| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| argS | aspS | MSMAS_3315 | MSMAS_1255 | Arginyl-tRNA synthetase; Belongs to the class-I aminoacyl-tRNA synthetase family. | Aspartyl-tRNA synthetase / Aspartyl-tRNA(Asn) synthetase; 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). | 0.917 |
| argS | gltX | MSMAS_3315 | MSMAS_2930 | Arginyl-tRNA synthetase; Belongs to the class-I aminoacyl-tRNA synthetase family. | Glutamyl-tRNA synthetase / Glutamyl-tRNA(Gln) 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). | 0.942 |
| argS | ileS | MSMAS_3315 | MSMAS_1715 | Arginyl-tRNA synthetase; Belongs to the class-I 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 2 subfamily. | 0.976 |
| argS | leuS | MSMAS_3315 | MSMAS_1017 | Arginyl-tRNA synthetase; Belongs to the class-I aminoacyl-tRNA synthetase family. | Leucyl-tRNA synthetase; Belongs to the class-I aminoacyl-tRNA synthetase family. | 0.981 |
| argS | lysS | MSMAS_3315 | MSMAS_2768 | Arginyl-tRNA synthetase; Belongs to the class-I aminoacyl-tRNA synthetase family. | Lysyl-tRNA synthetase (class II); Belongs to the class-II aminoacyl-tRNA synthetase family. | 0.949 |
| argS | metG | MSMAS_3315 | MSMAS_0438 | Arginyl-tRNA synthetase; Belongs to the class-I 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. | 0.953 |
| argS | pheT | MSMAS_3315 | MSMAS_1915 | Arginyl-tRNA synthetase; Belongs to the class-I aminoacyl-tRNA synthetase family. | Phenylalanyl-tRNA synthetase beta chain. | 0.818 |
| argS | proS | MSMAS_3315 | MSMAS_0606 | Arginyl-tRNA synthetase; Belongs to the class-I aminoacyl-tRNA synthetase family. | Prolyl-tRNA synthetase, archaeal/eukaryal 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). | 0.907 |
| argS | rpl2 | MSMAS_3315 | MSMAS_2557 | Arginyl-tRNA synthetase; Belongs to the class-I aminoacyl-tRNA synthetase family. | LSU ribosomal protein L8e (L2p); One of the primary rRNA binding proteins. Required for association of the 30S and 50S subunits to form the 70S ribosome, for tRNA binding and peptide bond formation. It has been suggested to have peptidyltransferase activity; this is somewhat controversial. Makes several contacts with the 16S rRNA in the 70S ribosome. Belongs to the universal ribosomal protein uL2 family. | 0.848 |
| argS | valS | MSMAS_3315 | MSMAS_0986 | Arginyl-tRNA synthetase; Belongs to the class-I 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 2 subfamily. | 0.849 |
| aspS | argS | MSMAS_1255 | MSMAS_3315 | Aspartyl-tRNA synthetase / Aspartyl-tRNA(Asn) synthetase; 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). | Arginyl-tRNA synthetase; Belongs to the class-I aminoacyl-tRNA synthetase family. | 0.917 |
| aspS | gltX | MSMAS_1255 | MSMAS_2930 | Aspartyl-tRNA synthetase / Aspartyl-tRNA(Asn) synthetase; 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). | Glutamyl-tRNA synthetase / Glutamyl-tRNA(Gln) 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). | 0.908 |
| aspS | ileS | MSMAS_1255 | MSMAS_1715 | Aspartyl-tRNA synthetase / Aspartyl-tRNA(Asn) synthetase; 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). | 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. | 0.920 |
| aspS | leuS | MSMAS_1255 | MSMAS_1017 | Aspartyl-tRNA synthetase / Aspartyl-tRNA(Asn) synthetase; 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). | Leucyl-tRNA synthetase; Belongs to the class-I aminoacyl-tRNA synthetase family. | 0.940 |
| aspS | lysS | MSMAS_1255 | MSMAS_2768 | Aspartyl-tRNA synthetase / Aspartyl-tRNA(Asn) synthetase; 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). | Lysyl-tRNA synthetase (class II); Belongs to the class-II aminoacyl-tRNA synthetase family. | 0.865 |
| aspS | metG | MSMAS_1255 | MSMAS_0438 | Aspartyl-tRNA synthetase / Aspartyl-tRNA(Asn) synthetase; 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). | 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. | 0.945 |
| aspS | pheT | MSMAS_1255 | MSMAS_1915 | Aspartyl-tRNA synthetase / Aspartyl-tRNA(Asn) synthetase; 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). | Phenylalanyl-tRNA synthetase beta chain. | 0.551 |
| aspS | proS | MSMAS_1255 | MSMAS_0606 | Aspartyl-tRNA synthetase / Aspartyl-tRNA(Asn) synthetase; 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). | Prolyl-tRNA synthetase, archaeal/eukaryal 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). | 0.959 |
| aspS | rpl2 | MSMAS_1255 | MSMAS_2557 | Aspartyl-tRNA synthetase / Aspartyl-tRNA(Asn) synthetase; 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). | LSU ribosomal protein L8e (L2p); One of the primary rRNA binding proteins. Required for association of the 30S and 50S subunits to form the 70S ribosome, for tRNA binding and peptide bond formation. It has been suggested to have peptidyltransferase activity; this is somewhat controversial. Makes several contacts with the 16S rRNA in the 70S ribosome. Belongs to the universal ribosomal protein uL2 family. | 0.887 |
| aspS | valS | MSMAS_1255 | MSMAS_0986 | Aspartyl-tRNA synthetase / Aspartyl-tRNA(Asn) synthetase; 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). | 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 2 subfamily. | 0.751 |