node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
argS | aspS | RradSPS_1604 | RradSPS_1355 | argS: arginine--tRNA ligase; TIGRFAM:TIGR00456:Arginine-tRNA ligase, class Ia; COG:COG0018: Arginyl-tRNA synthetase [Translation ribosomal structure and biogenesis]; Pfam:PF00750:Arginyl-tRNA synthetase, class Ia, core; Hamap:MF_00123:Arginine-tRNA ligase, class Ia; PRINTS:PR01038:Arginyl-tRNA synthetase, class Ia, core; ProSitePatterns:PS00178:Aminoacyl-tRNA synthetase, class I, conserved site; SMART:SM00836:DALR anticodon binding; SUPERFAMILY:SSF52374:No Description;KEGG: 00970; Reactome: REACT_71. | 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. | 0.587 |
argS | ileS | RradSPS_1604 | RradSPS_0548 | argS: arginine--tRNA ligase; TIGRFAM:TIGR00456:Arginine-tRNA ligase, class Ia; COG:COG0018: Arginyl-tRNA synthetase [Translation ribosomal structure and biogenesis]; Pfam:PF00750:Arginyl-tRNA synthetase, class Ia, core; Hamap:MF_00123:Arginine-tRNA ligase, class Ia; PRINTS:PR01038:Arginyl-tRNA synthetase, class Ia, core; ProSitePatterns:PS00178:Aminoacyl-tRNA synthetase, class I, conserved site; SMART:SM00836:DALR anticodon binding; SUPERFAMILY:SSF52374:No Description;KEGG: 00970; Reactome: REACT_71. | ileS: isoleucine--tRNA ligase; 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. | 0.920 |
argS | leuS | RradSPS_1604 | RradSPS_2761 | argS: arginine--tRNA ligase; TIGRFAM:TIGR00456:Arginine-tRNA ligase, class Ia; COG:COG0018: Arginyl-tRNA synthetase [Translation ribosomal structure and biogenesis]; Pfam:PF00750:Arginyl-tRNA synthetase, class Ia, core; Hamap:MF_00123:Arginine-tRNA ligase, class Ia; PRINTS:PR01038:Arginyl-tRNA synthetase, class Ia, core; ProSitePatterns:PS00178:Aminoacyl-tRNA synthetase, class I, conserved site; SMART:SM00836:DALR anticodon binding; SUPERFAMILY:SSF52374:No Description;KEGG: 00970; Reactome: REACT_71. | 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. | 0.877 |
argS | metG | RradSPS_1604 | RradSPS_0379 | argS: arginine--tRNA ligase; TIGRFAM:TIGR00456:Arginine-tRNA ligase, class Ia; COG:COG0018: Arginyl-tRNA synthetase [Translation ribosomal structure and biogenesis]; Pfam:PF00750:Arginyl-tRNA synthetase, class Ia, core; Hamap:MF_00123:Arginine-tRNA ligase, class Ia; PRINTS:PR01038:Arginyl-tRNA synthetase, class Ia, core; ProSitePatterns:PS00178:Aminoacyl-tRNA synthetase, class I, conserved site; SMART:SM00836:DALR anticodon binding; SUPERFAMILY:SSF52374:No Description;KEGG: 00970; Reactome: REACT_71. | 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. | 0.937 |
argS | pheS | RradSPS_1604 | RradSPS_1281 | argS: arginine--tRNA ligase; TIGRFAM:TIGR00456:Arginine-tRNA ligase, class Ia; COG:COG0018: Arginyl-tRNA synthetase [Translation ribosomal structure and biogenesis]; Pfam:PF00750:Arginyl-tRNA synthetase, class Ia, core; Hamap:MF_00123:Arginine-tRNA ligase, class Ia; PRINTS:PR01038:Arginyl-tRNA synthetase, class Ia, core; ProSitePatterns:PS00178:Aminoacyl-tRNA synthetase, class I, conserved site; SMART:SM00836:DALR anticodon binding; SUPERFAMILY:SSF52374:No Description;KEGG: 00970; Reactome: REACT_71. | pheS: phenylalanine--tRNA ligase, alpha subunit; TIGRFAM:TIGR00468:Phenylalanyl-tRNA synthetase, class IIc, alpha subunit; COG:COG0016: Phenylalanyl-tRNA synthetase alpha subunit [Translation ribosomal structure and biogenesis]; Pfam:PF01409:Phenylalanyl-tRNA synthetase; Hamap:MF_00281:Phenylalanine-tRNA ligase alpha chain 1, bacterial; ProSiteProfiles:PS50862:Aminoacyl-tRNA synthetase, class II; SUPERFAMILY:SSF55681:No Description;KEGG: 00970. | 0.511 |
