| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| PAE2266 | alaS | PAE2266 | PAE3565 | glycyl-tRNA synthetase; Protein synthesis; tRNA aminoacylation. | 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. | 0.753 |
| PAE2266 | gltX | PAE2266 | PAE2969 | glycyl-tRNA synthetase; Protein synthesis; tRNA aminoacylation. | 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). | 0.639 |
| PAE2266 | guaA | PAE2266 | PAE3369 | glycyl-tRNA synthetase; Protein synthesis; tRNA aminoacylation. | GMP synthetase (glutamine-hydrolysing); Catalyzes the synthesis of GMP from XMP. | 0.757 |
| PAE2266 | hisS | PAE2266 | PAE1553 | glycyl-tRNA synthetase; Protein synthesis; tRNA aminoacylation. | histidyl-tRNA synthetase; Protein synthesis; tRNA aminoacylation; Belongs to the class-II aminoacyl-tRNA synthetase family. | 0.648 |
| PAE2266 | ileS | PAE2266 | PAE1617 | glycyl-tRNA synthetase; Protein synthesis; tRNA aminoacylation. | isoleucyl-tRNA synthetase; 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. | 0.897 |
| PAE2266 | leuS | PAE2266 | PAE1107 | glycyl-tRNA synthetase; Protein synthesis; tRNA aminoacylation. | leucyl-tRNA synthetase; Protein synthesis; tRNA aminoacylation; Belongs to the class-I aminoacyl-tRNA synthetase family. | 0.880 |
| PAE2266 | pheT | PAE2266 | PAE1669 | glycyl-tRNA synthetase; Protein synthesis; tRNA aminoacylation. | phenylalanyl-tRNA synthetase beta subunit; Protein synthesis; tRNA aminoacylation. | 0.695 |
| PAE2266 | thrS | PAE2266 | PAE1748 | glycyl-tRNA synthetase; Protein synthesis; tRNA aminoacylation. | 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); Belongs to the class-II aminoacyl-tRNA synthetase family. | 0.602 |
| PAE2266 | valS | PAE2266 | PAE2297 | glycyl-tRNA synthetase; Protein synthesis; tRNA aminoacylation. | 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 (By similarity); Belongs to the class-I aminoacyl-tRNA synthetase family. ValS type 2 subfamily. | 0.845 |
| alaS | PAE2266 | PAE3565 | PAE2266 | 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. | glycyl-tRNA synthetase; Protein synthesis; tRNA aminoacylation. | 0.753 |
| alaS | gltX | PAE3565 | PAE2969 | 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). | 0.735 |
| alaS | guaA | PAE3565 | PAE3369 | 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. | GMP synthetase (glutamine-hydrolysing); Catalyzes the synthesis of GMP from XMP. | 0.799 |
| alaS | hisS | PAE3565 | PAE1553 | 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; Protein synthesis; tRNA aminoacylation; Belongs to the class-II aminoacyl-tRNA synthetase family. | 0.811 |
| alaS | ileS | PAE3565 | PAE1617 | 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. | isoleucyl-tRNA synthetase; 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. | 0.841 |
| alaS | leuS | PAE3565 | PAE1107 | 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. | leucyl-tRNA synthetase; Protein synthesis; tRNA aminoacylation; Belongs to the class-I aminoacyl-tRNA synthetase family. | 0.885 |
| alaS | nac | PAE3565 | PAE3566 | 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. | Conserved hypothetical protein; Contacts the emerging nascent chain on the ribosome. Belongs to the NAC-alpha family. | 0.845 |
| alaS | pheT | PAE3565 | PAE1669 | 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 subunit; Protein synthesis; tRNA aminoacylation. | 0.722 |
| alaS | thrS | PAE3565 | PAE1748 | 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); Belongs to the class-II aminoacyl-tRNA synthetase family. | 0.822 |
| alaS | valS | PAE3565 | PAE2297 | 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 (By similarity); Belongs to the class-I aminoacyl-tRNA synthetase family. ValS type 2 subfamily. | 0.807 |
| gltX | PAE2266 | PAE2969 | PAE2266 | 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). | glycyl-tRNA synthetase; Protein synthesis; tRNA aminoacylation. | 0.639 |