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Conserved domains on  [gi|492167823|ref|WP_005768577|]
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uracil-DNA glycosylase [Coxiella burnetii]

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

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];
9-222 1.24e-157

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


:

Pssm-ID: 440456  Cd Length: 221  Bit Score: 435.24  E-value: 1.24e-157
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492167823   9 TWQTVLGEEKQEPYFQEILDFVKKERKAGKIIYPPQKDIFNALKLTPYEAVKVVILGQDPYHGPNQAHGLAFSVRPGVPA 88
Cdd:COG0692    8 SWKEALAEEFEKPYFQALGAFLKAEYAAGKTIYPPGEDIFRAFNLTPFDDVKVVILGQDPYHGPGQAHGLSFSVPPGVPL 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492167823  89 PPSLQNIFKELHADLGVSIPSHGFLEKWAKQGVLLLNAALTVEAGKPQSHANIGWHRFTDKVIESLNDHPEGIVFLLWGS 168
Cdd:COG0692   88 PPSLRNIYKELEDDLGIPIPNHGDLTSWAEQGVLLLNTVLTVRAGQAGSHAGKGWETFTDAVIRALNARKEPVVFLLWGA 167
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 492167823 169 YAQKKSQLITNLRHRILKAPHPSPLSAARGFLGCRHFSKANQLLHEMGRGEIDW 222
Cdd:COG0692  168 YAQKKAALIDASKHLVLESPHPSPLSAHRGFFGSKPFSKANAYLEEQGKTPIDW 221
 
Name Accession Description Interval E-value
Ung COG0692
Uracil-DNA glycosylase [Replication, recombination and repair];
9-222 1.24e-157

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


Pssm-ID: 440456  Cd Length: 221  Bit Score: 435.24  E-value: 1.24e-157
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492167823   9 TWQTVLGEEKQEPYFQEILDFVKKERKAGKIIYPPQKDIFNALKLTPYEAVKVVILGQDPYHGPNQAHGLAFSVRPGVPA 88
Cdd:COG0692    8 SWKEALAEEFEKPYFQALGAFLKAEYAAGKTIYPPGEDIFRAFNLTPFDDVKVVILGQDPYHGPGQAHGLSFSVPPGVPL 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492167823  89 PPSLQNIFKELHADLGVSIPSHGFLEKWAKQGVLLLNAALTVEAGKPQSHANIGWHRFTDKVIESLNDHPEGIVFLLWGS 168
Cdd:COG0692   88 PPSLRNIYKELEDDLGIPIPNHGDLTSWAEQGVLLLNTVLTVRAGQAGSHAGKGWETFTDAVIRALNARKEPVVFLLWGA 167
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 492167823 169 YAQKKSQLITNLRHRILKAPHPSPLSAARGFLGCRHFSKANQLLHEMGRGEIDW 222
Cdd:COG0692  168 YAQKKAALIDASKHLVLESPHPSPLSAHRGFFGSKPFSKANAYLEEQGKTPIDW 221
PRK05254 PRK05254
uracil-DNA glycosylase; Provisional
1-224 4.20e-154

uracil-DNA glycosylase; Provisional


Pssm-ID: 235376  Cd Length: 224  Bit Score: 426.49  E-value: 4.20e-154
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492167823   1 MTTMAETQTWQTVLGEEKQEPYFQEILDFVKKERKAGKIIYPPQKDIFNALKLTPYEAVKVVILGQDPYHGPNQAHGLAF 80
Cdd:PRK05254   1 PMKMLLEPSWKEVLKPEFKKPYFQELLEFLRAERAAGKTIYPPGEDIFRAFNLTPFDDVKVVILGQDPYHGPGQAHGLSF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492167823  81 SVRPGVPAPPSLQNIFKELHADLGVSIPSHGFLEKWAKQGVLLLNAALTVEAGKPQSHANIGWHRFTDKVIESLNDHPEG 160
Cdd:PRK05254  81 SVPPGVPIPPSLRNIFKELEDDLGFPIPNHGDLTSWAEQGVLLLNTVLTVEAGQANSHAGKGWETFTDAVIKALNERREP 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 492167823 161 IVFLLWGSYAQKKSQLITNLRHRILKAPHPSPLSAARGFLGCRHFSKANQLLHEMGRGEIDWAL 224
Cdd:PRK05254 161 VVFILWGSHAQKKKALIDNSKHLILESPHPSPLSAHRGFFGSKHFSKANALLKQHGKTPIDWQL 224
UDG-F1-like cd10027
Uracil DNA glycosylase family 1 subfamily, includes Human uracil DNA glycosylase and similar ...
22-222 2.46e-136

