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Conserved domains on  [gi|491993977|ref|WP_005711048|]
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uracil-DNA glycosylase [Glaesserella parasuis]

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];
1-216 6.18e-157

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


:

Pssm-ID: 440456  Cd Length: 221  Bit Score: 432.93  E-value: 6.18e-157
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491993977   1 MNSWTDAIGEEKTQPYFQHILQYVHQERLVGKVIYPPQNEVFSAFALTEFKDVKVVILGQDPYHGPNQAHGLSFSVKPGI 80
Cdd:COG0692    6 EPSWKEALAEEFEKPYFQALGAFLKAEYAAGKTIYPPGEDIFRAFNLTPFDDVKVVILGQDPYHGPGQAHGLSFSVPPGV 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491993977  81 VPPPSLVNMYKELSQDVGFQIPSHGYLIEWAKQGVLLLNTVLTVEQGKAHSHANIGWETFTDKVIHQLNLHRENLVFLLW 160
Cdd:COG0692   86 PLPPSLRNIYKELEDDLGIPIPNHGDLTSWAEQGVLLLNTVLTVRAGQAGSHAGKGWETFTDAVIRALNARKEPVVFLLW 165

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 491993977 161 GSHAQKKGQFIDRSRHCVLTAPHPSPLSAHRGFLGCRHFSKTNDYLRSHGVEEINW 216
Cdd:COG0692  166 GAYAQKKAALIDASKHLVLESPHPSPLSAHRGFFGSKPFSKANAYLEEQGKTPIDW 221
 
Name Accession Description Interval E-value
Ung COG0692
Uracil-DNA glycosylase [Replication, recombination and repair];
1-216 6.18e-157

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


Pssm-ID: 440456  Cd Length: 221  Bit Score: 432.93  E-value: 6.18e-157
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491993977   1 MNSWTDAIGEEKTQPYFQHILQYVHQERLVGKVIYPPQNEVFSAFALTEFKDVKVVILGQDPYHGPNQAHGLSFSVKPGI 80
Cdd:COG0692    6 EPSWKEALAEEFEKPYFQALGAFLKAEYAAGKTIYPPGEDIFRAFNLTPFDDVKVVILGQDPYHGPGQAHGLSFSVPPGV 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491993977  81 VPPPSLVNMYKELSQDVGFQIPSHGYLIEWAKQGVLLLNTVLTVEQGKAHSHANIGWETFTDKVIHQLNLHRENLVFLLW 160
Cdd:COG0692   86 PLPPSLRNIYKELEDDLGIPIPNHGDLTSWAEQGVLLLNTVLTVRAGQAGSHAGKGWETFTDAVIRALNARKEPVVFLLW 165

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 491993977 161 GSHAQKKGQFIDRSRHCVLTAPHPSPLSAHRGFLGCRHFSKTNDYLRSHGVEEINW 216
Cdd:COG0692  166 GAYAQKKAALIDASKHLVLESPHPSPLSAHRGFFGSKPFSKANAYLEEQGKTPIDW 221
PRK05254 PRK05254
uracil-DNA glycosylase; Provisional
 1-218 1.44e-154

uracil-DNA glycosylase; Provisional


Pssm-ID: 235376  Cd Length: 224  Bit Score: 427.26  E-value: 1.44e-154
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491993977   1 MNSWTDAIGEEKTQPYFQHILQYVHQERLVGKVIYPPQNEVFSAFALTEFKDVKVVILGQDPYHGPNQAHGLSFSVKPGI 80
Cdd:PRK05254   7 EPSWKEVLKPEFKKPYFQELLEFLRAERAAGKTIYPPGEDIFRAFNLTPFDDVKVVILGQDPYHGPGQAHGLSFSVPPGV 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491993977  81 VPPPSLVNMYKELSQDVGFQIPSHGYLIEWAKQGVLLLNTVLTVEQGKAHSHANIGWETFTDKVIHQLNLHRENLVFLLW 160
Cdd:PRK05254  87 PIPPSLRNIFKELEDDLGFPIPNHGDLTSWAEQGVLLLNTVLTVEAGQANSHAGKGWETFTDAVIKALNERREPVVFILW 166

