| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| Rv1364c | dtd | Rv1364c | Rv1897c | Rv1364c, (MTCY02B10.28c), len: 653 aa. Possible sigma factor regulatory protein, some similarity to RSBU_BACSU|P40399 sigma factor sibg regulation protein from Bacillus subtilis (335 aa), FASTA scores: opt: 224, E(): 2e-07, (25.8% identity in 244 aa overlap). Also known as mursiF. | Conserved hypothetical protein; 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. | 0.509 |
| Rv1364c | relA | Rv1364c | Rv2583c | Rv1364c, (MTCY02B10.28c), len: 653 aa. Possible sigma factor regulatory protein, some similarity to RSBU_BACSU|P40399 sigma factor sibg regulation protein from Bacillus subtilis (335 aa), FASTA scores: opt: 224, E(): 2e-07, (25.8% identity in 244 aa overlap). Also known as mursiF. | Guanosine-3',5'-bis(diphosphate) 3'-pyrophosphohydrolase; 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. This enzyme catalyzes both the formation of pppGpp, which is then hydrolyzed to form ppGpp, as well as the hydrolysis of ppGpp. RelA is probably a key factor in the pathogenesis of M.tuberculosis as it regulates the intracellular concentrations of (p)ppGpp. | 0.613 |
| Rv1896c | Rv1898 | Rv1896c | Rv1898 | Conserved hypothetical protein; Exhibits S-adenosyl-L-methionine-dependent methyltransferase activity. | Rv1898, (MTCY180.20c), len: 102 aa. Conserved hypothetical protein, some similarity to other hypothetical proteins e.g. Q58452 from methanococcus jannasch II (100 aa), FASTA results: opt: 152, E(): 9.1e-05, (31.5% identity in 92 aa overlap); and AE000771|AE000771_2 from Aquifex aeolicus (157 aa), FASTA results: opt: 246, E(): 3.2e-11,(39.0% identity in 100 aa overlap); Belongs to the UPF0045 family. | 0.599 |
| Rv1896c | dtd | Rv1896c | Rv1897c | Conserved hypothetical protein; Exhibits S-adenosyl-L-methionine-dependent methyltransferase activity. | Conserved hypothetical protein; 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. | 0.863 |
| Rv1898 | Rv1896c | Rv1898 | Rv1896c | Rv1898, (MTCY180.20c), len: 102 aa. Conserved hypothetical protein, some similarity to other hypothetical proteins e.g. Q58452 from methanococcus jannasch II (100 aa), FASTA results: opt: 152, E(): 9.1e-05, (31.5% identity in 92 aa overlap); and AE000771|AE000771_2 from Aquifex aeolicus (157 aa), FASTA results: opt: 246, E(): 3.2e-11,(39.0% identity in 100 aa overlap); Belongs to the UPF0045 family. | Conserved hypothetical protein; Exhibits S-adenosyl-L-methionine-dependent methyltransferase activity. | 0.599 |
| Rv1898 | dtd | Rv1898 | Rv1897c | Rv1898, (MTCY180.20c), len: 102 aa. Conserved hypothetical protein, some similarity to other hypothetical proteins e.g. Q58452 from methanococcus jannasch II (100 aa), FASTA results: opt: 152, E(): 9.1e-05, (31.5% identity in 92 aa overlap); and AE000771|AE000771_2 from Aquifex aeolicus (157 aa), FASTA results: opt: 246, E(): 3.2e-11,(39.0% identity in 100 aa overlap); Belongs to the UPF0045 family. | Conserved hypothetical protein; 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. | 0.762 |
| Rv3013 | dtd | Rv3013 | Rv1897c | Conserved protein; Rv3013, (MTV012.27), len: 218 aa. Conserved protein,equivalent to O33103|MLCB637_11c hypothetical 24.4 KDA protein from Mycobacterium leprae (230 aa), FASTA scores: opt: 1188, E(): 2.6e-67, (83.95% identity in 218 aa overlap). Equivalent to AAK47422 from Mycobacterium tuberculosis strain CDC1551 (240 aa) but shorter 22 aa. A core mycobacterial gene; conserved in mycobacterial strains (See Marmiesse et al., 2004). | Conserved hypothetical protein; 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. | 0.405 |
