| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| asnS | gltX-2 | CLOSPI_01760 | CLOSPI_01358 | asparagine--tRNA ligase; KEGG: ctc:CTC00143 9.4e-152 asparaginyl-tRNA synthetase K01893; COG: COG0017 Aspartyl/asparaginyl-tRNA synthetases; Psort location: Cytoplasmic, score: 10.00. | glutamate--tRNA ligase; 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); Belongs to the class-I aminoacyl-tRNA synthetase family. Glutamate--tRNA ligase type 1 subfamily. | 0.957 |
| asnS | ileS | CLOSPI_01760 | CLOSPI_01977 | asparagine--tRNA ligase; KEGG: ctc:CTC00143 9.4e-152 asparaginyl-tRNA synthetase K01893; COG: COG0017 Aspartyl/asparaginyl-tRNA synthetases; Psort location: Cytoplasmic, score: 10.00. | isoleucine--tRNA ligase; 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 1 subfamily. | 0.982 |
| asnS | leuS | CLOSPI_01760 | CLOSPI_01091 | asparagine--tRNA ligase; KEGG: ctc:CTC00143 9.4e-152 asparaginyl-tRNA synthetase K01893; COG: COG0017 Aspartyl/asparaginyl-tRNA synthetases; Psort location: Cytoplasmic, score: 10.00. | leucine--tRNA ligase; KEGG: gka:GK2842 0. leuS; leucyl-tRNA synthetase K01869; COG: COG0495 Leucyl-tRNA synthetase; Psort location: Cytoplasmic, score: 9.98; Belongs to the class-I aminoacyl-tRNA synthetase family. | 0.991 |
| asnS | metG | CLOSPI_01760 | CLOSPI_02389 | asparagine--tRNA ligase; KEGG: ctc:CTC00143 9.4e-152 asparaginyl-tRNA synthetase K01893; COG: COG0017 Aspartyl/asparaginyl-tRNA synthetases; Psort location: Cytoplasmic, score: 10.00. | 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. | 0.985 |
| asnS | proS | CLOSPI_01760 | CLOSPI_00040 | asparagine--tRNA ligase; KEGG: ctc:CTC00143 9.4e-152 asparaginyl-tRNA synthetase K01893; COG: COG0017 Aspartyl/asparaginyl-tRNA synthetases; Psort location: Cytoplasmic, score: 10.00. | proline--tRNA ligase; 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). | 0.979 |
| gltX-2 | asnS | CLOSPI_01358 | CLOSPI_01760 | glutamate--tRNA ligase; 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); Belongs to the class-I aminoacyl-tRNA synthetase family. Glutamate--tRNA ligase type 1 subfamily. | asparagine--tRNA ligase; KEGG: ctc:CTC00143 9.4e-152 asparaginyl-tRNA synthetase K01893; COG: COG0017 Aspartyl/asparaginyl-tRNA synthetases; Psort location: Cytoplasmic, score: 10.00. | 0.957 |
| gltX-2 | ileS | CLOSPI_01358 | CLOSPI_01977 | glutamate--tRNA ligase; 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); Belongs to the class-I aminoacyl-tRNA synthetase family. Glutamate--tRNA ligase type 1 subfamily. | isoleucine--tRNA ligase; 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 1 subfamily. | 0.971 |
| gltX-2 | leuS | CLOSPI_01358 | CLOSPI_01091 | glutamate--tRNA ligase; 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); Belongs to the class-I aminoacyl-tRNA synthetase family. Glutamate--tRNA ligase type 1 subfamily. | leucine--tRNA ligase; KEGG: gka:GK2842 0. leuS; leucyl-tRNA synthetase K01869; COG: COG0495 Leucyl-tRNA synthetase; Psort location: Cytoplasmic, score: 9.98; Belongs to the class-I aminoacyl-tRNA synthetase family. | 0.972 |
| gltX-2 | metG | CLOSPI_01358 | CLOSPI_02389 | glutamate--tRNA ligase; 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); Belongs to the class-I aminoacyl-tRNA synthetase family. Glutamate--tRNA ligase 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. | 0.985 |
| gltX-2 | proS | CLOSPI_01358 | CLOSPI_00040 | glutamate--tRNA ligase; 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); Belongs to the class-I aminoacyl-tRNA synthetase family. Glutamate--tRNA ligase type 1 subfamily. | proline--tRNA ligase; 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). | 0.932 |
