node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
Sfum_0983 | Sfum_2111 | Sfum_0983 | Sfum_2111 | Metal dependent phosphohydrolase; KEGG: dps:DP1905 GTP pyrophosphokinase; PFAM: TGS domain protein; metal-dependent phosphohydrolase, HD sub domain; RelA/SpoT domain protein; SMART: metal-dependent phosphohydrolase, HD region. | (p)ppGpp synthetase I, SpoT/RelA; 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. | 0.926 |
Sfum_0983 | Sfum_3561 | Sfum_0983 | Sfum_3561 | Metal dependent phosphohydrolase; KEGG: dps:DP1905 GTP pyrophosphokinase; PFAM: TGS domain protein; metal-dependent phosphohydrolase, HD sub domain; RelA/SpoT domain protein; SMART: metal-dependent phosphohydrolase, HD region. | PFAM: metal-dependent phosphohydrolase, HD sub domain; SMART: metal-dependent phosphohydrolase, HD region; KEGG: bcn:Bcen_5857 metal dependent phosphohydrolase. | 0.920 |
Sfum_0983 | dtd | Sfum_0983 | Sfum_2470 | Metal dependent phosphohydrolase; KEGG: dps:DP1905 GTP pyrophosphokinase; PFAM: TGS domain protein; metal-dependent phosphohydrolase, HD sub domain; RelA/SpoT domain protein; SMART: metal-dependent phosphohydrolase, HD region. | 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. | 0.465 |
Sfum_2111 | Sfum_0983 | Sfum_2111 | Sfum_0983 | (p)ppGpp synthetase I, SpoT/RelA; 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. | Metal dependent phosphohydrolase; KEGG: dps:DP1905 GTP pyrophosphokinase; PFAM: TGS domain protein; metal-dependent phosphohydrolase, HD sub domain; RelA/SpoT domain protein; SMART: metal-dependent phosphohydrolase, HD region. | 0.926 |
Sfum_2111 | Sfum_3561 | Sfum_2111 | Sfum_3561 | (p)ppGpp synthetase I, SpoT/RelA; 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. | PFAM: metal-dependent phosphohydrolase, HD sub domain; SMART: metal-dependent phosphohydrolase, HD region; KEGG: bcn:Bcen_5857 metal dependent phosphohydrolase. | 0.948 |
Sfum_2111 | dtd | Sfum_2111 | Sfum_2470 | (p)ppGpp synthetase I, SpoT/RelA; 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. | 0.465 |
Sfum_2469 | Sfum_2471 | Sfum_2469 | Sfum_2471 | KEGG: sat:SYN_00898 hypothetical cytosolic protein. | PFAM: Radical SAM domain protein; SMART: Elongator protein 3/MiaB/NifB; KEGG: sat:SYN_02176 Fe-S oxidoreductase. | 0.410 |
Sfum_2469 | dtd | Sfum_2469 | Sfum_2470 | KEGG: sat:SYN_00898 hypothetical cytosolic protein. | 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. | 0.639 |
Sfum_2471 | Sfum_2469 | Sfum_2471 | Sfum_2469 | PFAM: Radical SAM domain protein; SMART: Elongator protein 3/MiaB/NifB; KEGG: sat:SYN_02176 Fe-S oxidoreductase. | KEGG: sat:SYN_00898 hypothetical cytosolic protein. | 0.410 |
Sfum_2471 | dtd | Sfum_2471 | Sfum_2470 | PFAM: Radical SAM domain protein; SMART: Elongator protein 3/MiaB/NifB; KEGG: sat:SYN_02176 Fe-S oxidoreductase. | 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. | 0.516 |
Sfum_3561 | Sfum_0983 | Sfum_3561 | Sfum_0983 | PFAM: metal-dependent phosphohydrolase, HD sub domain; SMART: metal-dependent phosphohydrolase, HD region; KEGG: bcn:Bcen_5857 metal dependent phosphohydrolase. | Metal dependent phosphohydrolase; KEGG: dps:DP1905 GTP pyrophosphokinase; PFAM: TGS domain protein; metal-dependent phosphohydrolase, HD sub domain; RelA/SpoT domain protein; SMART: metal-dependent phosphohydrolase, HD region. | 0.920 |
Sfum_3561 | Sfum_2111 | Sfum_3561 | Sfum_2111 | PFAM: metal-dependent phosphohydrolase, HD sub domain; SMART: metal-dependent phosphohydrolase, HD region; KEGG: bcn:Bcen_5857 metal dependent phosphohydrolase. | (p)ppGpp synthetase I, SpoT/RelA; 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. | 0.948 |
Sfum_3561 | dtd | Sfum_3561 | Sfum_2470 | PFAM: metal-dependent phosphohydrolase, HD sub domain; SMART: metal-dependent phosphohydrolase, HD region; KEGG: bcn:Bcen_5857 metal dependent phosphohydrolase. | 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. | 0.465 |
dtd | Sfum_0983 | Sfum_2470 | Sfum_0983 | 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. | Metal dependent phosphohydrolase; KEGG: dps:DP1905 GTP pyrophosphokinase; PFAM: TGS domain protein; metal-dependent phosphohydrolase, HD sub domain; RelA/SpoT domain protein; SMART: metal-dependent phosphohydrolase, HD region. | 0.465 |
dtd | Sfum_2111 | Sfum_2470 | Sfum_2111 | 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 I, SpoT/RelA; 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. | 0.465 |
dtd | Sfum_2469 | Sfum_2470 | Sfum_2469 | 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. | KEGG: sat:SYN_00898 hypothetical cytosolic protein. | 0.639 |
dtd | Sfum_2471 | Sfum_2470 | Sfum_2471 | 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. | PFAM: Radical SAM domain protein; SMART: Elongator protein 3/MiaB/NifB; KEGG: sat:SYN_02176 Fe-S oxidoreductase. | 0.516 |
dtd | Sfum_3561 | Sfum_2470 | Sfum_3561 | 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. | PFAM: metal-dependent phosphohydrolase, HD sub domain; SMART: metal-dependent phosphohydrolase, HD region; KEGG: bcn:Bcen_5857 metal dependent phosphohydrolase. | 0.465 |