| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| Afer_0082 | alaS | Afer_0082 | Afer_0951 | Histidine--tRNA ligase; PFAM: tRNA synthetase class II (G H P and S); KEGG: cms:CMS_2457 histidyl-tRNA synthetase. | 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. | 0.756 |
| Afer_0082 | aspS | Afer_0082 | Afer_0534 | Histidine--tRNA ligase; PFAM: tRNA synthetase class II (G H P and S); KEGG: cms:CMS_2457 histidyl-tRNA synthetase. | 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. | 0.845 |
| Afer_0082 | gatB | Afer_0082 | Afer_1549 | Histidine--tRNA ligase; PFAM: tRNA synthetase class II (G H P and S); KEGG: cms:CMS_2457 histidyl-tRNA synthetase. | glutamyl-tRNA(Gln) amidotransferase, B subunit; Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl- tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an activated phospho-Asp- tRNA(Asn) or phospho-Glu-tRNA(Gln); Belongs to the GatB/GatE family. GatB subfamily. | 0.400 |
| Afer_0082 | gltX | Afer_0082 | Afer_1528 | Histidine--tRNA ligase; PFAM: tRNA synthetase class II (G H P and S); KEGG: cms:CMS_2457 histidyl-tRNA synthetase. | glutamyl-tRNA synthetase; 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). | 0.464 |
| Afer_0082 | guaA | Afer_0082 | Afer_0460 | Histidine--tRNA ligase; PFAM: tRNA synthetase class II (G H P and S); KEGG: cms:CMS_2457 histidyl-tRNA synthetase. | GMP synthase, large subunit; Catalyzes the synthesis of GMP from XMP. | 0.822 |
| Afer_0082 | pheT | Afer_0082 | Afer_1673 | Histidine--tRNA ligase; PFAM: tRNA synthetase class II (G H P and S); KEGG: cms:CMS_2457 histidyl-tRNA synthetase. | KEGG: ade:Adeh_1971 phenylalanyl-tRNA synthetase beta subunit; TIGRFAM: phenylalanyl-tRNA synthetase, beta subunit. | 0.648 |
| Afer_0082 | valS | Afer_0082 | Afer_0307 | Histidine--tRNA ligase; PFAM: tRNA synthetase class II (G H P and S); KEGG: cms:CMS_2457 histidyl-tRNA synthetase. | aminoacyl-tRNA synthetase class Ia; 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. | 0.728 |
| Afer_0533 | aspS | Afer_0533 | Afer_0534 | PFAM: AAA ATPase central domain protein; ATPase associated with various cellular activities AAA_5; magnesium chelatase ChlI subunit; SMART: AAA ATPase; KEGG: rxy:Rxyl_1040 recombination factor protein RarA. | 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. | 0.828 |
| Afer_0533 | guaA | Afer_0533 | Afer_0460 | PFAM: AAA ATPase central domain protein; ATPase associated with various cellular activities AAA_5; magnesium chelatase ChlI subunit; SMART: AAA ATPase; KEGG: rxy:Rxyl_1040 recombination factor protein RarA. | GMP synthase, large subunit; Catalyzes the synthesis of GMP from XMP. | 0.569 |
| Afer_0533 | pheT | Afer_0533 | Afer_1673 | PFAM: AAA ATPase central domain protein; ATPase associated with various cellular activities AAA_5; magnesium chelatase ChlI subunit; SMART: AAA ATPase; KEGG: rxy:Rxyl_1040 recombination factor protein RarA. | KEGG: ade:Adeh_1971 phenylalanyl-tRNA synthetase beta subunit; TIGRFAM: phenylalanyl-tRNA synthetase, beta subunit. | 0.568 |
| Afer_1219 | aspS | Afer_1219 | Afer_0534 | PFAM: protein of unknown function DUF28; KEGG: gme:Gmet_0743 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. | 0.810 |
| Afer_1219 | pheT | Afer_1219 | Afer_1673 | PFAM: protein of unknown function DUF28; KEGG: gme:Gmet_0743 hypothetical protein. | KEGG: ade:Adeh_1971 phenylalanyl-tRNA synthetase beta subunit; TIGRFAM: phenylalanyl-tRNA synthetase, beta subunit. | 0.700 |
| alaS | Afer_0082 | Afer_0951 | Afer_0082 | 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. | Histidine--tRNA ligase; PFAM: tRNA synthetase class II (G H P and S); KEGG: cms:CMS_2457 histidyl-tRNA synthetase. | 0.756 |
| alaS | aspS | Afer_0951 | Afer_0534 | 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 | gatB | Afer_0951 | Afer_1549 | 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(Gln) amidotransferase, B subunit; Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl- tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an activated phospho-Asp- tRNA(Asn) or phospho-Glu-tRNA(Gln); Belongs to the GatB/GatE family. GatB subfamily. | 0.463 |
| alaS | gltX | Afer_0951 | Afer_1528 | 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; 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). | 0.826 |
| alaS | guaA | Afer_0951 | Afer_0460 | 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, large subunit; Catalyzes the synthesis of GMP from XMP. | 0.695 |
| alaS | pheT | Afer_0951 | Afer_1673 | 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: ade:Adeh_1971 phenylalanyl-tRNA synthetase beta subunit; TIGRFAM: phenylalanyl-tRNA synthetase, beta subunit. | 0.929 |
| alaS | valS | Afer_0951 | Afer_0307 | 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. | aminoacyl-tRNA synthetase class Ia; 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. | 0.802 |
| aspS | Afer_0082 | Afer_0534 | Afer_0082 | 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. | Histidine--tRNA ligase; PFAM: tRNA synthetase class II (G H P and S); KEGG: cms:CMS_2457 histidyl-tRNA synthetase. | 0.845 |