node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
ABO34573.1 | aspS | MmarC5_0257 | MmarC5_1792 | TIGRFAM: selenocysteine-specific translation elongation factor; small GTP-binding protein; PFAM: protein synthesis factor, GTP-binding; elongation factor Tu, domain 2 protein; KEGG: mmp:MMP1336 archaeal translation factor specialized for selenocysteine insertion. | 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). | 0.844 |
ABO34573.1 | gatA | MmarC5_0257 | MmarC5_0065 | TIGRFAM: selenocysteine-specific translation elongation factor; small GTP-binding protein; PFAM: protein synthesis factor, GTP-binding; elongation factor Tu, domain 2 protein; KEGG: mmp:MMP1336 archaeal translation factor specialized for selenocysteine insertion. | 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). | 0.692 |
ABO34573.1 | gatE | MmarC5_0257 | MmarC5_0325 | TIGRFAM: selenocysteine-specific translation elongation factor; small GTP-binding protein; PFAM: protein synthesis factor, GTP-binding; elongation factor Tu, domain 2 protein; KEGG: mmp:MMP1336 archaeal translation factor specialized for selenocysteine insertion. | glutamyl-tRNA(Gln) amidotransferase subunit E; 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). The GatDE system is specific for glutamate and does not act on aspartate. | 0.663 |
ABO34573.1 | gltX | MmarC5_0257 | MmarC5_0583 | TIGRFAM: selenocysteine-specific translation elongation factor; small GTP-binding protein; PFAM: protein synthesis factor, GTP-binding; elongation factor Tu, domain 2 protein; KEGG: mmp:MMP1336 archaeal translation factor specialized for selenocysteine insertion. | 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). | 0.894 |
ABO34573.1 | rpl18e | MmarC5_0257 | MmarC5_0270 | TIGRFAM: selenocysteine-specific translation elongation factor; small GTP-binding protein; PFAM: protein synthesis factor, GTP-binding; elongation factor Tu, domain 2 protein; KEGG: mmp:MMP1336 archaeal translation factor specialized for selenocysteine insertion. | PFAM: ribosomal protein L15; KEGG: mmp:MMP1323 LSU ribosomal protein L18E; Belongs to the eukaryotic ribosomal protein eL18 family. | 0.851 |
ABO34642.1 | gatD | MmarC5_0326 | MmarC5_0324 | PFAM: protein of unknown function DUF87; KEGG: mmp:MMP1264 hypothetical protein. | glutamyl-tRNA(Gln) amidotransferase subunit D; 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). The GatDE system is specific for glutamate and does not act on aspartate. | 0.556 |
ABO34642.1 | gatE | MmarC5_0326 | MmarC5_0325 | PFAM: protein of unknown function DUF87; KEGG: mmp:MMP1264 hypothetical protein. | glutamyl-tRNA(Gln) amidotransferase subunit E; 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). The GatDE system is specific for glutamate and does not act on aspartate. | 0.855 |
ABO35338.1 | aspS | MmarC5_1032 | MmarC5_1792 | TIGRFAM: Asp-tRNA(Asn)/Glu-tRNA(Gln) amidotransferase, subunit C, putative; KEGG: mmp:MMP0575 Asp-tRNAAsn/Glu-tRNAGln amidotransferase subunit C. | 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). | 0.991 |
ABO35338.1 | gatA | MmarC5_1032 | MmarC5_0065 | TIGRFAM: Asp-tRNA(Asn)/Glu-tRNA(Gln) amidotransferase, subunit C, putative; KEGG: mmp:MMP0575 Asp-tRNAAsn/Glu-tRNAGln amidotransferase subunit C. | 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). | 0.999 |
ABO35338.1 | gatB | MmarC5_1032 | MmarC5_0753 | TIGRFAM: Asp-tRNA(Asn)/Glu-tRNA(Gln) amidotransferase, subunit C, putative; KEGG: mmp:MMP0575 Asp-tRNAAsn/Glu-tRNAGln amidotransferase subunit C. | 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. | 0.999 |
ABO35338.1 | gatD | MmarC5_1032 | MmarC5_0324 | TIGRFAM: Asp-tRNA(Asn)/Glu-tRNA(Gln) amidotransferase, subunit C, putative; KEGG: mmp:MMP0575 Asp-tRNAAsn/Glu-tRNAGln amidotransferase subunit C. | glutamyl-tRNA(Gln) amidotransferase subunit D; 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). The GatDE system is specific for glutamate and does not act on aspartate. | 0.914 |
ABO35338.1 | gatE | MmarC5_1032 | MmarC5_0325 | TIGRFAM: Asp-tRNA(Asn)/Glu-tRNA(Gln) amidotransferase, subunit C, putative; KEGG: mmp:MMP0575 Asp-tRNAAsn/Glu-tRNAGln amidotransferase subunit C. | glutamyl-tRNA(Gln) amidotransferase subunit E; 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). The GatDE system is specific for glutamate and does not act on aspartate. | 0.914 |
ABO35338.1 | gltX | MmarC5_1032 | MmarC5_0583 | TIGRFAM: Asp-tRNA(Asn)/Glu-tRNA(Gln) amidotransferase, subunit C, putative; KEGG: mmp:MMP0575 Asp-tRNAAsn/Glu-tRNAGln amidotransferase subunit C. | 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). | 0.430 |
aspS | ABO34573.1 | MmarC5_1792 | MmarC5_0257 | 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). | TIGRFAM: selenocysteine-specific translation elongation factor; small GTP-binding protein; PFAM: protein synthesis factor, GTP-binding; elongation factor Tu, domain 2 protein; KEGG: mmp:MMP1336 archaeal translation factor specialized for selenocysteine insertion. | 0.844 |
aspS | ABO35338.1 | MmarC5_1792 | MmarC5_1032 | 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). | TIGRFAM: Asp-tRNA(Asn)/Glu-tRNA(Gln) amidotransferase, subunit C, putative; KEGG: mmp:MMP0575 Asp-tRNAAsn/Glu-tRNAGln amidotransferase subunit C. | 0.991 |
aspS | gatA | MmarC5_1792 | MmarC5_0065 | 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). | 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). | 0.997 |
aspS | gatB | MmarC5_1792 | MmarC5_0753 | 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). | 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. | 0.999 |
aspS | gatD | MmarC5_1792 | MmarC5_0324 | 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). | glutamyl-tRNA(Gln) amidotransferase subunit D; 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). The GatDE system is specific for glutamate and does not act on aspartate. | 0.819 |
aspS | gatE | MmarC5_1792 | MmarC5_0325 | 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). | glutamyl-tRNA(Gln) amidotransferase subunit E; 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). The GatDE system is specific for glutamate and does not act on aspartate. | 0.836 |
aspS | gltX | MmarC5_1792 | MmarC5_0583 | 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). | 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). | 0.984 |