|
Name |
Accession |
Description |
Interval |
E-value |
| Ung |
COG0692 |
Uracil-DNA glycosylase [Replication, recombination and repair]; |
5-221 |
3.30e-146 |
|
Uracil-DNA glycosylase [Replication, recombination and repair];
Pssm-ID: 440456 Cd Length: 221 Bit Score: 406.35 E-value: 3.30e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189327977 5 DLLPESWRGVLGEELQKPYVKELADFVEEERSKG-PVYPPREQVFAALDATPYEKVKVLVLGQDPYHGEGQGHGLCFSVR 83
Cdd:COG0692 3 VLLEPSWKEALAEEFEKPYFQALGAFLKAEYAAGkTIYPPGEDIFRAFNLTPFDDVKVVILGQDPYHGPGQAHGLSFSVP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189327977 84 PGVKTPPSLRNIYKEMQEELGLPVPDNGYLMPWAEQGVLLLNAVLTVRGGEANSHKGKGWEKITDAVIRAVAERPDPAVF 163
Cdd:COG0692 83 PGVPLPPSLRNIYKELEDDLGIPIPNHGDLTSWAEQGVLLLNTVLTVRAGQAGSHAGKGWETFTDAVIRALNARKEPVVF 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2189327977 164 VLWGNYAQKKLPLIDEERHVVVKGAHPSPLSAKK-FFGSRPFTQINEAVAAQGHQPIDW 221
Cdd:COG0692 163 LLWGAYAQKKAALIDASKHLVLESPHPSPLSAHRgFFGSKPFSKANAYLEEQGKTPIDW 221
|
|
| PRK05254 |
PRK05254 |
uracil-DNA glycosylase; Provisional |
3-223 |
6.11e-142 |
|
uracil-DNA glycosylase; Provisional
Pssm-ID: 235376 Cd Length: 224 Bit Score: 395.68 E-value: 6.11e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189327977 3 DIDLLPESWRGVLGEELQKPYVKELADFVEEERSKG-PVYPPREQVFAALDATPYEKVKVLVLGQDPYHGEGQGHGLCFS 81
Cdd:PRK05254 2 MKMLLEPSWKEVLKPEFKKPYFQELLEFLRAERAAGkTIYPPGEDIFRAFNLTPFDDVKVVILGQDPYHGPGQAHGLSFS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189327977 82 VRPGVKTPPSLRNIYKEMQEELGLPVPDNGYLMPWAEQGVLLLNAVLTVRGGEANSHKGKGWEKITDAVIRAVAERPDPA 161
Cdd:PRK05254 82 VPPGVPIPPSLRNIFKELEDDLGFPIPNHGDLTSWAEQGVLLLNTVLTVEAGQANSHAGKGWETFTDAVIKALNERREPV 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2189327977 162 VFVLWGNYAQKKLPLIDEERHVVVKGAHPSPLSAKK-FFGSRPFTQINEAVAAQGHQPIDWRI 223
Cdd:PRK05254 162 VFILWGSHAQKKKALIDNSKHLILESPHPSPLSAHRgFFGSKHFSKANALLKQHGKTPIDWQL 224
|
|
| UDG-F1-like |
cd10027 |
Uracil DNA glycosylase family 1 subfamily, includes Human uracil DNA glycosylase and similar ... |
23-221 |
7.77e-125 |
|
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: 351.37 E-value: 7.77e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189327977 23 YVKELADFVEEERSKGPVYPPREQVFAALDATPYEKVKVLVLGQDPYHGEGQGHGLCFSVRPGVKTPPSLRNIYKEMQEE 102
Cdd:cd10027 1 YFKKLEAFLEEEYKKKTIYPPKEDIFRAFELTPLDDVKVVILGQDPYHGPGQAHGLAFSVPPGVKIPPSLRNIFKELKSD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189327977 103 LGLPVPDNGYLMPWAEQGVLLLNAVLTVRGGEANSHKGKGWEKITDAVIRAVAERPDPAVFVLWGNYAQKKLPLIDEERH 182