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: 380.64  E-value: 2.46e-136
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492167823  22 YFQEILDFVKKERKAgKIIYPPQKDIFNALKLTPYEAVKVVILGQDPYHGPNQAHGLAFSVRPGVPAPPSLQNIFKELHA 101
Cdd:cd10027    1 YFKKLEAFLEEEYKK-KTIYPPKEDIFRAFELTPLDDVKVVILGQDPYHGPGQAHGLAFSVPPGVKIPPSLRNIFKELKS 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492167823 102 DLGVSIPSHGFLEKWAKQGVLLLNAALTVEAGKPQSHANIGWHRFTDKVIESLNDHPEGIVFLLWGSYAQKKSQLITNLR 181
Cdd:cd10027   80 DLGIFPPKHGDLSSWAKQGVLLLNTVLTVEAGKPGSHKNIGWETFTDAVIKALSEKNENVVFLLWGNHAQKKKKLIDKKK 159
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 492167823 182 HRILKAPHPSPLSAARGFLGCRHFSKANQLLHEMGRGEIDW 222
Cdd:cd10027  160 HLVLESSHPSPLSAYRGFFGSKHFSKANEYLKKHGKKPIDW 200
ung TIGR00628
uracil-DNA glycosylase; All proteins in this family for which functions are known are ...
10-217 4.20e-121

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: 342.66  E-value: 4.20e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492167823   10 WQTVLGEEKQEPYFQEILDFVKKERkAGKIIYPPQKDIFNALKLTPYEAVKVVILGQDPYHGPNQAHGLAFSVRPGVPAP 89
Cdd:TIGR00628   4 WRAFLQPEFKKPYFQELLAFYKRER-AQETVYPPKEDVFAWTRLCPPEDVKVVILGQDPYHGPGQAHGLAFSVKRGVPIP 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492167823   90 PSLQNIFKELHADLG-VSIPSHGFLEKWAKQGVLLLNAALTVEAGKPQSHANIGWHRFTDKVIESLNDHPEGIVFLLWGS 168
Cdd:TIGR00628  83 PSLKNIFKELEADYPdFPPPKHGCLEAWARQGVLLLNTVLTVRRGQPGSHSGLGWERFTDAVISRLSERLDGLVFMLWGA 162
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 492167823  169 YAQKKSQLITNLRHRILKAPHPSPLSAARGFLGCRHFSKANQLLHEMGR 217
Cdd:TIGR00628 163 HAQKKKSLIDAKKHLVLKSPHPSPLSARRGFFGCRHFSKANEYLEKHGK 211
UDG smart00986
Uracil DNA glycosylase superfamily;
53-212 2.14e-35

Uracil DNA glycosylase superfamily;


Pssm-ID: 214956  Cd Length: 156  Bit Score: 122.88  E-value: 2.14e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492167823    53 LTPYEAVKVVILGQDPY------HGP-NQAHGLAFSVRPGV----PAPPSLQNIFKELHADlgvsiPSHGFLEKWAKQGV 121
Cdd:smart00986   2 GTGDPNAKVLIVGQAPGaseedrGGPfVGAAGLLLSVMLGVaglpRLPPYLTNIVKCRPPD-----AGNRRPTSWELQGC 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492167823   122 LLlnAALTVEAGKPQSHANIGWHRFTDKVIESLNDHPegIVFLLWGSYAQKKSQLitnlrHRILKAPHPSPLSAARgfLG 201
Cdd:smart00986  77 LL--PWLTVELALARPHLILLLGKFAAQALLGLLRRP--LVFGLRGRVAQLKGKG-----HRVLPLPHPSPLNRNF--FP 145
                          170
                   ....*....|.
gi 492167823   202 CRHFSKANQLL 212
Cdd:smart00986 146 AKKFAAWNDLL 156
UDG pfam03167
Uracil DNA glycosylase superfamily;
57-209 1.01e-20

