| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| OPJ56775.1 | aspS | CLOTH_00570 | CLOTH_00600 | Putative metallo-hydrolase. | aspartate--tRNA ligase; 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. | 0.858 |
| OPJ56775.1 | dtd | CLOTH_00570 | CLOTH_00560 | Putative metallo-hydrolase. | D-tyrosyl-tRNA(Tyr) deacylase; An aminoacyl-tRNA editing enzyme that deacylates mischarged D-aminoacyl-tRNAs. Also deacylates mischarged glycyl-tRNA(Ala), protecting cells against glycine mischarging by AlaRS. Acts via tRNA- based rather than protein-based catalysis; rejects L-amino acids rather than detecting D-amino acids in the active site. By recycling D- aminoacyl-tRNA to D-amino acids and free tRNA molecules, this enzyme counteracts the toxicity associated with the formation of D-aminoacyl- tRNA entities in vivo and helps enforce protein L-homochirality. Belongs to the DTD family. | 0.845 |
| OPJ56775.1 | hemZ | CLOTH_00570 | CLOTH_00580 | Putative metallo-hydrolase. | Oxygen-independent coproporphyrinogen-III oxidase-like protein HemZ. | 0.856 |
| OPJ56775.1 | hisS | CLOTH_00570 | CLOTH_00590 | Putative metallo-hydrolase. | histidine--tRNA ligase. | 0.872 |
| OPJ56775.1 | relA | CLOTH_00570 | CLOTH_00550 | Putative metallo-hydrolase. | GTP pyrophosphokinase; In eubacteria ppGpp (guanosine 3'-diphosphate 5-' diphosphate) is a mediator of the stringent response that coordinates a variety of cellular activities in response to changes in nutritional abundance. | 0.880 |
| aspS | OPJ56775.1 | CLOTH_00600 | CLOTH_00570 | aspartate--tRNA ligase; 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. | Putative metallo-hydrolase. | 0.858 |
| aspS | cysS | CLOTH_00600 | CLOTH_18820 | aspartate--tRNA ligase; 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. | cysteine--tRNA ligase; Belongs to the class-I aminoacyl-tRNA synthetase family. | 0.461 |
| aspS | dtd | CLOTH_00600 | CLOTH_00560 | aspartate--tRNA ligase; 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. | D-tyrosyl-tRNA(Tyr) deacylase; An aminoacyl-tRNA editing enzyme that deacylates mischarged D-aminoacyl-tRNAs. Also deacylates mischarged glycyl-tRNA(Ala), protecting cells against glycine mischarging by AlaRS. Acts via tRNA- based rather than protein-based catalysis; rejects L-amino acids rather than detecting D-amino acids in the active site. By recycling D- aminoacyl-tRNA to D-amino acids and free tRNA molecules, this enzyme counteracts the toxicity associated with the formation of D-aminoacyl- tRNA entities in vivo and helps enforce protein L-homochirality. Belongs to the DTD family. | 0.822 |
| aspS | guaA | CLOTH_00600 | CLOTH_11700 | aspartate--tRNA ligase; 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; Catalyzes the synthesis of GMP from XMP. | 0.889 |
| aspS | hemZ | CLOTH_00600 | CLOTH_00580 | aspartate--tRNA ligase; 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. | Oxygen-independent coproporphyrinogen-III oxidase-like protein HemZ. | 0.832 |
| aspS | hisS | CLOTH_00600 | CLOTH_00590 | aspartate--tRNA ligase; 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. | histidine--tRNA ligase. | 0.984 |
| aspS | lysS | CLOTH_00600 | CLOTH_19520 | aspartate--tRNA ligase; 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. | lysine--tRNA ligase; Belongs to the class-II aminoacyl-tRNA synthetase family. | 0.754 |
| aspS | relA | CLOTH_00600 | CLOTH_00550 | aspartate--tRNA ligase; 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. | GTP pyrophosphokinase; In eubacteria ppGpp (guanosine 3'-diphosphate 5-' diphosphate) is a mediator of the stringent response that coordinates a variety of cellular activities in response to changes in nutritional abundance. | 0.813 |
| aspS | valS | CLOTH_00600 | CLOTH_07940 | aspartate--tRNA ligase; 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. | valine--tRNA ligase; 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. | 0.835 |
| cysS | aspS | CLOTH_18820 | CLOTH_00600 | cysteine--tRNA ligase; Belongs to the class-I aminoacyl-tRNA synthetase family. | aspartate--tRNA ligase; 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. | 0.461 |
| cysS | guaA | CLOTH_18820 | CLOTH_11700 | cysteine--tRNA ligase; Belongs to the class-I aminoacyl-tRNA synthetase family. | GMP synthase; Catalyzes the synthesis of GMP from XMP. | 0.750 |
| cysS | hisS | CLOTH_18820 | CLOTH_00590 | cysteine--tRNA ligase; Belongs to the class-I aminoacyl-tRNA synthetase family. | histidine--tRNA ligase. | 0.818 |
| cysS | lysS | CLOTH_18820 | CLOTH_19520 | cysteine--tRNA ligase; Belongs to the class-I aminoacyl-tRNA synthetase family. | lysine--tRNA ligase; Belongs to the class-II aminoacyl-tRNA synthetase family. | 0.578 |
| cysS | valS | CLOTH_18820 | CLOTH_07940 | cysteine--tRNA ligase; Belongs to the class-I aminoacyl-tRNA synthetase family. | valine--tRNA ligase; 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. | 0.692 |
| dtd | OPJ56775.1 | CLOTH_00560 | CLOTH_00570 | D-tyrosyl-tRNA(Tyr) deacylase; An aminoacyl-tRNA editing enzyme that deacylates mischarged D-aminoacyl-tRNAs. Also deacylates mischarged glycyl-tRNA(Ala), protecting cells against glycine mischarging by AlaRS. Acts via tRNA- based rather than protein-based catalysis; rejects L-amino acids rather than detecting D-amino acids in the active site. By recycling D- aminoacyl-tRNA to D-amino acids and free tRNA molecules, this enzyme counteracts the toxicity associated with the formation of D-aminoacyl- tRNA entities in vivo and helps enforce protein L-homochirality. Belongs to the DTD family. | Putative metallo-hydrolase. | 0.845 |