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Conserved domains on  [gi|2330900340|ref|WP_265639752|]
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uracil-DNA glycosylase [Citrobacter portucalensis]

Protein Classification

uracil-DNA glycosylase( domain architecture ID 10012283)

Family 1 uracil-DNA glycosylase, similar to Escherichia coli UNG and human UNG1 and -2, and which catalyzes the removal of uracil from DNA

EC:  3.2.2.27
Gene Ontology:  GO:0004844
PubMed:  11716455

Graphical summary

 Zoom to residue level

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List of domain hits

Name Accession Description Interval E-value
PRK05254 PRK05254
uracil-DNA glycosylase; Provisional
1-220 6.16e-154

uracil-DNA glycosylase; Provisional


:

Pssm-ID: 235376  Cd Length: 224  Bit Score: 426.11  E-value: 6.16e-154
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2330900340   1 MATELTWHDVLAEEKQQPYFVNTLHTVAGERQSGMTIYPPQKDVFNAFRFTELGDVKVVILGQDPYHGPGQAHGLAFSVR 80
Cdd:PRK05254    4 MLLEPSWKEVLKPEFKKPYFQELLEFLRAERAAGKTIYPPGEDIFRAFNLTPFDDVKVVILGQDPYHGPGQAHGLSFSVP 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2330900340  81 PGIATPPSLLNMYKELEATIpGFTRPTHGYLESWARQGVLLLNTVLTVRAGQAHSHASLGWETFTDKVISLINQHREGVV 160
Cdd:PRK05254   84 PGVPIPPSLRNIFKELEDDL-GFPIPNHGDLTSWAEQGVLLLNTVLTVEAGQANSHAGKGWETFTDAVIKALNERREPVV 162
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2330900340 161 FLLWGSHAQKKGAIIDTHRHHVLKAPHPSPLSAHRGFFGCNHFVLANEWLEQRGEKPIDW 220
Cdd:PRK05254  163 FILWGSHAQKKKALIDNSKHLILESPHPSPLSAHRGFFGSKHFSKANALLKQHGKTPIDW 222
 
Name Accession Description Interval E-value
PRK05254 PRK05254
uracil-DNA glycosylase; Provisional
1-220 6.16e-154

uracil-DNA glycosylase; Provisional


Pssm-ID: 235376  Cd Length: 224  Bit Score: 426.11  E-value: 6.16e-154
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2330900340   1 MATELTWHDVLAEEKQQPYFVNTLHTVAGERQSGMTIYPPQKDVFNAFRFTELGDVKVVILGQDPYHGPGQAHGLAFSVR 80
Cdd:PRK05254    4 MLLEPSWKEVLKPEFKKPYFQELLEFLRAERAAGKTIYPPGEDIFRAFNLTPFDDVKVVILGQDPYHGPGQAHGLSFSVP 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2330900340  81 PGIATPPSLLNMYKELEATIpGFTRPTHGYLESWARQGVLLLNTVLTVRAGQAHSHASLGWETFTDKVISLINQHREGVV 160
Cdd:PRK05254   84 PGVPIPPSLRNIFKELEDDL-GFPIPNHGDLTSWAEQGVLLLNTVLTVEAGQANSHAGKGWETFTDAVIKALNERREPVV 162
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2330900340 161 FLLWGSHAQKKGAIIDTHRHHVLKAPHPSPLSAHRGFFGCNHFVLANEWLEQRGEKPIDW 220
Cdd:PRK05254  163 FILWGSHAQKKKALIDNSKHLILESPHPSPLSAHRGFFGSKHFSKANALLKQHGKTPIDW 222
Ung COG0692
Uracil-DNA glycosylase [Replication, recombination and repair];
4-220 8.56e-154

