|
Name |
Accession |
Description |
Interval |
E-value |
| Ung |
COG0692 |
Uracil-DNA glycosylase [Replication, recombination and repair]; |
3-213 |
7.59e-140 |
|
Uracil-DNA glycosylase [Replication, recombination and repair];
Pssm-ID: 440456 Cd Length: 221 Bit Score: 389.79 E-value: 7.59e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487750253 3 WSEVFHDITTRHDFQAMHDFLEKEY-TTQTVYPDKQNIYQAFDLTPFEDIKVVILGQDPYHGPNQAHGLAFSVQPHAKFP 81
Cdd:COG0692 9 WKEALAEEFEKPYFQALGAFLKAEYaAGKTIYPPGEDIFRAFNLTPFDDVKVVILGQDPYHGPGQAHGLSFSVPPGVPLP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487750253 82 PSLRNMYQELENDIGC-HRTSPHLQDWAREGVLLLNTVLTVRQGEAHSHRNIGWETFTDEIIQAVSNYREHVVFILWGRP 160
Cdd:COG0692 89 PSLRNIYKELEDDLGIpIPNHGDLTSWAEQGVLLLNTVLTVRAGQAGSHAGKGWETFTDAVIRALNARKEPVVFLLWGAY 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 487750253 161 AQQKERFIDTSKHLIIKSPHPSPLSAFRGFFGSKPYSTTNNYLKSKGKTPVQW 213
Cdd:COG0692 169 AQKKAALIDASKHLVLESPHPSPLSAHRGFFGSKPFSKANAYLEEQGKTPIDW 221
|
|
| PRK05254 |
PRK05254 |
uracil-DNA glycosylase; Provisional |
1-214 |
1.07e-137 |
|
uracil-DNA glycosylase; Provisional
Pssm-ID: 235376 Cd Length: 224 Bit Score: 384.50 E-value: 1.07e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487750253 1 MKWSEVFHDITTRHDFQAMHDFLEKE-YTTQTVYPDKQNIYQAFDLTPFEDIKVVILGQDPYHGPNQAHGLAFSVQPHAK 79
Cdd:PRK05254 8 PSWKEVLKPEFKKPYFQELLEFLRAErAAGKTIYPPGEDIFRAFNLTPFDDVKVVILGQDPYHGPGQAHGLSFSVPPGVP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487750253 80 FPPSLRNMYQELENDIGCHR-TSPHLQDWAREGVLLLNTVLTVRQGEAHSHRNIGWETFTDEIIQAVSNYREHVVFILWG 158
Cdd:PRK05254 88 IPPSLRNIFKELEDDLGFPIpNHGDLTSWAEQGVLLLNTVLTVEAGQANSHAGKGWETFTDAVIKALNERREPVVFILWG 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 487750253 159 RPAQQKERFIDTSKHLIIKSPHPSPLSAFRGFFGSKPYSTTNNYLKSKGKTPVQWC 214
Cdd:PRK05254 168 SHAQKKKALIDNSKHLILESPHPSPLSAHRGFFGSKHFSKANALLKQHGKTPIDWQ 223
|
|
| UDG-F1-like |
cd10027 |
Uracil DNA glycosylase family 1 subfamily, includes Human uracil DNA glycosylase and similar ... |
16-213 |
6.67e-127 |
|
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: 356.37 E-value: 6.67e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487750253 16 FQAMHDFLEKEYTTQTVYPDKQNIYQAFDLTPFEDIKVVILGQDPYHGPNQAHGLAFSVQPHAKFPPSLRNMYQELENDI 95
Cdd:cd10027 2 FKKLEAFLEEEYKKKTIYPPKEDIFRAFELTPLDDVKVVILGQDPYHGPGQAHGLAFSVPPGVKIPPSLRNIFKELKSDL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487750253 96 GC-HRTSPHLQDWAREGVLLLNTVLTVRQGEAHSHRNIGWETFTDEIIQAVSNYREHVVFILWGRPAQQKERFIDTSKHL 174
Cdd:cd10027 82 GIfPPKHGDLSSWAKQGVLLLNTVLTVEAGKPGSHKNIGWETFTDAVIKALSEKNENVVFLLWGNHAQKKKKLIDKKKHL 161
|
170 180 190
....*....|....*....|....*....|....*....
