| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| ADY52974.1 | alaS | Pedsa_2427 | Pedsa_1387 | COGs: COG0172 Seryl-tRNA synthetase; InterPro IPR006195: IPR 015866: IPR 002314: IPR 018156: IPR 002317; KEGG: phe:Phep_0415 seryl-tRNA synthetase; PFAM: tRNA synthetase class II (G H P and S); Seryl-tRNA synthetase, class IIa-like; PRIAM: Serine--tRNA ligase; SPTR: Serine-tRNA synthetase; TIGRFAM: seryl-tRNA synthetase; PFAM: Seryl-tRNA synthetase N-terminal domain; tRNA synthetase class II core domain (G, H, P, S and T); TIGRFAM: seryl-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. | 0.636 |
| ADY52974.1 | argS | Pedsa_2427 | Pedsa_0767 | COGs: COG0172 Seryl-tRNA synthetase; InterPro IPR006195: IPR 015866: IPR 002314: IPR 018156: IPR 002317; KEGG: phe:Phep_0415 seryl-tRNA synthetase; PFAM: tRNA synthetase class II (G H P and S); Seryl-tRNA synthetase, class IIa-like; PRIAM: Serine--tRNA ligase; SPTR: Serine-tRNA synthetase; TIGRFAM: seryl-tRNA synthetase; PFAM: Seryl-tRNA synthetase N-terminal domain; tRNA synthetase class II core domain (G, H, P, S and T); TIGRFAM: seryl-tRNA synthetase. | COGs: COG0018 Arginyl-tRNA synthetase; InterPro IPR015945: IPR 001412: IPR 001278: IPR 005148: IPR 008909; KEGG: phe:Phep_2318 arginyl-tRNA synthetase; PFAM: DALR anticodon binding domain protein; Arginyl-tRNA synthetase, class Ic, core; arginyl tRNA synthetase domain protein; PRIAM: Arginine--tRNA ligase; SPTR: Arginine--tRNA ligase; TIGRFAM: arginyl-tRNA synthetase; PFAM: DALR anticodon binding domain; Arginyl tRNA synthetase N terminal domain; tRNA synthetases class I (R); TIGRFAM: arginyl-tRNA synthetase. | 0.708 |
| ADY52974.1 | aspS | Pedsa_2427 | Pedsa_3014 | COGs: COG0172 Seryl-tRNA synthetase; InterPro IPR006195: IPR 015866: IPR 002314: IPR 018156: IPR 002317; KEGG: phe:Phep_0415 seryl-tRNA synthetase; PFAM: tRNA synthetase class II (G H P and S); Seryl-tRNA synthetase, class IIa-like; PRIAM: Serine--tRNA ligase; SPTR: Serine-tRNA synthetase; TIGRFAM: seryl-tRNA synthetase; PFAM: Seryl-tRNA synthetase N-terminal domain; tRNA synthetase class II core domain (G, H, P, S and T); TIGRFAM: seryl-tRNA synthetase. | aspartyl-tRNA synthetase; Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp- AMP and then transferred to the acceptor end of tRNA(Asp). Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily. | 0.508 |
| ADY52974.1 | guaA | Pedsa_2427 | Pedsa_1938 | COGs: COG0172 Seryl-tRNA synthetase; InterPro IPR006195: IPR 015866: IPR 002314: IPR 018156: IPR 002317; KEGG: phe:Phep_0415 seryl-tRNA synthetase; PFAM: tRNA synthetase class II (G H P and S); Seryl-tRNA synthetase, class IIa-like; PRIAM: Serine--tRNA ligase; SPTR: Serine-tRNA synthetase; TIGRFAM: seryl-tRNA synthetase; PFAM: Seryl-tRNA synthetase N-terminal domain; tRNA synthetase class II core domain (G, H, P, S and T); TIGRFAM: seryl-tRNA synthetase. | GMP synthase, large subunit; Catalyzes the synthesis of GMP from XMP. | 0.527 |
| ADY52974.1 | leuS | Pedsa_2427 | Pedsa_0250 | COGs: COG0172 Seryl-tRNA synthetase; InterPro IPR006195: IPR 015866: IPR 002314: IPR 018156: IPR 002317; KEGG: phe:Phep_0415 seryl-tRNA synthetase; PFAM: tRNA synthetase class II (G H P and S); Seryl-tRNA synthetase, class IIa-like; PRIAM: Serine--tRNA ligase; SPTR: Serine-tRNA synthetase; TIGRFAM: seryl-tRNA synthetase; PFAM: Seryl-tRNA synthetase N-terminal domain; tRNA synthetase class II core domain (G, H, P, S and T); TIGRFAM: seryl-tRNA synthetase. | COGs: COG0495 Leucyl-tRNA synthetase; InterPro IPR002302: IPR 015413: IPR 013155: IPR 001412; KEGG: phe:Phep_3538 leucyl-tRNA synthetase; PFAM: tRNA synthetase class I (M); tRNA synthetase valyl/leucyl anticodon-binding; SPTR: Leucyl-tRNA synthetase; TIGRFAM: leucyl-tRNA synthetase; PFAM: tRNA synthetases class I (I, L, M and V); Anticodon-binding domain; tRNA synthetases class I (M); TIGRFAM: leucyl-tRNA synthetase, eubacterial and mitochondrial family; Belongs to the class-I aminoacyl-tRNA synthetase family. | 0.402 |
