node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
alaS | argS | Dde_2374 | Dde_2295 | alanyl-tRNA synthetase; 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. | TIGRFAM: Arginyl-tRNA synthetase, class Ic; KEGG: dvm:DvMF_0850 arginyl-tRNA synthetase. | 0.630 |
alaS | aspS | Dde_2374 | Dde_0012 | alanyl-tRNA synthetase; 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. | aspartyl-tRNA synthetase; 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. | 0.793 |
alaS | ileS | Dde_2374 | Dde_2142 | alanyl-tRNA synthetase; 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. | 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 class-I aminoacyl-tRNA synthetase family. IleS type 1 subfamily. | 0.856 |
alaS | leuS | Dde_2374 | Dde_2439 | alanyl-tRNA synthetase; 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. | TIGRFAM: Leucyl-tRNA synthetase, class Ia, bacterial/mitochondrial; KEGG: dvl:Dvul_1861 leucyl-tRNA synthetase; Belongs to the class-I aminoacyl-tRNA synthetase family. | 0.856 |
alaS | metG | Dde_2374 | Dde_1594 | alanyl-tRNA synthetase; 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. | 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. | 0.911 |
alaS | pheS | Dde_2374 | Dde_2635 | alanyl-tRNA synthetase; 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. | KEGG: dvl:Dvul_0711 phenylalanyl-tRNA synthetase subunit alpha; TIGRFAM: Phenylalanyl-tRNA synthetase, class IIc, alpha subunit; PFAM: Phenylalanyl-tRNA synthetase alpha chain; Phenylalanyl-tRNA synthetase, class II, N-terminal; Belongs to the class-II aminoacyl-tRNA synthetase family. Phe-tRNA synthetase alpha subunit type 1 subfamily. | 0.478 |
alaS | pheT | Dde_2374 | Dde_2634 | alanyl-tRNA synthetase; 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. | TIGRFAM: Phenylalanyl-tRNA synthetase, class IIc, beta subunit, bacterial; KEGG: dvl:Dvul_0712 phenylalanyl-tRNA synthetase subunit beta. | 0.898 |
alaS | proS | Dde_2374 | Dde_2206 | alanyl-tRNA synthetase; 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. | 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 [...] | 0.679 |
alaS | tyrS | Dde_2374 | Dde_0228 | alanyl-tRNA synthetase; 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. | Tyrosyl-tRNA synthetase; Catalyzes the attachment of 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); Belongs to the class-I aminoacyl-tRNA synthetase family. TyrS type 2 subfamily. | 0.742 |
alaS | valS | Dde_2374 | Dde_2839 | alanyl-tRNA synthetase; 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. | 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. | 0.903 |
argS | alaS | Dde_2295 | Dde_2374 | TIGRFAM: Arginyl-tRNA synthetase, class Ic; KEGG: dvm:DvMF_0850 arginyl-tRNA synthetase. | alanyl-tRNA synthetase; 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. | 0.630 |
argS | aspS | Dde_2295 | Dde_0012 | TIGRFAM: Arginyl-tRNA synthetase, class Ic; KEGG: dvm:DvMF_0850 arginyl-tRNA synthetase. | aspartyl-tRNA synthetase; 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. | 0.726 |
argS | ileS | Dde_2295 | Dde_2142 | TIGRFAM: Arginyl-tRNA synthetase, class Ic; KEGG: dvm:DvMF_0850 arginyl-tRNA synthetase. | 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 class-I aminoacyl-tRNA synthetase family. IleS type 1 subfamily. | 0.968 |
argS | leuS | Dde_2295 | Dde_2439 | TIGRFAM: Arginyl-tRNA synthetase, class Ic; KEGG: dvm:DvMF_0850 arginyl-tRNA synthetase. | TIGRFAM: Leucyl-tRNA synthetase, class Ia, bacterial/mitochondrial; KEGG: dvl:Dvul_1861 leucyl-tRNA synthetase; Belongs to the class-I aminoacyl-tRNA synthetase family. | 0.925 |
argS | metG | Dde_2295 | Dde_1594 | TIGRFAM: Arginyl-tRNA synthetase, class Ic; KEGG: dvm:DvMF_0850 arginyl-tRNA synthetase. | 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. | 0.960 |
argS | pheS | Dde_2295 | Dde_2635 | TIGRFAM: Arginyl-tRNA synthetase, class Ic; KEGG: dvm:DvMF_0850 arginyl-tRNA synthetase. | KEGG: dvl:Dvul_0711 phenylalanyl-tRNA synthetase subunit alpha; TIGRFAM: Phenylalanyl-tRNA synthetase, class IIc, alpha subunit; PFAM: Phenylalanyl-tRNA synthetase alpha chain; Phenylalanyl-tRNA synthetase, class II, N-terminal; Belongs to the class-II aminoacyl-tRNA synthetase family. Phe-tRNA synthetase alpha subunit type 1 subfamily. | 0.653 |
argS | pheT | Dde_2295 | Dde_2634 | TIGRFAM: Arginyl-tRNA synthetase, class Ic; KEGG: dvm:DvMF_0850 arginyl-tRNA synthetase. | TIGRFAM: Phenylalanyl-tRNA synthetase, class IIc, beta subunit, bacterial; KEGG: dvl:Dvul_0712 phenylalanyl-tRNA synthetase subunit beta. | 0.899 |
argS | proS | Dde_2295 | Dde_2206 | TIGRFAM: Arginyl-tRNA synthetase, class Ic; KEGG: dvm:DvMF_0850 arginyl-tRNA synthetase. | 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 [...] | 0.963 |
argS | tyrS | Dde_2295 | Dde_0228 | TIGRFAM: Arginyl-tRNA synthetase, class Ic; KEGG: dvm:DvMF_0850 arginyl-tRNA synthetase. | Tyrosyl-tRNA synthetase; Catalyzes the attachment of 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); Belongs to the class-I aminoacyl-tRNA synthetase family. TyrS type 2 subfamily. | 0.788 |
argS | valS | Dde_2295 | Dde_2839 | TIGRFAM: Arginyl-tRNA synthetase, class Ic; KEGG: dvm:DvMF_0850 arginyl-tRNA synthetase. | 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. | 0.769 |