|
Name |
Accession |
Description |
Interval |
E-value |
| Ung |
COG0692 |
Uracil-DNA glycosylase [Replication, recombination and repair]; |
8-226 |
1.15e-167 |
|
Uracil-DNA glycosylase [Replication, recombination and repair];
Pssm-ID: 440456 Cd Length: 221 Bit Score: 460.67 E-value: 1.15e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595947 8 IKLEASWKEALREEFDKPYMKQLGEFLRQEKAAGKVIFPPGPLIFNALNTTPLENVKVVIIGQDPYHGPGQAHGLCFSVQ 87
Cdd:COG0692 3 VLLEPSWKEALAEEFEKPYFQALGAFLKAEYAAGKTIYPPGEDIFRAFNLTPFDDVKVVILGQDPYHGPGQAHGLSFSVP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595947 88 PGVPTPPSLQNIYKELNRDLNIPIPNNGYLQRWAEQGVLLLNTSLTVEQAKAGSHANAGWQPFTDRVIEVVNERCERLVF 167
Cdd:COG0692 83 PGVPLPPSLRNIYKELEDDLGIPIPNHGDLTSWAEQGVLLLNTVLTVRAGQAGSHAGKGWETFTDAVIRALNARKEPVVF 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 15595947 168 LLWGSHAQSKQKLIDPQRHLILKSAHPSPLSAYRGFLGNGHFSRTNKFLEQNGKTPIDW 226
Cdd:COG0692 163 LLWGAYAQKKAALIDASKHLVLESPHPSPLSAHRGFFGSKPFSKANAYLEEQGKTPIDW 221
|
|
| PRK05254 |
PRK05254 |
uracil-DNA glycosylase; Provisional |
5-228 |
4.81e-163 |
|
uracil-DNA glycosylase; Provisional
Pssm-ID: 235376 Cd Length: 224 Bit Score: 449.22 E-value: 4.81e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595947 5 DDRIKLEASWKEALREEFDKPYMKQLGEFLRQEKAAGKVIFPPGPLIFNALNTTPLENVKVVIIGQDPYHGPGQAHGLCF 84
Cdd:PRK05254 1 PMKMLLEPSWKEVLKPEFKKPYFQELLEFLRAERAAGKTIYPPGEDIFRAFNLTPFDDVKVVILGQDPYHGPGQAHGLSF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595947 85 SVQPGVPTPPSLQNIYKELNRDLNIPIPNNGYLQRWAEQGVLLLNTSLTVEQAKAGSHANAGWQPFTDRVIEVVNERCER 164
Cdd:PRK05254 81 SVPPGVPIPPSLRNIFKELEDDLGFPIPNHGDLTSWAEQGVLLLNTVLTVEAGQANSHAGKGWETFTDAVIKALNERREP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15595947 165 LVFLLWGSHAQSKQKLIDPQRHLILKSAHPSPLSAYRGFLGNGHFSRTNKFLEQNGKTPIDWSL 228
Cdd:PRK05254 161 VVFILWGSHAQKKKALIDNSKHLILESPHPSPLSAHRGFFGSKHFSKANALLKQHGKTPIDWQL 224
|
|
| UDG-F1-like |
cd10027 |
Uracil DNA glycosylase family 1 subfamily, includes Human uracil DNA glycosylase and similar ... |
26-226 |
3.59e-135 |
|
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: 377.56 E-value: 3.59e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595947 26 YMKQLGEFLRQEKAAgKVIFPPGPLIFNALNTTPLENVKVVIIGQDPYHGPGQAHGLCFSVQPGVPTPPSLQNIYKELNR 105
Cdd:cd10027 1 YFKKLEAFLEEEYKK-KTIYPPKEDIFRAFELTPLDDVKVVILGQDPYHGPGQAHGLAFSVPPGVKIPPSLRNIFKELKS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595947 106 DLNIPIPNNGYLQRWAEQGVLLLNTSLTVEQAKAGSHANAGWQPFTDRVIEVVNERCERLVFLLWGSHAQSKQKLIDPQR 185
Cdd:cd10027 80 DLGIFPPKHGDLSSWAKQGVLLLNTVLTVEAGKPGSHKNIGWETFTDAVIKALSEKNENVVFLLWGNHAQKKKKLIDKKK 159