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 491993977 161 GSHAQKKGQFIDRSRHCVLTAPHPSPLSAHRGFLGCRHFSKTNDYLRSHGVEEINWQL 218
Cdd:PRK05254 167 GSHAQKKKALIDNSKHLILESPHPSPLSAHRGFFGSKHFSKANALLKQHGKTPIDWQL 224
UDG-F1-like cd10027
Uracil DNA glycosylase family 1 subfamily, includes Human uracil DNA glycosylase and similar ...
 16-216 6.78e-132

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: 369.09  E-value: 6.78e-132
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491993977  16 YFQHILQYVHQERLvGKVIYPPQNEVFSAFALTEFKDVKVVILGQDPYHGPNQAHGLSFSVKPGIVPPPSLVNMYKELSQ 95
Cdd:cd10027    1 YFKKLEAFLEEEYK-KKTIYPPKEDIFRAFELTPLDDVKVVILGQDPYHGPGQAHGLAFSVPPGVKIPPSLRNIFKELKS 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491993977  96 DVGFQIPSHGYLIEWAKQGVLLLNTVLTVEQGKAHSHANIGWETFTDKVIHQLNLHRENLVFLLWGSHAQKKGQFIDRSR 175
Cdd:cd10027   80 DLGIFPPKHGDLSSWAKQGVLLLNTVLTVEAGKPGSHKNIGWETFTDAVIKALSEKNENVVFLLWGNHAQKKKKLIDKKK 159

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 491993977 176 HCVLTAPHPSPLSAHRGFLGCRHFSKTNDYLRSHGVEEINW 216
Cdd:cd10027  160 HLVLESSHPSPLSAYRGFFGSKHFSKANEYLKKHGKKPIDW 200
ung TIGR00628
uracil-DNA glycosylase; All proteins in this family for which functions are known are ...
 3-210 1.83e-120

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: 340.73  E-value: 1.83e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491993977    3 SWTDAIGEEKTQPYFQHILQYVHQERLvGKVIYPPQNEVFSAFALTEFKDVKVVILGQDPYHGPNQAHGLSFSVKPGIVP 82
Cdd:TIGR00628   3 SWRAFLQPEFKKPYFQELLAFYKRERA-QETVYPPKEDVFAWTRLCPPEDVKVVILGQDPYHGPGQAHGLAFSVKRGVPI 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491993977   83 PPSLVNMYKELSQDVG-FQIPSHGYLIEWAKQGVLLLNTVLTVEQGKAHSHANIGWETFTDKVIHQLNLHRENLVFLLWG 161
Cdd:TIGR00628  82 PPSLKNIFKELEADYPdFPPPKHGCLEAWARQGVLLLNTVLTVRRGQPGSHSGLGWERFTDAVISRLSERLDGLVFMLWG 161

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 491993977  162 SHAQKKGQFIDRSRHCVLTAPHPSPLSAHRGFLGCRHFSKTNDYLRSHG 210
Cdd:TIGR00628 162 AHAQKKKSLIDAKKHLVLKSPHPSPLSARRGFFGCRHFSKANEYLEKHG 210
UDG smart00986
Uracil DNA glycosylase superfamily;
50-206 4.09e-36

Uracil DNA glycosylase superfamily;


Pssm-ID: 214956  Cd Length: 156  Bit Score: 124.42  E-value: 4.09e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491993977    50 FKDVKVVILGQDPY------HGP-NQAHGLSFSVKPGIVP----PPSLVNMYKELSQDvgfqiPSHGYLIEWAKQGVLLl 118
Cdd:smart00986   5 DPNAKVLIVGQAPGaseedrGGPfVGAAGLLLSVMLGVAGlprlPPYLTNIVKCRPPD-----AGNRRPTSWELQGCLL- 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491993977   119 nTVLTVEQGKAHSHANIGWETFTDKVIhqLNLHRENLVFLLWGSHAQKKGQfidrsRHCVLTAPHPSPLSAHRgfLGCRH 198
Cdd:smart00986  79 -PWLTVELALARPHLILLLGKFAAQAL--LGLLRRPLVFGLRGRVAQLKGK-----GHRVLPLPHPSPLNRNF--FPAKK 148


                   ....*...
gi 491993977   199 FSKTNDYL 206
Cdd:smart00986 149 FAAWNDLL 156
UDG pfam03167
Uracil DNA glycosylase superfamily;
51-205 1.54e-23

Uracil DNA glycosylase superfamily;


