| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| HisS | aspS | CLOSCI_01141 | CLOSCI_01142 | Putative histidine--tRNA ligase; KEGG: lxx:Lxx17220 1.3e-74 hisS; histidyl-tRNA synthetase K01892; COG: COG0124 Histidyl-tRNA synthetase; Psort location: Cytoplasmic, score: 10.00; Belongs to the class-II aminoacyl-tRNA synthetase family. | 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. | 0.933 |
| HisS | aspS-2 | CLOSCI_01141 | CLOSCI_03166 | Putative histidine--tRNA ligase; KEGG: lxx:Lxx17220 1.3e-74 hisS; histidyl-tRNA synthetase K01892; COG: COG0124 Histidyl-tRNA synthetase; Psort location: Cytoplasmic, score: 10.00; Belongs to the class-II aminoacyl-tRNA synthetase family. | 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. | 0.815 |
| HisS | aspS-3 | CLOSCI_01141 | CLOSCI_03776 | Putative histidine--tRNA ligase; KEGG: lxx:Lxx17220 1.3e-74 hisS; histidyl-tRNA synthetase K01892; COG: COG0124 Histidyl-tRNA synthetase; Psort location: Cytoplasmic, score: 10.00; Belongs to the class-II aminoacyl-tRNA synthetase family. | 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 2 subfamily. | 0.686 |
| HisS | guaA | CLOSCI_01141 | CLOSCI_03102 | Putative histidine--tRNA ligase; KEGG: lxx:Lxx17220 1.3e-74 hisS; histidyl-tRNA synthetase K01892; COG: COG0124 Histidyl-tRNA synthetase; Psort location: Cytoplasmic, score: 10.00; Belongs to the class-II aminoacyl-tRNA synthetase family. | GMP synthase (glutamine-hydrolyzing) domain protein; Catalyzes the synthesis of GMP from XMP. | 0.646 |
| HisS | hemZ | CLOSCI_01141 | CLOSCI_01140 | Putative histidine--tRNA ligase; KEGG: lxx:Lxx17220 1.3e-74 hisS; histidyl-tRNA synthetase K01892; COG: COG0124 Histidyl-tRNA synthetase; Psort location: Cytoplasmic, score: 10.00; Belongs to the class-II aminoacyl-tRNA synthetase family. | KEGG: cpe:CPE1935 9.2e-90 hemZ; probable coproporphyrinogen III oxidase K02495; COG: COG0635 Coproporphyrinogen III oxidase and related Fe-S oxidoreductases; Psort location: Cytoplasmic, score: 9.98. | 0.843 |
| HisS | valS | CLOSCI_01141 | CLOSCI_02273 | Putative histidine--tRNA ligase; KEGG: lxx:Lxx17220 1.3e-74 hisS; histidyl-tRNA synthetase K01892; COG: COG0124 Histidyl-tRNA synthetase; Psort location: Cytoplasmic, score: 10.00; Belongs to the class-II aminoacyl-tRNA synthetase family. | 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. | 0.722 |
| aspS | HisS | CLOSCI_01142 | CLOSCI_01141 | 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. | Putative histidine--tRNA ligase; KEGG: lxx:Lxx17220 1.3e-74 hisS; histidyl-tRNA synthetase K01892; COG: COG0124 Histidyl-tRNA synthetase; Psort location: Cytoplasmic, score: 10.00; Belongs to the class-II aminoacyl-tRNA synthetase family. | 0.933 |
| aspS | aspS-2 | CLOSCI_01142 | CLOSCI_03166 | 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. | 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. | 0.910 |
| aspS | aspS-3 | CLOSCI_01142 | CLOSCI_03776 | 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. | 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 2 subfamily. | 0.932 |
| aspS | gatB | CLOSCI_01142 | CLOSCI_03164 | 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. | 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. | 0.796 |
| aspS | gatB-2 | CLOSCI_01142 | CLOSCI_03772 | 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. | 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. | 0.952 |
| aspS | gatC | CLOSCI_01142 | CLOSCI_03774 | 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. | 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. | 0.781 |
| aspS | guaA | CLOSCI_01142 | CLOSCI_03102 | 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) domain protein; Catalyzes the synthesis of GMP from XMP. | 0.692 |
| aspS | hemZ | CLOSCI_01142 | CLOSCI_01140 | 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. | KEGG: cpe:CPE1935 9.2e-90 hemZ; probable coproporphyrinogen III oxidase K02495; COG: COG0635 Coproporphyrinogen III oxidase and related Fe-S oxidoreductases; Psort location: Cytoplasmic, score: 9.98. | 0.698 |
| aspS | nifJ | CLOSCI_01142 | CLOSCI_01585 | 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. | Pyruvate synthase; KEGG: cno:NT01CX_1854 0. nifJ; pyruvate:ferredoxin (flavodoxin) oxidoreductase K00168; COG: COG1013 Pyruvate:ferredoxin oxidoreductase and related 2-oxoacid:ferredoxin oxidoreductases, beta subunit; Psort location: Cytoplasmic, score: 8.87. | 0.718 |
| aspS | valS | CLOSCI_01142 | CLOSCI_02273 | 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. | 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. | 0.714 |
| aspS-2 | HisS | CLOSCI_03166 | CLOSCI_01141 | 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. | Putative histidine--tRNA ligase; KEGG: lxx:Lxx17220 1.3e-74 hisS; histidyl-tRNA synthetase K01892; COG: COG0124 Histidyl-tRNA synthetase; Psort location: Cytoplasmic, score: 10.00; Belongs to the class-II aminoacyl-tRNA synthetase family. | 0.815 |
| aspS-2 | aspS | CLOSCI_03166 | CLOSCI_01142 | 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. | 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. | 0.910 |
| aspS-2 | aspS-3 | CLOSCI_03166 | CLOSCI_03776 | 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. | 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 2 subfamily. | 0.932 |
| aspS-2 | gatB | CLOSCI_03166 | CLOSCI_03164 | 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. | 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. | 0.962 |