nucleoside triphosphate pyrophosphohydrolase [Bacillus toyonensis]
Protein Classification
nucleoside triphosphate pyrophosphohydrolase( domain architecture ID 11467694)
nucleoside triphosphate pyrophosphohydrolase hydrolyzes ribonucleoside triphosphates (NTPs) and deoxyribonucleoside triphosphates (dNTPs) into their corresponding nucleoside monophosphates and pyrophosphate
List of domain hits
| Name | Accession | Description | Interval | E-value | |||||
| YabN | COG3956 | Uncharacterized conserved protein YabN, contains tetrapyrrole methylase and MazG-like ... |
225-486 | 1.03e-153 | |||||
Uncharacterized conserved protein YabN, contains tetrapyrrole methylase and MazG-like pyrophosphatase domain [General function prediction only]; : Pssm-ID: 443156 [Multi-domain] Cd Length: 268 Bit Score: 438.01 E-value: 1.03e-153
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| YabN_N_like | cd11723 | N-terminal S-AdoMet-dependent tetrapyrrole methylase domain of Bacillus subtilis YabN and ... |
5-223 | 2.15e-117 | |||||
N-terminal S-AdoMet-dependent tetrapyrrole methylase domain of Bacillus subtilis YabN and similar domains; This family includes the S-AdoMet (S-adenosyl-L-methionine or SAM)-dependent tetrapyrrole methylase (TP-methylase) domain of Bacillus subtilis YabN, and similar domains. YabN is a fusion of an N-terminal TP-methylase and a C-terminal MazG-type nucleotide pyrophosphohydrolase domain. MazG-like NTP-PPases have been implicated in house-cleaning functions such as degrading abnormal (d)NTPs. TP-methylases use S-AdoMet in the methylation of diverse substrates. Most TP-methylase family members catalyze various methylation steps in cobalamin (vitamin B12) biosynthesis, other members like diphthine synthase and ribosomal RNA small subunit methyltransferase I (RsmI) act on other substrates. The specific function of YabN's TP-methylase domain is not known. : Pssm-ID: 381177 Cd Length: 218 Bit Score: 343.70 E-value: 2.15e-117
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| Name | Accession | Description | Interval | E-value | |||||
| YabN | COG3956 | Uncharacterized conserved protein YabN, contains tetrapyrrole methylase and MazG-like ... |
225-486 | 1.03e-153 | |||||
Uncharacterized conserved protein YabN, contains tetrapyrrole methylase and MazG-like pyrophosphatase domain [General function prediction only]; Pssm-ID: 443156 [Multi-domain] Cd Length: 268 Bit Score: 438.01 E-value: 1.03e-153
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| mazG | PRK09562 | nucleoside triphosphate pyrophosphohydrolase; Reviewed |
232-486 | 9.68e-136 | |||||
nucleoside triphosphate pyrophosphohydrolase; Reviewed Pssm-ID: 236569 [Multi-domain] Cd Length: 262 Bit Score: 391.83 E-value: 9.68e-136
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| YabN_N_like | cd11723 | N-terminal S-AdoMet-dependent tetrapyrrole methylase domain of Bacillus subtilis YabN and ... |
5-223 | 2.15e-117 | |||||
N-terminal S-AdoMet-dependent tetrapyrrole methylase domain of Bacillus subtilis YabN and similar domains; This family includes the S-AdoMet (S-adenosyl-L-methionine or SAM)-dependent tetrapyrrole methylase (TP-methylase) domain of Bacillus subtilis YabN, and similar domains. YabN is a fusion of an N-terminal TP-methylase and a C-terminal MazG-type nucleotide pyrophosphohydrolase domain. MazG-like NTP-PPases have been implicated in house-cleaning functions such as degrading abnormal (d)NTPs. TP-methylases use S-AdoMet in the methylation of diverse substrates. Most TP-methylase family members catalyze various methylation steps in cobalamin (vitamin B12) biosynthesis, other members like diphthine synthase and ribosomal RNA small subunit methyltransferase I (RsmI) act on other substrates. The specific function of YabN's TP-methylase domain is not known. Pssm-ID: 381177 Cd Length: 218 Bit Score: 343.70 E-value: 2.15e-117
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| mazG | TIGR00444 | MazG family protein; This family of prokaryotic proteins has no known function. It includes ... |
239-482 | 2.37e-107 | |||||
MazG family protein; This family of prokaryotic proteins has no known function. It includes the uncharacterized protein MazG in E. coli. [Unknown function, General] Pssm-ID: 273082 [Multi-domain] Cd Length: 248 Bit Score: 319.08 E-value: 2.37e-107
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| NTP-PPase_MazG_Nterm | cd11528 | Nucleoside Triphosphate Pyrophosphohydrolase (EC 3.6.1.8) N-terminal tandem-domain of MazG ... |
