| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| AEB84351.1 | alaS | Alide2_1976 | Alide2_2899 | Ribosomal protein S1; Binds mRNA; thus facilitating recognition of the initiation point. It is needed to translate mRNA with a short Shine-Dalgarno (SD) purine-rich sequence. | 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. | 0.511 |
| AEB84351.1 | leuS | Alide2_1976 | Alide2_4464 | Ribosomal protein S1; Binds mRNA; thus facilitating recognition of the initiation point. It is needed to translate mRNA with a short Shine-Dalgarno (SD) purine-rich sequence. | TIGRFAM: Leucyl-tRNA synthetase, class Ia, bacterial/mitochondrial; KEGG: ajs:Ajs_3917 leucyl-tRNA synthetase; Belongs to the class-I aminoacyl-tRNA synthetase family. | 0.493 |
| AEB84351.1 | lysS | Alide2_1976 | Alide2_1287 | Ribosomal protein S1; Binds mRNA; thus facilitating recognition of the initiation point. It is needed to translate mRNA with a short Shine-Dalgarno (SD) purine-rich sequence. | TIGRFAM: Lysyl-tRNA synthetase, class II; KEGG: ajs:Ajs_3250 lysyl-tRNA synthetase; PFAM: Aminoacyl-tRNA synthetase, class II (D/K/N); Nucleic acid binding, OB-fold, tRNA/helicase-type; Belongs to the class-II aminoacyl-tRNA synthetase family. | 0.646 |
| AEB84351.1 | metG | Alide2_1976 | Alide2_1030 | Ribosomal protein S1; Binds mRNA; thus facilitating recognition of the initiation point. It is needed to translate mRNA with a short Shine-Dalgarno (SD) purine-rich sequence. | 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. | 0.663 |
| AEB84351.1 | pheT | Alide2_1976 | Alide2_2825 | Ribosomal protein S1; Binds mRNA; thus facilitating recognition of the initiation point. It is needed to translate mRNA with a short Shine-Dalgarno (SD) purine-rich sequence. | TIGRFAM: Phenylalanyl-tRNA synthetase, class IIc, beta subunit, bacterial; KEGG: ajs:Ajs_2395 phenylalanyl-tRNA synthetase subunit beta; HAMAP: Phenylalanyl-tRNA synthetase, class IIc, beta subunit, bacterial; Belongs to the phenylalanyl-tRNA synthetase beta subunit family. Type 1 subfamily. | 0.738 |
| AEB84351.1 | rplT | Alide2_1976 | Alide2_2827 | Ribosomal protein S1; Binds mRNA; thus facilitating recognition of the initiation point. It is needed to translate mRNA with a short Shine-Dalgarno (SD) purine-rich sequence. | 50S ribosomal protein L20; Binds directly to 23S ribosomal RNA and is necessary for the in vitro assembly process of the 50S ribosomal subunit. It is not involved in the protein synthesizing functions of that subunit. | 0.942 |
| AEB84351.1 | rpmA | Alide2_1976 | Alide2_0890 | Ribosomal protein S1; Binds mRNA; thus facilitating recognition of the initiation point. It is needed to translate mRNA with a short Shine-Dalgarno (SD) purine-rich sequence. | TIGRFAM: Ribosomal protein L27; HAMAP: Ribosomal protein L27; KEGG: dia:Dtpsy_0771 50S ribosomal protein L27; PFAM: Ribosomal protein L27; Belongs to the bacterial ribosomal protein bL27 family. | 0.969 |
| AEB84351.1 | thrS | Alide2_1976 | Alide2_2830 | Ribosomal protein S1; Binds mRNA; thus facilitating recognition of the initiation point. It is needed to translate mRNA with a short Shine-Dalgarno (SD) purine-rich sequence. | threonyl-tRNA synthetase; 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). | 0.846 |
