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dCTP pyrophosphatase 1 [Homo sapiens]
nucleotide pyrophosphohydrolase( domain architecture ID 10183967)
nucleotide pyrophosphohydrolase similar to mammalian dCTP diphosphatase, which hydrolyzes deoxynucleoside triphosphates (dNTPs) to the corresponding nucleoside monophosphates
List of domain hits
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Name | Accession | Description | Interval | E-value | |||
NTP-PPase_RS21-C6_like | cd11537 | Nucleoside Triphosphate Pyrophosphohydrolase (EC 3.6.1.8) MazG-like domain found in mouse ... |
35-125 | 3.80e-44 | |||
Nucleoside Triphosphate Pyrophosphohydrolase (EC 3.6.1.8) MazG-like domain found in mouse RS21-C6 protein and its homologs; RS21-C6 proteins, highly expressed in all vertebrate genomes and green plants, act as house-cleaning enzymes, removing 5-methyl dCTP (m5dCTP) in order to prevent gene silencing. They 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, RS21-C6 contains a single MazG-like domain and functions as a tetramer (a dimer of dimers) with a typical four-helical bundle. Divalent ions, such as Mg2+, are required for its pyrophosphatase activity. This family also includes a pyrophosphatase from Archaeoglobus fulgidus (Af1178). Although its biological role remains unclear, Af1178 shows significant sequence similarity to the mouse RS21-C6 protein. : Pssm-ID: 212144 Cd Length: 90 Bit Score: 140.73 E-value: 3.80e-44
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Name | Accession | Description | Interval | E-value | |||
NTP-PPase_RS21-C6_like | cd11537 | Nucleoside Triphosphate Pyrophosphohydrolase (EC 3.6.1.8) MazG-like domain found in mouse ... |
35-125 | 3.80e-44 | |||
Nucleoside Triphosphate Pyrophosphohydrolase (EC 3.6.1.8) MazG-like domain found in mouse RS21-C6 protein and its homologs; RS21-C6 proteins, highly expressed in all vertebrate genomes and green plants, act as house-cleaning enzymes, removing 5-methyl dCTP (m5dCTP) in order to prevent gene silencing. They 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, RS21-C6 contains a single MazG-like domain and functions as a tetramer (a dimer of dimers) with a typical four-helical bundle. Divalent ions, such as Mg2+, are required for its pyrophosphatase activity. This family also includes a pyrophosphatase from Archaeoglobus fulgidus (Af1178). Although its biological role remains unclear, Af1178 shows significant sequence similarity to the mouse RS21-C6 protein. Pssm-ID: 212144 Cd Length: 90 Bit Score: 140.73 E-value: 3.80e-44
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MazG | COG1694 | NTP pyrophosphatase, house-cleaning of non-canonical NTPs [Defense mechanisms]; |
32-129 | 1.37e-33 | |||
NTP pyrophosphatase, house-cleaning of non-canonical NTPs [Defense mechanisms]; Pssm-ID: 441300 Cd Length: 95 Bit Score: 114.14 E-value: 1.37e-33
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MazG-like | pfam12643 | MazG-like family; This family of short proteins are distantly related to the MazG enzyme. This ... |
63-144 | 9.44e-11 | |||
MazG-like family; This family of short proteins are distantly related to the MazG enzyme. This suggests that these proteins are enzymes that catalyze a related reaction. Pssm-ID: 463653 Cd Length: 85 Bit Score: 55.27 E-value: 9.44e-11
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Name | Accession | Description | Interval | E-value | |||
NTP-PPase_RS21-C6_like | cd11537 | Nucleoside Triphosphate Pyrophosphohydrolase (EC 3.6.1.8) MazG-like domain found in mouse ... |
35-125 | 3.80e-44 | |||
Nucleoside Triphosphate Pyrophosphohydrolase (EC 3.6.1.8) MazG-like domain found in mouse RS21-C6 protein and its homologs; RS21-C6 proteins, highly expressed in all vertebrate genomes and green plants, act as house-cleaning enzymes, removing 5-methyl dCTP (m5dCTP) in order to prevent gene silencing. They 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, RS21-C6 contains a single MazG-like domain and functions as a tetramer (a dimer of dimers) with a typical four-helical bundle. Divalent ions, such as Mg2+, are required for its pyrophosphatase activity. This family also includes a pyrophosphatase from Archaeoglobus fulgidus (Af1178). Although its biological role remains unclear, Af1178 shows significant sequence similarity to the mouse RS21-C6 protein. Pssm-ID: 212144 Cd Length: 90 Bit Score: 140.73 E-value: 3.80e-44
