node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
alaS | aspS | RSc0797 | RSc0466 | Probable alanyl-trna synthetase (alanine--trna ligase) (alars) protein; 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. | Probable aspartyl-trna synthetase (aspartate--trna ligase)(asprs) protein; 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. | 0.912 |
alaS | cysS | RSc0797 | RSc1167 | Probable alanyl-trna synthetase (alanine--trna ligase) (alars) protein; 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. | Probable cysteinyl-trna synthetase (cysteine--trna ligase)(cysrs) protein; Belongs to the class-I aminoacyl-tRNA synthetase family. | 0.805 |
alaS | ileS | RSc0797 | RSc2458 | Probable alanyl-trna synthetase (alanine--trna ligase) (alars) protein; 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. | Probable isoleucyl-trna synthetase protein; 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. | 0.831 |
alaS | leuS | RSc0797 | RSc2744 | Probable alanyl-trna synthetase (alanine--trna ligase) (alars) protein; 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. | Probable leucyl-trna synthetase (leucine--trna ligase) (leurs) protein; Belongs to the class-I aminoacyl-tRNA synthetase family. | 0.867 |
alaS | metG1 | RSc0797 | RSc2381 | Probable alanyl-trna synthetase (alanine--trna ligase) (alars) protein; 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. | Probable methionyl-trna synthetase (methionine--trna ligase)(metrs) protein; Is required not only for elongation of protein synthesis but also for the initiation of all mRNA translation through initiator tRNA(fMet) aminoacylation. | 0.825 |
alaS | pheT | RSc0797 | RSc1582 | Probable alanyl-trna synthetase (alanine--trna ligase) (alars) protein; 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. | Probable phenylalanyl-trna synthetase beta chain (phenylalanine--trna ligase beta chain) (phers) protein; Belongs to the phenylalanyl-tRNA synthetase beta subunit family. Type 1 subfamily. | 0.925 |
alaS | purL | RSc0797 | RSc1722 | Probable alanyl-trna synthetase (alanine--trna ligase) (alars) protein; 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. | Phosphoribosylformylglycinamidine synthase; Phosphoribosylformylglycinamidine synthase involved in the purines biosynthetic pathway. Catalyzes the ATP-dependent conversion of formylglycinamide ribonucleotide (FGAR) and glutamine to yield formylglycinamidine ribonucleotide (FGAM) and glutamate. | 0.818 |
alaS | recA | RSc0797 | RSc0551 | Probable alanyl-trna synthetase (alanine--trna ligase) (alars) protein; 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. | Probable protein reca (recombinase a); Can catalyze the hydrolysis of ATP in the presence of single- stranded DNA, the ATP-dependent uptake of single-stranded DNA by duplex DNA, and the ATP-dependent hybridization of homologous single-stranded DNAs. It interacts with LexA causing its activation and leading to its autocatalytic cleavage.; Belongs to the RecA family. | 0.797 |
alaS | thrS | RSc0797 | RSc1577 | Probable alanyl-trna synthetase (alanine--trna ligase) (alars) protein; 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. | Probable threonyl-trna synthetase (threonine--trna ligase) protein; 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 | valS | RSc0797 | RSc2236 | Probable alanyl-trna synthetase (alanine--trna ligase) (alars) protein; 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. | Probable valyl-trna synthetase (valine--trna ligase) protein; 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. | 0.849 |
aspS | alaS | RSc0466 | RSc0797 | Probable aspartyl-trna synthetase (aspartate--trna ligase)(asprs) protein; 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. | Probable alanyl-trna synthetase (alanine--trna ligase) (alars) protein; 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. | 0.912 |
aspS | cysS | RSc0466 | RSc1167 | Probable aspartyl-trna synthetase (aspartate--trna ligase)(asprs) protein; 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. | Probable cysteinyl-trna synthetase (cysteine--trna ligase)(cysrs) protein; Belongs to the class-I aminoacyl-tRNA synthetase family. | 0.566 |
aspS | ileS | RSc0466 | RSc2458 | Probable aspartyl-trna synthetase (aspartate--trna ligase)(asprs) protein; 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. | Probable isoleucyl-trna synthetase protein; 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. | 0.805 |
aspS | leuS | RSc0466 | RSc2744 | Probable aspartyl-trna synthetase (aspartate--trna ligase)(asprs) protein; 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. | Probable leucyl-trna synthetase (leucine--trna ligase) (leurs) protein; Belongs to the class-I aminoacyl-tRNA synthetase family. | 0.721 |
aspS | metG1 | RSc0466 | RSc2381 | Probable aspartyl-trna synthetase (aspartate--trna ligase)(asprs) protein; 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. | Probable methionyl-trna synthetase (methionine--trna ligase)(metrs) protein; Is required not only for elongation of protein synthesis but also for the initiation of all mRNA translation through initiator tRNA(fMet) aminoacylation. | 0.752 |
aspS | pheT | RSc0466 | RSc1582 | Probable aspartyl-trna synthetase (aspartate--trna ligase)(asprs) protein; 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. | Probable phenylalanyl-trna synthetase beta chain (phenylalanine--trna ligase beta chain) (phers) protein; Belongs to the phenylalanyl-tRNA synthetase beta subunit family. Type 1 subfamily. | 0.826 |
aspS | purL | RSc0466 | RSc1722 | Probable aspartyl-trna synthetase (aspartate--trna ligase)(asprs) protein; 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. | Phosphoribosylformylglycinamidine synthase; Phosphoribosylformylglycinamidine synthase involved in the purines biosynthetic pathway. Catalyzes the ATP-dependent conversion of formylglycinamide ribonucleotide (FGAR) and glutamine to yield formylglycinamidine ribonucleotide (FGAM) and glutamate. | 0.727 |
aspS | thrS | RSc0466 | RSc1577 | Probable aspartyl-trna synthetase (aspartate--trna ligase)(asprs) protein; 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. | Probable threonyl-trna synthetase (threonine--trna ligase) protein; 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). | 0.625 |
aspS | valS | RSc0466 | RSc2236 | Probable aspartyl-trna synthetase (aspartate--trna ligase)(asprs) protein; 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. | Probable valyl-trna synthetase (valine--trna ligase) protein; 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. | 0.792 |
cysS | alaS | RSc1167 | RSc0797 | Probable cysteinyl-trna synthetase (cysteine--trna ligase)(cysrs) protein; Belongs to the class-I aminoacyl-tRNA synthetase family. | Probable alanyl-trna synthetase (alanine--trna ligase) (alars) protein; 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. | 0.805 |