| AEB84351.1 | valS | Alide2_1976 | Alide2_1639 | Ribosomal protein S1; Binds mRNA; thus facilitating recognition of the initiation point. It is needed to translate mRNA with a short Shine-Dalgarno (SD) purine-rich sequence. | 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. | 0.739 |
| alaS | AEB84351.1 | Alide2_2899 | Alide2_1976 | 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. | Ribosomal protein S1; Binds mRNA; thus facilitating recognition of the initiation point. It is needed to translate mRNA with a short Shine-Dalgarno (SD) purine-rich sequence. | 0.511 |
| alaS | leuS | Alide2_2899 | Alide2_4464 | 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. | TIGRFAM: Leucyl-tRNA synthetase, class Ia, bacterial/mitochondrial; KEGG: ajs:Ajs_3917 leucyl-tRNA synthetase; Belongs to the class-I aminoacyl-tRNA synthetase family. | 0.882 |
| alaS | lysS | Alide2_2899 | Alide2_1287 | 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. | TIGRFAM: Lysyl-tRNA synthetase, class II; KEGG: ajs:Ajs_3250 lysyl-tRNA synthetase; PFAM: Aminoacyl-tRNA synthetase, class II (D/K/N); Nucleic acid binding, OB-fold, tRNA/helicase-type; Belongs to the class-II aminoacyl-tRNA synthetase family. | 0.662 |
| alaS | metG | Alide2_2899 | Alide2_1030 | 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. | 0.882 |
| alaS | pheT | Alide2_2899 | Alide2_2825 | 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. | TIGRFAM: Phenylalanyl-tRNA synthetase, class IIc, beta subunit, bacterial; KEGG: ajs:Ajs_2395 phenylalanyl-tRNA synthetase subunit beta; HAMAP: Phenylalanyl-tRNA synthetase, class IIc, beta subunit, bacterial; Belongs to the phenylalanyl-tRNA synthetase beta subunit family. Type 1 subfamily. | 0.948 |
| alaS | thrS | Alide2_2899 | Alide2_2830 | 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. | threonyl-tRNA synthetase; 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). | 0.891 |
| alaS | valS | Alide2_2899 | Alide2_1639 | 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. | 0.906 |
| leuS | AEB84351.1 | Alide2_4464 | Alide2_1976 | TIGRFAM: Leucyl-tRNA synthetase, class Ia, bacterial/mitochondrial; KEGG: ajs:Ajs_3917 leucyl-tRNA synthetase; Belongs to the class-I aminoacyl-tRNA synthetase family. | Ribosomal protein S1; Binds mRNA; thus facilitating recognition of the initiation point. It is needed to translate mRNA with a short Shine-Dalgarno (SD) purine-rich sequence. | 0.493 |
| leuS | alaS | Alide2_4464 | Alide2_2899 | TIGRFAM: Leucyl-tRNA synthetase, class Ia, bacterial/mitochondrial; KEGG: ajs:Ajs_3917 leucyl-tRNA synthetase; 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. | 0.882 |
| leuS | lysS | Alide2_4464 | Alide2_1287 | TIGRFAM: Leucyl-tRNA synthetase, class Ia, bacterial/mitochondrial; KEGG: ajs:Ajs_3917 leucyl-tRNA synthetase; Belongs to the class-I aminoacyl-tRNA synthetase family. | TIGRFAM: Lysyl-tRNA synthetase, class II; KEGG: ajs:Ajs_3250 lysyl-tRNA synthetase; PFAM: Aminoacyl-tRNA synthetase, class II (D/K/N); Nucleic acid binding, OB-fold, tRNA/helicase-type; Belongs to the class-II aminoacyl-tRNA synthetase family. | 0.945 |
| leuS | metG | Alide2_4464 | Alide2_1030 | TIGRFAM: Leucyl-tRNA synthetase, class Ia, bacterial/mitochondrial; KEGG: ajs:Ajs_3917 leucyl-tRNA synthetase; 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. | 0.989 |