node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
CCD30280.1 | alaS | CAGGBEG34_700001 | CAGGBEG34_20027 | Putative Glycyl-tRNA synthetase, beta subunit (fragment); Evidence 3:Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe:putative enzyme. | Alanyl-tRNA synthetase (Alanine--tRNA ligase) (AlaRS); 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. | 0.504 |
CCD30280.1 | aspS | CAGGBEG34_700001 | CAGGBEG34_100025 | Putative Glycyl-tRNA synthetase, beta subunit (fragment); Evidence 3:Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe:putative enzyme. | Fragment of Putative Fic family protein; 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. | 0.623 |
CCD30280.1 | glyQ | CAGGBEG34_700001 | CAGGBEG34_530003 | Putative Glycyl-tRNA synthetase, beta subunit (fragment); Evidence 3:Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe:putative enzyme. | Glycine tRNA synthetase, alpha subunit (Glycine--tRNA ligase alpha chain) (GlyRS); Evidence 2a:Function of homologous gene experimentally demonstrated in an other organism; Product type e:enzyme. | 0.997 |
CCD30280.1 | ileS | CAGGBEG34_700001 | CAGGBEG34_260028 | Putative Glycyl-tRNA synthetase, beta subunit (fragment); Evidence 3:Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe:putative enzyme. | Isoleucine tRNA synthetase (Isoleucine--tRNA ligase) (IleRS); 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. | 0.602 |
CCD30280.1 | pheT | CAGGBEG34_700001 | CAGGBEG34_200026 | Putative Glycyl-tRNA synthetase, beta subunit (fragment); Evidence 3:Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe:putative enzyme. | Phenylalanyl-tRNA synthetase beta chain (Phenylalanine--tRNA ligase beta chain) (PheRS); Evidence 2a:Function of homologous gene experimentally demonstrated in an other organism; Product type e:enzyme; Belongs to the phenylalanyl-tRNA synthetase beta subunit family. Type 1 subfamily. | 0.675 |
CCD30280.1 | valS | CAGGBEG34_700001 | CAGGBEG34_240006 | Putative Glycyl-tRNA synthetase, beta subunit (fragment); Evidence 3:Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe:putative enzyme. | Valyl-tRNA synthetase (Valine--tRNA ligase) (ValRS); 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. | 0.637 |
alaS | CCD30280.1 | CAGGBEG34_20027 | CAGGBEG34_700001 | Alanyl-tRNA synthetase (Alanine--tRNA ligase) (AlaRS); 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 Glycyl-tRNA synthetase, beta subunit (fragment); Evidence 3:Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe:putative enzyme. | 0.504 |
alaS | aspS | CAGGBEG34_20027 | CAGGBEG34_100025 | Alanyl-tRNA synthetase (Alanine--tRNA ligase) (AlaRS); 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. | Fragment of Putative Fic family protein; 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. | 0.866 |
alaS | glyQ | CAGGBEG34_20027 | CAGGBEG34_530003 | Alanyl-tRNA synthetase (Alanine--tRNA ligase) (AlaRS); 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. | Glycine tRNA synthetase, alpha subunit (Glycine--tRNA ligase alpha chain) (GlyRS); Evidence 2a:Function of homologous gene experimentally demonstrated in an other organism; Product type e:enzyme. | 0.538 |
alaS | guaA | CAGGBEG34_20027 | CAGGBEG34_180086 | Alanyl-tRNA synthetase (Alanine--tRNA ligase) (AlaRS); 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) (Glutamine amidotransferase) (GMP synthetase); Catalyzes the synthesis of GMP from XMP. | 0.754 |
alaS | hisS | CAGGBEG34_20027 | CAGGBEG34_280035 | Alanyl-tRNA synthetase (Alanine--tRNA ligase) (AlaRS); 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. | Histidine tRNA synthetase (Histidine--tRNA ligase) (HisRS); Evidence 2a:Function of homologous gene experimentally demonstrated in an other organism; Product type e:enzyme. | 0.639 |
alaS | ileS | CAGGBEG34_20027 | CAGGBEG34_260028 | Alanyl-tRNA synthetase (Alanine--tRNA ligase) (AlaRS); 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 (Isoleucine--tRNA ligase) (IleRS); 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. | 0.725 |
alaS | metG | CAGGBEG34_20027 | CAGGBEG34_250041 | Alanyl-tRNA synthetase (Alanine--tRNA ligase) (AlaRS); 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. | 0.867 |
alaS | pheT | CAGGBEG34_20027 | CAGGBEG34_200026 | Alanyl-tRNA synthetase (Alanine--tRNA ligase) (AlaRS); 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) (PheRS); Evidence 2a:Function of homologous gene experimentally demonstrated in an other organism; Product type e:enzyme; Belongs to the phenylalanyl-tRNA synthetase beta subunit family. Type 1 subfamily. | 0.901 |
alaS | valS | CAGGBEG34_20027 | CAGGBEG34_240006 | Alanyl-tRNA synthetase (Alanine--tRNA ligase) (AlaRS); 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) (ValRS); 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. | 0.789 |
aspS | CCD30280.1 | CAGGBEG34_100025 | CAGGBEG34_700001 | Fragment of Putative Fic family protein; 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. | Putative Glycyl-tRNA synthetase, beta subunit (fragment); Evidence 3:Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe:putative enzyme. | 0.623 |
aspS | alaS | CAGGBEG34_100025 | CAGGBEG34_20027 | Fragment of Putative Fic family protein; 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 (Alanine--tRNA ligase) (AlaRS); 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. | 0.866 |
aspS | glyQ | CAGGBEG34_100025 | CAGGBEG34_530003 | Fragment of Putative Fic family protein; 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. | Glycine tRNA synthetase, alpha subunit (Glycine--tRNA ligase alpha chain) (GlyRS); Evidence 2a:Function of homologous gene experimentally demonstrated in an other organism; Product type e:enzyme. | 0.505 |
aspS | guaA | CAGGBEG34_100025 | CAGGBEG34_180086 | Fragment of Putative Fic family protein; 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) (Glutamine amidotransferase) (GMP synthetase); Catalyzes the synthesis of GMP from XMP. | 0.850 |
aspS | hisS | CAGGBEG34_100025 | CAGGBEG34_280035 | Fragment of Putative Fic family protein; 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. | Histidine tRNA synthetase (Histidine--tRNA ligase) (HisRS); Evidence 2a:Function of homologous gene experimentally demonstrated in an other organism; Product type e:enzyme. | 0.887 |