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.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22004055   1 MPEGPELHLASHFVNETCKGLVFGGCVEKSSVSRNPEVPFESSAYHISALARGKELRLTLSPLPGS-----QPPQKPLSL 75
Cdd:cd08967   1 MPEGPELHLASLFVNKMCKGLIFTGAVEKSSVSKNPEVPFACKAYTISAESRGKELRLILSPLPAAngkkeCKSQEEMRI 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 22004055  76 VFRFGMSGSFQLVPAEALPRHAHLRFYTAPPaPRLALCFVDIRRFGHWDPGG 127
Cdd:cd08967  81 VFRFGMSGSFQFTPVDEIPKHAHLRFYTKEE-PKRVLSFVDIRRFGTWQVGG 131

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]

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22004055    52 RGKELRLTLSplpgsqppqKPLsLVFRFGMSGSFQLVPA-EALPRHAHLRFYTAPpapRLALCFVDIRRFGHWDPGGEWQ 130
Cdd:TIGR00577  57 RGKYLLFELD---------DGA-LVSHLRMEGKYRLEAVpDAPDKHDHVDFLFDD---GTELRYHDPRRFGTWLLLDRGQ 123

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22004055   131 pGRGPCVLLEY------ERFRENVLRNLSdKAFDRPICEALLDQRFFNGIGNYLRAEILYRLKIPPFEKARTVleALQQC 204
Cdd:TIGR00577 124 -VENIPLLAKLgpeplsEDFTAEYLFEKL-AKSKRKIKTALLDQRLVAGIGNIYADEVLFRAGIHPERLASSL--SKEEC 199

                         170
                  ....*....|....*..
gi 22004055   205 RpspelTLSQKIKAKLQ 221
Cdd:TIGR00577 200 E-----LLHRAIKEVLR 211

N-terminal domain of metazoan Nei-like glycosylase 1 (NEIL1); This family contains the N-terminal domain of metazoan NEIL1. 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. NEIL1 recognizes the oxidized pyrimidines 2,6-diamino-4-hydroxy-5-formamidopyrimidine (FapyG) and 4,6-diamino- 5-formamidopyrimidine (FapyA), thymine glycol (Tg) and 5-hydroxyuracil (5-OHU). However, even though it has weak activity on 8-oxo-7,8-dihydroguanine (8-oxoG), it does show strong preference for the products of its further oxidation: spiroiminodihydantoin and guanidinohydantoin. In addition to this MeNeil1_N domain, enzymes belonging to this family contain a helix-two turn-helix (H2TH) domain and a zincless finger motif. This characteristic "zincless finger" motif, is a structural equivalent of the zinc finger common to other members of the Fpg/Nei family. Neil1 is one of three homologs found in eukaryotes and its lineage extends back as far as early metazoans.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22004055   1 MPEGPELHLASHFVNETCKGLVFGGCVEKSSVSRNPEVPFESSAYHISALARGKELRLTLSPLPGS-----QPPQKPLSL 75
Cdd:cd08967   1 MPEGPELHLASLFVNKMCKGLIFTGAVEKSSVSKNPEVPFACKAYTISAESRGKELRLILSPLPAAngkkeCKSQEEMRI 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 22004055  76 VFRFGMSGSFQLVPAEALPRHAHLRFYTAPPaPRLALCFVDIRRFGHWDPGG 127
Cdd:cd08967  81 VFRFGMSGSFQFTPVDEIPKHAHLRFYTKEE-PKRVLSFVDIRRFGTWQVGG 131

Formamidopyrimidine-DNA glycosylase N-terminal domain; Formamidopyrimidine-DNA glycosylase (Fpg) is a DNA repair enzyme that excises oxidized purines from damaged DNA. This family is the N-terminal domain contains eight beta-strands, forming a beta-sandwich with two alpha-helices parallel to its edges.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22004055     1 MPEGPELHLASHFVNETCKGLVfggcVEKSSVSRNPEVPFESSAYHISALA---------RGKELRLTLSplpgsqppqK 71
Cdd:pfam01149   1 MPELPEVETVRRGLRRHLVGKT----IASVEVLDDKNLRGPSPEEFAAALTgrkvtsvgrRGKYLLLELD---------S 67

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 22004055    72 PLSLVFRFGMSGSFQLVPAEALPRHAHLRFYTappAPRLALCFVDIRRFGHW 123
Cdd:pfam01149  68 GGHLVVHLGMTGWLLIKTEEWPPKHDHVRLEL---DDGRELRFTDPRRFGRV 116