Uracil DNA glycosylase superfamily;


Pssm-ID: 397331  Cd Length: 154  Bit Score: 84.71  E-value: 1.01e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492167823   57 EAVKVVILGQDPYHGpNQAHGLAFSVRPGvpappslqNIFKELHADLGVSIPSHgflekwAKQGVLLLNAALTV--EAGK 134
Cdd:pfam03167   6 PNAKVLIVGEAPGAD-EDATGLPFVGRAG--------NLLWKLLNAAGLTRDLF------SPQGVYITNVVKCRpgNRRK 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492167823  135 PQSHA-NIGWhRFTDKVIESLNDHpegiVFLLWGSYAQK---KSQLITNLR--------HRILKAPHPSPLSAARgflgC 202
Cdd:pfam03167  71 PTSHEiDACW-PYLEAEIELLRPR----VIVLLGKTAAKallGLKKITKLRgklidlkgIPVLPTPHPSPLLRNK----L 141

                  ....*..
gi 492167823  203 RHFSKAN 209
Cdd:pfam03167 142 NPFLKAN 148
 
Name Accession Description Interval E-value
Ung COG0692
Uracil-DNA glycosylase [Replication, recombination and repair];
9-222 1.24e-157

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


Pssm-ID: 440456  Cd Length: 221  Bit Score: 435.24  E-value: 1.24e-157
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492167823   9 TWQTVLGEEKQEPYFQEILDFVKKERKAGKIIYPPQKDIFNALKLTPYEAVKVVILGQDPYHGPNQAHGLAFSVRPGVPA 88
Cdd:COG0692    8 SWKEALAEEFEKPYFQALGAFLKAEYAAGKTIYPPGEDIFRAFNLTPFDDVKVVILGQDPYHGPGQAHGLSFSVPPGVPL 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492167823  89 PPSLQNIFKELHADLGVSIPSHGFLEKWAKQGVLLLNAALTVEAGKPQSHANIGWHRFTDKVIESLNDHPEGIVFLLWGS 168
Cdd:COG0692   88 PPSLRNIYKELEDDLGIPIPNHGDLTSWAEQGVLLLNTVLTVRAGQAGSHAGKGWETFTDAVIRALNARKEPVVFLLWGA 167
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 492167823 169 YAQKKSQLITNLRHRILKAPHPSPLSAARGFLGCRHFSKANQLLHEMGRGEIDW 222
Cdd:COG0692  168 YAQKKAALIDASKHLVLESPHPSPLSAHRGFFGSKPFSKANAYLEEQGKTPIDW 221
PRK05254 PRK05254
uracil-DNA glycosylase; Provisional
1-224 4.20e-154

uracil-DNA glycosylase; Provisional


Pssm-ID: 235376  Cd Length: 224  Bit Score: 426.49  E-value: 4.20e-154
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492167823   1 MTTMAETQTWQTVLGEEKQEPYFQEILDFVKKERKAGKIIYPPQKDIFNALKLTPYEAVKVVILGQDPYHGPNQAHGLAF 80
Cdd:PRK05254   1 PMKMLLEPSWKEVLKPEFKKPYFQELLEFLRAERAAGKTIYPPGEDIFRAFNLTPFDDVKVVILGQDPYHGPGQAHGLSF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492167823  81 SVRPGVPAPPSLQNIFKELHADLGVSIPSHGFLEKWAKQGVLLLNAALTVEAGKPQSHANIGWHRFTDKVIESLNDHPEG 160
Cdd:PRK05254  81 SVPPGVPIPPSLRNIFKELEDDLGFPIPNHGDLTSWAEQGVLLLNTVLTVEAGQANSHAGKGWETFTDAVIKALNERREP 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 492167823 161 IVFLLWGSYAQKKSQLITNLRHRILKAPHPSPLSAARGFLGCRHFSKANQLLHEMGRGEIDWAL 224
Cdd:PRK05254 161 VVFILWGSHAQKKKALIDNSKHLILESPHPSPLSAHRGFFGSKHFSKANALLKQHGKTPIDWQL 224
UDG-F1-like cd10027
Uracil DNA glycosylase family 1 subfamily, includes Human uracil DNA glycosylase and similar ...
22-222 2.46e-136

