| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| AGB48602.1 | AGB49971.1 | Metho_0329 | Metho_1787 | Phosphoglycerol geranylgeranyltransferase; Prenyltransferase that catalyzes the transfer of the geranylgeranyl moiety of geranylgeranyl diphosphate (GGPP) to the C3 hydroxyl of sn-glycerol-1-phosphate (G1P). This reaction is the first ether-bond-formation step in the biosynthesis of archaeal membrane lipids. | TIGRFAM: DNA topoisomerase I, archaeal. | 0.423 |
| AGB48602.1 | gatA | Metho_0329 | Metho_0332 | Phosphoglycerol geranylgeranyltransferase; Prenyltransferase that catalyzes the transfer of the geranylgeranyl moiety of geranylgeranyl diphosphate (GGPP) to the C3 hydroxyl of sn-glycerol-1-phosphate (G1P). This reaction is the first ether-bond-formation step in the biosynthesis of archaeal membrane lipids. | glutamyl-tRNA(Gln) and/or aspartyl-tRNA(Asn) 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). | 0.813 |
| AGB48602.1 | gatB | Metho_0329 | Metho_0331 | Phosphoglycerol geranylgeranyltransferase; Prenyltransferase that catalyzes the transfer of the geranylgeranyl moiety of geranylgeranyl diphosphate (GGPP) to the C3 hydroxyl of sn-glycerol-1-phosphate (G1P). This reaction is the first ether-bond-formation step in the biosynthesis of archaeal membrane lipids. | glutamyl-tRNA(Gln) and/or aspartyl-tRNA(Asn) 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. | 0.812 |
| AGB48602.1 | gatC | Metho_0329 | Metho_0333 | Phosphoglycerol geranylgeranyltransferase; Prenyltransferase that catalyzes the transfer of the geranylgeranyl moiety of geranylgeranyl diphosphate (GGPP) to the C3 hydroxyl of sn-glycerol-1-phosphate (G1P). This reaction is the first ether-bond-formation step in the biosynthesis of archaeal membrane lipids. | glutamyl-tRNA(Gln) and/or aspartyl-tRNA(Asn) 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. | 0.783 |
| AGB49284.1 | AGB49971.1 | Metho_1047 | Metho_1787 | metal-binding-domain/4Fe-4S-binding-domain containing ABC transporter, ATP-binding protein; TIGRFAM: MJ0570-related uncharacterized domain; TIGR00289 family protein; asparagine synthase (glutamine-hydrolyzing); arCOG00187 universal archaeal metal-binding-domain/4Fe-4S-binding-domain containing ABC transporter, ATP-binding protein. | TIGRFAM: DNA topoisomerase I, archaeal. | 0.748 |
| AGB49284.1 | aspS | Metho_1047 | Metho_1011 | metal-binding-domain/4Fe-4S-binding-domain containing ABC transporter, ATP-binding protein; TIGRFAM: MJ0570-related uncharacterized domain; TIGR00289 family protein; asparagine synthase (glutamine-hydrolyzing); arCOG00187 universal archaeal metal-binding-domain/4Fe-4S-binding-domain containing ABC transporter, ATP-binding protein. | aspartyl-tRNA synthetase, archaeal type; 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). | 0.673 |
| AGB49284.1 | gatA | Metho_1047 | Metho_0332 | metal-binding-domain/4Fe-4S-binding-domain containing ABC transporter, ATP-binding protein; TIGRFAM: MJ0570-related uncharacterized domain; TIGR00289 family protein; asparagine synthase (glutamine-hydrolyzing); arCOG00187 universal archaeal metal-binding-domain/4Fe-4S-binding-domain containing ABC transporter, ATP-binding protein. | glutamyl-tRNA(Gln) and/or aspartyl-tRNA(Asn) 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). | 0.835 |
| AGB49284.1 | gatB | Metho_1047 | Metho_0331 | metal-binding-domain/4Fe-4S-binding-domain containing ABC transporter, ATP-binding protein; TIGRFAM: MJ0570-related uncharacterized domain; TIGR00289 family protein; asparagine synthase (glutamine-hydrolyzing); arCOG00187 universal archaeal metal-binding-domain/4Fe-4S-binding-domain containing ABC transporter, ATP-binding protein. | glutamyl-tRNA(Gln) and/or aspartyl-tRNA(Asn) 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. | 0.890 |
