node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
asnS | aspS | DSY4952 | DSY2431 | Hypothetical protein; Similarity to COG0017 Aspartyl/asparaginyl-tRNA synthetases(Evalue: 1E-162). | Hypothetical 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. | 0.426 |
asnS | gltX | DSY4952 | DSY0445 | Hypothetical protein; Similarity to COG0017 Aspartyl/asparaginyl-tRNA synthetases(Evalue: 1E-162). | Hypothetical protein; 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). | 0.913 |
asnS | hisG | DSY4952 | DSY3914 | Hypothetical protein; Similarity to COG0017 Aspartyl/asparaginyl-tRNA synthetases(Evalue: 1E-162). | Hypothetical protein; Catalyzes the condensation of ATP and 5-phosphoribose 1- diphosphate to form N'-(5'-phosphoribosyl)-ATP (PR-ATP). Has a crucial role in the pathway because the rate of histidine biosynthesis seems to be controlled primarily by regulation of HisG enzymatic activity. Belongs to the ATP phosphoribosyltransferase family. Short subfamily. | 0.648 |
asnS | hisS | DSY4952 | DSY2432 | Hypothetical protein; Similarity to COG0017 Aspartyl/asparaginyl-tRNA synthetases(Evalue: 1E-162). | Hypothetical protein; Similarity to COG0124 Histidyl-tRNA synthetase(Evalue: 1E-120). | 0.832 |
asnS | ileS | DSY4952 | DSY2882 | Hypothetical protein; Similarity to COG0017 Aspartyl/asparaginyl-tRNA synthetases(Evalue: 1E-162). | Hypothetical 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. | 0.948 |
asnS | leuS | DSY4952 | DSY3158 | Hypothetical protein; Similarity to COG0017 Aspartyl/asparaginyl-tRNA synthetases(Evalue: 1E-162). | Hypothetical protein; Similarity to COG0495 Leucyl-tRNA synthetase(Evalue: 0); Belongs to the class-I aminoacyl-tRNA synthetase family. | 0.916 |
asnS | serS | DSY4952 | DSY0008 | Hypothetical protein; Similarity to COG0017 Aspartyl/asparaginyl-tRNA synthetases(Evalue: 1E-162). | 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). | 0.778 |
asnS | thrS | DSY4952 | DSY0240 | Hypothetical protein; Similarity to COG0017 Aspartyl/asparaginyl-tRNA synthetases(Evalue: 1E-162). | Hypothetical 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). | 0.801 |
asnS | valS | DSY4952 | DSY3188 | Hypothetical protein; Similarity to COG0017 Aspartyl/asparaginyl-tRNA synthetases(Evalue: 1E-162). | Hypothetical 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. | 0.615 |
aspS | asnS | DSY2431 | DSY4952 | Hypothetical 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. | Hypothetical protein; Similarity to COG0017 Aspartyl/asparaginyl-tRNA synthetases(Evalue: 1E-162). | 0.426 |
aspS | fmt | DSY2431 | DSY2693 | Hypothetical 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. | Hypothetical protein; Attaches a formyl group to the free amino group of methionyl- tRNA(fMet). The formyl group appears to play a dual role in the initiator identity of N-formylmethionyl-tRNA by promoting its recognition by IF2 and preventing the misappropriation of this tRNA by the elongation apparatus; Belongs to the Fmt family. | 0.474 |
aspS | gltX | DSY2431 | DSY0445 | Hypothetical 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. | Hypothetical protein; 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). | 0.608 |
aspS | hisS | DSY2431 | DSY2432 | Hypothetical 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. | Hypothetical protein; Similarity to COG0124 Histidyl-tRNA synthetase(Evalue: 1E-120). | 0.979 |
aspS | ileS | DSY2431 | DSY2882 | Hypothetical 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. | Hypothetical 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. | 0.673 |
aspS | leuS | DSY2431 | DSY3158 | Hypothetical 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. | Hypothetical protein; Similarity to COG0495 Leucyl-tRNA synthetase(Evalue: 0); Belongs to the class-I aminoacyl-tRNA synthetase family. | 0.639 |
aspS | serS | DSY2431 | DSY0008 | Hypothetical 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. | 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). | 0.573 |
aspS | thrS | DSY2431 | DSY0240 | Hypothetical 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. | Hypothetical 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). | 0.623 |
aspS | valS | DSY2431 | DSY3188 | Hypothetical 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. | Hypothetical 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. | 0.830 |
fmt | aspS | DSY2693 | DSY2431 | Hypothetical protein; Attaches a formyl group to the free amino group of methionyl- tRNA(fMet). The formyl group appears to play a dual role in the initiator identity of N-formylmethionyl-tRNA by promoting its recognition by IF2 and preventing the misappropriation of this tRNA by the elongation apparatus; Belongs to the Fmt family. | Hypothetical 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. | 0.474 |
fmt | hisS | DSY2693 | DSY2432 | Hypothetical protein; Attaches a formyl group to the free amino group of methionyl- tRNA(fMet). The formyl group appears to play a dual role in the initiator identity of N-formylmethionyl-tRNA by promoting its recognition by IF2 and preventing the misappropriation of this tRNA by the elongation apparatus; Belongs to the Fmt family. | Hypothetical protein; Similarity to COG0124 Histidyl-tRNA synthetase(Evalue: 1E-120). | 0.793 |