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Conserved domains on  [gi|1935828150|gb|QPH73631|]
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uracil-DNA glycosylase [Neisseria meningitidis]

Protein Classification

uracil-DNA glycosylase( domain architecture ID 10786350)

uracil-DNA glycosylase (UDG) excises uracil residues from the DNA which can arise as a result of misincorporation of dUMP residues by DNA polymerase or due to deamination of cytosine

CATH:  3.40.470.10
EC:  3.2.2.27
Gene Ontology:  GO:0004844|GO:0006281|GO:0006284
PubMed:  11716455|10946227|25550433

Graphical summary

 Zoom to residue level

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List of domain hits

 Name Accession Description Interval E-value
Ung COG0692
Uracil-DNA glycosylase [Replication, recombination and repair];
1-217 6.64e-156

Uracil-DNA glycosylase [Replication, recombination and repair];


:

Pssm-ID: 440456  Cd Length: 221  Bit Score: 430.23  E-value: 6.64e-156
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935828150   1 MDTWHDALGGEKQQPYFQEILNAVRQERLSGQIIYPPAADVFNAFRLTAFDRVKAVILGQDPYHGAGQAHGLAFSVRQGI 80
Cdd:COG0692     6 EPSWKEALAEEFEKPYFQALGAFLKAEYAAGKTIYPPGEDIFRAFNLTPFDDVKVVILGQDPYHGPGQAHGLSFSVPPGV 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935828150  81 RIPPSLLNIYKELETDIeGFSIPAHGCLTAWAEQGVLLLNTVLTVRAGQAHSHALLGWERFTDTVIRQLATHRKHLVFML 160
Cdd:COG0692    86 PLPPSLRNIYKELEDDL-GIPIPNHGDLTSWAEQGVLLLNTVLTVRAGQAGSHAGKGWETFTDAVIRALNARKEPVVFLL 164

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1935828150 161 WGGYAQQKGRLIDSQNHLILTAPHPSPLSAYRGFFGCRHFSQANSYLSRHGIDPINW 217
Cdd:COG0692   165 WGAYAQKKAALIDASKHLVLESPHPSPLSAHRGFFGSKPFSKANAYLEEQGKTPIDW 221
 
Name Accession Description Interval E-value
Ung COG0692
Uracil-DNA glycosylase [Replication, recombination and repair];
1-217 6.64e-156

Uracil-DNA glycosylase [Replication, recombination and repair];


Pssm-ID: 440456  Cd Length: 221  Bit Score: 430.23  E-value: 6.64e-156
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935828150   1 MDTWHDALGGEKQQPYFQEILNAVRQERLSGQIIYPPAADVFNAFRLTAFDRVKAVILGQDPYHGAGQAHGLAFSVRQGI 80
Cdd:COG0692     6 EPSWKEALAEEFEKPYFQALGAFLKAEYAAGKTIYPPGEDIFRAFNLTPFDDVKVVILGQDPYHGPGQAHGLSFSVPPGV 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935828150  81 RIPPSLLNIYKELETDIeGFSIPAHGCLTAWAEQGVLLLNTVLTVRAGQAHSHALLGWERFTDTVIRQLATHRKHLVFML 160
Cdd:COG0692    86 PLPPSLRNIYKELEDDL-GIPIPNHGDLTSWAEQGVLLLNTVLTVRAGQAGSHAGKGWETFTDAVIRALNARKEPVVFLL 164

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1935828150 161 WGGYAQQKGRLIDSQNHLILTAPHPSPLSAYRGFFGCRHFSQANSYLSRHGIDPINW 217
Cdd:COG0692   165 WGAYAQKKAALIDASKHLVLESPHPSPLSAHRGFFGSKPFSKANAYLEEQGKTPIDW 221
PRK05254 PRK05254
uracil-DNA glycosylase; Provisional
 1-219 5.12e-153

uracil-DNA glycosylase; Provisional


Pssm-ID: 235376  Cd Length: 224  Bit Score: 423.41  E-value: 5.12e-153
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935828150   1 MDTWHDALGGEKQQPYFQEILNAVRQERLSGQIIYPPAADVFNAFRLTAFDRVKAVILGQDPYHGAGQAHGLAFSVRQGI 80
Cdd:PRK05254    7 EPSWKEVLKPEFKKPYFQELLEFLRAERAAGKTIYPPGEDIFRAFNLTPFDDVKVVILGQDPYHGPGQAHGLSFSVPPGV 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935828150  81 RIPPSLLNIYKELETDIeGFSIPAHGCLTAWAEQGVLLLNTVLTVRAGQAHSHALLGWERFTDTVIRQLATHRKHLVFML 160
Cdd:PRK05254   87 PIPPSLRNIFKELEDDL-GFPIPNHGDLTSWAEQGVLLLNTVLTVEAGQANSHAGKGWETFTDAVIKALNERREPVVFIL 165

