MULTISPECIES: A/G-specific adenine glycosylase [Staphylococcus]
Protein Classification
A/G-specific adenine glycosylase( domain architecture ID 11439777)
A/G-specific adenine glycosylase prevents DNA mutations by excising adenine (A) from the oxidatively damaged guanine (7,8-dihydro-8-oxoguanine or 7-oxoG):adenine base pair
List of domain hits
| Name | Accession | Description | Interval | E-value | ||||||
| MutY | COG1194 | Adenine-specific DNA glycosylase, acts on AG and A-oxoG pairs [Replication, recombination and ... |
3-345 | 1.67e-171 | ||||||
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: 480.40 E-value: 1.67e-171
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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 ... |
3-345 | 1.67e-171 | ||||||
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: 480.40 E-value: 1.67e-171
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| mutY | TIGR01084 | A/G-specific adenine glycosylase; This equivalog model identifies mutY members of the ... |
7-277 | 5.26e-114 | ||||||
A/G-specific adenine glycosylase; This equivalog model identifies mutY members of the pfam00730 superfamily (HhH-GPD: Helix-hairpin-helix and Gly/Pro rich loop followed by a conserved aspartate). The major members of the superfamily are nth and mutY. [DNA metabolism, DNA replication, recombination, and repair] Pssm-ID: 130156 Cd Length: 275 Bit Score: 332.07 E-value: 5.26e-114
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| PRK10880 | PRK10880 | adenine DNA glycosylase; |
3-296 | 6.79e-71 | ||||||
adenine DNA glycosylase; Pssm-ID: 182805 [Multi-domain] Cd Length: 350 Bit Score: 224.59 E-value: 6.79e-71
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| ENDO3c | cd00056 | endonuclease III; includes endonuclease III (DNA-(apurinic or apyrimidinic site) lyase), ... |
31-187 | 3.24e-47 | ||||||
endonuclease III; includes endonuclease III (DNA-(apurinic or apyrimidinic site) lyase), alkylbase DNA glycosidases (Alka-family) and other DNA glycosidases Pssm-ID: 238013 [Multi-domain] Cd Length: 158 Bit Score: 157.02 E-value: 3.24e-47
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| ENDO3c | smart00478 | endonuclease III; includes endonuclease III (DNA-(apurinic or apyrimidinic site) lyase), ... |
39-189 | 2.85e-34 | ||||||
endonuclease III; includes endonuclease III (DNA-(apurinic or apyrimidinic site) lyase), alkylbase DNA glycosidases (Alka-family) and other DNA glycosidases Pssm-ID: 214684 [Multi-domain] Cd Length: 149 Bit Score: 123.14 E-value: 2.85e-34
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| HhH-GPD | pfam00730 | HhH-GPD superfamily base excision DNA repair protein; This family contains a diverse range of ... |
35-148 | 4.93e-27 | ||||||
HhH-GPD superfamily base excision DNA repair protein; This family contains a diverse range of structurally related DNA repair proteins. The superfamily is called the HhH-GPD family after its hallmark Helix-hairpin-helix and Gly/Pro rich loop followed by a conserved aspartate. This includes endonuclease III, EC:4.2.99.18 and MutY an A/G-specific adenine glycosylase, both have a C terminal 4Fe-4S cluster. The family also includes 8-oxoguanine DNA glycosylases. The methyl-CPG binding protein MBD4 also contains a related domain that is a thymine DNA glycosylase. The family also includes DNA-3-methyladenine glycosylase II EC:3.2.2.21 and other members of the AlkA family. Pssm-ID: 425841 [Multi-domain] Cd Length: 141 Bit Score: 103.90 E-value: 4.93e-27
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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 ... |
3-345 | 1.67e-171 | ||||||
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: 480.40 E-value: 1.67e-171
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| mutY | TIGR01084 | A/G-specific adenine glycosylase; This equivalog model identifies mutY members of the ... |
7-277 | 5.26e-114 | ||||||
A/G-specific adenine glycosylase; This equivalog model identifies mutY members of the pfam00730 superfamily (HhH-GPD: Helix-hairpin-helix and Gly/Pro rich loop followed by a conserved aspartate). The major members of the superfamily are nth and mutY. [DNA metabolism, DNA replication, recombination, and repair] Pssm-ID: 130156 Cd Length: 275 Bit Score: 332.07 E-value: 5.26e-114
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| PRK10880 | PRK10880 | adenine DNA glycosylase; |
3-296 | 6.79e-71 | ||||||
adenine DNA glycosylase; Pssm-ID: 182805 [Multi-domain] Cd Length: 350 Bit Score: 224.59 E-value: 6.79e-71