Pssm-ID: 397331  Cd Length: 154  Bit Score: 92.02  E-value: 1.54e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491993977   51 KDVKVVILGQDPYHGpNQAHGLSFSVKPGIVPPPSLVNMykELSQDVGfqipshgyliewAKQGVLLLNTVLTVEQGKAH 130
Cdd:pfam03167   6 PNAKVLIVGEAPGAD-EDATGLPFVGRAGNLLWKLLNAA--GLTRDLF------------SPQGVYITNVVKCRPGNRRK 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491993977  131 SHA---NIGWEtFTDKVIHQLNLHrenlVFLLWGSHAQKK-----------GQFIDRSRHCVLTAPHPSPLSAHRgflgC 196
Cdd:pfam03167  71 PTSheiDACWP-YLEAEIELLRPR----VIVLLGKTAAKAllglkkitklrGKLIDLKGIPVLPTPHPSPLLRNK----L 141


                  ....*....
gi 491993977  197 RHFSKTNDY 205
Cdd:pfam03167 142 NPFLKANAW 150
 
Name Accession Description Interval E-value
Ung COG0692
Uracil-DNA glycosylase [Replication, recombination and repair];
1-216 6.18e-157

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


Pssm-ID: 440456  Cd Length: 221  Bit Score: 432.93  E-value: 6.18e-157
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491993977   1 MNSWTDAIGEEKTQPYFQHILQYVHQERLVGKVIYPPQNEVFSAFALTEFKDVKVVILGQDPYHGPNQAHGLSFSVKPGI 80
Cdd:COG0692    6 EPSWKEALAEEFEKPYFQALGAFLKAEYAAGKTIYPPGEDIFRAFNLTPFDDVKVVILGQDPYHGPGQAHGLSFSVPPGV 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491993977  81 VPPPSLVNMYKELSQDVGFQIPSHGYLIEWAKQGVLLLNTVLTVEQGKAHSHANIGWETFTDKVIHQLNLHRENLVFLLW 160
Cdd:COG0692   86 PLPPSLRNIYKELEDDLGIPIPNHGDLTSWAEQGVLLLNTVLTVRAGQAGSHAGKGWETFTDAVIRALNARKEPVVFLLW 165

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 491993977 161 GSHAQKKGQFIDRSRHCVLTAPHPSPLSAHRGFLGCRHFSKTNDYLRSHGVEEINW 216
Cdd:COG0692  166 GAYAQKKAALIDASKHLVLESPHPSPLSAHRGFFGSKPFSKANAYLEEQGKTPIDW 221
PRK05254 PRK05254
uracil-DNA glycosylase; Provisional
 1-218 1.44e-154

uracil-DNA glycosylase; Provisional


Pssm-ID: 235376  Cd Length: 224  Bit Score: 427.26  E-value: 1.44e-154
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491993977   1 MNSWTDAIGEEKTQPYFQHILQYVHQERLVGKVIYPPQNEVFSAFALTEFKDVKVVILGQDPYHGPNQAHGLSFSVKPGI 80
Cdd:PRK05254   7 EPSWKEVLKPEFKKPYFQELLEFLRAERAAGKTIYPPGEDIFRAFNLTPFDDVKVVILGQDPYHGPGQAHGLSFSVPPGV 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491993977  81 VPPPSLVNMYKELSQDVGFQIPSHGYLIEWAKQGVLLLNTVLTVEQGKAHSHANIGWETFTDKVIHQLNLHRENLVFLLW 160
Cdd:PRK05254  87 PIPPSLRNIFKELEDDLGFPIPNHGDLTSWAEQGVLLLNTVLTVEAGQANSHAGKGWETFTDAVIKALNERREPVVFILW 166

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 491993977 161 GSHAQKKGQFIDRSRHCVLTAPHPSPLSAHRGFLGCRHFSKTNDYLRSHGVEEINWQL 218
Cdd:PRK05254 167 GSHAQKKKALIDNSKHLILESPHPSPLSAHRGFFGSKHFSKANALLKQHGKTPIDWQL 224
UDG-F1-like cd10027
Uracil DNA glycosylase family 1 subfamily, includes Human uracil DNA glycosylase and similar ...
 16-216 6.78e-132

