| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| KB13_1038 | KB13_380 | KB13_1038 | KB13_380 | Peptidase M22, glycoprotease; [O] COG1214 Inactive homolog of metal-dependent proteases, putative molecular chaperone. | Helicase c2; [KL] COG1199 Rad3-related DNA helicases. | 0.793 |
| KB13_1038 | proS | KB13_1038 | KB13_554 | Peptidase M22, glycoprotease; [O] COG1214 Inactive homolog of metal-dependent proteases, putative molecular chaperone. | 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). As ProRS can inadvertently accommodate and process non-cognate amino acids such as alanine and cysteine, to avoid such errors it has two additional distinct editing activities against alanine. One activity is designated as 'pretransfer' editing and involves the tRNA(Pro)-independent hydrolysis of activated Ala-AMP. The other activity is designated 'posttransfer' editing and involves dea [...] | 0.792 |
| KB13_380 | KB13_1038 | KB13_380 | KB13_1038 | Helicase c2; [KL] COG1199 Rad3-related DNA helicases. | Peptidase M22, glycoprotease; [O] COG1214 Inactive homolog of metal-dependent proteases, putative molecular chaperone. | 0.793 |
| KB13_380 | proS | KB13_380 | KB13_554 | Helicase c2; [KL] COG1199 Rad3-related DNA helicases. | 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). As ProRS can inadvertently accommodate and process non-cognate amino acids such as alanine and cysteine, to avoid such errors it has two additional distinct editing activities against alanine. One activity is designated as 'pretransfer' editing and involves the tRNA(Pro)-independent hydrolysis of activated Ala-AMP. The other activity is designated 'posttransfer' editing and involves dea [...] | 0.811 |
| argS | glnS | KB13_453 | KB13_287 | [J] COG0018 Arginyl-tRNA synthetase. | [J] COG0008 Glutamyl- and glutaminyl-tRNA synthetases. | 0.928 |
| argS | gltX | KB13_453 | KB13_746 | [J] COG0018 Arginyl-tRNA synthetase. | 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); Belongs to the class-I aminoacyl-tRNA synthetase family. Glutamate--tRNA ligase type 1 subfamily. | 0.946 |
| argS | ileS | KB13_453 | KB13_743 | [J] COG0018 Arginyl-tRNA synthetase. | 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 1 subfamily. | 0.981 |
| argS | leuS | KB13_453 | KB13_288 | [J] COG0018 Arginyl-tRNA synthetase. | [J] COG0495 Leucyl-tRNA synthetase; Belongs to the class-I aminoacyl-tRNA synthetase family. | 0.944 |
| argS | lysS | KB13_453 | KB13_349 | [J] COG0018 Arginyl-tRNA synthetase. | [J] COG0173 Aspartyl-tRNA synthetase; Belongs to the class-II aminoacyl-tRNA synthetase family. | 0.882 |
| argS | metG | KB13_453 | KB13_818 | [J] COG0018 Arginyl-tRNA synthetase. | 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. | 0.968 |
| argS | proS | KB13_453 | KB13_554 | [J] COG0018 Arginyl-tRNA synthetase. | 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). As ProRS can inadvertently accommodate and process non-cognate amino acids such as alanine and cysteine, to avoid such errors it has two additional distinct editing activities against alanine. One activity is designated as 'pretransfer' editing and involves the tRNA(Pro)-independent hydrolysis of activated Ala-AMP. The other activity is designated 'posttransfer' editing and involves dea [...] | 0.975 |
| dusB | glnS | KB13_879 | KB13_287 | tRNA-dihydrouridine synthase B; Catalyzes the synthesis of 5,6-dihydrouridine (D), a modified base found in the D-loop of most tRNAs, via the reduction of the C5-C6 double bond in target uridines; Belongs to the Dus family. DusB subfamily. | [J] COG0008 Glutamyl- and glutaminyl-tRNA synthetases. | 0.574 |
| dusB | gltX | KB13_879 | KB13_746 | tRNA-dihydrouridine synthase B; Catalyzes the synthesis of 5,6-dihydrouridine (D), a modified base found in the D-loop of most tRNAs, via the reduction of the C5-C6 double bond in target uridines; Belongs to the Dus family. DusB subfamily. | 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); Belongs to the class-I aminoacyl-tRNA synthetase family. Glutamate--tRNA ligase type 1 subfamily. | 0.579 |
| dusB | proS | KB13_879 | KB13_554 | tRNA-dihydrouridine synthase B; Catalyzes the synthesis of 5,6-dihydrouridine (D), a modified base found in the D-loop of most tRNAs, via the reduction of the C5-C6 double bond in target uridines; Belongs to the Dus family. DusB subfamily. | 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). As ProRS can inadvertently accommodate and process non-cognate amino acids such as alanine and cysteine, to avoid such errors it has two additional distinct editing activities against alanine. One activity is designated as 'pretransfer' editing and involves the tRNA(Pro)-independent hydrolysis of activated Ala-AMP. The other activity is designated 'posttransfer' editing and involves dea [...] | 0.837 |
| glnS | argS | KB13_287 | KB13_453 | [J] COG0008 Glutamyl- and glutaminyl-tRNA synthetases. | [J] COG0018 Arginyl-tRNA synthetase. | 0.928 |
| glnS | dusB | KB13_287 | KB13_879 | [J] COG0008 Glutamyl- and glutaminyl-tRNA synthetases. | tRNA-dihydrouridine synthase B; Catalyzes the synthesis of 5,6-dihydrouridine (D), a modified base found in the D-loop of most tRNAs, via the reduction of the C5-C6 double bond in target uridines; Belongs to the Dus family. DusB subfamily. | 0.574 |
| glnS | ileS | KB13_287 | KB13_743 | [J] COG0008 Glutamyl- and glutaminyl-tRNA synthetases. | 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 1 subfamily. | 0.941 |
| glnS | leuS | KB13_287 | KB13_288 | [J] COG0008 Glutamyl- and glutaminyl-tRNA synthetases. | [J] COG0495 Leucyl-tRNA synthetase; Belongs to the class-I aminoacyl-tRNA synthetase family. | 0.935 |
| glnS | lysS | KB13_287 | KB13_349 | [J] COG0008 Glutamyl- and glutaminyl-tRNA synthetases. | [J] COG0173 Aspartyl-tRNA synthetase; Belongs to the class-II aminoacyl-tRNA synthetase family. | 0.902 |
| glnS | metG | KB13_287 | KB13_818 | [J] COG0008 Glutamyl- and glutaminyl-tRNA synthetases. | 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. | 0.952 |