node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
Gura_1900 | Gura_3098 | Gura_1900 | Gura_3098 | PFAM: ribosomal protein L7Ae/L30e/S12e/Gadd45; protein of unknown function DUF448. | PFAM: beta-ketoacyl synthase; short-chain dehydrogenase/reductase SDR; phosphopantetheine-binding; KR. | 0.584 |
Gura_1900 | gatA | Gura_1900 | Gura_4324 | PFAM: ribosomal protein L7Ae/L30e/S12e/Gadd45; protein of unknown function DUF448. | aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit A; 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). | 0.822 |
Gura_1900 | gatB | Gura_1900 | Gura_4323 | PFAM: ribosomal protein L7Ae/L30e/S12e/Gadd45; protein of unknown function DUF448. | aspartyl/glutamyl-tRNA(Asn/Gln) 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. | 0.697 |
Gura_1900 | gatC | Gura_1900 | Gura_4325 | PFAM: ribosomal protein L7Ae/L30e/S12e/Gadd45; protein of unknown function DUF448. | aspartyl/glutamyl-tRNA(Asn/Gln) 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. | 0.698 |
Gura_1900 | glnS | Gura_1900 | Gura_4167 | PFAM: ribosomal protein L7Ae/L30e/S12e/Gadd45; protein of unknown function DUF448. | TIGRFAM: glutaminyl-tRNA synthetase; PFAM: glutamyl-tRNA synthetase, class Ic. | 0.954 |
Gura_1900 | gltX | Gura_1900 | Gura_2300 | PFAM: ribosomal protein L7Ae/L30e/S12e/Gadd45; protein of unknown function DUF448. | glutamyl-tRNA synthetase; Catalyzes the attachment of glutamate to tRNA(Glu) in a two- step reaction: glutamate is first activated by ATP to form Glu-AMP and then transferred to the acceptor end of tRNA(Glu). | 0.954 |
Gura_1900 | gluQ | Gura_1900 | Gura_2226 | PFAM: ribosomal protein L7Ae/L30e/S12e/Gadd45; protein of unknown function DUF448. | glutamyl-tRNA synthetase, class Ic; Catalyzes the tRNA-independent activation of glutamate in presence of ATP and the subsequent transfer of glutamate onto a tRNA(Asp). Glutamate is transferred on the 2-amino-5-(4,5-dihydroxy-2- cyclopenten-1-yl) moiety of the queuosine in the wobble position of the QUC anticodon; Belongs to the class-I aminoacyl-tRNA synthetase family. GluQ subfamily. | 0.954 |
Gura_1900 | guaA | Gura_1900 | Gura_3123 | PFAM: ribosomal protein L7Ae/L30e/S12e/Gadd45; protein of unknown function DUF448. | GMP synthase (glutamine-hydrolyzing); Catalyzes the synthesis of GMP from XMP. | 0.524 |
Gura_3098 | Gura_1900 | Gura_3098 | Gura_1900 | PFAM: beta-ketoacyl synthase; short-chain dehydrogenase/reductase SDR; phosphopantetheine-binding; KR. | PFAM: ribosomal protein L7Ae/L30e/S12e/Gadd45; protein of unknown function DUF448. | 0.584 |
Gura_3098 | asnS | Gura_3098 | Gura_2958 | PFAM: beta-ketoacyl synthase; short-chain dehydrogenase/reductase SDR; phosphopantetheine-binding; KR. | TIGRFAM: asparaginyl-tRNA synthetase; PFAM: tRNA synthetase, class II (D, K and N); nucleic acid binding, OB-fold, tRNA/helicase-type. | 0.625 |
Gura_3098 | aspS | Gura_3098 | Gura_2196 | PFAM: beta-ketoacyl synthase; short-chain dehydrogenase/reductase SDR; phosphopantetheine-binding; KR. | 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. | 0.523 |
Gura_3098 | gatA | Gura_3098 | Gura_4324 | PFAM: beta-ketoacyl synthase; short-chain dehydrogenase/reductase SDR; phosphopantetheine-binding; KR. | aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit A; 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). | 0.809 |
Gura_3098 | gatB | Gura_3098 | Gura_4323 | PFAM: beta-ketoacyl synthase; short-chain dehydrogenase/reductase SDR; phosphopantetheine-binding; KR. | aspartyl/glutamyl-tRNA(Asn/Gln) 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. | 0.665 |
Gura_3098 | glnS | Gura_3098 | Gura_4167 | PFAM: beta-ketoacyl synthase; short-chain dehydrogenase/reductase SDR; phosphopantetheine-binding; KR. | TIGRFAM: glutaminyl-tRNA synthetase; PFAM: glutamyl-tRNA synthetase, class Ic. | 0.622 |
Gura_3098 | gltX | Gura_3098 | Gura_2300 | PFAM: beta-ketoacyl synthase; short-chain dehydrogenase/reductase SDR; phosphopantetheine-binding; KR. | glutamyl-tRNA synthetase; Catalyzes the attachment of glutamate to tRNA(Glu) in a two- step reaction: glutamate is first activated by ATP to form Glu-AMP and then transferred to the acceptor end of tRNA(Glu). | 0.616 |
Gura_3098 | gluQ | Gura_3098 | Gura_2226 | PFAM: beta-ketoacyl synthase; short-chain dehydrogenase/reductase SDR; phosphopantetheine-binding; KR. | glutamyl-tRNA synthetase, class Ic; Catalyzes the tRNA-independent activation of glutamate in presence of ATP and the subsequent transfer of glutamate onto a tRNA(Asp). Glutamate is transferred on the 2-amino-5-(4,5-dihydroxy-2- cyclopenten-1-yl) moiety of the queuosine in the wobble position of the QUC anticodon; Belongs to the class-I aminoacyl-tRNA synthetase family. GluQ subfamily. | 0.616 |
Gura_3098 | guaA | Gura_3098 | Gura_3123 | PFAM: beta-ketoacyl synthase; short-chain dehydrogenase/reductase SDR; phosphopantetheine-binding; KR. | GMP synthase (glutamine-hydrolyzing); Catalyzes the synthesis of GMP from XMP. | 0.723 |
asnS | Gura_3098 | Gura_2958 | Gura_3098 | TIGRFAM: asparaginyl-tRNA synthetase; PFAM: tRNA synthetase, class II (D, K and N); nucleic acid binding, OB-fold, tRNA/helicase-type. | PFAM: beta-ketoacyl synthase; short-chain dehydrogenase/reductase SDR; phosphopantetheine-binding; KR. | 0.625 |
asnS | aspS | Gura_2958 | Gura_2196 | TIGRFAM: asparaginyl-tRNA synthetase; PFAM: tRNA synthetase, class II (D, K and N); nucleic acid binding, OB-fold, tRNA/helicase-type. | 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. | 0.437 |
asnS | gatA | Gura_2958 | Gura_4324 | TIGRFAM: asparaginyl-tRNA synthetase; PFAM: tRNA synthetase, class II (D, K and N); nucleic acid binding, OB-fold, tRNA/helicase-type. | aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit A; 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). | 0.986 |