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1935828150 161 WGGYAQQKGRLIDSQNHLILTAPHPSPLSAYRGFFGCRHFSQANSYLSRHGIDPINWKL 219
Cdd:PRK05254  166 WGSHAQKKKALIDNSKHLILESPHPSPLSAHRGFFGSKHFSKANALLKQHGKTPIDWQL 224
UDG-F1-like cd10027
Uracil DNA glycosylase family 1 subfamily, includes Human uracil DNA glycosylase and similar ...
 16-217 4.43e-134

Uracil DNA glycosylase family 1 subfamily, includes Human uracil DNA glycosylase and similar proteins; Uracil DNA glycosylase family 1 is the most efficient of all uracil-DNA glycosylases (UDGs, also known as UNGs) and shows a specificity for uracil in DNA. UDG catalyzes the removal of uracil from DNA to initiate the DNA base excision repair pathway. Uracil in DNA can arise as a result of mis-incorporation of dUMP residues by DNA polymerase or deamination of cytosine. Uracil mispaired with guanine in DNA is one of the major pro-mutagenic events, causing G:C->A:T mutations. Thus, UDG is an essential enzyme for maintaining the integrity of genetic information. UDGs have been classified into various families on the basis of their substrate specificity, conserved motifs, and structural similarities. Although these families demonstrate different substrate specificities, often the function of one enzyme can be complemented by the other.


Pssm-ID: 381678  Cd Length: 200  Bit Score: 374.48  E-value: 4.43e-134
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935828150  16 YFQEILNAVRQERLSgQIIYPPAADVFNAFRLTAFDRVKAVILGQDPYHGAGQAHGLAFSVRQGIRIPPSLLNIYKELET 95
Cdd:cd10027     1 YFKKLEAFLEEEYKK-KTIYPPKEDIFRAFELTPLDDVKVVILGQDPYHGPGQAHGLAFSVPPGVKIPPSLRNIFKELKS 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935828150  96 DIEGFsIPAHGCLTAWAEQGVLLLNTVLTVRAGQAHSHALLGWERFTDTVIRQLATHRKHLVFMLWGGYAQQKGRLIDSQ 175
Cdd:cd10027    80 DLGIF-PPKHGDLSSWAKQGVLLLNTVLTVEAGKPGSHKNIGWETFTDAVIKALSEKNENVVFLLWGNHAQKKKKLIDKK 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1935828150 176 NHLILTAPHPSPLSAYRGFFGCRHFSQANSYLSRHGIDPINW 217
Cdd:cd10027   159 KHLVLESSHPSPLSAYRGFFGSKHFSKANEYLKKHGKKPIDW 200
ung TIGR00628
uracil-DNA glycosylase; All proteins in this family for which functions are known are ...
 2-212 1.75e-128

uracil-DNA glycosylase; All proteins in this family for which functions are known are uracil-DNA glycosylases that function in base excision repair. 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: 273182  Cd Length: 211  Bit Score: 360.76  E-value: 1.75e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935828150   2 DTWHDALGGEKQQPYFQEILNAVRQERlSGQIIYPPAADVFNAFRLTAFDRVKAVILGQDPYHGAGQAHGLAFSVRQGIR 81
Cdd:TIGR00628   2 PSWRAFLQPEFKKPYFQELLAFYKRER-AQETVYPPKEDVFAWTRLCPPEDVKVVILGQDPYHGPGQAHGLAFSVKRGVP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935828150  82 IPPSLLNIYKELETDIEGFSIPAHGCLTAWAEQGVLLLNTVLTVRAGQAHSHALLGWERFTDTVIRQLATHRKHLVFMLW 161
Cdd:TIGR00628  81 IPPSLKNIFKELEADYPDFPPPKHGCLEAWARQGVLLLNTVLTVRRGQPGSHSGLGWERFTDAVISRLSERLDGLVFMLW 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1935828150 162 GGYAQQKGRLIDSQNHLILTAPHPSPLSAYRGFFGCRHFSQANSYLSRHGI 212
Cdd:TIGR00628 161 GAHAQKKKSLIDAKKHLVLKSPHPSPLSARRGFFGCRHFSKANEYLEKHGK 211
UDG smart00986
Uracil DNA glycosylase superfamily;
47-207 3.06e-33

Uracil DNA glycosylase superfamily;


