| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| alaS | argS | Metli_1605 | Metli_0346 | 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; PFAM: DALR anticodon binding domain; Arginyl tRNA synthetase N terminal domain; tRNA synthetases class I (R); TIGRFAM: arginyl-tRNA synthetase; COGs: COG0018 Arginyl-tRNA synthetase; HAMAP: Arginyl-tRNA synthetase, class Ic; InterPro IPR001278:IPR005148:IPR015945:IPR008909; KEGG: mem:Memar_2213 arginyl-tRNA synthetase; PFAM: DALR anticodon binding; Arginyl-tRNA synthetase, class Ic, core; Arginyl tRNA synthetase, class Ic, N-terminal; SPTR: Arginyl-tRNA synthetase; TIGRFAM: Arginyl-tRNA synthetase, class Ic; Belongs to the class-I aminoacyl-tRNA synthetase family. | 0.754 |
| alaS | aspS | Metli_1605 | Metli_0373 | 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). | 0.738 |
| alaS | gltX | Metli_1605 | Metli_0610 | 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). | 0.725 |
| alaS | ileS | Metli_1605 | Metli_2138 | 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. | 0.969 |
| alaS | leuS | Metli_1605 | Metli_1768 | 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. | PFAM: tRNA synthetases class I (I, L, M and V); tRNA synthetases class I (M); Anticodon-binding domain; TIGRFAM: leucyl-tRNA synthetase, archaeal and cytosolic family; COGs: COG0495 Leucyl-tRNA synthetase; InterPro IPR004493:IPR015413:IPR013155; KEGG: mem:Memar_2008 leucyl-tRNA synthetase; PFAM: Valyl/Leucyl/Isoleucyl-tRNA synthetase, class I, anticodon-binding; Aminoacyl-tRNA synthetase, class I (M); SPTR: Leucyl-tRNA synthetase; TIGRFAM: Leucyl-tRNA synthetase, class Ia, archaeal/eukaryotic cytosolic. | 0.968 |
| alaS | lysS | Metli_1605 | Metli_1483 | 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. | PFAM: tRNA synthetases class II (D, K and N); OB-fold nucleic acid binding domain; TIGRFAM: lysyl-tRNA synthetase, eukaryotic and non-spirochete bacterial; COGs: COG1190 Lysyl-tRNA synthetase (class II); HAMAP: Lysyl-tRNA synthetase; InterPro IPR002313:IPR004365:IPR004364; KEGG: mem:Memar_2341 lysyl-tRNA synthetase; PFAM: Aminoacyl-tRNA synthetase, class II (D/K/N); Nucleic acid binding, OB-fold, tRNA/helicase-type; SPTR: Lysyl-tRNA synthetase; TIGRFAM: Lysyl-tRNA synthetase, class II; Belongs to the class-II aminoacyl-tRNA synthetase family. | 0.640 |
| alaS | metG | Metli_1605 | Metli_1761 | 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; Is required not only for elongation of protein synthesis but also for the initiation of all mRNA translation through initiator tRNA(fMet) aminoacylation. | 0.845 |
| alaS | pheT | Metli_1605 | Metli_0550 | 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; PFAM: tRNA synthetases class II core domain (F); tRNA synthetase B5 domain; B3/4 domain; TIGRFAM: phenylalanyl-tRNA synthetase, beta subunit; COGs: COG0072 Phenylalanyl-tRNA synthetase beta subunit; HAMAP: Phenylalanyl-tRNA synthetase beta chain; InterPro IPR004531:IPR005146:IPR005147; KEGG: mem:Memar_0644 phenylalanyl-tRNA synthetase subunit beta; PFAM: tRNA synthetase, B5; B3/B4 tRNA-binding domain; SPTR: Phenylalanyl-tRNA synthetase beta chain; TIGRFAM: Phenylalanyl-tRNA synthetase, class IIc, beta subunit, archae/euk cytosolic. | 0.722 |
