node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
CBW74206.1 | alaS | RBRH_00073 | RBRH_01067 | Tetratricopeptide repeat family protein; COG: FOG: TPR repeat. | Alanyl-tRNA synthetase (EC 6.1.1.7); 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. | 0.849 |
CBW74411.1 | alaS | RBRH_01066 | RBRH_01067 | Unnamed protein product. | Alanyl-tRNA synthetase (EC 6.1.1.7); 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. | 0.773 |
CBW75242.1 | alaS | RBRH_02567 | RBRH_01067 | Insecticidal toxin complex protein TccB. | Alanyl-tRNA synthetase (EC 6.1.1.7); 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. | 0.838 |
alaS | CBW74206.1 | RBRH_01067 | RBRH_00073 | Alanyl-tRNA synthetase (EC 6.1.1.7); 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. | Tetratricopeptide repeat family protein; COG: FOG: TPR repeat. | 0.849 |
alaS | CBW74411.1 | RBRH_01067 | RBRH_01066 | Alanyl-tRNA synthetase (EC 6.1.1.7); 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. | Unnamed protein product. | 0.773 |
alaS | CBW75242.1 | RBRH_01067 | RBRH_02567 | Alanyl-tRNA synthetase (EC 6.1.1.7); 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. | Insecticidal toxin complex protein TccB. | 0.838 |
alaS | aspS | RBRH_01067 | RBRH_02095 | Alanyl-tRNA synthetase (EC 6.1.1.7); 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 (EC 6.1.1.12); 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. | 0.856 |
alaS | leuS | RBRH_01067 | RBRH_03180 | Alanyl-tRNA synthetase (EC 6.1.1.7); 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. | Leucyl-tRNA synthetase (EC 6.1.1.4); COG: Leucyl-tRNA synthetase; Pfam: Anticodon-binding domain::PF08264<br>tRNA synthetases class I (I, L, M and V)::PF00133<br>tRNA synthetases class I (M)::PF09334; Belongs to the class-I aminoacyl-tRNA synthetase family. | 0.831 |
alaS | metG | RBRH_01067 | RBRH_03128 | Alanyl-tRNA synthetase (EC 6.1.1.7); 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 (EC 6.1.1.10); Is required not only for elongation of protein synthesis but also for the initiation of all mRNA translation through initiator tRNA(fMet) aminoacylation. | 0.797 |
alaS | pheT | RBRH_01067 | RBRH_02833 | Alanyl-tRNA synthetase (EC 6.1.1.7); 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. | Phenylalanyl-tRNA synthetase beta chain (EC 6.1.1.20); COG: Phenylalanyl-tRNA synthetase beta subunit; Pfam: B3/4 domain::PF03483<br>Ferredoxin-fold anticodon binding domain::PF03147<br>Putative tRNA binding domain::PF01588<br>tRNA synthetase B5 domain::PF03484. | 0.884 |
alaS | recA | RBRH_01067 | RBRH_01977 | Alanyl-tRNA synthetase (EC 6.1.1.7); 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. | RecA protein; Can catalyze the hydrolysis of ATP in the presence of single- stranded DNA, the ATP-dependent uptake of single-stranded DNA by duplex DNA, and the ATP-dependent hybridization of homologous single-stranded DNAs. It interacts with LexA causing its activation and leading to its autocatalytic cleavage; Belongs to the RecA family. | 0.761 |
alaS | thrS | RBRH_01067 | RBRH_02828 | Alanyl-tRNA synthetase (EC 6.1.1.7); 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 (EC 6.1.1.3); 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). | 0.845 |
alaS | valS | RBRH_01067 | RBRH_01058 | Alanyl-tRNA synthetase (EC 6.1.1.7); 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 (EC 6.1.1.9); 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. | 0.820 |
aspS | alaS | RBRH_02095 | RBRH_01067 | Aspartyl-tRNA synthetase (EC 6.1.1.12); 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 (EC 6.1.1.7); 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. | 0.856 |
aspS | leuS | RBRH_02095 | RBRH_03180 | Aspartyl-tRNA synthetase (EC 6.1.1.12); 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. | Leucyl-tRNA synthetase (EC 6.1.1.4); COG: Leucyl-tRNA synthetase; Pfam: Anticodon-binding domain::PF08264<br>tRNA synthetases class I (I, L, M and V)::PF00133<br>tRNA synthetases class I (M)::PF09334; Belongs to the class-I aminoacyl-tRNA synthetase family. | 0.632 |
aspS | metG | RBRH_02095 | RBRH_03128 | Aspartyl-tRNA synthetase (EC 6.1.1.12); 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. | Methionyl-tRNA synthetase (EC 6.1.1.10); Is required not only for elongation of protein synthesis but also for the initiation of all mRNA translation through initiator tRNA(fMet) aminoacylation. | 0.641 |
aspS | pheT | RBRH_02095 | RBRH_02833 | Aspartyl-tRNA synthetase (EC 6.1.1.12); 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. | Phenylalanyl-tRNA synthetase beta chain (EC 6.1.1.20); COG: Phenylalanyl-tRNA synthetase beta subunit; Pfam: B3/4 domain::PF03483<br>Ferredoxin-fold anticodon binding domain::PF03147<br>Putative tRNA binding domain::PF01588<br>tRNA synthetase B5 domain::PF03484. | 0.791 |
aspS | thrS | RBRH_02095 | RBRH_02828 | Aspartyl-tRNA synthetase (EC 6.1.1.12); 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. | Threonyl-tRNA synthetase (EC 6.1.1.3); 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). | 0.509 |
aspS | valS | RBRH_02095 | RBRH_01058 | Aspartyl-tRNA synthetase (EC 6.1.1.12); 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. | Valyl-tRNA synthetase (EC 6.1.1.9); 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. | 0.796 |
leuS | alaS | RBRH_03180 | RBRH_01067 | Leucyl-tRNA synthetase (EC 6.1.1.4); COG: Leucyl-tRNA synthetase; Pfam: Anticodon-binding domain::PF08264<br>tRNA synthetases class I (I, L, M and V)::PF00133<br>tRNA synthetases class I (M)::PF09334; Belongs to the class-I aminoacyl-tRNA synthetase family. | Alanyl-tRNA synthetase (EC 6.1.1.7); 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. | 0.831 |