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: 380.64  E-value: 2.46e-136
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492167823  22 YFQEILDFVKKERKAgKIIYPPQKDIFNALKLTPYEAVKVVILGQDPYHGPNQAHGLAFSVRPGVPAPPSLQNIFKELHA 101
Cdd:cd10027    1 YFKKLEAFLEEEYKK-KTIYPPKEDIFRAFELTPLDDVKVVILGQDPYHGPGQAHGLAFSVPPGVKIPPSLRNIFKELKS 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492167823 102 DLGVSIPSHGFLEKWAKQGVLLLNAALTVEAGKPQSHANIGWHRFTDKVIESLNDHPEGIVFLLWGSYAQKKSQLITNLR 181
Cdd:cd10027   80 DLGIFPPKHGDLSSWAKQGVLLLNTVLTVEAGKPGSHKNIGWETFTDAVIKALSEKNENVVFLLWGNHAQKKKKLIDKKK 159
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 492167823 182 HRILKAPHPSPLSAARGFLGCRHFSKANQLLHEMGRGEIDW 222
Cdd:cd10027  160 HLVLESSHPSPLSAYRGFFGSKHFSKANEYLKKHGKKPIDW 200
ung TIGR00628
uracil-DNA glycosylase; All proteins in this family for which functions are known are ...
10-217 4.20e-121

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: 342.66  E-value: 4.20e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492167823   10 WQTVLGEEKQEPYFQEILDFVKKERkAGKIIYPPQKDIFNALKLTPYEAVKVVILGQDPYHGPNQAHGLAFSVRPGVPAP 89
Cdd:TIGR00628   4 WRAFLQPEFKKPYFQELLAFYKRER-AQETVYPPKEDVFAWTRLCPPEDVKVVILGQDPYHGPGQAHGLAFSVKRGVPIP 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492167823   90 PSLQNIFKELHADLG-VSIPSHGFLEKWAKQGVLLLNAALTVEAGKPQSHANIGWHRFTDKVIESLNDHPEGIVFLLWGS 168
Cdd:TIGR00628  83 PSLKNIFKELEADYPdFPPPKHGCLEAWARQGVLLLNTVLTVRRGQPGSHSGLGWERFTDAVISRLSERLDGLVFMLWGA 162
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 492167823  169 YAQKKSQLITNLRHRILKAPHPSPLSAARGFLGCRHFSKANQLLHEMGR 217
Cdd:TIGR00628 163 HAQKKKSLIDAKKHLVLKSPHPSPLSARRGFFGCRHFSKANEYLEKHGK 211
PHA03347 PHA03347
uracil DNA glycosylase; Provisional
24-225 1.93e-85

uracil DNA glycosylase; Provisional


Pssm-ID: 177588  Cd Length: 252  Bit Score: 253.82  E-value: 1.93e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492167823  24 QEILDFVKKERKAgKIIYPPQKDIFNALKLTPYEAVKVVILGQDPYHGpNQAHGLAFSVRPGVPAPPSLQNIFKELHA-D 102
Cdd:PHA03347  45 LALLNCVRELRKQ-TVIYPPEDRIMAWSYLCDPEDIKVVILGQDPYHG-GQANGLAFSVAYGFPVPPSLRNIFAELHRsV 122
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492167823 103 LGVSIPSHGFLEKWAKQGVLLLNAALTVEAGKPQSHANIGWHRFTDKVIESLNDHPEGIVFLLWGSYAQKKSQLITNLRH 182
Cdd:PHA03347 123 PDFSPPDHGCLDAWARQGVLLLNTILTVEKGKPGSHSDLGWAWFTDYIISSLSEKLKACVFMLWGSKAIDKASLINSQKH 202
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 492167823 183 RILKAPHPSPLSAARG-------FLGCRHFSKANQLLHEMGRGEIDWALD 225
Cdd:PHA03347 203 LVLKAQHPSPLAANSTrsstwpkFLGCNHFVLANKYLTQHGKGPIDWNLE 252
PHA03202 PHA03202
uracil DNA glycosylase; Provisional
9-225 5.08e-78