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


Pssm-ID: 440456  Cd Length: 221  Bit Score: 425.61  E-value: 8.56e-154
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2330900340   4 ELTWHDVLAEEKQQPYFVNTLHTVAGERQSGMTIYPPQKDVFNAFRFTELGDVKVVILGQDPYHGPGQAHGLAFSVRPGI 83
Cdd:COG0692     6 EPSWKEALAEEFEKPYFQALGAFLKAEYAAGKTIYPPGEDIFRAFNLTPFDDVKVVILGQDPYHGPGQAHGLSFSVPPGV 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2330900340  84 ATPPSLLNMYKELEATIpGFTRPTHGYLESWARQGVLLLNTVLTVRAGQAHSHASLGWETFTDKVISLINQHREGVVFLL 163
Cdd:COG0692    86 PLPPSLRNIYKELEDDL-GIPIPNHGDLTSWAEQGVLLLNTVLTVRAGQAGSHAGKGWETFTDAVIRALNARKEPVVFLL 164
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2330900340 164 WGSHAQKKGAIIDTHRHHVLKAPHPSPLSAHRGFFGCNHFVLANEWLEQRGEKPIDW 220
Cdd:COG0692   165 WGAYAQKKAALIDASKHLVLESPHPSPLSAHRGFFGSKPFSKANAYLEEQGKTPIDW 221
UDG-F1-like cd10027
Uracil DNA glycosylase family 1 subfamily, includes Human uracil DNA glycosylase and similar ...
19-220 4.31e-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: 374.86  E-value: 4.31e-134
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2330900340  19 YFVNTLHTVAGERQSGmTIYPPQKDVFNAFRFTELGDVKVVILGQDPYHGPGQAHGLAFSVRPGIATPPSLLNMYKELEA 98
Cdd:cd10027     1 YFKKLEAFLEEEYKKK-TIYPPKEDIFRAFELTPLDDVKVVILGQDPYHGPGQAHGLAFSVPPGVKIPPSLRNIFKELKS 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2330900340  99 TIPGFTrPTHGYLESWARQGVLLLNTVLTVRAGQAHSHASLGWETFTDKVISLINQHREGVVFLLWGSHAQKKGAIIDTH 178
Cdd:cd10027    80 DLGIFP-PKHGDLSSWAKQGVLLLNTVLTVEAGKPGSHKNIGWETFTDAVIKALSEKNENVVFLLWGNHAQKKKKLIDKK 158
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 2330900340 179 RHHVLKAPHPSPLSAHRGFFGCNHFVLANEWLEQRGEKPIDW 220
Cdd:cd10027   159 KHLVLESSHPSPLSAYRGFFGSKHFSKANEYLKKHGKKPIDW 200
ung TIGR00628
uracil-DNA glycosylase; All proteins in this family for which functions are known are ...
7-215 7.81e-129

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: 361.92  E-value: 7.81e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2330900340   7 WHDVLAEEKQQPYFVNTLHTVAGERQSGmTIYPPQKDVFNAFRFTELGDVKVVILGQDPYHGPGQAHGLAFSVRPGIATP 86
Cdd:TIGR00628   4 WRAFLQPEFKKPYFQELLAFYKRERAQE-TVYPPKEDVFAWTRLCPPEDVKVVILGQDPYHGPGQAHGLAFSVKRGVPIP 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2330900340  87 PSLLNMYKELEATIPGFTRPTHGYLESWARQGVLLLNTVLTVRAGQAHSHASLGWETFTDKVISLINQHREGVVFLLWGS 166
Cdd:TIGR00628  83 PSLKNIFKELEADYPDFPPPKHGCLEAWARQGVLLLNTVLTVRRGQPGSHSGLGWERFTDAVISRLSERLDGLVFMLWGA 162
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 2330900340 167 HAQKKGAIIDTHRHHVLKAPHPSPLSAHRGFFGCNHFVLANEWLEQRGE 215
Cdd:TIGR00628 163 HAQKKKSLIDAKKHLVLKSPHPSPLSARRGFFGCRHFSKANEYLEKHGK 211
UDG smart00986
Uracil DNA glycosylase superfamily;
55-210 2.58e-34

Uracil DNA glycosylase superfamily;


Pssm-ID: 214956  Cd Length: 156  Bit Score: 120.18  E-value: 2.58e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2330900340   55 DVKVVILGQDPYHGPGQ-------AHGLAFSVRPGIA----TPPSLLNMYKELEATIPgftrptHGYLESWARQGVLLln 123
Cdd:smart00986   7 NAKVLIVGQAPGASEEDrggpfvgAAGLLLSVMLGVAglprLPPYLTNIVKCRPPDAG------NRRPTSWELQGCLL-- 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2330900340  124 TVLTVRAGQAHSHASLGWETFTDKVISLINqhREGVVFLLWGSHAQKKGaiidtHRHHVLKAPHPSPLSAHRgfFGCNHF 203
Cdd:smart00986  79 PWLTVELALARPHLILLLGKFAAQALLGLL--RRPLVFGLRGRVAQLKG-----KGHRVLPLPHPSPLNRNF--FPAKKF 149

