| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| Msil_0675 | alaS | Msil_0675 | Msil_3523 | 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. | 0.501 |
| Msil_0675 | leuS | Msil_0675 | Msil_0336 | 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; KEGG: bid:Bind_0225 leucyl-tRNA synthetase; Belongs to the class-I aminoacyl-tRNA synthetase family. | 0.513 |
| Msil_0675 | pheT | Msil_0675 | Msil_1838 | 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. | KEGG: bid:Bind_3247 phenylalanyl-tRNA synthetase, beta subunit; TIGRFAM: phenylalanyl-tRNA synthetase, beta subunit; Belongs to the phenylalanyl-tRNA synthetase beta subunit family. Type 1 subfamily. | 0.739 |
| Msil_0675 | rplT | Msil_0675 | Msil_1836 | 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. | 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. | 0.943 |
| Msil_0675 | rpmA | Msil_0675 | Msil_3282 | 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. | PFAM: ribosomal protein L27; KEGG: bid:Bind_0417 ribosomal protein L27; Belongs to the bacterial ribosomal protein bL27 family. | 0.969 |
| Msil_0675 | thrS | Msil_0675 | Msil_3538 | 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). | 0.812 |
| Msil_0675 | valS | Msil_0675 | Msil_1688 | 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. | 0.673 |
| alaS | Msil_0675 | Msil_3523 | Msil_0675 | 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. | 0.501 |
| alaS | cysS | Msil_3523 | Msil_0135 | 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: bid:Bind_1915 cysteinyl-tRNA synthetase; TIGRFAM: cysteinyl-tRNA synthetase; PFAM: tRNA synthetase class I (M); Cysteinyl-tRNA synthetase class Ia; Belongs to the class-I aminoacyl-tRNA synthetase family. | 0.642 |
| alaS | leuS | Msil_3523 | Msil_0336 | 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; KEGG: bid:Bind_0225 leucyl-tRNA synthetase; Belongs to the class-I aminoacyl-tRNA synthetase family. | 0.850 |
| alaS | metG | Msil_3523 | Msil_0541 | 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; Belongs to the class-I aminoacyl-tRNA synthetase family. MetG type 2B subfamily. | 0.722 |
| alaS | pheT | Msil_3523 | Msil_1838 | 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: bid:Bind_3247 phenylalanyl-tRNA synthetase, beta subunit; TIGRFAM: phenylalanyl-tRNA synthetase, beta subunit; Belongs to the phenylalanyl-tRNA synthetase beta subunit family. Type 1 subfamily. | 0.882 |
| alaS | thrS | Msil_3523 | Msil_3538 | 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). | 0.850 |
| alaS | valS | Msil_3523 | Msil_1688 | 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. | 0.876 |
| cysS | alaS | Msil_0135 | Msil_3523 | KEGG: bid:Bind_1915 cysteinyl-tRNA synthetase; TIGRFAM: cysteinyl-tRNA synthetase; PFAM: tRNA synthetase class I (M); Cysteinyl-tRNA synthetase class Ia; 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. | 0.642 |
| cysS | leuS | Msil_0135 | Msil_0336 | KEGG: bid:Bind_1915 cysteinyl-tRNA synthetase; TIGRFAM: cysteinyl-tRNA synthetase; PFAM: tRNA synthetase class I (M); Cysteinyl-tRNA synthetase class Ia; Belongs to the class-I aminoacyl-tRNA synthetase family. | TIGRFAM: leucyl-tRNA synthetase; KEGG: bid:Bind_0225 leucyl-tRNA synthetase; Belongs to the class-I aminoacyl-tRNA synthetase family. | 0.736 |
| cysS | metG | Msil_0135 | Msil_0541 | KEGG: bid:Bind_1915 cysteinyl-tRNA synthetase; TIGRFAM: cysteinyl-tRNA synthetase; PFAM: tRNA synthetase class I (M); Cysteinyl-tRNA synthetase class Ia; 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; Belongs to the class-I aminoacyl-tRNA synthetase family. MetG type 2B subfamily. | 0.575 |
| cysS | pheT | Msil_0135 | Msil_1838 | KEGG: bid:Bind_1915 cysteinyl-tRNA synthetase; TIGRFAM: cysteinyl-tRNA synthetase; PFAM: tRNA synthetase class I (M); Cysteinyl-tRNA synthetase class Ia; Belongs to the class-I aminoacyl-tRNA synthetase family. | KEGG: bid:Bind_3247 phenylalanyl-tRNA synthetase, beta subunit; TIGRFAM: phenylalanyl-tRNA synthetase, beta subunit; Belongs to the phenylalanyl-tRNA synthetase beta subunit family. Type 1 subfamily. | 0.661 |
| cysS | thrS | Msil_0135 | Msil_3538 | KEGG: bid:Bind_1915 cysteinyl-tRNA synthetase; TIGRFAM: cysteinyl-tRNA synthetase; PFAM: tRNA synthetase class I (M); Cysteinyl-tRNA synthetase class Ia; Belongs to the class-I aminoacyl-tRNA synthetase family. | 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). | 0.800 |
| cysS | valS | Msil_0135 | Msil_1688 | KEGG: bid:Bind_1915 cysteinyl-tRNA synthetase; TIGRFAM: cysteinyl-tRNA synthetase; PFAM: tRNA synthetase class I (M); Cysteinyl-tRNA synthetase class Ia; 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 1 subfamily. | 0.698 |