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: 369.09  E-value: 6.78e-132
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491993977  16 YFQHILQYVHQERLvGKVIYPPQNEVFSAFALTEFKDVKVVILGQDPYHGPNQAHGLSFSVKPGIVPPPSLVNMYKELSQ 95
Cdd:cd10027    1 YFKKLEAFLEEEYK-KKTIYPPKEDIFRAFELTPLDDVKVVILGQDPYHGPGQAHGLAFSVPPGVKIPPSLRNIFKELKS 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491993977  96 DVGFQIPSHGYLIEWAKQGVLLLNTVLTVEQGKAHSHANIGWETFTDKVIHQLNLHRENLVFLLWGSHAQKKGQFIDRSR 175
Cdd:cd10027   80 DLGIFPPKHGDLSSWAKQGVLLLNTVLTVEAGKPGSHKNIGWETFTDAVIKALSEKNENVVFLLWGNHAQKKKKLIDKKK 159

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 491993977 176 HCVLTAPHPSPLSAHRGFLGCRHFSKTNDYLRSHGVEEINW 216
Cdd:cd10027  160 HLVLESSHPSPLSAYRGFFGSKHFSKANEYLKKHGKKPIDW 200
ung TIGR00628
uracil-DNA glycosylase; All proteins in this family for which functions are known are ...
 3-210 1.83e-120

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: 340.73  E-value: 1.83e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491993977    3 SWTDAIGEEKTQPYFQHILQYVHQERLvGKVIYPPQNEVFSAFALTEFKDVKVVILGQDPYHGPNQAHGLSFSVKPGIVP 82
Cdd:TIGR00628   3 SWRAFLQPEFKKPYFQELLAFYKRERA-QETVYPPKEDVFAWTRLCPPEDVKVVILGQDPYHGPGQAHGLAFSVKRGVPI 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491993977   83 PPSLVNMYKELSQDVG-FQIPSHGYLIEWAKQGVLLLNTVLTVEQGKAHSHANIGWETFTDKVIHQLNLHRENLVFLLWG 161
Cdd:TIGR00628  82 PPSLKNIFKELEADYPdFPPPKHGCLEAWARQGVLLLNTVLTVRRGQPGSHSGLGWERFTDAVISRLSERLDGLVFMLWG 161

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 491993977  162 SHAQKKGQFIDRSRHCVLTAPHPSPLSAHRGFLGCRHFSKTNDYLRSHG 210
Cdd:TIGR00628 162 AHAQKKKSLIDAKKHLVLKSPHPSPLSARRGFFGCRHFSKANEYLEKHG 210
PHA03347 PHA03347
uracil DNA glycosylase; Provisional
 33-218 8.52e-81

uracil DNA glycosylase; Provisional


Pssm-ID: 177588  Cd Length: 252  Bit Score: 241.49  E-value: 8.52e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491993977  33 VIYPPQNEVFSAFALTEFKDVKVVILGQDPYHGpNQAHGLSFSVKPGIVPPPSLVNMYKELSQDV-GFQIPSHGYLIEWA 111
Cdd:PHA03347  59 VIYPPEDRIMAWSYLCDPEDIKVVILGQDPYHG-GQANGLAFSVAYGFPVPPSLRNIFAELHRSVpDFSPPDHGCLDAWA 137

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491993977 112 KQGVLLLNTVLTVEQGKAHSHANIGWETFTDKVIHQLNLHRENLVFLLWGSHAQKKGQFIDRSRHCVLTAPHPSPLSAHR 191
Cdd:PHA03347 138 RQGVLLLNTILTVEKGKPGSHSDLGWAWFTDYIISSLSEKLKACVFMLWGSKAIDKASLINSQKHLVLKAQHPSPLAANS 217

                        170       180       190
                 ....*....|....*....|....*....|....
gi 491993977 192 G-------FLGCRHFSKTNDYLRSHGVEEINWQL 218
Cdd:PHA03347 218 TrsstwpkFLGCNHFVLANKYLTQHGKGPIDWNL 251
PHA03200 PHA03200
uracil DNA glycosylase; Provisional
 18-218 7.04e-73

uracil DNA glycosylase; Provisional


Pssm-ID: 165467  Cd Length: 255  Bit Score: 221.52  E-value: 7.04e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491993977  18 QHILQYVHQERLVGkVIYPPQNEVFSAFALTEFKDVKVVILGQDPYHGpNQAHGLSFSVKPGIVPPPSLVNMYKELSQDV 97
Cdd:PHA03200  51 RRIVDAVDRDRQRL-TVYPPPEDVHRWSRLCSPEDVKVVIVGQDPYHD-GSACGLAFGTVRGRSAPPSLKNVFRELERTV 128