Formamidopyrimidine-DNA glycosylase N-terminal domain; This entry represents the catalytic domain of DNA glycosylase/AP lyase enzymes, which are involved in base excision repair of DNA damaged by oxidation or by mutagenic agents. Most damage to bases in DNA is repaired by the base excision repair pathway. These enzymes are primarily from bacteria, and have both DNA glycosylase activity and AP lyase activity. Examples include formamidopyrimidine-DNA glycosylases (Fpg; MutM) and endonuclease VIII (Nei). Formamidopyrimidine-DNA glycosylases (Fpg, MutM) is a trifunctional DNA base excision repair enzyme that removes a wide range of oxidation-damaged bases (N-glycosylase activity; ) and cleaves both the 3'- and 5'-phosphodiester bonds of the resulting apurinic/apyrimidinic site (AP lyase activity; ). Fpg has a preference for oxidised purines, excising oxidized purine bases such as 7,8-dihydro-8-oxoguanine (8-oxoG). ITs AP (apurinic/apyrimidinic) lyase activity introduces nicks in the DNA strand, cleaving the DNA backbone by beta-delta elimination to generate a single-strand break at the site of the removed base with both 3'- and 5'-phosphates. Fpg is a monomer composed of 2 domains connected by a flexible hinge. The two DNA-binding motifs (a zinc finger and the helix-two-turns-helix motifs) suggest that the oxidized base is flipped out from double-stranded DNA in the binding mode and excised by a catalytic mechanism similar to that of bifunctional base excision repair enzymes. Fpg binds one ion of zinc at the C-terminus, which contains four conserved and essential cysteines.. Endonuclease VIII (Nei) has the same enzyme activities as Fpg above, but with a preference for oxidized pyrimidines, such as thymine glycol, 5,6-dihydrouracil and 5,6-dihydrothymine. These protein contains three structural domains: an N-terminal catalytic core domain, a central helix-two turn-helix (H2TH) module and a C-terminal zinc finger (see PDB:1K82). The N-terminal catalytic domain and the C-terminal zinc finger straddle the DNA with the long axis of the protein oriented roughly orthogonal to the helical axis of the DNA. Residues that contact DNA are located in the catalytic domain and in a beta-hairpin loop formed by the zinc finger.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22004055      2 PEGPELHLASHFVNETCKGLVFGGCVEKSS-VSRNPEvPFE---SSAYHISALARGKELRLTLSPlpgsqppqkPLSLVF 77
Cdd:smart00898   1 PELPEVETVRRGLAPALAGRTITRVEVVRPpQLRFPD-EFAaalSGRTITSVRRRGKYLLLRLLG---------GLTLVV 70

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 22004055     78 RFGMSGSFQLVPAEA-LPRHAHLRFYTAPPaprLALCFVDIRRFGHWD 124
Cdd:smart00898  71 HLGMSGSLRVVPAGTpPPKHDHVRLVLDDG---TELRFNDPRRFGAVR 115

bifunctional DNA-formamidopyrimidine glycosylase/DNA-(apurinic or apyrimidinic site) lyase;

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22004055   52 RGKELRLTLSplpgsqppqKPLSLVFRFGMSGSFQLVPAEALPR-HAHLRFYTAPpapRLALCFVDIRRFGHWDpggeWQ 130
Cdd:PRK01103  56 RGKYLLLDLD---------DGGTLISHLGMSGSLRLLPEDTPPEkHDHVDFVLDD---GTVLRYNDPRRFGAML----LT 119

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22004055  131 PgrgpcvllEYERFRENVLRNLS----DKAFD------------RPICEALLDQRFFNGIGNYLRAEILYRLKIPPFEKA 194
Cdd:PRK01103 120 P--------KGDLEAHPLLAHLGpeplSDAFDgeylaaklrkkkTAIKPALLDQTVVVGVGNIYADEALFRAGIHPERPA 191

                        170       180
                 ....*....|....*....|....*..
gi 22004055  195 RTVleALQQCRpspelTLSQKIKAKLQ 221
Cdd:PRK01103 192 GSL--SRAEAE-----RLVDAIKAVLA 211

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.

