node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
Bind_0433 | Bind_1302 | Bind_0433 | Bind_1302 | PFAM: glutamyl-tRNA synthetase class Ic; KEGG: rpc:RPC_4885 glutamyl-Q tRNA(Asp) synthetase; Belongs to the class-I aminoacyl-tRNA synthetase family. | PFAM: Amidase; KEGG: cak:Caul_3620 amidase. | 0.677 |
Bind_0433 | aspS | Bind_0433 | Bind_1396 | PFAM: glutamyl-tRNA synthetase class Ic; KEGG: rpc:RPC_4885 glutamyl-Q tRNA(Asp) synthetase; Belongs to the class-I aminoacyl-tRNA synthetase 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. | 0.517 |
Bind_0433 | gatA | Bind_0433 | Bind_1878 | PFAM: glutamyl-tRNA synthetase class Ic; KEGG: rpc:RPC_4885 glutamyl-Q tRNA(Asp) synthetase; Belongs to the class-I aminoacyl-tRNA synthetase family. | 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). | 0.677 |
Bind_0433 | gatB | Bind_0433 | Bind_1877 | PFAM: glutamyl-tRNA synthetase class Ic; KEGG: rpc:RPC_4885 glutamyl-Q tRNA(Asp) synthetase; Belongs to the class-I aminoacyl-tRNA synthetase 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. | 0.714 |
Bind_0433 | guaA | Bind_0433 | Bind_2895 | PFAM: glutamyl-tRNA synthetase class Ic; KEGG: rpc:RPC_4885 glutamyl-Q tRNA(Asp) synthetase; Belongs to the class-I aminoacyl-tRNA synthetase family. | GMP synthase, large subunit; Catalyzes the synthesis of GMP from XMP. | 0.622 |
Bind_0433 | pheT | Bind_0433 | Bind_3247 | PFAM: glutamyl-tRNA synthetase class Ic; KEGG: rpc:RPC_4885 glutamyl-Q tRNA(Asp) synthetase; Belongs to the class-I aminoacyl-tRNA synthetase family. | KEGG: mex:Mext_1630 phenylalanyl-tRNA synthetase, beta subunit; TIGRFAM: phenylalanyl-tRNA synthetase, beta subunit. | 0.801 |
Bind_1302 | Bind_0433 | Bind_1302 | Bind_0433 | PFAM: Amidase; KEGG: cak:Caul_3620 amidase. | PFAM: glutamyl-tRNA synthetase class Ic; KEGG: rpc:RPC_4885 glutamyl-Q tRNA(Asp) synthetase; Belongs to the class-I aminoacyl-tRNA synthetase family. | 0.677 |
Bind_1302 | aspS | Bind_1302 | Bind_1396 | PFAM: Amidase; KEGG: cak:Caul_3620 amidase. | 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. | 0.559 |
Bind_1302 | atpF3 | Bind_1302 | Bind_2778 | PFAM: Amidase; KEGG: cak:Caul_3620 amidase. | H+transporting two-sector ATPase B/B' subunit; 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. | 0.501 |
Bind_1302 | gatB | Bind_1302 | Bind_1877 | PFAM: Amidase; KEGG: cak:Caul_3620 amidase. | 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. | 0.989 |
Bind_1302 | gatC | Bind_1302 | Bind_1879 | PFAM: Amidase; KEGG: cak:Caul_3620 amidase. | 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 |
Bind_1302 | gltX1 | Bind_1302 | Bind_1410 | PFAM: Amidase; KEGG: cak:Caul_3620 amidase. | 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); Belongs to the class-I aminoacyl-tRNA synthetase family. Glutamate--tRNA ligase type 1 subfamily. | 0.677 |
Bind_1302 | gltX2 | Bind_1302 | Bind_3674 | PFAM: Amidase; KEGG: cak:Caul_3620 amidase. | 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); Belongs to the class-I aminoacyl-tRNA synthetase family. Glutamate--tRNA ligase type 1 subfamily. | 0.677 |
Bind_1302 | guaA | Bind_1302 | Bind_2895 | PFAM: Amidase; KEGG: cak:Caul_3620 amidase. | GMP synthase, large subunit; Catalyzes the synthesis of GMP from XMP. | 0.572 |
Bind_1302 | pheT | Bind_1302 | Bind_3247 | PFAM: Amidase; KEGG: cak:Caul_3620 amidase. | KEGG: mex:Mext_1630 phenylalanyl-tRNA synthetase, beta subunit; TIGRFAM: phenylalanyl-tRNA synthetase, beta subunit. | 0.439 |
aspS | Bind_0433 | Bind_1396 | Bind_0433 | 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: glutamyl-tRNA synthetase class Ic; KEGG: rpc:RPC_4885 glutamyl-Q tRNA(Asp) synthetase; Belongs to the class-I aminoacyl-tRNA synthetase family. | 0.517 |
aspS | Bind_1302 | Bind_1396 | Bind_1302 | 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: cak:Caul_3620 amidase. | 0.559 |
aspS | gatA | Bind_1396 | Bind_1878 | 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). | 0.785 |
aspS | gatB | Bind_1396 | Bind_1877 | 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. | 0.992 |
aspS | gatC | Bind_1396 | Bind_1879 | 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, 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. | 0.892 |