Pssm-ID: 214956  Cd Length: 156  Bit Score: 117.10  E-value: 3.06e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935828150   47 LTAFDRVKAVILGQDPYHGAGQ-------AHGLAFSVRQGI----RIPPSLLNIYKELETDiegfsiPAHGCLTAWAEQG 115
Cdd:smart00986   2 GTGDPNAKVLIVGQAPGASEEDrggpfvgAAGLLLSVMLGVaglpRLPPYLTNIVKCRPPD------AGNRRPTSWELQG 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935828150  116 VLLlnTVLTVRAGQAHSHALLGWERFTDTVIRQLAthRKHLVFMLWGGYAQQKGRLidsqnHLILTAPHPSPLSAYRgfF 195
Cdd:smart00986  76 CLL--PWLTVELALARPHLILLLGKFAAQALLGLL--RRPLVFGLRGRVAQLKGKG-----HRVLPLPHPSPLNRNF--F 144

                          170
                   ....*....|..
gi 1935828150  196 GCRHFSQANSYL 207
Cdd:smart00986 145 PAKKFAAWNDLL 156
UDG pfam03167
Uracil DNA glycosylase superfamily;
53-206 7.20e-20

Uracil DNA glycosylase superfamily;


Pssm-ID: 397331  Cd Length: 154  Bit Score: 82.39  E-value: 7.20e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935828150  53 VKAVILGQDPYHgAGQAHGLAFSVRQGiRIPPSLLNIyKELETDIEgfsipahgcltawAEQGVLLLNTVLTVR--AGQA 130
Cdd:pfam03167   8 AKVLIVGEAPGA-DEDATGLPFVGRAG-NLLWKLLNA-AGLTRDLF-------------SPQGVYITNVVKCRPgnRRKP 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935828150 131 HSHAL-LGWERFtdtvIRQLATHRKHlVFMLWGGYAQQK-----------GRLIDSQNHLILTAPHPSPLSAYRgffgCR 198
Cdd:pfam03167  72 TSHEIdACWPYL----EAEIELLRPR-VIVLLGKTAAKAllglkkitklrGKLIDLKGIPVLPTPHPSPLLRNK----LN 142


                  ....*...
gi 1935828150 199 HFSQANSY 206
Cdd:pfam03167 143 PFLKANAW 150
 
Name Accession Description Interval E-value
Ung COG0692
Uracil-DNA glycosylase [Replication, recombination and repair];
1-217 6.64e-156

Uracil-DNA glycosylase [Replication, recombination and repair];


Pssm-ID: 440456  Cd Length: 221  Bit Score: 430.23  E-value: 6.64e-156
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935828150   1 MDTWHDALGGEKQQPYFQEILNAVRQERLSGQIIYPPAADVFNAFRLTAFDRVKAVILGQDPYHGAGQAHGLAFSVRQGI 80
Cdd:COG0692     6 EPSWKEALAEEFEKPYFQALGAFLKAEYAAGKTIYPPGEDIFRAFNLTPFDDVKVVILGQDPYHGPGQAHGLSFSVPPGV 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935828150  81 RIPPSLLNIYKELETDIeGFSIPAHGCLTAWAEQGVLLLNTVLTVRAGQAHSHALLGWERFTDTVIRQLATHRKHLVFML 160
Cdd:COG0692    86 PLPPSLRNIYKELEDDL-GIPIPNHGDLTSWAEQGVLLLNTVLTVRAGQAGSHAGKGWETFTDAVIRALNARKEPVVFLL 164

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1935828150 161 WGGYAQQKGRLIDSQNHLILTAPHPSPLSAYRGFFGCRHFSQANSYLSRHGIDPINW 217
Cdd:COG0692   165 WGAYAQKKAALIDASKHLVLESPHPSPLSAHRGFFGSKPFSKANAYLEEQGKTPIDW 221
PRK05254 PRK05254
uracil-DNA glycosylase; Provisional
 1-219 5.12e-153

uracil-DNA glycosylase; Provisional


Pssm-ID: 235376  Cd Length: 224  Bit Score: 423.41  E-value: 5.12e-153
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935828150   1 MDTWHDALGGEKQQPYFQEILNAVRQERLSGQIIYPPAADVFNAFRLTAFDRVKAVILGQDPYHGAGQAHGLAFSVRQGI 80
Cdd:PRK05254    7 EPSWKEVLKPEFKKPYFQELLEFLRAERAAGKTIYPPGEDIFRAFNLTPFDDVKVVILGQDPYHGPGQAHGLSFSVPPGV 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935828150  81 RIPPSLLNIYKELETDIeGFSIPAHGCLTAWAEQGVLLLNTVLTVRAGQAHSHALLGWERFTDTVIRQLATHRKHLVFML 160
Cdd:PRK05254   87 PIPPSLRNIFKELEDDL-GFPIPNHGDLTSWAEQGVLLLNTVLTVEAGQANSHAGKGWETFTDAVIKALNERREPVVFIL 165

