node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
argS | asnS | Hore_08210 | Hore_08140 | PFAM: tRNA synthetases class I (R); DALR anticodon binding domain; Arginyl tRNA synthetase N terminal domain; TIGRFAM: arginyl-tRNA synthetase. | asparaginyl-tRNA synthetase; PFAM: OB-fold nucleic acid binding domain; tRNA synthetases class II (D, K and N); TIGRFAM: asparaginyl-tRNA synthetase. | 0.895 |
argS | gatB | Hore_08210 | Hore_02340 | PFAM: tRNA synthetases class I (R); DALR anticodon binding domain; Arginyl tRNA synthetase N terminal domain; TIGRFAM: arginyl-tRNA synthetase. | 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. | 0.401 |
argS | gltX-2 | Hore_08210 | Hore_18780 | PFAM: tRNA synthetases class I (R); DALR anticodon binding domain; Arginyl tRNA synthetase N terminal domain; TIGRFAM: arginyl-tRNA synthetase. | 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. | 0.901 |
argS | ileS | Hore_08210 | Hore_09270 | PFAM: tRNA synthetases class I (R); DALR anticodon binding domain; Arginyl tRNA synthetase N terminal domain; TIGRFAM: arginyl-tRNA synthetase. | isoleucyl-tRNA synthetase; 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. | 0.962 |
argS | leuS | Hore_08210 | Hore_13370 | PFAM: tRNA synthetases class I (R); DALR anticodon binding domain; Arginyl tRNA synthetase N terminal domain; TIGRFAM: arginyl-tRNA synthetase. | PFAM: tRNA synthetases class I (I, L, M and V); Anticodon-binding domain; tRNA synthetases class I (M); TIGRFAM: leucyl-tRNA synthetase, eubacterial and mitochondrial family; Belongs to the class-I aminoacyl-tRNA synthetase family. | 0.935 |
argS | metG-2 | Hore_08210 | Hore_20300 | PFAM: tRNA synthetases class I (R); DALR anticodon binding domain; Arginyl tRNA synthetase N terminal domain; TIGRFAM: arginyl-tRNA synthetase. | 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. | 0.947 |
argS | polA | Hore_08210 | Hore_04860 | PFAM: tRNA synthetases class I (R); DALR anticodon binding domain; Arginyl tRNA synthetase N terminal domain; TIGRFAM: arginyl-tRNA synthetase. | DNA polymerase I; In addition to polymerase activity, this DNA polymerase exhibits 5'-3' exonuclease activity. | 0.628 |
argS | proS | Hore_08210 | Hore_07770 | PFAM: tRNA synthetases class I (R); DALR anticodon binding domain; Arginyl tRNA synthetase N terminal domain; TIGRFAM: arginyl-tRNA synthetase. | prolyl-tRNA synthetase; 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). As ProRS can inadvertently accommodate and process non-cognate amino acids such as alanine and cysteine, to avoid such errors it has two additional distinct editing activities against alanine. One activity is designated as 'pretransfer' editing and involves the tRNA(Pro)-independent hydrolysis of activated Ala-AMP. The other activity is designated 'posttransfer' editing and involves dea [...] | 0.956 |
asnS | argS | Hore_08140 | Hore_08210 | asparaginyl-tRNA synthetase; PFAM: OB-fold nucleic acid binding domain; tRNA synthetases class II (D, K and N); TIGRFAM: asparaginyl-tRNA synthetase. | PFAM: tRNA synthetases class I (R); DALR anticodon binding domain; Arginyl tRNA synthetase N terminal domain; TIGRFAM: arginyl-tRNA synthetase. | 0.895 |
asnS | gatA | Hore_08140 | Hore_02330 | asparaginyl-tRNA synthetase; PFAM: OB-fold nucleic acid binding domain; tRNA synthetases class II (D, K and N); TIGRFAM: asparaginyl-tRNA synthetase. | 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). | 0.987 |
asnS | gatB | Hore_08140 | Hore_02340 | asparaginyl-tRNA synthetase; PFAM: OB-fold nucleic acid binding domain; tRNA synthetases class II (D, K and N); TIGRFAM: asparaginyl-tRNA synthetase. | 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. | 0.998 |
asnS | gatC | Hore_08140 | Hore_02320 | asparaginyl-tRNA synthetase; PFAM: OB-fold nucleic acid binding domain; tRNA synthetases class II (D, K and N); TIGRFAM: asparaginyl-tRNA synthetase. | 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. | 0.971 |
asnS | gltX-2 | Hore_08140 | Hore_18780 | asparaginyl-tRNA synthetase; PFAM: OB-fold nucleic acid binding domain; tRNA synthetases class II (D, K and N); TIGRFAM: asparaginyl-tRNA synthetase. | 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. | 0.840 |
asnS | ileS | Hore_08140 | Hore_09270 | asparaginyl-tRNA synthetase; PFAM: OB-fold nucleic acid binding domain; tRNA synthetases class II (D, K and N); TIGRFAM: asparaginyl-tRNA synthetase. | isoleucyl-tRNA synthetase; 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. | 0.911 |
asnS | leuS | Hore_08140 | Hore_13370 | asparaginyl-tRNA synthetase; PFAM: OB-fold nucleic acid binding domain; tRNA synthetases class II (D, K and N); TIGRFAM: asparaginyl-tRNA synthetase. | PFAM: tRNA synthetases class I (I, L, M and V); Anticodon-binding domain; tRNA synthetases class I (M); TIGRFAM: leucyl-tRNA synthetase, eubacterial and mitochondrial family; Belongs to the class-I aminoacyl-tRNA synthetase family. | 0.893 |
asnS | metG-2 | Hore_08140 | Hore_20300 | asparaginyl-tRNA synthetase; PFAM: OB-fold nucleic acid binding domain; tRNA synthetases class II (D, K and N); TIGRFAM: asparaginyl-tRNA synthetase. | 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. | 0.936 |
asnS | polA | Hore_08140 | Hore_04860 | asparaginyl-tRNA synthetase; PFAM: OB-fold nucleic acid binding domain; tRNA synthetases class II (D, K and N); TIGRFAM: asparaginyl-tRNA synthetase. | DNA polymerase I; In addition to polymerase activity, this DNA polymerase exhibits 5'-3' exonuclease activity. | 0.938 |
asnS | proS | Hore_08140 | Hore_07770 | asparaginyl-tRNA synthetase; PFAM: OB-fold nucleic acid binding domain; tRNA synthetases class II (D, K and N); TIGRFAM: asparaginyl-tRNA synthetase. | prolyl-tRNA synthetase; 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). As ProRS can inadvertently accommodate and process non-cognate amino acids such as alanine and cysteine, to avoid such errors it has two additional distinct editing activities against alanine. One activity is designated as 'pretransfer' editing and involves the tRNA(Pro)-independent hydrolysis of activated Ala-AMP. The other activity is designated 'posttransfer' editing and involves dea [...] | 0.925 |
gatA | asnS | Hore_02330 | Hore_08140 | 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). | asparaginyl-tRNA synthetase; PFAM: OB-fold nucleic acid binding domain; tRNA synthetases class II (D, K and N); TIGRFAM: asparaginyl-tRNA synthetase. | 0.987 |
gatA | gatB | Hore_02330 | Hore_02340 | 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). | 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. | 0.999 |