|
Name |
Accession |
Description |
Interval |
E-value |
| PHA03200 |
PHA03200 |
uracil DNA glycosylase; Provisional |
1-250 |
0e+00 |
|
uracil DNA glycosylase; Provisional
Pssm-ID: 165467 Cd Length: 255 Bit Score: 496.56 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 137036 1 MALKQWMLANIADNKGSLLT--PDEQARVFCLSADWIRFLSLPDHDTVLLRDTVAAVEGARQLEMVYPAPEHVHRWSYLC 78
Cdd:PHA03200 1 MALRQWMLENIADEKKCMLNesPDEQAELFGINEDWLRFLNLSDHDISQLRRIVDAVDRDRQRLTVYPPPEDVHRWSRLC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 137036 79 PPEQVRVVIVGQDPYCDGSASGLAFGTLAGRPPPPSLNNVFRELARTVDGFQRPASGCLDAWARRGVLLLNTVFTVVHGQ 158
Cdd:PHA03200 81 SPEDVKVVIVGQDPYHDGSACGLAFGTVRGRSAPPSLKNVFRELERTVPNFSRPDSGCLDSWCRQGVLLLNTVFTVVHGQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 137036 159 PGSHRHLGWQTLSNHVIRRLSERREHLVFMLWGADAHTCEYLIDRRRHLVLKSCHPSPRN--TTRAFVGNDHFILANAYL 236
Cdd:PHA03200 161 PGSHEALGWQTLSDRVISRLSEKREHLVFMLWGAQAQKLEYLIDSRKHLILKSAHPSPRVkgARTPFIGNNHFVLANEYL 240
|
250
....*....|....
gi 137036 237 DTHYRETMDWRLCG 250
Cdd:PHA03200 241 STHGKRPIDWNILN 254
|
|
| ung |
TIGR00628 |
uracil-DNA glycosylase; All proteins in this family for which functions are known are ... |
31-241 |
1.97e-115 |
|
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: 329.17 E-value: 1.97e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 137036 31 SADWIRFLSlPDHDTVLLRDTVAAVEGARQLEMVYPAPEHVHRWSYLCPPEQVRVVIVGQDPYCD-GSASGLAFGTLAGR 109
Cdd:TIGR00628 1 SPSWRAFLQ-PEFKKPYFQELLAFYKRERAQETVYPPKEDVFAWTRLCPPEDVKVVILGQDPYHGpGQAHGLAFSVKRGV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 137036 110 PPPPSLNNVFRELARTVDGFQRPASGCLDAWARRGVLLLNTVFTVVHGQPGSHRHLGWQTLSNHVIRRLSERREHLVFML 189
Cdd:TIGR00628 80 PIPPSLKNIFKELEADYPDFPPPKHGCLEAWARQGVLLLNTVLTVRRGQPGSHSGLGWERFTDAVISRLSERLDGLVFML 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 137036 190 WGADAHTCEYLIDRRRHLVLKSCHPSPRNTTRAFVGNDHFILANAYLDTHYR 241
Cdd:TIGR00628 160 WGAHAQKKKSLIDAKKHLVLKSPHPSPLSARRGFFGCRHFSKANEYLEKHGK 211
|
|
| UDG-F1-like |
cd10027 |
Uracil DNA glycosylase family 1 subfamily, includes Human uracil DNA glycosylase and similar ... |
47-246 |
1.25e-97 |
|
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: 283.57 E-value: 1.25e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 137036 47 LLRDTVAAVEGARQLEMVYPAPEHVHRWSYLCPPEQVRVVIVGQDPYCD-GSASGLAFGTLAGRPPPPSLNNVFRELART 125
Cdd:cd10027 1 YFKKLEAFLEEEYKKKTIYPPKEDIFRAFELTPLDDVKVVILGQDPYHGpGQAHGLAFSVPPGVKIPPSLRNIFKELKSD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 137036 126 VDGFqRPASGCLDAWARRGVLLLNTVFTVVHGQPGSHRHLGWQTLSNHVIRRLSERREHLVFMLWGADAHTCEYLIDRRR 205
