node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
argS | earS | NS506_07216 | NS506_00890 | Arginine--tRNA ligase; Belongs to the class-I aminoacyl-tRNA synthetase family; KEGG: mej:Q7A_290 arginyl-tRNA synthetase. | Glutamate--tRNA ligase; Catalyzes the tRNA-independent activation of glutamate in presence of ATP and the subsequent transfer of glutamate onto a tRNA(Asp). Glutamate is transferred on the 2-amino-5-(4,5-dihydroxy-2- cyclopenten-1-yl) moiety of the queuosine in the wobble position of the QUC anticodon; Belongs to the class-I aminoacyl-tRNA synthetase family. GluQ subfamily. | 0.913 |
argS | gltX | NS506_07216 | NS506_06560 | Arginine--tRNA ligase; Belongs to the class-I aminoacyl-tRNA synthetase family; KEGG: mej:Q7A_290 arginyl-tRNA synthetase. | Glutamate--tRNA ligase; 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); Belongs to the class-I aminoacyl-tRNA synthetase family. Glutamate--tRNA ligase type 1 subfamily. | 0.963 |
argS | guaA-2 | NS506_07216 | NS506_07432 | Arginine--tRNA ligase; Belongs to the class-I aminoacyl-tRNA synthetase family; KEGG: mej:Q7A_290 arginyl-tRNA synthetase. | GMP synthase (glutamine-hydrolyzing); Catalyzes the synthesis of GMP from XMP. | 0.938 |
argS | iarS | NS506_07216 | NS506_03364 | Arginine--tRNA ligase; Belongs to the class-I aminoacyl-tRNA synthetase family; KEGG: mej:Q7A_290 arginyl-tRNA synthetase. | Isoleucine--tRNA ligase; 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. | 0.978 |
argS | larS | NS506_07216 | NS506_00989 | Arginine--tRNA ligase; Belongs to the class-I aminoacyl-tRNA synthetase family; KEGG: mej:Q7A_290 arginyl-tRNA synthetase. | Leucine--tRNA ligase; Belongs to the class-I aminoacyl-tRNA synthetase family; KEGG: ncy:NOCYR_5410 leucyl-tRNA synthetase. | 0.950 |
argS | metG | NS506_07216 | NS506_01618 | Arginine--tRNA ligase; Belongs to the class-I aminoacyl-tRNA synthetase family; KEGG: mej:Q7A_290 arginyl-tRNA synthetase. | Leucine--tRNA ligase; Is required not only for elongation of protein synthesis but also for the initiation of all mRNA translation through initiator tRNA(fMet) aminoacylation; Belongs to the class-I aminoacyl-tRNA synthetase family. MetG type 2B subfamily. | 0.958 |
argS | parS | NS506_07216 | NS506_06313 | Arginine--tRNA ligase; Belongs to the class-I aminoacyl-tRNA synthetase family; KEGG: mej:Q7A_290 arginyl-tRNA synthetase. | Proline--tRNA ligase; 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 involves deacy [...] | 0.960 |
argS | pheT | NS506_07216 | NS506_03626 | Arginine--tRNA ligase; Belongs to the class-I aminoacyl-tRNA synthetase family; KEGG: mej:Q7A_290 arginyl-tRNA synthetase. | Phenylalanine--tRNA ligase; Belongs to the phenylalanyl-tRNA synthetase beta subunit family. Type 1 subfamily; Contains 1 B5 domain; Contains 1 FDX-ACB domain; Contains 1 tRNA-binding domain; KEGG: asd:AS9A_1504 phenylalanyl-tRNA synthetase beta chain. | 0.942 |
argS | rarS | NS506_07216 | NS506_04811 | Arginine--tRNA ligase; Belongs to the class-I aminoacyl-tRNA synthetase family; KEGG: mej:Q7A_290 arginyl-tRNA synthetase. | Arginine--tRNA ligase; Forms part of a macromolecular complex that catalyzes the attachment of specific amino acids to cognate tRNAs during protein synthesis; Belongs to the class-I aminoacyl-tRNA synthetase family; KEGG: eco:b1876 arginyl-tRNA synthetase. | 0.909 |
argS | varS | NS506_07216 | NS506_06864 | Arginine--tRNA ligase; Belongs to the class-I aminoacyl-tRNA synthetase family; KEGG: mej:Q7A_290 arginyl-tRNA synthetase. | Valine--tRNA ligase; 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. | 0.911 |
earS | argS | NS506_00890 | NS506_07216 | Glutamate--tRNA ligase; Catalyzes the tRNA-independent activation of glutamate in presence of ATP and the subsequent transfer of glutamate onto a tRNA(Asp). Glutamate is transferred on the 2-amino-5-(4,5-dihydroxy-2- cyclopenten-1-yl) moiety of the queuosine in the wobble position of the QUC anticodon; Belongs to the class-I aminoacyl-tRNA synthetase family. GluQ subfamily. | Arginine--tRNA ligase; Belongs to the class-I aminoacyl-tRNA synthetase family; KEGG: mej:Q7A_290 arginyl-tRNA synthetase. | 0.913 |
earS | gltX | NS506_00890 | NS506_06560 | Glutamate--tRNA ligase; Catalyzes the tRNA-independent activation of glutamate in presence of ATP and the subsequent transfer of glutamate onto a tRNA(Asp). Glutamate is transferred on the 2-amino-5-(4,5-dihydroxy-2- cyclopenten-1-yl) moiety of the queuosine in the wobble position of the QUC anticodon; Belongs to the class-I aminoacyl-tRNA synthetase family. GluQ subfamily. | Glutamate--tRNA ligase; 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); Belongs to the class-I aminoacyl-tRNA synthetase family. Glutamate--tRNA ligase type 1 subfamily. | 0.914 |