argS | pheT | RradSPS_1604 | RradSPS_1282 | argS: arginine--tRNA ligase; TIGRFAM:TIGR00456:Arginine-tRNA ligase, class Ia; COG:COG0018: Arginyl-tRNA synthetase [Translation ribosomal structure and biogenesis]; Pfam:PF00750:Arginyl-tRNA synthetase, class Ia, core; Hamap:MF_00123:Arginine-tRNA ligase, class Ia; PRINTS:PR01038:Arginyl-tRNA synthetase, class Ia, core; ProSitePatterns:PS00178:Aminoacyl-tRNA synthetase, class I, conserved site; SMART:SM00836:DALR anticodon binding; SUPERFAMILY:SSF52374:No Description;KEGG: 00970; Reactome: REACT_71. | 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. | 0.855 |
argS | prfA | RradSPS_1604 | RradSPS_1594 | argS: arginine--tRNA ligase; TIGRFAM:TIGR00456:Arginine-tRNA ligase, class Ia; COG:COG0018: Arginyl-tRNA synthetase [Translation ribosomal structure and biogenesis]; Pfam:PF00750:Arginyl-tRNA synthetase, class Ia, core; Hamap:MF_00123:Arginine-tRNA ligase, class Ia; PRINTS:PR01038:Arginyl-tRNA synthetase, class Ia, core; ProSitePatterns:PS00178:Aminoacyl-tRNA synthetase, class I, conserved site; SMART:SM00836:DALR anticodon binding; SUPERFAMILY:SSF52374:No Description;KEGG: 00970; Reactome: REACT_71. | prfA: peptide chain release factor 1; Peptide chain release factor 1 directs the termination of translation in response to the peptide chain termination codons UAG and UAA. | 0.684 |
argS | proS | RradSPS_1604 | RradSPS_1045 | argS: arginine--tRNA ligase; TIGRFAM:TIGR00456:Arginine-tRNA ligase, class Ia; COG:COG0018: Arginyl-tRNA synthetase [Translation ribosomal structure and biogenesis]; Pfam:PF00750:Arginyl-tRNA synthetase, class Ia, core; Hamap:MF_00123:Arginine-tRNA ligase, class Ia; PRINTS:PR01038:Arginyl-tRNA synthetase, class Ia, core; ProSitePatterns:PS00178:Aminoacyl-tRNA synthetase, class I, conserved site; SMART:SM00836:DALR anticodon binding; SUPERFAMILY:SSF52374:No Description;KEGG: 00970; Reactome: REACT_71. | proline--tRNA ligase; 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). | 0.906 |
argS | tyrS | RradSPS_1604 | RradSPS_1287 | argS: arginine--tRNA ligase; TIGRFAM:TIGR00456:Arginine-tRNA ligase, class Ia; COG:COG0018: Arginyl-tRNA synthetase [Translation ribosomal structure and biogenesis]; Pfam:PF00750:Arginyl-tRNA synthetase, class Ia, core; Hamap:MF_00123:Arginine-tRNA ligase, class Ia; PRINTS:PR01038:Arginyl-tRNA synthetase, class Ia, core; ProSitePatterns:PS00178:Aminoacyl-tRNA synthetase, class I, conserved site; SMART:SM00836:DALR anticodon binding; SUPERFAMILY:SSF52374:No Description;KEGG: 00970; Reactome: REACT_71. | tyrS: tyrosine--tRNA ligase; 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 2 subfamily. | 0.806 |