gi 487750253 175 IIKSPHPSPLSAFRGFFGSKPYSTTNNYLKSKGKTPVQW 213
Cdd:cd10027 162 VLESSHPSPLSAYRGFFGSKHFSKANEYLKKHGKKPIDW 200
|
|
| ung |
TIGR00628 |
uracil-DNA glycosylase; All proteins in this family for which functions are known are ... |
16-208 |
2.21e-104 |
|
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: 299.51 E-value: 2.21e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487750253 16 FQAMHDFLEKEYTTQTVYPDKQNIYQAFDLTPFEDIKVVILGQDPYHGPNQAHGLAFSVQPHAKFPPSLRNMYQELENDI 95
Cdd:TIGR00628 17 FQELLAFYKRERAQETVYPPKEDVFAWTRLCPPEDVKVVILGQDPYHGPGQAHGLAFSVKRGVPIPPSLKNIFKELEADY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487750253 96 GCHRTSPH--LQDWAREGVLLLNTVLTVRQGEAHSHRNIGWETFTDEIIQAVSNYREHVVFILWGRPAQQKERFIDTSKH 173
Cdd:TIGR00628 97 PDFPPPKHgcLEAWARQGVLLLNTVLTVRRGQPGSHSGLGWERFTDAVISRLSERLDGLVFMLWGAHAQKKKSLIDAKKH 176
|
170 180 190
....*....|....*....|....*....|....*
gi 487750253 174 LIIKSPHPSPLSAFRGFFGSKPYSTTNNYLKSKGK 208
Cdd:TIGR00628 177 LVLKSPHPSPLSARRGFFGCRHFSKANEYLEKHGK 211
|
|
| UDG |
smart00986 |
Uracil DNA glycosylase superfamily; |
45-203 |
1.53e-33 |
|
Uracil DNA glycosylase superfamily;
Pssm-ID: 214956 Cd Length: 156 Bit Score: 117.87 E-value: 1.53e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487750253 45 LTPFEDIKVVILGQDPY------HGP-NQAHGLAFSVQPHA----KFPPSLRNMYQELENDIGCHRtsphLQDWAREGVL 113
Cdd:smart00986 2 GTGDPNAKVLIVGQAPGaseedrGGPfVGAAGLLLSVMLGVaglpRLPPYLTNIVKCRPPDAGNRR----PTSWELQGCL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487750253 114 LlnTVLTVRQGEAHSHRNIGWETFTDEIIQAVSnyREHVVFILWGRPAQQKERfidtsKHLIIKSPHPSPLSafRGFFGS 193
Cdd:smart00986 78 L--PWLTVELALARPHLILLLGKFAAQALLGLL--RRPLVFGLRGRVAQLKGK-----GHRVLPLPHPSPLN--RNFFPA 146
|
170
....*....|
gi 487750253 194 KPYSTTNNYL 203
Cdd:smart00986 147 KKFAAWNDLL 156
|
|
| UDG |
pfam03167 |
Uracil DNA glycosylase superfamily; |
46-194 |
4.55e-21 |
|
Uracil DNA glycosylase superfamily;
Pssm-ID: 397331 Cd Length: 154 Bit Score: 85.48 E-value: 4.55e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487750253 46 TPFEDIKVVILGQDPYHGpNQAHGLAFSVQPHAKFPPSLRNMyqELENDIGCHrtsphlqdwarEGVLLLNTVLTVRQGE 125
Cdd:pfam03167 3 FGPPNAKVLIVGEAPGAD-EDATGLPFVGRAGNLLWKLLNAA--GLTRDLFSP-----------QGVYITNVVKCRPGNR 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487750253 126 AHSHR---NIGWEtFTDEIIQAVSNyrehVVFILWGRPAQQK-----------ERFIDTSKHLIIKSPHPSPLSAFRGFF 191
Cdd:pfam03167 69 RKPTSheiDACWP-YLEAEIELLRP----RVIVLLGKTAAKAllglkkitklrGKLIDLKGIPVLPTPHPSPLLRNKLNP 143
|
...