Cdd:cd10027 81 LGIF-PPKHGDLSSWAKQGVLLLNTVLTVEAGKPGSHKNIGWETFTDAVIKALSEKNENVVFLLWGNHAQKKKKLIDKKK 159
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 137036 206 HLVLKSCHPSPRNTTRAFVGNDHFILANAYLDTHYRETMDW 246
Cdd:cd10027 160 HLVLESSHPSPLSAYRGFFGSKHFSKANEYLKKHGKKPIDW 200
|
|
| Ung |
COG0692 |
Uracil-DNA glycosylase [Replication, recombination and repair]; |
64-246 |
2.09e-84 |
|
Uracil-DNA glycosylase [Replication, recombination and repair];
Pssm-ID: 440456 Cd Length: 221 Bit Score: 250.73 E-value: 2.09e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 137036 64 VYPAPEHVHRWSYLCPPEQVRVVIVGQDPY-CDGSASGLAFGTLAGRPPPPSLNNVFRELARTVdGFQRPASGCLDAWAR 142
Cdd:COG0692 39 IYPPGEDIFRAFNLTPFDDVKVVILGQDPYhGPGQAHGLSFSVPPGVPLPPSLRNIYKELEDDL-GIPIPNHGDLTSWAE 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 137036 143 RGVLLLNTVFTVVHGQPGSHRHLGWQTLSNHVIRRLSERREHLVFMLWGADAHTCEYLIDRRRHLVLKSCHPSPRNTTRA 222
Cdd:COG0692 118 QGVLLLNTVLTVRAGQAGSHAGKGWETFTDAVIRALNARKEPVVFLLWGAYAQKKAALIDASKHLVLESPHPSPLSAHRG 197
|
170 180
....*....|....*....|....
gi 137036 223 FVGNDHFILANAYLDTHYRETMDW 246
Cdd:COG0692 198 FFGSKPFSKANAYLEEQGKTPIDW 221
|
|
| UDG |
smart00986 |
Uracil DNA glycosylase superfamily; |
79-236 |
1.18e-20 |
|
Uracil DNA glycosylase superfamily;
Pssm-ID: 214956 Cd Length: 156 Bit Score: 85.13 E-value: 1.18e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 137036 79 PPEQVRVVIVGQDPYCDGS--------ASGLAF----GTLAGRPPPPSLNNVFRELARTvdgfqrPASGCLDAWARRGVL 146
Cdd:smart00986 4 GDPNAKVLIVGQAPGASEEdrggpfvgAAGLLLsvmlGVAGLPRLPPYLTNIVKCRPPD------AGNRRPTSWELQGCL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 137036 147 LlnTVFTVVHGQPGSHRHLGWQTLSNHVIRRLSERreHLVFMLWGADAHtceylIDRRRHLVLKSCHPSPRNttRAFVGN 226
Cdd:smart00986 78 L--PWLTVELALARPHLILLLGKFAAQALLGLLRR--PLVFGLRGRVAQ-----LKGKGHRVLPLPHPSPLN--RNFFPA 146
|
170
....*....|
gi 137036 227 DHFILANAYL 236
Cdd:smart00986 147 KKFAAWNDLL 156
|
|
| UDG |
pfam03167 |
Uracil DNA glycosylase superfamily; |
78-237 |
3.42e-18 |
|
Uracil DNA glycosylase superfamily;
Pssm-ID: 397331 Cd Length: 154 Bit Score: 78.54 E-value: 3.42e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 137036 78 CPPEQVRVVIVGQDPYCDGSASGLAFGTLAGRPPPPSLNNVfrelartvdGFQRpasgclDAWARRGVLLLNTVFTVV-- 155
Cdd:pfam03167 3 FGPPNAKVLIVGEAPGADEDATGLPFVGRAGNLLWKLLNAA---------GLTR------DLFSPQGVYITNVVKCRPgn 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 137036 156 HGQPGSH-RHLGWQTLSNHvIRRLSERrehlVFMLWGADAH-----------TCEYLIDRRRHLVLKSCHPSPRNTTRaf 223
Cdd:pfam03167 68 RRKPTSHeIDACWPYLEAE-IELLRPR----VIVLLGKTAAkallglkkitkLRGKLIDLKGIPVLPTPHPSPLLRNK-- 140
|
170
....*....|....