Cdd:cd10027 81 LGIFPPKHGDLSSWAKQGVLLLNTVLTVEAGKPGSHKNIGWETFTDAVIKALSEKNENVVFLLWGNHAQKKKKLIDKKKH 160
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2189327977 183 VVVKGAHPSPLSAKK-FFGSRPFTQINEAVAAQGHQPIDW 221
Cdd:cd10027 161 LVLESSHPSPLSAYRgFFGSKHFSKANEYLKKHGKKPIDW 200
|
|
| ung |
TIGR00628 |
uracil-DNA glycosylase; All proteins in this family for which functions are known are ... |
8-209 |
4.64e-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: 304.52 E-value: 4.64e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189327977 8 PESWRGVLGEELQKPYVKELADFVEEERSKGPVYPPREQVFAALDATPYEKVKVLVLGQDPYHGEGQGHGLCFSVRPGVK 87
Cdd:TIGR00628 1 SPSWRAFLQPEFKKPYFQELLAFYKRERAQETVYPPKEDVFAWTRLCPPEDVKVVILGQDPYHGPGQAHGLAFSVKRGVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189327977 88 TPPSLRNIYKEMQEELG-LPVPDNGYLMPWAEQGVLLLNAVLTVRGGEANSHKGKGWEKITDAVIRAVAERPDPAVFVLW 166
Cdd:TIGR00628 81 IPPSLKNIFKELEADYPdFPPPKHGCLEAWARQGVLLLNTVLTVRRGQPGSHSGLGWERFTDAVISRLSERLDGLVFMLW 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2189327977 167 GNYAQKKLPLIDEERHVVVKGAHPSPLSAKK-FFGSRPFTQINE 209
Cdd:TIGR00628 161 GAHAQKKKSLIDAKKHLVLKSPHPSPLSARRgFFGCRHFSKANE 204
|
|
| UDG |
smart00986 |
Uracil DNA glycosylase superfamily; |
54-210 |
8.63e-30 |
|
Uracil DNA glycosylase superfamily;
Pssm-ID: 214956 Cd Length: 156 Bit Score: 108.24 E-value: 8.63e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189327977 54 TPYEKVKVLVLGQDPYHGEGQGH-------GLCFSVRPGV----KTPPSLRNIYKEMQeelglPVPDNGYLMPWAEQGVL 122
Cdd:smart00986 3 TGDPNAKVLIVGQAPGASEEDRGgpfvgaaGLLLSVMLGVaglpRLPPYLTNIVKCRP-----PDAGNRRPTSWELQGCL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189327977 123 LlnAVLTVRGGEANSHKGKGWEKITDAVIRAVAERpdPAVFVLWGNYAQKKLPLideerHVVVKGAHPSPLSAkKFFGSR 202
Cdd:smart00986 78 L--PWLTVELALARPHLILLLGKFAAQALLGLLRR--PLVFGLRGRVAQLKGKG-----HRVLPLPHPSPLNR-NFFPAK 147
|
....*...
gi 2189327977 203 PFTQINEA 210
Cdd:smart00986 148 KFAAWNDL 155
|
|
| UDG |
pfam03167 |
Uracil DNA glycosylase superfamily; |
57-209 |
1.51e-19 |
|
Uracil DNA glycosylase superfamily;
Pssm-ID: 397331 Cd Length: 154 Bit Score: 81.62 E-value: 1.51e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189327977 57 EKVKVLVLGQDPYHGEGQgHGLCFSVRPGvktppslrNIYKEMQEELGLPvpdngyLMPWAEQGVLLLNAVLTVRG--GE 134
Cdd:pfam03167 6 PNAKVLIVGEAPGADEDA-TGLPFVGRAG--------NLLWKLLNAAGLT------RDLFSPQGVYITNVVKCRPGnrRK 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189327977 135 ANSHKGK-GWEkITDAVIRAVAerpdPAVFVLWGNYAQKKL-----------PLIDEERHVVVKGAHPSPLSAKKffgSR 202
Cdd:pfam03167 71 PTSHEIDaCWP-YLEAEIELLR----PRVIVLLGKTAAKALlglkkitklrgKLIDLKGIPVLPTPHPSPLLRNK---LN 142
|
....*..