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491993977  98 -GFQIPSHGYLIEWAKQGVLLLNTVLTVEQGKAHSHANIGWETFTDKVIHQLNLHRENLVFLLWGSHAQKKGQFIDRSRH 176
Cdd:PHA03200 129 pNFSRPDSGCLDSWCRQGVLLLNTVFTVVHGQPGSHEALGWQTLSDRVISRLSEKREHLVFMLWGAQAQKLEYLIDSRKH 208

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 491993977 177 CVLTAPHPSP--LSAHRGFLGCRHFSKTNDYLRSHGVEEINWQL 218
Cdd:PHA03200 209 LILKSAHPSPrvKGARTPFIGNNHFVLANEYLSTHGKRPIDWNI 252
PHA03202 PHA03202
uracil DNA glycosylase; Provisional
 3-218 7.63e-67

uracil DNA glycosylase; Provisional


Pssm-ID: 165469  Cd Length: 313  Bit Score: 208.40  E-value: 7.63e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491993977   3 SWTDAIGEEKTQPYFQHILQYvHQERLVGKVIYPPQNEVFSAFALTEFKDVKVVILGQDPYHGPNQAHGLSFSVKPGIVP 82
Cdd:PHA03202  99 SWRPILEREMQQPYVRLLLNE-YKLRCAREEVFPPKEDIFAWTRFSPPEKVRVVIVGQDPYHAPGQAHGLAFSVRKGVPV 177

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491993977  83 PPSLVNMYKELSQDV-GFQIPSHGYLIEWAKQGVLLLNTVLTVEQGKAHSHANIGWETFTDKVIHQLNLHRENLVFLLWG 161
Cdd:PHA03202 178 PPSLRNIYSAVQKSYpSFRPPMHGFLEKWAEQGVLLINTTLTVARGKPGSHATLGWHRLVRAVIDRLCTTSQGLVFMLWG 257

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 491993977 162 SHAQKKGQfIDRSRHCVLTAPHPSPLSaHRGFLGCRHFSKTNDYLRSHGVEEINWQL 218
Cdd:PHA03202 258 AHAQKSCS-PNRQHHLVLTYGHPSPLS-RVNFRDCPHFLEANAYLTKTGRKPVDWQI 312
PHA03199 PHA03199
uracil DNA glycosylase; Provisional
 4-218 4.03e-63

uracil DNA glycosylase; Provisional


Pssm-ID: 165466  Cd Length: 304  Bit Score: 198.31  E-value: 4.03e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491993977   4 WTDAIGEEKTQPYFQHILQYVHQERLVGKVIYPPQNEVFsafALTEF---KDVKVVILGQDPYHGPNQAHGLSFSVKPGI 80
Cdd:PHA03199  91 WHDLLRDEFEEPYAKGIFEEYNQLLNNGEEIFPIKGDIF---AWTRFcgpEKIRVVIIGQDPYHGAGHAHGLAFSVKRGI 167

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491993977  81 VPPPSLVNMYKELSQDV-GFQIPSHGYLIEWAKQGVLLLNTVLTVEQGKAHSHANIGWETFTDKVIHQLNLHRENLVFLL 159
Cdd:PHA03199 168 PIPPSLKNIFAALMESYpHLPLPTHGCLDNWARQGVLLLNTTLTVKRGTPGSHFYLGWDMLIKRMLKRLCENRTGLVFML 247

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 491993977 160 WGSHAQKKGQfIDRSRHCVLTAPHPSPLSaHRGFLGCRHFSKTNDYLRSHGVEEINWQL 218
Cdd:PHA03199 248 WGAHAQKTIQ-PNPRCHLVLTHAHPSPLS-RSEFRNCKHFLQANEYFLKKGEPEIDWSI 304
PHA03201 PHA03201
uracil DNA glycosylase; Provisional
 2-216 9.12e-61

uracil DNA glycosylase; Provisional


Pssm-ID: 165468  Cd Length: 318  Bit Score: 192.80  E-value: 9.12e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491993977   2 NSWTDAIGEEKTQPYFQHILQYvHQERLVGKVIYPPQNEVFSAFALTEFKDVKVVILGQDPYHGPNQAHGLSFSVKPGIV 81
Cdd:PHA03201 104 DAWRPLLEPELANPLTARLMAE-YERRCRTEEVLPPREDVFSWTRYCTPDEVRVVIIGQDPYHQPGQAHGLAFSVRPGTP 182