                   ....*..
gi 2330900340  204 VLANEWL 210
Cdd:smart00986 150 AAWNDLL 156
UDG pfam03167
Uracil DNA glycosylase superfamily;
55-211 4.55e-25

Uracil DNA glycosylase superfamily;


Pssm-ID: 397331  Cd Length: 154  Bit Score: 96.26  E-value: 4.55e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2330900340  55 DVKVVILGQDPYHGpGQAHGLAFSVRPGiATPPSLLNmykeleatIPGFTRPTHgyleswARQGVLLLNTVLTVR--AGQ 132
Cdd:pfam03167   7 NAKVLIVGEAPGAD-EDATGLPFVGRAG-NLLWKLLN--------AAGLTRDLF------SPQGVYITNVVKCRPgnRRK 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2330900340 133 AHSHA-SLGWEtFTDKVISLINQHregvVFLLWGSHAQKK-----------GAIIDTHRHHVLKAPHPSPLSAHRgffgC 200
Cdd:pfam03167  71 PTSHEiDACWP-YLEAEIELLRPR----VIVLLGKTAAKAllglkkitklrGKLIDLKGIPVLPTPHPSPLLRNK----L 141
                         170
                  ....*....|.
gi 2330900340 201 NHFVLANEWLE 211
Cdd:pfam03167 142 NPFLKANAWED 152
 
Name Accession Description Interval E-value
PRK05254 PRK05254
uracil-DNA glycosylase; Provisional
1-220 6.16e-154

uracil-DNA glycosylase; Provisional


Pssm-ID: 235376  Cd Length: 224  Bit Score: 426.11  E-value: 6.16e-154
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2330900340   1 MATELTWHDVLAEEKQQPYFVNTLHTVAGERQSGMTIYPPQKDVFNAFRFTELGDVKVVILGQDPYHGPGQAHGLAFSVR 80
Cdd:PRK05254    4 MLLEPSWKEVLKPEFKKPYFQELLEFLRAERAAGKTIYPPGEDIFRAFNLTPFDDVKVVILGQDPYHGPGQAHGLSFSVP 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2330900340  81 PGIATPPSLLNMYKELEATIpGFTRPTHGYLESWARQGVLLLNTVLTVRAGQAHSHASLGWETFTDKVISLINQHREGVV 160
Cdd:PRK05254   84 PGVPIPPSLRNIFKELEDDL-GFPIPNHGDLTSWAEQGVLLLNTVLTVEAGQANSHAGKGWETFTDAVIKALNERREPVV 162
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2330900340 161 FLLWGSHAQKKGAIIDTHRHHVLKAPHPSPLSAHRGFFGCNHFVLANEWLEQRGEKPIDW 220
Cdd:PRK05254  163 FILWGSHAQKKKALIDNSKHLILESPHPSPLSAHRGFFGSKHFSKANALLKQHGKTPIDW 222
Ung COG0692
Uracil-DNA glycosylase [Replication, recombination and repair];
4-220 8.56e-154

