node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
EKX95215.1 | EKX95216.1 | HMPREF9163_02329 | HMPREF9163_02330 | Coproporphyrinogen dehydrogenase HemZ; KEGG: cth:Cthe_1341 1.4e-81 coproporphyrinogen III oxidase K02495; Psort location: Cytoplasmic, score: 9.97. | Transcriptional regulator, Fur family; KEGG: apb:SAR116_1155 4.7e-12 ferric uptake regulation protein, putative K03711; Psort location: Cytoplasmic, score: 9.97; Belongs to the Fur family. | 0.815 |
EKX95215.1 | aspS | HMPREF9163_02329 | HMPREF9163_02327 | Coproporphyrinogen dehydrogenase HemZ; KEGG: cth:Cthe_1341 1.4e-81 coproporphyrinogen III oxidase K02495; Psort location: Cytoplasmic, score: 9.97. | 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. | 0.813 |
EKX95215.1 | hisS | HMPREF9163_02329 | HMPREF9163_02328 | Coproporphyrinogen dehydrogenase HemZ; KEGG: cth:Cthe_1341 1.4e-81 coproporphyrinogen III oxidase K02495; Psort location: Cytoplasmic, score: 9.97. | histidine--tRNA ligase; KEGG: afn:Acfer_1513 1.4e-140 histidyl-tRNA synthetase K01892; Psort location: Cytoplasmic, score: 10.00. | 0.813 |
EKX95216.1 | EKX95215.1 | HMPREF9163_02330 | HMPREF9163_02329 | Transcriptional regulator, Fur family; KEGG: apb:SAR116_1155 4.7e-12 ferric uptake regulation protein, putative K03711; Psort location: Cytoplasmic, score: 9.97; Belongs to the Fur family. | Coproporphyrinogen dehydrogenase HemZ; KEGG: cth:Cthe_1341 1.4e-81 coproporphyrinogen III oxidase K02495; Psort location: Cytoplasmic, score: 9.97. | 0.815 |
EKX95216.1 | aspS | HMPREF9163_02330 | HMPREF9163_02327 | Transcriptional regulator, Fur family; KEGG: apb:SAR116_1155 4.7e-12 ferric uptake regulation protein, putative K03711; Psort location: Cytoplasmic, score: 9.97; Belongs to the Fur 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 |
EKX95216.1 | hisS | HMPREF9163_02330 | HMPREF9163_02328 | Transcriptional regulator, Fur family; KEGG: apb:SAR116_1155 4.7e-12 ferric uptake regulation protein, putative K03711; Psort location: Cytoplasmic, score: 9.97; Belongs to the Fur family. | histidine--tRNA ligase; KEGG: afn:Acfer_1513 1.4e-140 histidyl-tRNA synthetase K01892; Psort location: Cytoplasmic, score: 10.00. | 0.817 |
EKY01593.1 | alaS | HMPREF9163_00185 | HMPREF9163_00837 | 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). As ProRS can inadvertently accommodate and process non-cognate amino acids such as alanine and cysteine, to avoid such errors it has two additional distinct editing activities against alanine. One activity is designated as 'pretransfer' editing and involves the tRNA(Pro)-independent hydrolysis of activated Ala-AMP. The other activity is designated 'posttransfer' editing and involves deacy [...] | 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. | 0.640 |
EKY01593.1 | aspS | HMPREF9163_00185 | HMPREF9163_02327 | 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). As ProRS can inadvertently accommodate and process non-cognate amino acids such as alanine and cysteine, to avoid such errors it has two additional distinct editing activities against alanine. One activity is designated as 'pretransfer' editing and involves the tRNA(Pro)-independent hydrolysis of activated Ala-AMP. The other activity is designated 'posttransfer' editing and involves deacy [...] | 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 |
EKY01593.1 | gatA | HMPREF9163_00185 | HMPREF9163_00913 | 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). As ProRS can inadvertently accommodate and process non-cognate amino acids such as alanine and cysteine, to avoid such errors it has two additional distinct editing activities against alanine. One activity is designated as 'pretransfer' editing and involves the tRNA(Pro)-independent hydrolysis of activated Ala-AMP. The other activity is designated 'posttransfer' editing and involves deacy [...] | aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase, A subunit; Allows the formation of correctly charged Gln-tRNA(Gln) through the transamidation of misacylated Glu-tRNA(Gln) in organisms which lack glutaminyl-tRNA synthetase. The reaction takes place in the presence of glutamine and ATP through an activated gamma-phospho-Glu- tRNA(Gln). | 0.410 |
