|
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
|
|
|