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


Pssm-ID: 440456  Cd Length: 221  Bit Score: 425.61  E-value: 8.56e-154
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2330900340   4 ELTWHDVLAEEKQQPYFVNTLHTVAGERQSGMTIYPPQKDVFNAFRFTELGDVKVVILGQDPYHGPGQAHGLAFSVRPGI 83
Cdd:COG0692     6 EPSWKEALAEEFEKPYFQALGAFLKAEYAAGKTIYPPGEDIFRAFNLTPFDDVKVVILGQDPYHGPGQAHGLSFSVPPGV 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2330900340  84 ATPPSLLNMYKELEATIpGFTRPTHGYLESWARQGVLLLNTVLTVRAGQAHSHASLGWETFTDKVISLINQHREGVVFLL 163
Cdd:COG0692    86 PLPPSLRNIYKELEDDL-GIPIPNHGDLTSWAEQGVLLLNTVLTVRAGQAGSHAGKGWETFTDAVIRALNARKEPVVFLL 164
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2330900340 164 WGSHAQKKGAIIDTHRHHVLKAPHPSPLSAHRGFFGCNHFVLANEWLEQRGEKPIDW 220
Cdd:COG0692   165 WGAYAQKKAALIDASKHLVLESPHPSPLSAHRGFFGSKPFSKANAYLEEQGKTPIDW 221
UDG-F1-like cd10027
Uracil DNA glycosylase family 1 subfamily, includes Human uracil DNA glycosylase and similar ...
19-220 4.31e-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: 374.86  E-value: 4.31e-134
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2330900340  19 YFVNTLHTVAGERQSGmTIYPPQKDVFNAFRFTELGDVKVVILGQDPYHGPGQAHGLAFSVRPGIATPPSLLNMYKELEA 98
Cdd:cd10027     1 YFKKLEAFLEEEYKKK-TIYPPKEDIFRAFELTPLDDVKVVILGQDPYHGPGQAHGLAFSVPPGVKIPPSLRNIFKELKS 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2330900340  99 TIPGFTrPTHGYLESWARQGVLLLNTVLTVRAGQAHSHASLGWETFTDKVISLINQHREGVVFLLWGSHAQKKGAIIDTH 178
Cdd:cd10027    80 DLGIFP-PKHGDLSSWAKQGVLLLNTVLTVEAGKPGSHKNIGWETFTDAVIKALSEKNENVVFLLWGNHAQKKKKLIDKK 158
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 2330900340 179 RHHVLKAPHPSPLSAHRGFFGCNHFVLANEWLEQRGEKPIDW 220
Cdd:cd10027   159 KHLVLESSHPSPLSAYRGFFGSKHFSKANEYLKKHGKKPIDW 200
ung TIGR00628
uracil-DNA glycosylase; All proteins in this family for which functions are known are ...
7-215 7.81e-129

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: 361.92  E-value: 7.81e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2330900340   7 WHDVLAEEKQQPYFVNTLHTVAGERQSGmTIYPPQKDVFNAFRFTELGDVKVVILGQDPYHGPGQAHGLAFSVRPGIATP 86
Cdd:TIGR00628   4 WRAFLQPEFKKPYFQELLAFYKRERAQE-TVYPPKEDVFAWTRLCPPEDVKVVILGQDPYHGPGQAHGLAFSVKRGVPIP 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2330900340  87 PSLLNMYKELEATIPGFTRPTHGYLESWARQGVLLLNTVLTVRAGQAHSHASLGWETFTDKVISLINQHREGVVFLLWGS 166
Cdd:TIGR00628  83 PSLKNIFKELEADYPDFPPPKHGCLEAWARQGVLLLNTVLTVRRGQPGSHSGLGWERFTDAVISRLSERLDGLVFMLWGA 162
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 2330900340 167 HAQKKGAIIDTHRHHVLKAPHPSPLSAHRGFFGCNHFVLANEWLEQRGE 215
Cdd:TIGR00628 163 HAQKKKSLIDAKKHLVLKSPHPSPLSARRGFFGCRHFSKANEYLEKHGK 211
PHA03347 PHA03347
uracil DNA glycosylase; Provisional
21-220 1.19e-91

uracil DNA glycosylase; Provisional


Pssm-ID: 177588  Cd Length: 252  Bit Score: 269.61  E-value: 1.19e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2330900340  21 VNTLHTVAGERQSgMTIYPPQKDVFNAFRFTELGDVKVVILGQDPYHGpGQAHGLAFSVRPGIATPPSLLNMYKELEATI 100
Cdd:PHA03347   45 LALLNCVRELRKQ-TVIYPPEDRIMAWSYLCDPEDIKVVILGQDPYHG-GQANGLAFSVAYGFPVPPSLRNIFAELHRSV 122
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2330900340 101 PGFTRPTHGYLESWARQGVLLLNTVLTVRAGQAHSHASLGWETFTDKVISLINQHREGVVFLLWGSHAQKKGAIIDTHRH 180
Cdd:PHA03347  123 PDFSPPDHGCLDAWARQGVLLLNTILTVEKGKPGSHSDLGWAWFTDYIISSLSEKLKACVFMLWGSKAIDKASLINSQKH 202
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 2330900340 181 HVLKAPHPSPLSAHRG-------FFGCNHFVLANEWLEQRGEKPIDW 220
Cdd:PHA03347  203 LVLKAQHPSPLAANSTrsstwpkFLGCNHFVLANKYLTQHGKGPIDW 249
PHA03200 PHA03200
uracil DNA glycosylase; Provisional
21-220 9.28e-84

