node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
AHY46577.1 | aspS | RradSPS_1294 | RradSPS_1355 | TIGR01033: DNA-binding regulatory protein, YebC/PmpR family; TIGRFAM:TIGR01033:Transcriptional regulator TACO1-like; COG:COG0217: Uncharacterized conserved protein [Function unknown]; Pfam:PF01709:Transcriptional regulator TACO1-like; Hamap:MF_00693:Transcriptional regulator TACO1-like; SUPERFAMILY:SSF75625:No Description. | aspartate--tRNA ligase; 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. | 0.828 |
AHY46577.1 | metG | RradSPS_1294 | RradSPS_0379 | TIGR01033: DNA-binding regulatory protein, YebC/PmpR family; TIGRFAM:TIGR01033:Transcriptional regulator TACO1-like; COG:COG0217: Uncharacterized conserved protein [Function unknown]; Pfam:PF01709:Transcriptional regulator TACO1-like; Hamap:MF_00693:Transcriptional regulator TACO1-like; SUPERFAMILY:SSF75625:No Description. | metG: methionine--tRNA ligase; Is required not only for elongation of protein synthesis but also for the initiation of all mRNA translation through initiator tRNA(fMet) aminoacylation. | 0.548 |
alaS | aspS | RradSPS_1363 | RradSPS_1355 | alaS: alanine--tRNA ligase; 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. | aspartate--tRNA ligase; 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. | 0.916 |
alaS | gatB | RradSPS_1363 | RradSPS_0719 | alaS: alanine--tRNA ligase; 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. | gatB: aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase, B subunit; Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl- tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an activated phospho-Asp- tRNA(Asn) or phospho-Glu-tRNA(Gln); Belongs to the GatB/GatE family. GatB subfamily. | 0.461 |
alaS | guaA | RradSPS_1363 | RradSPS_0697 | alaS: alanine--tRNA ligase; 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. | GMP synthase (glutamine-hydrolyzing), C-terminal domain; Catalyzes the synthesis of GMP from XMP. | 0.644 |
alaS | hisS | RradSPS_1363 | RradSPS_1335 | alaS: alanine--tRNA ligase; 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. | hisS: histidine--tRNA ligase; TIGRFAM:TIGR00442:Histidine-tRNA ligase; COG:COG0124: Histidyl-tRNA synthetase [Translation ribosomal structure and biogenesis]; Pfam:PF13393:Histidyl-tRNA synthetase; Hamap:MF_00127:Histidine-tRNA ligase; PIRSF:PIRSF001549:Histidine-tRNA ligase/ATP phosphoribosyltransferase regulatory subunit; ProSiteProfiles:PS50862:Aminoacyl-tRNA synthetase, class II; SUPERFAMILY:SSF55681:No Description;KEGG: 00970; Reactome: REACT_71. | 0.689 |
alaS | leuS | RradSPS_1363 | RradSPS_2761 | alaS: alanine--tRNA ligase; 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:TIGR00396:Leucine-tRNA ligase, bacterial/mitochondrial; COG:COG0495: Leucyl-tRNA synthetase [Translation ribosomal structure and biogenesis]; Pfam:PF13603:Leucyl-tRNA synthetase, editing domain; Hamap:MF_00049_B:Leucine-tRNA ligase, bacterial/mitochondrial; PRINTS:PR00985:Leucine-tRNA ligase, bacterial/mitochondrial; SUPERFAMILY:SSF52374:No Description;KEGG: 00290; KEGG: 00970; leuS_bact; Belongs to the class-I aminoacyl-tRNA synthetase family. | 0.806 |
alaS | metG | RradSPS_1363 | RradSPS_0379 | alaS: alanine--tRNA ligase; 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. | metG: methionine--tRNA ligase; Is required not only for elongation of protein synthesis but also for the initiation of all mRNA translation through initiator tRNA(fMet) aminoacylation. | 0.868 |
alaS | pheT | RradSPS_1363 | RradSPS_1282 | alaS: alanine--tRNA ligase; 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:TIGR00472:Phenylalanine-tRNA ligase, class IIc, beta subunit, bacterial; COG:COG0072: Phenylalanyl-tRNA synthetase beta subunit [Translation ribosomal structure and biogenesis]; Pfam:PF03483:B3/B4 tRNA-binding domain; Hamap:MF_00283:Phenylalanine-tRNA ligase, class IIc, beta subunit, bacterial; ProSiteProfiles:PS51483:tRNA synthetase, B5-domain; SMART:SM00873:B3/B4 tRNA-binding domain; SUPERFAMILY:SSF56037:Phenylalanyl-tRNA synthetase, B3/B4;KEGG: 00970; pheT_bact. | 0.892 |