| dtd | Rv1364c | Rv1897c | Rv1364c | Conserved hypothetical protein; 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. | Rv1364c, (MTCY02B10.28c), len: 653 aa. Possible sigma factor regulatory protein, some similarity to RSBU_BACSU|P40399 sigma factor sibg regulation protein from Bacillus subtilis (335 aa), FASTA scores: opt: 224, E(): 2e-07, (25.8% identity in 244 aa overlap). Also known as mursiF. | 0.509 |
| dtd | Rv1896c | Rv1897c | Rv1896c | Conserved hypothetical protein; 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. | Conserved hypothetical protein; Exhibits S-adenosyl-L-methionine-dependent methyltransferase activity. | 0.863 |
| dtd | Rv1898 | Rv1897c | Rv1898 | Conserved hypothetical protein; 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. | Rv1898, (MTCY180.20c), len: 102 aa. Conserved hypothetical protein, some similarity to other hypothetical proteins e.g. Q58452 from methanococcus jannasch II (100 aa), FASTA results: opt: 152, E(): 9.1e-05, (31.5% identity in 92 aa overlap); and AE000771|AE000771_2 from Aquifex aeolicus (157 aa), FASTA results: opt: 246, E(): 3.2e-11,(39.0% identity in 100 aa overlap); Belongs to the UPF0045 family. | 0.762 |
| dtd | Rv3013 | Rv1897c | Rv3013 | Conserved hypothetical protein; 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. | Conserved protein; Rv3013, (MTV012.27), len: 218 aa. Conserved protein,equivalent to O33103|MLCB637_11c hypothetical 24.4 KDA protein from Mycobacterium leprae (230 aa), FASTA scores: opt: 1188, E(): 2.6e-67, (83.95% identity in 218 aa overlap). Equivalent to AAK47422 from Mycobacterium tuberculosis strain CDC1551 (240 aa) but shorter 22 aa. A core mycobacterial gene; conserved in mycobacterial strains (See Marmiesse et al., 2004). | 0.405 |
| dtd | relA | Rv1897c | Rv2583c | Conserved hypothetical protein; 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. | Guanosine-3',5'-bis(diphosphate) 3'-pyrophosphohydrolase; 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. This enzyme catalyzes both the formation of pppGpp, which is then hydrolyzed to form ppGpp, as well as the hydrolysis of ppGpp. RelA is probably a key factor in the pathogenesis of M.tuberculosis as it regulates the intracellular concentrations of (p)ppGpp. | 0.432 |
| relA | Rv1364c | Rv2583c | Rv1364c | Guanosine-3',5'-bis(diphosphate) 3'-pyrophosphohydrolase; 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. This enzyme catalyzes both the formation of pppGpp, which is then hydrolyzed to form ppGpp, as well as the hydrolysis of ppGpp. RelA is probably a key factor in the pathogenesis of M.tuberculosis as it regulates the intracellular concentrations of (p)ppGpp. | Rv1364c, (MTCY02B10.28c), len: 653 aa. Possible sigma factor regulatory protein, some similarity to RSBU_BACSU|P40399 sigma factor sibg regulation protein from Bacillus subtilis (335 aa), FASTA scores: opt: 224, E(): 2e-07, (25.8% identity in 244 aa overlap). Also known as mursiF. | 0.613 |
| relA | dtd | Rv2583c | Rv1897c | Guanosine-3',5'-bis(diphosphate) 3'-pyrophosphohydrolase; 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. This enzyme catalyzes both the formation of pppGpp, which is then hydrolyzed to form ppGpp, as well as the hydrolysis of ppGpp. RelA is probably a key factor in the pathogenesis of M.tuberculosis as it regulates the intracellular concentrations of (p)ppGpp. | Conserved hypothetical protein; 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. | 0.432 |
