|
Name |
Accession |
Description |
Interval |
E-value |
| Ung |
COG0692 |
Uracil-DNA glycosylase [Replication, recombination and repair]; |
3-213 |
6.24e-144 |
|
Uracil-DNA glycosylase [Replication, recombination and repair];
Pssm-ID: 440456 Cd Length: 221 Bit Score: 400.19 E-value: 6.24e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579942094 3 WSQIFHDITTKHDFKAMHDFLEKEYS-TAIVYPDRENIYQAFDLTPFENIKVVILGQDPYHGPNQAHGLAFSVQPNAKFP 81
Cdd:COG0692 9 WKEALAEEFEKPYFQALGAFLKAEYAaGKTIYPPGEDIFRAFNLTPFDDVKVVILGQDPYHGPGQAHGLSFSVPPGVPLP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579942094 82 PSLRNMYKELADDIGC-VRQTPHLQDWAREGVLLLNTVLTVRQGEANSHRDIGWETFTDEIIKAVSDYKEHVVFILWGKP 160
Cdd:COG0692 89 PSLRNIYKELEDDLGIpIPNHGDLTSWAEQGVLLLNTVLTVRAGQAGSHAGKGWETFTDAVIRALNARKEPVVFLLWGAY 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 579942094 161 AQQKIKLIDTSKHCIIKSVHPSPLSAYRGFFGSKPYSKANAYLESVGKSPINW 213
Cdd:COG0692 169 AQKKAALIDASKHLVLESPHPSPLSAHRGFFGSKPFSKANAYLEEQGKTPIDW 221
|
|
| PRK05254 |
PRK05254 |
uracil-DNA glycosylase; Provisional |
1-214 |
3.53e-142 |
|
uracil-DNA glycosylase; Provisional
Pssm-ID: 235376 Cd Length: 224 Bit Score: 395.68 E-value: 3.53e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579942094 1 MEWSQIFHDITTKHDFKAMHDFLEKE-YSTAIVYPDRENIYQAFDLTPFENIKVVILGQDPYHGPNQAHGLAFSVQPNAK 79
Cdd:PRK05254 8 PSWKEVLKPEFKKPYFQELLEFLRAErAAGKTIYPPGEDIFRAFNLTPFDDVKVVILGQDPYHGPGQAHGLSFSVPPGVP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579942094 80 FPPSLRNMYKELADDIGCVR-QTPHLQDWAREGVLLLNTVLTVRQGEANSHRDIGWETFTDEIIKAVSDYKEHVVFILWG 158
Cdd:PRK05254 88 IPPSLRNIFKELEDDLGFPIpNHGDLTSWAEQGVLLLNTVLTVEAGQANSHAGKGWETFTDAVIKALNERREPVVFILWG 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 579942094 159 KPAQQKIKLIDTSKHCIIKSVHPSPLSAYRGFFGSKPYSKANAYLESVGKSPINWC 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 |
1.23e-131 |
|
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: 368.32 E-value: 1.23e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579942094 16 FKAMHDFLEKEYSTAIVYPDRENIYQAFDLTPFENIKVVILGQDPYHGPNQAHGLAFSVQPNAKFPPSLRNMYKELADDI 95
Cdd:cd10027 2 FKKLEAFLEEEYKKKTIYPPKEDIFRAFELTPLDDVKVVILGQDPYHGPGQAHGLAFSVPPGVKIPPSLRNIFKELKSDL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579942094 96 GC-VRQTPHLQDWAREGVLLLNTVLTVRQGEANSHRDIGWETFTDEIIKAVSDYKEHVVFILWGKPAQQKIKLIDTSKHC 174
Cdd:cd10027 82 GIfPPKHGDLSSWAKQGVLLLNTVLTVEAGKPGSHKNIGWETFTDAVIKALSEKNENVVFLLWGNHAQKKKKLIDKKKHL 161
|
170 180 190
....*....|....*....|....*....|....*....
