adenine DNA glycosylase isoform X4 [Mus musculus]
DNA_Glycosylase_C domain-containing protein( domain architecture ID 10130797)
DNA_Glycosylase_C domain-containing protein
List of domain hits
Name | Accession | Description | Interval | E-value | ||||
MutY super family | cl34172 | Adenine-specific DNA glycosylase, acts on AG and A-oxoG pairs [Replication, recombination and ... |
1-214 | 5.23e-43 | ||||
Adenine-specific DNA glycosylase, acts on AG and A-oxoG pairs [Replication, recombination and repair]; The actual alignment was detected with superfamily member COG1194: Pssm-ID: 440807 [Multi-domain] Cd Length: 350 Bit Score: 149.13 E-value: 5.23e-43
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Name | Accession | Description | Interval | E-value | ||||
MutY | COG1194 | Adenine-specific DNA glycosylase, acts on AG and A-oxoG pairs [Replication, recombination and ... |
1-214 | 5.23e-43 | ||||
Adenine-specific DNA glycosylase, acts on AG and A-oxoG pairs [Replication, recombination and repair]; Pssm-ID: 440807 [Multi-domain] Cd Length: 350 Bit Score: 149.13 E-value: 5.23e-43
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NUDIX_DNA_Glycosylase_C-MutY | cd03431 | C-terminal domain of DNA glycosylase; DNA glycosylase (MutY in bacteria and hMYH in humans) is ... |
82-209 | 9.72e-32 | ||||
C-terminal domain of DNA glycosylase; DNA glycosylase (MutY in bacteria and hMYH in humans) is responsible for repairing misread A*oxoG residues to C*G by removing the inappropriately paired adenine base from the DNA backbone. It belongs to the NUDIX hydrolase superfamily and is important for the repair of various genotoxic lesions. Enzymes belonging to this superfamily requires a divalent cation, such as Mg2+ or Mn2+ for their activity. They are also recognized by a highly conserved 23-residue NUDIX motif (GX5EX7REUXEEXGU, where U = I, L or V). However, DNA glycosylase does not seem to contain this signature motif. DNA glycosylase consists of 2 domains: the N-terminal domain contains the catalytic properties of the enzyme and the C-terminal domain affects substrate (oxoG) binding and enzymatic turnover. The C-terminal domain is highly similar to MutT, based on secondary structure and topology, despite low sequence identity. MutT sanitizes the nucleotide precursor pool by hydrolyzing oxo-dGTP to oxo-dGMO and inorganic pyrophosphate. The similarity strongly suggests that the two proteins share a common evolutionary origin. Pssm-ID: 467537 [Multi-domain] Cd Length: 118 Bit Score: 113.17 E-value: 9.72e-32
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NUDIX_4 | pfam14815 | NUDIX domain; |
103-211 | 1.17e-23 | ||||
NUDIX domain; Pssm-ID: 464330 [Multi-domain] Cd Length: 114 Bit Score: 91.99 E-value: 1.17e-23
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PRK10880 | PRK10880 | adenine DNA glycosylase; |
1-167 | 2.46e-07 | ||||
adenine DNA glycosylase; Pssm-ID: 182805 [Multi-domain] Cd Length: 350 Bit Score: 50.86 E-value: 2.46e-07
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FES | smart00525 | iron-sulpphur binding domain in DNA-(apurinic or apyrimidinic site) lyase (subfamily of ENDO3); ... |
7-27 | 1.37e-03 | ||||
iron-sulpphur binding domain in DNA-(apurinic or apyrimidinic site) lyase (subfamily of ENDO3); Pssm-ID: 197771 [Multi-domain] Cd Length: 21 Bit Score: 35.22 E-value: 1.37e-03
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Name | Accession | Description | Interval | E-value | ||||
MutY | COG1194 | Adenine-specific DNA glycosylase, acts on AG and A-oxoG pairs [Replication, recombination and ... |
1-214 | 5.23e-43 | ||||
Adenine-specific DNA glycosylase, acts on AG and A-oxoG pairs [Replication, recombination and repair]; Pssm-ID: 440807 [Multi-domain] Cd Length: 350 Bit Score: 149.13 E-value: 5.23e-43
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NUDIX_DNA_Glycosylase_C-MutY | cd03431 | C-terminal domain of DNA glycosylase; DNA glycosylase (MutY in bacteria and hMYH in humans) is ... |
82-209 | 9.72e-32 | ||||
C-terminal domain of DNA glycosylase; DNA glycosylase (MutY in bacteria and hMYH in humans) is responsible for repairing misread A*oxoG residues to C*G by removing the inappropriately paired adenine base from the DNA backbone. It belongs to the NUDIX hydrolase superfamily and is important for the repair of various genotoxic lesions. Enzymes belonging to this superfamily requires a divalent cation, such as Mg2+ or Mn2+ for their activity. They are also recognized by a highly conserved 23-residue NUDIX motif (GX5EX7REUXEEXGU, where U = I, L or V). However, DNA glycosylase does not seem to contain this signature motif. DNA glycosylase consists of 2 domains: the N-terminal domain contains the catalytic properties of the enzyme and the C-terminal domain affects substrate (oxoG) binding and enzymatic turnover. The C-terminal domain is highly similar to MutT, based on secondary structure and topology, despite low sequence identity. MutT sanitizes the nucleotide precursor pool by hydrolyzing oxo-dGTP to oxo-dGMO and inorganic pyrophosphate. The similarity strongly suggests that the two proteins share a common evolutionary origin. Pssm-ID: 467537 [Multi-domain] Cd Length: 118 Bit Score: 113.17 E-value: 9.72e-32