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491993977  82 PPPSLVNMY---KELSQDVgfQIPSHGYLIEWAKQGVLLLNTVLTVEQGKAHSHANIGWETFTDKVIHQLNLHRENLVFL 158
Cdd:PHA03201 183 APPSLRNILaavRNCCPDA--RMSGHGCLEKWARGGVLLLNTTLTVRRGEPASHAKIGWDRFVGSVVRRLAASRPGLVFM 260

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 491993977 159 LWGSHAQKKGQfIDRSRHCVLTAPHPSPLSaHRGFLGCRHFSKTNDYLRSHGVEEINW 216
Cdd:PHA03201 261 LWGAHAQNAIR-PDPRVHRVLTYSHPSPLS-KVPFGSCRHFCLANQYLRERSLAPIDW 316
PHA03204 PHA03204
uracil DNA glycosylase; Provisional
 3-218 2.00e-58

uracil DNA glycosylase; Provisional


Pssm-ID: 165471  Cd Length: 322  Bit Score: 187.09  E-value: 2.00e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491993977   3 SWTDAIGEEKTQPYFQHILQYvHQERLVGKVIYPPQNEVFSAFALTEFKDVKVVILGQDPYHGPNQAHGLSFSVKPGIVP 82
Cdd:PHA03204 105 RWKEILLPELCCPTGSKILAE-YERRARYEEVYPPKSDIFAWTRYCAPDHVKVVIVGQDPYANPGQAHGLAFSVKPGSPI 183

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491993977  83 PPSLVNMYKEL-----SQDVGfqipSHGYLIEWAKQGVLLLNTVLTVEQGKAHSHANIGWETFTDKVIHQLNLHRENLVF 157
Cdd:PHA03204 184 PPSLKNILAAVkacypSIELG----SHGCLEDWAKRGVLLLNSVLTVKRGDPGSHHSVGWQILVRNVLRRLSQSTRGIVF 259

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491993977 158 LLWGSHAQKKGQFIDRS-RHCVLTAPHPSPLSaHRGFLGCRHFSKTNDYLRSHGVEEINWQL 218
Cdd:PHA03204 260 MLWGAQAQTMYFQTDNDdRHLVLKYSHPSPLS-RKPFAHCTHFKDANEFLCKMGKGAIDWSL 320
UDG-F1-like cd19371
Uracil DNA glycosylase family 1, includes Human uracil DNA glycosylase, Vaccinia virus protein ...
 55-188 1.78e-52

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: 165.59  E-value: 1.78e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491993977  55 VVILGQDPYHGPNQAHGLSFSVKPGIVPPPSLVNMYKELSQDVG-FQIPSHGYLIEWAKQGVLLLNTVLTVEQGKAHSHA 133
Cdd:cd19371    1 VVIIGQDPYPSPGHAGGLAFSVTSEVPPPKSLRNIYKELERDYSsFLPPGNGTLEFWARQGVLLLNAALTCESGKPKSHY 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 491993977 134 nIGWETFTDKVIHQLNLHRENLVFLLWGSHAQKKGQFIDRSRHCVLTAPHPSPLS 188
Cdd:cd19371   81 -LLWEPFIKAFIRYISAHNKGLVFLLFGSDAQKLRKKINGRNVHVFKADHPSPAD 134
UDG smart00986
Uracil DNA glycosylase superfamily;
50-206 4.09e-36

Uracil DNA glycosylase superfamily;


Pssm-ID: 214956  Cd Length: 156  Bit Score: 124.42  E-value: 4.09e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491993977    50 FKDVKVVILGQDPY------HGP-NQAHGLSFSVKPGIVP----PPSLVNMYKELSQDvgfqiPSHGYLIEWAKQGVLLl 118
Cdd:smart00986   5 DPNAKVLIVGQAPGaseedrGGPfVGAAGLLLSVMLGVAGlprlPPYLTNIVKCRPPD-----AGNRRPTSWELQGCLL- 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491993977   119 nTVLTVEQGKAHSHANIGWETFTDKVIhqLNLHRENLVFLLWGSHAQKKGQfidrsRHCVLTAPHPSPLSAHRgfLGCRH 198
Cdd:smart00986  79 -PWLTVELALARPHLILLLGKFAAQAL--LGLLRRPLVFGLRGRVAQLKGK-----GHRVLPLPHPSPLNRNF--FPAKK 148