gi 579942094 175 IIKSVHPSPLSAYRGFFGSKPYSKANAYLESVGKSPINW 213
Cdd:cd10027 162 VLESSHPSPLSAYRGFFGSKHFSKANEYLKKHGKKPIDW 200
|
|
| ung |
TIGR00628 |
uracil-DNA glycosylase; All proteins in this family for which functions are known are ... |
16-208 |
1.39e-106 |
|
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: 305.29 E-value: 1.39e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579942094 16 FKAMHDFLEKEYSTAIVYPDRENIYQAFDLTPFENIKVVILGQDPYHGPNQAHGLAFSVQPNAKFPPSLRNMYKELADDI 95
Cdd:TIGR00628 17 FQELLAFYKRERAQETVYPPKEDVFAWTRLCPPEDVKVVILGQDPYHGPGQAHGLAFSVKRGVPIPPSLKNIFKELEADY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579942094 96 GCVRQTPH--LQDWAREGVLLLNTVLTVRQGEANSHRDIGWETFTDEIIKAVSDYKEHVVFILWGKPAQQKIKLIDTSKH 173
Cdd:TIGR00628 97 PDFPPPKHgcLEAWARQGVLLLNTVLTVRRGQPGSHSGLGWERFTDAVISRLSERLDGLVFMLWGAHAQKKKSLIDAKKH 176
|
170 180 190
....*....|....*....|....*....|....*
gi 579942094 174 CIIKSVHPSPLSAYRGFFGSKPYSKANAYLESVGK 208
Cdd:TIGR00628 177 LVLKSPHPSPLSARRGFFGCRHFSKANEYLEKHGK 211
|
|
| UDG |
smart00986 |
Uracil DNA glycosylase superfamily; |
45-203 |
1.75e-35 |
|
Uracil DNA glycosylase superfamily;
Pssm-ID: 214956 Cd Length: 156 Bit Score: 122.88 E-value: 1.75e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579942094 45 LTPFENIKVVILGQDPY------HGP-NQAHGLAFSVQPNA----KFPPSLRNMYKELADDIGCVRQTPhlqdWAREGVL 113
Cdd:smart00986 2 GTGDPNAKVLIVGQAPGaseedrGGPfVGAAGLLLSVMLGVaglpRLPPYLTNIVKCRPPDAGNRRPTS----WELQGCL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579942094 114 LlnTVLTVRQGEANSHRDIGWETFTDEIIKAVSdyKEHVVFILWGKPAQQKIKLidtskHCIIKSVHPSPLSAYRgfFGS 193
Cdd:smart00986 78 L--PWLTVELALARPHLILLLGKFAAQALLGLL--RRPLVFGLRGRVAQLKGKG-----HRVLPLPHPSPLNRNF--FPA 146
|
170
....*....|
gi 579942094 194 KPYSKANAYL 203
Cdd:smart00986 147 KKFAAWNDLL 156
|
|
| UDG |
pfam03167 |
Uracil DNA glycosylase superfamily; |
46-204 |
1.57e-23 |
|
Uracil DNA glycosylase superfamily;
Pssm-ID: 397331 Cd Length: 154 Bit Score: 92.02 E-value: 1.57e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579942094 46 TPFENIKVVILGQDPYHGpNQAHGLAFSVQPNAKFPPSLRNMykeladdiGCVRQTPHLQdwareGVLLLNTVLTVRQGE 125
Cdd:pfam03167 3 FGPPNAKVLIVGEAPGAD-EDATGLPFVGRAGNLLWKLLNAA--------GLTRDLFSPQ-----GVYITNVVKCRPGNR 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579942094 126 ANSHR---DIGWEtFTDEIIKAVSDykehVVFILWGKPAQQKI-----------KLIDTSKHCIIKSVHPSPLSAYRgff 191
Cdd:pfam03167 69 RKPTSheiDACWP-YLEAEIELLRP----RVIVLLGKTAAKALlglkkitklrgKLIDLKGIPVLPTPHPSPLLRNK--- 140
|
170
....*....|...