gi 487750253 192 GSK 194
Cdd:pfam03167 144 FLK 146
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Ung |
COG0692 |
Uracil-DNA glycosylase [Replication, recombination and repair]; |
3-213 |
7.59e-140 |
|
Uracil-DNA glycosylase [Replication, recombination and repair];
Pssm-ID: 440456 Cd Length: 221 Bit Score: 389.79 E-value: 7.59e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487750253 3 WSEVFHDITTRHDFQAMHDFLEKEY-TTQTVYPDKQNIYQAFDLTPFEDIKVVILGQDPYHGPNQAHGLAFSVQPHAKFP 81
Cdd:COG0692 9 WKEALAEEFEKPYFQALGAFLKAEYaAGKTIYPPGEDIFRAFNLTPFDDVKVVILGQDPYHGPGQAHGLSFSVPPGVPLP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487750253 82 PSLRNMYQELENDIGC-HRTSPHLQDWAREGVLLLNTVLTVRQGEAHSHRNIGWETFTDEIIQAVSNYREHVVFILWGRP 160
Cdd:COG0692 89 PSLRNIYKELEDDLGIpIPNHGDLTSWAEQGVLLLNTVLTVRAGQAGSHAGKGWETFTDAVIRALNARKEPVVFLLWGAY 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 487750253 161 AQQKERFIDTSKHLIIKSPHPSPLSAFRGFFGSKPYSTTNNYLKSKGKTPVQW 213
Cdd:COG0692 169 AQKKAALIDASKHLVLESPHPSPLSAHRGFFGSKPFSKANAYLEEQGKTPIDW 221
|
|
| PRK05254 |
PRK05254 |
uracil-DNA glycosylase; Provisional |
1-214 |
1.07e-137 |
|
uracil-DNA glycosylase; Provisional
Pssm-ID: 235376 Cd Length: 224 Bit Score: 384.50 E-value: 1.07e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487750253 1 MKWSEVFHDITTRHDFQAMHDFLEKE-YTTQTVYPDKQNIYQAFDLTPFEDIKVVILGQDPYHGPNQAHGLAFSVQPHAK 79
Cdd:PRK05254 8 PSWKEVLKPEFKKPYFQELLEFLRAErAAGKTIYPPGEDIFRAFNLTPFDDVKVVILGQDPYHGPGQAHGLSFSVPPGVP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487750253 80 FPPSLRNMYQELENDIGCHR-TSPHLQDWAREGVLLLNTVLTVRQGEAHSHRNIGWETFTDEIIQAVSNYREHVVFILWG 158
Cdd:PRK05254 88 IPPSLRNIFKELEDDLGFPIpNHGDLTSWAEQGVLLLNTVLTVEAGQANSHAGKGWETFTDAVIKALNERREPVVFILWG 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 487750253 159 RPAQQKERFIDTSKHLIIKSPHPSPLSAFRGFFGSKPYSTTNNYLKSKGKTPVQWC 214
Cdd:PRK05254 168 SHAQKKKALIDNSKHLILESPHPSPLSAHRGFFGSKHFSKANALLKQHGKTPIDWQ 223
|
|
| UDG-F1-like |
cd10027 |
Uracil DNA glycosylase family 1 subfamily, includes Human uracil DNA glycosylase and similar ... |
16-213 |
6.67e-127 |
|
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: 356.37 E-value: 6.67e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487750253 16 FQAMHDFLEKEYTTQTVYPDKQNIYQAFDLTPFEDIKVVILGQDPYHGPNQAHGLAFSVQPHAKFPPSLRNMYQELENDI 95
Cdd:cd10027 2 FKKLEAFLEEEYKKKTIYPPKEDIFRAFELTPLDDVKVVILGQDPYHGPGQAHGLAFSVPPGVKIPPSLRNIFKELKSDL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487750253 96 GC-HRTSPHLQDWAREGVLLLNTVLTVRQGEAHSHRNIGWETFTDEIIQAVSNYREHVVFILWGRPAQQKERFIDTSKHL 174
Cdd:cd10027 82 GIfPPKHGDLSSWAKQGVLLLNTVLTVEAGKPGSHKNIGWETFTDAVIKALSEKNENVVFLLWGNHAQKKKKLIDKKKHL 161
|
170 180 190
....*....|....*....|....*....|....*....