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1935828150 161 WGGYAQQKGRLIDSQNHLILTAPHPSPLSAYRGFFGCRHFSQANSYLSRHGIDPINWKL 219
Cdd:PRK05254  166 WGSHAQKKKALIDNSKHLILESPHPSPLSAHRGFFGSKHFSKANALLKQHGKTPIDWQL 224
UDG-F1-like cd10027
Uracil DNA glycosylase family 1 subfamily, includes Human uracil DNA glycosylase and similar ...
 16-217 4.43e-134

Uracil DNA glycosylase family 1 subfamily, includes Human uracil DNA glycosylase and similar proteins; Uracil DNA glycosylase family 1 is the most efficient of all uracil-DNA glycosylases (UDGs, also known as UNGs) and shows a specificity for uracil in DNA. UDG catalyzes the removal of uracil from DNA to initiate the DNA base excision repair pathway. Uracil in DNA can arise as a result of mis-incorporation of dUMP residues by DNA polymerase or deamination of cytosine. Uracil mispaired with guanine in DNA is one of the major pro-mutagenic events, causing G:C->A:T mutations. Thus, UDG is an essential enzyme for maintaining the integrity of genetic information. UDGs have been classified into various families on the basis of their substrate specificity, conserved motifs, and structural similarities. Although these families demonstrate different substrate specificities, often the function of one enzyme can be complemented by the other.


Pssm-ID: 381678  Cd Length: 200  Bit Score: 374.48  E-value: 4.43e-134
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935828150  16 YFQEILNAVRQERLSgQIIYPPAADVFNAFRLTAFDRVKAVILGQDPYHGAGQAHGLAFSVRQGIRIPPSLLNIYKELET 95
Cdd:cd10027     1 YFKKLEAFLEEEYKK-KTIYPPKEDIFRAFELTPLDDVKVVILGQDPYHGPGQAHGLAFSVPPGVKIPPSLRNIFKELKS 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935828150  96 DIEGFsIPAHGCLTAWAEQGVLLLNTVLTVRAGQAHSHALLGWERFTDTVIRQLATHRKHLVFMLWGGYAQQKGRLIDSQ 175
Cdd:cd10027    80 DLGIF-PPKHGDLSSWAKQGVLLLNTVLTVEAGKPGSHKNIGWETFTDAVIKALSEKNENVVFLLWGNHAQKKKKLIDKK 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1935828150 176 NHLILTAPHPSPLSAYRGFFGCRHFSQANSYLSRHGIDPINW 217
Cdd:cd10027   159 KHLVLESSHPSPLSAYRGFFGSKHFSKANEYLKKHGKKPIDW 200
ung TIGR00628
uracil-DNA glycosylase; All proteins in this family for which functions are known are ...
 2-212 1.75e-128

uracil-DNA glycosylase; All proteins in this family for which functions are known are uracil-DNA glycosylases that function in base excision repair. 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: 273182  Cd Length: 211  Bit Score: 360.76  E-value: 1.75e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935828150   2 DTWHDALGGEKQQPYFQEILNAVRQERlSGQIIYPPAADVFNAFRLTAFDRVKAVILGQDPYHGAGQAHGLAFSVRQGIR 81
Cdd:TIGR00628   2 PSWRAFLQPEFKKPYFQELLAFYKRER-AQETVYPPKEDVFAWTRLCPPEDVKVVILGQDPYHGPGQAHGLAFSVKRGVP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935828150  82 IPPSLLNIYKELETDIEGFSIPAHGCLTAWAEQGVLLLNTVLTVRAGQAHSHALLGWERFTDTVIRQLATHRKHLVFMLW 161
Cdd:TIGR00628  81 IPPSLKNIFKELEADYPDFPPPKHGCLEAWARQGVLLLNTVLTVRRGQPGSHSGLGWERFTDAVISRLSERLDGLVFMLW 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1935828150 162 GGYAQQKGRLIDSQNHLILTAPHPSPLSAYRGFFGCRHFSQANSYLSRHGI 212
Cdd:TIGR00628 161 GAHAQKKKSLIDAKKHLVLKSPHPSPLSARRGFFGCRHFSKANEYLEKHGK 211
PHA03347 PHA03347
uracil DNA glycosylase; Provisional
 18-219 1.17e-89

