| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| alaS | glyQ | bbp_364 | bbp_127 | 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; Belongs to the class-II aminoacyl-tRNA synthetase family. | COG0752; glycine--tRNA ligase alpha chain; GlyRS. | 0.715 |
| alaS | glyS | bbp_364 | bbp_126 | 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; Belongs to the class-II aminoacyl-tRNA synthetase family. | glycyl-tRNA synthetase beta chain (Glycine--tRNA ligase beta chain) (GlyRS); COG0751. | 0.698 |
| alaS | ileS | bbp_364 | bbp_139 | 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; Belongs to the class-II aminoacyl-tRNA synthetase family. | 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 1 subfamily. | 0.658 |
| alaS | leuS | bbp_364 | bbp_395 | 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; Belongs to the class-II aminoacyl-tRNA synthetase family. | leucyl-tRNA synthetase; COG0495; leucine-tRNA ligase; LEURS; Belongs to the class-I aminoacyl-tRNA synthetase family. | 0.725 |
| alaS | metG | bbp_364 | bbp_103 | 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; Belongs to the class-II aminoacyl-tRNA synthetase family. | 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. | 0.934 |
| alaS | pheT | bbp_364 | bbp_124 | 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; Belongs to the class-II aminoacyl-tRNA synthetase family. | COG0073; COG0072; phenylalanine-tRNA ligase beta chain; PheRS; Belongs to the phenylalanyl-tRNA synthetase beta subunit family. Type 1 subfamily. | 0.803 |
| alaS | smpB | bbp_364 | bbp_235 | 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; Belongs to the class-II aminoacyl-tRNA synthetase family. | SsrA-binding protein; Required for rescue of stalled ribosomes mediated by trans- translation. Binds to transfer-messenger RNA (tmRNA), required for stable association of tmRNA with ribosomes. tmRNA and SmpB together mimic tRNA shape, replacing the anticodon stem-loop with SmpB. tmRNA is encoded by the ssrA gene; the 2 termini fold to resemble tRNA(Ala) and it encodes a 'tag peptide', a short internal open reading frame. During trans-translation Ala-aminoacylated tmRNA acts like a tRNA, entering the A-site of stalled ribosomes, displacing the stalled mRNA. The ribosome then switches to [...] | 0.585 |
| alaS | thrS | bbp_364 | bbp_119 | 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; Belongs to the class-II aminoacyl-tRNA synthetase family. | 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). | 0.679 |
| alaS | valS | bbp_364 | bbp_331 | 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; Belongs to the class-II aminoacyl-tRNA synthetase family. | 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. | 0.893 |
| alaS | yqgF | bbp_364 | bbp_492 | 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; Belongs to the class-II aminoacyl-tRNA synthetase family. | Hypothetical 16.0 kDa protein; Could be a nuclease involved in processing of the 5'-end of pre-16S rRNA; Belongs to the YqgF nuclease family. | 0.665 |
| glyQ | alaS | bbp_127 | bbp_364 | COG0752; glycine--tRNA ligase alpha chain; GlyRS. | 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; Belongs to the class-II aminoacyl-tRNA synthetase family. | 0.715 |
| glyQ | glyS | bbp_127 | bbp_126 | COG0752; glycine--tRNA ligase alpha chain; GlyRS. | glycyl-tRNA synthetase beta chain (Glycine--tRNA ligase beta chain) (GlyRS); COG0751. | 0.999 |
| glyQ | ileS | bbp_127 | bbp_139 | COG0752; glycine--tRNA ligase alpha chain; GlyRS. | 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 1 subfamily. | 0.690 |
| glyQ | leuS | bbp_127 | bbp_395 | COG0752; glycine--tRNA ligase alpha chain; GlyRS. | leucyl-tRNA synthetase; COG0495; leucine-tRNA ligase; LEURS; Belongs to the class-I aminoacyl-tRNA synthetase family. | 0.549 |
| glyQ | metG | bbp_127 | bbp_103 | COG0752; glycine--tRNA ligase alpha chain; GlyRS. | 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. | 0.698 |
| glyQ | pheT | bbp_127 | bbp_124 | COG0752; glycine--tRNA ligase alpha chain; GlyRS. | COG0073; COG0072; phenylalanine-tRNA ligase beta chain; PheRS; Belongs to the phenylalanyl-tRNA synthetase beta subunit family. Type 1 subfamily. | 0.632 |
| glyQ | valS | bbp_127 | bbp_331 | COG0752; glycine--tRNA ligase alpha chain; GlyRS. | 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. | 0.531 |
| glyS | alaS | bbp_126 | bbp_364 | glycyl-tRNA synthetase beta chain (Glycine--tRNA ligase beta chain) (GlyRS); COG0751. | 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; Belongs to the class-II aminoacyl-tRNA synthetase family. | 0.698 |
| glyS | glyQ | bbp_126 | bbp_127 | glycyl-tRNA synthetase beta chain (Glycine--tRNA ligase beta chain) (GlyRS); COG0751. | COG0752; glycine--tRNA ligase alpha chain; GlyRS. | 0.999 |
| glyS | ileS | bbp_126 | bbp_139 | glycyl-tRNA synthetase beta chain (Glycine--tRNA ligase beta chain) (GlyRS); COG0751. | 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 1 subfamily. | 0.712 |