| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| AEM78318.1 | AEM78319.1 | Thewi_0888 | Thewi_0889 | PFAM: GCN5-related N-acetyltransferase; KEGG: tbo:Thebr_1565 GCN5-like N-acetyltransferase. | KEGG: thx:Thet_0726 FolC bifunctional protein; TIGRFAM: Folylpolyglutamate synthetase; PFAM: Mur ligase, C-terminal; Mur ligase, central; Belongs to the folylpolyglutamate synthase family. | 0.700 |
| AEM78318.1 | valS | Thewi_0888 | Thewi_0887 | PFAM: GCN5-related N-acetyltransferase; KEGG: tbo:Thebr_1565 GCN5-like N-acetyltransferase. | 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. | 0.746 |
| AEM78319.1 | AEM78318.1 | Thewi_0889 | Thewi_0888 | KEGG: thx:Thet_0726 FolC bifunctional protein; TIGRFAM: Folylpolyglutamate synthetase; PFAM: Mur ligase, C-terminal; Mur ligase, central; Belongs to the folylpolyglutamate synthase family. | PFAM: GCN5-related N-acetyltransferase; KEGG: tbo:Thebr_1565 GCN5-like N-acetyltransferase. | 0.700 |
| AEM78319.1 | guaA | Thewi_0889 | Thewi_0667 | KEGG: thx:Thet_0726 FolC bifunctional protein; TIGRFAM: Folylpolyglutamate synthetase; PFAM: Mur ligase, C-terminal; Mur ligase, central; Belongs to the folylpolyglutamate synthase family. | GMP synthase (glutamine-hydrolyzing); Catalyzes the synthesis of GMP from XMP. | 0.656 |
| AEM78319.1 | hisS | Thewi_0889 | Thewi_1179 | KEGG: thx:Thet_0726 FolC bifunctional protein; TIGRFAM: Folylpolyglutamate synthetase; PFAM: Mur ligase, C-terminal; Mur ligase, central; Belongs to the folylpolyglutamate synthase family. | TIGRFAM: Histidyl-tRNA synthetase, class IIa, subgroup; HAMAP: Histidyl-tRNA synthetase, class IIa, subgroup; KEGG: tbo:Thebr_1062 histidyl-tRNA synthetase; PFAM: Aminoacyl-tRNA synthetase, class II (G/ H/ P/ S), conserved region; Anticodon-binding. | 0.433 |
| AEM78319.1 | valS | Thewi_0889 | Thewi_0887 | KEGG: thx:Thet_0726 FolC bifunctional protein; TIGRFAM: Folylpolyglutamate synthetase; PFAM: Mur ligase, C-terminal; Mur ligase, central; Belongs to the folylpolyglutamate synthase family. | 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. | 0.879 |
| alaS | aspS | Thewi_1196 | Thewi_1180 | 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. | 0.554 |
| alaS | guaA | Thewi_1196 | Thewi_0667 | 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. | GMP synthase (glutamine-hydrolyzing); Catalyzes the synthesis of GMP from XMP. | 0.458 |
| alaS | hisS | Thewi_1196 | Thewi_1179 | 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: Histidyl-tRNA synthetase, class IIa, subgroup; HAMAP: Histidyl-tRNA synthetase, class IIa, subgroup; KEGG: tbo:Thebr_1062 histidyl-tRNA synthetase; PFAM: Aminoacyl-tRNA synthetase, class II (G/ H/ P/ S), conserved region; Anticodon-binding. | 0.464 |
| alaS | ileS | Thewi_1196 | Thewi_1531 | 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. | 0.753 |
| alaS | leuS | Thewi_1196 | Thewi_0350 | 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: tit:Thit_0284 leucyl-tRNA synthetase; TIGRFAM: Leucyl-tRNA synthetase, class Ia, bacterial/mitochondrial; Belongs to the class-I aminoacyl-tRNA synthetase family. | 0.669 |
| alaS | pheT | Thewi_1196 | Thewi_1649 | 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; HAMAP: Phenylalanyl-tRNA synthetase, class IIc, beta subunit, bacterial; KEGG: tpd:Teth39_0772 phenylalanyl-tRNA synthetase subunit beta; Belongs to the phenylalanyl-tRNA synthetase beta subunit family. Type 1 subfamily. | 0.742 |
| alaS | thrS | Thewi_1196 | Thewi_1659 | 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). | 0.807 |
| alaS | valS | Thewi_1196 | Thewi_0887 | 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. | 0.791 |
| aspS | alaS | Thewi_1180 | Thewi_1196 | 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. | 0.554 |
| aspS | guaA | Thewi_1180 | Thewi_0667 | 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. | GMP synthase (glutamine-hydrolyzing); Catalyzes the synthesis of GMP from XMP. | 0.870 |
| aspS | hisS | Thewi_1180 | Thewi_1179 | 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: Histidyl-tRNA synthetase, class IIa, subgroup; HAMAP: Histidyl-tRNA synthetase, class IIa, subgroup; KEGG: tbo:Thebr_1062 histidyl-tRNA synthetase; PFAM: Aminoacyl-tRNA synthetase, class II (G/ H/ P/ S), conserved region; Anticodon-binding. | 0.983 |
| aspS | ileS | Thewi_1180 | Thewi_1531 | 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. | 0.619 |
| aspS | leuS | Thewi_1180 | Thewi_0350 | 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. | KEGG: tit:Thit_0284 leucyl-tRNA synthetase; TIGRFAM: Leucyl-tRNA synthetase, class Ia, bacterial/mitochondrial; Belongs to the class-I aminoacyl-tRNA synthetase family. | 0.641 |
| aspS | pheT | Thewi_1180 | Thewi_1649 | 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: Phenylalanyl-tRNA synthetase, class IIc, beta subunit, bacterial; HAMAP: Phenylalanyl-tRNA synthetase, class IIc, beta subunit, bacterial; KEGG: tpd:Teth39_0772 phenylalanyl-tRNA synthetase subunit beta; Belongs to the phenylalanyl-tRNA synthetase beta subunit family. Type 1 subfamily. | 0.732 |