uracil DNA glycosylase; Provisional


Pssm-ID: 177588  Cd Length: 252  Bit Score: 264.22  E-value: 1.17e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935828150  18 QEILNAVRQERLSgQIIYPPAADVFNAFRLTAFDRVKAVILGQDPYHGaGQAHGLAFSVRQGIRIPPSLLNIYKELETDI 97
Cdd:PHA03347   45 LALLNCVRELRKQ-TVIYPPEDRIMAWSYLCDPEDIKVVILGQDPYHG-GQANGLAFSVAYGFPVPPSLRNIFAELHRSV 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935828150  98 EGFSIPAHGCLTAWAEQGVLLLNTVLTVRAGQAHSHALLGWERFTDTVIRQLATHRKHLVFMLWGGYAQQKGRLIDSQNH 177
Cdd:PHA03347  123 PDFSPPDHGCLDAWARQGVLLLNTILTVEKGKPGSHSDLGWAWFTDYIISSLSEKLKACVFMLWGSKAIDKASLINSQKH 202

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1935828150 178 LILTAPHPSPLSA---YRG----FFGCRHFSQANSYLSRHGIDPINWKL 219
Cdd:PHA03347  203 LVLKAQHPSPLAAnstRSStwpkFLGCNHFVLANKYLTQHGKGPIDWNL 251
PHA03200 PHA03200
uracil DNA glycosylase; Provisional
 18-219 8.11e-83

uracil DNA glycosylase; Provisional


Pssm-ID: 165467  Cd Length: 255  Bit Score: 246.95  E-value: 8.11e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935828150  18 QEILNAVRQERLSGqIIYPPAADVFNAFRLTAFDRVKAVILGQDPYHGaGQAHGLAFSVRQGIRIPPSLLNIYKELETDI 97
Cdd:PHA03200   51 RRIVDAVDRDRQRL-TVYPPPEDVHRWSRLCSPEDVKVVIVGQDPYHD-GSACGLAFGTVRGRSAPPSLKNVFRELERTV 128

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935828150  98 EGFSIPAHGCLTAWAEQGVLLLNTVLTVRAGQAHSHALLGWERFTDTVIRQLATHRKHLVFMLWGGYAQQKGRLIDSQNH 177
Cdd:PHA03200  129 PNFSRPDSGCLDSWCRQGVLLLNTVFTVVHGQPGSHEALGWQTLSDRVISRLSEKREHLVFMLWGAQAQKLEYLIDSRKH 208

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1935828150 178 LILTAPHPSP--LSAYRGFFGCRHFSQANSYLSRHGIDPINWKL 219
Cdd:PHA03200  209 LILKSAHPSPrvKGARTPFIGNNHFVLANEYLSTHGKRPIDWNI 252
PHA03202 PHA03202
uracil DNA glycosylase; Provisional
 3-219 1.23e-78

uracil DNA glycosylase; Provisional


Pssm-ID: 165469  Cd Length: 313  Bit Score: 238.44  E-value: 1.23e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935828150   3 TWHDALGGEKQQPYFQEILNAVRQeRLSGQIIYPPAADVFNAFRLTAFDRVKAVILGQDPYHGAGQAHGLAFSVRQGIRI 82
Cdd:PHA03202   99 SWRPILEREMQQPYVRLLLNEYKL-RCAREEVFPPKEDIFAWTRFSPPEKVRVVIVGQDPYHAPGQAHGLAFSVRKGVPV 177

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935828150  83 PPSLLNIYKELETDIEGFSIPAHGCLTAWAEQGVLLLNTVLTVRAGQAHSHALLGWERFTDTVIRQLATHRKHLVFMLWG 162
Cdd:PHA03202  178 PPSLRNIYSAVQKSYPSFRPPMHGFLEKWAEQGVLLINTTLTVARGKPGSHATLGWHRLVRAVIDRLCTTSQGLVFMLWG 257

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1935828150 163 GYAqQKGRLIDSQNHLILTAPHPSPLSAYrGFFGCRHFSQANSYLSRHGIDPINWKL 219
Cdd:PHA03202  258 AHA-QKSCSPNRQHHLVLTYGHPSPLSRV-NFRDCPHFLEANAYLTKTGRKPVDWQI 312
PHA03199 PHA03199
uracil DNA glycosylase; Provisional
 4-219 1.16e-74

uracil DNA glycosylase; Provisional


Pssm-ID: 165466  Cd Length: 304  Bit Score: 227.97  E-value: 1.16e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935828150   4 WHDALGGEKQQPYFQEILNAVRQERLSGQIIYPPAADVFNAFRLTAFDRVKAVILGQDPYHGAGQAHGLAFSVRQGIRIP 83
Cdd:PHA03199   91 WHDLLRDEFEEPYAKGIFEEYNQLLNNGEEIFPIKGDIFAWTRFCGPEKIRVVIIGQDPYHGAGHAHGLAFSVKRGIPIP 170