gi 579942094 192 gSKPYSKANAYLE 204
Cdd:pfam03167 141 -LNPFLKANAWED 152
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Ung |
COG0692 |
Uracil-DNA glycosylase [Replication, recombination and repair]; |
3-213 |
6.24e-144 |
|
Uracil-DNA glycosylase [Replication, recombination and repair];
Pssm-ID: 440456 Cd Length: 221 Bit Score: 400.19 E-value: 6.24e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579942094 3 WSQIFHDITTKHDFKAMHDFLEKEYS-TAIVYPDRENIYQAFDLTPFENIKVVILGQDPYHGPNQAHGLAFSVQPNAKFP 81
Cdd:COG0692 9 WKEALAEEFEKPYFQALGAFLKAEYAaGKTIYPPGEDIFRAFNLTPFDDVKVVILGQDPYHGPGQAHGLSFSVPPGVPLP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579942094 82 PSLRNMYKELADDIGC-VRQTPHLQDWAREGVLLLNTVLTVRQGEANSHRDIGWETFTDEIIKAVSDYKEHVVFILWGKP 160
Cdd:COG0692 89 PSLRNIYKELEDDLGIpIPNHGDLTSWAEQGVLLLNTVLTVRAGQAGSHAGKGWETFTDAVIRALNARKEPVVFLLWGAY 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 579942094 161 AQQKIKLIDTSKHCIIKSVHPSPLSAYRGFFGSKPYSKANAYLESVGKSPINW 213
Cdd:COG0692 169 AQKKAALIDASKHLVLESPHPSPLSAHRGFFGSKPFSKANAYLEEQGKTPIDW 221
|
|
| PRK05254 |
PRK05254 |
uracil-DNA glycosylase; Provisional |
1-214 |
3.53e-142 |
|
uracil-DNA glycosylase; Provisional
Pssm-ID: 235376 Cd Length: 224 Bit Score: 395.68 E-value: 3.53e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579942094 1 MEWSQIFHDITTKHDFKAMHDFLEKE-YSTAIVYPDRENIYQAFDLTPFENIKVVILGQDPYHGPNQAHGLAFSVQPNAK 79
Cdd:PRK05254 8 PSWKEVLKPEFKKPYFQELLEFLRAErAAGKTIYPPGEDIFRAFNLTPFDDVKVVILGQDPYHGPGQAHGLSFSVPPGVP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579942094 80 FPPSLRNMYKELADDIGCVR-QTPHLQDWAREGVLLLNTVLTVRQGEANSHRDIGWETFTDEIIKAVSDYKEHVVFILWG 158
Cdd:PRK05254 88 IPPSLRNIFKELEDDLGFPIpNHGDLTSWAEQGVLLLNTVLTVEAGQANSHAGKGWETFTDAVIKALNERREPVVFILWG 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 579942094 159 KPAQQKIKLIDTSKHCIIKSVHPSPLSAYRGFFGSKPYSKANAYLESVGKSPINWC 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 |
1.23e-131 |
|
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: 368.32 E-value: 1.23e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579942094 16 FKAMHDFLEKEYSTAIVYPDRENIYQAFDLTPFENIKVVILGQDPYHGPNQAHGLAFSVQPNAKFPPSLRNMYKELADDI 95
Cdd:cd10027 2 FKKLEAFLEEEYKKKTIYPPKEDIFRAFELTPLDDVKVVILGQDPYHGPGQAHGLAFSVPPGVKIPPSLRNIFKELKSDL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579942094 96 GC-VRQTPHLQDWAREGVLLLNTVLTVRQGEANSHRDIGWETFTDEIIKAVSDYKEHVVFILWGKPAQQKIKLIDTSKHC 174
Cdd:cd10027 82 GIfPPKHGDLSSWAKQGVLLLNTVLTVEAGKPGSHKNIGWETFTDAVIKALSEKNENVVFLLWGNHAQKKKKLIDKKKHL 161
|
170 180 190
....*....|....*....|....*....|....*....