gi 137036 224 vgNDHFILANAYLD 237
Cdd:pfam03167 141 --LNPFLKANAWED 152
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PHA03200 |
PHA03200 |
uracil DNA glycosylase; Provisional |
1-250 |
0e+00 |
|
uracil DNA glycosylase; Provisional
Pssm-ID: 165467 Cd Length: 255 Bit Score: 496.56 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 137036 1 MALKQWMLANIADNKGSLLT--PDEQARVFCLSADWIRFLSLPDHDTVLLRDTVAAVEGARQLEMVYPAPEHVHRWSYLC 78
Cdd:PHA03200 1 MALRQWMLENIADEKKCMLNesPDEQAELFGINEDWLRFLNLSDHDISQLRRIVDAVDRDRQRLTVYPPPEDVHRWSRLC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 137036 79 PPEQVRVVIVGQDPYCDGSASGLAFGTLAGRPPPPSLNNVFRELARTVDGFQRPASGCLDAWARRGVLLLNTVFTVVHGQ 158
Cdd:PHA03200 81 SPEDVKVVIVGQDPYHDGSACGLAFGTVRGRSAPPSLKNVFRELERTVPNFSRPDSGCLDSWCRQGVLLLNTVFTVVHGQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 137036 159 PGSHRHLGWQTLSNHVIRRLSERREHLVFMLWGADAHTCEYLIDRRRHLVLKSCHPSPRN--TTRAFVGNDHFILANAYL 236
Cdd:PHA03200 161 PGSHEALGWQTLSDRVISRLSEKREHLVFMLWGAQAQKLEYLIDSRKHLILKSAHPSPRVkgARTPFIGNNHFVLANEYL 240
|
250
....*....|....
gi 137036 237 DTHYRETMDWRLCG 250
Cdd:PHA03200 241 STHGKRPIDWNILN 254
|
|
| ung |
TIGR00628 |
uracil-DNA glycosylase; All proteins in this family for which functions are known are ... |
31-241 |
1.97e-115 |
|
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: 329.17 E-value: 1.97e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 137036 31 SADWIRFLSlPDHDTVLLRDTVAAVEGARQLEMVYPAPEHVHRWSYLCPPEQVRVVIVGQDPYCD-GSASGLAFGTLAGR 109
Cdd:TIGR00628 1 SPSWRAFLQ-PEFKKPYFQELLAFYKRERAQETVYPPKEDVFAWTRLCPPEDVKVVILGQDPYHGpGQAHGLAFSVKRGV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 137036 110 PPPPSLNNVFRELARTVDGFQRPASGCLDAWARRGVLLLNTVFTVVHGQPGSHRHLGWQTLSNHVIRRLSERREHLVFML 189
Cdd:TIGR00628 80 PIPPSLKNIFKELEADYPDFPPPKHGCLEAWARQGVLLLNTVLTVRRGQPGSHSGLGWERFTDAVISRLSERLDGLVFML 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 137036 190 WGADAHTCEYLIDRRRHLVLKSCHPSPRNTTRAFVGNDHFILANAYLDTHYR 241
Cdd:TIGR00628 160 WGAHAQKKKSLIDAKKHLVLKSPHPSPLSARRGFFGCRHFSKANEYLEKHGK 211
|
|
| UDG-F1-like |
cd10027 |
Uracil DNA glycosylase family 1 subfamily, includes Human uracil DNA glycosylase and similar ... |
47-246 |
1.25e-97 |
|