uracil DNA glycosylase; Provisional


Pssm-ID: 165467  Cd Length: 255  Bit Score: 249.64  E-value: 9.28e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2330900340  21 VNTLHTVAGERQSGMtIYPPQKDVFNAFRFTELGDVKVVILGQDPYHGpGQAHGLAFSVRPGIATPPSLLNMYKELEATI 100
Cdd:PHA03200   51 RRIVDAVDRDRQRLT-VYPPPEDVHRWSRLCSPEDVKVVIVGQDPYHD-GSACGLAFGTVRGRSAPPSLKNVFRELERTV 128
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2330900340 101 PGFTRPTHGYLESWARQGVLLLNTVLTVRAGQAHSHASLGWETFTDKVISLINQHREGVVFLLWGSHAQKKGAIIDTHRH 180
Cdd:PHA03200  129 PNFSRPDSGCLDSWCRQGVLLLNTVFTVVHGQPGSHEALGWQTLSDRVISRLSEKREHLVFMLWGAQAQKLEYLIDSRKH 208
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 2330900340 181 HVLKAPHPSP--LSAHRGFFGCNHFVLANEWLEQRGEKPIDW 220
Cdd:PHA03200  209 LILKSAHPSPrvKGARTPFIGNNHFVLANEYLSTHGKRPIDW 250
PHA03202 PHA03202
uracil DNA glycosylase; Provisional
6-221 1.14e-77

uracil DNA glycosylase; Provisional


Pssm-ID: 165469  Cd Length: 313  Bit Score: 236.13  E-value: 1.14e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2330900340   6 TWHDVLAEEKQQPYfVNTLHTVAGERQSGMTIYPPQKDVFNAFRFTELGDVKVVILGQDPYHGPGQAHGLAFSVRPGIAT 85
Cdd:PHA03202   99 SWRPILEREMQQPY-VRLLLNEYKLRCAREEVFPPKEDIFAWTRFSPPEKVRVVIVGQDPYHAPGQAHGLAFSVRKGVPV 177
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2330900340  86 PPSLLNMYKELEATIPGFTRPTHGYLESWARQGVLLLNTVLTVRAGQAHSHASLGWETFTDKVISLINQHREGVVFLLWG 165
Cdd:PHA03202  178 PPSLRNIYSAVQKSYPSFRPPMHGFLEKWAEQGVLLINTTLTVARGKPGSHATLGWHRLVRAVIDRLCTTSQGLVFMLWG 257
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2330900340 166 SHAQKKGAIIDTHrHHVLKAPHPSPLSaHRGFFGCNHFVLANEWLEQRGEKPIDWM 221
Cdd:PHA03202  258 AHAQKSCSPNRQH-HLVLTYGHPSPLS-RVNFRDCPHFLEANAYLTKTGRKPVDWQ 311
PHA03199 PHA03199
uracil DNA glycosylase; Provisional
7-220 1.26e-70

uracil DNA glycosylase; Provisional


Pssm-ID: 165466  Cd Length: 304  Bit Score: 217.95  E-value: 1.26e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2330900340   7 WHDVLAEEKQQPYFVNTLHTVAGERQSGMTIYPPQKDVFNAFRFTELGDVKVVILGQDPYHGPGQAHGLAFSVRPGIATP 86
Cdd:PHA03199   91 WHDLLRDEFEEPYAKGIFEEYNQLLNNGEEIFPIKGDIFAWTRFCGPEKIRVVIIGQDPYHGAGHAHGLAFSVKRGIPIP 170
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2330900340  87 PSLLNMYKELEATIPGFTRPTHGYLESWARQGVLLLNTVLTVRAGQAHSHASLGWETFTDKVISLINQHREGVVFLLWGS 166
Cdd:PHA03199  171 PSLKNIFAALMESYPHLPLPTHGCLDNWARQGVLLLNTTLTVKRGTPGSHFYLGWDMLIKRMLKRLCENRTGLVFMLWGA 250
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2330900340 167 HAQKKGAiIDTHRHHVLKAPHPSPLSaHRGFFGCNHFVLANEWLEQRGEKPIDW 220
Cdd:PHA03199  251 HAQKTIQ-PNPRCHLVLTHAHPSPLS-RSEFRNCKHFLQANEYFLKKGEPEIDW 302
PHA03201 PHA03201
uracil DNA glycosylase; Provisional
37-220 4.07e-69