gi 579942094 175 IIKSVHPSPLSAYRGFFGSKPYSKANAYLESVGKSPINW 213
Cdd:cd10027 162 VLESSHPSPLSAYRGFFGSKHFSKANEYLKKHGKKPIDW 200
|
|
| ung |
TIGR00628 |
uracil-DNA glycosylase; All proteins in this family for which functions are known are ... |
16-208 |
1.39e-106 |
|
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: 305.29 E-value: 1.39e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579942094 16 FKAMHDFLEKEYSTAIVYPDRENIYQAFDLTPFENIKVVILGQDPYHGPNQAHGLAFSVQPNAKFPPSLRNMYKELADDI 95
Cdd:TIGR00628 17 FQELLAFYKRERAQETVYPPKEDVFAWTRLCPPEDVKVVILGQDPYHGPGQAHGLAFSVKRGVPIPPSLKNIFKELEADY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579942094 96 GCVRQTPH--LQDWAREGVLLLNTVLTVRQGEANSHRDIGWETFTDEIIKAVSDYKEHVVFILWGKPAQQKIKLIDTSKH 173
Cdd:TIGR00628 97 PDFPPPKHgcLEAWARQGVLLLNTVLTVRRGQPGSHSGLGWERFTDAVISRLSERLDGLVFMLWGAHAQKKKSLIDAKKH 176
|
170 180 190
....*....|....*....|....*....|....*
gi 579942094 174 CIIKSVHPSPLSAYRGFFGSKPYSKANAYLESVGK 208
Cdd:TIGR00628 177 LVLKSPHPSPLSARRGFFGCRHFSKANEYLEKHGK 211
|
|
| PHA03347 |
PHA03347 |
uracil DNA glycosylase; Provisional |
29-213 |
9.98e-69 |
|
uracil DNA glycosylase; Provisional
Pssm-ID: 177588 Cd Length: 252 Bit Score: 210.68 E-value: 9.98e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579942094 29 TAIVYPDRENIYQAFDLTPFENIKVVILGQDPYHGpNQAHGLAFSVQPNAKFPPSLRNMYKELADDIGCVRQTPH--LQD 106
Cdd:PHA03347 57 QTVIYPPEDRIMAWSYLCDPEDIKVVILGQDPYHG-GQANGLAFSVAYGFPVPPSLRNIFAELHRSVPDFSPPDHgcLDA 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579942094 107 WAREGVLLLNTVLTVRQGEANSHRDIGWETFTDEIIKAVSDYKEHVVFILWGKPAQQKIKLIDTSKHCIIKSVHPSPLSA 186
Cdd:PHA03347 136 WARQGVLLLNTILTVEKGKPGSHSDLGWAWFTDYIISSLSEKLKACVFMLWGSKAIDKASLINSQKHLVLKAQHPSPLAA 215
|
170 180 190
....*....|....*....|....*....|....