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: 283.57 E-value: 1.25e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 137036 47 LLRDTVAAVEGARQLEMVYPAPEHVHRWSYLCPPEQVRVVIVGQDPYCD-GSASGLAFGTLAGRPPPPSLNNVFRELART 125
Cdd:cd10027 1 YFKKLEAFLEEEYKKKTIYPPKEDIFRAFELTPLDDVKVVILGQDPYHGpGQAHGLAFSVPPGVKIPPSLRNIFKELKSD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 137036 126 VDGFqRPASGCLDAWARRGVLLLNTVFTVVHGQPGSHRHLGWQTLSNHVIRRLSERREHLVFMLWGADAHTCEYLIDRRR 205
Cdd:cd10027 81 LGIF-PPKHGDLSSWAKQGVLLLNTVLTVEAGKPGSHKNIGWETFTDAVIKALSEKNENVVFLLWGNHAQKKKKLIDKKK 159
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 137036 206 HLVLKSCHPSPRNTTRAFVGNDHFILANAYLDTHYRETMDW 246
Cdd:cd10027 160 HLVLESSHPSPLSAYRGFFGSKHFSKANEYLKKHGKKPIDW 200
|
|
| PHA03347 |
PHA03347 |
uracil DNA glycosylase; Provisional |
30-248 |
3.72e-91 |
|
uracil DNA glycosylase; Provisional
Pssm-ID: 177588 Cd Length: 252 Bit Score: 269.23 E-value: 3.72e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 137036 30 LSADWIRFLSLPDHDTVLLRDTVAAVEGARQLEMVYPAPEHVHRWSYLCPPEQVRVVIVGQDPYCDGSASGLAFGTLAGR 109
Cdd:PHA03347 26 LSDPWLDFLQLSPFLKQKLLALLNCVRELRKQTVIYPPEDRIMAWSYLCDPEDIKVVILGQDPYHGGQANGLAFSVAYGF 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 137036 110 PPPPSLNNVFRELARTVDGFQRPASGCLDAWARRGVLLLNTVFTVVHGQPGSHRHLGWQTLSNHVIRRLSERREHLVFML 189
Cdd:PHA03347 106 PVPPSLRNIFAELHRSVPDFSPPDHGCLDAWARQGVLLLNTILTVEKGKPGSHSDLGWAWFTDYIISSLSEKLKACVFML 185
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 137036 190 WGADAHTCEYLIDRRRHLVLKSCHPSP--RNTTRA-----FVGNDHFILANAYLDTHYRETMDWRL 248
Cdd:PHA03347 186 WGSKAIDKASLINSQKHLVLKAQHPSPlaANSTRSstwpkFLGCNHFVLANKYLTQHGKGPIDWNL 251
|
|
| PRK05254 |
PRK05254 |
uracil-DNA glycosylase; Provisional |
64-248 |
3.57e-86 |
|
uracil-DNA glycosylase; Provisional
Pssm-ID: 235376 Cd Length: 224 Bit Score: 255.46 E-value: 3.57e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 137036 64 VYPAPEHVHRWSYLCPPEQVRVVIVGQDPYCD-GSASGLAFGTLAGRPPPPSLNNVFRELARTVdGFQRPASGCLDAWAR 142
Cdd:PRK05254 40 IYPPGEDIFRAFNLTPFDDVKVVILGQDPYHGpGQAHGLSFSVPPGVPIPPSLRNIFKELEDDL-GFPIPNHGDLTSWAE 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 137036 143 RGVLLLNTVFTVVHGQPGSHRHLGWQTLSNHVIRRLSERREHLVFMLWGADAHTCEYLIDRRRHLVLKSCHPSPRNTTRA 222
Cdd:PRK05254 119 QGVLLLNTVLTVEAGQANSHAGKGWETFTDAVIKALNERREPVVFILWGSHAQKKKALIDNSKHLILESPHPSPLSAHRG 198
|
170 180
....*....|....*....|....*.
