N-terminal domain of the plant and fungal Nei and related proteins; This family contains the N-terminal domain of plant and Fungi Nei and related proteins. 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. The plant and fungal FpgNei glycosylases prefer the oxidized pyrimidines spiroiminodihydantoin (Sp), guanidinohydantoin (Gh) over 8-oxoguanine in double stranded oligonucleotides and also show weak activity on single stranded DNA. In addition to this domain, enzymes belonging to this family contain a helix-two turn-helix (H2TH) domain and a characteristic zincless finger motif. They share a common ancestor not shared with other eukaryotic members of the FpgNei family.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 996646464   1 MPEIAE-------------GKKIAKVSAPDDANVFGKVGTSgpAFEKAVKGRKVVSVGSQGKYFWVTFDK-PPHAVMHLG 66
Cdd:cd08972    1 MPELPEverarrlleehclGKKITKVDAQDDDKVFGGVTPG--AFQKALLGRTITSAHRKGKYFWLTLDGdAPVPVMHFG 78

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 996646464  67 MTGWIHIKGDKTAYTNYYKKMKEGEADiWPPKYWKFHIETEgtPKVSAAFTDPRRFGRIRLV 128
Cdd:cd08972   79 MTGAISIKGVKTIYYKMLRPPKEEDQT-WPPRFYKFVLTLE--DGTELAFTDPRRLGRVRLV 137

N-terminal domain of the plant and fungal Nei and related proteins; This family contains the N-terminal domain of plant and Fungi Nei and related proteins. 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. The plant and fungal FpgNei glycosylases prefer the oxidized pyrimidines spiroiminodihydantoin (Sp), guanidinohydantoin (Gh) over 8-oxoguanine in double stranded oligonucleotides and also show weak activity on single stranded DNA. In addition to this domain, enzymes belonging to this family contain a helix-two turn-helix (H2TH) domain and a characteristic zincless finger motif. They share a common ancestor not shared with other eukaryotic members of the FpgNei family.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 996646464   1 MPEIAE-------------GKKIAKVSAPDDANVFGKVGTSgpAFEKAVKGRKVVSVGSQGKYFWVTFDK-PPHAVMHLG 66
Cdd:cd08972    1 MPELPEverarrlleehclGKKITKVDAQDDDKVFGGVTPG--AFQKALLGRTITSAHRKGKYFWLTLDGdAPVPVMHFG 78

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 996646464  67 MTGWIHIKGDKTAYTNYYKKMKEGEADiWPPKYWKFHIETEgtPKVSAAFTDPRRFGRIRLV 128
Cdd:cd08972   79 MTGAISIKGVKTIYYKMLRPPKEEDQT-WPPRFYKFVLTLE--DGTELAFTDPRRLGRVRLV 137

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 996646464    7 GKKIAKVSAPDDANVfgKVGTSGPAFEKAVKGRKVVSVGSQGKYFWVTFDKPpHAVMHLGMTGwihikgdktaytnyykK 86
Cdd:TIGR00577  19 GKTIKSVEVVLRNPV--LRPAGSEDLQKRLLGQTILSIQRRGKYLLFELDDG-ALVSHLRMEG----------------K 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 996646464   87 MKEGEADIWPPKYWKFHIETEGTPKVSaaFTDPRRFGRIRLVDCPGADIrsHSPLKENGPDPvvDVDIFTETYLRQKMQS 166
Cdd:TIGR00577  80 YRLEAVPDAPDKHDHVDFLFDDGTELR--YHDPRRFGTWLLLDRGQVEN--IPLLAKLGPEP--LSEDFTAEYLFEKLAK 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 996646464  167 RHVPVKALLLDQSHISGIGNWVADEVLYQSRLHPEQYCDTFNEGEMKKLYEAVRYVCQTAVDKLGDSdefpddwLFNYRW 246
Cdd:TIGR00577 154 SKRKIKTALLDQRLVAGIGNIYADEVLFRAGIHPERLASSLSKEECELLHRAIKEVLRKAIEMGGTT-------IRDFSQ 226

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 996646464  247 GKGSkgaaselpNGEKLAFITVGGR-----TSCYAPGRQKKTGQ 285
Cdd:TIGR00577 227 SDGH--------NGYFQQELQVYGRkgepcRRCGTTIEKEKVGG 262

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

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 996646464   1 MPEIAE-------------GKKIAKVSAPDDANVFgkvgTSGPAFEKAVKGRKVVSVGSQGKYFWVTFDKPPHAVMHLGM 67
Cdd:PRK01103   1 MPELPEvetvrrglephlvGKTITRVEVRRPKLRW----PVPEDFAERLSGQTILAVGRRGKYLLLDLDDGGTLISHLGM 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 996646464  68 TGwihikgdktaytnyykKMKEGEADIWPPKYwkFHIE---TEGTpkvSAAFTDPRRFGRIRLvdCPGADIRSHSPLKEN 144
Cdd:PRK01103  77 SG----------------SLRLLPEDTPPEKH--DHVDfvlDDGT---VLRYNDPRRFGAMLL--TPKGDLEAHPLLAHL 133