gi 579942094 187 ---YRG----FFGSKPYSKANAYLESVGKSPINW 213
Cdd:PHA03347 216 nstRSStwpkFLGCNHFVLANKYLTQHGKGPIDW 249
|
|
| PHA03200 |
PHA03200 |
uracil DNA glycosylase; Provisional |
21-213 |
1.05e-64 |
|
uracil DNA glycosylase; Provisional
Pssm-ID: 165467 Cd Length: 255 Bit Score: 200.72 E-value: 1.05e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579942094 21 DFLEKEYSTAIVYPDRENIYQAFDLTPFENIKVVILGQDPYHGpNQAHGLAFSVQPNAKFPPSLRNMYKELADDI----- 95
Cdd:PHA03200 55 DAVDRDRQRLTVYPPPEDVHRWSRLCSPEDVKVVIVGQDPYHD-GSACGLAFGTVRGRSAPPSLKNVFRELERTVpnfsr 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579942094 96 ---GCvrqtphLQDWAREGVLLLNTVLTVRQGEANSHRDIGWETFTDEIIKAVSDYKEHVVFILWGKPAQQKIKLIDTSK 172
Cdd:PHA03200 134 pdsGC------LDSWCRQGVLLLNTVFTVVHGQPGSHEALGWQTLSDRVISRLSEKREHLVFMLWGAQAQKLEYLIDSRK 207
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 579942094 173 HCIIKSVHPSP--LSAYRGFFGSKPYSKANAYLESVGKSPINW 213
Cdd:PHA03200 208 HLILKSAHPSPrvKGARTPFIGNNHFVLANEYLSTHGKRPIDW 250
|
|
| PHA03201 |
PHA03201 |
uracil DNA glycosylase; Provisional |
24-213 |
3.16e-54 |
|
uracil DNA glycosylase; Provisional
Pssm-ID: 165468 Cd Length: 318 Bit Score: 175.85 E-value: 3.16e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579942094 24 EKEYSTAIVYPDRENIYQAFDLTPFENIKVVILGQDPYHGPNQAHGLAFSVQPNAKFPPSLRNMYKELADDIGCVRQTPH 103
Cdd:PHA03201 127 ERRCRTEEVLPPREDVFSWTRYCTPDEVRVVIIGQDPYHQPGQAHGLAFSVRPGTPAPPSLRNILAAVRNCCPDARMSGH 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579942094 104 --LQDWAREGVLLLNTVLTVRQGEANSHRDIGWETFTDEIIKAVSDYKEHVVFILWGKPAQQKIKlIDTSKHCIIKSVHP 181
Cdd:PHA03201 207 gcLEKWARGGVLLLNTTLTVRRGEPASHAKIGWDRFVGSVVRRLAASRPGLVFMLWGAHAQNAIR-PDPRVHRVLTYSHP 285
|
170 180 190
....*....|....*....|....*....|...
gi 579942094 182 SPLSayRGFFGS-KPYSKANAYLESVGKSPINW 213
Cdd:PHA03201 286 SPLS--KVPFGScRHFCLANQYLRERSLAPIDW 316
|
|
| PHA03202 |
PHA03202 |
uracil DNA glycosylase; Provisional |
32-213 |
1.06e-52 |
|
uracil DNA glycosylase; Provisional
Pssm-ID: 165469 Cd Length: 313 Bit Score: 171.80 E-value: 1.06e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579942094 32 VYPDRENIYQAFDLTPFENIKVVILGQDPYHGPNQAHGLAFSVQPNAKFPPSLRNMYKELADDIGCVRQTPH--LQDWAR 109
Cdd:PHA03202 129 VFPPKEDIFAWTRFSPPEKVRVVIVGQDPYHAPGQAHGLAFSVRKGVPVPPSLRNIYSAVQKSYPSFRPPMHgfLEKWAE 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579942094 110 EGVLLLNTVLTVRQGEANSHRDIGWETFTDEIIKAVSDYKEHVVFILWGKPAQQKIKlIDTSKHCIIKSVHPSPLSayRG 189
