| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| TP_0696 | cmk | TP_0696 | TP_0279 | Nicotinamidase, putative; Similar to GP:2183283 percent identity: 33.69; identified by sequence similarity; putative. | Ribosomal protein S1 (rpsA); Similar to SP:P02349 GB:V00342 GB:V00352 GB:X04864 PID:42837 percent identity: 36.77; identified by sequence similarity; putative. | 0.447 |
| TP_0696 | gatA | TP_0696 | TP_1020 | Nicotinamidase, putative; Similar to GP:2183283 percent identity: 33.69; identified by sequence similarity; putative. | glu-tRNA amidotransferase, subunit A (gatA); Allows the formation of correctly charged Gln-tRNA(Gln) through the transamidation of misacylated Glu-tRNA(Gln) in organisms which lack glutaminyl-tRNA synthetase. The reaction takes place in the presence of glutamine and ATP through an activated gamma-phospho-Glu- tRNA(Gln) (By similarity). | 0.786 |
| TP_0696 | nadE | TP_0696 | TP_0780 | Nicotinamidase, putative; Similar to GP:2183283 percent identity: 33.69; identified by sequence similarity; putative. | NH(3)-dependent NAD(+) synthetase (nadE); Catalyzes the ATP-dependent amidation of deamido-NAD to form NAD. | 0.738 |
| asnS | aspS | TP_0609 | TP_0985 | asparaginyl-tRNA synthetase (asnS); Similar to PID:1001350 SP:P52276 PID:1001357 percent identity: 54.92; identified by sequence similarity; putative. | aspartyl-tRNA synthetase (aspS); Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn); Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily. | 0.862 |
| asnS | cmk | TP_0609 | TP_0279 | asparaginyl-tRNA synthetase (asnS); Similar to PID:1001350 SP:P52276 PID:1001357 percent identity: 54.92; identified by sequence similarity; putative. | Ribosomal protein S1 (rpsA); Similar to SP:P02349 GB:V00342 GB:V00352 GB:X04864 PID:42837 percent identity: 36.77; identified by sequence similarity; putative. | 0.640 |
| asnS | gatA | TP_0609 | TP_1020 | asparaginyl-tRNA synthetase (asnS); Similar to PID:1001350 SP:P52276 PID:1001357 percent identity: 54.92; identified by sequence similarity; putative. | glu-tRNA amidotransferase, subunit A (gatA); Allows the formation of correctly charged Gln-tRNA(Gln) through the transamidation of misacylated Glu-tRNA(Gln) in organisms which lack glutaminyl-tRNA synthetase. The reaction takes place in the presence of glutamine and ATP through an activated gamma-phospho-Glu- tRNA(Gln) (By similarity). | 0.991 |
| asnS | gatB | TP_0609 | TP_1021 | asparaginyl-tRNA synthetase (asnS); Similar to PID:1001350 SP:P52276 PID:1001357 percent identity: 54.92; identified by sequence similarity; putative. | glu-tRNA amidotransferase, subunit B (gatB); Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl- tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an activated phospho-Asp- tRNA(Asn) or phospho-Glu-tRNA(Gln) (By similarity); Belongs to the GatB/GatE family. GatB subfamily. | 0.993 |
| asnS | gatC | TP_0609 | TP_1019 | asparaginyl-tRNA synthetase (asnS); Similar to PID:1001350 SP:P52276 PID:1001357 percent identity: 54.92; identified by sequence similarity; putative. | glu-tRNA amidotransferase, subunit C (gatC); Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl- tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an activated phospho-Asp- tRNA(Asn) or phospho-Glu-tRNA(Gln) (By similarity); Belongs to the GatC family. | 0.934 |
| asnS | gltX | TP_0609 | TP_0673 | asparaginyl-tRNA synthetase (asnS); Similar to PID:1001350 SP:P52276 PID:1001357 percent identity: 54.92; identified by sequence similarity; putative. | glutamyl-tRNA synthetase (gltX); 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). | 0.970 |
| asnS | metG | TP_0609 | TP_0798 | asparaginyl-tRNA synthetase (asnS); Similar to PID:1001350 SP:P52276 PID:1001357 percent identity: 54.92; identified by sequence similarity; putative. | methionyl-tRNA synthetase (metG); 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 |
| asnS | nadE | TP_0609 | TP_0780 | asparaginyl-tRNA synthetase (asnS); Similar to PID:1001350 SP:P52276 PID:1001357 percent identity: 54.92; identified by sequence similarity; putative. | NH(3)-dependent NAD(+) synthetase (nadE); Catalyzes the ATP-dependent amidation of deamido-NAD to form NAD. | 0.434 |
| asnS | proS | TP_0609 | TP_0160 | asparaginyl-tRNA synthetase (asnS); Similar to PID:1001350 SP:P52276 PID:1001357 percent identity: 54.92; identified by sequence similarity; putative. | prolyl-tRNA synthetase (proS); 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 invol [...] | 0.993 |
| aspS | asnS | TP_0985 | TP_0609 | aspartyl-tRNA synthetase (aspS); Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn); Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily. | asparaginyl-tRNA synthetase (asnS); Similar to PID:1001350 SP:P52276 PID:1001357 percent identity: 54.92; identified by sequence similarity; putative. | 0.862 |
| aspS | cmk | TP_0985 | TP_0279 | aspartyl-tRNA synthetase (aspS); Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn); Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily. | Ribosomal protein S1 (rpsA); Similar to SP:P02349 GB:V00342 GB:V00352 GB:X04864 PID:42837 percent identity: 36.77; identified by sequence similarity; putative. | 0.713 |
| aspS | gatA | TP_0985 | TP_1020 | aspartyl-tRNA synthetase (aspS); Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn); Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily. | glu-tRNA amidotransferase, subunit A (gatA); Allows the formation of correctly charged Gln-tRNA(Gln) through the transamidation of misacylated Glu-tRNA(Gln) in organisms which lack glutaminyl-tRNA synthetase. The reaction takes place in the presence of glutamine and ATP through an activated gamma-phospho-Glu- tRNA(Gln) (By similarity). | 0.928 |
| aspS | gatB | TP_0985 | TP_1021 | aspartyl-tRNA synthetase (aspS); Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn); Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily. | glu-tRNA amidotransferase, subunit B (gatB); Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl- tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an activated phospho-Asp- tRNA(Asn) or phospho-Glu-tRNA(Gln) (By similarity); Belongs to the GatB/GatE family. GatB subfamily. | 0.998 |
| aspS | gatC | TP_0985 | TP_1019 | aspartyl-tRNA synthetase (aspS); Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn); Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily. | glu-tRNA amidotransferase, subunit C (gatC); Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl- tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an activated phospho-Asp- tRNA(Asn) or phospho-Glu-tRNA(Gln) (By similarity); Belongs to the GatC family. | 0.981 |
| aspS | gltX | TP_0985 | TP_0673 | aspartyl-tRNA synthetase (aspS); Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn); Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily. | glutamyl-tRNA synthetase (gltX); 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). | 0.813 |
| aspS | metG | TP_0985 | TP_0798 | aspartyl-tRNA synthetase (aspS); Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn); Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily. | methionyl-tRNA synthetase (metG); Is required not only for elongation of protein synthesis but also for the initiation of all mRNA translation through initiator tRNA(fMet) aminoacylation. | 0.870 |
| aspS | proS | TP_0985 | TP_0160 | aspartyl-tRNA synthetase (aspS); Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn); Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily. | prolyl-tRNA synthetase (proS); 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 invol [...] | 0.939 |