| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| ADU48357.1 | alaS | Intca_1845 | Intca_1587 | COGs: COG0124 Histidyl-tRNA synthetase; InterProIPR006195: IPR004516: IPR002314: IPR004154: IPR 015807; KEGG: kfl:Kfla_4391 histidyl-tRNA synthetase; PFAM: tRNA synthetase class II (G H P and S); Anticodon-binding domain protein; PRIAM: Histidine--tRNA ligase; SPTR: Histidyl-tRNA synthetase; TIGRFAM: histidyl-tRNA synthetase; PFAM: Anticodon binding domain; tRNA synthetase class II core domain (G, H, P, S and T); TIGRFAM: 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. | 0.687 |
| ADU48357.1 | aspS-2 | Intca_1845 | Intca_1578 | COGs: COG0124 Histidyl-tRNA synthetase; InterProIPR006195: IPR004516: IPR002314: IPR004154: IPR 015807; KEGG: kfl:Kfla_4391 histidyl-tRNA synthetase; PFAM: tRNA synthetase class II (G H P and S); Anticodon-binding domain protein; PRIAM: Histidine--tRNA ligase; SPTR: Histidyl-tRNA synthetase; TIGRFAM: histidyl-tRNA synthetase; PFAM: Anticodon binding domain; tRNA synthetase class II core domain (G, H, P, S and T); TIGRFAM: 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. | 0.889 |
| ADU48357.1 | gltX | Intca_1845 | Intca_2337 | COGs: COG0124 Histidyl-tRNA synthetase; InterProIPR006195: IPR004516: IPR002314: IPR004154: IPR 015807; KEGG: kfl:Kfla_4391 histidyl-tRNA synthetase; PFAM: tRNA synthetase class II (G H P and S); Anticodon-binding domain protein; PRIAM: Histidine--tRNA ligase; SPTR: Histidyl-tRNA synthetase; TIGRFAM: histidyl-tRNA synthetase; PFAM: Anticodon binding domain; tRNA synthetase class II core domain (G, H, P, S and T); TIGRFAM: 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); Belongs to the class-I aminoacyl-tRNA synthetase family. Glutamate--tRNA ligase type 1 subfamily. | 0.577 |
| ADU48357.1 | glyQ | Intca_1845 | Intca_0538 | COGs: COG0124 Histidyl-tRNA synthetase; InterProIPR006195: IPR004516: IPR002314: IPR004154: IPR 015807; KEGG: kfl:Kfla_4391 histidyl-tRNA synthetase; PFAM: tRNA synthetase class II (G H P and S); Anticodon-binding domain protein; PRIAM: Histidine--tRNA ligase; SPTR: Histidyl-tRNA synthetase; TIGRFAM: histidyl-tRNA synthetase; PFAM: Anticodon binding domain; tRNA synthetase class II core domain (G, H, P, S and T); TIGRFAM: histidyl-tRNA synthetase. | COGs: COG0751 Glycyl-tRNA synthetase beta subunit; InterPro IPR006194: IPR002310: IPR002311: IPR015944; KEGG: kfl:Kfla_5824 glycyl-tRNA synthetase, beta subunit; PFAM: glycyl-tRNA synthetase alpha subunit; glycyl-tRNA synthetase beta subunit; PRIAM: Glycine--tRNA ligase; SPTR: Glycyl-tRNA synthetase, beta subunit; TIGRFAM: glycyl-tRNA synthetase, beta subunit; glycyl-tRNA synthetase, alpha subunit; PFAM: Glycyl-tRNA synthetase beta subunit; Glycyl-tRNA synthetase alpha subunit; TIGRFAM: glycyl-tRNA synthetase, tetrameric type, beta subunit; glycyl-tRNA synthetase, tetrameric type, alph [...] | 0.920 |
| ADU48357.1 | guaA | Intca_1845 | Intca_1035 | COGs: COG0124 Histidyl-tRNA synthetase; InterProIPR006195: IPR004516: IPR002314: IPR004154: IPR 015807; KEGG: kfl:Kfla_4391 histidyl-tRNA synthetase; PFAM: tRNA synthetase class II (G H P and S); Anticodon-binding domain protein; PRIAM: Histidine--tRNA ligase; SPTR: Histidyl-tRNA synthetase; TIGRFAM: histidyl-tRNA synthetase; PFAM: Anticodon binding domain; tRNA synthetase class II core domain (G, H, P, S and T); TIGRFAM: histidyl-tRNA synthetase. | GMP synthase (glutamine-hydrolyzing); Catalyzes the synthesis of GMP from XMP. | 0.768 |
| ADU48357.1 | pheT | Intca_1845 | Intca_1553 | COGs: COG0124 Histidyl-tRNA synthetase; InterProIPR006195: IPR004516: IPR002314: IPR004154: IPR 015807; KEGG: kfl:Kfla_4391 histidyl-tRNA synthetase; PFAM: tRNA synthetase class II (G H P and S); Anticodon-binding domain protein; PRIAM: Histidine--tRNA ligase; SPTR: Histidyl-tRNA synthetase; TIGRFAM: histidyl-tRNA synthetase; PFAM: Anticodon binding domain; tRNA synthetase class II core domain (G, H, P, S and T); TIGRFAM: histidyl-tRNA synthetase. | COGs: COG0072 Phenylalanyl-tRNA synthetase beta subunit; InterProIPR002547: IPR005121: IPR004532: IPR005146: IPR 005147; KEGG: kra:Krad_3163 phenylalanyl-tRNA synthetase, beta subunit; PFAM: B3/4 domain protein; t-RNA-binding domain-containing protein; tRNA synthetase B5; ferredoxin-fold anticodon-binding; SPTR: Phenylalanyl-tRNA synthetase beta subunit; TIGRFAM: phenylalanyl-tRNA synthetase, beta subunit; PFAM: tRNA synthetase B5 domain; Ferredoxin-fold anticodon binding domain; B3/4 domain; Putative tRNA binding domain; TIGRFAM: phenylalanyl-tRNA synthetase, beta subunit, non-spiroch [...] | 0.728 |
