| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| alaS | argS | TP_1017 | TP_0831 | alanyl-tRNA synthetase (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 (By similarity). | arginyl-tRNA synthetase (argS); Similar to GB:AE000783 percent identity: 43.07; identified by sequence similarity; putative. | 0.635 |
| alaS | aspS | TP_1017 | TP_0985 | alanyl-tRNA synthetase (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 (By similarity). | aspartyl-tRNA synthetase (aspS); Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn); Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily. | 0.912 |
| alaS | cmk | TP_1017 | TP_0279 | alanyl-tRNA synthetase (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 (By similarity). | Ribosomal protein S1 (rpsA); Similar to SP:P02349 GB:V00342 GB:V00352 GB:X04864 PID:42837 percent identity: 36.77; identified by sequence similarity; putative. | 0.591 |
| alaS | ileS | TP_1017 | TP_0452 | alanyl-tRNA synthetase (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 (By similarity). | isoleucyl-tRNA synthetase (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. | 0.926 |
| alaS | leuS | TP_1017 | TP_0586 | alanyl-tRNA synthetase (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 (By similarity). | leucyl-tRNA synthetase (leuS); Similar to GB:AE000783 percent identity: 50.60; identified by sequence similarity; putative; Belongs to the class-I aminoacyl-tRNA synthetase family. | 0.949 |
| alaS | proS | TP_1017 | TP_0160 | alanyl-tRNA synthetase (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 (By similarity). | prolyl-tRNA synthetase (proS); 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). As ProRS can inadvertently accommodate and process non-cognate amino acids such as alanine and cysteine, to avoid such errors it has two additional distinct editing activities against alanine. One activity is designated as 'pretransfer' editing and involves the tRNA(Pro)-independent hydrolysis of activated Ala-AMP. The other activity is designated 'posttransfer' editing and invol [...] | 0.754 |
| alaS | rpoB | TP_1017 | TP_0241 | alanyl-tRNA synthetase (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 (By similarity). | DNA-directed RNA polymerase, beta subunit (rpoB); DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. | 0.591 |
| alaS | serS | TP_1017 | TP_0647 | alanyl-tRNA synthetase (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 (By similarity). | seryl-tRNA synthetase (serS); Catalyzes the attachment of serine to tRNA(Ser). Is also able to aminoacylate tRNA(Sec) with serine, to form the misacylated tRNA L- seryl-tRNA(Sec), which will be further converted into selenocysteinyl- tRNA(Sec). | 0.616 |
| alaS | thrS | TP_1017 | TP_0837 | alanyl-tRNA synthetase (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 (By similarity). | threonyl-tRNA synthetase (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). | 0.871 |
| alaS | valS | TP_1017 | TP_1035 | alanyl-tRNA synthetase (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 (By similarity). | valyl-tRNA synthetase (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 1 subfamily. | 0.923 |
| argS | alaS | TP_0831 | TP_1017 | arginyl-tRNA synthetase (argS); Similar to GB:AE000783 percent identity: 43.07; identified by sequence similarity; putative. | alanyl-tRNA synthetase (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 (By similarity). | 0.635 |
| argS | aspS | TP_0831 | TP_0985 | arginyl-tRNA synthetase (argS); Similar to GB:AE000783 percent identity: 43.07; identified by sequence similarity; putative. | aspartyl-tRNA synthetase (aspS); Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn); Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily. | 0.793 |
| argS | cmk | TP_0831 | TP_0279 | arginyl-tRNA synthetase (argS); Similar to GB:AE000783 percent identity: 43.07; identified by sequence similarity; putative. | Ribosomal protein S1 (rpsA); Similar to SP:P02349 GB:V00342 GB:V00352 GB:X04864 PID:42837 percent identity: 36.77; identified by sequence similarity; putative. | 0.795 |
| argS | ileS | TP_0831 | TP_0452 | arginyl-tRNA synthetase (argS); Similar to GB:AE000783 percent identity: 43.07; identified by sequence similarity; putative. | isoleucyl-tRNA synthetase (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. | 0.996 |
| argS | leuS | TP_0831 | TP_0586 | arginyl-tRNA synthetase (argS); Similar to GB:AE000783 percent identity: 43.07; identified by sequence similarity; putative. | leucyl-tRNA synthetase (leuS); Similar to GB:AE000783 percent identity: 50.60; identified by sequence similarity; putative; Belongs to the class-I aminoacyl-tRNA synthetase family. | 0.985 |
| argS | proS | TP_0831 | TP_0160 | arginyl-tRNA synthetase (argS); Similar to GB:AE000783 percent identity: 43.07; identified by sequence similarity; putative. | prolyl-tRNA synthetase (proS); 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). As ProRS can inadvertently accommodate and process non-cognate amino acids such as alanine and cysteine, to avoid such errors it has two additional distinct editing activities against alanine. One activity is designated as 'pretransfer' editing and involves the tRNA(Pro)-independent hydrolysis of activated Ala-AMP. The other activity is designated 'posttransfer' editing and invol [...] | 0.997 |
| argS | rpoB | TP_0831 | TP_0241 | arginyl-tRNA synthetase (argS); Similar to GB:AE000783 percent identity: 43.07; identified by sequence similarity; putative. | DNA-directed RNA polymerase, beta subunit (rpoB); DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. | 0.831 |
| argS | serS | TP_0831 | TP_0647 | arginyl-tRNA synthetase (argS); Similar to GB:AE000783 percent identity: 43.07; identified by sequence similarity; putative. | seryl-tRNA synthetase (serS); Catalyzes the attachment of serine to tRNA(Ser). Is also able to aminoacylate tRNA(Sec) with serine, to form the misacylated tRNA L- seryl-tRNA(Sec), which will be further converted into selenocysteinyl- tRNA(Sec). | 0.846 |
| argS | thrS | TP_0831 | TP_0837 | arginyl-tRNA synthetase (argS); Similar to GB:AE000783 percent identity: 43.07; identified by sequence similarity; putative. | threonyl-tRNA synthetase (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). | 0.817 |
| argS | valS | TP_0831 | TP_1035 | arginyl-tRNA synthetase (argS); Similar to GB:AE000783 percent identity: 43.07; identified by sequence similarity; putative. | valyl-tRNA synthetase (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 1 subfamily. | 0.900 |