uracil DNA glycosylase; Provisional


Pssm-ID: 165469  Cd Length: 313  Bit Score: 237.29  E-value: 5.08e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492167823   9 TWQTVLGEEKQEPYFQEILDFVKKeRKAGKIIYPPQKDIFNALKLTPYEAVKVVILGQDPYHGPNQAHGLAFSVRPGVPA 88
Cdd:PHA03202  99 SWRPILEREMQQPYVRLLLNEYKL-RCAREEVFPPKEDIFAWTRFSPPEKVRVVIVGQDPYHAPGQAHGLAFSVRKGVPV 177
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492167823  89 PPSLQNIFKELHADL-GVSIPSHGFLEKWAKQGVLLLNAALTVEAGKPQSHANIGWHRFTDKVIESLNDHPEGIVFLLWG 167
Cdd:PHA03202 178 PPSLRNIYSAVQKSYpSFRPPMHGFLEKWAEQGVLLINTTLTVARGKPGSHATLGWHRLVRAVIDRLCTTSQGLVFMLWG 257
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 492167823 168 SYAQKKSQlITNLRHRILKAPHPSPLSAArGFLGCRHFSKANQLLHEMGRGEIDWALD 225
Cdd:PHA03202 258 AHAQKSCS-PNRQHHLVLTYGHPSPLSRV-NFRDCPHFLEANAYLTKTGRKPVDWQIE 313
PHA03200 PHA03200
uracil DNA glycosylase; Provisional
24-225 7.06e-69

uracil DNA glycosylase; Provisional


Pssm-ID: 165467  Cd Length: 255  Bit Score: 211.89  E-value: 7.06e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492167823  24 QEILDFVKKERKAGkIIYPPQKDIFNALKLTPYEAVKVVILGQDPYHGpNQAHGLAFSVRPGVPAPPSLQNIFKELHADL 103
Cdd:PHA03200  51 RRIVDAVDRDRQRL-TVYPPPEDVHRWSRLCSPEDVKVVIVGQDPYHD-GSACGLAFGTVRGRSAPPSLKNVFRELERTV 128
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492167823 104 -GVSIPSHGFLEKWAKQGVLLLNAALTVEAGKPQSHANIGWHRFTDKVIESLNDHPEGIVFLLWGSYAQKKSQLITNLRH 182
Cdd:PHA03200 129 pNFSRPDSGCLDSWCRQGVLLLNTVFTVVHGQPGSHEALGWQTLSDRVISRLSEKREHLVFMLWGAQAQKLEYLIDSRKH 208
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 492167823 183 RILKAPHPSP--LSAARGFLGCRHFSKANQLLHEMGRGEIDWALD 225
Cdd:PHA03200 209 LILKSAHPSPrvKGARTPFIGNNHFVLANEYLSTHGKRPIDWNIL 253
PHA03199 PHA03199
uracil DNA glycosylase; Provisional
10-224 4.99e-68

uracil DNA glycosylase; Provisional


Pssm-ID: 165466  Cd Length: 304  Bit Score: 211.40  E-value: 4.99e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492167823  10 WQTVLGEEKQEPYFQEILDFVKKERKAGKIIYPPQKDIFNALKLTPYEAVKVVILGQDPYHGPNQAHGLAFSVRPGVPAP 89
Cdd:PHA03199  91 WHDLLRDEFEEPYAKGIFEEYNQLLNNGEEIFPIKGDIFAWTRFCGPEKIRVVIIGQDPYHGAGHAHGLAFSVKRGIPIP 170
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492167823  90 PSLQNIFKELHADL-GVSIPSHGFLEKWAKQGVLLLNAALTVEAGKPQSHANIGWHRFTDKVIESLNDHPEGIVFLLWGS 168
Cdd:PHA03199 171 PSLKNIFAALMESYpHLPLPTHGCLDNWARQGVLLLNTTLTVKRGTPGSHFYLGWDMLIKRMLKRLCENRTGLVFMLWGA 250
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 492167823 169 YAQKKSQliTNLR-HRILKAPHPSPLSAARgFLGCRHFSKANQLLHEMGRGEIDWAL 224
Cdd:PHA03199 251 HAQKTIQ--PNPRcHLVLTHAHPSPLSRSE-FRNCKHFLQANEYFLKKGEPEIDWSI 304
PHA03204 PHA03204
uracil DNA glycosylase; Provisional
10-224 8.52e-68