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MazG | COG1694 | NTP pyrophosphatase, house-cleaning of non-canonical NTPs [Defense mechanisms]; |
32-129 | 1.37e-33 | |||
NTP pyrophosphatase, house-cleaning of non-canonical NTPs [Defense mechanisms]; Pssm-ID: 441300 Cd Length: 95 Bit Score: 114.14 E-value: 1.37e-33
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NTP-PPase | cd11523 | Nucleoside Triphosphate Pyrophosphohydrolase (EC 3.6.1.8) MazG-like domain superfamily; This ... |
36-107 | 7.33e-13 | |||
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: 60.48 E-value: 7.33e-13
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NTP-PPase_SsMazG | cd11535 | Nucleoside Triphosphate Pyrophosphohydrolase (EC 3.6.1.8) MazG-like domain found in Sulfolobus ... |
36-123 | 7.13e-12 | |||
Nucleoside Triphosphate Pyrophosphohydrolase (EC 3.6.1.8) MazG-like domain found in Sulfolobus solfataricus (Ss) and its homologs from archaea and bacteria; This family includes a MazG-like protein from Sulfolobus solfataricus (SsMazG) and its homologs from archaea and bacteria. Although its biological roles remain still unclear, SsMazG shows significant sequence similarity to the NTP-PPase MazG proteins. However, unlike typical tandem-domain MazG proteins, SsMazG contains a single MazG-like domain. It is predicted that SsMazG might participate in house-cleaning by preventing incorporation of the oxidation product 2-oxo-(d)ATP (iso-dGTP), a mutagenic derivative of ATP, into DNA. Pssm-ID: 212142 Cd Length: 76 Bit Score: 57.99 E-value: 7.13e-12
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MazG-like | pfam12643 | MazG-like family; This family of short proteins are distantly related to the MazG enzyme. This ... |
63-144 | 9.44e-11 | |||
MazG-like family; This family of short proteins are distantly related to the MazG enzyme. This suggests that these proteins are enzymes that catalyze a related reaction. Pssm-ID: 463653 Cd Length: 85 Bit Score: 55.27 E-value: 9.44e-11
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NTP-PPase_iMazG | cd11536 | Nucleoside Triphosphate Pyrophosphohydrolase (EC 3.6.1.8) MazG-like domain found in ... |
45-129 | 7.76e-09 | |||
Nucleoside Triphosphate Pyrophosphohydrolase (EC 3.6.1.8) MazG-like domain found in integron-associated MazG (iMazG) proteins; This family corresponds to the iMazG proteins representing a new subfamily of MazG NTP-PPases. iMazG is likely to act as a house-cleaning enzyme capable of removing aberrant dNTPs, preventing the incorporation of damaging non-canonical nucleotides into host-cell DNA. It can convert dNTP to dNMP and pyrophosphate by cleaving between the alpha- and beta-phosphates of its dNTP substrates, with a marked preference for dCTP and dATP. Unlike typical tandem-domain MazG proteins, iMazG contains a single MazG-like domain and functions as a tetramer (a dimer of dimers) with a typical four-helical bundle. The divalent ions, such as Mg2+, are required for its pyrophosphatase activity. Pssm-ID: 212143 Cd Length: 90 Bit Score: 50.52 E-value: 7.76e-09
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NTP-PPase_u4 | cd11541 | Nucleoside Triphosphate Pyrophosphohydrolase (EC 3.6.1.8) MazG-like domain found in a group of ... |
55-114 | 1.05e-07 | |||
Nucleoside Triphosphate Pyrophosphohydrolase (EC 3.6.1.8) MazG-like domain found in a group of uncharacterized proteins from bacteria and archaea; This family corresponds to a group of uncharacterized hypothetical proteins from bacteria, showing a high 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, members in this family consist of a single MazG-like domain that contains a well conserved divalent ion-binding motif EXX[E/D]. Pssm-ID: 212148 Cd Length: 91 Bit Score: 47.22 E-value: 1.05e-07