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 15595947 186 HLILKSAHPSPLSAYRGFLGNGHFSRTNKFLEQNGKTPIDW 226
Cdd:cd10027 160 HLVLESSHPSPLSAYRGFFGSKHFSKANEYLKKHGKKPIDW 200
|
|
| ung |
TIGR00628 |
uracil-DNA glycosylase; All proteins in this family for which functions are known are ... |
11-221 |
8.18e-119 |
|
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: 336.88 E-value: 8.18e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595947 11 EASWKEALREEFDKPYMKQLGEFLRQEKAaGKVIFPPGPLIFNALNTTPLENVKVVIIGQDPYHGPGQAHGLCFSVQPGV 90
Cdd:TIGR00628 1 SPSWRAFLQPEFKKPYFQELLAFYKRERA-QETVYPPKEDVFAWTRLCPPEDVKVVILGQDPYHGPGQAHGLAFSVKRGV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595947 91 PTPPSLQNIYKELNRDL-NIPIPNNGYLQRWAEQGVLLLNTSLTVEQAKAGSHANAGWQPFTDRVIEVVNERCERLVFLL 169
Cdd:TIGR00628 80 PIPPSLKNIFKELEADYpDFPPPKHGCLEAWARQGVLLLNTVLTVRRGQPGSHSGLGWERFTDAVISRLSERLDGLVFML 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 15595947 170 WGSHAQSKQKLIDPQRHLILKSAHPSPLSAYRGFLGNGHFSRTNKFLEQNGK 221
Cdd:TIGR00628 160 WGAHAQKKKSLIDAKKHLVLKSPHPSPLSARRGFFGCRHFSKANEYLEKHGK 211
|
|
| UDG |
smart00986 |
Uracil DNA glycosylase superfamily; |
58-216 |
8.22e-33 |
|
Uracil DNA glycosylase superfamily;
Pssm-ID: 214956 Cd Length: 156 Bit Score: 116.33 E-value: 8.22e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595947 58 TPLENVKVVIIGQDPYHGPGQ-------AHGLCFSVQPGV----PTPPSLQNIYKELNrdlniPIPNNGYLQRWAEQGVL 126
Cdd:smart00986 3 TGDPNAKVLIVGQAPGASEEDrggpfvgAAGLLLSVMLGVaglpRLPPYLTNIVKCRP-----PDAGNRRPTSWELQGCL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595947 127 LlnTSLTVEQAKAGSHANAGWQPFTDRVIEVVNERceRLVFLLWGSHAQSKQKLidpqrHLILKSAHPSPLSAYRgfLGN 206
Cdd:smart00986 78 L--PWLTVELALARPHLILLLGKFAAQALLGLLRR--PLVFGLRGRVAQLKGKG-----HRVLPLPHPSPLNRNF--FPA 146
|
170
....*....|
gi 15595947 207 GHFSRTNKFL 216
Cdd:smart00986 147 KKFAAWNDLL 156
|
|
| UDG |
pfam03167 |
Uracil DNA glycosylase superfamily; |
61-217 |
9.02e-21 |
|
Uracil DNA glycosylase superfamily;
Pssm-ID: 397331 Cd Length: 154 Bit Score: 85.09 E-value: 9.02e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595947 61 ENVKVVIIGQDPYHGpGQAHGLCFSVQPGVPTPPSLQNIykELNRDLNIPipnngylqrwaeQGVLLLNTSLTVEQAKAG 140
Cdd:pfam03167 6 PNAKVLIVGEAPGAD-EDATGLPFVGRAGNLLWKLLNAA--GLTRDLFSP------------QGVYITNVVKCRPGNRRK 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595947 141 SHA---NAGWqPFTDRVIEVVNERcerlVFLLWGSHAQSK-----------QKLIDPQRHLILKSAHPSPLSAYRgflgN 206
Cdd:pfam03167 71 PTSheiDACW-PYLEAEIELLRPR----VIVLLGKTAAKAllglkkitklrGKLIDLKGIPVLPTPHPSPLLRNK----L 141
|
170
....*....|.