Cdd:PHA03202 209 QGVLLINTTLTVARGKPGSHATLGWHRLVRAVIDRLCTTSQGLVFMLWGAHAQKSCS-PNRQHHLVLTYGHPSPLS--RV 285
|
170 180
....*....|....*....|....*
gi 579942094 190 FFGSKP-YSKANAYLESVGKSPINW 213
Cdd:PHA03202 286 NFRDCPhFLEANAYLTKTGRKPVDW 310
|
|
| UDG-F1-like |
cd19371 |
Uracil DNA glycosylase family 1, includes Human uracil DNA glycosylase, Vaccinia virus protein ... |
53-185 |
9.94e-48 |
|
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: 153.26 E-value: 9.94e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579942094 53 VVILGQDPYHGPNQAHGLAFSVQPNAKFPPSLRNMYKELADDIGC--VRQTPHLQDWAREGVLLLNTVLTVRQGEANSHR 130
Cdd:cd19371 1 VVIIGQDPYPSPGHAGGLAFSVTSEVPPPKSLRNIYKELERDYSSflPPGNGTLEFWARQGVLLLNAALTCESGKPKSHY 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 579942094 131 DiGWETFTDEIIKAVSDYKEHVVFILWGKPAQQKIKLIDTSKHCIIKSVHPSPLS 185
Cdd:cd19371 81 L-LWEPFIKAFIRYISAHNKGLVFLLFGSDAQKLRKKINGRNVHVFKADHPSPAD 134
|
|
| PHA03204 |
PHA03204 |
uracil DNA glycosylase; Provisional |
24-213 |
1.66e-47 |
|
uracil DNA glycosylase; Provisional
Pssm-ID: 165471 Cd Length: 322 Bit Score: 158.58 E-value: 1.66e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579942094 24 EKEYSTAIVYPDRENIYQAFDLTPFENIKVVILGQDPYHGPNQAHGLAFSVQPNAKFPPSLRNMYK---------ELADD 94
Cdd:PHA03204 127 ERRARYEEVYPPKSDIFAWTRYCAPDHVKVVIVGQDPYANPGQAHGLAFSVKPGSPIPPSLKNILAavkacypsiELGSH 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579942094 95 iGCvrqtphLQDWAREGVLLLNTVLTVRQGEANSHRDIGWETFTDEIIKAVSDYKEHVVFILWGKPAQQKIKLIDTS-KH 173
Cdd:PHA03204 207 -GC------LEDWAKRGVLLLNSVLTVKRGDPGSHHSVGWQILVRNVLRRLSQSTRGIVFMLWGAQAQTMYFQTDNDdRH 279
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 579942094 174 CIIKSVHPSPLSAyRGFFGSKPYSKANAYLESVGKSPINW 213
Cdd:PHA03204 280 LVLKYSHPSPLSR-KPFAHCTHFKDANEFLCKMGKGAIDW 318
|
|
| PHA03199 |
PHA03199 |
uracil DNA glycosylase; Provisional |
32-213 |
6.10e-45 |
|
uracil DNA glycosylase; Provisional
Pssm-ID: 165466 Cd Length: 304 Bit Score: 151.70 E-value: 6.10e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579942094 32 VYPDRENIYQAFDLTPFENIKVVILGQDPYHGPNQAHGLAFSVQPNAKFPPSLRNMYKELADDIGCVRQTPH--LQDWAR 109
Cdd:PHA03199 121 IFPIKGDIFAWTRFCGPEKIRVVIIGQDPYHGAGHAHGLAFSVKRGIPIPPSLKNIFAALMESYPHLPLPTHgcLDNWAR 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579942094 110 EGVLLLNTVLTVRQGEANSHRDIGWETFTDEIIKAVSDYKEHVVFILWGKPAQQKIKlIDTSKHCIIKSVHPSPLSAYRg 189
Cdd:PHA03199 201 QGVLLLNTTLTVKRGTPGSHFYLGWDMLIKRMLKRLCENRTGLVFMLWGAHAQKTIQ-PNPRCHLVLTHAHPSPLSRSE- 278
|
170 180
....*....|....*....|....
