| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| RPA2844 | serS | RPA2844 | RPA2845 | Pseudo gene of Fe+3 siderophore transport receptor; Signal predicted by SignalP 2.0 HMM (Signal peptideprobabilty 0.994) with cleavage site probability 0.874 atresidue 31. | seryl-tRNA synthetase; Catalyzes the attachment of serine to tRNA(Ser). Is also able to aminoacylate tRNA(Sec) with serine, to form the misacylated tRNA L- seryl-tRNA(Sec), which will be further converted into selenocysteinyl- tRNA(Sec). | 0.789 |
| RPA3394 | serS | RPA3394 | RPA2845 | DUF37; Could be involved in insertion of integral membrane proteins into the membrane; Belongs to the UPF0161 family. | seryl-tRNA synthetase; Catalyzes the attachment of serine to tRNA(Ser). Is also able to aminoacylate tRNA(Sec) with serine, to form the misacylated tRNA L- seryl-tRNA(Sec), which will be further converted into selenocysteinyl- tRNA(Sec). | 0.823 |
| alaS | argS | RPA3847 | RPA2854 | 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. | arginyl-tRNA synthetase; Observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished. | 0.878 |
| alaS | cysS | RPA3847 | RPA1997 | 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. | cysteine-tRNA ligase; Observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished; Belongs to the class-I aminoacyl-tRNA synthetase family. | 0.778 |
| alaS | metG | RPA3847 | RPA2777 | 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. | 0.743 |
| alaS | proS | RPA3847 | RPA2928 | 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. | 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). Can inadvertently accommodate and process cysteine. The misacylated Cys-tRNA(Pro) is not edited by ProRS. | 0.742 |
| alaS | serS | RPA3847 | RPA2845 | 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. | seryl-tRNA synthetase; Catalyzes the attachment of serine to tRNA(Ser). Is also able to aminoacylate tRNA(Sec) with serine, to form the misacylated tRNA L- seryl-tRNA(Sec), which will be further converted into selenocysteinyl- tRNA(Sec). | 0.705 |
| alaS | thrS | RPA3847 | RPA3406 | 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). Also edits incorrectly charged L-seryl-tRNA(Thr). | 0.913 |
| alaS | trpS | RPA3847 | RPA0455 | 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. | trytophanyl-tRNA synthetase; Catalyzes the attachment of tryptophan to tRNA(Trp). Belongs to the class-I aminoacyl-tRNA synthetase family. | 0.515 |
| alaS | valS | RPA3847 | RPA2583 | 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. | 0.920 |
| argS | alaS | RPA2854 | RPA3847 | arginyl-tRNA synthetase; Observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished. | 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. | 0.878 |
| argS | cysS | RPA2854 | RPA1997 | arginyl-tRNA synthetase; Observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished. | cysteine-tRNA ligase; Observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished; Belongs to the class-I aminoacyl-tRNA synthetase family. | 0.620 |
| argS | metG | RPA2854 | RPA2777 | arginyl-tRNA synthetase; Observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished. | 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. | 0.964 |
| argS | proS | RPA2854 | RPA2928 | arginyl-tRNA synthetase; Observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished. | 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). Can inadvertently accommodate and process cysteine. The misacylated Cys-tRNA(Pro) is not edited by ProRS. | 0.968 |
| argS | serS | RPA2854 | RPA2845 | arginyl-tRNA synthetase; Observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished. | seryl-tRNA synthetase; Catalyzes the attachment of serine to tRNA(Ser). Is also able to aminoacylate tRNA(Sec) with serine, to form the misacylated tRNA L- seryl-tRNA(Sec), which will be further converted into selenocysteinyl- tRNA(Sec). | 0.685 |
| argS | thrS | RPA2854 | RPA3406 | arginyl-tRNA synthetase; Observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished. | 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). Also edits incorrectly charged L-seryl-tRNA(Thr). | 0.697 |
| argS | trpS | RPA2854 | RPA0455 | arginyl-tRNA synthetase; Observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished. | trytophanyl-tRNA synthetase; Catalyzes the attachment of tryptophan to tRNA(Trp). Belongs to the class-I aminoacyl-tRNA synthetase family. | 0.610 |
| argS | valS | RPA2854 | RPA2583 | arginyl-tRNA synthetase; Observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished. | 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. | 0.768 |
| cysS | alaS | RPA1997 | RPA3847 | cysteine-tRNA ligase; Observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished; 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. | 0.778 |
| cysS | argS | RPA1997 | RPA2854 | cysteine-tRNA ligase; Observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished; Belongs to the class-I aminoacyl-tRNA synthetase family. | arginyl-tRNA synthetase; Observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished. | 0.620 |