uracil DNA glycosylase; Provisional


Pssm-ID: 165468  Cd Length: 318  Bit Score: 214.37  E-value: 4.07e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2330900340  37 IYPPQKDVFNAFRFTELGDVKVVILGQDPYHGPGQAHGLAFSVRPGIATPPSLLNMYKELEATIPGFTRPTHGYLESWAR 116
Cdd:PHA03201  135 VLPPREDVFSWTRYCTPDEVRVVIIGQDPYHQPGQAHGLAFSVRPGTPAPPSLRNILAAVRNCCPDARMSGHGCLEKWAR 214
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2330900340 117 QGVLLLNTVLTVRAGQAHSHASLGWETFTDKVISLINQHREGVVFLLWGSHAQKkgAI-IDTHRHHVLKAPHPSPLSahR 195
Cdd:PHA03201  215 GGVLLLNTTLTVRRGEPASHAKIGWDRFVGSVVRRLAASRPGLVFMLWGAHAQN--AIrPDPRVHRVLTYSHPSPLS--K 290
                         170       180
                  ....*....|....*....|....*.
gi 2330900340 196 GFFG-CNHFVLANEWLEQRGEKPIDW 220
Cdd:PHA03201  291 VPFGsCRHFCLANQYLRERSLAPIDW 316
PHA03204 PHA03204
uracil DNA glycosylase; Provisional
37-220 1.21e-63

uracil DNA glycosylase; Provisional


Pssm-ID: 165471  Cd Length: 322  Bit Score: 200.57  E-value: 1.21e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2330900340  37 IYPPQKDVFNAFRFTELGDVKVVILGQDPYHGPGQAHGLAFSVRPGIATPPSLLNMYKELEATIPGFTRPTHGYLESWAR 116
Cdd:PHA03204  135 VYPPKSDIFAWTRYCAPDHVKVVIVGQDPYANPGQAHGLAFSVKPGSPIPPSLKNILAAVKACYPSIELGSHGCLEDWAK 214
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2330900340 117 QGVLLLNTVLTVRAGQAHSHASLGWETFTDKVISLINQHREGVVFLLWGSHAQKKGAIIDTH-RHHVLKAPHPSPLSaHR 195
Cdd:PHA03204  215 RGVLLLNSVLTVKRGDPGSHHSVGWQILVRNVLRRLSQSTRGIVFMLWGAQAQTMYFQTDNDdRHLVLKYSHPSPLS-RK 293
                         170       180
                  ....*....|....*....|....*
gi 2330900340 196 GFFGCNHFVLANEWLEQRGEKPIDW 220
Cdd:PHA03204  294 PFAHCTHFKDANEFLCKMGKGAIDW 318
UDG-F1-like cd19371
Uracil DNA glycosylase family 1, includes Human uracil DNA glycosylase, Vaccinia virus protein ...
58-192 7.47e-60

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: 184.46  E-value: 7.47e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2330900340  58 VVILGQDPYHGPGQAHGLAFSVRPGIATPPSLLNMYKELEATIPGFTRPTHGYLESWARQGVLLLNTVLTVRAGQAHSHa 137
Cdd:cd19371     1 VVIIGQDPYPSPGHAGGLAFSVTSEVPPPKSLRNIYKELERDYSSFLPPGNGTLEFWARQGVLLLNAALTCESGKPKSH- 79
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2330900340 138 SLGWETFTDKVISLINQHREGVVFLLWGSHAQKKGAIIDTHRHHVLKAPHPSPLS 192
Cdd:cd19371    80 YLLWEPFIKAFIRYISAHNKGLVFLLFGSDAQKLRKKINGRNVHVFKADHPSPAD 134
UDG smart00986
Uracil DNA glycosylase superfamily;
55-210 2.58e-34

Uracil DNA glycosylase superfamily;