gi 487750253 175 IIKSPHPSPLSAFRGFFGSKPYSTTNNYLKSKGKTPVQW 213
Cdd:cd10027 162 VLESSHPSPLSAYRGFFGSKHFSKANEYLKKHGKKPIDW 200
|
|
| ung |
TIGR00628 |
uracil-DNA glycosylase; All proteins in this family for which functions are known are ... |
16-208 |
2.21e-104 |
|
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: 299.51 E-value: 2.21e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487750253 16 FQAMHDFLEKEYTTQTVYPDKQNIYQAFDLTPFEDIKVVILGQDPYHGPNQAHGLAFSVQPHAKFPPSLRNMYQELENDI 95
Cdd:TIGR00628 17 FQELLAFYKRERAQETVYPPKEDVFAWTRLCPPEDVKVVILGQDPYHGPGQAHGLAFSVKRGVPIPPSLKNIFKELEADY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487750253 96 GCHRTSPH--LQDWAREGVLLLNTVLTVRQGEAHSHRNIGWETFTDEIIQAVSNYREHVVFILWGRPAQQKERFIDTSKH 173
Cdd:TIGR00628 97 PDFPPPKHgcLEAWARQGVLLLNTVLTVRRGQPGSHSGLGWERFTDAVISRLSERLDGLVFMLWGAHAQKKKSLIDAKKH 176
|
170 180 190
....*....|....*....|....*....|....*
gi 487750253 174 LIIKSPHPSPLSAFRGFFGSKPYSTTNNYLKSKGK 208
Cdd:TIGR00628 177 LVLKSPHPSPLSARRGFFGCRHFSKANEYLEKHGK 211
|
|
| PHA03347 |
PHA03347 |
uracil DNA glycosylase; Provisional |
28-213 |
2.62e-69 |
|
uracil DNA glycosylase; Provisional
Pssm-ID: 177588 Cd Length: 252 Bit Score: 212.22 E-value: 2.62e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487750253 28 TTQTVYPDKQNIYQAFDLTPFEDIKVVILGQDPYHGpNQAHGLAFSVQPHAKFPPSLRNMYQELENDIGCHRTSPH--LQ 105
Cdd:PHA03347 56 KQTVIYPPEDRIMAWSYLCDPEDIKVVILGQDPYHG-GQANGLAFSVAYGFPVPPSLRNIFAELHRSVPDFSPPDHgcLD 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487750253 106 DWAREGVLLLNTVLTVRQGEAHSHRNIGWETFTDEIIQAVSNYREHVVFILWGRPAQQKERFIDTSKHLIIKSPHPSPLS 185
Cdd:PHA03347 135 AWARQGVLLLNTILTVEKGKPGSHSDLGWAWFTDYIISSLSEKLKACVFMLWGSKAIDKASLINSQKHLVLKAQHPSPLA 214
|
170 180 190
....*....|....*....|....*....|....*
gi 487750253 186 AFRG-------FFGSKPYSTTNNYLKSKGKTPVQW 213
Cdd:PHA03347 215 ANSTrsstwpkFLGCNHFVLANKYLTQHGKGPIDW 249
|
|
| PHA03200 |
PHA03200 |
uracil DNA glycosylase; Provisional |
21-213 |
6.05e-62 |
|
uracil DNA glycosylase; Provisional
Pssm-ID: 165467 Cd Length: 255 Bit Score: 193.79 E-value: 6.05e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487750253 21 DFLEKEYTTQTVYPDKQNIYQAFDLTPFEDIKVVILGQDPYHGpNQAHGLAFSVQPHAKFPPSLRNMYQELENDI----- 95