| alaS | proS | Metli_1605 | Metli_1933 | 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; 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). | 0.800 |
| alaS | valS | Metli_1605 | Metli_0854 | 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 2 subfamily. | 0.936 |
| argS | alaS | Metli_0346 | Metli_1605 | Arginyl-tRNA synthetase; PFAM: DALR anticodon binding domain; Arginyl tRNA synthetase N terminal domain; tRNA synthetases class I (R); TIGRFAM: arginyl-tRNA synthetase; COGs: COG0018 Arginyl-tRNA synthetase; HAMAP: Arginyl-tRNA synthetase, class Ic; InterPro IPR001278:IPR005148:IPR015945:IPR008909; KEGG: mem:Memar_2213 arginyl-tRNA synthetase; PFAM: DALR anticodon binding; Arginyl-tRNA synthetase, class Ic, core; Arginyl tRNA synthetase, class Ic, N-terminal; SPTR: Arginyl-tRNA synthetase; TIGRFAM: Arginyl-tRNA synthetase, class Ic; 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. | 0.754 |
| argS | aspS | Metli_0346 | Metli_0373 | Arginyl-tRNA synthetase; PFAM: DALR anticodon binding domain; Arginyl tRNA synthetase N terminal domain; tRNA synthetases class I (R); TIGRFAM: arginyl-tRNA synthetase; COGs: COG0018 Arginyl-tRNA synthetase; HAMAP: Arginyl-tRNA synthetase, class Ic; InterPro IPR001278:IPR005148:IPR015945:IPR008909; KEGG: mem:Memar_2213 arginyl-tRNA synthetase; PFAM: DALR anticodon binding; Arginyl-tRNA synthetase, class Ic, core; Arginyl tRNA synthetase, class Ic, N-terminal; SPTR: Arginyl-tRNA synthetase; TIGRFAM: Arginyl-tRNA synthetase, class Ic; Belongs to the class-I aminoacyl-tRNA synthetase family. | 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). | 0.979 |
| argS | gltX | Metli_0346 | Metli_0610 | Arginyl-tRNA synthetase; PFAM: DALR anticodon binding domain; Arginyl tRNA synthetase N terminal domain; tRNA synthetases class I (R); TIGRFAM: arginyl-tRNA synthetase; COGs: COG0018 Arginyl-tRNA synthetase; HAMAP: Arginyl-tRNA synthetase, class Ic; InterPro IPR001278:IPR005148:IPR015945:IPR008909; KEGG: mem:Memar_2213 arginyl-tRNA synthetase; PFAM: DALR anticodon binding; Arginyl-tRNA synthetase, class Ic, core; Arginyl tRNA synthetase, class Ic, N-terminal; SPTR: Arginyl-tRNA synthetase; TIGRFAM: Arginyl-tRNA synthetase, class Ic; Belongs to the class-I aminoacyl-tRNA synthetase family. | 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). | 0.992 |
| argS | ileS | Metli_0346 | Metli_2138 | Arginyl-tRNA synthetase; PFAM: DALR anticodon binding domain; Arginyl tRNA synthetase N terminal domain; tRNA synthetases class I (R); TIGRFAM: arginyl-tRNA synthetase; COGs: COG0018 Arginyl-tRNA synthetase; HAMAP: Arginyl-tRNA synthetase, class Ic; InterPro IPR001278:IPR005148:IPR015945:IPR008909; KEGG: mem:Memar_2213 arginyl-tRNA synthetase; PFAM: DALR anticodon binding; Arginyl-tRNA synthetase, class Ic, core; Arginyl tRNA synthetase, class Ic, N-terminal; SPTR: Arginyl-tRNA synthetase; TIGRFAM: Arginyl-tRNA synthetase, class Ic; Belongs to the class-I aminoacyl-tRNA synthetase family. | 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. | 0.996 |
