node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
asnS | aspS | dsat_0966 | dsat_2759 | TIGRFAM: asparaginyl-tRNA synthetase; HAMAP : Asparaginyl-tRNA synthetase; KEGG: dvl:Dvul_0001 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. | 0.795 |
asnS | gatA | dsat_0966 | dsat_2627 | TIGRFAM: asparaginyl-tRNA synthetase; HAMAP : Asparaginyl-tRNA synthetase; KEGG: dvl:Dvul_0001 asparaginyl-tRNA synthetase; PFAM: tRNA synthetase class II (D K and N), nucleic acid binding OB-fold tRNA/helicase-type. | Glutamyl-tRNA(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). | 0.964 |
asnS | gatB | dsat_0966 | dsat_2312 | TIGRFAM: asparaginyl-tRNA synthetase; HAMAP : Asparaginyl-tRNA synthetase; KEGG: dvl:Dvul_0001 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 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. | 0.997 |
asnS | gatC | dsat_0966 | dsat_2628 | TIGRFAM: asparaginyl-tRNA synthetase; HAMAP : Asparaginyl-tRNA synthetase; KEGG: dvl:Dvul_0001 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 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. | 0.925 |
asnS | glnS | dsat_0966 | dsat_0995 | TIGRFAM: asparaginyl-tRNA synthetase; HAMAP : Asparaginyl-tRNA synthetase; KEGG: dvl:Dvul_0001 asparaginyl-tRNA synthetase; PFAM: tRNA synthetase class II (D K and N), nucleic acid binding OB-fold tRNA/helicase-type. | TIGRFAM: glutaminyl-tRNA synthetase; HAMAP : Glutaminyl-tRNA synthetase; KEGG: dvm:DvMF_1485 glutaminyl-tRNA synthetase; PFAM: Glutamyl/glutaminyl-tRNA synthetase, class Ic, catalytic domain-containing protein, Glutamyl/glutaminyl-tRNA synthetase, class Ic, anti-codon binding domain-containing protein. | 0.808 |
asnS | gltX | dsat_0966 | dsat_0607 | TIGRFAM: asparaginyl-tRNA synthetase; HAMAP : Asparaginyl-tRNA synthetase; KEGG: dvl:Dvul_0001 asparaginyl-tRNA synthetase; PFAM: tRNA synthetase class II (D K and N), nucleic acid binding OB-fold tRNA/helicase-type. | 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). | 0.801 |
aspS | asnS | dsat_2759 | dsat_0966 | 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; HAMAP : Asparaginyl-tRNA synthetase; KEGG: dvl:Dvul_0001 asparaginyl-tRNA synthetase; PFAM: tRNA synthetase class II (D K and N), nucleic acid binding OB-fold tRNA/helicase-type. | 0.795 |
aspS | dsat_2101 | dsat_2759 | dsat_2101 | 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: pyruvate ferredoxin/flavodoxin oxidoreductase; PFAM: pyruvate flavodoxin/ferredoxin oxidoreductase domain protein, 4Fe-4S ferredoxin iron-sulfur binding domain-containing protein, Pyruvate/ketoisovalerate oxidoreductase, Pyruvate-flavodoxin oxidoreductase, EKR domain-containing protein, thiamine pyrophosphate TPP-binding domain-containing protein; KEGG: dvl:Dvul_0348 pyruvate flavodoxin/ferredoxin oxidoreductase domain-containing protein; SMART: Pyruvate-flavodoxin oxidoreductase, EKR domain-containing protein. | 0.812 |
aspS | gatA | dsat_2759 | dsat_2627 | 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 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). | 0.901 |
aspS | gatB | dsat_2759 | dsat_2312 | 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. | 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. | 0.997 |
aspS | gatC | dsat_2759 | dsat_2628 | 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. | 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. | 0.973 |
aspS | glnS | dsat_2759 | dsat_0995 | 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: glutaminyl-tRNA synthetase; HAMAP : Glutaminyl-tRNA synthetase; KEGG: dvm:DvMF_1485 glutaminyl-tRNA synthetase; PFAM: Glutamyl/glutaminyl-tRNA synthetase, class Ic, catalytic domain-containing protein, Glutamyl/glutaminyl-tRNA synthetase, class Ic, anti-codon binding domain-containing protein. | 0.748 |
aspS | gltX | dsat_2759 | dsat_0607 | 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 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). | 0.629 |
atpH | dsat_2101 | dsat_0223 | dsat_2101 | ATP synthase subunit delta; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. | TIGRFAM: pyruvate ferredoxin/flavodoxin oxidoreductase; PFAM: pyruvate flavodoxin/ferredoxin oxidoreductase domain protein, 4Fe-4S ferredoxin iron-sulfur binding domain-containing protein, Pyruvate/ketoisovalerate oxidoreductase, Pyruvate-flavodoxin oxidoreductase, EKR domain-containing protein, thiamine pyrophosphate TPP-binding domain-containing protein; KEGG: dvl:Dvul_0348 pyruvate flavodoxin/ferredoxin oxidoreductase domain-containing protein; SMART: Pyruvate-flavodoxin oxidoreductase, EKR domain-containing protein. | 0.645 |
atpH | gatA | dsat_0223 | dsat_2627 | ATP synthase subunit delta; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. | Glutamyl-tRNA(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). | 0.426 |
atpH | gatB | dsat_0223 | dsat_2312 | ATP synthase subunit delta; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. | 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. | 0.687 |
atpH | gatC | dsat_0223 | dsat_2628 | ATP synthase subunit delta; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. | 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. | 0.745 |
atpH | rpsZ | dsat_0223 | dsat_2542 | ATP synthase subunit delta; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. | Ribosomal protein S14, type Z; Binds 16S rRNA, required for the assembly of 30S particles and may also be responsible for determining the conformation of the 16S rRNA at the A site. | 0.846 |
dsat_2101 | aspS | dsat_2101 | dsat_2759 | TIGRFAM: pyruvate ferredoxin/flavodoxin oxidoreductase; PFAM: pyruvate flavodoxin/ferredoxin oxidoreductase domain protein, 4Fe-4S ferredoxin iron-sulfur binding domain-containing protein, Pyruvate/ketoisovalerate oxidoreductase, Pyruvate-flavodoxin oxidoreductase, EKR domain-containing protein, thiamine pyrophosphate TPP-binding domain-containing protein; KEGG: dvl:Dvul_0348 pyruvate flavodoxin/ferredoxin oxidoreductase domain-containing protein; SMART: Pyruvate-flavodoxin oxidoreductase, EKR domain-containing protein. | 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. | 0.812 |
dsat_2101 | atpH | dsat_2101 | dsat_0223 | TIGRFAM: pyruvate ferredoxin/flavodoxin oxidoreductase; PFAM: pyruvate flavodoxin/ferredoxin oxidoreductase domain protein, 4Fe-4S ferredoxin iron-sulfur binding domain-containing protein, Pyruvate/ketoisovalerate oxidoreductase, Pyruvate-flavodoxin oxidoreductase, EKR domain-containing protein, thiamine pyrophosphate TPP-binding domain-containing protein; KEGG: dvl:Dvul_0348 pyruvate flavodoxin/ferredoxin oxidoreductase domain-containing protein; SMART: Pyruvate-flavodoxin oxidoreductase, EKR domain-containing protein. | ATP synthase subunit delta; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. | 0.645 |