node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
AF_1970 | alaS | AF_1970 | AF_2255 | TPR domain-containing protein; Similar to GB:L04733 SP:Q07866 PID:307085 percent identity: 29.03; identified by sequence similarity; putative. | alanyl-tRNA synthetase (alaS); 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). Incorrectly charged aminoacyl-tRNA(Ala) is also edited in situ by the editing domain. | 0.939 |
AF_2369 | alaS | AF_2369 | AF_2255 | Predicted coding region AF_2369; Hypothetical protein; identified by GeneMark; putative. | alanyl-tRNA synthetase (alaS); 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). Incorrectly charged aminoacyl-tRNA(Ala) is also edited in situ by the editing domain. | 0.939 |
alaS | AF_1970 | AF_2255 | AF_1970 | alanyl-tRNA synthetase (alaS); 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). Incorrectly charged aminoacyl-tRNA(Ala) is also edited in situ by the editing domain. | TPR domain-containing protein; Similar to GB:L04733 SP:Q07866 PID:307085 percent identity: 29.03; identified by sequence similarity; putative. | 0.939 |
alaS | AF_2369 | AF_2255 | AF_2369 | alanyl-tRNA synthetase (alaS); 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). Incorrectly charged aminoacyl-tRNA(Ala) is also edited in situ by the editing domain. | Predicted coding region AF_2369; Hypothetical protein; identified by GeneMark; putative. | 0.939 |
alaS | glyS | AF_2255 | AF_0916 | alanyl-tRNA synthetase (alaS); 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). Incorrectly charged aminoacyl-tRNA(Ala) is also edited in situ by the editing domain. | glycyl-tRNA synthetase (glyS); Catalyzes the attachment of glycine to tRNA(Gly). | 0.935 |
alaS | hisS | AF_2255 | AF_1642 | alanyl-tRNA synthetase (alaS); 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). Incorrectly charged aminoacyl-tRNA(Ala) is also edited in situ by the editing domain. | histidyl-tRNA synthetase (hisS); Similar to GB:L77117 SP:Q58406 PID:1591660 percent identity: 45.97; identified by sequence similarity; putative; Belongs to the class-II aminoacyl-tRNA synthetase family. | 0.932 |
alaS | ileS | AF_2255 | AF_0633 | alanyl-tRNA synthetase (alaS); 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). Incorrectly charged aminoacyl-tRNA(Ala) is also edited in situ by the editing domain. | isoleucyl-tRNA synthetase (ileS); 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 2 subfamily. | 0.937 |
alaS | leuS | AF_2255 | AF_2421 | alanyl-tRNA synthetase (alaS); 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). Incorrectly charged aminoacyl-tRNA(Ala) is also edited in situ by the editing domain. | leucyl-tRNA synthetase (leuS); Similar to GB:L77117 SP:Q58050 PID:1591345 percent identity: 49.68; identified by sequence similarity; putative; Belongs to the class-I aminoacyl-tRNA synthetase family. | 0.915 |
alaS | metG | AF_2255 | AF_1453 | alanyl-tRNA synthetase (alaS); 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). Incorrectly charged aminoacyl-tRNA(Ala) is also edited in situ by the editing domain. | methionyl-tRNA synthetase (metS); Is required not only for elongation of protein synthesis but also for the initiation of all mRNA translation through initiator tRNA(fMet) aminoacylation. | 0.863 |
alaS | thrS | AF_2255 | AF_0548 | alanyl-tRNA synthetase (alaS); 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). Incorrectly charged aminoacyl-tRNA(Ala) is also edited in situ by the editing domain. | threonyl-tRNA synthetase (thrS); 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) (By similarity); Belongs to the class-II aminoacyl-tRNA synthetase family. | 0.889 |
alaS | tyrS | AF_2255 | AF_0776 | alanyl-tRNA synthetase (alaS); 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). Incorrectly charged aminoacyl-tRNA(Ala) is also edited in situ by the editing domain. | tyrosyl-tRNA synthetase (tyrS); Catalyzes the attachment of tyrosine to tRNA(Tyr) in a two- step reaction: tyrosine is first activated by ATP to form Tyr-AMP and then transferred to the acceptor end of tRNA(Tyr); Belongs to the class-I aminoacyl-tRNA synthetase family. TyrS type 3 subfamily. | 0.888 |
alaS | valS | AF_2255 | AF_2224 | alanyl-tRNA synthetase (alaS); 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). Incorrectly charged aminoacyl-tRNA(Ala) is also edited in situ by the editing domain. | valyl-tRNA synthetase (valS); 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 2 subfamily. | 0.931 |
glyS | alaS | AF_0916 | AF_2255 | glycyl-tRNA synthetase (glyS); Catalyzes the attachment of glycine to tRNA(Gly). | alanyl-tRNA synthetase (alaS); 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). Incorrectly charged aminoacyl-tRNA(Ala) is also edited in situ by the editing domain. | 0.935 |
glyS | hisS | AF_0916 | AF_1642 | glycyl-tRNA synthetase (glyS); Catalyzes the attachment of glycine to tRNA(Gly). | histidyl-tRNA synthetase (hisS); Similar to GB:L77117 SP:Q58406 PID:1591660 percent identity: 45.97; identified by sequence similarity; putative; Belongs to the class-II aminoacyl-tRNA synthetase family. | 0.749 |
glyS | ileS | AF_0916 | AF_0633 | glycyl-tRNA synthetase (glyS); Catalyzes the attachment of glycine to tRNA(Gly). | isoleucyl-tRNA synthetase (ileS); 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 2 subfamily. | 0.948 |
glyS | leuS | AF_0916 | AF_2421 | glycyl-tRNA synthetase (glyS); Catalyzes the attachment of glycine to tRNA(Gly). | leucyl-tRNA synthetase (leuS); Similar to GB:L77117 SP:Q58050 PID:1591345 percent identity: 49.68; identified by sequence similarity; putative; Belongs to the class-I aminoacyl-tRNA synthetase family. | 0.926 |
glyS | metG | AF_0916 | AF_1453 | glycyl-tRNA synthetase (glyS); Catalyzes the attachment of glycine to tRNA(Gly). | methionyl-tRNA synthetase (metS); Is required not only for elongation of protein synthesis but also for the initiation of all mRNA translation through initiator tRNA(fMet) aminoacylation. | 0.809 |
glyS | thrS | AF_0916 | AF_0548 | glycyl-tRNA synthetase (glyS); Catalyzes the attachment of glycine to tRNA(Gly). | threonyl-tRNA synthetase (thrS); 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) (By similarity); Belongs to the class-II aminoacyl-tRNA synthetase family. | 0.659 |
glyS | tyrS | AF_0916 | AF_0776 | glycyl-tRNA synthetase (glyS); Catalyzes the attachment of glycine to tRNA(Gly). | tyrosyl-tRNA synthetase (tyrS); Catalyzes the attachment of tyrosine to tRNA(Tyr) in a two- step reaction: tyrosine is first activated by ATP to form Tyr-AMP and then transferred to the acceptor end of tRNA(Tyr); Belongs to the class-I aminoacyl-tRNA synthetase family. TyrS type 3 subfamily. | 0.945 |
glyS | valS | AF_0916 | AF_2224 | glycyl-tRNA synthetase (glyS); Catalyzes the attachment of glycine to tRNA(Gly). | valyl-tRNA synthetase (valS); 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 2 subfamily. | 0.848 |