| argS | leuS | Metli_0346 | Metli_1768 | Arginyl-tRNA synthetase; PFAM: DALR anticodon binding domain; Arginyl tRNA synthetase N terminal domain; tRNA synthetases class I (R); TIGRFAM: arginyl-tRNA synthetase; COGs: COG0018 Arginyl-tRNA synthetase; HAMAP: Arginyl-tRNA synthetase, class Ic; InterPro IPR001278:IPR005148:IPR015945:IPR008909; KEGG: mem:Memar_2213 arginyl-tRNA synthetase; PFAM: DALR anticodon binding; Arginyl-tRNA synthetase, class Ic, core; Arginyl tRNA synthetase, class Ic, N-terminal; SPTR: Arginyl-tRNA synthetase; TIGRFAM: Arginyl-tRNA synthetase, class Ic; Belongs to the class-I aminoacyl-tRNA synthetase family. | PFAM: tRNA synthetases class I (I, L, M and V); tRNA synthetases class I (M); Anticodon-binding domain; TIGRFAM: leucyl-tRNA synthetase, archaeal and cytosolic family; COGs: COG0495 Leucyl-tRNA synthetase; InterPro IPR004493:IPR015413:IPR013155; KEGG: mem:Memar_2008 leucyl-tRNA synthetase; PFAM: Valyl/Leucyl/Isoleucyl-tRNA synthetase, class I, anticodon-binding; Aminoacyl-tRNA synthetase, class I (M); SPTR: Leucyl-tRNA synthetase; TIGRFAM: Leucyl-tRNA synthetase, class Ia, archaeal/eukaryotic cytosolic. | 0.991 |
| argS | lysS | Metli_0346 | Metli_1483 | Arginyl-tRNA synthetase; PFAM: DALR anticodon binding domain; Arginyl tRNA synthetase N terminal domain; tRNA synthetases class I (R); TIGRFAM: arginyl-tRNA synthetase; COGs: COG0018 Arginyl-tRNA synthetase; HAMAP: Arginyl-tRNA synthetase, class Ic; InterPro IPR001278:IPR005148:IPR015945:IPR008909; KEGG: mem:Memar_2213 arginyl-tRNA synthetase; PFAM: DALR anticodon binding; Arginyl-tRNA synthetase, class Ic, core; Arginyl tRNA synthetase, class Ic, N-terminal; SPTR: Arginyl-tRNA synthetase; TIGRFAM: Arginyl-tRNA synthetase, class Ic; Belongs to the class-I aminoacyl-tRNA synthetase family. | PFAM: tRNA synthetases class II (D, K and N); OB-fold nucleic acid binding domain; TIGRFAM: lysyl-tRNA synthetase, eukaryotic and non-spirochete bacterial; COGs: COG1190 Lysyl-tRNA synthetase (class II); HAMAP: Lysyl-tRNA synthetase; InterPro IPR002313:IPR004365:IPR004364; KEGG: mem:Memar_2341 lysyl-tRNA synthetase; PFAM: Aminoacyl-tRNA synthetase, class II (D/K/N); Nucleic acid binding, OB-fold, tRNA/helicase-type; SPTR: Lysyl-tRNA synthetase; TIGRFAM: Lysyl-tRNA synthetase, class II; Belongs to the class-II aminoacyl-tRNA synthetase family. | 0.993 |
| argS | metG | Metli_0346 | Metli_1761 | Arginyl-tRNA synthetase; PFAM: DALR anticodon binding domain; Arginyl tRNA synthetase N terminal domain; tRNA synthetases class I (R); TIGRFAM: arginyl-tRNA synthetase; COGs: COG0018 Arginyl-tRNA synthetase; HAMAP: Arginyl-tRNA synthetase, class Ic; InterPro IPR001278:IPR005148:IPR015945:IPR008909; KEGG: mem:Memar_2213 arginyl-tRNA synthetase; PFAM: DALR anticodon binding; Arginyl-tRNA synthetase, class Ic, core; Arginyl tRNA synthetase, class Ic, N-terminal; SPTR: Arginyl-tRNA synthetase; TIGRFAM: Arginyl-tRNA synthetase, class Ic; Belongs to the class-I aminoacyl-tRNA synthetase family. | 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. | 0.994 |