argS | valS | RradSPS_1604 | RradSPS_1545 | argS: arginine--tRNA ligase; TIGRFAM:TIGR00456:Arginine-tRNA ligase, class Ia; COG:COG0018: Arginyl-tRNA synthetase [Translation ribosomal structure and biogenesis]; Pfam:PF00750:Arginyl-tRNA synthetase, class Ia, core; Hamap:MF_00123:Arginine-tRNA ligase, class Ia; PRINTS:PR01038:Arginyl-tRNA synthetase, class Ia, core; ProSitePatterns:PS00178:Aminoacyl-tRNA synthetase, class I, conserved site; SMART:SM00836:DALR anticodon binding; SUPERFAMILY:SSF52374:No Description;KEGG: 00970; Reactome: REACT_71. | 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. | 0.756 |
aspS | argS | RradSPS_1355 | RradSPS_1604 | 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. | argS: arginine--tRNA ligase; TIGRFAM:TIGR00456:Arginine-tRNA ligase, class Ia; COG:COG0018: Arginyl-tRNA synthetase [Translation ribosomal structure and biogenesis]; Pfam:PF00750:Arginyl-tRNA synthetase, class Ia, core; Hamap:MF_00123:Arginine-tRNA ligase, class Ia; PRINTS:PR01038:Arginyl-tRNA synthetase, class Ia, core; ProSitePatterns:PS00178:Aminoacyl-tRNA synthetase, class I, conserved site; SMART:SM00836:DALR anticodon binding; SUPERFAMILY:SSF52374:No Description;KEGG: 00970; Reactome: REACT_71. | 0.587 |
aspS | ileS | RradSPS_1355 | RradSPS_0548 | 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. | ileS: isoleucine--tRNA ligase; 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. | 0.702 |
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 | pheS | RradSPS_1355 | RradSPS_1281 | 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. | pheS: phenylalanine--tRNA ligase, alpha subunit; TIGRFAM:TIGR00468:Phenylalanyl-tRNA synthetase, class IIc, alpha subunit; COG:COG0016: Phenylalanyl-tRNA synthetase alpha subunit [Translation ribosomal structure and biogenesis]; Pfam:PF01409:Phenylalanyl-tRNA synthetase; Hamap:MF_00281:Phenylalanine-tRNA ligase alpha chain 1, bacterial; ProSiteProfiles:PS50862:Aminoacyl-tRNA synthetase, class II; SUPERFAMILY:SSF55681:No Description;KEGG: 00970. | 0.580 |
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 | proS | RradSPS_1355 | RradSPS_1045 | 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. | proline--tRNA ligase; 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). | 0.665 |
aspS | tyrS | RradSPS_1355 | RradSPS_1287 | 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. | tyrS: tyrosine--tRNA ligase; 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 2 subfamily. | 0.621 |
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 |
ileS | argS | RradSPS_0548 | RradSPS_1604 | ileS: isoleucine--tRNA ligase; 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. | argS: arginine--tRNA ligase; TIGRFAM:TIGR00456:Arginine-tRNA ligase, class Ia; COG:COG0018: Arginyl-tRNA synthetase [Translation ribosomal structure and biogenesis]; Pfam:PF00750:Arginyl-tRNA synthetase, class Ia, core; Hamap:MF_00123:Arginine-tRNA ligase, class Ia; PRINTS:PR01038:Arginyl-tRNA synthetase, class Ia, core; ProSitePatterns:PS00178:Aminoacyl-tRNA synthetase, class I, conserved site; SMART:SM00836:DALR anticodon binding; SUPERFAMILY:SSF52374:No Description;KEGG: 00970; Reactome: REACT_71. | 0.920 |