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| ENDO3c | cd00056 | endonuclease III; includes endonuclease III (DNA-(apurinic or apyrimidinic site) lyase), ... |
31-187 | 3.24e-47 | ||||||
endonuclease III; includes endonuclease III (DNA-(apurinic or apyrimidinic site) lyase), alkylbase DNA glycosidases (Alka-family) and other DNA glycosidases Pssm-ID: 238013 [Multi-domain] Cd Length: 158 Bit Score: 157.02 E-value: 3.24e-47
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| ENDO3c | smart00478 | endonuclease III; includes endonuclease III (DNA-(apurinic or apyrimidinic site) lyase), ... |
39-189 | 2.85e-34 | ||||||
endonuclease III; includes endonuclease III (DNA-(apurinic or apyrimidinic site) lyase), alkylbase DNA glycosidases (Alka-family) and other DNA glycosidases Pssm-ID: 214684 [Multi-domain] Cd Length: 149 Bit Score: 123.14 E-value: 2.85e-34
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| PRK13910 | PRK13910 | DNA glycosylase MutY; Provisional |
39-261 | 3.01e-31 | ||||||
DNA glycosylase MutY; Provisional Pssm-ID: 172427 [Multi-domain] Cd Length: 289 Bit Score: 119.36 E-value: 3.01e-31
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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 ... |
227-341 | 2.64e-30 | ||||||
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: 111.63 E-value: 2.64e-30
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| HhH-GPD | pfam00730 | HhH-GPD superfamily base excision DNA repair protein; This family contains a diverse range of ... |
35-148 | 4.93e-27 | ||||||
HhH-GPD superfamily base excision DNA repair protein; This family contains a diverse range of structurally related DNA repair proteins. The superfamily is called the HhH-GPD family after its hallmark Helix-hairpin-helix and Gly/Pro rich loop followed by a conserved aspartate. This includes endonuclease III, EC:4.2.99.18 and MutY an A/G-specific adenine glycosylase, both have a C terminal 4Fe-4S cluster. The family also includes 8-oxoguanine DNA glycosylases. The methyl-CPG binding protein MBD4 also contains a related domain that is a thymine DNA glycosylase. The family also includes DNA-3-methyladenine glycosylase II EC:3.2.2.21 and other members of the AlkA family. Pssm-ID: 425841 [Multi-domain] Cd Length: 141 Bit Score: 103.90 E-value: 4.93e-27
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| Nth | COG0177 | Endonuclease III [Replication, recombination and repair]; |
23-211 | 5.49e-27 | ||||||
Endonuclease III [Replication, recombination and repair]; Pssm-ID: 439947 [Multi-domain] Cd Length: 198 Bit Score: 105.18 E-value: 5.49e-27
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| NUDIX_4 | pfam14815 | NUDIX domain; |
234-339 | 4.39e-25 | ||||||
NUDIX domain; Pssm-ID: 464330 [Multi-domain] Cd Length: 114 Bit Score: 97.77 E-value: 4.39e-25
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| YjhB | COG1051 | ADP-ribose pyrophosphatase YjhB, NUDIX family [Nucleotide transport and metabolism]; |
236-333 | 1.84e-08 | ||||||
ADP-ribose pyrophosphatase YjhB, NUDIX family [Nucleotide transport and metabolism]; Pssm-ID: 440671 [Multi-domain] Cd Length: 125 Bit Score: 52.29 E-value: 1.84e-08
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| PRK10702 | PRK10702 | endonuclease III; Provisional |
61-212 | 2.02e-08 | ||||||
endonuclease III; Provisional Pssm-ID: 182661 [Multi-domain] Cd Length: 211 Bit Score: 53.87 E-value: 2.02e-08
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| NUDIX_Hydrolase | cd02883 | NUDIX hydrolase superfamily; NUDIX hydrolase is a superfamily of enzymes found in all three ... |
236-323 | 2.36e-06 | ||||||
NUDIX hydrolase superfamily; NUDIX hydrolase is a superfamily of enzymes found in all three kingdoms of life, and it catalyzes the hydrolysis of NUcleoside DIphosphates linked to other moieties, X. Enzymes belonging to this superfamily require a divalent cation, such as Mg2+ or Mn2+ for their activity. Members of this family 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. Substrates of NUDIX hydrolase include intact and oxidatively damaged nucleoside triphosphates, dinucleoside polyphosphates, nucleotide-sugars and dinucleotide enzymes. These substrates are metabolites or cell signaling molecules that require regulation during different stages of the cell cycle or during periods of stress. In general, the role of the NUDIX hydrolase is to sanitize the nucleotide pools and to maintain cell viability, thereby serving as