node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
EDM99274.1 | argS | BACCAP_03203 | BACCAP_04827 | 5'-3' exonuclease, N-terminal resolvase-like domain protein; KEGG: msm:MSMEG_3839 1.6e-11 DNA polymerase I K00961; COG: COG0749 DNA polymerase I - 3-5 exonuclease and polymerase domains. | arginine--tRNA ligase; KEGG: tte:TTE2533 3.5e-145 argS; arginyl-tRNA synthetase K01887; COG: COG0018 Arginyl-tRNA synthetase; Psort location: Cytoplasmic, score:9.26. | 0.460 |
EDM99274.1 | aspS-2 | BACCAP_03203 | BACCAP_03630 | 5'-3' exonuclease, N-terminal resolvase-like domain protein; KEGG: msm:MSMEG_3839 1.6e-11 DNA polymerase I K00961; COG: COG0749 DNA polymerase I - 3-5 exonuclease and polymerase domains. | aspartate--tRNA ligase; 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 2 subfamily. | 0.980 |
EDM99274.1 | leuS | BACCAP_03203 | BACCAP_02301 | 5'-3' exonuclease, N-terminal resolvase-like domain protein; KEGG: msm:MSMEG_3839 1.6e-11 DNA polymerase I K00961; COG: COG0749 DNA polymerase I - 3-5 exonuclease and polymerase domains. | leucine--tRNA ligase; KEGG: gka:GK2842 1.5e-238 leuS; leucyl-tRNA synthetase K01869; COG: COG0495 Leucyl-tRNA synthetase; Psort location: Cytoplasmic, score:9.26; Belongs to the class-I aminoacyl-tRNA synthetase family. | 0.418 |
EDM99274.1 | metG | BACCAP_03203 | BACCAP_03269 | 5'-3' exonuclease, N-terminal resolvase-like domain protein; KEGG: msm:MSMEG_3839 1.6e-11 DNA polymerase I K00961; COG: COG0749 DNA polymerase I - 3-5 exonuclease and polymerase domains. | methionine--tRNA ligase; Is required not only for elongation of protein synthesis but also for the initiation of all mRNA translation through initiator tRNA(fMet) aminoacylation. | 0.755 |
EDM99274.1 | polA | BACCAP_03203 | BACCAP_02250 | 5'-3' exonuclease, N-terminal resolvase-like domain protein; KEGG: msm:MSMEG_3839 1.6e-11 DNA polymerase I K00961; COG: COG0749 DNA polymerase I - 3-5 exonuclease and polymerase domains. | DNA-directed DNA polymerase; In addition to polymerase activity, this DNA polymerase exhibits 5'-3' exonuclease activity. | 0.980 |
argS | EDM99274.1 | BACCAP_04827 | BACCAP_03203 | arginine--tRNA ligase; KEGG: tte:TTE2533 3.5e-145 argS; arginyl-tRNA synthetase K01887; COG: COG0018 Arginyl-tRNA synthetase; Psort location: Cytoplasmic, score:9.26. | 5'-3' exonuclease, N-terminal resolvase-like domain protein; KEGG: msm:MSMEG_3839 1.6e-11 DNA polymerase I K00961; COG: COG0749 DNA polymerase I - 3-5 exonuclease and polymerase domains. | 0.460 |
argS | aspS-2 | BACCAP_04827 | BACCAP_03630 | arginine--tRNA ligase; KEGG: tte:TTE2533 3.5e-145 argS; arginyl-tRNA synthetase K01887; COG: COG0018 Arginyl-tRNA synthetase; Psort location: Cytoplasmic, score:9.26. | aspartate--tRNA ligase; 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 2 subfamily. | 0.886 |
argS | ileS | BACCAP_04827 | BACCAP_01336 | arginine--tRNA ligase; KEGG: tte:TTE2533 3.5e-145 argS; arginyl-tRNA synthetase K01887; COG: COG0018 Arginyl-tRNA synthetase; Psort location: Cytoplasmic, score:9.26. | Putative isoleucine--tRNA ligase; Catalyzes the attachment of isoleucine to tRNA(Ile). As IleRS can inadvertently accommodate and process structurally similar amino acids such as valine, to avoid such errors it has two additional distinct tRNA(Ile)-dependent editing activities. One activity is designated as 'pretransfer' editing and involves the hydrolysis of activated Val-AMP. The other activity is designated 'posttransfer' editing and involves deacylation of mischarged Val-tRNA(Ile). Belongs to the class-I aminoacyl-tRNA synthetase family. IleS type 1 subfamily. | 0.995 |
argS | leuS | BACCAP_04827 | BACCAP_02301 | arginine--tRNA ligase; KEGG: tte:TTE2533 3.5e-145 argS; arginyl-tRNA synthetase K01887; COG: COG0018 Arginyl-tRNA synthetase; Psort location: Cytoplasmic, score:9.26. | leucine--tRNA ligase; KEGG: gka:GK2842 1.5e-238 leuS; leucyl-tRNA synthetase K01869; COG: COG0495 Leucyl-tRNA synthetase; Psort location: Cytoplasmic, score:9.26; Belongs to the class-I aminoacyl-tRNA synthetase family. | 0.981 |