| gltX-2 | rplF | CLOSPI_01358 | CLOSPI_01584 | glutamate--tRNA ligase; 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); Belongs to the class-I aminoacyl-tRNA synthetase family. Glutamate--tRNA ligase type 1 subfamily. | Ribosomal protein L6; This protein binds to the 23S rRNA, and is important in its secondary structure. It is located near the subunit interface in the base of the L7/L12 stalk, and near the tRNA binding site of the peptidyltransferase center; Belongs to the universal ribosomal protein uL6 family. | 0.953 |
| gltX-2 | rplN | CLOSPI_01358 | CLOSPI_01579 | glutamate--tRNA ligase; 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); Belongs to the class-I aminoacyl-tRNA synthetase family. Glutamate--tRNA ligase type 1 subfamily. | Ribosomal protein L14; Binds to 23S rRNA. Forms part of two intersubunit bridges in the 70S ribosome; Belongs to the universal ribosomal protein uL14 family. | 0.932 |
| gltX-2 | rplR | CLOSPI_01358 | CLOSPI_01585 | glutamate--tRNA ligase; 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); Belongs to the class-I aminoacyl-tRNA synthetase family. Glutamate--tRNA ligase type 1 subfamily. | Ribosomal protein L18; This is one of the proteins that binds and probably mediates the attachment of the 5S RNA into the large ribosomal subunit, where it forms part of the central protuberance. | 0.958 |
| gltX-2 | rplV | CLOSPI_01358 | CLOSPI_01574 | glutamate--tRNA ligase; 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); Belongs to the class-I aminoacyl-tRNA synthetase family. Glutamate--tRNA ligase type 1 subfamily. | Ribosomal protein L22; The globular domain of the protein is located near the polypeptide exit tunnel on the outside of the subunit, while an extended beta-hairpin is found that lines the wall of the exit tunnel in the center of the 70S ribosome. | 0.944 |
| gltX-2 | rplW | CLOSPI_01358 | CLOSPI_01571 | glutamate--tRNA ligase; 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); Belongs to the class-I aminoacyl-tRNA synthetase family. Glutamate--tRNA ligase type 1 subfamily. | Ribosomal protein L23; One of the early assembly proteins it binds 23S rRNA. One of the proteins that surrounds the polypeptide exit tunnel on the outside of the ribosome. Forms the main docking site for trigger factor binding to the ribosome; Belongs to the universal ribosomal protein uL23 family. | 0.948 |
| ileS | asnS | CLOSPI_01977 | CLOSPI_01760 | isoleucine--tRNA ligase; 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 1 subfamily. | asparagine--tRNA ligase; KEGG: ctc:CTC00143 9.4e-152 asparaginyl-tRNA synthetase K01893; COG: COG0017 Aspartyl/asparaginyl-tRNA synthetases; Psort location: Cytoplasmic, score: 10.00. | 0.982 |
| ileS | gltX-2 | CLOSPI_01977 | CLOSPI_01358 | isoleucine--tRNA ligase; 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 1 subfamily. | glutamate--tRNA ligase; 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); Belongs to the class-I aminoacyl-tRNA synthetase family. Glutamate--tRNA ligase type 1 subfamily. | 0.971 |
| ileS | leuS | CLOSPI_01977 | CLOSPI_01091 | isoleucine--tRNA ligase; 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 1 subfamily. | leucine--tRNA ligase; KEGG: gka:GK2842 0. leuS; leucyl-tRNA synthetase K01869; COG: COG0495 Leucyl-tRNA synthetase; Psort location: Cytoplasmic, score: 9.98; Belongs to the class-I aminoacyl-tRNA synthetase family. | 0.987 |
| ileS | metG | CLOSPI_01977 | CLOSPI_02389 | isoleucine--tRNA ligase; 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 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. | 0.994 |
| ileS | proS | CLOSPI_01977 | CLOSPI_00040 | isoleucine--tRNA ligase; 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 1 subfamily. | proline--tRNA ligase; 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). | 0.987 |