gi 2189327977 203 PFTQINE 209
Cdd:pfam03167 143 PFLKANA 149
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Ung |
COG0692 |
Uracil-DNA glycosylase [Replication, recombination and repair]; |
5-221 |
3.30e-146 |
|
Uracil-DNA glycosylase [Replication, recombination and repair];
Pssm-ID: 440456 Cd Length: 221 Bit Score: 406.35 E-value: 3.30e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189327977 5 DLLPESWRGVLGEELQKPYVKELADFVEEERSKG-PVYPPREQVFAALDATPYEKVKVLVLGQDPYHGEGQGHGLCFSVR 83
Cdd:COG0692 3 VLLEPSWKEALAEEFEKPYFQALGAFLKAEYAAGkTIYPPGEDIFRAFNLTPFDDVKVVILGQDPYHGPGQAHGLSFSVP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189327977 84 PGVKTPPSLRNIYKEMQEELGLPVPDNGYLMPWAEQGVLLLNAVLTVRGGEANSHKGKGWEKITDAVIRAVAERPDPAVF 163
Cdd:COG0692 83 PGVPLPPSLRNIYKELEDDLGIPIPNHGDLTSWAEQGVLLLNTVLTVRAGQAGSHAGKGWETFTDAVIRALNARKEPVVF 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2189327977 164 VLWGNYAQKKLPLIDEERHVVVKGAHPSPLSAKK-FFGSRPFTQINEAVAAQGHQPIDW 221
Cdd:COG0692 163 LLWGAYAQKKAALIDASKHLVLESPHPSPLSAHRgFFGSKPFSKANAYLEEQGKTPIDW 221
|
|
| PRK05254 |
PRK05254 |
uracil-DNA glycosylase; Provisional |
3-223 |
6.11e-142 |
|
uracil-DNA glycosylase; Provisional
Pssm-ID: 235376 Cd Length: 224 Bit Score: 395.68 E-value: 6.11e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189327977 3 DIDLLPESWRGVLGEELQKPYVKELADFVEEERSKG-PVYPPREQVFAALDATPYEKVKVLVLGQDPYHGEGQGHGLCFS 81
Cdd:PRK05254 2 MKMLLEPSWKEVLKPEFKKPYFQELLEFLRAERAAGkTIYPPGEDIFRAFNLTPFDDVKVVILGQDPYHGPGQAHGLSFS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189327977 82 VRPGVKTPPSLRNIYKEMQEELGLPVPDNGYLMPWAEQGVLLLNAVLTVRGGEANSHKGKGWEKITDAVIRAVAERPDPA 161
Cdd:PRK05254 82 VPPGVPIPPSLRNIFKELEDDLGFPIPNHGDLTSWAEQGVLLLNTVLTVEAGQANSHAGKGWETFTDAVIKALNERREPV 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2189327977 162 VFVLWGNYAQKKLPLIDEERHVVVKGAHPSPLSAKK-FFGSRPFTQINEAVAAQGHQPIDWRI 223
Cdd:PRK05254 162 VFILWGSHAQKKKALIDNSKHLILESPHPSPLSAHRgFFGSKHFSKANALLKQHGKTPIDWQL 224
|
|
| UDG-F1-like |
cd10027 |
Uracil DNA glycosylase family 1 subfamily, includes Human uracil DNA glycosylase and similar ... |
23-221 |
7.77e-125 |
|
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: 351.37 E-value: 7.77e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189327977 23 YVKELADFVEEERSKGPVYPPREQVFAALDATPYEKVKVLVLGQDPYHGEGQGHGLCFSVRPGVKTPPSLRNIYKEMQEE 102
Cdd:cd10027 1 YFKKLEAFLEEEYKKKTIYPPKEDIFRAFELTPLDDVKVVILGQDPYHGPGQAHGLAFSVPPGVKIPPSLRNIFKELKSD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189327977 103 LGLPVPDNGYLMPWAEQGVLLLNAVLTVRGGEANSHKGKGWEKITDAVIRAVAERPDPAVFVLWGNYAQKKLPLIDEERH 182
Cdd:cd10027 81 LGIFPPKHGDLSSWAKQGVLLLNTVLTVEAGKPGSHKNIGWETFTDAVIKALSEKNENVVFLLWGNHAQKKKKLIDKKKH 160