argS | metG | BACCAP_04827 | BACCAP_03269 | arginine--tRNA ligase; KEGG: tte:TTE2533 3.5e-145 argS; arginyl-tRNA synthetase K01887; COG: COG0018 Arginyl-tRNA synthetase; Psort location: Cytoplasmic, score:9.26. | methionine--tRNA ligase; Is required not only for elongation of protein synthesis but also for the initiation of all mRNA translation through initiator tRNA(fMet) aminoacylation. | 0.990 |
argS | polA | BACCAP_04827 | BACCAP_02250 | arginine--tRNA ligase; KEGG: tte:TTE2533 3.5e-145 argS; arginyl-tRNA synthetase K01887; COG: COG0018 Arginyl-tRNA synthetase; Psort location: Cytoplasmic, score:9.26. | DNA-directed DNA polymerase; In addition to polymerase activity, this DNA polymerase exhibits 5'-3' exonuclease activity. | 0.460 |
argS | proS | BACCAP_04827 | BACCAP_03073 | arginine--tRNA ligase; KEGG: tte:TTE2533 3.5e-145 argS; arginyl-tRNA synthetase K01887; COG: COG0018 Arginyl-tRNA synthetase; Psort location: Cytoplasmic, score:9.26. | proline--tRNA ligase; Catalyzes the attachment of proline to tRNA(Pro) in a two- step reaction: proline is first activated by ATP to form Pro-AMP and then transferred to the acceptor end of tRNA(Pro). | 0.991 |
aspS-2 | EDM99274.1 | BACCAP_03630 | BACCAP_03203 | aspartate--tRNA ligase; 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 2 subfamily. | 5'-3' exonuclease, N-terminal resolvase-like domain protein; KEGG: msm:MSMEG_3839 1.6e-11 DNA polymerase I K00961; COG: COG0749 DNA polymerase I - 3-5 exonuclease and polymerase domains. | 0.980 |
aspS-2 | argS | BACCAP_03630 | BACCAP_04827 | aspartate--tRNA ligase; 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 2 subfamily. | arginine--tRNA ligase; KEGG: tte:TTE2533 3.5e-145 argS; arginyl-tRNA synthetase K01887; COG: COG0018 Arginyl-tRNA synthetase; Psort location: Cytoplasmic, score:9.26. | 0.886 |
aspS-2 | gatA | BACCAP_03630 | BACCAP_03632 | aspartate--tRNA ligase; 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 2 subfamily. | aspartyl/glutamyl-tRNA(Asn/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). | 0.998 |
aspS-2 | gatB | BACCAP_03630 | BACCAP_03633 | aspartate--tRNA ligase; 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 2 subfamily. | aspartyl/glutamyl-tRNA(Asn/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. | 0.999 |
aspS-2 | gatC | BACCAP_03630 | BACCAP_03631 | aspartate--tRNA ligase; 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 2 subfamily. | aspartyl/glutamyl-tRNA(Asn/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. | 0.992 |
aspS-2 | ileS | BACCAP_03630 | BACCAP_01336 | aspartate--tRNA ligase; 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 2 subfamily. | Putative isoleucine--tRNA ligase; Catalyzes the attachment of isoleucine to tRNA(Ile). As IleRS can inadvertently accommodate and process structurally similar amino acids such as valine, to avoid such errors it has two additional distinct tRNA(Ile)-dependent editing activities. One activity is designated as 'pretransfer' editing and involves the hydrolysis of activated Val-AMP. The other activity is designated 'posttransfer' editing and involves deacylation of mischarged Val-tRNA(Ile). Belongs to the class-I aminoacyl-tRNA synthetase family. IleS type 1 subfamily. | 0.905 |
aspS-2 | leuS | BACCAP_03630 | BACCAP_02301 | aspartate--tRNA ligase; 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 2 subfamily. | leucine--tRNA ligase; KEGG: gka:GK2842 1.5e-238 leuS; leucyl-tRNA synthetase K01869; COG: COG0495 Leucyl-tRNA synthetase; Psort location: Cytoplasmic, score:9.26; Belongs to the class-I aminoacyl-tRNA synthetase family. | 0.895 |
aspS-2 | metG | BACCAP_03630 | BACCAP_03269 | aspartate--tRNA ligase; 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 2 subfamily. | methionine--tRNA ligase; Is required not only for elongation of protein synthesis but also for the initiation of all mRNA translation through initiator tRNA(fMet) aminoacylation. | 0.971 |