gi 15595947 207 GHFSRTNKFLE 217
Cdd:pfam03167 142 NPFLKANAWED 152
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Ung |
COG0692 |
Uracil-DNA glycosylase [Replication, recombination and repair]; |
8-226 |
1.15e-167 |
|
Uracil-DNA glycosylase [Replication, recombination and repair];
Pssm-ID: 440456 Cd Length: 221 Bit Score: 460.67 E-value: 1.15e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595947 8 IKLEASWKEALREEFDKPYMKQLGEFLRQEKAAGKVIFPPGPLIFNALNTTPLENVKVVIIGQDPYHGPGQAHGLCFSVQ 87
Cdd:COG0692 3 VLLEPSWKEALAEEFEKPYFQALGAFLKAEYAAGKTIYPPGEDIFRAFNLTPFDDVKVVILGQDPYHGPGQAHGLSFSVP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595947 88 PGVPTPPSLQNIYKELNRDLNIPIPNNGYLQRWAEQGVLLLNTSLTVEQAKAGSHANAGWQPFTDRVIEVVNERCERLVF 167
Cdd:COG0692 83 PGVPLPPSLRNIYKELEDDLGIPIPNHGDLTSWAEQGVLLLNTVLTVRAGQAGSHAGKGWETFTDAVIRALNARKEPVVF 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 15595947 168 LLWGSHAQSKQKLIDPQRHLILKSAHPSPLSAYRGFLGNGHFSRTNKFLEQNGKTPIDW 226
Cdd:COG0692 163 LLWGAYAQKKAALIDASKHLVLESPHPSPLSAHRGFFGSKPFSKANAYLEEQGKTPIDW 221
|
|
| PRK05254 |
PRK05254 |
uracil-DNA glycosylase; Provisional |
5-228 |
4.81e-163 |
|
uracil-DNA glycosylase; Provisional
Pssm-ID: 235376 Cd Length: 224 Bit Score: 449.22 E-value: 4.81e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595947 5 DDRIKLEASWKEALREEFDKPYMKQLGEFLRQEKAAGKVIFPPGPLIFNALNTTPLENVKVVIIGQDPYHGPGQAHGLCF 84
Cdd:PRK05254 1 PMKMLLEPSWKEVLKPEFKKPYFQELLEFLRAERAAGKTIYPPGEDIFRAFNLTPFDDVKVVILGQDPYHGPGQAHGLSF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595947 85 SVQPGVPTPPSLQNIYKELNRDLNIPIPNNGYLQRWAEQGVLLLNTSLTVEQAKAGSHANAGWQPFTDRVIEVVNERCER 164
Cdd:PRK05254 81 SVPPGVPIPPSLRNIFKELEDDLGFPIPNHGDLTSWAEQGVLLLNTVLTVEAGQANSHAGKGWETFTDAVIKALNERREP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15595947 165 LVFLLWGSHAQSKQKLIDPQRHLILKSAHPSPLSAYRGFLGNGHFSRTNKFLEQNGKTPIDWSL 228
Cdd:PRK05254 161 VVFILWGSHAQKKKALIDNSKHLILESPHPSPLSAHRGFFGSKHFSKANALLKQHGKTPIDWQL 224
|
|
| UDG-F1-like |
cd10027 |
Uracil DNA glycosylase family 1 subfamily, includes Human uracil DNA glycosylase and similar ... |
26-226 |
3.59e-135 |
|
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: 377.56 E-value: 3.59e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595947 26 YMKQLGEFLRQEKAAgKVIFPPGPLIFNALNTTPLENVKVVIIGQDPYHGPGQAHGLCFSVQPGVPTPPSLQNIYKELNR 105
Cdd:cd10027 1 YFKKLEAFLEEEYKK-KTIYPPKEDIFRAFELTPLDDVKVVILGQDPYHGPGQAHGLAFSVPPGVKIPPSLRNIFKELKS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595947 106 DLNIPIPNNGYLQRWAEQGVLLLNTSLTVEQAKAGSHANAGWQPFTDRVIEVVNERCERLVFLLWGSHAQSKQKLIDPQR 185
Cdd:cd10027 80 DLGIFPPKHGDLSSWAKQGVLLLNTVLTVEAGKPGSHKNIGWETFTDAVIKALSEKNENVVFLLWGNHAQKKKKLIDKKK 159
