node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
Mmc1_2541 | ileS | Mmc1_2541 | Mmc1_2147 | KEGG: pfo:Pfl_3001 DNA topoisomerase III; TIGRFAM: DNA topoisomerase III; PFAM: TOPRIM domain protein; DNA topoisomerase, type IA, central domain protein; DNA topoisomerase, type IA, Zn finger domain protein; SMART: DNA topoisomerase I, ATP-binding; DNA topoisomerase I, DNA-binding; Toprim sub 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 1 subfamily. | 0.462 |
Mmc1_2541 | leuS | Mmc1_2541 | Mmc1_0432 | KEGG: pfo:Pfl_3001 DNA topoisomerase III; TIGRFAM: DNA topoisomerase III; PFAM: TOPRIM domain protein; DNA topoisomerase, type IA, central domain protein; DNA topoisomerase, type IA, Zn finger domain protein; SMART: DNA topoisomerase I, ATP-binding; DNA topoisomerase I, DNA-binding; Toprim sub domain protein. | TIGRFAM: leucyl-tRNA synthetase; KEGG: pca:Pcar_1413 leucyl-tRNA synthetase; Belongs to the class-I aminoacyl-tRNA synthetase family. | 0.980 |
Mmc1_2541 | metG | Mmc1_2541 | Mmc1_1856 | KEGG: pfo:Pfl_3001 DNA topoisomerase III; TIGRFAM: DNA topoisomerase III; PFAM: TOPRIM domain protein; DNA topoisomerase, type IA, central domain protein; DNA topoisomerase, type IA, Zn finger domain protein; SMART: DNA topoisomerase I, ATP-binding; DNA topoisomerase I, DNA-binding; Toprim sub domain protein. | methionyl-tRNA synthetase; Is required not only for elongation of protein synthesis but also for the initiation of all mRNA translation through initiator tRNA(fMet) aminoacylation. | 0.640 |
Mmc1_2541 | pheT | Mmc1_2541 | Mmc1_0368 | KEGG: pfo:Pfl_3001 DNA topoisomerase III; TIGRFAM: DNA topoisomerase III; PFAM: TOPRIM domain protein; DNA topoisomerase, type IA, central domain protein; DNA topoisomerase, type IA, Zn finger domain protein; SMART: DNA topoisomerase I, ATP-binding; DNA topoisomerase I, DNA-binding; Toprim sub domain protein. | TIGRFAM: phenylalanyl-tRNA synthetase, beta subunit; KEGG: pca:Pcar_1423 phenylalanyl-tRNA synthetase, beta subunit. | 0.578 |
Mmc1_2541 | topA | Mmc1_2541 | Mmc1_3660 | KEGG: pfo:Pfl_3001 DNA topoisomerase III; TIGRFAM: DNA topoisomerase III; PFAM: TOPRIM domain protein; DNA topoisomerase, type IA, central domain protein; DNA topoisomerase, type IA, Zn finger domain protein; SMART: DNA topoisomerase I, ATP-binding; DNA topoisomerase I, DNA-binding; Toprim sub domain protein. | DNA topoisomerase I; Releases the supercoiling and torsional tension of DNA, which is introduced during the DNA replication and transcription, by transiently cleaving and rejoining one strand of the DNA duplex. Introduces a single-strand break via transesterification at a target site in duplex DNA. The scissile phosphodiester is attacked by the catalytic tyrosine of the enzyme, resulting in the formation of a DNA- (5'-phosphotyrosyl)-enzyme intermediate and the expulsion of a 3'-OH DNA strand. The free DNA strand then undergoes passage around the unbroken strand, thus removing DNA supe [...] | 0.640 |
Mmc1_2541 | valS | Mmc1_2541 | Mmc1_1474 | KEGG: pfo:Pfl_3001 DNA topoisomerase III; TIGRFAM: DNA topoisomerase III; PFAM: TOPRIM domain protein; DNA topoisomerase, type IA, central domain protein; DNA topoisomerase, type IA, Zn finger domain protein; SMART: DNA topoisomerase I, ATP-binding; DNA topoisomerase I, DNA-binding; Toprim sub 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 1 subfamily. | 0.527 |
Mmc1_3652 | argS | Mmc1_3652 | Mmc1_0704 | PFAM: glutamyl-tRNA synthetase, class Ic; KEGG: mag:amb4312 glutamyl- and glutaminyl-tRNA synthetase; Belongs to the class-I aminoacyl-tRNA synthetase family. | KEGG: jan:Jann_1507 arginyl-tRNA synthetase; TIGRFAM: arginyl-tRNA synthetase. | 0.844 |
Mmc1_3652 | ileS | Mmc1_3652 | Mmc1_2147 | PFAM: glutamyl-tRNA synthetase, class Ic; KEGG: mag:amb4312 glutamyl- and glutaminyl-tRNA synthetase; Belongs to the class-I aminoacyl-tRNA synthetase family. | 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 1 subfamily. | 0.908 |
Mmc1_3652 | leuS | Mmc1_3652 | Mmc1_0432 | PFAM: glutamyl-tRNA synthetase, class Ic; KEGG: mag:amb4312 glutamyl- and glutaminyl-tRNA synthetase; Belongs to the class-I aminoacyl-tRNA synthetase family. | TIGRFAM: leucyl-tRNA synthetase; KEGG: pca:Pcar_1413 leucyl-tRNA synthetase; Belongs to the class-I aminoacyl-tRNA synthetase family. | 0.858 |
