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endonuclease 8-like 2 isoform a [Homo sapiens]
MeNeil2_N and Nei domain-containing protein( domain architecture ID 12963208)
MeNeil2_N and Nei domain-containing protein
List of domain hits
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Name | Accession | Description | Interval | E-value | ||||
MeNeil2_N | cd08968 | N-terminal domain of metazoan Nei-like glycosylase 2 (NEIL2); This family contains the ... |
1-185 | 9.59e-73 | ||||
N-terminal domain of metazoan Nei-like glycosylase 2 (NEIL2); This family contains the N-terminal domain of the metazoan protein Neil2. It belongs to the FpgNei_N, [N-terminal domain of Fpg (formamidopyrimidine-DNA glycosylase, MutM)_Nei (endonuclease VIII)] domain superfamily. DNA glycosylases maintain genome integrity by recognizing base lesions created by ionizing radiation, alkylating or oxidizing agents, and endogenous reactive oxygen species. They initiate the base-excision repair process, which is completed with the help of enzymes such as phosphodiesterases, AP endonucleases, DNA polymerases and DNA ligases. DNA glycosylases cleave the N-glycosyl bond between the sugar and the damaged base, creating an AP (apurinic/apyrimidinic) site. Most FpgNei DNA glycosylases use their N-terminal proline residue as the key catalytic nucleophile, and the reaction proceeds via a Schiff base intermediate. NEIL2 repairs 5-hydroxyuracil (5-OHU) and other oxidized derivatives of cytosine, but it shows preference for DNA bubble structures. In addition to this MeNeil2_N domain, NEIL2 contains a helix-two turn-helix (H2TH) domain and a characteristic CHCC zinc finger motif. Neil2 is one of three homologs found in eukaryotes. : Pssm-ID: 176802 Cd Length: 126 Bit Score: 220.79 E-value: 9.59e-73
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Nei super family | cl33822 | Formamidopyrimidine-DNA glycosylase [Replication, recombination and repair]; |
126-320 | 1.73e-21 | ||||
Formamidopyrimidine-DNA glycosylase [Replication, recombination and repair]; The actual alignment was detected with superfamily member COG0266: Pssm-ID: 440036 [Multi-domain] Cd Length: 272 Bit Score: 92.11 E-value: 1.73e-21
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Name | Accession | Description | Interval | E-value | ||||
MeNeil2_N | cd08968 | N-terminal domain of metazoan Nei-like glycosylase 2 (NEIL2); This family contains the ... |
1-185 | 9.59e-73 | ||||
N-terminal domain of metazoan Nei-like glycosylase 2 (NEIL2); This family contains the N-terminal domain of the metazoan protein Neil2. It belongs to the FpgNei_N, [N-terminal domain of Fpg (formamidopyrimidine-DNA glycosylase, MutM)_Nei (endonuclease VIII)] domain superfamily. DNA glycosylases maintain genome integrity by recognizing base lesions created by ionizing radiation, alkylating or oxidizing agents, and endogenous reactive oxygen species. They initiate the base-excision repair process, which is completed with the help of enzymes such as phosphodiesterases, AP endonucleases, DNA polymerases and DNA ligases. DNA glycosylases cleave the N-glycosyl bond between the sugar and the damaged base, creating an AP (apurinic/apyrimidinic) site. Most FpgNei DNA glycosylases use their N-terminal proline residue as the key catalytic nucleophile, and the reaction proceeds via a Schiff base intermediate. NEIL2 repairs 5-hydroxyuracil (5-OHU) and other oxidized derivatives of cytosine, but it shows preference for DNA bubble structures. In addition to this MeNeil2_N domain, NEIL2 contains a helix-two turn-helix (H2TH) domain and a characteristic CHCC zinc finger motif. Neil2 is one of three homologs found in eukaryotes. Pssm-ID: 176802 Cd Length: 126 Bit Score: 220.79 E-value: 9.59e-73
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Nei | COG0266 | Formamidopyrimidine-DNA glycosylase [Replication, recombination and repair]; |
126-320 | 1.73e-21 | ||||
Formamidopyrimidine-DNA glycosylase [Replication, recombination and repair]; Pssm-ID: 440036 [Multi-domain] Cd Length: 272 Bit Score: 92.11 E-value: 1.73e-21
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PRK01103 | PRK01103 | bifunctional DNA-formamidopyrimidine glycosylase/DNA-(apurinic or apyrimidinic site) lyase; |
219-321 | 4.81e-17 | ||||
bifunctional DNA-formamidopyrimidine glycosylase/DNA-(apurinic or apyrimidinic site) lyase; Pssm-ID: 234899 [Multi-domain] Cd Length: 274 Bit Score: 79.74 E-value: 4.81e-17