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 15595947 186 HLILKSAHPSPLSAYRGFLGNGHFSRTNKFLEQNGKTPIDW 226
Cdd:cd10027 160 HLVLESSHPSPLSAYRGFFGSKHFSKANEYLKKHGKKPIDW 200
|
|
| ung |
TIGR00628 |
uracil-DNA glycosylase; All proteins in this family for which functions are known are ... |
11-221 |
8.18e-119 |
|
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: 336.88 E-value: 8.18e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595947 11 EASWKEALREEFDKPYMKQLGEFLRQEKAaGKVIFPPGPLIFNALNTTPLENVKVVIIGQDPYHGPGQAHGLCFSVQPGV 90
Cdd:TIGR00628 1 SPSWRAFLQPEFKKPYFQELLAFYKRERA-QETVYPPKEDVFAWTRLCPPEDVKVVILGQDPYHGPGQAHGLAFSVKRGV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595947 91 PTPPSLQNIYKELNRDL-NIPIPNNGYLQRWAEQGVLLLNTSLTVEQAKAGSHANAGWQPFTDRVIEVVNERCERLVFLL 169
Cdd:TIGR00628 80 PIPPSLKNIFKELEADYpDFPPPKHGCLEAWARQGVLLLNTVLTVRRGQPGSHSGLGWERFTDAVISRLSERLDGLVFML 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 15595947 170 WGSHAQSKQKLIDPQRHLILKSAHPSPLSAYRGFLGNGHFSRTNKFLEQNGK 221
Cdd:TIGR00628 160 WGAHAQKKKSLIDAKKHLVLKSPHPSPLSARRGFFGCRHFSKANEYLEKHGK 211
|
|
| PHA03347 |
PHA03347 |
uracil DNA glycosylase; Provisional |
5-228 |
2.27e-85 |
|
uracil DNA glycosylase; Provisional
Pssm-ID: 177588 Cd Length: 252 Bit Score: 253.82 E-value: 2.27e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595947 5 DDRIKLEASWKEALreefdkpymkQLGEFLRQ----------EKAAGKVIFPPGPLIFNALNTTPLENVKVVIIGQDPYH 74
Cdd:PHA03347 21 DEDLLLSDPWLDFL----------QLSPFLKQkllallncvrELRKQTVIYPPEDRIMAWSYLCDPEDIKVVILGQDPYH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595947 75 GpGQAHGLCFSVQPGVPTPPSLQNIYKELNR-DLNIPIPNNGYLQRWAEQGVLLLNTSLTVEQAKAGSHANAGWQPFTDR 153
Cdd:PHA03347 91 G-GQANGLAFSVAYGFPVPPSLRNIFAELHRsVPDFSPPDHGCLDAWARQGVLLLNTILTVEKGKPGSHSDLGWAWFTDY 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595947 154 VIEVVNERCERLVFLLWGSHAQSKQKLIDPQRHLILKSAHPSPLSA---YRG----FLGNGHFSRTNKFLEQNGKTPIDW 226
Cdd:PHA03347 170 IISSLSEKLKACVFMLWGSKAIDKASLINSQKHLVLKAQHPSPLAAnstRSStwpkFLGCNHFVLANKYLTQHGKGPIDW 249
|
..
gi 15595947 227 SL 228
Cdd:PHA03347 250 NL 251
|
|
| PHA03200 |
PHA03200 |
uracil DNA glycosylase; Provisional |
61-228 |
1.35e-72 |
|
uracil DNA glycosylase; Provisional
Pssm-ID: 165467 Cd Length: 255 Bit Score: 221.52 E-value: 1.35e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595947 61 ENVKVVIIGQDPYHGpGQAHGLCFSVQPGVPTPPSLQNIYKELNRDL-NIPIPNNGYLQRWAEQGVLLLNTSLTVEQAKA 139
Cdd:PHA03200 83 EDVKVVIVGQDPYHD-GSACGLAFGTVRGRSAPPSLKNVFRELERTVpNFSRPDSGCLDSWCRQGVLLLNTVFTVVHGQP 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595947 140 GSHANAGWQPFTDRVIEVVNERCERLVFLLWGSHAQSKQKLIDPQRHLILKSAHPSP--LSAYRGFLGNGHFSRTNKFLE 217
Cdd:PHA03200 162 GSHEALGWQTLSDRVISRLSEKREHLVFMLWGAQAQKLEYLIDSRKHLILKSAHPSPrvKGARTPFIGNNHFVLANEYLS 241
|
170
....*....|.