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2189327977 183 VVVKGAHPSPLSAKK-FFGSRPFTQINEAVAAQGHQPIDW 221
Cdd:cd10027 161 LVLESSHPSPLSAYRgFFGSKHFSKANEYLKKHGKKPIDW 200
|
|
| ung |
TIGR00628 |
uracil-DNA glycosylase; All proteins in this family for which functions are known are ... |
8-209 |
4.64e-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: 304.52 E-value: 4.64e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189327977 8 PESWRGVLGEELQKPYVKELADFVEEERSKGPVYPPREQVFAALDATPYEKVKVLVLGQDPYHGEGQGHGLCFSVRPGVK 87
Cdd:TIGR00628 1 SPSWRAFLQPEFKKPYFQELLAFYKRERAQETVYPPKEDVFAWTRLCPPEDVKVVILGQDPYHGPGQAHGLAFSVKRGVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189327977 88 TPPSLRNIYKEMQEELG-LPVPDNGYLMPWAEQGVLLLNAVLTVRGGEANSHKGKGWEKITDAVIRAVAERPDPAVFVLW 166
Cdd:TIGR00628 81 IPPSLKNIFKELEADYPdFPPPKHGCLEAWARQGVLLLNTVLTVRRGQPGSHSGLGWERFTDAVISRLSERLDGLVFMLW 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2189327977 167 GNYAQKKLPLIDEERHVVVKGAHPSPLSAKK-FFGSRPFTQINE 209
Cdd:TIGR00628 161 GAHAQKKKSLIDAKKHLVLKSPHPSPLSARRgFFGCRHFSKANE 204
|
|
| PHA03347 |
PHA03347 |
uracil DNA glycosylase; Provisional |
1-223 |
1.27e-66 |
|
uracil DNA glycosylase; Provisional
Pssm-ID: 177588 Cd Length: 252 Bit Score: 205.67 E-value: 1.27e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189327977 1 MTDIDLLPESWRgvlgEELQ-KPYVKE----LADFVEEERSKGPVYPPREQVFAALDATPYEKVKVLVLGQDPYHGeGQG 75
Cdd:PHA03347 20 GDEDLLLSDPWL----DFLQlSPFLKQkllaLLNCVRELRKQTVIYPPEDRIMAWSYLCDPEDIKVVILGQDPYHG-GQA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189327977 76 HGLCFSVRPGVKTPPSLRNIYKEMQEEL-GLPVPDNGYLMPWAEQGVLLLNAVLTVRGGEANSHKGKGWEKITDAVIRAV 154
Cdd:PHA03347 95 NGLAFSVAYGFPVPPSLRNIFAELHRSVpDFSPPDHGCLDAWARQGVLLLNTILTVEKGKPGSHSDLGWAWFTDYIISSL 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2189327977 155 AERPDPAVFVLWGNYAQKKLPLIDEERHVVVKGAHPSPLSAK--------KFFGSRPFTQINEAVAAQGHQPIDWRI 223
Cdd:PHA03347 175 SEKLKACVFMLWGSKAIDKASLINSQKHLVLKAQHPSPLAANstrsstwpKFLGCNHFVLANKYLTQHGKGPIDWNL 251
|
|
| PHA03202 |
PHA03202 |
uracil DNA glycosylase; Provisional |
10-223 |
3.33e-65 |
|
uracil DNA glycosylase; Provisional
Pssm-ID: 165469 Cd Length: 313 Bit Score: 204.16 E-value: 3.33e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189327977 10 SWRGVLGEELQKPYVKELADFVEEERSKGPVYPPREQVFAALDATPYEKVKVLVLGQDPYHGEGQGHGLCFSVRPGVKTP 89
Cdd:PHA03202 99 SWRPILEREMQQPYVRLLLNEYKLRCAREEVFPPKEDIFAWTRFSPPEKVRVVIVGQDPYHAPGQAHGLAFSVRKGVPVP 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189327977 90 PSLRNIYKEMQEEL-GLPVPDNGYLMPWAEQGVLLLNAVLTVRGGEANSHKGKGWEKITDAVIRAVAERPDPAVFVLWGN 168