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935828150  84 PSLLNIYKELETDIEGFSIPAHGCLTAWAEQGVLLLNTVLTVRAGQAHSHALLGWERFTDTVIRQLATHRKHLVFMLWGG 163
Cdd:PHA03199  171 PSLKNIFAALMESYPHLPLPTHGCLDNWARQGVLLLNTTLTVKRGTPGSHFYLGWDMLIKRMLKRLCENRTGLVFMLWGA 250

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1935828150 164 YAQQKGRlIDSQNHLILTAPHPSPLSAYRgFFGCRHFSQANSYLSRHGIDPINWKL 219
Cdd:PHA03199  251 HAQKTIQ-PNPRCHLVLTHAHPSPLSRSE-FRNCKHFLQANEYFLKKGEPEIDWSI 304
PHA03201 PHA03201
uracil DNA glycosylase; Provisional
 2-217 2.33e-69

uracil DNA glycosylase; Provisional


Pssm-ID: 165468  Cd Length: 318  Bit Score: 214.76  E-value: 2.33e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935828150   2 DTWHDALGGEKQQPYFQEILnAVRQERLSGQIIYPPAADVFNAFRLTAFDRVKAVILGQDPYHGAGQAHGLAFSVRQGIR 81
Cdd:PHA03201  104 DAWRPLLEPELANPLTARLM-AEYERRCRTEEVLPPREDVFSWTRYCTPDEVRVVIIGQDPYHQPGQAHGLAFSVRPGTP 182

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935828150  82 IPPSLLNIYKELETDIEGFSIPAHGCLTAWAEQGVLLLNTVLTVRAGQAHSHALLGWERFTDTVIRQLATHRKHLVFMLW 161
Cdd:PHA03201  183 APPSLRNILAAVRNCCPDARMSGHGCLEKWARGGVLLLNTTLTVRRGEPASHAKIGWDRFVGSVVRRLAASRPGLVFMLW 262

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1935828150 162 GGYAQQKGRlIDSQNHLILTAPHPSPLSayRGFFG-CRHFSQANSYLSRHGIDPINW 217
Cdd:PHA03201  263 GAHAQNAIR-PDPRVHRVLTYSHPSPLS--KVPFGsCRHFCLANQYLRERSLAPIDW 316
PHA03204 PHA03204
uracil DNA glycosylase; Provisional
 4-219 5.93e-66

uracil DNA glycosylase; Provisional


Pssm-ID: 165471  Cd Length: 322  Bit Score: 206.35  E-value: 5.93e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935828150   4 WHDALGGEKQQPYFQEILnAVRQERLSGQIIYPPAADVFNAFRLTAFDRVKAVILGQDPYHGAGQAHGLAFSVRQGIRIP 83
Cdd:PHA03204  106 WKEILLPELCCPTGSKIL-AEYERRARYEEVYPPKSDIFAWTRYCAPDHVKVVIVGQDPYANPGQAHGLAFSVKPGSPIP 184

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935828150  84 PSLLNIYKELETDIEGFSIPAHGCLTAWAEQGVLLLNTVLTVRAGQAHSHALLGWERFTDTVIRQLATHRKHLVFMLWGG 163
Cdd:PHA03204  185 PSLKNILAAVKACYPSIELGSHGCLEDWAKRGVLLLNSVLTVKRGDPGSHHSVGWQILVRNVLRRLSQSTRGIVFMLWGA 264

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1935828150 164 YAQQKGRLIDSQN-HLILTAPHPSPLSAyRGFFGCRHFSQANSYLSRHGIDPINWKL 219
Cdd:PHA03204  265 QAQTMYFQTDNDDrHLVLKYSHPSPLSR-KPFAHCTHFKDANEFLCKMGKGAIDWSL 320
UDG-F1-like cd19371
Uracil DNA glycosylase family 1, includes Human uracil DNA glycosylase, Vaccinia virus protein ...
 56-189 6.44e-53

