node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
argS | aspS | MmarC5_0568 | MmarC5_1792 | KEGG: mmp:MMP1026 arginyl-tRNA synthetase; TIGRFAM: arginyl-tRNA synthetase; Belongs to the class-I aminoacyl-tRNA synthetase family. | 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). | 0.967 |
argS | gltX | MmarC5_0568 | MmarC5_0583 | KEGG: mmp:MMP1026 arginyl-tRNA synthetase; TIGRFAM: arginyl-tRNA synthetase; Belongs to the class-I aminoacyl-tRNA synthetase family. | 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). | 0.982 |
argS | ileS | MmarC5_0568 | MmarC5_0104 | KEGG: mmp:MMP1026 arginyl-tRNA synthetase; TIGRFAM: arginyl-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 2 subfamily. | 0.995 |
argS | leuS | MmarC5_0568 | MmarC5_0879 | KEGG: mmp:MMP1026 arginyl-tRNA synthetase; TIGRFAM: arginyl-tRNA synthetase; Belongs to the class-I aminoacyl-tRNA synthetase family. | TIGRFAM: leucyl-tRNA synthetase; KEGG: mmp:MMP0697 leucyl-tRNA synthetase; Belongs to the class-I aminoacyl-tRNA synthetase family. | 0.993 |
argS | metG | MmarC5_0568 | MmarC5_1347 | KEGG: mmp:MMP1026 arginyl-tRNA synthetase; TIGRFAM: arginyl-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. | 0.989 |
argS | pheT | MmarC5_0568 | MmarC5_0336 | KEGG: mmp:MMP1026 arginyl-tRNA synthetase; TIGRFAM: arginyl-tRNA synthetase; Belongs to the class-I aminoacyl-tRNA synthetase family. | TIGRFAM: phenylalanyl-tRNA synthetase, beta subunit; PFAM: tRNA synthetase, B5; KEGG: mmp:MMP1255 phenylalanyl-tRNA synthetase beta subunit. | 0.869 |
argS | proS | MmarC5_0568 | MmarC5_0880 | KEGG: mmp:MMP1026 arginyl-tRNA synthetase; TIGRFAM: arginyl-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). | 0.953 |
argS | thrS | MmarC5_0568 | MmarC5_1223 | KEGG: mmp:MMP1026 arginyl-tRNA synthetase; TIGRFAM: arginyl-tRNA synthetase; Belongs to the class-I aminoacyl-tRNA synthetase family. | threonyl-tRNA synthetase; 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); Belongs to the class-II aminoacyl-tRNA synthetase family. | 0.908 |
argS | topA | MmarC5_0568 | MmarC5_0781 | KEGG: mmp:MMP1026 arginyl-tRNA synthetase; TIGRFAM: arginyl-tRNA synthetase; Belongs to the class-I aminoacyl-tRNA synthetase family. | 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 [...] | 0.539 |
argS | tyrS | MmarC5_0568 | MmarC5_1410 | KEGG: mmp:MMP1026 arginyl-tRNA synthetase; TIGRFAM: arginyl-tRNA synthetase; Belongs to the class-I aminoacyl-tRNA synthetase family. | 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. | 0.926 |
aspS | argS | MmarC5_1792 | MmarC5_0568 | 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). | KEGG: mmp:MMP1026 arginyl-tRNA synthetase; TIGRFAM: arginyl-tRNA synthetase; Belongs to the class-I aminoacyl-tRNA synthetase family. | 0.967 |
aspS | gltX | MmarC5_1792 | MmarC5_0583 | 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). | 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). | 0.984 |
aspS | ileS | MmarC5_1792 | MmarC5_0104 | 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). | 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. | 0.972 |
aspS | leuS | MmarC5_1792 | MmarC5_0879 | 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). | TIGRFAM: leucyl-tRNA synthetase; KEGG: mmp:MMP0697 leucyl-tRNA synthetase; Belongs to the class-I aminoacyl-tRNA synthetase family. | 0.978 |
aspS | metG | MmarC5_1792 | MmarC5_1347 | 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). | 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. | 0.977 |
aspS | pheT | MmarC5_1792 | MmarC5_0336 | 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). | TIGRFAM: phenylalanyl-tRNA synthetase, beta subunit; PFAM: tRNA synthetase, B5; KEGG: mmp:MMP1255 phenylalanyl-tRNA synthetase beta subunit. | 0.530 |
aspS | proS | MmarC5_1792 | MmarC5_0880 | 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). | 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). | 0.929 |
aspS | thrS | MmarC5_1792 | MmarC5_1223 | 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). | threonyl-tRNA synthetase; 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); Belongs to the class-II aminoacyl-tRNA synthetase family. | 0.802 |
aspS | topA | MmarC5_1792 | MmarC5_0781 | 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). | 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 [...] | 0.903 |
aspS | tyrS | MmarC5_1792 | MmarC5_1410 | 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). | 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. | 0.833 |