node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
Dde_2070 | Dde_2336 | Dde_2070 | Dde_2336 | Sporulation domain-containing protein; PFAM: Sporulation/cell division region, bacteria; KEGG: dvm:DvMF_0405 hypothetical protein. | KEGG: psl:Psta_3109 hypothetical protein. | 0.600 |
Dde_2070 | alaS | Dde_2070 | Dde_2374 | Sporulation domain-containing protein; PFAM: Sporulation/cell division region, bacteria; KEGG: dvm:DvMF_0405 hypothetical protein. | 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. | 0.881 |
Dde_2336 | Dde_2070 | Dde_2336 | Dde_2070 | KEGG: psl:Psta_3109 hypothetical protein. | Sporulation domain-containing protein; PFAM: Sporulation/cell division region, bacteria; KEGG: dvm:DvMF_0405 hypothetical protein. | 0.600 |
Dde_2336 | Dde_3707 | Dde_2336 | Dde_3707 | KEGG: psl:Psta_3109 hypothetical protein. | KEGG: dvl:Dvul_2712 hypothetical protein. | 0.600 |
Dde_2336 | alaS | Dde_2336 | Dde_2374 | KEGG: psl:Psta_3109 hypothetical protein. | 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. | 0.774 |
Dde_2336 | pheT | Dde_2336 | Dde_2634 | KEGG: psl:Psta_3109 hypothetical protein. | TIGRFAM: Phenylalanyl-tRNA synthetase, class IIc, beta subunit, bacterial; KEGG: dvl:Dvul_0712 phenylalanyl-tRNA synthetase subunit beta. | 0.516 |
Dde_3707 | Dde_2336 | Dde_3707 | Dde_2336 | KEGG: dvl:Dvul_2712 hypothetical protein. | KEGG: psl:Psta_3109 hypothetical protein. | 0.600 |
Dde_3707 | alaS | Dde_3707 | Dde_2374 | KEGG: dvl:Dvul_2712 hypothetical protein. | 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. | 0.881 |
alaS | Dde_2070 | Dde_2374 | Dde_2070 | 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. | Sporulation domain-containing protein; PFAM: Sporulation/cell division region, bacteria; KEGG: dvm:DvMF_0405 hypothetical protein. | 0.881 |
alaS | Dde_2336 | Dde_2374 | Dde_2336 | 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: psl:Psta_3109 hypothetical protein. | 0.774 |
alaS | Dde_3707 | Dde_2374 | Dde_3707 | 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_2712 hypothetical protein. | 0.881 |
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 | 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 | thrS | Dde_2374 | Dde_2639 | 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. | 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). Also edits incorrectly charged L-seryl-tRNA(Thr). | 0.800 |
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 |
aspS | alaS | Dde_0012 | Dde_2374 | 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. | 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. | 0.793 |
aspS | ileS | Dde_0012 | Dde_2142 | 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. | 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. | 0.756 |