236-347 | 3.66e-66 | |||||
Nucleoside Triphosphate Pyrophosphohydrolase (EC 3.6.1.8) N-terminal tandem-domain of MazG proteins from Escherichia coli and bacterial homologs; MazG is a NTP-PPase that hydrolyzes all canonical NTPs into their corresponding nucleoside monophosphates and pyrophosphate. The prototype of this family is MazG proteins from Escherichia coli (EcMazG) that represents the most abundant form consisting two sequence-related domains in tandem, this family corresponding to the N-terminal MazG-like domain. EcMazG functions as a regulator of cellular response to starvation by lowering the cellular concentration of guanosine 3',5'-bispyrophosphate (ppGpp). EcMazG exists as a dimer; each monomer contains two tandem MazG-like domains with similarly folded globular structures. However, only the C-terminal domain has well-ordered active site and exhibits an NTPase activity responsible for the regulation of bacterial cell survival under nutritional stress. Divalent ions, such as Mg2+ or Mn2+, are required for activity; however, this domain does not exhibit an NTPase activity despite containing structural features such as the EEXX(E/D) motif and key basic catalytic residues responsible for nucleotide pyrophosphohydrolysis activity. It is suggested that the N-terminal domain of EcMazG might have a house-cleaning function by hydrolyzing noncanonical NTPs whose incorporation into the nascent DNA leads to increased mutagenesis and DNA damage. Pssm-ID: 212135 Cd Length: 114 Bit Score: 208.52 E-value: 3.66e-66
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| MazG | pfam03819 | MazG nucleotide pyrophosphohydrolase domain; This domain is about 100 amino acid residues in ... |
255-328 | 9.70e-32 | |||||
MazG nucleotide pyrophosphohydrolase domain; This domain is about 100 amino acid residues in length. It is found in the MazG protein from E. coli. It contains four conserved negatively charged residues that probably form an active site or metal binding site. This domain is found in isolation in some proteins as well as associated with pfam00590. This domain is clearly related to pfam01503 another pyrophosphohydrolase involved in histidine biosynthesis. This family may be structurally related to the NUDIX domain pfam00293 (Bateman A pers. obs.). Pssm-ID: 427525 Cd Length: 74 Bit Score: 116.16 E-value: 9.70e-32
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| TP_methylase | pfam00590 | Tetrapyrrole (Corrin/Porphyrin) Methylases; This family uses S-AdoMet in the methylation of ... |
5-207 | 1.87e-17 | |||||
Tetrapyrrole (Corrin/Porphyrin) Methylases; This family uses S-AdoMet in the methylation of diverse substrates. This family includes a related group of bacterial proteins of unknown function. This family includes the methylase Dipthine synthase. Pssm-ID: 425769 [Multi-domain] Cd Length: 209 Bit Score: 80.85 E-value: 1.87e-17
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| Name | Accession | Description | Interval | E-value | |||||
| YabN | COG3956 | Uncharacterized conserved protein YabN, contains tetrapyrrole methylase and MazG-like ... |
225-486 | 1.03e-153 | |||||
Uncharacterized conserved protein YabN, contains tetrapyrrole methylase and MazG-like pyrophosphatase domain [General function prediction only]; Pssm-ID: 443156 [Multi-domain] Cd Length: 268 Bit Score: 438.01 E-value: 1.03e-153
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| mazG | PRK09562 | nucleoside triphosphate pyrophosphohydrolase; Reviewed |
232-486 | 9.68e-136 | |||||
nucleoside triphosphate pyrophosphohydrolase; Reviewed Pssm-ID: 236569 [Multi-domain] Cd Length: 262 Bit Score: 391.83 E-value: 9.68e-136
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| YabN_N_like | cd11723 | N-terminal S-AdoMet-dependent tetrapyrrole methylase domain of Bacillus subtilis YabN and ... |
5-223 | 2.15e-117 | |||||
N-terminal S-AdoMet-dependent tetrapyrrole methylase domain of Bacillus subtilis YabN and similar domains; This family includes the S-AdoMet (S-adenosyl-L-methionine or SAM)-dependent tetrapyrrole methylase (TP-methylase) domain of Bacillus subtilis YabN, and similar domains. YabN is a fusion of an N-terminal TP-methylase and a C-terminal MazG-type nucleotide pyrophosphohydrolase domain. MazG-like NTP-PPases have been implicated in house-cleaning functions such as degrading abnormal (d)NTPs. TP-methylases use S-AdoMet in the methylation of diverse substrates. Most TP-methylase family members catalyze various methylation steps in cobalamin (vitamin B12) biosynthesis, other members like diphthine synthase and ribosomal RNA small subunit methyltransferase I (RsmI) act on other substrates. The specific function of YabN's TP-methylase domain is not known. Pssm-ID: 381177 Cd Length: 218 Bit Score: 343.70 E-value: 2.15e-117
