node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
alaS | aspS | RC1_0900 | RC1_1540 | 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). Also edits incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) via its editing domain. | 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. | 0.870 |
alaS | glyQ | RC1_0900 | RC1_1669 | 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). Also edits incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) via its editing domain. | PF02091 TIGR00388: glycyl-tRNA synthetase, alpha subunit; With a good score above the trusted cutoff and characterized homologs; identified by match to protein family HMM PF00815 match to protein family HMM TIGR00069. | 0.852 |
alaS | glyS | RC1_0900 | RC1_1668 | 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). Also edits incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) via its editing domain. | PF02092 TIGR00211: glycyl-tRNA synthetase, beta subunit; With a good score above the trusted cutoff and characterized homologs; identified by match to protein family HMM PF06793. | 0.854 |
alaS | ileS | RC1_0900 | RC1_3585 | 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). Also edits incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) via its 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 1 subfamily. | 0.911 |
alaS | leuS | RC1_0900 | RC1_2551 | 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). Also edits incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) via its editing domain. | leucyl-tRNA synthetase LeuS; TIGR00396 With a good score above the trusted cutoff and characterized homologs; identified by match to protein family HMM PF06319; Belongs to the class-I aminoacyl-tRNA synthetase family. | 0.931 |
alaS | pheT | RC1_0900 | RC1_2318 | 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). Also edits incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) via its editing domain. | phenylalanyl-tRNA synthetase, beta subunit PheT; TIGR00472 With a good score above the trusted cutoff and characterized homologs; identified by match to protein family HMM PF01327 match to protein family HMM TIGR00079; Belongs to the phenylalanyl-tRNA synthetase beta subunit family. Type 1 subfamily. | 0.937 |
alaS | proS | RC1_0900 | RC1_1216 | 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). Also edits incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) via its editing domain. | prolyl-tRNA synthetase ProS; TIGR00409 identified by match to protein family HMM PF01148. | 0.685 |
alaS | thrS | RC1_0900 | RC1_2819 | 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). Also edits incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) via its 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). | 0.910 |
alaS | valS | RC1_0900 | RC1_1162 | 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). Also edits incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) via its 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 1 subfamily. | 0.915 |
aspS | alaS | RC1_1540 | RC1_0900 | 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. | 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). Also edits incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) via its editing domain. | 0.870 |
aspS | glyQ | RC1_1540 | RC1_1669 | 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. | PF02091 TIGR00388: glycyl-tRNA synthetase, alpha subunit; With a good score above the trusted cutoff and characterized homologs; identified by match to protein family HMM PF00815 match to protein family HMM TIGR00069. | 0.773 |
aspS | glyS | RC1_1540 | RC1_1668 | 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. | PF02092 TIGR00211: glycyl-tRNA synthetase, beta subunit; With a good score above the trusted cutoff and characterized homologs; identified by match to protein family HMM PF06793. | 0.818 |
aspS | ileS | RC1_1540 | RC1_3585 | 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. | 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 1 subfamily. | 0.869 |
aspS | leuS | RC1_1540 | RC1_2551 | 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. | leucyl-tRNA synthetase LeuS; TIGR00396 With a good score above the trusted cutoff and characterized homologs; identified by match to protein family HMM PF06319; Belongs to the class-I aminoacyl-tRNA synthetase family. | 0.803 |
aspS | pheT | RC1_1540 | RC1_2318 | 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. | phenylalanyl-tRNA synthetase, beta subunit PheT; TIGR00472 With a good score above the trusted cutoff and characterized homologs; identified by match to protein family HMM PF01327 match to protein family HMM TIGR00079; Belongs to the phenylalanyl-tRNA synthetase beta subunit family. Type 1 subfamily. | 0.836 |
aspS | proS | RC1_1540 | RC1_1216 | 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; TIGR00409 identified by match to protein family HMM PF01148. | 0.851 |
aspS | rpsG | RC1_1540 | RC1_0707 | 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 S7; One of the primary rRNA binding proteins, it binds directly to 16S rRNA where it nucleates assembly of the head domain of the 30S subunit. Is located at the subunit interface close to the decoding center, probably blocks exit of the E-site tRNA; Belongs to the universal ribosomal protein uS7 family. | 0.515 |
aspS | thrS | RC1_1540 | RC1_2819 | 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. | 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). | 0.723 |
aspS | valS | RC1_1540 | RC1_1162 | 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. | 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 1 subfamily. | 0.886 |
glyQ | alaS | RC1_1669 | RC1_0900 | PF02091 TIGR00388: glycyl-tRNA synthetase, alpha subunit; With a good score above the trusted cutoff and characterized homologs; identified by match to protein family HMM PF00815 match to protein family HMM TIGR00069. | 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). Also edits incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) via its editing domain. | 0.852 |