node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
ADR21640.1 | aspS | Ftrac_1652 | Ftrac_2962 | Protein of unknown function DUF28; COGs: COG0217 conserved hypothetical protein; InterPro IPR002876; KEGG: wsu:WS1016 hypothetical protein; PFAM: protein of unknown function DUF28; SPTR: UPF0082 protein WS1016; PFAM: Domain of unknown function DUF28; TIGRFAM: DNA-binding regulatory protein, YebC/PmpR family. | aspartyl-tRNA synthetase; Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp- AMP and then transferred to the acceptor end of tRNA(Asp). Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily. | 0.782 |
ADR21640.1 | metG | Ftrac_1652 | Ftrac_1005 | Protein of unknown function DUF28; COGs: COG0217 conserved hypothetical protein; InterPro IPR002876; KEGG: wsu:WS1016 hypothetical protein; PFAM: protein of unknown function DUF28; SPTR: UPF0082 protein WS1016; PFAM: Domain of unknown function DUF28; TIGRFAM: DNA-binding regulatory protein, YebC/PmpR family. | methionyl-tRNA synthetase; Is required not only for elongation of protein synthesis but also for the initiation of all mRNA translation through initiator tRNA(fMet) aminoacylation. | 0.510 |
alaS | aspS | Ftrac_2911 | Ftrac_2962 | alanyl-tRNA synthetase; Catalyzes the attachment of alanine to tRNA(Ala) in a two- step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) via its editing domain. | aspartyl-tRNA synthetase; Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp- AMP and then transferred to the acceptor end of tRNA(Asp). Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily. | 0.884 |
alaS | gatB | Ftrac_2911 | Ftrac_2912 | alanyl-tRNA synthetase; Catalyzes the attachment of alanine to tRNA(Ala) in a two- step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) via its editing domain. | 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. | 0.879 |
alaS | guaA | Ftrac_2911 | Ftrac_3641 | alanyl-tRNA synthetase; Catalyzes the attachment of alanine to tRNA(Ala) in a two- step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) via its editing domain. | GMP synthase, large subunit; Catalyzes the synthesis of GMP from XMP. | 0.557 |
alaS | hisS | Ftrac_2911 | Ftrac_1513 | alanyl-tRNA synthetase; Catalyzes the attachment of alanine to tRNA(Ala) in a two- step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) via its editing domain. | COGs: COG0124 Histidyl-tRNA synthetase; InterProIPR006195: IPR002314: IPR004154: IPR015807: IPR 004516; KEGG: dfe:Dfer_1143 histidyl-tRNA synthetase; PFAM: tRNA synthetase class II (G H P and S); Anticodon-binding domain protein; PRIAM: Histidine--tRNA ligase; SPTR: Histidyl-tRNA synthetase; TIGRFAM: histidyl-tRNA synthetase; PFAM: Anticodon binding domain; tRNA synthetase class II core domain (G, H, P, S and T); TIGRFAM: histidyl-tRNA synthetase. | 0.667 |
alaS | leuS | Ftrac_2911 | Ftrac_1194 | alanyl-tRNA synthetase; Catalyzes the attachment of alanine to tRNA(Ala) in a two- step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) via its editing domain. | COGs: COG0495 Leucyl-tRNA synthetase; InterPro IPR001412: IPR002300: IPR013155: IPR002302; KEGG: phe:Phep_3538 leucyl-tRNA synthetase; PFAM: tRNA synthetase valyl/leucyl anticodon-binding; aminoacyl-tRNA synthetase class Ia; SPTR: Leucyl-tRNA synthetase; TIGRFAM: leucyl-tRNA synthetase; PFAM: tRNA synthetases class I (I, L, M and V); Anticodon-binding domain; TIGRFAM: leucyl-tRNA synthetase, eubacterial and mitochondrial family. | 0.741 |
alaS | metG | Ftrac_2911 | Ftrac_1005 | alanyl-tRNA synthetase; Catalyzes the attachment of alanine to tRNA(Ala) in a two- step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) via its editing domain. | methionyl-tRNA synthetase; Is required not only for elongation of protein synthesis but also for the initiation of all mRNA translation through initiator tRNA(fMet) aminoacylation. | 0.826 |
alaS | pheT | Ftrac_2911 | Ftrac_2869 | alanyl-tRNA synthetase; Catalyzes the attachment of alanine to tRNA(Ala) in a two- step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) via its editing domain. | COGs: COG0072 Phenylalanyl-tRNA synthetase beta subunit; InterProIPR002547: IPR005121: IPR004532: IPR005146: IPR 005147; KEGG: sli:Slin_0287 phenylalanyl-tRNA synthetase, beta subunit; PFAM: B3/4 domain protein; t-RNA-binding domain-containing protein; tRNA synthetase B5; ferredoxin-fold anticodon-binding; SPTR: Phenylalanyl-tRNA synthetase, beta subunit; TIGRFAM: phenylalanyl-tRNA synthetase, beta subunit; PFAM: tRNA synthetase B5 domain; B3/4 domain; Ferredoxin-fold anticodon binding domain; Putative tRNA binding domain; TIGRFAM: phenylalanyl-tRNA synthetase, beta subunit, non-spiroc [...] | 0.854 |
alaS | valS | Ftrac_2911 | Ftrac_0821 | alanyl-tRNA synthetase; Catalyzes the attachment of alanine to tRNA(Ala) in a two- step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) via its editing domain. | 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 1 subfamily. | 0.811 |