Cdd:PHA03202 179 PSLRNIYSAVQKSYpSFRPPMHGFLEKWAEQGVLLINTTLTVARGKPGSHATLGWHRLVRAVIDRLCTTSQGLVFMLWGA 258
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2189327977 169 YAQKKLPlIDEERHVVVKGAHPSPLSAKKFFGSRPFTQINEAVAAQGHQPIDWRI 223
Cdd:PHA03202 259 HAQKSCS-PNRQHHLVLTYGHPSPLSRVNFRDCPHFLEANAYLTKTGRKPVDWQI 312
|
|
| PHA03200 |
PHA03200 |
uracil DNA glycosylase; Provisional |
25-225 |
1.98e-60 |
|
uracil DNA glycosylase; Provisional
Pssm-ID: 165467 Cd Length: 255 Bit Score: 190.32 E-value: 1.98e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189327977 25 KELADFVEEERSKGPVYPPREQVFAALDATPYEKVKVLVLGQDPYHgEGQGHGLCFSVRPGVKTPPSLRNIYKEMQEEL- 103
Cdd:PHA03200 51 RRIVDAVDRDRQRLTVYPPPEDVHRWSRLCSPEDVKVVIVGQDPYH-DGSACGLAFGTVRGRSAPPSLKNVFRELERTVp 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189327977 104 GLPVPDNGYLMPWAEQGVLLLNAVLTVRGGEANSHKGKGWEKITDAVIRAVAERPDPAVFVLWGNYAQKKLPLIDEERHV 183
Cdd:PHA03200 130 NFSRPDSGCLDSWCRQGVLLLNTVFTVVHGQPGSHEALGWQTLSDRVISRLSEKREHLVFMLWGAQAQKLEYLIDSRKHL 209
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2189327977 184 VVKGAHPSP---LSAKKFFGSRPFTQINEAVAAQGHQPIDWRIPN 225
Cdd:PHA03200 210 ILKSAHPSPrvkGARTPFIGNNHFVLANEYLSTHGKRPIDWNILN 254
|
|
| PHA03199 |
PHA03199 |
uracil DNA glycosylase; Provisional |
8-223 |
6.86e-54 |
|
uracil DNA glycosylase; Provisional
Pssm-ID: 165466 Cd Length: 304 Bit Score: 175.19 E-value: 6.86e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189327977 8 PEsWRGVLGEELQKPYVKELadFVEEER---SKGPVYPPREQVFAALDATPYEKVKVLVLGQDPYHGEGQGHGLCFSVRP 84
Cdd:PHA03199 89 PE-WHDLLRDEFEEPYAKGI--FEEYNQllnNGEEIFPIKGDIFAWTRFCGPEKIRVVIIGQDPYHGAGHAHGLAFSVKR 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189327977 85 GVKTPPSLRNIYKEMQEEL-GLPVPDNGYLMPWAEQGVLLLNAVLTVRGGEANSHKGKGWEKITDAVIRAVAERPDPAVF 163
Cdd:PHA03199 166 GIPIPPSLKNIFAALMESYpHLPLPTHGCLDNWARQGVLLLNTTLTVKRGTPGSHFYLGWDMLIKRMLKRLCENRTGLVF 245
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189327977 164 VLWGNYAQKKLPLIDEErHVVVKGAHPSPLSAKKFFGSRPFTQINEAVAAQGHQPIDWRI 223
Cdd:PHA03199 246 MLWGAHAQKTIQPNPRC-HLVLTHAHPSPLSRSEFRNCKHFLQANEYFLKKGEPEIDWSI 304
|
|
| PHA03204 |
PHA03204 |
uracil DNA glycosylase; Provisional |
9-223 |
1.07e-50 |
|
uracil DNA glycosylase; Provisional
Pssm-ID: 165471 Cd Length: 322 Bit Score: 167.44 E-value: 1.07e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189327977 9 ESWRGVLGEELQKPYVKELADFVEEERSKGPVYPPREQVFAALDATPYEKVKVLVLGQDPYHGEGQGHGLCFSVRPGVKT 88
Cdd:PHA03204 104 CRWKEILLPELCCPTGSKILAEYERRARYEEVYPPKSDIFAWTRYCAPDHVKVVIVGQDPYANPGQAHGLAFSVKPGSPI 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189327977 89 PPSLRNIYKEMQE-----ELGlpvpDNGYLMPWAEQGVLLLNAVLTVRGGEANSHKGKGWEKITDAVIRAVAERPDPAVF 163