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fpg | TIGR00577 | DNA-formamidopyrimidine glycosylase; All proteins in the FPG family with known functions are ... |
220-319 | 8.03e-15 | ||||
DNA-formamidopyrimidine glycosylase; All proteins in the FPG family with known functions are FAPY-DNA glycosylases that function in base excision repair. Homologous to endonuclease VIII (nei). This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair] Pssm-ID: 273150 [Multi-domain] Cd Length: 272 Bit Score: 73.49 E-value: 8.03e-15
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H2TH | pfam06831 | Formamidopyrimidine-DNA glycosylase H2TH domain; Formamidopyrimidine-DNA glycosylase (Fpg) is ... |
220-266 | 9.83e-12 | ||||
Formamidopyrimidine-DNA glycosylase H2TH domain; Formamidopyrimidine-DNA glycosylase (Fpg) is a DNA repair enzyme that excises oxidized purines from damaged DNA. This family is the central domain containing the DNA-binding helix-two turn-helix domain. Pssm-ID: 399664 [Multi-domain] Cd Length: 89 Bit Score: 60.38 E-value: 9.83e-12
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Name | Accession | Description | Interval | E-value | ||||
MeNeil2_N | cd08968 | N-terminal domain of metazoan Nei-like glycosylase 2 (NEIL2); This family contains the ... |
1-185 | 9.59e-73 | ||||
N-terminal domain of metazoan Nei-like glycosylase 2 (NEIL2); This family contains the N-terminal domain of the metazoan protein Neil2. It belongs to the FpgNei_N, [N-terminal domain of Fpg (formamidopyrimidine-DNA glycosylase, MutM)_Nei (endonuclease VIII)] domain superfamily. DNA glycosylases maintain genome integrity by recognizing base lesions created by ionizing radiation, alkylating or oxidizing agents, and endogenous reactive oxygen species. They initiate the base-excision repair process, which is completed with the help of enzymes such as phosphodiesterases, AP endonucleases, DNA polymerases and DNA ligases. DNA glycosylases cleave the N-glycosyl bond between the sugar and the damaged base, creating an AP (apurinic/apyrimidinic) site. Most FpgNei DNA glycosylases use their N-terminal proline residue as the key catalytic nucleophile, and the reaction proceeds via a Schiff base intermediate. NEIL2 repairs 5-hydroxyuracil (5-OHU) and other oxidized derivatives of cytosine, but it shows preference for DNA bubble structures. In addition to this MeNeil2_N domain, NEIL2 contains a helix-two turn-helix (H2TH) domain and a characteristic CHCC zinc finger motif. Neil2 is one of three homologs found in eukaryotes. Pssm-ID: 176802 Cd Length: 126 Bit Score: 220.79 E-value: 9.59e-73
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Nei | COG0266 | Formamidopyrimidine-DNA glycosylase [Replication, recombination and repair]; |
126-320 | 1.73e-21 | ||||
Formamidopyrimidine-DNA glycosylase [Replication, recombination and repair]; Pssm-ID: 440036 [Multi-domain] Cd Length: 272 Bit Score: 92.11 E-value: 1.73e-21
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PRK01103 | PRK01103 | bifunctional DNA-formamidopyrimidine glycosylase/DNA-(apurinic or apyrimidinic site) lyase; |
219-321 | 4.81e-17 | ||||
bifunctional DNA-formamidopyrimidine glycosylase/DNA-(apurinic or apyrimidinic site) lyase; Pssm-ID: 234899 [Multi-domain] Cd Length: 274 Bit Score: 79.74 E-value: 4.81e-17
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fpg | TIGR00577 | DNA-formamidopyrimidine glycosylase; All proteins in the FPG family with known functions are ... |
220-319 | 8.03e-15 | ||||
DNA-formamidopyrimidine glycosylase; All proteins in the FPG family with known functions are FAPY-DNA glycosylases that function in base excision repair. Homologous to endonuclease VIII (nei). This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair] Pssm-ID: 273150 [Multi-domain] Cd Length: 272 Bit Score: 73.49 E-value: 8.03e-15
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H2TH | pfam06831 | Formamidopyrimidine-DNA glycosylase H2TH domain; Formamidopyrimidine-DNA glycosylase (Fpg) is ... |
220-266 | 9.83e-12 | ||||
Formamidopyrimidine-DNA glycosylase H2TH domain; Formamidopyrimidine-DNA glycosylase (Fpg) is a DNA repair enzyme that excises oxidized purines from damaged DNA. This family is the central domain containing the DNA-binding helix-two turn-helix domain. Pssm-ID: 399664 [Multi-domain] Cd Length: 89 Bit Score: 60.38 E-value: 9.83e-12
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FpgNei_N | cd08773 | N-terminal domain of Fpg (formamidopyrimidine-DNA glycosylase, MutM)_Nei (endonuclease VIII) ... |