Mmc1_3652 | metG | Mmc1_3652 | Mmc1_1856 | PFAM: glutamyl-tRNA synthetase, class Ic; KEGG: mag:amb4312 glutamyl- and glutaminyl-tRNA synthetase; Belongs to the class-I aminoacyl-tRNA synthetase family. | methionyl-tRNA synthetase; Is required not only for elongation of protein synthesis but also for the initiation of all mRNA translation through initiator tRNA(fMet) aminoacylation. | 0.936 |
Mmc1_3652 | pheT | Mmc1_3652 | Mmc1_0368 | PFAM: glutamyl-tRNA synthetase, class Ic; KEGG: mag:amb4312 glutamyl- and glutaminyl-tRNA synthetase; Belongs to the class-I aminoacyl-tRNA synthetase family. | TIGRFAM: phenylalanyl-tRNA synthetase, beta subunit; KEGG: pca:Pcar_1423 phenylalanyl-tRNA synthetase, beta subunit. | 0.801 |
Mmc1_3652 | proS | Mmc1_3652 | Mmc1_1767 | PFAM: glutamyl-tRNA synthetase, class Ic; KEGG: mag:amb4312 glutamyl- and glutaminyl-tRNA synthetase; Belongs to the class-I aminoacyl-tRNA synthetase family. | prolyl-tRNA synthetase; Catalyzes the attachment of proline to tRNA(Pro) in a two- step reaction: proline is first activated by ATP to form Pro-AMP and then transferred to the acceptor end of tRNA(Pro). As ProRS can inadvertently accommodate and process non-cognate amino acids such as alanine and cysteine, to avoid such errors it has two additional distinct editing activities against alanine. One activity is designated as 'pretransfer' editing and involves the tRNA(Pro)-independent hydrolysis of activated Ala-AMP. The other activity is designated 'posttransfer' editing and involves dea [...] | 0.848 |
Mmc1_3652 | valS | Mmc1_3652 | Mmc1_1474 | PFAM: glutamyl-tRNA synthetase, class Ic; KEGG: mag:amb4312 glutamyl- and glutaminyl-tRNA synthetase; Belongs to the class-I aminoacyl-tRNA synthetase family. | 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 1 subfamily. | 0.401 |
argS | Mmc1_3652 | Mmc1_0704 | Mmc1_3652 | KEGG: jan:Jann_1507 arginyl-tRNA synthetase; TIGRFAM: arginyl-tRNA synthetase. | PFAM: glutamyl-tRNA synthetase, class Ic; KEGG: mag:amb4312 glutamyl- and glutaminyl-tRNA synthetase; Belongs to the class-I aminoacyl-tRNA synthetase family. | 0.844 |
argS | gltX | Mmc1_0704 | Mmc1_0944 | KEGG: jan:Jann_1507 arginyl-tRNA synthetase; TIGRFAM: arginyl-tRNA synthetase. | glutamyl-tRNA synthetase; 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). | 0.866 |
argS | ileS | Mmc1_0704 | Mmc1_2147 | KEGG: jan:Jann_1507 arginyl-tRNA synthetase; TIGRFAM: arginyl-tRNA synthetase. | 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 1 subfamily. | 0.946 |
argS | leuS | Mmc1_0704 | Mmc1_0432 | KEGG: jan:Jann_1507 arginyl-tRNA synthetase; TIGRFAM: arginyl-tRNA synthetase. | TIGRFAM: leucyl-tRNA synthetase; KEGG: pca:Pcar_1413 leucyl-tRNA synthetase; Belongs to the class-I aminoacyl-tRNA synthetase family. | 0.889 |
argS | metG | Mmc1_0704 | Mmc1_1856 | KEGG: jan:Jann_1507 arginyl-tRNA synthetase; TIGRFAM: arginyl-tRNA synthetase. | methionyl-tRNA synthetase; Is required not only for elongation of protein synthesis but also for the initiation of all mRNA translation through initiator tRNA(fMet) aminoacylation. | 0.954 |
argS | pheT | Mmc1_0704 | Mmc1_0368 | KEGG: jan:Jann_1507 arginyl-tRNA synthetase; TIGRFAM: arginyl-tRNA synthetase. | TIGRFAM: phenylalanyl-tRNA synthetase, beta subunit; KEGG: pca:Pcar_1423 phenylalanyl-tRNA synthetase, beta subunit. | 0.897 |
argS | proS | Mmc1_0704 | Mmc1_1767 | KEGG: jan:Jann_1507 arginyl-tRNA synthetase; TIGRFAM: arginyl-tRNA synthetase. | prolyl-tRNA synthetase; Catalyzes the attachment of proline to tRNA(Pro) in a two- step reaction: proline is first activated by ATP to form Pro-AMP and then transferred to the acceptor end of tRNA(Pro). As ProRS can inadvertently accommodate and process non-cognate amino acids such as alanine and cysteine, to avoid such errors it has two additional distinct editing activities against alanine. One activity is designated as 'pretransfer' editing and involves the tRNA(Pro)-independent hydrolysis of activated Ala-AMP. The other activity is designated 'posttransfer' editing and involves dea [...] | 0.950 |