gi 137036 223 FVGNDHFILANAYLDTHYRETMDWRL 248
Cdd:PRK05254 199 FFGSKHFSKANALLKQHGKTPIDWQL 224
|
|
| Ung |
COG0692 |
Uracil-DNA glycosylase [Replication, recombination and repair]; |
64-246 |
2.09e-84 |
|
Uracil-DNA glycosylase [Replication, recombination and repair];
Pssm-ID: 440456 Cd Length: 221 Bit Score: 250.73 E-value: 2.09e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 137036 64 VYPAPEHVHRWSYLCPPEQVRVVIVGQDPY-CDGSASGLAFGTLAGRPPPPSLNNVFRELARTVdGFQRPASGCLDAWAR 142
Cdd:COG0692 39 IYPPGEDIFRAFNLTPFDDVKVVILGQDPYhGPGQAHGLSFSVPPGVPLPPSLRNIYKELEDDL-GIPIPNHGDLTSWAE 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 137036 143 RGVLLLNTVFTVVHGQPGSHRHLGWQTLSNHVIRRLSERREHLVFMLWGADAHTCEYLIDRRRHLVLKSCHPSPRNTTRA 222
Cdd:COG0692 118 QGVLLLNTVLTVRAGQAGSHAGKGWETFTDAVIRALNARKEPVVFLLWGAYAQKKAALIDASKHLVLESPHPSPLSAHRG 197
|
170 180
....*....|....*....|....
gi 137036 223 FVGNDHFILANAYLDTHYRETMDW 246
Cdd:COG0692 198 FFGSKPFSKANAYLEEQGKTPIDW 221
|
|
| PHA03204 |
PHA03204 |
uracil DNA glycosylase; Provisional |
62-248 |
2.41e-60 |
|
uracil DNA glycosylase; Provisional
Pssm-ID: 165471 Cd Length: 322 Bit Score: 192.87 E-value: 2.41e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 137036 62 EMVYPAPEHVHRWSYLCPPEQVRVVIVGQDPYCD-GSASGLAFGTLAGRPPPPSLNNVFRELARTVDGFQRPASGCLDAW 140
Cdd:PHA03204 133 EEVYPPKSDIFAWTRYCAPDHVKVVIVGQDPYANpGQAHGLAFSVKPGSPIPPSLKNILAAVKACYPSIELGSHGCLEDW 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 137036 141 ARRGVLLLNTVFTVVHGQPGSHRHLGWQTLSNHVIRRLSERREHLVFMLWGADAHTCEYLIDRR-RHLVLKSCHPSPRnT 219
Cdd:PHA03204 213 AKRGVLLLNSVLTVKRGDPGSHHSVGWQILVRNVLRRLSQSTRGIVFMLWGAQAQTMYFQTDNDdRHLVLKYSHPSPL-S 291
|
170 180
....*....|....*....|....*....
gi 137036 220 TRAFVGNDHFILANAYLDTHYRETMDWRL 248
Cdd:PHA03204 292 RKPFAHCTHFKDANEFLCKMGKGAIDWSL 320
|
|
| PHA03202 |
PHA03202 |
uracil DNA glycosylase; Provisional |
62-248 |
1.43e-59 |
|
uracil DNA glycosylase; Provisional
Pssm-ID: 165469 Cd Length: 313 Bit Score: 190.68 E-value: 1.43e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 137036 62 EMVYPAPEHVHRWSYLCPPEQVRVVIVGQDPY-CDGSASGLAFGTLAGRPPPPSLNNVFRELARTVDGFQRPASGCLDAW 140
Cdd:PHA03202 127 EEVFPPKEDIFAWTRFSPPEKVRVVIVGQDPYhAPGQAHGLAFSVRKGVPVPPSLRNIYSAVQKSYPSFRPPMHGFLEKW 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 137036 141 ARRGVLLLNTVFTVVHGQPGSHRHLGWQTLSNHVIRRLSERREHLVFMLWGADAH-TCEylIDRRRHLVLKSCHPSPRNT 219
Cdd:PHA03202 207 AEQGVLLINTTLTVARGKPGSHATLGWHRLVRAVIDRLCTTSQGLVFMLWGAHAQkSCS--PNRQHHLVLTYGHPSPLSR 284
|
170 180
....*....|....*....|....*....