surveillance and "house-cleaning" enzymes. Substrate specificity is used to define child families within the superfamily. Differences in substrate specificity are determined by the N-terminal extension or by residues in variable loop regions. Mechanistically, substrate hydrolysis occurs by a nucleophilic substitution reaction, with variation in the numbers and roles of divalent cations required. This superfamily consists of at least nine families: IPP (isopentenyl diphosphate) isomerase, ADP ribose pyrophosphatase, mutT pyrophosphohydrolase, coenzyme-A pyrophosphatase, MTH1-7,8-dihydro-8-oxoguanine-triphosphatase, diadenosine tetraphosphate hydrolase, NADH pyrophosphatase, GDP-mannose hydrolase and the c-terminal portion of the mutY adenine glycosylase. Pssm-ID: 467528 [Multi-domain] Cd Length: 106 Bit Score: 45.86 E-value: 2.36e-06
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| NUDIX_Hydrolase | cd18882 | uncharacterized NUDIX hydrolase subfamily; NUDIX hydrolase is a superfamily of enzymes found ... |
236-326 | 1.57e-05 | ||||||
uncharacterized NUDIX hydrolase subfamily; NUDIX hydrolase is a superfamily of enzymes found in all three kingdoms of life, and it catalyzes the hydrolysis of NUcleoside DIphosphates linked to other moieties, X. Enzymes belonging to this superfamily require a divalent cation, such as Mg2+ or Mn2+ for their activity. Members of this family 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. Substrates of NUDIX hydrolase include intact and oxidatively damaged nucleoside triphosphates, dinucleoside polyphosphates, nucleotide-sugars and dinucleotide enzymes. These substrates are metabolites or cell signaling molecules that require regulation during different stages of the cell cycle or during periods of stress. In general, the role of the NUDIX hydrolase is to sanitize the nucleotide pools and to maintain cell viability, thereby serving as surveillance and "house-cleaning" enzymes. Substrate specificity is used to define child families within the superfamily. Differences in substrate specificity are determined by the N-terminal extension or by residues in variable loop regions. Mechanistically, substrate hydrolysis occurs by a nucleophilic substitution reaction, with variation in the numbers and roles of divalent cations required. This superfamily consists of at least nine families: IPP (isopentenyl diphosphate) isomerase, ADP ribose pyrophosphatase, mutT pyrophosphohydrolase, coenzyme-A pyrophosphatase, MTH1-7,8-dihydro-8-oxoguanine-triphosphatase, diadenosine tetraphosphate hydrolase, NADH pyrophosphatase, GDP-mannose hydrolase and the c-terminal portion of the mutY adenine glycosylase. Pssm-ID: 467593 [Multi-domain] Cd Length: 130 Bit Score: 43.78 E-value: 1.57e-05
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| NUDIX | pfam00293 | NUDIX domain; |
236-341 | 3.17e-05 | ||||||
NUDIX domain; Pssm-ID: 395229 [Multi-domain] Cd Length: 132 Bit Score: 43.24 E-value: 3.17e-05
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| HHH | pfam00633 | Helix-hairpin-helix motif; The helix-hairpin-helix DNA-binding motif is found to be duplicated ... |
99-128 | 3.18e-05 | ||||||
Helix-hairpin-helix motif; The helix-hairpin-helix DNA-binding motif is found to be duplicated in the central domain of RuvA. The HhH domain of DisA, a bacterial checkpoint control protein, is a DNA-binding domain. Pssm-ID: 425789 [Multi-domain] Cd Length: 30 Bit Score: 40.48 E-value: 3.18e-05
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| NUDIX_MutT_NudA_like | cd03425 | MutT pyrophosphohydrolase; The MutT pyrophosphohydrolase is a prototypical NUDIX hydrolase ... |
240-333 | 6.55e-05 | ||||||
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: 42.05 E-value: 6.55e-05
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| NUDIX_MTH2_Nudt15 | cd04678 | MutT homolog 2; MutT Homolog 2 (MTH2; EC 3.6.1.9), also known as NUDIX (nucleoside ... |
236-284 | 3.65e-04 | ||||||