| AGB49284.1 | gatC | Metho_1047 | Metho_0333 | metal-binding-domain/4Fe-4S-binding-domain containing ABC transporter, ATP-binding protein; TIGRFAM: MJ0570-related uncharacterized domain; TIGR00289 family protein; asparagine synthase (glutamine-hydrolyzing); arCOG00187 universal archaeal metal-binding-domain/4Fe-4S-binding-domain containing ABC transporter, ATP-binding protein. | glutamyl-tRNA(Gln) and/or aspartyl-tRNA(Asn) 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. | 0.853 |
| AGB49284.1 | gatD | Metho_1047 | Metho_1010 | metal-binding-domain/4Fe-4S-binding-domain containing ABC transporter, ATP-binding protein; TIGRFAM: MJ0570-related uncharacterized domain; TIGR00289 family protein; asparagine synthase (glutamine-hydrolyzing); arCOG00187 universal archaeal metal-binding-domain/4Fe-4S-binding-domain containing ABC transporter, ATP-binding 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. | 0.690 |
| AGB49284.1 | gltX | Metho_1047 | Metho_0813 | metal-binding-domain/4Fe-4S-binding-domain containing ABC transporter, ATP-binding protein; TIGRFAM: MJ0570-related uncharacterized domain; TIGR00289 family protein; asparagine synthase (glutamine-hydrolyzing); arCOG00187 universal archaeal metal-binding-domain/4Fe-4S-binding-domain containing ABC transporter, ATP-binding protein. | glutamyl-tRNA synthetase, archaeal and eukaryotic family; 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). | 0.776 |
| AGB49284.1 | valS | Metho_1047 | Metho_1867 | metal-binding-domain/4Fe-4S-binding-domain containing ABC transporter, ATP-binding protein; TIGRFAM: MJ0570-related uncharacterized domain; TIGR00289 family protein; asparagine synthase (glutamine-hydrolyzing); arCOG00187 universal archaeal metal-binding-domain/4Fe-4S-binding-domain containing ABC transporter, ATP-binding protein. | 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 2 subfamily. | 0.878 |
| AGB49971.1 | AGB48602.1 | Metho_1787 | Metho_0329 | TIGRFAM: DNA topoisomerase I, archaeal. | Phosphoglycerol geranylgeranyltransferase; Prenyltransferase that catalyzes the transfer of the geranylgeranyl moiety of geranylgeranyl diphosphate (GGPP) to the C3 hydroxyl of sn-glycerol-1-phosphate (G1P). This reaction is the first ether-bond-formation step in the biosynthesis of archaeal membrane lipids. | 0.423 |
| AGB49971.1 | AGB49284.1 | Metho_1787 | Metho_1047 | TIGRFAM: DNA topoisomerase I, archaeal. | metal-binding-domain/4Fe-4S-binding-domain containing ABC transporter, ATP-binding protein; TIGRFAM: MJ0570-related uncharacterized domain; TIGR00289 family protein; asparagine synthase (glutamine-hydrolyzing); arCOG00187 universal archaeal metal-binding-domain/4Fe-4S-binding-domain containing ABC transporter, ATP-binding protein. | 0.748 |
| AGB49971.1 | aspS | Metho_1787 | Metho_1011 | TIGRFAM: DNA topoisomerase I, archaeal. | aspartyl-tRNA synthetase, archaeal type; 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). | 0.515 |
| AGB49971.1 | gatA | Metho_1787 | Metho_0332 | TIGRFAM: DNA topoisomerase I, archaeal. | glutamyl-tRNA(Gln) and/or aspartyl-tRNA(Asn) 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). | 0.736 |
| AGB49971.1 | gatB | Metho_1787 | Metho_0331 | TIGRFAM: DNA topoisomerase I, archaeal. | glutamyl-tRNA(Gln) and/or aspartyl-tRNA(Asn) 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. | 0.758 |
| AGB49971.1 | gatC | Metho_1787 | Metho_0333 | TIGRFAM: DNA topoisomerase I, archaeal. | glutamyl-tRNA(Gln) and/or aspartyl-tRNA(Asn) 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. | 0.741 |
| AGB49971.1 | valS | Metho_1787 | Metho_1867 | TIGRFAM: DNA topoisomerase I, archaeal. | 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 2 subfamily. | 0.435 |
| aspS | AGB49284.1 | Metho_1011 | Metho_1047 | aspartyl-tRNA synthetase, archaeal type; 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). | metal-binding-domain/4Fe-4S-binding-domain containing ABC transporter, ATP-binding protein; TIGRFAM: MJ0570-related uncharacterized domain; TIGR00289 family protein; asparagine synthase (glutamine-hydrolyzing); arCOG00187 universal archaeal metal-binding-domain/4Fe-4S-binding-domain containing ABC transporter, ATP-binding protein. | 0.673 |