uracil DNA glycosylase; Provisional


Pssm-ID: 165471  Cd Length: 322  Bit Score: 211.36  E-value: 8.52e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492167823  10 WQTVLGEEKQEPYFQEILdfVKKERKAG-KIIYPPQKDIFNALKLTPYEAVKVVILGQDPYHGPNQAHGLAFSVRPGVPA 88
Cdd:PHA03204 106 WKEILLPELCCPTGSKIL--AEYERRARyEEVYPPKSDIFAWTRYCAPDHVKVVIVGQDPYANPGQAHGLAFSVKPGSPI 183
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492167823  89 PPSLQNIFKELHADL-GVSIPSHGFLEKWAKQGVLLLNAALTVEAGKPQSHANIGWHRFTDKVIESLNDHPEGIVFLLWG 167
Cdd:PHA03204 184 PPSLKNILAAVKACYpSIELGSHGCLEDWAKRGVLLLNSVLTVKRGDPGSHHSVGWQILVRNVLRRLSQSTRGIVFMLWG 263
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 492167823 168 SYAQKKS-QLITNLRHRILKAPHPSPLSaARGFLGCRHFSKANQLLHEMGRGEIDWAL 224
Cdd:PHA03204 264 AQAQTMYfQTDNDDRHLVLKYSHPSPLS-RKPFAHCTHFKDANEFLCKMGKGAIDWSL 320
PHA03201 PHA03201
uracil DNA glycosylase; Provisional
10-223 4.61e-64

uracil DNA glycosylase; Provisional


Pssm-ID: 165468  Cd Length: 318  Bit Score: 201.66  E-value: 4.61e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492167823  10 WQTVLGEEKQEPYFQEILDFVKKERKAGKIIyPPQKDIFNALKLTPYEAVKVVILGQDPYHGPNQAHGLAFSVRPGVPAP 89
Cdd:PHA03201 106 WRPLLEPELANPLTARLMAEYERRCRTEEVL-PPREDVFSWTRYCTPDEVRVVIIGQDPYHQPGQAHGLAFSVRPGTPAP 184
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492167823  90 PSLQNIF---KELHADLGVSipSHGFLEKWAKQGVLLLNAALTVEAGKPQSHANIGWHRFTDKVIESLNDHPEGIVFLLW 166
Cdd:PHA03201 185 PSLRNILaavRNCCPDARMS--GHGCLEKWARGGVLLLNTTLTVRRGEPASHAKIGWDRFVGSVVRRLAASRPGLVFMLW 262
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 492167823 167 GSYAQkkSQLITNLR-HRILKAPHPSPLSAARgFLGCRHFSKANQLLHEMGRGEIDWA 223
Cdd:PHA03201 263 GAHAQ--NAIRPDPRvHRVLTYSHPSPLSKVP-FGSCRHFCLANQYLRERSLAPIDWS 317
UDG-F1-like cd19371
Uracil DNA glycosylase family 1, includes Human uracil DNA glycosylase, Vaccinia virus protein ...
61-194 1.02e-54

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: 171.36  E-value: 1.02e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492167823  61 VVILGQDPYHGPNQAHGLAFSVRPGVPAPPSLQNIFKELHADLGV-SIPSHGFLEKWAKQGVLLLNAALTVEAGKPQSHA 139
Cdd:cd19371    1 VVIIGQDPYPSPGHAGGLAFSVTSEVPPPKSLRNIYKELERDYSSfLPPGNGTLEFWARQGVLLLNAALTCESGKPKSHY 80
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 492167823 140 nIGWHRFTDKVIESLNDHPEGIVFLLWGSYAQKKSQLITNLRHRILKAPHPSPLS 194
Cdd:cd19371   81 -LLWEPFIKAFIRYISAHNKGLVFLLFGSDAQKLRKKINGRNVHVFKADHPSPAD 134
UDG smart00986
Uracil DNA glycosylase superfamily;
53-212 2.14e-35

Uracil DNA glycosylase superfamily;