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 22004055   159 RPICEALLDQRFFNGIGNYLRAEILYRLKIPPFEKARTVleALQQCRpspelTLSQKIKAKLQ 221
Cdd:pfam06831  24 RPIKTALLDQTLVAGLGNIYADEVLFRAGIHPERLANSL--SKEECE-----LLHQAIKAVLQ 79

N-terminal domain of metazoan Nei-like glycosylase 1 (NEIL1); This family contains the N-terminal domain of metazoan NEIL1. 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. NEIL1 recognizes the oxidized pyrimidines 2,6-diamino-4-hydroxy-5-formamidopyrimidine (FapyG) and 4,6-diamino- 5-formamidopyrimidine (FapyA), thymine glycol (Tg) and 5-hydroxyuracil (5-OHU). However, even though it has weak activity on 8-oxo-7,8-dihydroguanine (8-oxoG), it does show strong preference for the products of its further oxidation: spiroiminodihydantoin and guanidinohydantoin. In addition to this MeNeil1_N domain, enzymes belonging to this family contain a helix-two turn-helix (H2TH) domain and a zincless finger motif. This characteristic "zincless finger" motif, is a structural equivalent of the zinc finger common to other members of the Fpg/Nei family. Neil1 is one of three homologs found in eukaryotes and its lineage extends back as far as early metazoans.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22004055   1 MPEGPELHLASHFVNETCKGLVFGGCVEKSSVSRNPEVPFESSAYHISALARGKELRLTLSPLPGS-----QPPQKPLSL 75
Cdd:cd08967   1 MPEGPELHLASLFVNKMCKGLIFTGAVEKSSVSKNPEVPFACKAYTISAESRGKELRLILSPLPAAngkkeCKSQEEMRI 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 22004055  76 VFRFGMSGSFQLVPAEALPRHAHLRFYTAPPaPRLALCFVDIRRFGHWDPGG 127
Cdd:cd08967  81 VFRFGMSGSFQFTPVDEIPKHAHLRFYTKEE-PKRVLSFVDIRRFGTWQVGG 131

Formamidopyrimidine-DNA glycosylase N-terminal domain; Formamidopyrimidine-DNA glycosylase (Fpg) is a DNA repair enzyme that excises oxidized purines from damaged DNA. This family is the N-terminal domain contains eight beta-strands, forming a beta-sandwich with two alpha-helices parallel to its edges.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22004055     1 MPEGPELHLASHFVNETCKGLVfggcVEKSSVSRNPEVPFESSAYHISALA---------RGKELRLTLSplpgsqppqK 71
Cdd:pfam01149   1 MPELPEVETVRRGLRRHLVGKT----IASVEVLDDKNLRGPSPEEFAAALTgrkvtsvgrRGKYLLLELD---------S 67

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 22004055    72 PLSLVFRFGMSGSFQLVPAEALPRHAHLRFYTappAPRLALCFVDIRRFGHW 123
Cdd:pfam01149  68 GGHLVVHLGMTGWLLIKTEEWPPKHDHVRLEL---DDGRELRFTDPRRFGRV 116

Formamidopyrimidine-DNA glycosylase N-terminal domain; This entry represents the catalytic domain of DNA glycosylase/AP lyase enzymes, which are involved in base excision repair of DNA damaged by oxidation or by mutagenic agents. Most damage to bases in DNA is repaired by the base excision repair pathway. These enzymes are primarily from bacteria, and have both DNA glycosylase activity and AP lyase activity. Examples include formamidopyrimidine-DNA glycosylases (Fpg; MutM) and endonuclease VIII (Nei). Formamidopyrimidine-DNA glycosylases (Fpg, MutM) is a trifunctional DNA base excision repair enzyme that removes a wide range of oxidation-damaged bases (N-glycosylase activity; ) and cleaves both the 3'- and 5'-phosphodiester bonds of the resulting apurinic/apyrimidinic site (AP lyase activity; ). Fpg has a preference for oxidised purines, excising oxidized purine bases such as 7,8-dihydro-8-oxoguanine (8-oxoG). ITs AP (apurinic/apyrimidinic) lyase activity introduces nicks in the DNA strand, cleaving the DNA backbone by beta-delta elimination to generate a single-strand break at the site of the removed base with both 3'- and 5'-phosphates. Fpg is a monomer composed of 2 domains connected by a flexible hinge. The two DNA-binding motifs (a zinc finger and the helix-two-turns-helix motifs) suggest that the oxidized base is flipped out from double-stranded DNA in the binding mode and excised by a catalytic mechanism similar to that of bifunctional base excision repair enzymes. Fpg binds one ion of zinc at the C-terminus, which contains four conserved and essential cysteines.. Endonuclease VIII (Nei) has the same enzyme activities as Fpg above, but with a preference for oxidized pyrimidines, such as thymine glycol, 5,6-dihydrouracil and 5,6-dihydrothymine. These protein contains three structural domains: an N-terminal catalytic core domain, a central helix-two turn-helix (H2TH) module and a C-terminal zinc finger (see PDB:1K82). The N-terminal catalytic domain and the C-terminal zinc finger straddle the DNA with the long axis of the protein oriented roughly orthogonal to the helical axis of the DNA. Residues that contact DNA are located in the catalytic domain and in a beta-hairpin loop formed by the zinc finger.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22004055      2 PEGPELHLASHFVNETCKGLVFGGCVEKSS-VSRNPEvPFE---SSAYHISALARGKELRLTLSPlpgsqppqkPLSLVF 77
Cdd:smart00898   1 PELPEVETVRRGLAPALAGRTITRVEVVRPpQLRFPD-EFAaalSGRTITSVRRRGKYLLLRLLG---------GLTLVV 70