Cdd:PHA03200 55 DAVDRDRQRLTVYPPPEDVHRWSRLCSPEDVKVVIVGQDPYHD-GSACGLAFGTVRGRSAPPSLKNVFRELERTVpnfsr 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487750253 96 ---GChrtsphLQDWAREGVLLLNTVLTVRQGEAHSHRNIGWETFTDEIIQAVSNYREHVVFILWGRPAQQKERFIDTSK 172
Cdd:PHA03200 134 pdsGC------LDSWCRQGVLLLNTVFTVVHGQPGSHEALGWQTLSDRVISRLSEKREHLVFMLWGAQAQKLEYLIDSRK 207
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 487750253 173 HLIIKSPHPSP--LSAFRGFFGSKPYSTTNNYLKSKGKTPVQW 213
Cdd:PHA03200 208 HLILKSAHPSPrvKGARTPFIGNNHFVLANEYLSTHGKRPIDW 250
|
|
| PHA03201 |
PHA03201 |
uracil DNA glycosylase; Provisional |
24-213 |
6.86e-52 |
|
uracil DNA glycosylase; Provisional
Pssm-ID: 165468 Cd Length: 318 Bit Score: 169.69 E-value: 6.86e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487750253 24 EKEYTTQTVYPDKQNIYQAFDLTPFEDIKVVILGQDPYHGPNQAHGLAFSVQPHAKFPPSLRNMYQELENDIGCHRTSPH 103
Cdd:PHA03201 127 ERRCRTEEVLPPREDVFSWTRYCTPDEVRVVIIGQDPYHQPGQAHGLAFSVRPGTPAPPSLRNILAAVRNCCPDARMSGH 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487750253 104 --LQDWAREGVLLLNTVLTVRQGEAHSHRNIGWETFTDEIIQAVSNYREHVVFILWGRPAQQKERfIDTSKHLIIKSPHP 181
Cdd:PHA03201 207 gcLEKWARGGVLLLNTTLTVRRGEPASHAKIGWDRFVGSVVRRLAASRPGLVFMLWGAHAQNAIR-PDPRVHRVLTYSHP 285
|
170 180 190
....*....|....*....|....*....|...
gi 487750253 182 SPLSafRGFFGS-KPYSTTNNYLKSKGKTPVQW 213
Cdd:PHA03201 286 SPLS--KVPFGScRHFCLANQYLRERSLAPIDW 316
|
|
| PHA03202 |
PHA03202 |
uracil DNA glycosylase; Provisional |
28-213 |
1.49e-50 |
|
uracil DNA glycosylase; Provisional
Pssm-ID: 165469 Cd Length: 313 Bit Score: 166.41 E-value: 1.49e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487750253 28 TTQTVYPDKQNIYQAFDLTPFEDIKVVILGQDPYHGPNQAHGLAFSVQPHAKFPPSLRNMYQELENDIGCHRTSPH--LQ 105
Cdd:PHA03202 125 AREEVFPPKEDIFAWTRFSPPEKVRVVIVGQDPYHAPGQAHGLAFSVRKGVPVPPSLRNIYSAVQKSYPSFRPPMHgfLE 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487750253 106 DWAREGVLLLNTVLTVRQGEAHSHRNIGWETFTDEIIQAVSNYREHVVFILWGRPAQqkeRFIDTSK--HLIIKSPHPSP 183
Cdd:PHA03202 205 KWAEQGVLLINTTLTVARGKPGSHATLGWHRLVRAVIDRLCTTSQGLVFMLWGAHAQ---KSCSPNRqhHLVLTYGHPSP 281
|
170 180 190
....*....|....*....|....*....|.