gi 579942094 190 FFGSKPYSKANAYLESVGKSPINW 213
Cdd:PHA03199 279 FRNCKHFLQANEYFLKKGEPEIDW 302
|
|
| UDG |
smart00986 |
Uracil DNA glycosylase superfamily; |
45-203 |
1.75e-35 |
|
Uracil DNA glycosylase superfamily;
Pssm-ID: 214956 Cd Length: 156 Bit Score: 122.88 E-value: 1.75e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579942094 45 LTPFENIKVVILGQDPY------HGP-NQAHGLAFSVQPNA----KFPPSLRNMYKELADDIGCVRQTPhlqdWAREGVL 113
Cdd:smart00986 2 GTGDPNAKVLIVGQAPGaseedrGGPfVGAAGLLLSVMLGVaglpRLPPYLTNIVKCRPPDAGNRRPTS----WELQGCL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579942094 114 LlnTVLTVRQGEANSHRDIGWETFTDEIIKAVSdyKEHVVFILWGKPAQQKIKLidtskHCIIKSVHPSPLSAYRgfFGS 193
Cdd:smart00986 78 L--PWLTVELALARPHLILLLGKFAAQALLGLL--RRPLVFGLRGRVAQLKGKG-----HRVLPLPHPSPLNRNF--FPA 146
|
170
....*....|
gi 579942094 194 KPYSKANAYL 203
Cdd:smart00986 147 KKFAAWNDLL 156
|
|
| UDG |
pfam03167 |
Uracil DNA glycosylase superfamily; |
46-204 |
1.57e-23 |
|
Uracil DNA glycosylase superfamily;
Pssm-ID: 397331 Cd Length: 154 Bit Score: 92.02 E-value: 1.57e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579942094 46 TPFENIKVVILGQDPYHGpNQAHGLAFSVQPNAKFPPSLRNMykeladdiGCVRQTPHLQdwareGVLLLNTVLTVRQGE 125
Cdd:pfam03167 3 FGPPNAKVLIVGEAPGAD-EDATGLPFVGRAGNLLWKLLNAA--------GLTRDLFSPQ-----GVYITNVVKCRPGNR 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579942094 126 ANSHR---DIGWEtFTDEIIKAVSDykehVVFILWGKPAQQKI-----------KLIDTSKHCIIKSVHPSPLSAYRgff 191
Cdd:pfam03167 69 RKPTSheiDACWP-YLEAEIELLRP----RVIVLLGKTAAKALlglkkitklrgKLIDLKGIPVLPTPHPSPLLRNK--- 140
|
170
....*....|...
gi 579942094 192 gSKPYSKANAYLE 204
Cdd:pfam03167 141 -LNPFLKANAWED 152
|
|
| UDG-like |
cd09593 |
uracil-DNA glycosylases (UDG) and related enzymes; Uracil-DNA glycosylases (UDGs) initiate ... |
53-186 |
4.72e-20 |
|
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: 82.05 E-value: 4.72e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579942094 53 VVILGQDPYHGPNQAHGLafsvqpnaKFPPSLRNMYKELADDIGCVRqtphlqdWAREGVLLLNTVLTVRQGEANSHRDi 132
Cdd:cd09593 1 VLIVGQNPGPHGARAGGV--------PPGPSGNRLWRLLAAAGGTPR-------LFRYGVGLTNTVPRGPPGAAAGSEK- 64
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 579942094 133 GWETFTDEII-KAVSDYKEHVVfILWGKPAQQKIKLIDTSK-------HCIIKSVHPSPLSA 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 ... |
34-215 |
1.40e-07 |
|
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: 50.13 E-value: 1.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579942094 34 PDRENIYQAFDlTPFENIKVVILGQDPYhgPNQAHGLAFsvqpnaKFPPSLRNMYKELADDIGCVRQTPHLQDW---ARE 110
Cdd:cd19372 26 PIPENFFKQLK-QPLRDKRVCICGIDPY--PTDATGVPF------ESPDFSKKTIRAIAEAISRRTGVSLYKGYnfaLVE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579942094 111 GVLLLNTVLTVRQGEANSHRdIGWETFTDEIIKAVSDYKEhvVFILWGKPAQQKIKLIDTSKHCIIKSVHPSPLSayRGF 190
Cdd:cd19372 97 GVLAWNYYLSCREGETKSHA-IHWERISKLLLQHIAKYVS--VLYCLGKTDFSNVRARLEVPVTVVVGYHPAARD--GQF 171
|
170 180
....*....|....*....|....*
gi 579942094 191 FGSKPYSKANAYLESVGKSPINWCE 215
Cdd:cd19372 172 DKERAFEIVNVLLELNGKPPVNWAQ 196
|
|
| |
