node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
Dde_0518 | asnS | Dde_0518 | Dde_0099 | PFAM: Amidase; KEGG: mxa:MXAN_2852 amidase family protein; Belongs to the amidase family. | TIGRFAM: Asparaginyl-tRNA synthetase, class IIb; KEGG: dvu:DVU0007 asparaginyl-tRNA synthetase; PFAM: Aminoacyl-tRNA synthetase, class II (D/K/N); Nucleic acid binding, OB-fold, tRNA/helicase-type. | 0.802 |
Dde_0518 | aspS | Dde_0518 | Dde_0012 | PFAM: Amidase; KEGG: mxa:MXAN_2852 amidase family protein; Belongs to the amidase family. | 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. | 0.802 |
Dde_0518 | gatB | Dde_0518 | Dde_2615 | PFAM: Amidase; KEGG: mxa:MXAN_2852 amidase family protein; Belongs to the amidase family. | glutamyl-tRNA(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. | 0.990 |
Dde_0518 | gatC | Dde_0518 | Dde_1021 | PFAM: Amidase; KEGG: mxa:MXAN_2852 amidase family protein; Belongs to the amidase family. | glutamyl-tRNA(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. | 0.982 |
Dde_0518 | glnS | Dde_0518 | Dde_0626 | PFAM: Amidase; KEGG: mxa:MXAN_2852 amidase family protein; Belongs to the amidase family. | TIGRFAM: Glutaminyl-tRNA synthetase, class Ic; KEGG: dvm:DvMF_1485 glutaminyl-tRNA synthetase; PFAM: Glutamyl/glutaminyl-tRNA synthetase, class Ic, catalytic domain; Glutamyl/glutaminyl-tRNA synthetase, class Ic, anti-codon binding domain. | 0.762 |
Dde_0518 | guaA | Dde_0518 | Dde_1470 | PFAM: Amidase; KEGG: mxa:MXAN_2852 amidase family protein; Belongs to the amidase family. | GMP synthase, large subunit; Catalyzes the synthesis of GMP from XMP. | 0.706 |
Dde_3237 | aspS | Dde_3237 | Dde_0012 | SMART: Pyruvate-flavodoxin oxidoreductase, EKR domain; TIGRFAM: Pyruvate-flavodoxin oxidoreductase; KEGG: dvl:Dvul_0348 pyruvate flavodoxin/ferredoxin oxidoreductase domain-containing protein; PFAM: Pyruvate flavodoxin/ferredoxin oxidoreductase, N-terminal; Pyruvate-flavodoxin oxidoreductase, EKR domain; 4Fe-4S ferredoxin, iron-sulphur binding, subgroup; Thiamine pyrophosphate enzyme, C-terminal TPP-binding; Pyruvate/ketoisovalerate oxidoreductase; Belongs to the pyruvate:ferredoxin/flavodoxin oxidoreductase family. | 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. | 0.790 |
Dde_3237 | gatC | Dde_3237 | Dde_1021 | SMART: Pyruvate-flavodoxin oxidoreductase, EKR domain; TIGRFAM: Pyruvate-flavodoxin oxidoreductase; KEGG: dvl:Dvul_0348 pyruvate flavodoxin/ferredoxin oxidoreductase domain-containing protein; PFAM: Pyruvate flavodoxin/ferredoxin oxidoreductase, N-terminal; Pyruvate-flavodoxin oxidoreductase, EKR domain; 4Fe-4S ferredoxin, iron-sulphur binding, subgroup; Thiamine pyrophosphate enzyme, C-terminal TPP-binding; Pyruvate/ketoisovalerate oxidoreductase; Belongs to the pyruvate:ferredoxin/flavodoxin oxidoreductase family. | glutamyl-tRNA(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. | 0.762 |
asnS | Dde_0518 | Dde_0099 | Dde_0518 | TIGRFAM: Asparaginyl-tRNA synthetase, class IIb; KEGG: dvu:DVU0007 asparaginyl-tRNA synthetase; PFAM: Aminoacyl-tRNA synthetase, class II (D/K/N); Nucleic acid binding, OB-fold, tRNA/helicase-type. | PFAM: Amidase; KEGG: mxa:MXAN_2852 amidase family protein; Belongs to the amidase family. | 0.802 |
