| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| alaS | argS | BF49_5887 | BF49_6785 | AlanyltRNA synthetase EC 6117; 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. | ArginyltRNA synthetase EC 61119. | 0.582 |
| alaS | guaA | BF49_5887 | BF49_1068 | AlanyltRNA synthetase EC 6117; 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 synthase glutaminehydrolyzing EC 6352; Catalyzes the synthesis of GMP from XMP. | 0.793 |
| alaS | ileS | BF49_5887 | BF49_3020 | AlanyltRNA synthetase EC 6117; 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. | IsoleucyltRNA synthetase EC 6115; 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). | 0.890 |
| alaS | leuS | BF49_5887 | BF49_0220 | AlanyltRNA synthetase EC 6117; 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. | LeucyltRNA synthetase EC 6114; Belongs to the class-I aminoacyl-tRNA synthetase family. | 0.925 |
| alaS | pheS | BF49_5887 | BF49_0136 | AlanyltRNA synthetase EC 6117; 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. | PhenylalanyltRNA synthetase alpha chain EC 61120; Belongs to the class-II aminoacyl-tRNA synthetase family. Phe-tRNA synthetase alpha subunit type 1 subfamily. | 0.670 |
| alaS | pheT | BF49_5887 | BF49_0138 | AlanyltRNA synthetase EC 6117; 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. | PhenylalanyltRNA synthetase beta chain EC 61120; Belongs to the phenylalanyl-tRNA synthetase beta subunit family. Type 1 subfamily. | 0.936 |
| alaS | proS | BF49_5887 | BF49_6688 | AlanyltRNA synthetase EC 6117; 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. | ProlyltRNA synthetase EC 61115 bacterial type; Catalyzes the attachment of proline to tRNA(Pro) in a two- step reaction: proline is first activated by ATP to form Pro-AMP and then transferred to the acceptor end of tRNA(Pro); Belongs to the class-II aminoacyl-tRNA synthetase family. ProS type 2 subfamily. | 0.694 |
| alaS | rpoB | BF49_5887 | BF49_6219 | AlanyltRNA synthetase EC 6117; 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. | DNAdirected RNA polymerase beta subunit EC 2776; DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. | 0.725 |
| alaS | thrS | BF49_5887 | BF49_6108 | AlanyltRNA synthetase EC 6117; 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. | ThreonyltRNA synthetase EC 6113; Belongs to the class-II aminoacyl-tRNA synthetase family. | 0.899 |
| alaS | tyrS | BF49_5887 | BF49_0729 | AlanyltRNA synthetase EC 6117; 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. | TyrosyltRNA synthetase EC 6111; Catalyzes the attachment of tyrosine to tRNA(Tyr) in a two- step reaction: tyrosine is first activated by ATP to form Tyr-AMP and then transferred to the acceptor end of tRNA(Tyr); Belongs to the class-I aminoacyl-tRNA synthetase family. TyrS type 1 subfamily. | 0.664 |
| argS | alaS | BF49_6785 | BF49_5887 | ArginyltRNA synthetase EC 61119. | AlanyltRNA synthetase EC 6117; 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. | 0.582 |
| argS | guaA | BF49_6785 | BF49_1068 | ArginyltRNA synthetase EC 61119. | GMP synthase glutaminehydrolyzing EC 6352; Catalyzes the synthesis of GMP from XMP. | 0.922 |
| argS | ileS | BF49_6785 | BF49_3020 | ArginyltRNA synthetase EC 61119. | IsoleucyltRNA synthetase EC 6115; 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). | 0.974 |
| argS | leuS | BF49_6785 | BF49_0220 | ArginyltRNA synthetase EC 61119. | LeucyltRNA synthetase EC 6114; Belongs to the class-I aminoacyl-tRNA synthetase family. | 0.948 |
| argS | pheS | BF49_6785 | BF49_0136 | ArginyltRNA synthetase EC 61119. | PhenylalanyltRNA synthetase alpha chain EC 61120; Belongs to the class-II aminoacyl-tRNA synthetase family. Phe-tRNA synthetase alpha subunit type 1 subfamily. | 0.656 |
| argS | pheT | BF49_6785 | BF49_0138 | ArginyltRNA synthetase EC 61119. | PhenylalanyltRNA synthetase beta chain EC 61120; Belongs to the phenylalanyl-tRNA synthetase beta subunit family. Type 1 subfamily. | 0.912 |
| argS | proS | BF49_6785 | BF49_6688 | ArginyltRNA synthetase EC 61119. | ProlyltRNA synthetase EC 61115 bacterial type; Catalyzes the attachment of proline to tRNA(Pro) in a two- step reaction: proline is first activated by ATP to form Pro-AMP and then transferred to the acceptor end of tRNA(Pro); Belongs to the class-II aminoacyl-tRNA synthetase family. ProS type 2 subfamily. | 0.981 |
| argS | rpoB | BF49_6785 | BF49_6219 | ArginyltRNA synthetase EC 61119. | DNAdirected RNA polymerase beta subunit EC 2776; DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. | 0.736 |
| argS | thrS | BF49_6785 | BF49_6108 | ArginyltRNA synthetase EC 61119. | ThreonyltRNA synthetase EC 6113; Belongs to the class-II aminoacyl-tRNA synthetase family. | 0.792 |
| argS | tyrS | BF49_6785 | BF49_0729 | ArginyltRNA synthetase EC 61119. | TyrosyltRNA synthetase EC 6111; Catalyzes the attachment of tyrosine to tRNA(Tyr) in a two- step reaction: tyrosine is first activated by ATP to form Tyr-AMP and then transferred to the acceptor end of tRNA(Tyr); Belongs to the class-I aminoacyl-tRNA synthetase family. TyrS type 1 subfamily. | 0.870 |