| ADU48357.1 | valS | Intca_1845 | Intca_1383 | COGs: COG0124 Histidyl-tRNA synthetase; InterProIPR006195: IPR004516: IPR002314: IPR004154: IPR 015807; KEGG: kfl:Kfla_4391 histidyl-tRNA synthetase; PFAM: tRNA synthetase class II (G H P and S); Anticodon-binding domain protein; PRIAM: Histidine--tRNA ligase; SPTR: Histidyl-tRNA synthetase; TIGRFAM: histidyl-tRNA synthetase; PFAM: Anticodon binding domain; tRNA synthetase class II core domain (G, H, P, S and T); TIGRFAM: histidyl-tRNA synthetase. | 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. | 0.825 |
| alaS | ADU48357.1 | Intca_1587 | Intca_1845 | 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. | COGs: COG0124 Histidyl-tRNA synthetase; InterProIPR006195: IPR004516: IPR002314: IPR004154: IPR 015807; KEGG: kfl:Kfla_4391 histidyl-tRNA synthetase; PFAM: tRNA synthetase class II (G H P and S); Anticodon-binding domain protein; PRIAM: Histidine--tRNA ligase; SPTR: Histidyl-tRNA synthetase; TIGRFAM: histidyl-tRNA synthetase; PFAM: Anticodon binding domain; tRNA synthetase class II core domain (G, H, P, S and T); TIGRFAM: histidyl-tRNA synthetase. | 0.687 |
| alaS | aspS | Intca_1587 | Intca_0647 | 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 2 subfamily. | 0.510 |
| alaS | aspS-2 | Intca_1587 | Intca_1578 | 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. | 0.858 |
| alaS | gatB | Intca_1587 | Intca_2374 | 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/glutamyl-tRNA(Asn/Gln) amidotransferase subunit B; 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. | 0.509 |
| alaS | gltX | Intca_1587 | Intca_2337 | 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); Belongs to the class-I aminoacyl-tRNA synthetase family. Glutamate--tRNA ligase type 1 subfamily. | 0.661 |
| alaS | glyQ | Intca_1587 | Intca_0538 | 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. | COGs: COG0751 Glycyl-tRNA synthetase beta subunit; InterPro IPR006194: IPR002310: IPR002311: IPR015944; KEGG: kfl:Kfla_5824 glycyl-tRNA synthetase, beta subunit; PFAM: glycyl-tRNA synthetase alpha subunit; glycyl-tRNA synthetase beta subunit; PRIAM: Glycine--tRNA ligase; SPTR: Glycyl-tRNA synthetase, beta subunit; TIGRFAM: glycyl-tRNA synthetase, beta subunit; glycyl-tRNA synthetase, alpha subunit; PFAM: Glycyl-tRNA synthetase beta subunit; Glycyl-tRNA synthetase alpha subunit; TIGRFAM: glycyl-tRNA synthetase, tetrameric type, beta subunit; glycyl-tRNA synthetase, tetrameric type, alph [...] | 0.966 |
| alaS | guaA | Intca_1587 | Intca_1035 | 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. | 0.703 |
| alaS | pheT | Intca_1587 | Intca_1553 | 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. | COGs: COG0072 Phenylalanyl-tRNA synthetase beta subunit; InterProIPR002547: IPR005121: IPR004532: IPR005146: IPR 005147; KEGG: kra:Krad_3163 phenylalanyl-tRNA synthetase, beta subunit; PFAM: B3/4 domain protein; t-RNA-binding domain-containing protein; tRNA synthetase B5; ferredoxin-fold anticodon-binding; SPTR: Phenylalanyl-tRNA synthetase beta subunit; TIGRFAM: phenylalanyl-tRNA synthetase, beta subunit; PFAM: tRNA synthetase B5 domain; Ferredoxin-fold anticodon binding domain; B3/4 domain; Putative tRNA binding domain; TIGRFAM: phenylalanyl-tRNA synthetase, beta subunit, non-spiroch [...] | 0.964 |
| alaS | valS | Intca_1587 | Intca_1383 | 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. | 0.834 |
| aspS | alaS | Intca_0647 | Intca_1587 | 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 2 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. | 0.510 |
| aspS | aspS-2 | Intca_0647 | Intca_1578 | 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 2 subfamily. | 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. | 0.939 |
| aspS | gatB | Intca_0647 | Intca_2374 | 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 2 subfamily. | aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit B; 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. | 0.991 |
| aspS | gatC | Intca_0647 | Intca_2376 | 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 2 subfamily. | aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit C; 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 GatC family. | 0.953 |