node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
argS | aspS | DR97_2406 | DR97_974 | Arginyl-trna synthetase; argS: arginine--tRNA ligase | Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Is 1.5 times more efficient at aminoacylating E.coli tRNA(Asp) over 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) | 0.914 |
argS | glnS | DR97_2406 | DR97_92 | Arginyl-trna synthetase; argS: arginine--tRNA ligase | Glutaminyl-trna synthetase; glnS: glutamine--tRNA ligase | 0.941 |
argS | glyS | DR97_2406 | DR97_2961 | Arginyl-trna synthetase; argS: arginine--tRNA ligase | Glycyl-trna synthetase subunit beta; glyS: glycine--tRNA ligase, beta subunit | 0.801 |
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 | 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 | polA | DR97_2406 | DR97_2871 | Arginyl-trna synthetase; argS: arginine--tRNA ligase | In addition to polymerase activity, this DNA polymerase exhibits 3'-5' and 5'-3' exonuclease activity | 0.600 |
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 | purL | DR97_2406 | DR97_4112 | Arginyl-trna synthetase; argS: arginine--tRNA ligase | Phosphoribosylformylglycinamidine synthase involved in the purines biosynthetic pathway. Catalyzes the ATP-dependent conversion of formylglycinamide ribonucleotide (FGAR) and glutamine to yield formylglycinamidine ribonucleotide (FGAM) and glutamate | 0.877 |
aspS | argS | DR97_974 | DR97_2406 | Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Is 1.5 times more efficient at aminoacylating E.coli tRNA(Asp) over 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; argS: arginine--tRNA ligase | 0.914 |
aspS | glnS | DR97_974 | DR97_92 | Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Is 1.5 times more efficient at aminoacylating E.coli tRNA(Asp) over 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) | Glutaminyl-trna synthetase; glnS: glutamine--tRNA ligase | 0.758 |
aspS | glyQ | DR97_974 | DR97_2962 | Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Is 1.5 times more efficient at aminoacylating E.coli tRNA(Asp) over 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) | glyQ: glycine--tRNA ligase, alpha subunit | 0.498 |
aspS | glyS | DR97_974 | DR97_2961 | Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Is 1.5 times more efficient at aminoacylating E.coli tRNA(Asp) over 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) | Glycyl-trna synthetase subunit beta; glyS: glycine--tRNA ligase, beta subunit | 0.870 |
aspS | ileS | DR97_974 | DR97_1864 | Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Is 1.5 times more efficient at aminoacylating E.coli tRNA(Asp) over 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) | 0.875 |
aspS | pheT | DR97_974 | DR97_5223 | Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Is 1.5 times more efficient at aminoacylating E.coli tRNA(Asp) over 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) | Belongs to the phenylalanyl-tRNA synthetase beta subunit family. Type 1 subfamily | 0.997 |
aspS | polA | DR97_974 | DR97_2871 | Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Is 1.5 times more efficient at aminoacylating E.coli tRNA(Asp) over 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) | In addition to polymerase activity, this DNA polymerase exhibits 3'-5' and 5'-3' exonuclease activity | 0.463 |
aspS | proS | DR97_974 | DR97_981 | Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Is 1.5 times more efficient at aminoacylating E.coli tRNA(Asp) over 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; 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 [...] | 0.831 |
aspS | purL | DR97_974 | DR97_4112 | Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Is 1.5 times more efficient at aminoacylating E.coli tRNA(Asp) over 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) | Phosphoribosylformylglycinamidine synthase involved in the purines biosynthetic pathway. Catalyzes the ATP-dependent conversion of formylglycinamide ribonucleotide (FGAR) and glutamine to yield formylglycinamidine ribonucleotide (FGAM) and glutamate | 0.732 |
glnS | argS | DR97_92 | DR97_2406 | Glutaminyl-trna synthetase; glnS: glutamine--tRNA ligase | Arginyl-trna synthetase; argS: arginine--tRNA ligase | 0.941 |
glnS | aspS | DR97_92 | DR97_974 | Glutaminyl-trna synthetase; glnS: glutamine--tRNA ligase | Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Is 1.5 times more efficient at aminoacylating E.coli tRNA(Asp) over 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) | 0.758 |
glnS | glyQ | DR97_92 | DR97_2962 | Glutaminyl-trna synthetase; glnS: glutamine--tRNA ligase | glyQ: glycine--tRNA ligase, alpha subunit | 0.421 |