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| mazG | TIGR00444 | MazG family protein; This family of prokaryotic proteins has no known function. It includes ... |
239-482 | 2.37e-107 | |||||
MazG family protein; This family of prokaryotic proteins has no known function. It includes the uncharacterized protein MazG in E. coli. [Unknown function, General] Pssm-ID: 273082 [Multi-domain] Cd Length: 248 Bit Score: 319.08 E-value: 2.37e-107
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| NTP-PPase_MazG_Nterm | cd11528 | Nucleoside Triphosphate Pyrophosphohydrolase (EC 3.6.1.8) N-terminal tandem-domain of MazG ... |
236-347 | 3.66e-66 | |||||
Nucleoside Triphosphate Pyrophosphohydrolase (EC 3.6.1.8) N-terminal tandem-domain of MazG proteins from Escherichia coli and bacterial homologs; MazG is a NTP-PPase that hydrolyzes all canonical NTPs into their corresponding nucleoside monophosphates and pyrophosphate. The prototype of this family is MazG proteins from Escherichia coli (EcMazG) that represents the most abundant form consisting two sequence-related domains in tandem, this family corresponding to the N-terminal MazG-like domain. EcMazG functions as a regulator of cellular response to starvation by lowering the cellular concentration of guanosine 3',5'-bispyrophosphate (ppGpp). EcMazG exists as a dimer; each monomer contains two tandem MazG-like domains with similarly folded globular structures. However, only the C-terminal domain has well-ordered active site and exhibits an NTPase activity responsible for the regulation of bacterial cell survival under nutritional stress. Divalent ions, such as Mg2+ or Mn2+, are required for activity; however, this domain does not exhibit an NTPase activity despite containing structural features such as the EEXX(E/D) motif and key basic catalytic residues responsible for nucleotide pyrophosphohydrolysis activity. It is suggested that the N-terminal domain of EcMazG might have a house-cleaning function by hydrolyzing noncanonical NTPs whose incorporation into the nascent DNA leads to increased mutagenesis and DNA damage. Pssm-ID: 212135 Cd Length: 114 Bit Score: 208.52 E-value: 3.66e-66
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| PRK12333 | PRK12333 | nucleoside triphosphate pyrophosphohydrolase; Reviewed |
236-447 | 1.62e-63 | |||||
nucleoside triphosphate pyrophosphohydrolase; Reviewed Pssm-ID: 237064 [Multi-domain] Cd Length: 204 Bit Score: 205.04 E-value: 1.62e-63
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| PRK12334 | PRK12334 | nucleoside triphosphate pyrophosphohydrolase; Reviewed |
238-451 | 3.91e-61 | |||||
nucleoside triphosphate pyrophosphohydrolase; Reviewed Pssm-ID: 237065 [Multi-domain] Cd Length: 277 Bit Score: 201.44 E-value: 3.91e-61
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| NTP-PPase_MazG_Cterm | cd11529 | Nucleoside Triphosphate Pyrophosphohydrolase (EC 3.6.1.8) C-terminal tandem-domain of MazG ... |
367-482 | 3.35e-52 | |||||
Nucleoside Triphosphate Pyrophosphohydrolase (EC 3.6.1.8) C-terminal tandem-domain of MazG proteins from Escherichia coli and bacterial homologs'; MazG is a NTP-PPase that hydrolyzes all canonical NTPs into their corresponding nucleoside monophosphates and pyrophosphate. The prototype of this family is MazG proteins from Escherichia coli (EcMazG) that represents the most abundant form consisting two sequence-related domains in tandem, this family corresponding to the C-terminal MazG-like domain. EcMazG functions as a regulator of cellular response to starvation by lowering the cellular concentration of guanosine 3',5'-bispyrophosphate (ppGpp). EcMazG exists as a dimer. Each monomer contains two tandem MazG-like domains with similarly folded globular structures. However, only the C-terminal domain has well-ordered active sites and exhibits an NTPase activity responsible for the regulation of bacterial cell survival under nutritional stress. Divalent ions, such as Mg2+ or Mn2+, are required for activity, along with structural features such as EEXX(E/D) motifs and key basic catalytic residues. It has been shown that the C-terminus NTPase activity is responsible for regulation of bacterial cell survival under nutritional stress. Pssm-ID: 212136 Cd Length: 116 Bit Score: 172.27 E-value: 3.35e-52
