node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
KQT44640.1 | KQT44641.1 | ASG43_14055 | ASG43_14060 | DNA recombinase; Derived by automated computational analysis using gene prediction method: Protein Homology. | Serine protease; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.451 |
KQT44640.1 | def | ASG43_14055 | ASG43_14050 | DNA recombinase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 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. | 0.575 |
KQT44640.1 | fmt | ASG43_14055 | ASG43_14045 | DNA recombinase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 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. | 0.516 |
KQT44640.1 | truA | ASG43_14055 | ASG43_14040 | DNA recombinase; Derived by automated computational analysis using gene prediction method: Protein Homology. | Pseudouridine synthase; Formation of pseudouridine at positions 38, 39 and 40 in the anticodon stem and loop of transfer RNAs. | 0.516 |
KQT44641.1 | KQT44640.1 | ASG43_14060 | ASG43_14055 | Serine protease; Derived by automated computational analysis using gene prediction method: Protein Homology. | DNA recombinase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.451 |
KQT44641.1 | def | ASG43_14060 | ASG43_14050 | Serine protease; Derived by automated computational analysis using gene prediction method: Protein Homology. | 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. | 0.457 |
KQT44641.1 | truA | ASG43_14060 | ASG43_14040 | Serine protease; Derived by automated computational analysis using gene prediction method: Protein Homology. | Pseudouridine synthase; Formation of pseudouridine at positions 38, 39 and 40 in the anticodon stem and loop of transfer RNAs. | 0.476 |
def | KQT44640.1 | ASG43_14050 | ASG43_14055 | 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. | DNA recombinase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.575 |
def | KQT44641.1 | ASG43_14050 | ASG43_14060 | 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. | Serine protease; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.457 |
def | fmt | ASG43_14050 | ASG43_14045 | 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. | 0.978 |
def | truA | ASG43_14050 | ASG43_14040 | 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. | Pseudouridine synthase; Formation of pseudouridine at positions 38, 39 and 40 in the anticodon stem and loop of transfer RNAs. | 0.736 |
fmt | KQT44640.1 | ASG43_14045 | ASG43_14055 | 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. | DNA recombinase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.516 |
fmt | def | ASG43_14045 | ASG43_14050 | 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. | 0.978 |
fmt | truA | ASG43_14045 | ASG43_14040 | 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. | Pseudouridine synthase; Formation of pseudouridine at positions 38, 39 and 40 in the anticodon stem and loop of transfer RNAs. | 0.853 |
truA | KQT44640.1 | ASG43_14040 | ASG43_14055 | Pseudouridine synthase; Formation of pseudouridine at positions 38, 39 and 40 in the anticodon stem and loop of transfer RNAs. | DNA recombinase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.516 |
truA | KQT44641.1 | ASG43_14040 | ASG43_14060 | Pseudouridine synthase; Formation of pseudouridine at positions 38, 39 and 40 in the anticodon stem and loop of transfer RNAs. | Serine protease; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.476 |
truA | def | ASG43_14040 | ASG43_14050 | Pseudouridine synthase; 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. | 0.736 |
truA | fmt | ASG43_14040 | ASG43_14045 | Pseudouridine synthase; 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. | 0.853 |