node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
RPA4754 | argS | RPA4754 | RPA2854 | Possible glutamyl-tRNA synthetase; Belongs to the class-I aminoacyl-tRNA synthetase family. | arginyl-tRNA synthetase; Observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished. | 0.869 |
RPA4754 | hisS | RPA4754 | RPA1178 | Possible glutamyl-tRNA synthetase; Belongs to the class-I aminoacyl-tRNA synthetase family. | Putative histidyl-tRNA synthetase; Observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished. | 0.420 |
RPA4754 | ileS | RPA4754 | RPA4377 | Possible glutamyl-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). | 0.933 |
RPA4754 | leuS | RPA4754 | RPA0287 | Possible glutamyl-tRNA synthetase; Belongs to the class-I aminoacyl-tRNA synthetase family. | leucyl-tRNA synthetase; Observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished; Belongs to the class-I aminoacyl-tRNA synthetase family. | 0.902 |
RPA4754 | metG | RPA4754 | RPA2777 | Possible glutamyl-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; Belongs to the class-I aminoacyl-tRNA synthetase family. MetG type 2B subfamily. | 0.936 |
RPA4754 | proS | RPA4754 | RPA2928 | Possible glutamyl-tRNA synthetase; Belongs to the class-I aminoacyl-tRNA synthetase family. | 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). Can inadvertently accommodate and process cysteine. The misacylated Cys-tRNA(Pro) is not edited by ProRS. | 0.884 |
RPA4754 | thrS | RPA4754 | RPA3406 | Possible glutamyl-tRNA synthetase; Belongs to the class-I 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). | 0.458 |
RPA4754 | valS | RPA4754 | RPA2583 | Possible glutamyl-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 1 subfamily. | 0.487 |
argS | RPA4754 | RPA2854 | RPA4754 | arginyl-tRNA synthetase; Observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished. | Possible glutamyl-tRNA synthetase; Belongs to the class-I aminoacyl-tRNA synthetase family. | 0.869 |
argS | glnS | RPA2854 | RPA2905 | arginyl-tRNA synthetase; Observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished. | glutaminyl-tRNA synthetase; Observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished. | 0.886 |
argS | gltX | RPA2854 | RPA2906 | arginyl-tRNA synthetase; Observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished. | glutamyl-tRNA 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); Belongs to the class-I aminoacyl-tRNA synthetase family. Glutamate--tRNA ligase type 1 subfamily. | 0.912 |
argS | hisS | RPA2854 | RPA1178 | arginyl-tRNA synthetase; Observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished. | Putative histidyl-tRNA synthetase; Observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished. | 0.583 |
argS | ileS | RPA2854 | RPA4377 | arginyl-tRNA synthetase; Observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished. | 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). | 0.978 |
argS | leuS | RPA2854 | RPA0287 | arginyl-tRNA synthetase; Observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished. | leucyl-tRNA synthetase; Observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished; Belongs to the class-I aminoacyl-tRNA synthetase family. | 0.909 |
argS | metG | RPA2854 | RPA2777 | arginyl-tRNA synthetase; Observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished. | 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; Belongs to the class-I aminoacyl-tRNA synthetase family. MetG type 2B subfamily. | 0.964 |
argS | proS | RPA2854 | RPA2928 | arginyl-tRNA synthetase; Observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished. | 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). Can inadvertently accommodate and process cysteine. The misacylated Cys-tRNA(Pro) is not edited by ProRS. | 0.968 |
argS | thrS | RPA2854 | RPA3406 | arginyl-tRNA synthetase; Observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished. | 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). | 0.697 |
argS | valS | RPA2854 | RPA2583 | arginyl-tRNA synthetase; Observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished. | 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. | 0.768 |
glnS | argS | RPA2905 | RPA2854 | glutaminyl-tRNA synthetase; Observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished. | arginyl-tRNA synthetase; Observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished. | 0.886 |
glnS | gltX | RPA2905 | RPA2906 | glutaminyl-tRNA synthetase; Observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished. | glutamyl-tRNA 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); Belongs to the class-I aminoacyl-tRNA synthetase family. Glutamate--tRNA ligase type 1 subfamily. | 0.753 |