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 22004055     78 RFGMSGSFQLVPAEA-LPRHAHLRFYTAPPaprLALCFVDIRRFGHWD 124
Cdd:smart00898  71 HLGMSGSLRVVPAGTpPPKHDHVRLVLDDG---TELRFNDPRRFGAVR 115

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]

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22004055    52 RGKELRLTLSplpgsqppqKPLsLVFRFGMSGSFQLVPA-EALPRHAHLRFYTAPpapRLALCFVDIRRFGHWDPGGEWQ 130
Cdd:TIGR00577  57 RGKYLLFELD---------DGA-LVSHLRMEGKYRLEAVpDAPDKHDHVDFLFDD---GTELRYHDPRRFGTWLLLDRGQ 123

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22004055   131 pGRGPCVLLEY------ERFRENVLRNLSdKAFDRPICEALLDQRFFNGIGNYLRAEILYRLKIPPFEKARTVleALQQC 204
Cdd:TIGR00577 124 -VENIPLLAKLgpeplsEDFTAEYLFEKL-AKSKRKIKTALLDQRLVAGIGNIYADEVLFRAGIHPERLASSL--SKEEC 199

                         170
                  ....*....|....*..
gi 22004055   205 RpspelTLSQKIKAKLQ 221
Cdd:TIGR00577 200 E-----LLHRAIKEVLR 211

N-terminal domain of Escherichia coli Fpg1/MutM and related bacterial DNA glycosylases; This family contains the N-terminal domain of Escherichia coli Fpg1/MutM and related bacterial DNA glycosylases. 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. Escherichia coli Fpg mainly recognizes and excises damaged purines such as 8-oxo-7,8-dihydroguanine (8-oxoG) and 2,6-diamino-4-hydroxy-5-formamidopyrimidine (FapyG). It is bifunctional, having both a DNA glycosylase (recognition activity) and a AP lyase activity. In addition to this EcFpg-like_N domain, enzymes belonging to this family contain a helix-two turn-helix (H2TH) domain and a zinc-finger motif, which also contribute residues to the active site.

                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 22004055  52 RGKELRLTLSPlpgsqppqkPLSLVFRFGMSGSFQLVPAEA-LPRHAHLRFYTAPPAprlALCFVDIRRFGHWD 124
Cdd:cd08966  56 RGKYLLFELDD---------GLVLVIHLGMTGRLLVVPPDEpPEKHDHVIFELDDGR---ELRFNDPRRFGTLL 117

formamidopyrimidine-DNA glycosylase; Provisional

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22004055    1 MPEGPELhlashfvnET-CKGL---VFGGCVEKSSVSRNPEV--PFESSAYhISALA---------RGKELRLTLSPLPG 65
Cdd:PRK13945   1 MPELPEV--------ETvRRGLeqlLLNFIIKGVEVLLERTIasPGGVEEF-IKGLKgsligqwqrRGKYLLASLKKEGS 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22004055   66 SQPPqkplSLVFRFGMSGSFQLV-PAEALPRHAHLRFYTAPPAprlALCFVDIRRFGH--WDPggewqPGRGPcvlleye 142
Cdd:PRK13945  72 ENAG----WLGVHLRMTGQFLWVeQSTPPCKHTRVRLFFEKNQ---ELRFVDIRSFGQmwWVP-----PGVSP------- 132

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22004055  143 rfrENVLRNLS-------DKAFD------------RPICEALLDQRFFNGIGNYLRAEILYRLKIPPFEKARTV-LEALQ 202
Cdd:PRK13945 133 ---ESIITGLQklgpepfSPEFSveylkkklkkrtRSIKTALLDQSIVAGIGNIYADESLFKAGIHPTTPAGQLkKKQLE 209

                 ....*
gi 22004055  203 QCRPS 207
Cdd:PRK13945 210 RLREA 214

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.

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 22004055   159 RPICEALLDQRFFNGIGNYLRAEILYRLKIPPFEKARTVleALQQCRpspelTLSQKIKAKLQ 221
Cdd:pfam06831  24 RPIKTALLDQTLVAGLGNIYADEVLFRAGIHPERLANSL--SKEECE-----LLHQAIKAVLQ 79