gi 487750253 184 LSafRGFFGSKP-YSTTNNYLKSKGKTPVQW 213
Cdd:PHA03202 282 LS--RVNFRDCPhFLEANAYLTKTGRKPVDW 310
|
|
| UDG-F1-like |
cd19371 |
Uracil DNA glycosylase family 1, includes Human uracil DNA glycosylase, Vaccinia virus protein ... |
53-185 |
8.39e-49 |
|
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: 155.96 E-value: 8.39e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487750253 53 VVILGQDPYHGPNQAHGLAFSVQPHAKFPPSLRNMYQELENDIGCH--RTSPHLQDWAREGVLLLNTVLTVRQGEAHSHR 130
Cdd:cd19371 1 VVIIGQDPYPSPGHAGGLAFSVTSEVPPPKSLRNIYKELERDYSSFlpPGNGTLEFWARQGVLLLNAALTCESGKPKSHY 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 487750253 131 nIGWETFTDEIIQAVSNYREHVVFILWGRPAQQKERFIDTSKHLIIKSPHPSPLS 185
Cdd:cd19371 81 -LLWEPFIKAFIRYISAHNKGLVFLLFGSDAQKLRKKINGRNVHVFKADHPSPAD 134
|
|
| PHA03204 |
PHA03204 |
uracil DNA glycosylase; Provisional |
24-213 |
3.42e-48 |
|
uracil DNA glycosylase; Provisional
Pssm-ID: 165471 Cd Length: 322 Bit Score: 160.51 E-value: 3.42e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487750253 24 EKEYTTQTVYPDKQNIYQAFDLTPFEDIKVVILGQDPYHGPNQAHGLAFSVQPHAKFPPSLRNMYQELEN-----DIGCH 98
Cdd:PHA03204 127 ERRARYEEVYPPKSDIFAWTRYCAPDHVKVVIVGQDPYANPGQAHGLAFSVKPGSPIPPSLKNILAAVKAcypsiELGSH 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487750253 99 RTsphLQDWAREGVLLLNTVLTVRQGEAHSHRNIGWETFTDEIIQAVSNYREHVVFILWGRPAQ----QKERfidTSKHL 174
Cdd:PHA03204 207 GC---LEDWAKRGVLLLNSVLTVKRGDPGSHHSVGWQILVRNVLRRLSQSTRGIVFMLWGAQAQtmyfQTDN---DDRHL 280
|
170 180 190
....*....|....*....|....*....|....*....
gi 487750253 175 IIKSPHPSPLSAfRGFFGSKPYSTTNNYLKSKGKTPVQW 213
Cdd:PHA03204 281 VLKYSHPSPLSR-KPFAHCTHFKDANEFLCKMGKGAIDW 318
|
|
| PHA03199 |
PHA03199 |
uracil DNA glycosylase; Provisional |
30-213 |
2.43e-43 |
|
uracil DNA glycosylase; Provisional
Pssm-ID: 165466 Cd Length: 304 Bit Score: 147.46 E-value: 2.43e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487750253 30 QTVYPDKQNIYQAFDLTPFEDIKVVILGQDPYHGPNQAHGLAFSVQPHAKFPPSLRNMYQELENDIGcHRTSPH---LQD 106
Cdd:PHA03199 119 EEIFPIKGDIFAWTRFCGPEKIRVVIIGQDPYHGAGHAHGLAFSVKRGIPIPPSLKNIFAALMESYP-HLPLPThgcLDN 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487750253 107 WAREGVLLLNTVLTVRQGEAHSHRNIGWETFTDEIIQAVSNYREHVVFILWGRPAQQKERfIDTSKHLIIKSPHPSPLSA 186
Cdd:PHA03199 198 WARQGVLLLNTTLTVKRGTPGSHFYLGWDMLIKRMLKRLCENRTGLVFMLWGAHAQKTIQ-PNPRCHLVLTHAHPSPLSR 276
|
170 180
....*....|....*....|....*..