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| MazG | pfam03819 | MazG nucleotide pyrophosphohydrolase domain; This domain is about 100 amino acid residues in ... |
255-328 | 9.70e-32 | |||||
MazG nucleotide pyrophosphohydrolase domain; This domain is about 100 amino acid residues in length. It is found in the MazG protein from E. coli. It contains four conserved negatively charged residues that probably form an active site or metal binding site. This domain is found in isolation in some proteins as well as associated with pfam00590. This domain is clearly related to pfam01503 another pyrophosphohydrolase involved in histidine biosynthesis. This family may be structurally related to the NUDIX domain pfam00293 (Bateman A pers. obs.). Pssm-ID: 427525 Cd Length: 74 Bit Score: 116.16 E-value: 9.70e-32
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| TP_methylase | cd09815 | S-AdoMet-dependent tetrapyrrole methylases; This superfamily uses S-AdoMet ... |
8-221 | 7.77e-30 | |||||
S-AdoMet-dependent tetrapyrrole methylases; This superfamily uses S-AdoMet (S-adenosyl-L-methionine or SAM) in the methylation of diverse substrates. Most members catalyze various methylation steps in cobalamin (vitamin B12) biosynthesis. There are two distinct cobalamin biosynthetic pathways in bacteria. The aerobic pathway requires oxygen, and cobalt is inserted late in the pathway; the anaerobic pathway does not require oxygen, and cobalt insertion is the first committed step towards cobalamin synthesis. The enzymes involved in the aerobic pathway are prefixed Cob and those of the anaerobic pathway Cbi. Most of the enzymes are shared by both pathways and a few enzymes are pathway-specific. Diphthine synthase and ribosomal RNA small subunit methyltransferase I (RsmI) are two superfamily members that are not involved in cobalamin biosynthesis. Diphthine synthase participates in the posttranslational modification of a specific histidine residue in elongation factor 2 (EF-2) of eukaryotes and archaea to diphthamide. RsmI catalyzes the 2-O-methylation of the ribose of cytidine 1402 (C1402) in 16S rRNA. Other superfamily members not involved in cobalamin biosynthesis include the N-terminal tetrapyrrole methylase domain of Bacillus subtilis YabN whose specific function is unknown, and Omphalotus olearius omphalotin methyltransferase which catalyzes the automethylation of its own C-terminus; this C terminus is subsequently released and macrocyclized to give Omphalotin A, a potent nematicide. Pssm-ID: 381167 [Multi-domain] Cd Length: 219 Bit Score: 115.95 E-value: 7.77e-30
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| OphMA_like | cd19916 | tetrapyrrole methylase family protein similar to Omphalotus olearius omphalotin ... |
5-222 | 2.91e-18 | |||||
tetrapyrrole methylase family protein similar to Omphalotus olearius omphalotin methyltransferase (OphMA) and Dendrothele bispora dbOphMA; OphMA, is the precursor protein of the fungal cyclic peptide Omphalotin A. Omphalotin A is a potent nematicide, having 9 out of 12 of its residues methylated at the backbone amide. Omphalotin A derives from the C-terminus of OphMA (also known as OphA). OphMA catalyzes the automethylation of its own C-terminus using S-adenosyl methionine (SAM); this C terminus is subsequently released and macrocyclized by the protease OphP to give Omphalotin A. Pssm-ID: 381179 Cd Length: 237 Bit Score: 83.68 E-value: 2.91e-18
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| TP_methylase | pfam00590 | Tetrapyrrole (Corrin/Porphyrin) Methylases; This family uses S-AdoMet in the methylation of ... |
5-207 | 1.87e-17 | |||||
Tetrapyrrole (Corrin/Porphyrin) Methylases; This family uses S-AdoMet in the methylation of diverse substrates. This family includes a related group of bacterial proteins of unknown function. This family includes the methylase Dipthine synthase. Pssm-ID: 425769 [Multi-domain] Cd Length: 209 Bit Score: 80.85 E-value: 1.87e-17
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| NTP-PPase_COG4997 | cd11532 | Nucleoside Triphosphate Pyrophosphohydrolase (EC 3.6.1.8) MazG-like domain found in a group of ... |
