node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
KRG20880.1 | alaS_2 | HT99x_02097 | HT99x_02392 | Bifunctional RNase H/acid phosphatase. | Alanine--tRNA ligase; Catalyzes the attachment of alanine to tRNA(Ala) in a two- step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) via its editing domain. | 0.711 |
KRG20880.1 | aspS | HT99x_02097 | HT99x_00233 | Bifunctional RNase H/acid phosphatase. | Aspartate--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). 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 class-II aminoacyl-tRNA synthetase family. Type 1 subfamily. | 0.583 |
KRG20880.1 | glyQ | HT99x_02097 | HT99x_00440 | Bifunctional RNase H/acid phosphatase. | Glycine--tRNA ligase alpha subunit. | 0.432 |
KRG20880.1 | glyS | HT99x_02097 | HT99x_00441 | Bifunctional RNase H/acid phosphatase. | Glycine--tRNA ligase beta subunit. | 0.685 |
KRG20880.1 | leuS | HT99x_02097 | HT99x_00908 | Bifunctional RNase H/acid phosphatase. | Leucine--tRNA ligase; Belongs to the class-I aminoacyl-tRNA synthetase family. | 0.959 |
KRG20880.1 | proS | HT99x_02097 | HT99x_01587 | Bifunctional RNase H/acid phosphatase. | 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 [...] | 0.979 |
KRG20880.1 | valS | HT99x_02097 | HT99x_01615 | Bifunctional RNase H/acid phosphatase. | 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. | 0.898 |
KRG22025.1 | KRG22026.1 | HT99x_00442 | HT99x_00443 | D-glycero-beta-D-manno-heptose-1,7-bisphosphate 7-phosphatase. | 2-acyl-glycerophospho-ethanolamine acyltransferase. | 0.690 |
KRG22025.1 | glyQ | HT99x_00442 | HT99x_00440 | D-glycero-beta-D-manno-heptose-1,7-bisphosphate 7-phosphatase. | Glycine--tRNA ligase alpha subunit. | 0.800 |
KRG22025.1 | glyS | HT99x_00442 | HT99x_00441 | D-glycero-beta-D-manno-heptose-1,7-bisphosphate 7-phosphatase. | Glycine--tRNA ligase beta subunit. | 0.801 |
KRG22026.1 | KRG22025.1 | HT99x_00443 | HT99x_00442 | 2-acyl-glycerophospho-ethanolamine acyltransferase. | D-glycero-beta-D-manno-heptose-1,7-bisphosphate 7-phosphatase. | 0.690 |
KRG22026.1 | glyQ | HT99x_00443 | HT99x_00440 | 2-acyl-glycerophospho-ethanolamine acyltransferase. | Glycine--tRNA ligase alpha subunit. | 0.689 |
KRG22026.1 | glyS | HT99x_00443 | HT99x_00441 | 2-acyl-glycerophospho-ethanolamine acyltransferase. | Glycine--tRNA ligase beta subunit. | 0.689 |
alaS_2 | KRG20880.1 | HT99x_02392 | HT99x_02097 | Alanine--tRNA ligase; Catalyzes the attachment of alanine to tRNA(Ala) in a two- step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) via its editing domain. | Bifunctional RNase H/acid phosphatase. | 0.711 |
alaS_2 | aspS | HT99x_02392 | HT99x_00233 | Alanine--tRNA ligase; Catalyzes the attachment of alanine to tRNA(Ala) in a two- step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) via its editing domain. | Aspartate--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). 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 class-II aminoacyl-tRNA synthetase family. Type 1 subfamily. | 0.911 |
alaS_2 | glyQ | HT99x_02392 | HT99x_00440 | Alanine--tRNA ligase; Catalyzes the attachment of alanine to tRNA(Ala) in a two- step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) via its editing domain. | Glycine--tRNA ligase alpha subunit. | 0.727 |
alaS_2 | glyS | HT99x_02392 | HT99x_00441 | Alanine--tRNA ligase; Catalyzes the attachment of alanine to tRNA(Ala) in a two- step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) via its editing domain. | Glycine--tRNA ligase beta subunit. | 0.677 |
alaS_2 | ileS | HT99x_02392 | HT99x_00718 | Alanine--tRNA ligase; Catalyzes the attachment of alanine to tRNA(Ala) in a two- step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) via its editing domain. | 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 1 subfamily. | 0.684 |
alaS_2 | leuS | HT99x_02392 | HT99x_00908 | Alanine--tRNA ligase; Catalyzes the attachment of alanine to tRNA(Ala) in a two- step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) via its editing domain. | Leucine--tRNA ligase; Belongs to the class-I aminoacyl-tRNA synthetase family. | 0.852 |
alaS_2 | proS | HT99x_02392 | HT99x_01587 | Alanine--tRNA ligase; Catalyzes the attachment of alanine to tRNA(Ala) in a two- step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) via its editing domain. | 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 [...] | 0.542 |