gi 487750253 187 FRgFFGSKPYSTTNNYLKSKGKTPVQW 213
Cdd:PHA03199 277 SE-FRNCKHFLQANEYFLKKGEPEIDW 302
|
|
| UDG |
smart00986 |
Uracil DNA glycosylase superfamily; |
45-203 |
1.53e-33 |
|
Uracil DNA glycosylase superfamily;
Pssm-ID: 214956 Cd Length: 156 Bit Score: 117.87 E-value: 1.53e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487750253 45 LTPFEDIKVVILGQDPY------HGP-NQAHGLAFSVQPHA----KFPPSLRNMYQELENDIGCHRtsphLQDWAREGVL 113
Cdd:smart00986 2 GTGDPNAKVLIVGQAPGaseedrGGPfVGAAGLLLSVMLGVaglpRLPPYLTNIVKCRPPDAGNRR----PTSWELQGCL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487750253 114 LlnTVLTVRQGEAHSHRNIGWETFTDEIIQAVSnyREHVVFILWGRPAQQKERfidtsKHLIIKSPHPSPLSafRGFFGS 193
Cdd:smart00986 78 L--PWLTVELALARPHLILLLGKFAAQALLGLL--RRPLVFGLRGRVAQLKGK-----GHRVLPLPHPSPLN--RNFFPA 146
|
170
....*....|
gi 487750253 194 KPYSTTNNYL 203
Cdd:smart00986 147 KKFAAWNDLL 156
|
|
| UDG |
pfam03167 |
Uracil DNA glycosylase superfamily; |
46-194 |
4.55e-21 |
|
Uracil DNA glycosylase superfamily;
Pssm-ID: 397331 Cd Length: 154 Bit Score: 85.48 E-value: 4.55e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487750253 46 TPFEDIKVVILGQDPYHGpNQAHGLAFSVQPHAKFPPSLRNMyqELENDIGCHrtsphlqdwarEGVLLLNTVLTVRQGE 125
Cdd:pfam03167 3 FGPPNAKVLIVGEAPGAD-EDATGLPFVGRAGNLLWKLLNAA--GLTRDLFSP-----------QGVYITNVVKCRPGNR 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487750253 126 AHSHR---NIGWEtFTDEIIQAVSNyrehVVFILWGRPAQQK-----------ERFIDTSKHLIIKSPHPSPLSAFRGFF 191
Cdd:pfam03167 69 RKPTSheiDACWP-YLEAEIELLRP----RVIVLLGKTAAKAllglkkitklrGKLIDLKGIPVLPTPHPSPLLRNKLNP 143
|
...
gi 487750253 192 GSK 194
Cdd:pfam03167 144 FLK 146
|
|
| UDG-like |
cd09593 |
uracil-DNA glycosylases (UDG) and related enzymes; Uracil-DNA glycosylases (UDGs) initiate ... |
53-186 |
1.43e-17 |
|
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: 75.50 E-value: 1.43e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487750253 53 VVILGQDPYHGPNQAHGLafsvqphaKFPPSLRNMYQELENDIGCHRtsphlqdWAREGVLLLNTVLTVRQGEAHSHRnI 132
Cdd:cd09593 1 VLIVGQNPGPHGARAGGV--------PPGPSGNRLWRLLAAAGGTPR-------LFRYGVGLTNTVPRGPPGAAAGSE-K 64
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 487750253 133 GWETFTDEII-QAVSNYREHVVfILWGRPAQQKERFIDTSK-------HLIIKSPHPSPLSA 186
Cdd:cd09593 65 KELRFCGRWLrKLLELLNPRVV-VLLGKKAQEAYLAVLTSSkgapgkgTEVLVLPHPSPRNR 125
|
|
| UDG_F1_VAVC_D4-like |
cd19372 |
Uracil DNA glycosylase family 1 subfamily, includes Vaccinia virus protein D4 and similar ... |
47-215 |
6.95e-06 |
|
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: 45.12 E-value: 6.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487750253 47 PFEDIKVVILGQDPYhgPNQAHGLAFSVQPHAKfpPSLRNMYQELENDIGCHRTSPHlqDWAR-EGVLLLNTVLTVRQGE 125
Cdd:cd19372 38 PLRDKRVCICGIDPY--PTDATGVPFESPDFSK--KTIRAIAEAISRRTGVSLYKGY--NFALvEGVLAWNYYLSCREGE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487750253 126 AHSHRnIGWETFTDEIIQAVSNYREhvVFILWGRPAQQKERFIDTSKHLIIKSPHPSPLSafRGFFGSKPYSTTNNYLKS 205
Cdd:cd19372 112 TKSHA-IHWERISKLLLQHIAKYVS--VLYCLGKTDFSNVRARLEVPVTVVVGYHPAARD--GQFDKERAFEIVNVLLEL 186
|
170
....*....|
gi 487750253 206 KGKTPVQWCE 215
Cdd:cd19372 187 NGKPPVNWAQ 196
|
|
| |