alaS | valS | RradSPS_1363 | RradSPS_1545 | alaS: alanine--tRNA ligase; 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. | valS: valine--tRNA ligase; 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. | 0.793 |
aspS | AHY46577.1 | RradSPS_1355 | RradSPS_1294 | aspartate--tRNA ligase; 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. | TIGR01033: DNA-binding regulatory protein, YebC/PmpR family; TIGRFAM:TIGR01033:Transcriptional regulator TACO1-like; COG:COG0217: Uncharacterized conserved protein [Function unknown]; Pfam:PF01709:Transcriptional regulator TACO1-like; Hamap:MF_00693:Transcriptional regulator TACO1-like; SUPERFAMILY:SSF75625:No Description. | 0.828 |
aspS | alaS | RradSPS_1355 | RradSPS_1363 | aspartate--tRNA ligase; 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. | alaS: alanine--tRNA ligase; 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. | 0.916 |
aspS | gatB | RradSPS_1355 | RradSPS_0719 | aspartate--tRNA ligase; 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. | gatB: aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase, B subunit; Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl- tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an activated phospho-Asp- tRNA(Asn) or phospho-Glu-tRNA(Gln); Belongs to the GatB/GatE family. GatB subfamily. | 0.986 |
aspS | gatC | RradSPS_1355 | RradSPS_0717 | aspartate--tRNA ligase; 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. | gatC: aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase, C subunit; Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl- tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an activated phospho-Asp- tRNA(Asn) or phospho-Glu-tRNA(Gln); Belongs to the GatC family. | 0.881 |
aspS | guaA | RradSPS_1355 | RradSPS_0697 | aspartate--tRNA ligase; 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. | GMP synthase (glutamine-hydrolyzing), C-terminal domain; Catalyzes the synthesis of GMP from XMP. | 0.808 |
aspS | hisS | RradSPS_1355 | RradSPS_1335 | aspartate--tRNA ligase; 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. | hisS: histidine--tRNA ligase; TIGRFAM:TIGR00442:Histidine-tRNA ligase; COG:COG0124: Histidyl-tRNA synthetase [Translation ribosomal structure and biogenesis]; Pfam:PF13393:Histidyl-tRNA synthetase; Hamap:MF_00127:Histidine-tRNA ligase; PIRSF:PIRSF001549:Histidine-tRNA ligase/ATP phosphoribosyltransferase regulatory subunit; ProSiteProfiles:PS50862:Aminoacyl-tRNA synthetase, class II; SUPERFAMILY:SSF55681:No Description;KEGG: 00970; Reactome: REACT_71. | 0.880 |
aspS | leuS | RradSPS_1355 | RradSPS_2761 | aspartate--tRNA ligase; 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. | TIGRFAM:TIGR00396:Leucine-tRNA ligase, bacterial/mitochondrial; COG:COG0495: Leucyl-tRNA synthetase [Translation ribosomal structure and biogenesis]; Pfam:PF13603:Leucyl-tRNA synthetase, editing domain; Hamap:MF_00049_B:Leucine-tRNA ligase, bacterial/mitochondrial; PRINTS:PR00985:Leucine-tRNA ligase, bacterial/mitochondrial; SUPERFAMILY:SSF52374:No Description;KEGG: 00290; KEGG: 00970; leuS_bact; Belongs to the class-I aminoacyl-tRNA synthetase family. | 0.760 |
aspS | metG | RradSPS_1355 | RradSPS_0379 | aspartate--tRNA ligase; 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. | metG: methionine--tRNA ligase; Is required not only for elongation of protein synthesis but also for the initiation of all mRNA translation through initiator tRNA(fMet) aminoacylation. | 0.772 |
aspS | pheT | RradSPS_1355 | RradSPS_1282 | aspartate--tRNA ligase; 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. | TIGRFAM:TIGR00472:Phenylalanine-tRNA ligase, class IIc, beta subunit, bacterial; COG:COG0072: Phenylalanyl-tRNA synthetase beta subunit [Translation ribosomal structure and biogenesis]; Pfam:PF03483:B3/B4 tRNA-binding domain; Hamap:MF_00283:Phenylalanine-tRNA ligase, class IIc, beta subunit, bacterial; ProSiteProfiles:PS51483:tRNA synthetase, B5-domain; SMART:SM00873:B3/B4 tRNA-binding domain; SUPERFAMILY:SSF56037:Phenylalanyl-tRNA synthetase, B3/B4;KEGG: 00970; pheT_bact. | 0.819 |
aspS | valS | RradSPS_1355 | RradSPS_1545 | aspartate--tRNA ligase; 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. | valS: valine--tRNA ligase; 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. | 0.788 |