Pssm-ID: 214956  Cd Length: 156  Bit Score: 122.88  E-value: 2.14e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492167823    53 LTPYEAVKVVILGQDPY------HGP-NQAHGLAFSVRPGV----PAPPSLQNIFKELHADlgvsiPSHGFLEKWAKQGV 121
Cdd:smart00986   2 GTGDPNAKVLIVGQAPGaseedrGGPfVGAAGLLLSVMLGVaglpRLPPYLTNIVKCRPPD-----AGNRRPTSWELQGC 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492167823   122 LLlnAALTVEAGKPQSHANIGWHRFTDKVIESLNDHPegIVFLLWGSYAQKKSQLitnlrHRILKAPHPSPLSAARgfLG 201
Cdd:smart00986  77 LL--PWLTVELALARPHLILLLGKFAAQALLGLLRRP--LVFGLRGRVAQLKGKG-----HRVLPLPHPSPLNRNF--FP 145
                          170
                   ....*....|.
gi 492167823   202 CRHFSKANQLL 212
Cdd:smart00986 146 AKKFAAWNDLL 156
UDG pfam03167
Uracil DNA glycosylase superfamily;
57-209 1.01e-20

Uracil DNA glycosylase superfamily;


Pssm-ID: 397331  Cd Length: 154  Bit Score: 84.71  E-value: 1.01e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492167823   57 EAVKVVILGQDPYHGpNQAHGLAFSVRPGvpappslqNIFKELHADLGVSIPSHgflekwAKQGVLLLNAALTV--EAGK 134
Cdd:pfam03167   6 PNAKVLIVGEAPGAD-EDATGLPFVGRAG--------NLLWKLLNAAGLTRDLF------SPQGVYITNVVKCRpgNRRK 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492167823  135 PQSHA-NIGWhRFTDKVIESLNDHpegiVFLLWGSYAQK---KSQLITNLR--------HRILKAPHPSPLSAARgflgC 202
Cdd:pfam03167  71 PTSHEiDACW-PYLEAEIELLRPR----VIVLLGKTAAKallGLKKITKLRgklidlkgIPVLPTPHPSPLLRNK----L 141

                  ....*..
gi 492167823  203 RHFSKAN 209
Cdd:pfam03167 142 NPFLKAN 148
UDG-like cd09593
uracil-DNA glycosylases (UDG) and related enzymes; Uracil-DNA glycosylases (UDGs) initiate ...
61-195 8.51e-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: 78.97  E-value: 8.51e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492167823  61 VVILGQDPYHGPNQAHglafsvrpGVPAPPSLQNIFKELHADlgvsipshGFLEKWAKQGVLLLNAALTVEAGKPQSHaN 140
Cdd:cd09593    1 VLIVGQNPGPHGARAG--------GVPPGPSGNRLWRLLAAA--------GGTPRLFRYGVGLTNTVPRGPPGAAAGS-E 63
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 492167823 141 IGWHRFTDKVIESLNDHPEGIVFLLWGSYAQKK-------SQLITNLRHRILKAPHPSPLSA 195
Cdd:cd09593   64 KKELRFCGRWLRKLLELLNPRVVVLLGKKAQEAylavltsSKGAPGKGTEVLVLPHPSPRNR 125
UDG-F1_NsUNG-like cd19373
Uracil DNA glycosylase family 1 subfamily, includes Nitratifractor salsuginis UNG and similar ...
62-190 2.81e-05

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: 43.28  E-value: 2.81e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492167823  62 VILGQDPYHGPNQAHGLAF---SVRP---------GVPAPPSLQNIFKELhadlgvsIPSHGFL---------------- 113
Cdd:cd19373    2 ILFGQDPYPREKSATGYAFidgAVKEifspkglskEVNRATSLRNFIKMA-------LVARGSLdpddlsqeaiakldks 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492167823 114 ----------EKWAKQGVLLLNAALTVEA-GKPQSHANiGWHRFTDKVIESLNDHpeGIVFLLWGSYAQKKSQLITNLRH 182
Cdd:cd19373   75 llvdtidelrENFEKSGVLLLNAALLFTSkEESNRHAR-AWRPFIEKLLEGLEAY--GPELILFGAHAKEIKKLKSARGF 151

                 ....*...
gi 492167823 183 RILKAPHP 190
Cdd:cd19373  152 PQVELEHP 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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