Uracil DNA glycosylase family 1, includes Human uracil DNA glycosylase, Vaccinia virus protein D4, Nitratifractor salsuginis UNG and similar proteins; Uracil DNA glycosylase family 1 is the most efficient of all uracil-DNA glycosylases (UDGs, also known as UNGs) and shows a specificity for uracil in DNA. UDG catalyzes the removal of uracil from DNA to initiate the DNA base excision repair pathway. Uracil in DNA can arise as a result of misincorporation of dUMP residues by DNA polymerase or deamination of cytosine. Uracil mispaired with guanine in DNA is one of the major pro-mutagenic events, causing G:C->A:T mutations. Thus, UDG is an essential enzyme for maintaining the integrity of genetic information. UDGs have been classified into various families on the basis of their substrate specificity, conserved motifs, and structural similarities. Although these families demonstrate different substrate specificities, often the function of one enzyme can be complemented by the other. More distant members of UDG family 1 include Nitratifractor salsuginis UNG (NsaUNG) and Vaccinia virus (VAVC) protein D4 uracil-DNA glycosylase, a subunit of the VACV DNA polymerase holoenzyme. NsaUNG only exhibits robust enzymatic activity on uracil-containing DNAs, in particular double-stranded uracil-containing substrates; it does not act on hypoxanthine- and xanthine-containing substrates. NsUNG is not inhibited by Ugi protein that specifically inhibits conventional family 1 UDGs. D4, in addition to excising uracil residues from DNA, is part of a heterodimeric processivity factor which potentiates the DNA polymerase activity.


Pssm-ID: 381686  Cd Length: 135  Bit Score: 166.74  E-value: 6.44e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935828150  56 VILGQDPYHGAGQAHGLAFSVRQGIRIPPSLLNIYKELETDIEGFSIPAHGCLTAWAEQGVLLLNTVLTVRAGQAHSHAL 135
Cdd:cd19371     2 VIIGQDPYPSPGHAGGLAFSVTSEVPPPKSLRNIYKELERDYSSFLPPGNGTLEFWARQGVLLLNAALTCESGKPKSHYL 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1935828150 136 LgWERFTDTVIRQLATHRKHLVFMLWGGYAQQKGRLIDSQNHLILTAPHPSPLS 189
Cdd:cd19371    82 L-WEPFIKAFIRYISAHNKGLVFLLFGSDAQKLRKKINGRNVHVFKADHPSPAD 134
UDG smart00986
Uracil DNA glycosylase superfamily;
47-207 3.06e-33

Uracil DNA glycosylase superfamily;


Pssm-ID: 214956  Cd Length: 156  Bit Score: 117.10  E-value: 3.06e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935828150   47 LTAFDRVKAVILGQDPYHGAGQ-------AHGLAFSVRQGI----RIPPSLLNIYKELETDiegfsiPAHGCLTAWAEQG 115
Cdd:smart00986   2 GTGDPNAKVLIVGQAPGASEEDrggpfvgAAGLLLSVMLGVaglpRLPPYLTNIVKCRPPD------AGNRRPTSWELQG 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935828150  116 VLLlnTVLTVRAGQAHSHALLGWERFTDTVIRQLAthRKHLVFMLWGGYAQQKGRLidsqnHLILTAPHPSPLSAYRgfF 195
Cdd:smart00986  76 CLL--PWLTVELALARPHLILLLGKFAAQALLGLL--RRPLVFGLRGRVAQLKGKG-----HRVLPLPHPSPLNRNF--F 144

                          170
                   ....*....|..
gi 1935828150  196 GCRHFSQANSYL 207
Cdd:smart00986 145 PAKKFAAWNDLL 156
UDG pfam03167
Uracil DNA glycosylase superfamily;
53-206 7.20e-20

Uracil DNA glycosylase superfamily;


Pssm-ID: 397331  Cd Length: 154  Bit Score: 82.39  E-value: 7.20e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935828150  53 VKAVILGQDPYHgAGQAHGLAFSVRQGiRIPPSLLNIyKELETDIEgfsipahgcltawAEQGVLLLNTVLTVR--AGQA 130
Cdd:pfam03167   8 AKVLIVGEAPGA-DEDATGLPFVGRAG-NLLWKLLNA-AGLTRDLF-------------SPQGVYITNVVKCRPgnRRKP 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935828150 131 HSHAL-LGWERFtdtvIRQLATHRKHlVFMLWGGYAQQK-----------GRLIDSQNHLILTAPHPSPLSAYRgffgCR 198
Cdd:pfam03167  72 TSHEIdACWPYL----EAEIELLRPR-VIVLLGKTAAKAllglkkitklrGKLIDLKGIPVLPTPHPSPLLRNK----LN 142


