongation apparatus; Belongs to the Fmt family. | 0.764 |
| truA | vapC | RPC_0807 | RPC_0805 | tRNA pseudouridine synthase A; Formation of pseudouridine at positions 38, 39 and 40 in the anticodon stem and loop of transfer RNAs. | PilT protein-like; Toxic component of a toxin-antitoxin (TA) system. An RNase. Belongs to the PINc/VapC protein family. | 0.443 |
| vapC | RPC_0804 | RPC_0805 | RPC_0804 | PilT protein-like; Toxic component of a toxin-antitoxin (TA) system. An RNase. Belongs to the PINc/VapC protein family. | Hypothetical protein. | 0.773 |
| vapC | def | RPC_0805 | RPC_0803 | PilT protein-like; Toxic component of a toxin-antitoxin (TA) system. An RNase. Belongs to the PINc/VapC protein family. | Peptide deformylase; Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions. | 0.601 |
| vapC | fmt | RPC_0805 | RPC_0806 | PilT protein-like; Toxic component of a toxin-antitoxin (TA) system. An RNase. Belongs to the PINc/VapC protein family. | methionyl-tRNA formyltransferase; Attaches a formyl group to the free amino group of methionyl- tRNA(fMet). The formyl group appears to play a dual role in the initiator identity of N-formylmethionyl-tRNA by promoting its recognition by IF2 and preventing the misappropriation of this tRNA by the elongation apparatus; Belongs to the Fmt family. | 0.701 |
| vapC | truA | RPC_0805 | RPC_0807 | PilT protein-like; Toxic component of a toxin-antitoxin (TA) system. An RNase. Belongs to the PINc/VapC protein family. | tRNA pseudouridine synthase A; Formation of pseudouridine at positions 38, 39 and 40 in the anticodon stem and loop of transfer RNAs. | 0.443 |