| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| AEN04868.1 | aspS | Halar_1111 | Halar_3227 | TIGRFAM: CocE/NonD hydrolase; KEGG: hwa:HQ1933A X-Pro dipeptidyl-peptidase. | 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). | 0.923 |
| AEN04868.1 | gltX | Halar_1111 | Halar_2103 | TIGRFAM: CocE/NonD hydrolase; KEGG: hwa:HQ1933A X-Pro dipeptidyl-peptidase. | 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). | 0.887 |
| AEN04868.1 | guaAB | Halar_1111 | Halar_2248 | TIGRFAM: CocE/NonD hydrolase; KEGG: hwa:HQ1933A X-Pro dipeptidyl-peptidase. | GMP synthase (glutamine-hydrolyzing) subunit B; Catalyzes the synthesis of GMP from XMP. | 0.801 |
| AEN04868.1 | ileS | Halar_1111 | Halar_1449 | TIGRFAM: CocE/NonD hydrolase; KEGG: hwa:HQ1933A X-Pro dipeptidyl-peptidase. | 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 2 subfamily. | 0.959 |
| AEN04868.1 | leuS | Halar_1111 | Halar_3165 | TIGRFAM: CocE/NonD hydrolase; KEGG: hwa:HQ1933A X-Pro dipeptidyl-peptidase. | TIGRFAM: Leucyl-tRNA synthetase, class Ia, archaeal/eukaryotic cytosolic; KEGG: hbo:Hbor_27430 leucyl-tRNA synthetase; Belongs to the class-I aminoacyl-tRNA synthetase family. | 0.926 |
| AEN04868.1 | metG | Halar_1111 | Halar_1001 | TIGRFAM: CocE/NonD hydrolase; KEGG: hwa:HQ1933A X-Pro dipeptidyl-peptidase. | 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. | 0.939 |
| AEN04868.1 | proS | Halar_1111 | Halar_0871 | TIGRFAM: CocE/NonD hydrolase; KEGG: hwa:HQ1933A X-Pro dipeptidyl-peptidase. | 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). | 0.840 |
| AEN04868.1 | pyrG | Halar_1111 | Halar_2249 | TIGRFAM: CocE/NonD hydrolase; KEGG: hwa:HQ1933A X-Pro dipeptidyl-peptidase. | CTP synthase; Catalyzes the ATP-dependent amination of UTP to CTP with either L-glutamine or ammonia as the source of nitrogen. Regulates intracellular CTP levels through interactions with the four ribonucleotide triphosphates. | 0.826 |
| AEN04868.1 | thrS | Halar_1111 | Halar_1622 | TIGRFAM: CocE/NonD hydrolase; KEGG: hwa:HQ1933A X-Pro dipeptidyl-peptidase. | KEGG: hla:Hlac_1764 threonyl-tRNA synthetase; TIGRFAM: Threonyl-tRNA synthetase, class IIa; PFAM: Aminoacyl-tRNA synthetase, class II (G/ H/ P/ S), conserved region; Threonyl/alanyl tRNA synthetase, SAD; TGS; Anticodon-binding; Belongs to the class-II aminoacyl-tRNA synthetase family. | 0.811 |
| AEN04868.1 | tyrS | Halar_1111 | Halar_2877 | TIGRFAM: CocE/NonD hydrolase; KEGG: hwa:HQ1933A X-Pro dipeptidyl-peptidase. | Tyrosyl-tRNA synthetase; Catalyzes the attachment of tyrosine to tRNA(Tyr) in a two- step reaction: tyrosine is first activated by ATP to form Tyr-AMP and then transferred to the acceptor end of tRNA(Tyr); Belongs to the class-I aminoacyl-tRNA synthetase family. TyrS type 3 subfamily. | 0.757 |
| aspS | AEN04868.1 | Halar_3227 | Halar_1111 | 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). | TIGRFAM: CocE/NonD hydrolase; KEGG: hwa:HQ1933A X-Pro dipeptidyl-peptidase. | 0.923 |
| aspS | gltX | Halar_3227 | Halar_2103 | 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). | 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). | 0.956 |
| aspS | ileS | Halar_3227 | Halar_1449 | 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). | 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 2 subfamily. | 0.977 |
| aspS | leuS | Halar_3227 | Halar_3165 | 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). | TIGRFAM: Leucyl-tRNA synthetase, class Ia, archaeal/eukaryotic cytosolic; KEGG: hbo:Hbor_27430 leucyl-tRNA synthetase; Belongs to the class-I aminoacyl-tRNA synthetase family. | 0.981 |
| aspS | metG | Halar_3227 | Halar_1001 | 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). | 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. | 0.993 |
| aspS | proS | Halar_3227 | Halar_0871 | 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). | 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). | 0.984 |
| aspS | thrS | Halar_3227 | Halar_1622 | 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). | KEGG: hla:Hlac_1764 threonyl-tRNA synthetase; TIGRFAM: Threonyl-tRNA synthetase, class IIa; PFAM: Aminoacyl-tRNA synthetase, class II (G/ H/ P/ S), conserved region; Threonyl/alanyl tRNA synthetase, SAD; TGS; Anticodon-binding; Belongs to the class-II aminoacyl-tRNA synthetase family. | 0.932 |
| aspS | tyrS | Halar_3227 | Halar_2877 | 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). | Tyrosyl-tRNA synthetase; Catalyzes the attachment of tyrosine to tRNA(Tyr) in a two- step reaction: tyrosine is first activated by ATP to form Tyr-AMP and then transferred to the acceptor end of tRNA(Tyr); Belongs to the class-I aminoacyl-tRNA synthetase family. TyrS type 3 subfamily. | 0.608 |
| gltX | AEN04868.1 | Halar_2103 | Halar_1111 | 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). | TIGRFAM: CocE/NonD hydrolase; KEGG: hwa:HQ1933A X-Pro dipeptidyl-peptidase. | 0.887 |
| gltX | aspS | Halar_2103 | Halar_3227 | 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). | 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). | 0.956 |