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 996646464 145 GPDPVVDVdiFTETYLRQKMQSRHVPVKALLLDQSHISGIGNWVADEVLYQSRLHPEQYCDTFNEGEMKKLYEAVRYVCQ 224
Cdd:PRK01103 134 GPEPLSDA--FDGEYLAAKLRKKKTAIKPALLDQTVVVGVGNIYADEALFRAGIHPERPAGSLSRAEAERLVDAIKAVLA 211

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 996646464 225 TAVDKLGDSdefpddwLFNYRWGKGSKGA-ASEL----------PN-GEKLAFITVGGRTSCYAPGRQKK 282
Cdd:PRK01103 212 EAIEQGGTT-------LRDYVNADGKPGYfQQSLqvygregepcRRcGTPIEKIKQGGRSTFFCPRCQKR 274

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 996646464     6 EGKKIAKVSApddanVFGKVGTSGPAFEKAVKGRKVVSVGSQGKYFWVTFDKPPHAVMHLGMTGWIHIKgdktaytnyyk 85
Cdd:smart00898  18 AGRTITRVEV-----VRPPQLRFPDEFAAALSGRTITSVRRRGKYLLLRLLGGLTLVVHLGMSGSLRVV----------- 81

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 996646464    86 kmkegEADIWPPKYWKFHIETEGTPKVsaAFTDPRRFGRIR 126
Cdd:smart00898  82 -----PAGTPPPKHDHVRLVLDDGTEL--RFNDPRRFGAVR 115

N-terminal domain of the plant and fungal Nei and related proteins; This family contains the N-terminal domain of plant and Fungi Nei and related proteins. 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. The plant and fungal FpgNei glycosylases prefer the oxidized pyrimidines spiroiminodihydantoin (Sp), guanidinohydantoin (Gh) over 8-oxoguanine in double stranded oligonucleotides and also show weak activity on single stranded DNA. In addition to this domain, enzymes belonging to this family contain a helix-two turn-helix (H2TH) domain and a characteristic zincless finger motif. They share a common ancestor not shared with other eukaryotic members of the FpgNei family.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 996646464   1 MPEIAE-------------GKKIAKVSAPDDANVFGKVGTSgpAFEKAVKGRKVVSVGSQGKYFWVTFDK-PPHAVMHLG 66
Cdd:cd08972    1 MPELPEverarrlleehclGKKITKVDAQDDDKVFGGVTPG--AFQKALLGRTITSAHRKGKYFWLTLDGdAPVPVMHFG 78

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 996646464  67 MTGWIHIKGDKTAYTNYYKKMKEGEADiWPPKYWKFHIETEgtPKVSAAFTDPRRFGRIRLV 128
Cdd:cd08972   79 MTGAISIKGVKTIYYKMLRPPKEEDQT-WPPRFYKFVLTLE--DGTELAFTDPRRLGRVRLV 137

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 996646464    7 GKKIAKVSAPDDANVfgKVGTSGPAFEKAVKGRKVVSVGSQGKYFWVTFDKPpHAVMHLGMTGwihikgdktaytnyykK 86
Cdd:TIGR00577  19 GKTIKSVEVVLRNPV--LRPAGSEDLQKRLLGQTILSIQRRGKYLLFELDDG-ALVSHLRMEG----------------K 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 996646464   87 MKEGEADIWPPKYWKFHIETEGTPKVSaaFTDPRRFGRIRLVDCPGADIrsHSPLKENGPDPvvDVDIFTETYLRQKMQS 166
Cdd:TIGR00577  80 YRLEAVPDAPDKHDHVDFLFDDGTELR--YHDPRRFGTWLLLDRGQVEN--IPLLAKLGPEP--LSEDFTAEYLFEKLAK 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 996646464  167 RHVPVKALLLDQSHISGIGNWVADEVLYQSRLHPEQYCDTFNEGEMKKLYEAVRYVCQTAVDKLGDSdefpddwLFNYRW 246
Cdd:TIGR00577 154 SKRKIKTALLDQRLVAGIGNIYADEVLFRAGIHPERLASSLSKEECELLHRAIKEVLRKAIEMGGTT-------IRDFSQ 226

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 996646464  247 GKGSkgaaselpNGEKLAFITVGGR-----TSCYAPGRQKKTGQ 285
Cdd:TIGR00577 227 SDGH--------NGYFQQELQVYGRkgepcRRCGTTIEKEKVGG 262

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

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 996646464   1 MPEIAE-------------GKKIAKVSAPDDANVFgkvgTSGPAFEKAVKGRKVVSVGSQGKYFWVTFDKPPHAVMHLGM 67
Cdd:PRK01103   1 MPELPEvetvrrglephlvGKTITRVEVRRPKLRW----PVPEDFAERLSGQTILAVGRRGKYLLLDLDDGGTLISHLGM 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 996646464  68 TGwihikgdktaytnyykKMKEGEADIWPPKYwkFHIE---TEGTpkvSAAFTDPRRFGRIRLvdCPGADIRSHSPLKEN 144
Cdd:PRK01103  77 SG----------------SLRLLPEDTPPEKH--DHVDfvlDDGT---VLRYNDPRRFGAMLL--TPKGDLEAHPLLAHL 133