gi 15595947 218 QNGKTPIDWSL 228
Cdd:PHA03200 242 THGKRPIDWNI 252
|
|
| PHA03202 |
PHA03202 |
uracil DNA glycosylase; Provisional |
13-228 |
5.68e-72 |
|
uracil DNA glycosylase; Provisional
Pssm-ID: 165469 Cd Length: 313 Bit Score: 221.88 E-value: 5.68e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595947 13 SWKEALREEFDKPYMKQL-GEFlrQEKAAGKVIFPPGPLIFNALNTTPLENVKVVIIGQDPYHGPGQAHGLCFSVQPGVP 91
Cdd:PHA03202 99 SWRPILEREMQQPYVRLLlNEY--KLRCAREEVFPPKEDIFAWTRFSPPEKVRVVIVGQDPYHAPGQAHGLAFSVRKGVP 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595947 92 TPPSLQNIYKELNRDL-NIPIPNNGYLQRWAEQGVLLLNTSLTVEQAKAGSHANAGWQPFTDRVIEVVNERCERLVFLLW 170
Cdd:PHA03202 177 VPPSLRNIYSAVQKSYpSFRPPMHGFLEKWAEQGVLLINTTLTVARGKPGSHATLGWHRLVRAVIDRLCTTSQGLVFMLW 256
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595947 171 GSHAqskQKLIDP--QRHLILKSAHPSPLSAYrGFLGNGHFSRTNKFLEQNGKTPIDWSL 228
Cdd:PHA03202 257 GAHA---QKSCSPnrQHHLVLTYGHPSPLSRV-NFRDCPHFLEANAYLTKTGRKPVDWQI 312
|
|
| PHA03199 |
PHA03199 |
uracil DNA glycosylase; Provisional |
6-228 |
1.59e-63 |
|
uracil DNA glycosylase; Provisional
Pssm-ID: 165466 Cd Length: 304 Bit Score: 199.85 E-value: 1.59e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595947 6 DRIKLEASWKEALREEFDKPYMKQLGEFLRQEKAAGKVIFPPGPLIFNALNTTPLENVKVVIIGQDPYHGPGQAHGLCFS 85
Cdd:PHA03199 83 DEFCIDPEWHDLLRDEFEEPYAKGIFEEYNQLLNNGEEIFPIKGDIFAWTRFCGPEKIRVVIIGQDPYHGAGHAHGLAFS 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595947 86 VQPGVPTPPSLQNIYKELNRDL-NIPIPNNGYLQRWAEQGVLLLNTSLTVEQAKAGSHANAGWQPFTDRVIEVVNERCER 164
Cdd:PHA03199 163 VKRGIPIPPSLKNIFAALMESYpHLPLPTHGCLDNWARQGVLLLNTTLTVKRGTPGSHFYLGWDMLIKRMLKRLCENRTG 242
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15595947 165 LVFLLWGSHAQsKQKLIDPQRHLILKSAHPSPLSAYRgFLGNGHFSRTNKFLEQNGKTPIDWSL 228
Cdd:PHA03199 243 LVFMLWGAHAQ-KTIQPNPRCHLVLTHAHPSPLSRSE-FRNCKHFLQANEYFLKKGEPEIDWSI 304
|
|
| PHA03204 |
PHA03204 |
uracil DNA glycosylase; Provisional |
10-228 |
1.26e-57 |
|
uracil DNA glycosylase; Provisional
Pssm-ID: 165471 Cd Length: 322 Bit Score: 185.16 E-value: 1.26e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595947 10 LEASWKEALREEFDKPY-MKQLGEFLRqeKAAGKVIFPPGPLIFNALNTTPLENVKVVIIGQDPYHGPGQAHGLCFSVQP 88
Cdd:PHA03204 102 IDCRWKEILLPELCCPTgSKILAEYER--RARYEEVYPPKSDIFAWTRYCAPDHVKVVIVGQDPYANPGQAHGLAFSVKP 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595947 89 GVPTPPSLQNIYKELNRDL-NIPIPNNGYLQRWAEQGVLLLNTSLTVEQAKAGSHANAGWQPFTDRVIEVVNERCERLVF 167
