node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
Dred_2333 | alaS | Dred_2333 | Dred_0769 | TIGRFAM: phage tail protein I; PFAM: Threonyl/alanyl tRNA synthetase, SAD; KEGG: bld:BLi02774 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. | 0.916 |
Dred_2333 | aspS | Dred_2333 | Dred_0757 | TIGRFAM: phage tail protein I; PFAM: Threonyl/alanyl tRNA synthetase, SAD; KEGG: bld:BLi02774 hypothetical protein. | 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. | 0.761 |
Dred_2333 | glyQ | Dred_2333 | Dred_2473 | TIGRFAM: phage tail protein I; PFAM: Threonyl/alanyl tRNA synthetase, SAD; KEGG: bld:BLi02774 hypothetical protein. | PFAM: glycyl-tRNA synthetase, alpha subunit; KEGG: mta:Moth_0603 glycyl-tRNA synthetase, alpha subunit. | 0.724 |
Dred_2333 | glyS | Dred_2333 | Dred_2472 | TIGRFAM: phage tail protein I; PFAM: Threonyl/alanyl tRNA synthetase, SAD; KEGG: bld:BLi02774 hypothetical protein. | KEGG: mta:Moth_0604 glycyl-tRNA synthetase, beta subunit. | 0.673 |
Dred_2333 | ileS | Dred_2333 | Dred_0718 | TIGRFAM: phage tail protein I; PFAM: Threonyl/alanyl tRNA synthetase, SAD; KEGG: bld:BLi02774 hypothetical protein. | 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. | 0.737 |
Dred_2333 | leuS | Dred_2333 | Dred_2515 | TIGRFAM: phage tail protein I; PFAM: Threonyl/alanyl tRNA synthetase, SAD; KEGG: bld:BLi02774 hypothetical protein. | TIGRFAM: leucyl-tRNA synthetase; KEGG: chy:CHY_0393 leucyl-tRNA synthetase; Belongs to the class-I aminoacyl-tRNA synthetase family. | 0.760 |
Dred_2333 | proS | Dred_2333 | Dred_1967 | TIGRFAM: phage tail protein I; PFAM: Threonyl/alanyl tRNA synthetase, SAD; KEGG: bld:BLi02774 hypothetical protein. | 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 [...] | 0.505 |
Dred_2333 | valS | Dred_2333 | Dred_2554 | TIGRFAM: phage tail protein I; PFAM: Threonyl/alanyl tRNA synthetase, SAD; KEGG: bld:BLi02774 hypothetical protein. | 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. | 0.794 |
Dred_2470 | glyQ | Dred_2470 | Dred_2473 | Protein of unknown function DUF299; Bifunctional serine/threonine kinase and phosphorylase involved in the regulation of the pyruvate, phosphate dikinase (PPDK) by catalyzing its phosphorylation/dephosphorylation. | PFAM: glycyl-tRNA synthetase, alpha subunit; KEGG: mta:Moth_0603 glycyl-tRNA synthetase, alpha subunit. | 0.651 |
Dred_2470 | glyS | Dred_2470 | Dred_2472 | Protein of unknown function DUF299; Bifunctional serine/threonine kinase and phosphorylase involved in the regulation of the pyruvate, phosphate dikinase (PPDK) by catalyzing its phosphorylation/dephosphorylation. | KEGG: mta:Moth_0604 glycyl-tRNA synthetase, beta subunit. | 0.768 |
alaS | Dred_2333 | Dred_0769 | Dred_2333 | 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: phage tail protein I; PFAM: Threonyl/alanyl tRNA synthetase, SAD; KEGG: bld:BLi02774 hypothetical protein. | 0.916 |
alaS | aspS | Dred_0769 | Dred_0757 | 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. | 0.900 |
alaS | glyQ | Dred_0769 | Dred_2473 | 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. | PFAM: glycyl-tRNA synthetase, alpha subunit; KEGG: mta:Moth_0603 glycyl-tRNA synthetase, alpha subunit. | 0.724 |
alaS | glyS | Dred_0769 | Dred_2472 | 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: mta:Moth_0604 glycyl-tRNA synthetase, beta subunit. | 0.675 |
alaS | ileS | Dred_0769 | Dred_0718 | 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. | 0.805 |
alaS | leuS | Dred_0769 | Dred_2515 | 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; KEGG: chy:CHY_0393 leucyl-tRNA synthetase; Belongs to the class-I aminoacyl-tRNA synthetase family. | 0.796 |
alaS | proS | Dred_0769 | Dred_1967 | 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 [...] | 0.513 |
alaS | valS | Dred_0769 | Dred_2554 | 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. | 0.826 |
aspS | Dred_2333 | Dred_0757 | Dred_2333 | 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. | TIGRFAM: phage tail protein I; PFAM: Threonyl/alanyl tRNA synthetase, SAD; KEGG: bld:BLi02774 hypothetical protein. | 0.761 |
aspS | alaS | Dred_0757 | Dred_0769 | 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. | 0.900 |