| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| Cphy_1115 | aspS | Cphy_1115 | Cphy_0553 | KEGG: cbf:CLI_0591 seryl-tRNA synthetase; TIGRFAM: seryl-tRNA synthetase; PFAM: tRNA synthetase class II (G H P and S); Seryl-tRNA synthetase, class IIa-like. | 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. | 0.576 |
| Cphy_1115 | guaA | Cphy_1115 | Cphy_0264 | KEGG: cbf:CLI_0591 seryl-tRNA synthetase; TIGRFAM: seryl-tRNA synthetase; PFAM: tRNA synthetase class II (G H P and S); Seryl-tRNA synthetase, class IIa-like. | GMP synthase, large subunit; Catalyzes the synthesis of GMP from XMP. | 0.622 |
| Cphy_1115 | ileS | Cphy_1115 | Cphy_3832 | KEGG: cbf:CLI_0591 seryl-tRNA synthetase; TIGRFAM: seryl-tRNA synthetase; PFAM: tRNA synthetase class II (G H P and S); Seryl-tRNA synthetase, class IIa-like. | 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. | 0.590 |
| Cphy_1115 | leuS | Cphy_1115 | Cphy_0938 | KEGG: cbf:CLI_0591 seryl-tRNA synthetase; TIGRFAM: seryl-tRNA synthetase; PFAM: tRNA synthetase class II (G H P and S); Seryl-tRNA synthetase, class IIa-like. | TIGRFAM: leucyl-tRNA synthetase; KEGG: gka:GK2842 leucyl-tRNA synthetase; Belongs to the class-I aminoacyl-tRNA synthetase family. | 0.652 |
| Cphy_1115 | metG | Cphy_1115 | Cphy_0025 | KEGG: cbf:CLI_0591 seryl-tRNA synthetase; TIGRFAM: seryl-tRNA synthetase; PFAM: tRNA synthetase class II (G H P and S); Seryl-tRNA synthetase, class IIa-like. | 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. | 0.832 |
| Cphy_1115 | pheT | Cphy_1115 | Cphy_3476 | KEGG: cbf:CLI_0591 seryl-tRNA synthetase; TIGRFAM: seryl-tRNA synthetase; PFAM: tRNA synthetase class II (G H P and S); Seryl-tRNA synthetase, class IIa-like. | KEGG: cth:Cthe_0215 phenylalanyl-tRNA synthetase, beta subunit; TIGRFAM: phenylalanyl-tRNA synthetase, beta subunit. | 0.713 |
| Cphy_1115 | proS | Cphy_1115 | Cphy_3837 | KEGG: cbf:CLI_0591 seryl-tRNA synthetase; TIGRFAM: seryl-tRNA synthetase; PFAM: tRNA synthetase class II (G H P and S); Seryl-tRNA synthetase, class IIa-like. | 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). | 0.597 |
| Cphy_1115 | thrS | Cphy_1115 | Cphy_0748 | KEGG: cbf:CLI_0591 seryl-tRNA synthetase; TIGRFAM: seryl-tRNA synthetase; PFAM: tRNA synthetase class II (G H P and S); Seryl-tRNA synthetase, class IIa-like. | TIGRFAM: threonyl-tRNA synthetase; PFAM: tRNA synthetase class II (G H P and S); TGS domain protein; Anticodon-binding domain protein; Threonyl/alanyl tRNA synthetase SAD; KEGG: cbe:Cbei_0293 threonyl-tRNA synthetase; Belongs to the class-II aminoacyl-tRNA synthetase family. | 0.543 |
| Cphy_1115 | thrS-2 | Cphy_1115 | Cphy_2665 | KEGG: cbf:CLI_0591 seryl-tRNA synthetase; TIGRFAM: seryl-tRNA synthetase; PFAM: tRNA synthetase class II (G H P and S); Seryl-tRNA synthetase, class IIa-like. | TIGRFAM: threonyl-tRNA synthetase; PFAM: tRNA synthetase class II (G H P and S); Anticodon-binding domain protein; Threonyl/alanyl tRNA synthetase SAD; KEGG: ctc:CTC02286 threonyl-tRNA synthetase; Belongs to the class-II aminoacyl-tRNA synthetase family. | 0.571 |
| Cphy_1115 | valS | Cphy_1115 | Cphy_0472 | KEGG: cbf:CLI_0591 seryl-tRNA synthetase; TIGRFAM: seryl-tRNA synthetase; PFAM: tRNA synthetase class II (G H P and S); Seryl-tRNA synthetase, class IIa-like. | 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. | 0.808 |
| aspS | Cphy_1115 | Cphy_0553 | Cphy_1115 | 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. | KEGG: cbf:CLI_0591 seryl-tRNA synthetase; TIGRFAM: seryl-tRNA synthetase; PFAM: tRNA synthetase class II (G H P and S); Seryl-tRNA synthetase, class IIa-like. | 0.576 |
| aspS | guaA | Cphy_0553 | Cphy_0264 | 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. | GMP synthase, large subunit; Catalyzes the synthesis of GMP from XMP. | 0.900 |
| aspS | ileS | Cphy_0553 | Cphy_3832 | 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. | 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. | 0.693 |
| aspS | leuS | Cphy_0553 | Cphy_0938 | 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. | TIGRFAM: leucyl-tRNA synthetase; KEGG: gka:GK2842 leucyl-tRNA synthetase; Belongs to the class-I aminoacyl-tRNA synthetase family. | 0.636 |
| aspS | metG | Cphy_0553 | Cphy_0025 | 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. | 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. | 0.738 |
| aspS | pheT | Cphy_0553 | Cphy_3476 | 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. | KEGG: cth:Cthe_0215 phenylalanyl-tRNA synthetase, beta subunit; TIGRFAM: phenylalanyl-tRNA synthetase, beta subunit. | 0.849 |
| aspS | proS | Cphy_0553 | Cphy_3837 | 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. | 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). | 0.737 |
| aspS | thrS | Cphy_0553 | Cphy_0748 | 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. | TIGRFAM: threonyl-tRNA synthetase; PFAM: tRNA synthetase class II (G H P and S); TGS domain protein; Anticodon-binding domain protein; Threonyl/alanyl tRNA synthetase SAD; KEGG: cbe:Cbei_0293 threonyl-tRNA synthetase; Belongs to the class-II aminoacyl-tRNA synthetase family. | 0.517 |
| aspS | thrS-2 | Cphy_0553 | Cphy_2665 | 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. | TIGRFAM: threonyl-tRNA synthetase; PFAM: tRNA synthetase class II (G H P and S); Anticodon-binding domain protein; Threonyl/alanyl tRNA synthetase SAD; KEGG: ctc:CTC02286 threonyl-tRNA synthetase; Belongs to the class-II aminoacyl-tRNA synthetase family. | 0.574 |
| aspS | valS | Cphy_0553 | Cphy_0472 | 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. | 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. | 0.876 |