| ADY52974.1 | lysS | Pedsa_2427 | Pedsa_1535 | COGs: COG0172 Seryl-tRNA synthetase; InterPro IPR006195: IPR 015866: IPR 002314: IPR 018156: IPR 002317; KEGG: phe:Phep_0415 seryl-tRNA synthetase; PFAM: tRNA synthetase class II (G H P and S); Seryl-tRNA synthetase, class IIa-like; PRIAM: Serine--tRNA ligase; SPTR: Serine-tRNA synthetase; TIGRFAM: seryl-tRNA synthetase; PFAM: Seryl-tRNA synthetase N-terminal domain; tRNA synthetase class II core domain (G, H, P, S and T); TIGRFAM: seryl-tRNA synthetase. | COGs: COG1190 Lysyl-tRNA synthetase (class II); InterPro IPR018149: IPR 002313: IPR 004365: IPR 004364: IPR 006195; KEGG: phe:Phep_1559 lysyl-tRNA synthetase; PFAM: tRNA synthetase class II (D K and N); nucleic acid binding OB-fold tRNA/helicase-type; SPTR: Lysyl-tRNA synthetase; TIGRFAM: lysyl-tRNA synthetase; PFAM: tRNA synthetases class II (D, K and N); OB-fold nucleic acid binding domain; TIGRFAM: lysyl-tRNA synthetase, eukaryotic and non-spirochete bacterial; Belongs to the class-II aminoacyl-tRNA synthetase family. | 0.742 |
| ADY52974.1 | thrS | Pedsa_2427 | Pedsa_0430 | COGs: COG0172 Seryl-tRNA synthetase; InterPro IPR006195: IPR 015866: IPR 002314: IPR 018156: IPR 002317; KEGG: phe:Phep_0415 seryl-tRNA synthetase; PFAM: tRNA synthetase class II (G H P and S); Seryl-tRNA synthetase, class IIa-like; PRIAM: Serine--tRNA ligase; SPTR: Serine-tRNA synthetase; TIGRFAM: seryl-tRNA synthetase; PFAM: Seryl-tRNA synthetase N-terminal domain; tRNA synthetase class II core domain (G, H, P, S and T); TIGRFAM: seryl-tRNA synthetase. | Ser-tRNA(Thr) hydrolase; 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). | 0.720 |
| ADY52974.1 | valS | Pedsa_2427 | Pedsa_1504 | COGs: COG0172 Seryl-tRNA synthetase; InterPro IPR006195: IPR 015866: IPR 002314: IPR 018156: IPR 002317; KEGG: phe:Phep_0415 seryl-tRNA synthetase; PFAM: tRNA synthetase class II (G H P and S); Seryl-tRNA synthetase, class IIa-like; PRIAM: Serine--tRNA ligase; SPTR: Serine-tRNA synthetase; TIGRFAM: seryl-tRNA synthetase; PFAM: Seryl-tRNA synthetase N-terminal domain; tRNA synthetase class II core domain (G, H, P, S and T); TIGRFAM: seryl-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; Belongs to the class-I aminoacyl-tRNA synthetase family. ValS type 1 subfamily. | 0.844 |
| alaS | ADY52974.1 | Pedsa_1387 | Pedsa_2427 | 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: COG0172 Seryl-tRNA synthetase; InterPro IPR006195: IPR 015866: IPR 002314: IPR 018156: IPR 002317; KEGG: phe:Phep_0415 seryl-tRNA synthetase; PFAM: tRNA synthetase class II (G H P and S); Seryl-tRNA synthetase, class IIa-like; PRIAM: Serine--tRNA ligase; SPTR: Serine-tRNA synthetase; TIGRFAM: seryl-tRNA synthetase; PFAM: Seryl-tRNA synthetase N-terminal domain; tRNA synthetase class II core domain (G, H, P, S and T); TIGRFAM: seryl-tRNA synthetase. | 0.636 |
| alaS | argS | Pedsa_1387 | Pedsa_0767 | 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: COG0018 Arginyl-tRNA synthetase; InterPro IPR015945: IPR 001412: IPR 001278: IPR 005148: IPR 008909; KEGG: phe:Phep_2318 arginyl-tRNA synthetase; PFAM: DALR anticodon binding domain protein; Arginyl-tRNA synthetase, class Ic, core; arginyl tRNA synthetase domain protein; PRIAM: Arginine--tRNA ligase; SPTR: Arginine--tRNA ligase; TIGRFAM: arginyl-tRNA synthetase; PFAM: DALR anticodon binding domain; Arginyl tRNA synthetase N terminal domain; tRNA synthetases class I (R); TIGRFAM: arginyl-tRNA synthetase. | 0.412 |
| alaS | aspS | Pedsa_1387 | Pedsa_3014 | 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; Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp- AMP and then transferred to the acceptor end of tRNA(Asp). Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily. | 0.835 |