gi 137036 220 TRaFVGNDHFILANAYLDTHYRETMDWRL 248
Cdd:PHA03202 285 VN-FRDCPHFLEANAYLTKTGRKPVDWQI 312
|
|
| PHA03199 |
PHA03199 |
uracil DNA glycosylase; Provisional |
28-246 |
2.96e-54 |
|
uracil DNA glycosylase; Provisional
Pssm-ID: 165466 Cd Length: 304 Bit Score: 176.73 E-value: 2.96e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 137036 28 FCLSADWirflslpdHDtvLLRDTVAA------VEGARQL----EMVYPAPEHVHRWSYLCPPEQVRVVIVGQDPY-CDG 96
Cdd:PHA03199 85 FCIDPEW--------HD--LLRDEFEEpyakgiFEEYNQLlnngEEIFPIKGDIFAWTRFCGPEKIRVVIIGQDPYhGAG 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 137036 97 SASGLAFGTLAGRPPPPSLNNVFRELARTVDGFQRPASGCLDAWARRGVLLLNTVFTVVHGQPGSHRHLGWQTLSNHVIR 176
Cdd:PHA03199 155 HAHGLAFSVKRGIPIPPSLKNIFAALMESYPHLPLPTHGCLDNWARQGVLLLNTTLTVKRGTPGSHFYLGWDMLIKRMLK 234
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 137036 177 RLSERREHLVFMLWGADAHTCEYlIDRRRHLVLKSCHPSPRNTTrAFVGNDHFILANAYLDTHYRETMDW 246
Cdd:PHA03199 235 RLCENRTGLVFMLWGAHAQKTIQ-PNPRCHLVLTHAHPSPLSRS-EFRNCKHFLQANEYFLKKGEPEIDW 302
|
|
| PHA03201 |
PHA03201 |
uracil DNA glycosylase; Provisional |
26-246 |
2.31e-52 |
|
uracil DNA glycosylase; Provisional
Pssm-ID: 165468 Cd Length: 318 Bit Score: 172.38 E-value: 2.31e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 137036 26 RVFCLSADWiRFLSLPDHDTVLLRDTVAAVEGARQLEMVYPAPEHVHRWSYLCPPEQVRVVIVGQDPYCD-GSASGLAFG 104
Cdd:PHA03201 98 RRFLVGDAW-RPLLEPELANPLTARLMAEYERRCRTEEVLPPREDVFSWTRYCTPDEVRVVIIGQDPYHQpGQAHGLAFS 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 137036 105 TLAGRPPPPSLNNVFRELARTVDGFQRPASGCLDAWARRGVLLLNTVFTVVHGQPGSHRHLGWQTLSNHVIRRLSERREH 184
Cdd:PHA03201 177 VRPGTPAPPSLRNILAAVRNCCPDARMSGHGCLEKWARGGVLLLNTTLTVRRGEPASHAKIGWDRFVGSVVRRLAASRPG 256
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 137036 185 LVFMLWGADAHTCeYLIDRRRHLVLKSCHPSPRNTTrAFVGNDHFILANAYLDTHYRETMDW 246
Cdd:PHA03201 257 LVFMLWGAHAQNA-IRPDPRVHRVLTYSHPSPLSKV-PFGSCRHFCLANQYLRERSLAPIDW 316
|
|
| UDG-F1-like |
cd19371 |
Uracil DNA glycosylase family 1, includes Human uracil DNA glycosylase, Vaccinia virus protein ... |
85-218 |
4.11e-44 |
|
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: 145.17 E-value: 4.11e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 137036 85 VVIVGQDPYCD-GSASGLAFGTLAGRPPPPSLNNVFRELARTVDGFQRPASGCLDAWARRGVLLLNTVFTVVHGQPGSHr 163
Cdd:cd19371 1 VVIIGQDPYPSpGHAGGLAFSVTSEVPPPKSLRNIYKELERDYSSFLPPGNGTLEFWARQGVLLLNAALTCESGKPKSH- 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 137036 164 HLGWQTLSNHVIRRLSERREHLVFMLWGADAHTCEYLIDRRRHLVLKSCHPSPRN 218
