node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
BRADO6498 | alaS | BRADO6498 | BRADO4981 | Putative Glutamyl-tRNA synthetase, class Ic; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme; Belongs to the class-I aminoacyl-tRNA synthetase family. | 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. | 0.604 |
BRADO6498 | argS | BRADO6498 | BRADO4052 | Putative Glutamyl-tRNA synthetase, class Ic; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme; Belongs to the class-I aminoacyl-tRNA synthetase family. | arginyl-tRNA synthetase; Function of strongly homologous gene; enzyme. | 0.851 |
BRADO6498 | ileS | BRADO6498 | BRADO6067 | Putative Glutamyl-tRNA synthetase, class Ic; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme; Belongs to the class-I aminoacyl-tRNA synthetase family. | Isoleucine 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). | 0.895 |
BRADO6498 | leuS | BRADO6498 | BRADO0189 | Putative Glutamyl-tRNA synthetase, class Ic; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme; Belongs to the class-I aminoacyl-tRNA synthetase family. | Leucine tRNA synthetase; Function of homologous gene experimentally demonstrated in an other organism; enzyme; Belongs to the class-I aminoacyl-tRNA synthetase family. | 0.862 |
BRADO6498 | metG | BRADO6498 | BRADO3829 | Putative Glutamyl-tRNA synthetase, class Ic; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme; Belongs to the class-I aminoacyl-tRNA synthetase family. | 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; Belongs to the class-I aminoacyl-tRNA synthetase family. MetG type 2B subfamily. | 0.886 |
BRADO6498 | pheT | BRADO6498 | BRADO0141 | Putative Glutamyl-tRNA synthetase, class Ic; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme; Belongs to the class-I aminoacyl-tRNA synthetase family. | Phenylalanyl-tRNA synthetase beta chain (Phenylalanine--tRNA ligase beta chain); Function of homologous gene experimentally demonstrated in an other organism; enzyme; Belongs to the phenylalanyl-tRNA synthetase beta subunit family. Type 1 subfamily. | 0.825 |
BRADO6498 | proS | BRADO6498 | BRADO4154 | Putative Glutamyl-tRNA synthetase, class Ic; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme; Belongs to the class-I aminoacyl-tRNA synthetase family. | Prolyl-tRNA synthetase (Proline--tRNA ligase) (ProRS); 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); Belongs to the class-II aminoacyl-tRNA synthetase family. ProS type 2 subfamily. | 0.856 |
BRADO6498 | valS | BRADO6498 | BRADO3881 | Putative Glutamyl-tRNA synthetase, class Ic; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme; Belongs to the class-I aminoacyl-tRNA synthetase family. | Valyl-tRNA synthetase (Valine--tRNA ligase); 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. | 0.529 |
alaS | BRADO6498 | BRADO4981 | BRADO6498 | 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. | Putative Glutamyl-tRNA synthetase, class Ic; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme; Belongs to the class-I aminoacyl-tRNA synthetase family. | 0.604 |
alaS | argS | BRADO4981 | BRADO4052 | 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. | arginyl-tRNA synthetase; Function of strongly homologous gene; enzyme. | 0.643 |
alaS | glnS | BRADO4981 | BRADO4124 | 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. | Glutaminyl-tRNA synthetase (Glutamine--tRNA ligase) (GlnRS); Function of homologous gene experimentally demonstrated in an other organism; enzyme. | 0.604 |
alaS | gltX | BRADO4981 | BRADO4125 | 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. | Glutamyl-tRNA synthetase (Glutamate--tRNA ligase) (GluRS); Catalyzes the attachment of glutamate to tRNA(Glu) in a two- step reaction: glutamate is first activated by ATP to form Glu-AMP and then transferred to the acceptor end of tRNA(Glu); Belongs to the class-I aminoacyl-tRNA synthetase family. Glutamate--tRNA ligase type 1 subfamily. | 0.790 |
alaS | ileS | BRADO4981 | BRADO6067 | 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. | Isoleucine 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). | 0.876 |
alaS | leuS | BRADO4981 | BRADO0189 | 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. | Leucine tRNA synthetase; Function of homologous gene experimentally demonstrated in an other organism; enzyme; Belongs to the class-I aminoacyl-tRNA synthetase family. | 0.890 |
alaS | metG | BRADO4981 | BRADO3829 | 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 (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; Belongs to the class-I aminoacyl-tRNA synthetase family. MetG type 2B subfamily. | 0.794 |
alaS | pheT | BRADO4981 | BRADO0141 | 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. | Phenylalanyl-tRNA synthetase beta chain (Phenylalanine--tRNA ligase beta chain); Function of homologous gene experimentally demonstrated in an other organism; enzyme; Belongs to the phenylalanyl-tRNA synthetase beta subunit family. Type 1 subfamily. | 0.927 |
alaS | proS | BRADO4981 | BRADO4154 | 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 (Proline--tRNA ligase) (ProRS); 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); Belongs to the class-II aminoacyl-tRNA synthetase family. ProS type 2 subfamily. | 0.690 |
alaS | valS | BRADO4981 | BRADO3881 | 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 (Valine--tRNA ligase); 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. | 0.921 |
argS | BRADO6498 | BRADO4052 | BRADO6498 | arginyl-tRNA synthetase; Function of strongly homologous gene; enzyme. | Putative Glutamyl-tRNA synthetase, class Ic; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme; Belongs to the class-I aminoacyl-tRNA synthetase family. | 0.851 |
argS | alaS | BRADO4052 | BRADO4981 | arginyl-tRNA synthetase; Function of strongly homologous gene; enzyme. | 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. | 0.643 |