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NTP-PPase_u5 | cd11542 | Nucleoside Triphosphate Pyrophosphohydrolase (EC 3.6.1.8) MazG-like domain found in a group of ... |
47-128 | 1.06e-04 | |||
Nucleoside Triphosphate Pyrophosphohydrolase (EC 3.6.1.8) MazG-like domain found in a group of uncharacterized proteins from bacteria and archaea; This family corresponds to a group of uncharacterized hypothetical proteins from bacteria, showing a high 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, members in this family consist of a single MazG-like domain that contains a well conserved divalent ion-binding motif EXX[E/D]. Pssm-ID: 212149 Cd Length: 99 Bit Score: 39.61 E-value: 1.06e-04
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NTP-PPase_BsYpjD | cd11531 | Nucleoside Triphosphate Pyrophosphohydrolase (EC 3.6.1.8) MazG-like domain putative ... |
53-129 | 5.65e-04 | |||
Nucleoside Triphosphate Pyrophosphohydrolase (EC 3.6.1.8) MazG-like domain putative pyrophosphatase YpjD from Bacillus subtilis and its bacterial homologs; This family includes a putative pyrophosphatase Ypjd from Bacillus subtilis (BsYpjD) and its homologs. Although its biological role has not been described in detail, BsYpjD shows 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, BsYpjD contains a single MazG-like domain. Pssm-ID: 212138 Cd Length: 93 Bit Score: 37.29 E-value: 5.65e-04
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NTP-PPase_u6 | cd11543 | Nucleoside Triphosphate Pyrophosphohydrolase EC 3.6.1.8) MazG-like domain found in a group of ... |
33-121 | 2.33e-03 | |||
Nucleoside Triphosphate Pyrophosphohydrolase EC 3.6.1.8) MazG-like domain found in a group of uncharacterized proteins from bacteria and archaea; This family corresponds to a group of uncharacterized hypothetical proteins from bacteria, showing a high 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, members in this family consist of a single MazG-like domain. Pssm-ID: 212150 Cd Length: 87 Bit Score: 35.37 E-value: 2.33e-03
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NTP-PPase_u1 | cd11538 | Nucleoside Triphosphate Pyrophosphohydrolase (EC 3.6.1.8) MazG-like domain found in a group of ... |
31-121 | 3.08e-03 | |||
Nucleoside Triphosphate Pyrophosphohydrolase (EC 3.6.1.8) MazG-like domain found in a group of uncharacterized proteins from bacteria; This family corresponds to a group of uncharacterized hypothetical proteins from bacteria, showing a high 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, members in this family consist of a single MazG-like domain that contains a well conserved divalent ion-binding motif EXX[E/D]. Pssm-ID: 212145 Cd Length: 97 Bit Score: 35.37 E-value: 3.08e-03
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MazG | pfam03819 | MazG nucleotide pyrophosphohydrolase domain; This domain is about 100 amino acid residues in ... |
53-130 | 3.62e-03 | |||
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: 34.50 E-value: 3.62e-03
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NTP-PPase_dUTPase | cd11527 | Nucleoside Triphosphate Pyrophosphohydrolase (EC 3.6.1.8) MazG-like domain found in dimeric ... |
54-128 | 7.13e-03 | |||
Nucleoside Triphosphate Pyrophosphohydrolase (EC 3.6.1.8) MazG-like domain found in dimeric 2-Deoxyuridine 5'-triphosphate nucleotidohydrolase and similar proteins; dUTPase (dUTP pyrophosphatase; EC 3.6.1.23) catalyzes the hydrolysis of dUTP to dUMP and pyrophosphate. It acts to ensure chromosomal integrity by reducing the effective ratio of dUTP/dTTP. Members in this family are dimeric dUTPases, such as those from Leishmania major, Trypanosoma cruzi, and Campylobacter jejuni, which differ from the monomeric and trimeric forms and adopt an all-alpha topology. A central four-helix bundle, consisting of two alpha-helices from the rigid domain and two helices from the mobile domain and connecting loops, form the active site in dimeric dUTPase-like proteins, requiring the presence of metal ion cofactors to hydrolyze both dUTP and dUDP. Pssm-ID: 212134 [Multi-domain] Cd Length: 94 Bit Score: 34.11 E-value: 7.13e-03
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