node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
NtpA | aspS | BPSL0645 | BPSL0644 | Similar to Escherichia coli dATP pyrophosphohydrolase NudB or NtpA SWALL:NUDB_ECOLI (SWALL:P24236) (150 aa) fasta scores: E(): 8.2e-16, 44.82% id in 145 aa, and to Ralstonia solanacearum probable datp pyrophosphohydrolase protein rsc0468 or rs04429 SWALL:Q8Y268 (EMBL:AL646059) (162 aa) fasta scores: E(): 8.4e-36, 64.55% id in 158 aa. | 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); Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily. | 0.770 |
alaS | aspS | BPSL2009 | BPSL0644 | 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); Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily. | 0.809 |
alaS | gatB | BPSL2009 | BPSL0189 | 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. | glutamyl-tRNA amidotransferase subunit B; 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. | 0.493 |
alaS | glnS | BPSL2009 | BPSL2012 | 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. | Similar to Escherichia coli glutaminyl-tRNA synthetase GlnS or b0680 SWALL:SYQ_ECOLI (SWALL:P00962) (553 aa) fasta scores: E(): 9.9e-131, 57.34% id in 558 aa, and to Ralstonia solanacearum glutaminyl-tRNA synthetase rsc0791 or rs05046 SWALL:Q8Y199 (EMBL:AL646061) (580 aa) fasta scores: E(): 1.9e-175, 70.35% id in 570 aa. | 0.534 |
alaS | guaA | BPSL2009 | BPSL2127 | 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. | GMP synthase [glutamine-hydrolyzing]; Catalyzes the synthesis of GMP from XMP. | 0.696 |
alaS | hisS | BPSL2009 | BPSL1514 | 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. | histidyl-tRNA synthetase; Similar to Escherichia coli, and Escherichia coli O157:H7 histidyl-tRNA synthetase HisS or b2514 or z3777 or ecs3376 SWALL:SYH_ECOLI (SWALL:P04804) (423 aa) fasta scores: E(): 1.2e-82, 54.52% id in 420 aa, and to Ralstonia solanacearum probable histidine-tRNA synthetase protein HisS or rsc1216 or rs02790 SWALL:Q8Y029 (EMBL:AL646063) (432 aa) fasta scores: E(): 1e-130, 75.4% id in 435 aa. | 0.773 |
alaS | metG | BPSL2009 | BPSL0998 | 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. | 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. | 0.862 |
alaS | pheT | BPSL2009 | BPSL1940 | 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. | Similar to Escherichia coli phenylalanyl-tRNA synthetase beta chain PheT or b1713 SWALL:SYFB_ECOLI (SWALL:P07395) (795 aa) fasta scores: E(): 3.2e-119, 41.84% id in 815 aa, and to Ralstonia solanacearum probable phenylalanyl-tRNA synthetase beta chain protein rsc1582 or rs05825 SWALL:Q8XZ24 (EMBL:AL646065) (809 aa) fasta scores: E(): 0, 67.53% id in 810 aa. | 0.919 |
alaS | valS | BPSL2009 | BPSL1980 | 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. | Putative 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. | 0.923 |
aspS | NtpA | BPSL0644 | BPSL0645 | 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); Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily. | Similar to Escherichia coli dATP pyrophosphohydrolase NudB or NtpA SWALL:NUDB_ECOLI (SWALL:P24236) (150 aa) fasta scores: E(): 8.2e-16, 44.82% id in 145 aa, and to Ralstonia solanacearum probable datp pyrophosphohydrolase protein rsc0468 or rs04429 SWALL:Q8Y268 (EMBL:AL646059) (162 aa) fasta scores: E(): 8.4e-36, 64.55% id in 158 aa. | 0.770 |
aspS | alaS | BPSL0644 | BPSL2009 | 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); Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily. | 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. | 0.809 |
aspS | gatB | BPSL0644 | BPSL0189 | 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); Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily. | glutamyl-tRNA amidotransferase subunit B; 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. | 0.993 |
aspS | gatC | BPSL0644 | BPSL0187 | 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); Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily. | glutamyl-tRNA amidotransferase subunit C; 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. | 0.887 |
aspS | glnS | BPSL0644 | BPSL2012 | 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); Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily. | Similar to Escherichia coli glutaminyl-tRNA synthetase GlnS or b0680 SWALL:SYQ_ECOLI (SWALL:P00962) (553 aa) fasta scores: E(): 9.9e-131, 57.34% id in 558 aa, and to Ralstonia solanacearum glutaminyl-tRNA synthetase rsc0791 or rs05046 SWALL:Q8Y199 (EMBL:AL646061) (580 aa) fasta scores: E(): 1.9e-175, 70.35% id in 570 aa. | 0.764 |
aspS | guaA | BPSL0644 | BPSL2127 | 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); Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily. | GMP synthase [glutamine-hydrolyzing]; Catalyzes the synthesis of GMP from XMP. | 0.824 |
aspS | hisS | BPSL0644 | BPSL1514 | 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); Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily. | histidyl-tRNA synthetase; Similar to Escherichia coli, and Escherichia coli O157:H7 histidyl-tRNA synthetase HisS or b2514 or z3777 or ecs3376 SWALL:SYH_ECOLI (SWALL:P04804) (423 aa) fasta scores: E(): 1.2e-82, 54.52% id in 420 aa, and to Ralstonia solanacearum probable histidine-tRNA synthetase protein HisS or rsc1216 or rs02790 SWALL:Q8Y029 (EMBL:AL646063) (432 aa) fasta scores: E(): 1e-130, 75.4% id in 435 aa. | 0.952 |
aspS | metG | BPSL0644 | BPSL0998 | 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); Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily. | 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. | 0.756 |
aspS | pheT | BPSL0644 | BPSL1940 | 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); Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily. | Similar to Escherichia coli phenylalanyl-tRNA synthetase beta chain PheT or b1713 SWALL:SYFB_ECOLI (SWALL:P07395) (795 aa) fasta scores: E(): 3.2e-119, 41.84% id in 815 aa, and to Ralstonia solanacearum probable phenylalanyl-tRNA synthetase beta chain protein rsc1582 or rs05825 SWALL:Q8XZ24 (EMBL:AL646065) (809 aa) fasta scores: E(): 0, 67.53% id in 810 aa. | 0.838 |
aspS | valS | BPSL0644 | BPSL1980 | 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); Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily. | Putative 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. | 0.909 |
gatB | alaS | BPSL0189 | BPSL2009 | glutamyl-tRNA amidotransferase subunit B; 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. | 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. | 0.493 |