| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| BT_4312 | alaS | BT_4312 | BT_3995 | seryl-tRNA synthetase. | alanyl-tRNA synthetase; 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. | 0.541 |
| BT_4312 | cysS | BT_4312 | BT_3351 | seryl-tRNA synthetase. | cysteinyl-tRNA synthetase; Belongs to the class-I aminoacyl-tRNA synthetase family. | 0.705 |
| BT_4312 | gltX | BT_4312 | BT_2748 | seryl-tRNA synthetase. | glutamyl-tRNA synthetase; Catalyzes the attachment of glutamate to tRNA(Glu) in a two- step reaction: glutamate is first activated by ATP to form Glu-AMP and then transferred to the acceptor end of tRNA(Glu); Belongs to the class-I aminoacyl-tRNA synthetase family. Glutamate--tRNA ligase type 1 subfamily. | 0.602 |
| BT_4312 | hisS | BT_4312 | BT_1840 | seryl-tRNA synthetase. | histidyl-tRNA synthetase. | 0.431 |
| BT_4312 | metG | BT_4312 | BT_2933 | seryl-tRNA synthetase. | Methionyl-tRNA synthetase; Is required not only for elongation of protein synthesis but also for the initiation of all mRNA translation through initiator tRNA(fMet) aminoacylation. | 0.589 |
| BT_4312 | pheT | BT_4312 | BT_0626 | seryl-tRNA synthetase. | phenylalanyl-tRNA synthetase beta chain; Belongs to the phenylalanyl-tRNA synthetase beta subunit family. Type 1 subfamily. | 0.689 |
| BT_4312 | thrS | BT_4312 | BT_0422 | seryl-tRNA synthetase. | threonyl-tRNA synthetase; 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). | 0.736 |
| BT_4312 | valS | BT_4312 | BT_4353 | seryl-tRNA synthetase. | valyl-tRNA synthetase; 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 1 subfamily. | 0.766 |
| alaS | BT_4312 | BT_3995 | BT_4312 | alanyl-tRNA synthetase; 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. | seryl-tRNA synthetase. | 0.541 |
| alaS | cysS | BT_3995 | BT_3351 | alanyl-tRNA synthetase; 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. | cysteinyl-tRNA synthetase; Belongs to the class-I aminoacyl-tRNA synthetase family. | 0.409 |
| alaS | gltX | BT_3995 | BT_2748 | alanyl-tRNA synthetase; 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. | glutamyl-tRNA synthetase; Catalyzes the attachment of glutamate to tRNA(Glu) in a two- step reaction: glutamate is first activated by ATP to form Glu-AMP and then transferred to the acceptor end of tRNA(Glu); Belongs to the class-I aminoacyl-tRNA synthetase family. Glutamate--tRNA ligase type 1 subfamily. | 0.843 |
| alaS | hisS | BT_3995 | BT_1840 | alanyl-tRNA synthetase; 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. | histidyl-tRNA synthetase. | 0.530 |
| alaS | metG | BT_3995 | BT_2933 | alanyl-tRNA synthetase; 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. | Methionyl-tRNA synthetase; Is required not only for elongation of protein synthesis but also for the initiation of all mRNA translation through initiator tRNA(fMet) aminoacylation. | 0.802 |
| alaS | pheT | BT_3995 | BT_0626 | alanyl-tRNA synthetase; 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. | phenylalanyl-tRNA synthetase beta chain; Belongs to the phenylalanyl-tRNA synthetase beta subunit family. Type 1 subfamily. | 0.811 |
| alaS | thrS | BT_3995 | BT_0422 | alanyl-tRNA synthetase; 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. | threonyl-tRNA synthetase; 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). | 0.746 |
| alaS | valS | BT_3995 | BT_4353 | alanyl-tRNA synthetase; 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. | valyl-tRNA synthetase; 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 1 subfamily. | 0.797 |
| cysS | BT_4312 | BT_3351 | BT_4312 | cysteinyl-tRNA synthetase; Belongs to the class-I aminoacyl-tRNA synthetase family. | seryl-tRNA synthetase. | 0.705 |
| cysS | alaS | BT_3351 | BT_3995 | cysteinyl-tRNA synthetase; Belongs to the class-I aminoacyl-tRNA synthetase family. | alanyl-tRNA synthetase; 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. | 0.409 |
| cysS | gltX | BT_3351 | BT_2748 | cysteinyl-tRNA synthetase; Belongs to the class-I aminoacyl-tRNA synthetase family. | glutamyl-tRNA synthetase; Catalyzes the attachment of glutamate to tRNA(Glu) in a two- step reaction: glutamate is first activated by ATP to form Glu-AMP and then transferred to the acceptor end of tRNA(Glu); Belongs to the class-I aminoacyl-tRNA synthetase family. Glutamate--tRNA ligase type 1 subfamily. | 0.542 |
| cysS | hisS | BT_3351 | BT_1840 | cysteinyl-tRNA synthetase; Belongs to the class-I aminoacyl-tRNA synthetase family. | histidyl-tRNA synthetase. | 0.817 |