| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| Msp_1323 | alaS | Msp_1323 | Msp_1262 | Conserved hypothetical protein; Related to flp pilus assembly protein PilF; cd00189. | AlaS; Catalyzes the attachment of alanine to tRNA(Ala) in a two- step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) via its editing domain. | 0.996 |
| Msp_1323 | rpl40e | Msp_1323 | Msp_1292 | Conserved hypothetical protein; Related to flp pilus assembly protein PilF; cd00189. | 50S ribosomal protein L40e; Belongs to the eukaryotic ribosomal protein eL40 family. | 0.819 |
| alaS | Msp_1323 | Msp_1262 | Msp_1323 | AlaS; Catalyzes the attachment of alanine to tRNA(Ala) in a two- step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) via its editing domain. | Conserved hypothetical protein; Related to flp pilus assembly protein PilF; cd00189. | 0.996 |
| alaS | glyS | Msp_1262 | Msp_1049 | AlaS; Catalyzes the attachment of alanine to tRNA(Ala) in a two- step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) via its editing domain. | GlyS; glycyl-tRNA synthetase; COG0423, pfam00587, cd00774. | 0.881 |
| alaS | hisS | Msp_1262 | Msp_0648 | AlaS; Catalyzes the attachment of alanine to tRNA(Ala) in a two- step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) via its editing domain. | HisS; histidyl-tRNA synthetase; Belongs to the class-II aminoacyl-tRNA synthetase family. | 0.834 |
| alaS | ileS | Msp_1262 | Msp_1468 | AlaS; Catalyzes the attachment of alanine to tRNA(Ala) in a two- step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) via its editing domain. | IleS; Catalyzes the attachment of isoleucine to tRNA(Ile). As IleRS can inadvertently accommodate and process structurally similar amino acids such as valine, to avoid such errors it has two additional distinct tRNA(Ile)-dependent editing activities. One activity is designated as 'pretransfer' editing and involves the hydrolysis of activated Val-AMP. The other activity is designated 'posttransfer' editing and involves deacylation of mischarged Val-tRNA(Ile). Belongs to the class-I aminoacyl-tRNA synthetase family. IleS type 2 subfamily. | 0.900 |
| alaS | leuS | Msp_1262 | Msp_0171 | AlaS; Catalyzes the attachment of alanine to tRNA(Ala) in a two- step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) via its editing domain. | LeuS; leucyl-tRNA synthetase; Belongs to the class-I aminoacyl-tRNA synthetase family. | 0.905 |
| alaS | metG | Msp_1262 | Msp_0083 | AlaS; Catalyzes the attachment of alanine to tRNA(Ala) in a two- step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) via its editing domain. | MetG; Is required not only for elongation of protein synthesis but also for the initiation of all mRNA translation through initiator tRNA(fMet) aminoacylation. | 0.827 |
| alaS | rpl40e | Msp_1262 | Msp_1292 | AlaS; Catalyzes the attachment of alanine to tRNA(Ala) in a two- step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) via its editing domain. | 50S ribosomal protein L40e; Belongs to the eukaryotic ribosomal protein eL40 family. | 0.792 |
| alaS | thrS | Msp_1262 | Msp_1573 | AlaS; Catalyzes the attachment of alanine to tRNA(Ala) in a two- step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) via its editing domain. | ThrS; Catalyzes the attachment of threonine to tRNA(Thr) in a two- step reaction: L-threonine is first activated by ATP to form Thr-AMP and then transferred to the acceptor end of tRNA(Thr). Also edits incorrectly charged L-seryl-tRNA(Thr); Belongs to the class-II aminoacyl-tRNA synthetase family. | 0.825 |
| alaS | trpS | Msp_1262 | Msp_0653 | AlaS; Catalyzes the attachment of alanine to tRNA(Ala) in a two- step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) via its editing domain. | TrpS; Catalyzes the attachment of tryptophan to tRNA(Trp). | 0.826 |
| alaS | valS | Msp_1262 | Msp_0499 | AlaS; Catalyzes the attachment of alanine to tRNA(Ala) in a two- step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) via its editing domain. | ValS; Catalyzes the attachment of valine to tRNA(Val). As ValRS can inadvertently accommodate and process structurally similar amino acids such as threonine, to avoid such errors, it has a 'posttransfer' editing activity that hydrolyzes mischarged Thr-tRNA(Val) in a tRNA- dependent manner; Belongs to the class-I aminoacyl-tRNA synthetase family. ValS type 2 subfamily. | 0.917 |
| glyS | alaS | Msp_1049 | Msp_1262 | GlyS; glycyl-tRNA synthetase; COG0423, pfam00587, cd00774. | AlaS; Catalyzes the attachment of alanine to tRNA(Ala) in a two- step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) via its editing domain. | 0.881 |
| glyS | hisS | Msp_1049 | Msp_0648 | GlyS; glycyl-tRNA synthetase; COG0423, pfam00587, cd00774. | HisS; histidyl-tRNA synthetase; Belongs to the class-II aminoacyl-tRNA synthetase family. | 0.666 |
| glyS | ileS | Msp_1049 | Msp_1468 | GlyS; glycyl-tRNA synthetase; COG0423, pfam00587, cd00774. | IleS; Catalyzes the attachment of isoleucine to tRNA(Ile). As IleRS can inadvertently accommodate and process structurally similar amino acids such as valine, to avoid such errors it has two additional distinct tRNA(Ile)-dependent editing activities. One activity is designated as 'pretransfer' editing and involves the hydrolysis of activated Val-AMP. The other activity is designated 'posttransfer' editing and involves deacylation of mischarged Val-tRNA(Ile). Belongs to the class-I aminoacyl-tRNA synthetase family. IleS type 2 subfamily. | 0.909 |
| glyS | leuS | Msp_1049 | Msp_0171 | GlyS; glycyl-tRNA synthetase; COG0423, pfam00587, cd00774. | LeuS; leucyl-tRNA synthetase; Belongs to the class-I aminoacyl-tRNA synthetase family. | 0.849 |
| glyS | metG | Msp_1049 | Msp_0083 | GlyS; glycyl-tRNA synthetase; COG0423, pfam00587, cd00774. | MetG; Is required not only for elongation of protein synthesis but also for the initiation of all mRNA translation through initiator tRNA(fMet) aminoacylation. | 0.807 |
| glyS | thrS | Msp_1049 | Msp_1573 | GlyS; glycyl-tRNA synthetase; COG0423, pfam00587, cd00774. | ThrS; Catalyzes the attachment of threonine to tRNA(Thr) in a two- step reaction: L-threonine is first activated by ATP to form Thr-AMP and then transferred to the acceptor end of tRNA(Thr). Also edits incorrectly charged L-seryl-tRNA(Thr); Belongs to the class-II aminoacyl-tRNA synthetase family. | 0.654 |
| glyS | trpS | Msp_1049 | Msp_0653 | GlyS; glycyl-tRNA synthetase; COG0423, pfam00587, cd00774. | TrpS; Catalyzes the attachment of tryptophan to tRNA(Trp). | 0.645 |
| glyS | valS | Msp_1049 | Msp_0499 | GlyS; glycyl-tRNA synthetase; COG0423, pfam00587, cd00774. | ValS; Catalyzes the attachment of valine to tRNA(Val). As ValRS can inadvertently accommodate and process structurally similar amino acids such as threonine, to avoid such errors, it has a 'posttransfer' editing activity that hydrolyzes mischarged Thr-tRNA(Val) in a tRNA- dependent manner; Belongs to the class-I aminoacyl-tRNA synthetase family. ValS type 2 subfamily. | 0.794 |