| alaS | guaA | Pedsa_1387 | Pedsa_1938 | 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. | 0.591 |
| alaS | ileS | Pedsa_1387 | Pedsa_2543 | 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. | Isoleucyl-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). Belongs to the class-I aminoacyl-tRNA synthetase family. IleS type 2 subfamily. | 0.819 |
| alaS | leuS | Pedsa_1387 | Pedsa_0250 | 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: COG0495 Leucyl-tRNA synthetase; InterPro IPR002302: IPR 015413: IPR 013155: IPR 001412; KEGG: phe:Phep_3538 leucyl-tRNA synthetase; PFAM: tRNA synthetase class I (M); tRNA synthetase valyl/leucyl anticodon-binding; SPTR: Leucyl-tRNA synthetase; TIGRFAM: leucyl-tRNA synthetase; PFAM: tRNA synthetases class I (I, L, M and V); Anticodon-binding domain; tRNA synthetases class I (M); TIGRFAM: leucyl-tRNA synthetase, eubacterial and mitochondrial family; Belongs to the class-I aminoacyl-tRNA synthetase family. | 0.853 |
| alaS | lysS | Pedsa_1387 | Pedsa_1535 | 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: COG1190 Lysyl-tRNA synthetase (class II); InterPro IPR018149: IPR 002313: IPR 004365: IPR 004364: IPR 006195; KEGG: phe:Phep_1559 lysyl-tRNA synthetase; PFAM: tRNA synthetase class II (D K and N); nucleic acid binding OB-fold tRNA/helicase-type; SPTR: Lysyl-tRNA synthetase; TIGRFAM: lysyl-tRNA synthetase; PFAM: tRNA synthetases class II (D, K and N); OB-fold nucleic acid binding domain; TIGRFAM: lysyl-tRNA synthetase, eukaryotic and non-spirochete bacterial; Belongs to the class-II aminoacyl-tRNA synthetase family. | 0.651 |
| alaS | rpoB | Pedsa_1387 | Pedsa_2264 | 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. | DNA-directed RNA polymerase subunit beta; DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. | 0.499 |
| alaS | thrS | Pedsa_1387 | Pedsa_0430 | 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. | Ser-tRNA(Thr) hydrolase; 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). | 0.812 |
| alaS | valS | Pedsa_1387 | Pedsa_1504 | 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; Belongs to the class-I aminoacyl-tRNA synthetase family. ValS type 1 subfamily. | 0.875 |
| argS | ADY52974.1 | Pedsa_0767 | Pedsa_2427 | COGs: COG0018 Arginyl-tRNA synthetase; InterPro IPR015945: IPR 001412: IPR 001278: IPR 005148: IPR 008909; KEGG: phe:Phep_2318 arginyl-tRNA synthetase; PFAM: DALR anticodon binding domain protein; Arginyl-tRNA synthetase, class Ic, core; arginyl tRNA synthetase domain protein; PRIAM: Arginine--tRNA ligase; SPTR: Arginine--tRNA ligase; TIGRFAM: arginyl-tRNA synthetase; PFAM: DALR anticodon binding domain; Arginyl tRNA synthetase N terminal domain; tRNA synthetases class I (R); TIGRFAM: arginyl-tRNA synthetase. | COGs: COG0172 Seryl-tRNA synthetase; InterPro IPR006195: IPR 015866: IPR 002314: IPR 018156: IPR 002317; KEGG: phe:Phep_0415 seryl-tRNA synthetase; PFAM: tRNA synthetase class II (G H P and S); Seryl-tRNA synthetase, class IIa-like; PRIAM: Serine--tRNA ligase; SPTR: Serine-tRNA synthetase; TIGRFAM: seryl-tRNA synthetase; PFAM: Seryl-tRNA synthetase N-terminal domain; tRNA synthetase class II core domain (G, H, P, S and T); TIGRFAM: seryl-tRNA synthetase. | 0.708 |
| argS | alaS | Pedsa_0767 | Pedsa_1387 | COGs: COG0018 Arginyl-tRNA synthetase; InterPro IPR015945: IPR 001412: IPR 001278: IPR 005148: IPR 008909; KEGG: phe:Phep_2318 arginyl-tRNA synthetase; PFAM: DALR anticodon binding domain protein; Arginyl-tRNA synthetase, class Ic, core; arginyl tRNA synthetase domain protein; PRIAM: Arginine--tRNA ligase; SPTR: Arginine--tRNA ligase; TIGRFAM: arginyl-tRNA synthetase; PFAM: DALR anticodon binding domain; Arginyl tRNA synthetase N terminal domain; tRNA synthetases class I (R); TIGRFAM: arginyl-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. | 0.412 |