asnS | aspS | Dde_0099 | Dde_0012 | TIGRFAM: Asparaginyl-tRNA synthetase, class IIb; KEGG: dvu:DVU0007 asparaginyl-tRNA synthetase; PFAM: Aminoacyl-tRNA synthetase, class II (D/K/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. | 0.429 |
asnS | gatA | Dde_0099 | Dde_1020 | TIGRFAM: Asparaginyl-tRNA synthetase, class IIb; KEGG: dvu:DVU0007 asparaginyl-tRNA synthetase; PFAM: Aminoacyl-tRNA synthetase, class II (D/K/N); Nucleic acid binding, OB-fold, tRNA/helicase-type. | glutamyl-tRNA(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). | 0.979 |
asnS | gatB | Dde_0099 | Dde_2615 | TIGRFAM: Asparaginyl-tRNA synthetase, class IIb; KEGG: dvu:DVU0007 asparaginyl-tRNA synthetase; PFAM: Aminoacyl-tRNA synthetase, class II (D/K/N); Nucleic acid binding, OB-fold, tRNA/helicase-type. | glutamyl-tRNA(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. | 0.992 |
asnS | gatC | Dde_0099 | Dde_1021 | TIGRFAM: Asparaginyl-tRNA synthetase, class IIb; KEGG: dvu:DVU0007 asparaginyl-tRNA synthetase; PFAM: Aminoacyl-tRNA synthetase, class II (D/K/N); Nucleic acid binding, OB-fold, tRNA/helicase-type. | glutamyl-tRNA(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. | 0.976 |
asnS | glnS | Dde_0099 | Dde_0626 | TIGRFAM: Asparaginyl-tRNA synthetase, class IIb; KEGG: dvu:DVU0007 asparaginyl-tRNA synthetase; PFAM: Aminoacyl-tRNA synthetase, class II (D/K/N); Nucleic acid binding, OB-fold, tRNA/helicase-type. | TIGRFAM: Glutaminyl-tRNA synthetase, class Ic; KEGG: dvm:DvMF_1485 glutaminyl-tRNA synthetase; PFAM: Glutamyl/glutaminyl-tRNA synthetase, class Ic, catalytic domain; Glutamyl/glutaminyl-tRNA synthetase, class Ic, anti-codon binding domain. | 0.850 |
asnS | guaA | Dde_0099 | Dde_1470 | TIGRFAM: Asparaginyl-tRNA synthetase, class IIb; KEGG: dvu:DVU0007 asparaginyl-tRNA synthetase; PFAM: Aminoacyl-tRNA synthetase, class II (D/K/N); Nucleic acid binding, OB-fold, tRNA/helicase-type. | GMP synthase, large subunit; Catalyzes the synthesis of GMP from XMP. | 0.621 |
aspS | Dde_0518 | Dde_0012 | Dde_0518 | 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. | PFAM: Amidase; KEGG: mxa:MXAN_2852 amidase family protein; Belongs to the amidase family. | 0.802 |
aspS | Dde_3237 | Dde_0012 | Dde_3237 | 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. | SMART: Pyruvate-flavodoxin oxidoreductase, EKR domain; TIGRFAM: Pyruvate-flavodoxin oxidoreductase; KEGG: dvl:Dvul_0348 pyruvate flavodoxin/ferredoxin oxidoreductase domain-containing protein; PFAM: Pyruvate flavodoxin/ferredoxin oxidoreductase, N-terminal; Pyruvate-flavodoxin oxidoreductase, EKR domain; 4Fe-4S ferredoxin, iron-sulphur binding, subgroup; Thiamine pyrophosphate enzyme, C-terminal TPP-binding; Pyruvate/ketoisovalerate oxidoreductase; Belongs to the pyruvate:ferredoxin/flavodoxin oxidoreductase family. | 0.790 |
aspS | asnS | Dde_0012 | Dde_0099 | 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. | TIGRFAM: Asparaginyl-tRNA synthetase, class IIb; KEGG: dvu:DVU0007 asparaginyl-tRNA synthetase; PFAM: Aminoacyl-tRNA synthetase, class II (D/K/N); Nucleic acid binding, OB-fold, tRNA/helicase-type. | 0.429 |
aspS | gatA | Dde_0012 | Dde_1020 | 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. | glutamyl-tRNA(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). | 0.853 |
aspS | gatB | Dde_0012 | Dde_2615 | 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. | glutamyl-tRNA(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. | 0.994 |