| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| alaS | aspS | SCA_1230 | SCA_1241 | Alanine--tRNA ligase; 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 | Aspartate--tRNA ligase; 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 | 0.630 |
| alaS | fusA | SCA_1230 | SCA_0206 | Alanine--tRNA ligase; 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 | Elongation factor G; Catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post- translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome | 0.795 |
| alaS | guaA | SCA_1230 | SCA_0050 | Alanine--tRNA ligase; 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 | 0.484 |
| alaS | hisS | SCA_1230 | SCA_1242 | Alanine--tRNA ligase; 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 | Histidine--tRNA ligase; Similar to histidyl-tRNA synthetase hisS (EC 6.1.1.21),,Bacillus subtilis, 424AA, Expect = 1e-141,Identities = 244/412 (59%), Positives = 319/412 (77%),Gaps = 1/412 (0%),(P60909) Histidyl-tRNA synthetase (EC 6.1.1.21) (Histidine--tRNA ligase) (HisRS),InterPro- Histidyl-tRNA synthetase class IIa; Hypothetical protein; Sca_1242 | 0.743 |
| alaS | lepA | SCA_1230 | SCA_1206 | Alanine--tRNA ligase; 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 | Elongation factor 4; Required for accurate and efficient protein synthesis under certain stress conditions. May act as a fidelity factor of the translation reaction, by catalyzing a one-codon backward translocation of tRNAs on improperly translocated ribosomes. Back- translocation proceeds from a post-translocation (POST) complex to a pre-translocation (PRE) complex, thus giving elongation factor G a second chance to translocate the tRNAs correctly. Binds to ribosomes in a GTP-dependent manner | 0.830 |
| alaS | lysS | SCA_1230 | SCA_0169 | Alanine--tRNA ligase; 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 | Lysine--tRNA ligase; (Q8CQV5) Lysyl-tRNA synthetase (EC 6.1.1.6) (Lysine--tRNA ligase) (LysRS),InterPro- Lysyl-tRNA synthetase class-2; Hypothetical protein; Sca_0169; Belongs to the class-II aminoacyl-tRNA synthetase family | 0.660 |
| alaS | metS | SCA_1230 | SCA_0140 | Alanine--tRNA ligase; 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 | Methionine--tRNA ligase; 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 | 0.885 |
| alaS | pheS | SCA_1230 | SCA_0756 | Alanine--tRNA ligase; 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 | Phenylalanine--tRNA ligase alpha subunit; (Q99QR1) Phenylalanyl-tRNA synthetase alpha chain (EC 6.1.1.20) (Phenylalanine--tRNA ligase alpha chain) (PheRS),InterPro- Phenylalanyl-tRNA synthetase alpha subunit; Hypothetical protein; Sca_0756; Belongs to the class-II aminoacyl-tRNA synthetase family. Phe-tRNA synthetase alpha subunit type 1 subfamily | 0.791 |
| alaS | pheT | SCA_1230 | SCA_0757 | Alanine--tRNA ligase; 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 | Phenylalanine--tRNA ligase beta subunit; (Q8CSY8) Phenylalanyl-tRNA synthetase beta chain (EC 6.1.1.20) (Phenylalanine--tRNA ligase beta chain) (PheRS),InterPro- Bacterial phenylalanyl-tRNA synthetase beta subunit; Hypothetical protein; Sca_0757 | 0.770 |
| alaS | valS | SCA_1230 | SCA_1269 | Alanine--tRNA ligase; 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 | Valine--tRNA ligase; 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 | 0.737 |
| aspS | alaS | SCA_1241 | SCA_1230 | Aspartate--tRNA ligase; 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 | Alanine--tRNA ligase; 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 | 0.630 |
| aspS | fusA | SCA_1241 | SCA_0206 | Aspartate--tRNA ligase; 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 | Elongation factor G; Catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post- translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome | 0.625 |
| aspS | hisS | SCA_1241 | SCA_1242 | Aspartate--tRNA ligase; 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 | Histidine--tRNA ligase; Similar to histidyl-tRNA synthetase hisS (EC 6.1.1.21),,Bacillus subtilis, 424AA, Expect = 1e-141,Identities = 244/412 (59%), Positives = 319/412 (77%),Gaps = 1/412 (0%),(P60909) Histidyl-tRNA synthetase (EC 6.1.1.21) (Histidine--tRNA ligase) (HisRS),InterPro- Histidyl-tRNA synthetase class IIa; Hypothetical protein; Sca_1242 | 0.968 |
| aspS | lepA | SCA_1241 | SCA_1206 | Aspartate--tRNA ligase; 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 | Elongation factor 4; Required for accurate and efficient protein synthesis under certain stress conditions. May act as a fidelity factor of the translation reaction, by catalyzing a one-codon backward translocation of tRNAs on improperly translocated ribosomes. Back- translocation proceeds from a post-translocation (POST) complex to a pre-translocation (PRE) complex, thus giving elongation factor G a second chance to translocate the tRNAs correctly. Binds to ribosomes in a GTP-dependent manner | 0.739 |
| aspS | lysS | SCA_1241 | SCA_0169 | Aspartate--tRNA ligase; 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 | Lysine--tRNA ligase; (Q8CQV5) Lysyl-tRNA synthetase (EC 6.1.1.6) (Lysine--tRNA ligase) (LysRS),InterPro- Lysyl-tRNA synthetase class-2; Hypothetical protein; Sca_0169; Belongs to the class-II aminoacyl-tRNA synthetase family | 0.495 |
| aspS | metS | SCA_1241 | SCA_0140 | Aspartate--tRNA ligase; 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 | Methionine--tRNA ligase; 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 | 0.753 |
| aspS | pheS | SCA_1241 | SCA_0756 | Aspartate--tRNA ligase; 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 | Phenylalanine--tRNA ligase alpha subunit; (Q99QR1) Phenylalanyl-tRNA synthetase alpha chain (EC 6.1.1.20) (Phenylalanine--tRNA ligase alpha chain) (PheRS),InterPro- Phenylalanyl-tRNA synthetase alpha subunit; Hypothetical protein; Sca_0756; Belongs to the class-II aminoacyl-tRNA synthetase family. Phe-tRNA synthetase alpha subunit type 1 subfamily | 0.814 |
| aspS | pheT | SCA_1241 | SCA_0757 | Aspartate--tRNA ligase; 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 | Phenylalanine--tRNA ligase beta subunit; (Q8CSY8) Phenylalanyl-tRNA synthetase beta chain (EC 6.1.1.20) (Phenylalanine--tRNA ligase beta chain) (PheRS),InterPro- Bacterial phenylalanyl-tRNA synthetase beta subunit; Hypothetical protein; Sca_0757 | 0.587 |
| aspS | valS | SCA_1241 | SCA_1269 | Aspartate--tRNA ligase; 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 | Valine--tRNA ligase; 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 | 0.808 |
| fusA | alaS | SCA_0206 | SCA_1230 | Elongation factor G; Catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post- translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome | Alanine--tRNA ligase; 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 | 0.795 |