Cdd:cd19371 80 YLLWEPFIKAFIRYISAHNKGLVFLLFGSDAQKLRKKINGRNVHVFKADHPSPAD 134
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|
| UDG |
smart00986 |
Uracil DNA glycosylase superfamily; |
79-236 |
1.18e-20 |
|
Uracil DNA glycosylase superfamily;
Pssm-ID: 214956 Cd Length: 156 Bit Score: 85.13 E-value: 1.18e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 137036 79 PPEQVRVVIVGQDPYCDGS--------ASGLAF----GTLAGRPPPPSLNNVFRELARTvdgfqrPASGCLDAWARRGVL 146
Cdd:smart00986 4 GDPNAKVLIVGQAPGASEEdrggpfvgAAGLLLsvmlGVAGLPRLPPYLTNIVKCRPPD------AGNRRPTSWELQGCL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 137036 147 LlnTVFTVVHGQPGSHRHLGWQTLSNHVIRRLSERreHLVFMLWGADAHtceylIDRRRHLVLKSCHPSPRNttRAFVGN 226
Cdd:smart00986 78 L--PWLTVELALARPHLILLLGKFAAQALLGLLRR--PLVFGLRGRVAQ-----LKGKGHRVLPLPHPSPLN--RNFFPA 146
|
170
....*....|
gi 137036 227 DHFILANAYL 236
Cdd:smart00986 147 KKFAAWNDLL 156
|
|
| UDG |
pfam03167 |
Uracil DNA glycosylase superfamily; |
78-237 |
3.42e-18 |
|
Uracil DNA glycosylase superfamily;
Pssm-ID: 397331 Cd Length: 154 Bit Score: 78.54 E-value: 3.42e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 137036 78 CPPEQVRVVIVGQDPYCDGSASGLAFGTLAGRPPPPSLNNVfrelartvdGFQRpasgclDAWARRGVLLLNTVFTVV-- 155
Cdd:pfam03167 3 FGPPNAKVLIVGEAPGADEDATGLPFVGRAGNLLWKLLNAA---------GLTR------DLFSPQGVYITNVVKCRPgn 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 137036 156 HGQPGSH-RHLGWQTLSNHvIRRLSERrehlVFMLWGADAH-----------TCEYLIDRRRHLVLKSCHPSPRNTTRaf 223
Cdd:pfam03167 68 RRKPTSHeIDACWPYLEAE-IELLRPR----VIVLLGKTAAkallglkkitkLRGKLIDLKGIPVLPTPHPSPLLRNK-- 140
|
170
....*....|....
gi 137036 224 vgNDHFILANAYLD 237
Cdd:pfam03167 141 --LNPFLKANAWED 152
|
|
| UDG-like |
cd09593 |
uracil-DNA glycosylases (UDG) and related enzymes; Uracil-DNA glycosylases (UDGs) initiate ... |
85-219 |
1.02e-12 |
|
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: 63.18 E-value: 1.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 137036 85 VVIVGQDPYCDGSASGlafgtlaGRPPPPSLNNVFRELArtvdgfqrpASGCLDAWARRGVLLLNTVFTVVHGQPGSHRH 164
Cdd:cd09593 1 VLIVGQNPGPHGARAG-------GVPPGPSGNRLWRLLA---------AAGGTPRLFRYGVGLTNTVPRGPPGAAAGSEK 64
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 137036 165 lGWQTLSNHVIRRLSERREHLVFMLWGADAH-------TCEYLIDRRRHLVLKSCHPSPRNT 219
Cdd:cd09593 65 -KELRFCGRWLRKLLELLNPRVVVLLGKKAQeaylavlTSSKGAPGKGTEVLVLPHPSPRNR 125
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