Cdd:PHA03204 180 GSPIPPSLKNILAAVKACYpSIELGSHGCLEDWAKRGVLLLNSVLTVKRGDPGSHHSVGWQILVRNVLRRLSQSTRGIVF 259
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15595947 168 LLWGSHAQSKQKLID-PQRHLILKSAHPSPLSAyRGFLGNGHFSRTNKFLEQNGKTPIDWSL 228
Cdd:PHA03204 260 MLWGAQAQTMYFQTDnDDRHLVLKYSHPSPLSR-KPFAHCTHFKDANEFLCKMGKGAIDWSL 320
|
|
| PHA03201 |
PHA03201 |
uracil DNA glycosylase; Provisional |
13-227 |
1.18e-56 |
|
uracil DNA glycosylase; Provisional
Pssm-ID: 165468 Cd Length: 318 Bit Score: 182.79 E-value: 1.18e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595947 13 SWKEALREEFDKPYMKQL-GEFLRQEKAagKVIFPPGPLIFNALNTTPLENVKVVIIGQDPYHGPGQAHGLCFSVQPGVP 91
Cdd:PHA03201 105 AWRPLLEPELANPLTARLmAEYERRCRT--EEVLPPREDVFSWTRYCTPDEVRVVIIGQDPYHQPGQAHGLAFSVRPGTP 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595947 92 TPPSLQNIYKEL-NRDLNIPIPNNGYLQRWAEQGVLLLNTSLTVEQAKAGSHANAGWQPFTDRVIEVVNERCERLVFLLW 170
Cdd:PHA03201 183 APPSLRNILAAVrNCCPDARMSGHGCLEKWARGGVLLLNTTLTVRRGEPASHAKIGWDRFVGSVVRRLAASRPGLVFMLW 262
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 15595947 171 GSHAQSKQKlIDPQRHLILKSAHPSPLSAYRgFLGNGHFSRTNKFLEQNGKTPIDWS 227
Cdd:PHA03201 263 GAHAQNAIR-PDPRVHRVLTYSHPSPLSKVP-FGSCRHFCLANQYLRERSLAPIDWS 317
|
|
| UDG-F1-like |
cd19371 |
Uracil DNA glycosylase family 1, includes Human uracil DNA glycosylase, Vaccinia virus protein ... |
65-198 |
2.30e-51 |
|
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: 163.27 E-value: 2.30e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595947 65 VVIIGQDPYHGPGQAHGLCFSVQPGVPTPPSLQNIYKELNRDLNIP-IPNNGYLQRWAEQGVLLLNTSLTVEQAKAGSHA 143
Cdd:cd19371 1 VVIIGQDPYPSPGHAGGLAFSVTSEVPPPKSLRNIYKELERDYSSFlPPGNGTLEFWARQGVLLLNAALTCESGKPKSHY 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 15595947 144 nAGWQPFTDRVIEVVNERCERLVFLLWGSHAQSKQKLIDPQRHLILKSAHPSPLS 198
Cdd:cd19371 81 -LLWEPFIKAFIRYISAHNKGLVFLLFGSDAQKLRKKINGRNVHVFKADHPSPAD 134
|
|
| UDG |
smart00986 |
Uracil DNA glycosylase superfamily; |
58-216 |
8.22e-33 |
|
Uracil DNA glycosylase superfamily;
Pssm-ID: 214956 Cd Length: 156 Bit Score: 116.33 E-value: 8.22e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595947 58 TPLENVKVVIIGQDPYHGPGQ-------AHGLCFSVQPGV----PTPPSLQNIYKELNrdlniPIPNNGYLQRWAEQGVL 126
Cdd:smart00986 3 TGDPNAKVLIVGQAPGASEEDrggpfvgAAGLLLSVMLGVaglpRLPPYLTNIVKCRP-----PDAGNRRPTSWELQGCL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595947 127 LlnTSLTVEQAKAGSHANAGWQPFTDRVIEVVNERceRLVFLLWGSHAQSKQKLidpqrHLILKSAHPSPLSAYRgfLGN 206
