node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
AMA42559.1 | dtd | AWJ11_09425 | AWJ11_14435 | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | 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. | 0.513 |
AMA43435.1 | AMA43437.1 | AWJ11_14430 | AWJ11_14440 | Proline iminopeptidase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the peptidase S33 family. | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.714 |
AMA43435.1 | dtd | AWJ11_14430 | AWJ11_14435 | Proline iminopeptidase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the peptidase S33 family. | 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. | 0.817 |
AMA43435.1 | glsA | AWJ11_14430 | AWJ11_14425 | Proline iminopeptidase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the peptidase S33 family. | Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the glutaminase family. | 0.532 |
AMA43437.1 | AMA43435.1 | AWJ11_14440 | AWJ11_14430 | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | Proline iminopeptidase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the peptidase S33 family. | 0.714 |
AMA43437.1 | dtd | AWJ11_14440 | AWJ11_14435 | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | 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. | 0.714 |
AMA43437.1 | glsA | AWJ11_14440 | AWJ11_14425 | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the glutaminase family. | 0.495 |
dtd | AMA42559.1 | AWJ11_14435 | AWJ11_09425 | 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. | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.513 |
dtd | AMA43435.1 | AWJ11_14435 | AWJ11_14430 | 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. | Proline iminopeptidase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the peptidase S33 family. | 0.817 |
dtd | AMA43437.1 | AWJ11_14435 | AWJ11_14440 | 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. | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.714 |
dtd | glsA | AWJ11_14435 | AWJ11_14425 | 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. | Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the glutaminase family. | 0.532 |
dtd | relA | AWJ11_14435 | AWJ11_04965 | 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. | (p)ppGpp synthetase; 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. | 0.460 |
dtd | spoT | AWJ11_14435 | AWJ11_10980 | 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. | (p)ppGpp synthetase; 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. | 0.460 |
glsA | AMA43435.1 | AWJ11_14425 | AWJ11_14430 | Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the glutaminase family. | Proline iminopeptidase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the peptidase S33 family. | 0.532 |
glsA | AMA43437.1 | AWJ11_14425 | AWJ11_14440 | Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the glutaminase family. | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.495 |
glsA | dtd | AWJ11_14425 | AWJ11_14435 | Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the glutaminase family. | 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. | 0.532 |
relA | dtd | AWJ11_04965 | AWJ11_14435 | (p)ppGpp synthetase; 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. | 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. | 0.460 |
relA | spoT | AWJ11_04965 | AWJ11_10980 | (p)ppGpp synthetase; 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. | (p)ppGpp synthetase; 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. | 0.919 |
spoT | dtd | AWJ11_10980 | AWJ11_14435 | (p)ppGpp synthetase; 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. | 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. | 0.460 |
spoT | relA | AWJ11_10980 | AWJ11_04965 | (p)ppGpp synthetase; 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. | (p)ppGpp synthetase; 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. | 0.919 |