MutT homolog 2; MutT Homolog 2 (MTH2; EC 3.6.1.9), also known as NUDIX (nucleoside diphosphate-linked moiety X)) motif 15/Nudt15, may catalyze the hydrolysis of nucleoside diphosphates, triphosphates including dGTP, dTTP, dCTP, their oxidized forms like 8-oxo-dGTP, and prodrug thiopurine derivatives 6-thio-dGTP and 6-thio-GTP. MTH2 may also play a role in DNA synthesis and cell cycle progression by stabilizing PCNA. Members of the NUDIX hydrolase superfamily catalyze the hydrolysis of NUcleoside DIphosphates linked to other moieties, X. Enzymes belonging to this superfamily require a divalent cation, such as Mg2+ or Mn2+, for their activity and contain a highly conserved 23-residue NUDIX motif (GX5EX7REUXEEXGU, where U = I, L or V), which functions as a metal binding and catalytic site. Substrates of NUDIX hydrolases include intact and oxidatively damaged nucleoside triphosphates, dinucleoside polyphosphates, nucleotide-sugars and dinucleotide enzymes. These substrates are metabolites or cell signaling molecules that require regulation during different stages of the cell cycle or during periods of stress. In general, the role of the NUDIX hydrolase is to sanitize the nucleotide pools and to maintain cell viability, thereby serving as surveillance _ "house-cleaning" enzymes. Substrate specificity is used to define families within the superfamily. Differences in substrate specificity are determined by the N-terminal extension or by residues in variable loop regions. Mechanistically, substrate hydrolysis occurs by a nucleophilic substitution reaction, with variation in the numbers and roles of divalent cations required. Pssm-ID: 467561 [Multi-domain] Cd Length: 128 Bit Score: 39.85 E-value: 3.65e-04
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| NUDIX_Hydrolase | cd04693 | uncharacterized NUDIX hydrolase subfamily; NUDIX hydrolase is a superfamily of enzymes found ... |
236-315 | 3.85e-04 | ||||||
uncharacterized NUDIX hydrolase subfamily; NUDIX hydrolase is a superfamily of enzymes found in all three kingdoms of life, and it catalyzes the hydrolysis of NUcleoside DIphosphates linked to other moieties, X. Enzymes belonging to this superfamily require a divalent cation, such as Mg2+ or Mn2+ for their activity. Members of this family 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. Substrates of NUDIX hydrolase include intact and oxidatively damaged nucleoside triphosphates, dinucleoside polyphosphates, nucleotide-sugars and dinucleotide enzymes. These substrates are metabolites or cell signaling molecules that require regulation during different stages of the cell cycle or during periods of stress. In general, the role of the NUDIX hydrolase is to sanitize the nucleotide pools and to maintain cell viability, thereby serving as surveillance and "house-cleaning" enzymes. Substrate specificity is used to define child families within the superfamily. Differences in substrate specificity are determined by the N-terminal extension or by residues in variable loop regions. Mechanistically, substrate hydrolysis occurs by a nucleophilic substitution reaction, with variation in the numbers and roles of divalent cations required. This superfamily consists of at least nine families: IPP (isopentenyl diphosphate) isomerase, ADP ribose pyrophosphatase, mutT pyrophosphohydrolase, coenzyme-A pyrophosphatase, MTH1-7,8-dihydro-8-oxoguanine-triphosphatase, diadenosine tetraphosphate hydrolase, NADH pyrophosphatase, GDP-mannose hydrolase and the c-terminal portion of the mutY adenine glycosylase. Pssm-ID: 467575 [Multi-domain] Cd Length: 157 Bit Score: 40.20 E-value: 3.85e-04
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| NUDIX_Hydrolase | cd04677 | uncharacterized NUDIX hydrolase subfamily; NUDIX hydrolase is a superfamily of enzymes found ... |
233-284 | 1.66e-03 | ||||||
uncharacterized NUDIX hydrolase subfamily; NUDIX hydrolase is a superfamily of enzymes found in all three kingdoms of life, and it catalyzes the hydrolysis of NUcleoside DIphosphates linked to other moieties, X. Enzymes belonging to this superfamily require a divalent cation, such as Mg2+ or Mn2+ for their activity. Members of this family 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. Substrates of NUDIX hydrolase include intact and oxidatively damaged nucleoside triphosphates, dinucleoside polyphosphates, nucleotide-sugars and dinucleotide enzymes. These substrates are metabolites or cell signaling molecules that require regulation during different stages of the cell cycle or during periods of stress. In general, the role of the NUDIX hydrolase is to sanitize the nucleotide pools and to maintain cell viability, thereby serving as surveillance and "house-cleaning" enzymes. Substrate specificity is used to define child families within the superfamily. Differences in substrate specificity are determined by the N-terminal extension or by residues in variable loop regions. Mechanistically, substrate hydrolysis occurs by a nucleophilic substitution reaction, with variation in the numbers and roles of divalent cations required. This superfamily consists of at least nine families: IPP (isopentenyl diphosphate) isomerase, ADP ribose pyrophosphatase, mutT pyrophosphohydrolase, coenzyme-A pyrophosphatase, MTH1-7,8-dihydro-8-oxoguanine-triphosphatase, diadenosine tetraphosphate hydrolase, NADH pyrophosphatase, GDP-mannose hydrolase and the c-terminal portion of the mutY adenine glycosylase. Pssm-ID: 467560 [Multi-domain] Cd Length: 137 Bit Score: 38.26 E-value: 1.66e-03