Cdd:PHA03204 184 PPSLKNILAAVKAcypsiELG----SHGCLEDWAKRGVLLLNSVLTVKRGDPGSHHSVGWQILVRNVLRRLSQSTRGIVF 259
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2189327977 164 VLWGNYAQKKLPLID-EERHVVVKGAHPSPLSAKKFFGSRPFTQINEAVAAQGHQPIDWRI 223
Cdd:PHA03204 260 MLWGAQAQTMYFQTDnDDRHLVLKYSHPSPLSRKPFAHCTHFKDANEFLCKMGKGAIDWSL 320
|
|
| PHA03201 |
PHA03201 |
uracil DNA glycosylase; Provisional |
6-221 |
4.22e-50 |
|
uracil DNA glycosylase; Provisional
Pssm-ID: 165468 Cd Length: 318 Bit Score: 165.84 E-value: 4.22e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189327977 6 LLPESWRGVLGEELQKPYVKELADFVEEERSKGPVYPPREQVFAALDATPYEKVKVLVLGQDPYHGEGQGHGLCFSVRPG 85
Cdd:PHA03201 101 LVGDAWRPLLEPELANPLTARLMAEYERRCRTEEVLPPREDVFSWTRYCTPDEVRVVIIGQDPYHQPGQAHGLAFSVRPG 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189327977 86 VKTPPSLRNIYKEMQEelglPVPD-----NGYLMPWAEQGVLLLNAVLTVRGGEANSHKGKGWEKITDAVIRAVAERPDP 160
Cdd:PHA03201 181 TPAPPSLRNILAAVRN----CCPDarmsgHGCLEKWARGGVLLLNTTLTVRRGEPASHAKIGWDRFVGSVVRRLAASRPG 256
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2189327977 161 AVFVLWGNYAQKKL-PliDEERHVVVKGAHPSPLSAKKFFGSRPFTQINEAVAAQGHQPIDW 221
Cdd:PHA03201 257 LVFMLWGAHAQNAIrP--DPRVHRVLTYSHPSPLSKVPFGSCRHFCLANQYLRERSLAPIDW 316
|
|
| UDG-F1-like |
cd19371 |
Uracil DNA glycosylase family 1, includes Human uracil DNA glycosylase, Vaccinia virus protein ... |
61-194 |
2.42e-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: 157.88 E-value: 2.42e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189327977 61 VLVLGQDPYHGEGQGHGLCFSVRPGVKTPPSLRNIYKEMQEELGLP-VPDNGYLMPWAEQGVLLLNAVLTVRGGEANSHk 139
Cdd:cd19371 1 VVIIGQDPYPSPGHAGGLAFSVTSEVPPPKSLRNIYKELERDYSSFlPPGNGTLEFWARQGVLLLNAALTCESGKPKSH- 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 2189327977 140 GKGWEKITDAVIRAVAERPDPAVFVLWGNYAQKKLPLIDEERHVVVKGAHPSPLS 194
Cdd:cd19371 80 YLLWEPFIKAFIRYISAHNKGLVFLLFGSDAQKLRKKINGRNVHVFKADHPSPAD 134
|
|
| UDG |
smart00986 |
Uracil DNA glycosylase superfamily; |
54-210 |
8.63e-30 |
|
Uracil DNA glycosylase superfamily;
Pssm-ID: 214956 Cd Length: 156 Bit Score: 108.24 E-value: 8.63e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189327977 54 TPYEKVKVLVLGQDPYHGEGQGH-------GLCFSVRPGV----KTPPSLRNIYKEMQeelglPVPDNGYLMPWAEQGVL 122
Cdd:smart00986 3 TGDPNAKVLIVGQAPGASEEDRGgpfvgaaGLLLSVMLGVaglpRLPPYLTNIVKCRP-----PDAGNRRPTSWELQGCL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189327977 123 LlnAVLTVRGGEANSHKGKGWEKITDAVIRAVAERpdPAVFVLWGNYAQKKLPLideerHVVVKGAHPSPLSAkKFFGSR 202
Cdd:smart00986 78 L--PWLTVELALARPHLILLLGKFAAQALLGLLRR--PLVFGLRGRVAQLKGKG-----HRVLPLPHPSPLNR-NFFPAK 147
|
....*...