Cdd:smart00986 78 L--PWLTVELALARPHLILLLGKFAAQALLGLLRR--PLVFGLRGRVAQLKGKG-----HRVLPLPHPSPLNRNF--FPA 146
|
170
....*....|
gi 15595947 207 GHFSRTNKFL 216
Cdd:smart00986 147 KKFAAWNDLL 156
|
|
| UDG |
pfam03167 |
Uracil DNA glycosylase superfamily; |
61-217 |
9.02e-21 |
|
Uracil DNA glycosylase superfamily;
Pssm-ID: 397331 Cd Length: 154 Bit Score: 85.09 E-value: 9.02e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595947 61 ENVKVVIIGQDPYHGpGQAHGLCFSVQPGVPTPPSLQNIykELNRDLNIPipnngylqrwaeQGVLLLNTSLTVEQAKAG 140
Cdd:pfam03167 6 PNAKVLIVGEAPGAD-EDATGLPFVGRAGNLLWKLLNAA--GLTRDLFSP------------QGVYITNVVKCRPGNRRK 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595947 141 SHA---NAGWqPFTDRVIEVVNERcerlVFLLWGSHAQSK-----------QKLIDPQRHLILKSAHPSPLSAYRgflgN 206
Cdd:pfam03167 71 PTSheiDACW-PYLEAEIELLRPR----VIVLLGKTAAKAllglkkitklrGKLIDLKGIPVLPTPHPSPLLRNK----L 141
|
170
....*....|.
gi 15595947 207 GHFSRTNKFLE 217
Cdd:pfam03167 142 NPFLKANAWED 152
|
|
| UDG-like |
cd09593 |
uracil-DNA glycosylases (UDG) and related enzymes; Uracil-DNA glycosylases (UDGs) initiate ... |
65-199 |
9.64e-16 |
|
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: 70.88 E-value: 9.64e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595947 65 VVIIGQDPYHGPGQAHglcfsvqpGVPTPPSLQNIYKELNRDlnipipnnGYLQRWAEQGVLLLNTSLTVEQAKAGSHaN 144
Cdd:cd09593 1 VLIVGQNPGPHGARAG--------GVPPGPSGNRLWRLLAAA--------GGTPRLFRYGVGLTNTVPRGPPGAAAGS-E 63
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15595947 145 AGWQPFTDRVIEVVNERCERLVFLLWGSHAQSK-------QKLIDPQRHLILKSAHPSPLSA 199
Cdd:cd09593 64 KKELRFCGRWLRKLLELLNPRVVVLLGKKAQEAylavltsSKGAPGKGTEVLVLPHPSPRNR 125
|
|
| UDG-F1_NsUNG-like |
cd19373 |
Uracil DNA glycosylase family 1 subfamily, includes Nitratifractor salsuginis UNG and similar ... |
66-194 |
6.64e-04 |
|
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: 39.04 E-value: 6.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595947 66 VIIGQDPYHGPGQAHGLCFsVQPGVPTPPSLQNIYKELNRD------LNIPIPNNGYL---------------------- 117
Cdd:cd19373 2 ILFGQDPYPREKSATGYAF-IDGAVKEIFSPKGLSKEVNRAtslrnfIKMALVARGSLdpddlsqeaiakldksllvdti 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595947 118 ----QRWAEQGVLLLNTSLTVE-QAKAGSHANAgWQPFTDRVIEVVNERCERLVflLWGSHAQSKQKLIDPQRHLILKSA 192
Cdd:cd19373 81 delrENFEKSGVLLLNAALLFTsKEESNRHARA-WRPFIEKLLEGLEAYGPELI--LFGAHAKEIKKLKSARGFPQVELE 157
|
..
gi 15595947 193 HP 194
Cdd:cd19373 158 HP 159
|
|
| |