2-179 | 2.75e-10 | ||||
N-terminal domain of Fpg (formamidopyrimidine-DNA glycosylase, MutM)_Nei (endonuclease VIII) base-excision repair DNA glycosylases; DNA glycosylases maintain genome integrity by recognizing base lesions created by ionizing radiation, alkylating or oxidizing agents, and endogenous reactive oxygen species. These enzymes initiate the base-excision repair process, which is completed with the help of enzymes such as phosphodiesterases, AP endonucleases, DNA polymerases and DNA ligases. DNA glycolsylases cleave the N-glycosyl bond between the sugar and the damaged base, creating an AP (apurinic/apyrimidinic) site. The FpgNei DNA glycosylases represent one of the two structural superfamilies of DNA glycosylases that recognize oxidized bases (the other is the HTH-GPD superfamily exemplified by Escherichia coli Nth). Most FpgNei DNA glycosylases use their N-terminal proline residue as the key catalytic nucleophile, and the reaction proceeds via a Schiff base intermediate. One exception is mouse Nei-like glycosylase 3 (Neil3) which forms a Schiff base intermediate via its N-terminal valine. In addition to this FpgNei_N domain, FpgNei proteins have a helix-two-turn-helix (H2TH) domain and a zinc (or zincless)-finger motif which also contribute residues to the active site. FpgNei DNA glycosylases have a broad substrate specificity. They are bifunctional, in addition to the glycosylase (recognition) activity, they have a lyase (cleaving) activity on the phosphodiester backbone of the DNA at the AP site. This superfamily includes eukaryotic, bacterial, and viral proteins. Pssm-ID: 176798 Cd Length: 117 Bit Score: 56.99 E-value: 2.75e-10
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PRK14811 | PRK14811 | formamidopyrimidine-DNA glycosylase; Provisional |
197-320 | 1.30e-09 | ||||
formamidopyrimidine-DNA glycosylase; Provisional Pssm-ID: 184831 [Multi-domain] Cd Length: 269 Bit Score: 57.88 E-value: 1.30e-09
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PRK13945 | PRK13945 | formamidopyrimidine-DNA glycosylase; Provisional |
220-320 | 2.24e-07 | ||||
formamidopyrimidine-DNA glycosylase; Provisional Pssm-ID: 184410 [Multi-domain] Cd Length: 282 Bit Score: 51.47 E-value: 2.24e-07
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PRK14810 | PRK14810 | formamidopyrimidine-DNA glycosylase; Provisional |
123-319 | 2.85e-07 | ||||
formamidopyrimidine-DNA glycosylase; Provisional Pssm-ID: 173271 [Multi-domain] Cd Length: 272 Bit Score: 51.06 E-value: 2.85e-07
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PRK10445 | PRK10445 | endonuclease VIII; Provisional |
196-320 | 1.09e-05 | ||||
endonuclease VIII; Provisional Pssm-ID: 182467 [Multi-domain] Cd Length: 263 Bit Score: 46.18 E-value: 1.09e-05
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BaFpgNei_N_2 | cd08974 | Uncharacterized bacterial subgroup of the N-terminal domain of Fpg (formamidopyrimidine-DNA ... |
131-182 | 9.02e-03 | ||||
Uncharacterized bacterial subgroup of the N-terminal domain of Fpg (formamidopyrimidine-DNA glycosylase, MutM)_Nei (endonuclease VIII) base-excision repair DNA glycosylases; This family is an uncharacterized bacterial subgroup of the FpgNei_N domain superfamily. DNA glycosylases maintain genome integrity by recognizing base lesions created by ionizing radiation, alkylating or oxidizing agents, and endogenous reactive oxygen species. They initiate the base-excision repair process, which is completed with the help of enzymes such as phosphodiesterases, AP endonucleases, DNA polymerases and DNA ligases. DNA glycosylases cleave the N-glycosyl bond between the sugar and the damaged base, creating an AP (apurinic/apyrimidinic) site. Most FpgNei DNA glycosylases use their N-terminal proline residue as the key catalytic nucleophile, and the reaction proceeds via a Schiff base intermediate. This N-terminal proline is conserved in this family. Escherichia coli Fpg prefers 8-oxo-7,8-dihydroguanine (8-oxoG) and oxidized purines, and Escherichia coli Nei recognizes oxidized pyrimidines. However, neither Escherichia coli Fpg or Nei belong to this family. In addition to this BaFpgNei_N_2 domain, enzymes belonging to this family contain a helix-two turn-helix (H2TH) domain. Most also contain a zinc-finger motif. Pssm-ID: 176808 Cd Length: 98 Bit Score: 35.38 E-value: 9.02e-03
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Blast search parameters | ||||
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