                  ....*...
gi 1935828150 199 HFSQANSY 206
Cdd:pfam03167 143 PFLKANAW 150
UDG-like cd09593
uracil-DNA glycosylases (UDG) and related enzymes; Uracil-DNA glycosylases (UDGs) initiate ...
 56-190 5.41e-19

uracil-DNA glycosylases (UDG) and related enzymes; Uracil-DNA glycosylases (UDGs) initiate repair of uracils in DNA. Uracil may arise from misincorporation of dUMP residues by DNA polymerase or via deamination of cytosine. Uracil in DNA mispaired with guanine is one of the major pro-mutagenic events, causing G:C->A:T mutations; thus, UDG is an essential enzyme for maintaining the integrity of genetic information. UDGs have been classified into various families on the basis of their substrate specificity, conserved motifs, and structural similarities. Although these families demonstrate different substrate specificities, often the function of one enzyme can be complemented by the other. UDG family 1 is the most efficient uracil-DNA glycosylase (UDG, also known as UNG) and shows a specificity for uracil in DNA. UDG family 2 includes thymine DNA glycosylase which removes uracil and thymine from G:U and G:T mismatches, and mismatch-specific uracil DNA glycosylase (MUG) which in Escherichia coli is highly specific to G:U mismatches, but also repairs G:T mismatches at high enzyme concentration. UDG family 3 includes Human SMUG1 which can remove uracil and its oxidized pyrimidine derivatives from, single-stranded DNA and double-stranded DNA with a preference for single-stranded DNA. Pedobacter heparinus SMUG2, which is UDG family 3 SMUG1-like, displays catalytic activities towards DNA containing uracil or hypoxanthine/xanthine. UDG family 4 includes Thermotoga maritima TTUDGA, a robust UDG which like family 1, acts on double-stranded and single-stranded uracil-containing DNA. UDG family 5 (UDGb) includes Thermus thermophilus HB8 TTUDGB which acts on double-stranded uracil-containing DNA; it is a hypoxanthine DNA glycosylase acting on double-stranded hypoxanthine-containing DNA except for the C/I base pair, as well as a xanthine DNA glycosylase which acts on both double-stranded and single-stranded xanthine-containing DNA. UDG family 6 hypoxanthine-DNA glycosylase lacks any detectable UDG activity; it excises hypoxanthine. Other UDG families include one represented by Bradyrhizobium diazoefficiens Blr0248 which prefers single-stranded DNA and removes uracil, 5-hydroxymethyl-uracil or xanthine from it.


Pssm-ID: 381677  Cd Length: 125  Bit Score: 79.35  E-value: 5.41e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935828150  56 VILGQDPYHGAGQAHGlafsvrqgIRIPPSLLNIYKELETDIEGFSipahgcltaWAEQGVLLLNTVLTVRAGQAHSHaL 135
Cdd:cd09593     2 LIVGQNPGPHGARAGG--------VPPGPSGNRLWRLLAAAGGTPR---------LFRYGVGLTNTVPRGPPGAAAGS-E 63

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1935828150 136 LGWERFTDTVIRQLATHRKHLVFMLWGGYAQQKGRLIDSQN-------HLILTAPHPSPLSA 190
Cdd:cd09593    64 KKELRFCGRWLRKLLELLNPRVVVLLGKKAQEAYLAVLTSSkgapgkgTEVLVLPHPSPRNR 125
UDG_F1_VAVC_D4-like cd19372
Uracil DNA glycosylase family 1 subfamily, includes Vaccinia virus protein D4 and similar ...
 114-217 3.53e-05

Uracil DNA glycosylase family 1 subfamily, includes Vaccinia virus protein D4 and similar proteins; Vaccinia virus (VAVC) protein D4 uracil-DNA glycosylase, is a subunit of the VACV DNA polymerase holoenzyme, and a more distant member of uracil DNA glycosylase (UDG) family 1. D4, in addition to excising uracil residues from DNA, is part of a heterodimeric processivity factor which potentiates the DNA polymerase activity. UDG catalyzes the removal of uracil from DNA to initiate the DNA base excision repair pathway. Uracil in DNA can arise as a result of mis-incorporation of dUMP residues by DNA polymerase or deamination of cytosine. Uracil mispaired with guanine in DNA is one of the major pro-mutagenic events, causing G:C->A:T mutations. Thus, UDG is an essential enzyme for maintaining the integrity of genetic information. UDGs have been classified into various families on the basis of their substrate specificity, conserved motifs, and structural similarities. Although these families demonstrate different substrate specificities, often the function of one enzyme can be complemented by the other.


Pssm-ID: 381687  Cd Length: 200  Bit Score: 43.20  E-value: 3.53e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935828150 114 QGVLLLNTVLTVRAGQAHSHALLgWERFTDTVIRQLATHRKHLVFMLWGGYAQQKGRLiDSQNHLILtAPHPsplsAYRG 193
Cdd:cd19372    96 EGVLAWNYYLSCREGETKSHAIH-WERISKLLLQHIAKYVSVLYCLGKTDFSNVRARL-EVPVTVVV-GYHP----AARD 168

                          90       100
                  ....*....|....*....|....*.
gi 1935828150 194 --FFGCRHFSQANSYLSRHGIDPINW 217
Cdd:cd19372   169 gqFDKERAFEIVNVLLELNGKPPVNW 194
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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