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NUDIX_4 | pfam14815 | NUDIX domain; |
103-211 | 1.17e-23 | ||||
NUDIX domain; Pssm-ID: 464330 [Multi-domain] Cd Length: 114 Bit Score: 91.99 E-value: 1.17e-23
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PRK10880 | PRK10880 | adenine DNA glycosylase; |
1-167 | 2.46e-07 | ||||
adenine DNA glycosylase; Pssm-ID: 182805 [Multi-domain] Cd Length: 350 Bit Score: 50.86 E-value: 2.46e-07
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PRK10546 | PRK10546 | pyrimidine (deoxy)nucleoside triphosphate diphosphatase; |
91-141 | 1.54e-05 | ||||
pyrimidine (deoxy)nucleoside triphosphate diphosphatase; Pssm-ID: 182536 [Multi-domain] Cd Length: 135 Bit Score: 43.58 E-value: 1.54e-05
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NUDIX_MutT_NudA_like | cd03425 | MutT pyrophosphohydrolase; The MutT pyrophosphohydrolase is a prototypical NUDIX hydrolase ... |
103-195 | 1.31e-04 | ||||
MutT pyrophosphohydrolase; The MutT pyrophosphohydrolase is a prototypical NUDIX hydrolase that catalyzes the hydrolysis of nucleoside and deoxynucleoside triphosphates (NTPs and dNTPs) by substitution at a beta-phosphorus to yield a nucleotide monophosphate (NMP) and inorganic pyrophosphate (PPi). This enzyme requires two divalent cations for activity; one coordinates the phosphoryl groups of the NTP/dNTP substrate, and the other coordinates to the enzyme. It also contains the NUDIX motif, a highly conserved 23-residue block (GX5EX7REUXEEXGU, where U = I, L or V), that functions as metal binding and catalytic site. MutT pyrophosphohydrolase is important in preventing errors in DNA replication by hydrolyzing mutagenic nucleotides such as 8-oxo-dGTP (a product of oxidative damage), which can mispair with template adenine during DNA replication, to guanine nucleotides. Pssm-ID: 467531 [Multi-domain] Cd Length: 123 Bit Score: 40.51 E-value: 1.31e-04
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Nth | COG0177 | Endonuclease III [Replication, recombination and repair]; |
3-28 | 3.13e-04 | ||||
Endonuclease III [Replication, recombination and repair]; Pssm-ID: 439947 [Multi-domain] Cd Length: 198 Bit Score: 40.85 E-value: 3.13e-04
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MutT | COG0494 | 8-oxo-dGTP pyrophosphatase MutT and related house-cleaning NTP pyrophosphohydrolases, NUDIX ... |
103-208 | 9.17e-04 | ||||
8-oxo-dGTP pyrophosphatase MutT and related house-cleaning NTP pyrophosphohydrolases, NUDIX family [Defense mechanisms]; Pssm-ID: 440260 [Multi-domain] Cd Length: 143 Bit Score: 38.48 E-value: 9.17e-04
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FES | smart00525 | iron-sulpphur binding domain in DNA-(apurinic or apyrimidinic site) lyase (subfamily of ENDO3); ... |
7-27 | 1.37e-03 | ||||
iron-sulpphur binding domain in DNA-(apurinic or apyrimidinic site) lyase (subfamily of ENDO3); Pssm-ID: 197771 [Multi-domain] Cd Length: 21 Bit Score: 35.22 E-value: 1.37e-03
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PRK10776 | PRK10776 | 8-oxo-dGTP diphosphatase MutT; |
107-167 | 1.92e-03 | ||||
8-oxo-dGTP diphosphatase MutT; Pssm-ID: 182721 [Multi-domain] Cd Length: 129 Bit Score: 37.27 E-value: 1.92e-03
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NUDIX_Ap6A_hydrolase | cd03673 | diadenosine hexaphosphate (Ap6A) hydrolase; Diadenosine hexaphosphate (Ap6A) hydrolase is a ... |
85-214 | 4.92e-03 | ||||
diadenosine hexaphosphate (Ap6A) hydrolase; Diadenosine hexaphosphate (Ap6A) hydrolase is a member of the NUDIX hydrolase superfamily. Ap6A hydrolase specifically hydrolyzes diadenosine polyphosphates, but not ATP or diadenosine triphosphate, and it generates ATP as the product. Ap6A, the most preferred substrate, hydrolyzes to produce two ATP molecules, which is a novel hydrolysis mode for Ap6A. These results indicate that Ap6A hydrolase is a diadenosine polyphosphate hydrolase. It requires the presence of a divalent cation, such as Mn2+, Mg2+, Zn2+, and Co2+, for activity. Members of the NUDIX hydrolase superfamily are recognized by a highly conserved 23-residue NUDIX motif (GX5EX7REUXEEXGU, where U = I, L or V), which forms a structural motif that functions as a metal binding and catalytic site. Pssm-ID: 467541 [Multi-domain] Cd Length: 131 Bit Score: 36.38 E-value: 4.92e-03
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PRK08999 | PRK08999 | Nudix family hydrolase; |
103-141 | 7.33e-03 | ||||
Nudix family hydrolase; Pssm-ID: 236361 [Multi-domain] Cd Length: 312 Bit Score: 37.16 E-value: 7.33e-03
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Blast search parameters | ||||
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