gi 2189327977 203 PFTQINEA 210
Cdd:smart00986 148 KFAAWNDL 155
|
|
| UDG |
pfam03167 |
Uracil DNA glycosylase superfamily; |
57-209 |
1.51e-19 |
|
Uracil DNA glycosylase superfamily;
Pssm-ID: 397331 Cd Length: 154 Bit Score: 81.62 E-value: 1.51e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189327977 57 EKVKVLVLGQDPYHGEGQgHGLCFSVRPGvktppslrNIYKEMQEELGLPvpdngyLMPWAEQGVLLLNAVLTVRG--GE 134
Cdd:pfam03167 6 PNAKVLIVGEAPGADEDA-TGLPFVGRAG--------NLLWKLLNAAGLT------RDLFSPQGVYITNVVKCRPGnrRK 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189327977 135 ANSHKGK-GWEkITDAVIRAVAerpdPAVFVLWGNYAQKKL-----------PLIDEERHVVVKGAHPSPLSAKKffgSR 202
Cdd:pfam03167 71 PTSHEIDaCWP-YLEAEIELLR----PRVIVLLGKTAAKALlglkkitklrgKLIDLKGIPVLPTPHPSPLLRNK---LN 142
|
....*..
gi 2189327977 203 PFTQINE 209
Cdd:pfam03167 143 PFLKANA 149
|
|
| UDG-like |
cd09593 |
uracil-DNA glycosylases (UDG) and related enzymes; Uracil-DNA glycosylases (UDGs) initiate ... |
61-195 |
1.63e-14 |
|
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: 67.41 E-value: 1.63e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189327977 61 VLVLGQDPYHGEGQGHGLCFsvrpgvktPPSLRNIYKEMQEELGLPVpdngylmpWAEQGVLLLNAVLTVRGGEANSHKg 140
Cdd:cd09593 1 VLIVGQNPGPHGARAGGVPP--------GPSGNRLWRLLAAAGGTPR--------LFRYGVGLTNTVPRGPPGAAAGSE- 63
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2189327977 141 KGWEKITDAVIRAVAERPDPAVFVLWGNYAQKKLPLIDEER-------HVVVKGAHPSPLSA 195
Cdd:cd09593 64 KKELRFCGRWLRKLLELLNPRVVVLLGKKAQEAYLAVLTSSkgapgkgTEVLVLPHPSPRNR 125
|
|
| UDG_F1_VAVC_D4-like |
cd19372 |
Uracil DNA glycosylase family 1 subfamily, includes Vaccinia virus protein D4 and similar ... |
21-221 |
6.05e-04 |
|
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: 39.73 E-value: 6.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189327977 21 KPYVKELADFVEEERS---KGPVYPPREQVFAALdATPYEKVKVLVLGQDPYHGEGQG---HGLCFSVRpgvktppSLRN 94
Cdd:cd19372 2 EPVINQLVDEYTEVAPwllRDETSPIPENFFKQL-KQPLRDKRVCICGIDPYPTDATGvpfESPDFSKK-------TIRA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189327977 95 IYKEMQEELGLPVPdNGYLMPWAEqGVLLLNAVLTVRGGEANSHKgKGWEKITDAVIRAVAERpdPAVFVLWGNYAQKKL 174
Cdd:cd19372 74 IAEAISRRTGVSLY-KGYNFALVE-GVLAWNYYLSCREGETKSHA-IHWERISKLLLQHIAKY--VSVLYCLGKTDFSNV 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2189327977 175 PLIDEERHVVVKGAHPSPlSAKKFFGSRPFTQINEAVAAQGHQPIDW 221
Cdd:cd19372 149 RARLEVPVTVVVGYHPAA-RDGQFDKERAFEIVNVLLELNGKPPVNW 194
|
|
| |