                   ....*...
gi 491993977   199 FSKTNDYL 206
Cdd:smart00986 149 FAAWNDLL 156
UDG pfam03167
Uracil DNA glycosylase superfamily;
51-205 1.54e-23

Uracil DNA glycosylase superfamily;


Pssm-ID: 397331  Cd Length: 154  Bit Score: 92.02  E-value: 1.54e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491993977   51 KDVKVVILGQDPYHGpNQAHGLSFSVKPGIVPPPSLVNMykELSQDVGfqipshgyliewAKQGVLLLNTVLTVEQGKAH 130
Cdd:pfam03167   6 PNAKVLIVGEAPGAD-EDATGLPFVGRAGNLLWKLLNAA--GLTRDLF------------SPQGVYITNVVKCRPGNRRK 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491993977  131 SHA---NIGWEtFTDKVIHQLNLHrenlVFLLWGSHAQKK-----------GQFIDRSRHCVLTAPHPSPLSAHRgflgC 196
Cdd:pfam03167  71 PTSheiDACWP-YLEAEIELLRPR----VIVLLGKTAAKAllglkkitklrGKLIDLKGIPVLPTPHPSPLLRNK----L 141


                  ....*....
gi 491993977  197 RHFSKTNDY 205
Cdd:pfam03167 142 NPFLKANAW 150
UDG-like cd09593
uracil-DNA glycosylases (UDG) and related enzymes; Uracil-DNA glycosylases (UDGs) initiate ...
 55-189 7.86e-18

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: 76.27  E-value: 7.86e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491993977  55 VVILGQDPYHGPNQAHGLSfsvkpgivPPPSLVNMYKELSQDvgfqipshGYLIEWAKQGVLLLNTVLTVeQGKAHSHAN 134
Cdd:cd09593    1 VLIVGQNPGPHGARAGGVP--------PGPSGNRLWRLLAAA--------GGTPRLFRYGVGLTNTVPRG-PPGAAAGSE 63

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491993977 135 IGWETFTDKVIHQLNLHRENLVFLLWGSHAQKKGQFIDRSR-------HCVLTAPHPSPLSA 189
Cdd:cd09593   64 KKELRFCGRWLRKLLELLNPRVVVLLGKKAQEAYLAVLTSSkgapgkgTEVLVLPHPSPRNR 125
UDG-F1_NsUNG-like cd19373
Uracil DNA glycosylase family 1 subfamily, includes Nitratifractor salsuginis UNG and similar ...
 56-184 4.92e-03

Uracil DNA glycosylase family 1 subfamily, includes 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. Nitratifractor salsuginis UNG (NsaUNG) only exhibits robust enzymatic activity on uracil-containing DNAs, in particular double-stranded uracil-containing substrates, and does not act on hypoxanthine- and xanthine-containing substrates. NsUNG is not inhibited by Ugi protein that specifically inhibits conventional family 1 UDGs. 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.


Pssm-ID: 381688  Cd Length: 174  Bit Score: 36.73  E-value: 4.92e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491993977  56 VILGQDPYHGPNQAHGLSF---SVKpGIVPPPSL---VNMYKELSQDVGFQIPSHGYLIE-------------------- 109
Cdd:cd19373    2 ILFGQDPYPREKSATGYAFidgAVK-EIFSPKGLskeVNRATSLRNFIKMALVARGSLDPddlsqeaiakldksllvdti 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491993977 110 ------WAKQGVLLLNTVLTVE-QGKAHSHANiGWETFTDKVIHQLNLHRENLVflLWGSHAQKKGQFIDRSRHCVLTAP 182
Cdd:cd19373   81 delrenFEKSGVLLLNAALLFTsKEESNRHAR-AWRPFIEKLLEGLEAYGPELI--LFGAHAKEIKKLKSARGFPQVELE 157


                 ..
gi 491993977 183 HP 184
Cdd:cd19373  158 HP 159
 
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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