258-323 | 3.62e-04 | |||||
Nucleoside Triphosphate Pyrophosphohydrolase (EC 3.6.1.8) MazG-like domain found in a group of uncharacterized proteins from archaea and bacteria; The family includes some uncharacterized hypothetical proteins from archaea and bacteria. Although their biological roles remain unclear, the family members show significant sequence similarity to the dimeric 2-deoxyuridine 5'-triphosphate nucleotidohydrolase (dUTP pyrophosphatase or dUTPase) and NTP-PPase MazG proteins. However, unlike typical tandem-domain MazG proteins, the family contains a single MazG-like domain. Pssm-ID: 212139 Cd Length: 95 Bit Score: 39.45 E-value: 3.62e-04
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| NTP-PPase_HisIE_like | cd11534 | Nucleoside Triphosphate Pyrophosphohydrolase (EC 3.6.1.8) MazG-like domain found in ... |
253-299 | 9.77e-04 | |||||
Nucleoside Triphosphate Pyrophosphohydrolase (EC 3.6.1.8) MazG-like domain found in Escherichia coli phosphoribosyl-ATP pyrophosphohydrolase (HisIE or PRATP-PH) and its homologs; This family includes Escherichia coli phosphoribosyl-ATP pyrophosphohydrolase, HisIE, and its homologs from all three kingdoms of life. E. coli HisIE is encoded by the hisIE gene, which is formed by hisE gene fused to hisl. HisIE is a bifunctional enzyme responsible for the second and third steps of the histidine-biosynthesis pathway. Its N-terminal and C-terminal domains have phosphoribosyl-AMP cyclohydrolase (HisI) and phosphoribosyl-ATP pyrophosphohydrolase (HisE or PRATP-PH) activity, respectively. This family corresponds to the C-terminal domain of HisIE and includes many hisE gene encoding proteins, all of which show significant sequence similarity to Mycobacterium tuberculosis phosphoribosyl-ATP pyrophosphohydrolase (HisE or PRATP-PH). These proteins may be responsible for only the second step in the histidine-biosynthetic pathway, irreversibly hydrolyzing phosphoribosyl-ATP (PRATP) to phosphoribosyl-AMP (PRAMP) and pyrophosphate. Pssm-ID: 212141 Cd Length: 84 Bit Score: 38.21 E-value: 9.77e-04
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| COG4997 | COG4997 | Predicted house-cleaning noncanonical NTP pyrophosphatase, all-alpha NTP-PPase (MazG) ... |
258-323 | 1.81e-03 | |||||
Predicted house-cleaning noncanonical NTP pyrophosphatase, all-alpha NTP-PPase (MazG) superfamily [General function prediction only]; Pssm-ID: 444021 Cd Length: 108 Bit Score: 37.91 E-value: 1.81e-03
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| NTP-PPase | cd11523 | Nucleoside Triphosphate Pyrophosphohydrolase (EC 3.6.1.8) MazG-like domain superfamily; This ... |
238-296 | 4.94e-03 | |||||
Nucleoside Triphosphate Pyrophosphohydrolase (EC 3.6.1.8) MazG-like domain superfamily; This superfamily contains enzymes that hydrolyze the alpha-beta phosphodiester bond of all canonical NTPs into monophosphate derivatives and pyrophosphate (PPi). Divalent ions, such as Mg2+ ion(s), are essential to activate a proposed water nucleophile and stabilize the charged intermediates to facilitate catalysis. These enzymes share a conserved divalent ion-binding motif EXX[E/D] in their active sites. They also share a highly conserved four-helix bundle, where one face forms the active site, while the other participates in oligomer assembly. The four-helix bundle consists of two central antiparallel alpha-helices that can be contained within a single protomer or form upon dimerization. The superfamily members include dimeric dUTP pyrophosphatases (dUTPases; EC 3.6.1.23), the nonspecific NTP-PPase MazG proteins, HisE-encoded phosphoribosyl ATP pyrophosphohydolase (PRA-PH), fungal histidine biosynthesis trifunctional proteins, and several uncharacterized protein families. Pssm-ID: 212133 Cd Length: 72 Bit Score: 35.83 E-value: 4.94e-03
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| MazG | COG1694 | NTP pyrophosphatase, house-cleaning of non-canonical NTPs [Defense mechanisms]; |
249-298 | 6.90e-03 | |||||
NTP pyrophosphatase, house-cleaning of non-canonical NTPs [Defense mechanisms]; Pssm-ID: 441300 Cd Length: 95 Bit Score: 35.94 E-value: 6.90e-03
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| hisE | PRK00400 | phosphoribosyl-ATP diphosphatase; |
254-299 | 7.49e-03 | |||||
phosphoribosyl-ATP diphosphatase; Pssm-ID: 179005 Cd Length: 105 Bit Score: 36.29 E-value: 7.49e-03
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