Pssm-ID: 214956  Cd Length: 156  Bit Score: 120.18  E-value: 2.58e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2330900340   55 DVKVVILGQDPYHGPGQ-------AHGLAFSVRPGIA----TPPSLLNMYKELEATIPgftrptHGYLESWARQGVLLln 123
Cdd:smart00986   7 NAKVLIVGQAPGASEEDrggpfvgAAGLLLSVMLGVAglprLPPYLTNIVKCRPPDAG------NRRPTSWELQGCLL-- 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2330900340  124 TVLTVRAGQAHSHASLGWETFTDKVISLINqhREGVVFLLWGSHAQKKGaiidtHRHHVLKAPHPSPLSAHRgfFGCNHF 203
Cdd:smart00986  79 PWLTVELALARPHLILLLGKFAAQALLGLL--RRPLVFGLRGRVAQLKG-----KGHRVLPLPHPSPLNRNF--FPAKKF 149

                   ....*..
gi 2330900340  204 VLANEWL 210
Cdd:smart00986 150 AAWNDLL 156
UDG pfam03167
Uracil DNA glycosylase superfamily;
55-211 4.55e-25

Uracil DNA glycosylase superfamily;


Pssm-ID: 397331  Cd Length: 154  Bit Score: 96.26  E-value: 4.55e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2330900340  55 DVKVVILGQDPYHGpGQAHGLAFSVRPGiATPPSLLNmykeleatIPGFTRPTHgyleswARQGVLLLNTVLTVR--AGQ 132
Cdd:pfam03167   7 NAKVLIVGEAPGAD-EDATGLPFVGRAG-NLLWKLLN--------AAGLTRDLF------SPQGVYITNVVKCRPgnRRK 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2330900340 133 AHSHA-SLGWEtFTDKVISLINQHregvVFLLWGSHAQKK-----------GAIIDTHRHHVLKAPHPSPLSAHRgffgC 200
Cdd:pfam03167  71 PTSHEiDACWP-YLEAEIELLRPR----VIVLLGKTAAKAllglkkitklrGKLIDLKGIPVLPTPHPSPLLRNK----L 141
                         170
                  ....*....|.
gi 2330900340 201 NHFVLANEWLE 211
Cdd:pfam03167 142 NPFLKANAWED 152
UDG-like cd09593
uracil-DNA glycosylases (UDG) and related enzymes; Uracil-DNA glycosylases (UDGs) initiate ...
58-193 1.84e-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: 80.51  E-value: 1.84e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2330900340  58 VVILGQDPYHGPGQAHGLAFsvrpgiatPPSLLNMYKELEATIPGFtrpthgyleSWARQGVLLLNTVLTVRAGQAHSHA 137
Cdd:cd09593     1 VLIVGQNPGPHGARAGGVPP--------GPSGNRLWRLLAAAGGTP---------RLFRYGVGLTNTVPRGPPGAAAGSE 63
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2330900340 138 SlGWETFTDKVISLINQHREGVVFLLWGSHAQKKG-------AIIDTHRHHVLKAPHPSPLSA 193
Cdd:cd09593    64 K-KELRFCGRWLRKLLELLNPRVVVLLGKKAQEAYlavltssKGAPGKGTEVLVLPHPSPRNR 125
UDG_F1_VAVC_D4-like cd19372
Uracil DNA glycosylase family 1 subfamily, includes Vaccinia virus protein D4 and similar ...
39-220 3.25e-03

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: 37.42  E-value: 3.25e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2330900340  39 PPQKDVFNAFRfTELGDVKVVILGQDPYhgPGQAHGLAFSvrpgiaTPPSLLNMYKELEATIPGFTRPTH--GYlESWAR 116
Cdd:cd19372    26 PIPENFFKQLK-QPLRDKRVCICGIDPY--PTDATGVPFE------SPDFSKKTIRAIAEAISRRTGVSLykGY-NFALV 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2330900340 117 QGVLLLNTVLTVRAGQAHSHAsLGWETFTDKVISLINQHREgVVFLLWGSHAQKKGAIIDTHRhHVLKAPHPSplSAHRG 196
Cdd:cd19372    96 EGVLAWNYYLSCREGETKSHA-IHWERISKLLLQHIAKYVS-VLYCLGKTDFSNVRARLEVPV-TVVVGYHPA--ARDGQ 170
                         170       180
                  ....*....|....*....|....
gi 2330900340 197 FFGCNHFVLANEWLEQRGEKPIDW 220
Cdd:cd19372   171 FDKERAFEIVNVLLELNGKPPVNW 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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