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 996646464 145 GPDPVVDVdiFTETYLRQKMQSRHVPVKALLLDQSHISGIGNWVADEVLYQSRLHPEQYCDTFNEGEMKKLYEAVRYVCQ 224
Cdd:PRK01103 134 GPEPLSDA--FDGEYLAAKLRKKKTAIKPALLDQTVVVGVGNIYADEALFRAGIHPERPAGSLSRAEAERLVDAIKAVLA 211

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 996646464 225 TAVDKLGDSdefpddwLFNYRWGKGSKGA-ASEL----------PN-GEKLAFITVGGRTSCYAPGRQKK 282
Cdd:PRK01103 212 EAIEQGGTT-------LRDYVNADGKPGYfQQSLqvygregepcRRcGTPIEKIKQGGRSTFFCPRCQKR 274

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        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 996646464  145 GPDPvvDVDIFTETYLRQKMQSRHVPVKALLLDQSHISGIGNWVADEVLYQSRLHPEQYCDTFNEGEMKKLYEAVRYVCQ 224
Cdd:pfam06831   2 GPEP--LSEDFTVDYFAERLAKKKRPIKTALLDQTLVAGLGNIYADEVLFRAGIHPERLANSLSKEECELLHQAIKAVLQ 79

                  ....*....
gi 996646464  225 TAVDKLGDS 233
Cdd:pfam06831  80 EAIEMGGGG 88

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 996646464     6 EGKKIAKVSApddanVFGKVGTSGPAFEKAVKGRKVVSVGSQGKYFWVTFDKPPHAVMHLGMTGWIHIKgdktaytnyyk 85
Cdd:smart00898  18 AGRTITRVEV-----VRPPQLRFPDEFAAALSGRTITSVRRRGKYLLLRLLGGLTLVVHLGMSGSLRVV----------- 81

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 996646464    86 kmkegEADIWPPKYWKFHIETEGTPKVsaAFTDPRRFGRIR 126
Cdd:smart00898  82 -----PAGTPPPKHDHVRLVLDDGTEL--RFNDPRRFGAVR 115

formamidopyrimidine-DNA glycosylase; Provisional

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 996646464   1 MPEIAEGKKIAKVSAPDDANV------FGKV----GTSGPAFEKAVKGRKVVSVGSQGKYFWVTFDKP----PHAVMHLG 66
Cdd:PRK14810   1 MPELPEVETVARGLAPRAAGRriataeFRNLriprKGDPDLMAARLAGRKILSVKRVGKHIVADLEGPgeprGQWIIHLG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 996646464  67 MTGwihikgdktaytnyykKMKEGEADIWPPKYwkfhieTEGTPKVSAA----FTDPRRFGRIrlvdcpGADIRSHSPLK 142
Cdd:PRK14810  81 MTG----------------KLLLGGPDTPSPKH------THAVLTLSSGkelrFVDSRQFGCI------EYSEAFPKRFA 132

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 996646464 143 ENGPDPV-VDVDIFTETYLRqkmqsRHVPVKALLLDQSHISGIGNWVADEVLYQSRLHPEQYCDTFNEGEMKKLYEAVRY 221
Cdd:PRK14810 133 RPGPEPLeISFEDFAALFRG-----RKTRIKSALLNQTLLRGVGNIYADEALFRAGIRPQRLASSLSRERLRKLHDAIGE 207

                        250
                 ....*....|..
gi 996646464 222 VCQTAVDKLGDS 233
Cdd:PRK14810 208 VLREAIELGGSS 219

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_4 domain, most enzymes belonging to this family contain a helix-two turn-helix (H2TH) domain and a zinc-finger motif.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 996646464   7 GKKIAKVSAPDDanvfgKVGTSGPA-FEKAVKGRKVVSVGSQGKYFWVTFDKPPHAVMHLGMTGWIHikgdktaytnYYK 85
Cdd:cd08976   19 HRKIVEVEVGDD-----KILGEPKAtLREVLEGRTFTETHRIGKYLFLKTKEGGWLVMHFGMTGKLD----------YYP 83

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 996646464  86 kmkegeADIWPPKYWKFHIETEGTPKVsaAFTDPRRFGRIRL 127
Cdd:cd08976   84 ------DDEDPPKHARLLLHFEDGFRL--AFECPRKFGRVRL 117

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_1 domain, enzymes belonging to this family contain a helix-two turn-helix (H2TH) domain and a zinc-finger motif.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 996646464   1 MPEIAE-------------GKKIAKVS-APDDANVfgkvgTSGPaFEKAVKGRKVVSVGSQGKYFWVTFDKPPHAVMHLG 66
Cdd:cd08973    1 MPELPEvevyaenlerrltGKTITRVElASKSLLV-----TPDP-PLEALEGRTVTGVRRHGKRLDFEFDNGLHLVLHLM 74

                 ....*....
gi 996646464  67 MTGWIHIKG 75
Cdd:cd08973   75 LAGWLYWTE 83