| argS | pheT | Metli_0346 | Metli_0550 | Arginyl-tRNA synthetase; PFAM: DALR anticodon binding domain; Arginyl tRNA synthetase N terminal domain; tRNA synthetases class I (R); TIGRFAM: arginyl-tRNA synthetase; COGs: COG0018 Arginyl-tRNA synthetase; HAMAP: Arginyl-tRNA synthetase, class Ic; InterPro IPR001278:IPR005148:IPR015945:IPR008909; KEGG: mem:Memar_2213 arginyl-tRNA synthetase; PFAM: DALR anticodon binding; Arginyl-tRNA synthetase, class Ic, core; Arginyl tRNA synthetase, class Ic, N-terminal; SPTR: Arginyl-tRNA synthetase; TIGRFAM: Arginyl-tRNA synthetase, class Ic; Belongs to the class-I aminoacyl-tRNA synthetase family. | Phenylalanyl-tRNA synthetase beta chain; PFAM: tRNA synthetases class II core domain (F); tRNA synthetase B5 domain; B3/4 domain; TIGRFAM: phenylalanyl-tRNA synthetase, beta subunit; COGs: COG0072 Phenylalanyl-tRNA synthetase beta subunit; HAMAP: Phenylalanyl-tRNA synthetase beta chain; InterPro IPR004531:IPR005146:IPR005147; KEGG: mem:Memar_0644 phenylalanyl-tRNA synthetase subunit beta; PFAM: tRNA synthetase, B5; B3/B4 tRNA-binding domain; SPTR: Phenylalanyl-tRNA synthetase beta chain; TIGRFAM: Phenylalanyl-tRNA synthetase, class IIc, beta subunit, archae/euk cytosolic. | 0.799 |
| argS | proS | Metli_0346 | Metli_1933 | Arginyl-tRNA synthetase; PFAM: DALR anticodon binding domain; Arginyl tRNA synthetase N terminal domain; tRNA synthetases class I (R); TIGRFAM: arginyl-tRNA synthetase; COGs: COG0018 Arginyl-tRNA synthetase; HAMAP: Arginyl-tRNA synthetase, class Ic; InterPro IPR001278:IPR005148:IPR015945:IPR008909; KEGG: mem:Memar_2213 arginyl-tRNA synthetase; PFAM: DALR anticodon binding; Arginyl-tRNA synthetase, class Ic, core; Arginyl tRNA synthetase, class Ic, N-terminal; SPTR: Arginyl-tRNA synthetase; TIGRFAM: Arginyl-tRNA synthetase, class Ic; Belongs to the class-I aminoacyl-tRNA synthetase family. | Prolyl-tRNA synthetase; 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). | 0.971 |
| argS | valS | Metli_0346 | Metli_0854 | Arginyl-tRNA synthetase; PFAM: DALR anticodon binding domain; Arginyl tRNA synthetase N terminal domain; tRNA synthetases class I (R); TIGRFAM: arginyl-tRNA synthetase; COGs: COG0018 Arginyl-tRNA synthetase; HAMAP: Arginyl-tRNA synthetase, class Ic; InterPro IPR001278:IPR005148:IPR015945:IPR008909; KEGG: mem:Memar_2213 arginyl-tRNA synthetase; PFAM: DALR anticodon binding; Arginyl-tRNA synthetase, class Ic, core; Arginyl tRNA synthetase, class Ic, N-terminal; SPTR: Arginyl-tRNA synthetase; TIGRFAM: Arginyl-tRNA synthetase, class Ic; Belongs to the class-I aminoacyl-tRNA synthetase family. | 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 2 subfamily. | 0.942 |