node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
argS | cysS | b1876 | b0526 | Arginine--tRNA ligase; Arginine tRNA synthetase; Protein involved in tRNA aminoacylation for protein translation | Cysteinyl-trna synthetase; Belongs to the class-I aminoacyl-tRNA synthetase family | 0.926 |
argS | gltX | b1876 | b2400 | Arginine--tRNA ligase; Arginine tRNA synthetase; Protein involved in tRNA aminoacylation for protein translation | 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) | 0.849 |
argS | hisS | b1876 | b2514 | Arginine--tRNA ligase; Arginine tRNA synthetase; Protein involved in tRNA aminoacylation for protein translation | Histidine--tRNA ligase; Histidine tRNA synthetase; Protein involved in tRNA aminoacylation for protein translation | 0.808 |
argS | ileS | b1876 | b0026 | Arginine--tRNA ligase; Arginine tRNA synthetase; Protein involved in tRNA aminoacylation for protein translation | 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) | 0.989 |
argS | leuS | b1876 | b0642 | Arginine--tRNA ligase; Arginine tRNA synthetase; Protein involved in tRNA aminoacylation for protein translation | Leucyl-trna synthetase; Belongs to the class-I aminoacyl-tRNA synthetase family | 0.984 |
argS | metG | b1876 | b2114 | Arginine--tRNA ligase; Arginine tRNA synthetase; Protein involved in tRNA aminoacylation for protein translation | 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 | 0.983 |
argS | serS | b1876 | b0893 | Arginine--tRNA ligase; Arginine tRNA synthetase; Protein involved in tRNA aminoacylation for protein translation | Seryl-trna synthetase; 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) | 0.883 |
argS | thrS | b1876 | b1719 | Arginine--tRNA ligase; Arginine tRNA synthetase; Protein involved in tRNA aminoacylation for protein translation | 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) The rate-limiting step is amino acid activation in the presence of tRNA . The 2'-OH of the acceptor base (adenine 76, A76) of tRNA(Thr) and His-309 collaborate to transfer L-Thr to the tRNA; substitution of 2'-OH of A76 with hydrogen or fluorine decreases transfer efficiency 760 and 100-fold respectively . The zinc ion in the active site discriminates against charging of the isos [...] | 0.863 |
argS | tyrS | b1876 | b1637 | Arginine--tRNA ligase; Arginine tRNA synthetase; Protein involved in tRNA aminoacylation for protein translation | Tyrosyl-trna synthetase; Catalyzes the attachment of L-tyrosine to tRNA(Tyr) in a two- step reaction: tyrosine is first activated by ATP to form Tyr-AMP and then transferred to the acceptor end of tRNA(Tyr) Can also mischarge tRNA(Tyr) with D-tyrosine, leading to the formation of D-tyrosyl-tRNA(Tyr), which can be hydrolyzed by the D-aminoacyl-tRNA deacylase . In vitro, can also use the non-natural amino acid azatyrosine | 0.900 |
argS | valS | b1876 | b4258 | Arginine--tRNA ligase; Arginine tRNA synthetase; Protein involved in tRNA aminoacylation for protein translation | 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 | 0.894 |
cysS | argS | b0526 | b1876 | Cysteinyl-trna synthetase; Belongs to the class-I aminoacyl-tRNA synthetase family | Arginine--tRNA ligase; Arginine tRNA synthetase; Protein involved in tRNA aminoacylation for protein translation | 0.926 |
cysS | gltX | b0526 | b2400 | Cysteinyl-trna synthetase; Belongs to the class-I aminoacyl-tRNA synthetase family | 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) | 0.883 |
cysS | hisS | b0526 | b2514 | Cysteinyl-trna synthetase; Belongs to the class-I aminoacyl-tRNA synthetase family | Histidine--tRNA ligase; Histidine tRNA synthetase; Protein involved in tRNA aminoacylation for protein translation | 0.876 |
cysS | ileS | b0526 | b0026 | Cysteinyl-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) | 0.937 |
cysS | leuS | b0526 | b0642 | Cysteinyl-trna synthetase; Belongs to the class-I aminoacyl-tRNA synthetase family | Leucyl-trna synthetase; Belongs to the class-I aminoacyl-tRNA synthetase family | 0.967 |
cysS | metG | b0526 | b2114 | Cysteinyl-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 | 0.877 |
cysS | serS | b0526 | b0893 | Cysteinyl-trna synthetase; Belongs to the class-I aminoacyl-tRNA synthetase family | Seryl-trna synthetase; 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) | 0.942 |
cysS | thrS | b0526 | b1719 | Cysteinyl-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) The rate-limiting step is amino acid activation in the presence of tRNA . The 2'-OH of the acceptor base (adenine 76, A76) of tRNA(Thr) and His-309 collaborate to transfer L-Thr to the tRNA; substitution of 2'-OH of A76 with hydrogen or fluorine decreases transfer efficiency 760 and 100-fold respectively . The zinc ion in the active site discriminates against charging of the isos [...] | 0.944 |
cysS | tyrS | b0526 | b1637 | Cysteinyl-trna synthetase; Belongs to the class-I aminoacyl-tRNA synthetase family | Tyrosyl-trna synthetase; Catalyzes the attachment of L-tyrosine to tRNA(Tyr) in a two- step reaction: tyrosine is first activated by ATP to form Tyr-AMP and then transferred to the acceptor end of tRNA(Tyr) Can also mischarge tRNA(Tyr) with D-tyrosine, leading to the formation of D-tyrosyl-tRNA(Tyr), which can be hydrolyzed by the D-aminoacyl-tRNA deacylase . In vitro, can also use the non-natural amino acid azatyrosine | 0.870 |
cysS | valS | b0526 | b4258 | Cysteinyl-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 | 0.939 |