node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
Mlab_1156 | Mlab_1157 | Mlab_1156 | Mlab_1157 | TIGRFAM: glycyl-tRNA synthetase; PFAM: tRNA synthetase, class II (G, H, P and S); Anticodon-binding domain protein. | PFAM: helix-hairpin-helix motif; helicase domain protein; ERCC4 domain protein; type III restriction enzyme, res subunit; DEAD/DEAH box helicase domain protein; SMART: Helix-hairpin-helix DNA-binding, class 1; DEAD-like helicases-like. | 0.822 |
Mlab_1156 | Mlab_1524 | Mlab_1156 | Mlab_1524 | TIGRFAM: glycyl-tRNA synthetase; PFAM: tRNA synthetase, class II (G, H, P and S); Anticodon-binding domain protein. | PFAM: peptidyl-prolyl cis-trans isomerase, cyclophilin type. | 0.785 |
Mlab_1156 | alaS | Mlab_1156 | Mlab_1380 | TIGRFAM: glycyl-tRNA synthetase; PFAM: tRNA synthetase, class II (G, H, P and S); Anticodon-binding domain protein. | 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. | 0.772 |
Mlab_1156 | argS | Mlab_1156 | Mlab_1508 | TIGRFAM: glycyl-tRNA synthetase; PFAM: tRNA synthetase, class II (G, H, P and S); Anticodon-binding domain protein. | TIGRFAM: arginyl-tRNA synthetase; Belongs to the class-I aminoacyl-tRNA synthetase family. | 0.760 |
Mlab_1156 | aspS | Mlab_1156 | Mlab_0039 | TIGRFAM: glycyl-tRNA synthetase; PFAM: tRNA synthetase, class II (G, H, P and S); Anticodon-binding domain protein. | aspartyl-tRNA synthetase; 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). | 0.816 |
Mlab_1156 | ileS | Mlab_1156 | Mlab_0186 | TIGRFAM: glycyl-tRNA synthetase; PFAM: tRNA synthetase, class II (G, H, P and S); Anticodon-binding domain protein. | Isoleucyl-tRNA synthetase; 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. | 0.850 |
Mlab_1156 | leuS | Mlab_1156 | Mlab_1404 | TIGRFAM: glycyl-tRNA synthetase; PFAM: tRNA synthetase, class II (G, H, P and S); Anticodon-binding domain protein. | TIGRFAM: leucyl-tRNA synthetase; Belongs to the class-I aminoacyl-tRNA synthetase family. | 0.794 |
Mlab_1156 | serS | Mlab_1156 | Mlab_0710 | TIGRFAM: glycyl-tRNA synthetase; PFAM: tRNA synthetase, class II (G, H, P and S); Anticodon-binding domain protein. | 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). | 0.735 |
Mlab_1156 | tyrS | Mlab_1156 | Mlab_1734 | TIGRFAM: glycyl-tRNA synthetase; PFAM: tRNA synthetase, class II (G, H, P and S); Anticodon-binding domain protein. | tyrosyl-tRNA synthetase; 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. | 0.758 |
Mlab_1156 | valS | Mlab_1156 | Mlab_0403 | TIGRFAM: glycyl-tRNA synthetase; PFAM: tRNA synthetase, class II (G, H, P and S); Anticodon-binding domain protein. | 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 2 subfamily. | 0.764 |
Mlab_1157 | Mlab_1156 | Mlab_1157 | Mlab_1156 | PFAM: helix-hairpin-helix motif; helicase domain protein; ERCC4 domain protein; type III restriction enzyme, res subunit; DEAD/DEAH box helicase domain protein; SMART: Helix-hairpin-helix DNA-binding, class 1; DEAD-like helicases-like. | TIGRFAM: glycyl-tRNA synthetase; PFAM: tRNA synthetase, class II (G, H, P and S); Anticodon-binding domain protein. | 0.822 |
Mlab_1157 | aspS | Mlab_1157 | Mlab_0039 | PFAM: helix-hairpin-helix motif; helicase domain protein; ERCC4 domain protein; type III restriction enzyme, res subunit; DEAD/DEAH box helicase domain protein; SMART: Helix-hairpin-helix DNA-binding, class 1; DEAD-like helicases-like. | aspartyl-tRNA synthetase; 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). | 0.452 |
Mlab_1524 | Mlab_1156 | Mlab_1524 | Mlab_1156 | PFAM: peptidyl-prolyl cis-trans isomerase, cyclophilin type. | TIGRFAM: glycyl-tRNA synthetase; PFAM: tRNA synthetase, class II (G, H, P and S); Anticodon-binding domain protein. | 0.785 |
Mlab_1524 | argS | Mlab_1524 | Mlab_1508 | PFAM: peptidyl-prolyl cis-trans isomerase, cyclophilin type. | TIGRFAM: arginyl-tRNA synthetase; Belongs to the class-I aminoacyl-tRNA synthetase family. | 0.798 |
Mlab_1524 | tyrS | Mlab_1524 | Mlab_1734 | PFAM: peptidyl-prolyl cis-trans isomerase, cyclophilin type. | tyrosyl-tRNA synthetase; 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. | 0.749 |
Mlab_1524 | valS | Mlab_1524 | Mlab_0403 | PFAM: peptidyl-prolyl cis-trans isomerase, cyclophilin type. | 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 2 subfamily. | 0.802 |
alaS | Mlab_1156 | Mlab_1380 | Mlab_1156 | 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. | TIGRFAM: glycyl-tRNA synthetase; PFAM: tRNA synthetase, class II (G, H, P and S); Anticodon-binding domain protein. | 0.772 |
alaS | argS | Mlab_1380 | Mlab_1508 | 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. | TIGRFAM: arginyl-tRNA synthetase; Belongs to the class-I aminoacyl-tRNA synthetase family. | 0.683 |
alaS | aspS | Mlab_1380 | Mlab_0039 | 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. | aspartyl-tRNA synthetase; 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). | 0.714 |
alaS | ileS | Mlab_1380 | Mlab_0186 | 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. | Isoleucyl-tRNA synthetase; 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. | 0.835 |