node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
argS | ileS | DR97_2406 | DR97_1864 | Arginyl-trna synthetase; argS: arginine--tRNA ligase | 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) | 0.997 |
argS | leuS | DR97_2406 | DR97_3878 | Arginyl-trna synthetase; argS: arginine--tRNA ligase | Leucyl-trna synthetase; Belongs to the class-I aminoacyl-tRNA synthetase family | 0.992 |
argS | lysS | DR97_2406 | DR97_4177 | Arginyl-trna synthetase; argS: arginine--tRNA ligase | Lysyl-trna synthetase, class ii; Belongs to the class-II aminoacyl-tRNA synthetase family | 0.994 |
argS | metG | DR97_2406 | DR97_4439 | Arginyl-trna synthetase; argS: arginine--tRNA ligase | 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 | 0.996 |
argS | pheS | DR97_2406 | DR97_5222 | Arginyl-trna synthetase; argS: arginine--tRNA ligase | Phenylalanyl-trna synthetase subunit alpha; Belongs to the class-II aminoacyl-tRNA synthetase family. Phe-tRNA synthetase alpha subunit type 1 subfamily | 0.732 |
argS | pheT | DR97_2406 | DR97_5223 | Arginyl-trna synthetase; argS: arginine--tRNA ligase | Belongs to the phenylalanyl-tRNA synthetase beta subunit family. Type 1 subfamily | 0.956 |
argS | proS | DR97_2406 | DR97_981 | Arginyl-trna synthetase; argS: arginine--tRNA ligase | Prolyl-trna synthetase; 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 dea [...] | 0.994 |
argS | valS | DR97_2406 | DR97_4032 | Arginyl-trna synthetase; argS: arginine--tRNA ligase | 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 | 0.921 |
fmt | leuS | DR97_2971 | DR97_3878 | Methionyl-trna formyltransferase; Attaches a formyl group to the free amino group of methionyl- tRNA(fMet). The formyl group appears to play a dual role in the initiator identity of N-formylmethionyl-tRNA by promoting its recognition by IF2 and preventing the misappropriation of this tRNA by the elongation apparatus | Leucyl-trna synthetase; Belongs to the class-I aminoacyl-tRNA synthetase family | 0.459 |
fmt | metG | DR97_2971 | DR97_4439 | Methionyl-trna formyltransferase; Attaches a formyl group to the free amino group of methionyl- tRNA(fMet). The formyl group appears to play a dual role in the initiator identity of N-formylmethionyl-tRNA by promoting its recognition by IF2 and preventing the misappropriation of this tRNA by the elongation apparatus | 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 | 0.980 |
fmt | metH | DR97_2971 | DR97_34 | Methionyl-trna formyltransferase; Attaches a formyl group to the free amino group of methionyl- tRNA(fMet). The formyl group appears to play a dual role in the initiator identity of N-formylmethionyl-tRNA by promoting its recognition by IF2 and preventing the misappropriation of this tRNA by the elongation apparatus | 5-methyltetrahydrofolate--homocysteine methyltransferase; Catalyzes the transfer of a methyl group from methyl- cobalamin to homocysteine, yielding enzyme-bound cob(I)alamin and methionine. Subsequently, remethylates the cofactor using methyltetrahydrofolate (By similarity) | 0.917 |
fmt | pheS | DR97_2971 | DR97_5222 | Methionyl-trna formyltransferase; Attaches a formyl group to the free amino group of methionyl- tRNA(fMet). The formyl group appears to play a dual role in the initiator identity of N-formylmethionyl-tRNA by promoting its recognition by IF2 and preventing the misappropriation of this tRNA by the elongation apparatus | Phenylalanyl-trna synthetase subunit alpha; Belongs to the class-II aminoacyl-tRNA synthetase family. Phe-tRNA synthetase alpha subunit type 1 subfamily | 0.721 |
fmt | pheT | DR97_2971 | DR97_5223 | Methionyl-trna formyltransferase; Attaches a formyl group to the free amino group of methionyl- tRNA(fMet). The formyl group appears to play a dual role in the initiator identity of N-formylmethionyl-tRNA by promoting its recognition by IF2 and preventing the misappropriation of this tRNA by the elongation apparatus | Belongs to the phenylalanyl-tRNA synthetase beta subunit family. Type 1 subfamily | 0.861 |
ileS | argS | DR97_1864 | DR97_2406 | 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) | Arginyl-trna synthetase; argS: arginine--tRNA ligase | 0.997 |
ileS | leuS | DR97_1864 | DR97_3878 | 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) | Leucyl-trna synthetase; Belongs to the class-I aminoacyl-tRNA synthetase family | 0.997 |
ileS | lysS | DR97_1864 | DR97_4177 | 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) | Lysyl-trna synthetase, class ii; Belongs to the class-II aminoacyl-tRNA synthetase family | 0.985 |
ileS | metG | DR97_1864 | DR97_4439 | 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) | 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 | 0.989 |
ileS | pheS | DR97_1864 | DR97_5222 | 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) | Phenylalanyl-trna synthetase subunit alpha; Belongs to the class-II aminoacyl-tRNA synthetase family. Phe-tRNA synthetase alpha subunit type 1 subfamily | 0.889 |
ileS | pheT | DR97_1864 | DR97_5223 | 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 phenylalanyl-tRNA synthetase beta subunit family. Type 1 subfamily | 0.967 |
ileS | proS | DR97_1864 | DR97_981 | 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) | Prolyl-trna synthetase; 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 dea [...] | 0.993 |