earS | guaA-2 | NS506_00890 | NS506_07432 | Glutamate--tRNA ligase; Catalyzes the tRNA-independent activation of glutamate in presence of ATP and the subsequent transfer of glutamate onto a tRNA(Asp). Glutamate is transferred on the 2-amino-5-(4,5-dihydroxy-2- cyclopenten-1-yl) moiety of the queuosine in the wobble position of the QUC anticodon; Belongs to the class-I aminoacyl-tRNA synthetase family. GluQ subfamily. | GMP synthase (glutamine-hydrolyzing); Catalyzes the synthesis of GMP from XMP. | 0.741 |
earS | iarS | NS506_00890 | NS506_03364 | Glutamate--tRNA ligase; Catalyzes the tRNA-independent activation of glutamate in presence of ATP and the subsequent transfer of glutamate onto a tRNA(Asp). Glutamate is transferred on the 2-amino-5-(4,5-dihydroxy-2- cyclopenten-1-yl) moiety of the queuosine in the wobble position of the QUC anticodon; Belongs to the class-I aminoacyl-tRNA synthetase family. GluQ subfamily. | Isoleucine--tRNA ligase; 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. | 0.934 |
earS | larS | NS506_00890 | NS506_00989 | Glutamate--tRNA ligase; Catalyzes the tRNA-independent activation of glutamate in presence of ATP and the subsequent transfer of glutamate onto a tRNA(Asp). Glutamate is transferred on the 2-amino-5-(4,5-dihydroxy-2- cyclopenten-1-yl) moiety of the queuosine in the wobble position of the QUC anticodon; Belongs to the class-I aminoacyl-tRNA synthetase family. GluQ subfamily. | Leucine--tRNA ligase; Belongs to the class-I aminoacyl-tRNA synthetase family; KEGG: ncy:NOCYR_5410 leucyl-tRNA synthetase. | 0.912 |
earS | metG | NS506_00890 | NS506_01618 | Glutamate--tRNA ligase; Catalyzes the tRNA-independent activation of glutamate in presence of ATP and the subsequent transfer of glutamate onto a tRNA(Asp). Glutamate is transferred on the 2-amino-5-(4,5-dihydroxy-2- cyclopenten-1-yl) moiety of the queuosine in the wobble position of the QUC anticodon; Belongs to the class-I aminoacyl-tRNA synthetase family. GluQ subfamily. | Leucine--tRNA ligase; Is required not only for elongation of protein synthesis but also for the initiation of all mRNA translation through initiator tRNA(fMet) aminoacylation; Belongs to the class-I aminoacyl-tRNA synthetase family. MetG type 2B subfamily. | 0.940 |
earS | parS | NS506_00890 | NS506_06313 | Glutamate--tRNA ligase; Catalyzes the tRNA-independent activation of glutamate in presence of ATP and the subsequent transfer of glutamate onto a tRNA(Asp). Glutamate is transferred on the 2-amino-5-(4,5-dihydroxy-2- cyclopenten-1-yl) moiety of the queuosine in the wobble position of the QUC anticodon; Belongs to the class-I aminoacyl-tRNA synthetase family. GluQ subfamily. | Proline--tRNA ligase; 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 involves deacy [...] | 0.918 |
earS | pheT | NS506_00890 | NS506_03626 | Glutamate--tRNA ligase; Catalyzes the tRNA-independent activation of glutamate in presence of ATP and the subsequent transfer of glutamate onto a tRNA(Asp). Glutamate is transferred on the 2-amino-5-(4,5-dihydroxy-2- cyclopenten-1-yl) moiety of the queuosine in the wobble position of the QUC anticodon; Belongs to the class-I aminoacyl-tRNA synthetase family. GluQ subfamily. | Phenylalanine--tRNA ligase; Belongs to the phenylalanyl-tRNA synthetase beta subunit family. Type 1 subfamily; Contains 1 B5 domain; Contains 1 FDX-ACB domain; Contains 1 tRNA-binding domain; KEGG: asd:AS9A_1504 phenylalanyl-tRNA synthetase beta chain. | 0.864 |
earS | varS | NS506_00890 | NS506_06864 | Glutamate--tRNA ligase; Catalyzes the tRNA-independent activation of glutamate in presence of ATP and the subsequent transfer of glutamate onto a tRNA(Asp). Glutamate is transferred on the 2-amino-5-(4,5-dihydroxy-2- cyclopenten-1-yl) moiety of the queuosine in the wobble position of the QUC anticodon; Belongs to the class-I aminoacyl-tRNA synthetase family. GluQ subfamily. | Valine--tRNA ligase; 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. | 0.590 |
gltX | argS | NS506_06560 | NS506_07216 | Glutamate--tRNA ligase; 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); Belongs to the class-I aminoacyl-tRNA synthetase family. Glutamate--tRNA ligase type 1 subfamily. | Arginine--tRNA ligase; Belongs to the class-I aminoacyl-tRNA synthetase family; KEGG: mej:Q7A_290 arginyl-tRNA synthetase. | 0.963 |