EKY01593.1 | guaA | HMPREF9163_00185 | HMPREF9163_00883 | 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). As ProRS can inadvertently accommodate and process non-cognate amino acids such as alanine and cysteine, to avoid such errors it has two additional distinct editing activities against alanine. One activity is designated as 'pretransfer' editing and involves the tRNA(Pro)-independent hydrolysis of activated Ala-AMP. The other activity is designated 'posttransfer' editing and involves deacy [...] | GMP synthase domain protein; Catalyzes the synthesis of GMP from XMP. | 0.765 |
EKY01593.1 | hisS | HMPREF9163_00185 | HMPREF9163_02328 | 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). As ProRS can inadvertently accommodate and process non-cognate amino acids such as alanine and cysteine, to avoid such errors it has two additional distinct editing activities against alanine. One activity is designated as 'pretransfer' editing and involves the tRNA(Pro)-independent hydrolysis of activated Ala-AMP. The other activity is designated 'posttransfer' editing and involves deacy [...] | histidine--tRNA ligase; KEGG: afn:Acfer_1513 1.4e-140 histidyl-tRNA synthetase K01892; Psort location: Cytoplasmic, score: 10.00. | 0.515 |
EKY01593.1 | valS | HMPREF9163_00185 | HMPREF9163_01936 | 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). As ProRS can inadvertently accommodate and process non-cognate amino acids such as alanine and cysteine, to avoid such errors it has two additional distinct editing activities against alanine. One activity is designated as 'pretransfer' editing and involves the tRNA(Pro)-independent hydrolysis of activated Ala-AMP. The other activity is designated 'posttransfer' editing and involves deacy [...] | 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. | 0.736 |
alaS | EKY01593.1 | HMPREF9163_00837 | HMPREF9163_00185 | 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. | 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). As ProRS can inadvertently accommodate and process non-cognate amino acids such as alanine and cysteine, to avoid such errors it has two additional distinct editing activities against alanine. One activity is designated as 'pretransfer' editing and involves the tRNA(Pro)-independent hydrolysis of activated Ala-AMP. The other activity is designated 'posttransfer' editing and involves deacy [...] | 0.640 |
alaS | aspS | HMPREF9163_00837 | HMPREF9163_02327 | 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. | 0.842 |
alaS | gatB | HMPREF9163_00837 | HMPREF9163_00912 | 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. | 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. | 0.559 |
alaS | guaA | HMPREF9163_00837 | HMPREF9163_00883 | 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 domain protein; Catalyzes the synthesis of GMP from XMP. | 0.778 |
alaS | hisS | HMPREF9163_00837 | HMPREF9163_02328 | 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. | histidine--tRNA ligase; KEGG: afn:Acfer_1513 1.4e-140 histidyl-tRNA synthetase K01892; Psort location: Cytoplasmic, score: 10.00. | 0.849 |
alaS | valS | HMPREF9163_00837 | HMPREF9163_01936 | 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. | 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. | 0.878 |
aspS | EKX95215.1 | HMPREF9163_02327 | HMPREF9163_02329 | 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. | Coproporphyrinogen dehydrogenase HemZ; KEGG: cth:Cthe_1341 1.4e-81 coproporphyrinogen III oxidase K02495; Psort location: Cytoplasmic, score: 9.97. | 0.813 |
aspS | EKX95216.1 | HMPREF9163_02327 | HMPREF9163_02330 | 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. | Transcriptional regulator, Fur family; KEGG: apb:SAR116_1155 4.7e-12 ferric uptake regulation protein, putative K03711; Psort location: Cytoplasmic, score: 9.97; Belongs to the Fur family. | 0.815 |