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| FES | smart00525 | iron-sulpphur binding domain in DNA-(apurinic or apyrimidinic site) lyase (subfamily of ENDO3); ... |
190-210 | 3.00e-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: 34.45 E-value: 3.00e-03
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| HP0602 | COG2231 | 3-Methyladenine DNA glycosylase, HhH-GPD/Endo3 superfamily [Replication, recombination and ... |
61-208 | 3.35e-03 | ||||||
3-Methyladenine DNA glycosylase, HhH-GPD/Endo3 superfamily [Replication, recombination and repair]; Pssm-ID: 441832 [Multi-domain] Cd Length: 220 Bit Score: 38.29 E-value: 3.35e-03
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| EndIII_4Fe-2S | pfam10576 | Iron-sulfur binding domain of endonuclease III; Escherichia coli endonuclease III (EC 4.2.99. ... |
191-207 | 4.08e-03 | ||||||
Iron-sulfur binding domain of endonuclease III; Escherichia coli endonuclease III (EC 4.2.99.18) is a DNA repair enzyme that acts both as a DNA N-glycosylase, removing oxidized pyrimidines from DNA, and as an apurinic/apyrimidinic (AP) endonuclease, introducing a single-strand nick at the site from which the damaged base was removed. Endonuclease III is an iron-sulfur protein that binds a single 4Fe-4S cluster. The 4Fe-4S cluster does not seem to be important for catalytic activity, but is probably involved in the proper positioning of the enzyme along the DNA strand. The 4Fe-4S cluster is bound by four cysteines which are all located in a 17 amino acid region at the C-terminal end of endonuclease III. A similar region is also present in the central section of mutY and in the C-terminus of ORF-10 and of the Micro-coccus UV endonuclease. Pssm-ID: 463153 [Multi-domain] Cd Length: 17 Bit Score: 34.28 E-value: 4.08e-03
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| MutT | COG0494 | 8-oxo-dGTP pyrophosphatase MutT and related house-cleaning NTP pyrophosphohydrolases, NUDIX ... |
236-326 | 6.15e-03 | ||||||
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: 36.55 E-value: 6.15e-03
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| NUDIX_Hydrolase | cd04697 | uncharacterized NUDIX hydrolase subfamily; NUDIX hydrolase is a superfamily of enzymes found ... |
227-289 | 7.73e-03 | ||||||
uncharacterized NUDIX hydrolase subfamily; NUDIX hydrolase is a superfamily of enzymes found in all three kingdoms of life, and it catalyzes the hydrolysis of NUcleoside DIphosphates linked to other moieties, X. Enzymes belonging to this superfamily require a divalent cation, such as Mg2+ or Mn2+ for their activity. Members of this family 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. Substrates of NUDIX hydrolase include intact and oxidatively damaged nucleoside triphosphates, dinucleoside polyphosphates, nucleotide-sugars and dinucleotide enzymes. These substrates are metabolites or cell signaling molecules that require regulation during different stages of the cell cycle or during periods of stress. In general, the role of the NUDIX hydrolase is to sanitize the nucleotide pools and to maintain cell viability, thereby serving as surveillance and "house-cleaning" enzymes. Substrate specificity is used to define child families within the superfamily. Differences in substrate specificity are determined by the N-terminal extension or by residues in variable loop regions. Mechanistically, substrate hydrolysis occurs by a nucleophilic substitution reaction, with variation in the numbers and roles of divalent cations required. This superfamily consists of at least nine families: IPP (isopentenyl diphosphate) isomerase, ADP ribose pyrophosphatase, mutT pyrophosphohydrolase, coenzyme-A pyrophosphatase, MTH1-7,8-dihydro-8-oxoguanine-triphosphatase, diadenosine tetraphosphate hydrolase, NADH pyrophosphatase, GDP-mannose hydrolase and the c-terminal portion of the mutY adenine glycosylase. Pssm-ID: 467578 [Multi-domain] Cd Length: 157 Bit Score: 36.44 E-value: 7.73e-03
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