aspS | ADR21640.1 | Ftrac_2962 | Ftrac_1652 | aspartyl-tRNA synthetase; Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp- AMP and then transferred to the acceptor end of tRNA(Asp). Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily. | Protein of unknown function DUF28; COGs: COG0217 conserved hypothetical protein; InterPro IPR002876; KEGG: wsu:WS1016 hypothetical protein; PFAM: protein of unknown function DUF28; SPTR: UPF0082 protein WS1016; PFAM: Domain of unknown function DUF28; TIGRFAM: DNA-binding regulatory protein, YebC/PmpR family. | 0.782 |
aspS | alaS | Ftrac_2962 | Ftrac_2911 | aspartyl-tRNA synthetase; Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp- AMP and then transferred to the acceptor end of tRNA(Asp). Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily. | alanyl-tRNA synthetase; Catalyzes the attachment of alanine to tRNA(Ala) in a two- step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) via its editing domain. | 0.884 |
aspS | gatB | Ftrac_2962 | Ftrac_2912 | aspartyl-tRNA synthetase; Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp- AMP and then transferred to the acceptor end of tRNA(Asp). 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. | 0.974 |
aspS | gatC | Ftrac_2962 | Ftrac_3468 | aspartyl-tRNA synthetase; Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp- AMP and then transferred to the acceptor end of tRNA(Asp). 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. | 0.782 |
aspS | guaA | Ftrac_2962 | Ftrac_3641 | aspartyl-tRNA synthetase; Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp- AMP and then transferred to the acceptor end of tRNA(Asp). Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily. | GMP synthase, large subunit; Catalyzes the synthesis of GMP from XMP. | 0.782 |
aspS | hisS | Ftrac_2962 | Ftrac_1513 | aspartyl-tRNA synthetase; Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp- AMP and then transferred to the acceptor end of tRNA(Asp). Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily. | COGs: COG0124 Histidyl-tRNA synthetase; InterProIPR006195: IPR002314: IPR004154: IPR015807: IPR 004516; KEGG: dfe:Dfer_1143 histidyl-tRNA synthetase; PFAM: tRNA synthetase class II (G H P and S); Anticodon-binding domain protein; PRIAM: Histidine--tRNA ligase; SPTR: Histidyl-tRNA synthetase; TIGRFAM: histidyl-tRNA synthetase; PFAM: Anticodon binding domain; tRNA synthetase class II core domain (G, H, P, S and T); TIGRFAM: histidyl-tRNA synthetase. | 0.815 |
aspS | leuS | Ftrac_2962 | Ftrac_1194 | aspartyl-tRNA synthetase; Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp- AMP and then transferred to the acceptor end of tRNA(Asp). Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily. | COGs: COG0495 Leucyl-tRNA synthetase; InterPro IPR001412: IPR002300: IPR013155: IPR002302; KEGG: phe:Phep_3538 leucyl-tRNA synthetase; PFAM: tRNA synthetase valyl/leucyl anticodon-binding; aminoacyl-tRNA synthetase class Ia; SPTR: Leucyl-tRNA synthetase; TIGRFAM: leucyl-tRNA synthetase; PFAM: tRNA synthetases class I (I, L, M and V); Anticodon-binding domain; TIGRFAM: leucyl-tRNA synthetase, eubacterial and mitochondrial family. | 0.693 |
aspS | metG | Ftrac_2962 | Ftrac_1005 | aspartyl-tRNA synthetase; Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp- AMP and then transferred to the acceptor end of tRNA(Asp). Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily. | methionyl-tRNA synthetase; Is required not only for elongation of protein synthesis but also for the initiation of all mRNA translation through initiator tRNA(fMet) aminoacylation. | 0.686 |
aspS | pheT | Ftrac_2962 | Ftrac_2869 | aspartyl-tRNA synthetase; Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp- AMP and then transferred to the acceptor end of tRNA(Asp). Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily. | COGs: COG0072 Phenylalanyl-tRNA synthetase beta subunit; InterProIPR002547: IPR005121: IPR004532: IPR005146: IPR 005147; KEGG: sli:Slin_0287 phenylalanyl-tRNA synthetase, beta subunit; PFAM: B3/4 domain protein; t-RNA-binding domain-containing protein; tRNA synthetase B5; ferredoxin-fold anticodon-binding; SPTR: Phenylalanyl-tRNA synthetase, beta subunit; TIGRFAM: phenylalanyl-tRNA synthetase, beta subunit; PFAM: tRNA synthetase B5 domain; B3/4 domain; Ferredoxin-fold anticodon binding domain; Putative tRNA binding domain; TIGRFAM: phenylalanyl-tRNA synthetase, beta subunit, non-spiroc [...] | 0.762 |
aspS | valS | Ftrac_2962 | Ftrac_0821 | aspartyl-tRNA synthetase; Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp- AMP and then transferred to the acceptor end of tRNA(Asp). Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily. | 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 1 subfamily. | 0.757 |