|
Name |
Accession |
Description |
Interval |
E-value |
| Ung |
COG0692 |
Uracil-DNA glycosylase [Replication, recombination and repair]; |
96-310 |
5.81e-141 |
|
Uracil-DNA glycosylase [Replication, recombination and repair];
Pssm-ID: 440456 Cd Length: 221 Bit Score: 396.72 E-value: 5.81e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19718751 96 ESWKKHLSGEFGKPYFIKLMGFVAEERK-HYTVYPPPHQVFTWTQMCDIKDVKVVILGQDPYHGPNQAHGLCFSVQRPVP 174
Cdd:COG0692 7 PSWKEALAEEFEKPYFQALGAFLKAEYAaGKTIYPPGEDIFRAFNLTPFDDVKVVILGQDPYHGPGQAHGLSFSVPPGVP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19718751 175 PPPSLENIYKELSTDIeDFVHPGHGDLSGWAKQGVLLLNAVLTVRAHQANSHKERGWEQFTDAVVSWLNQNSNGLVFLLW 254
Cdd:COG0692 87 LPPSLRNIYKELEDDL-GIPIPNHGDLTSWAEQGVLLLNTVLTVRAGQAGSHAGKGWETFTDAVIRALNARKEPVVFLLW 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 19718751 255 GSYAQKKGSAIDRKRHHVLQTAHPSPLSVYRGFFGCRHFSKTNELLQKSGKKPIDW 310
Cdd:COG0692 166 GAYAQKKAALIDASKHLVLESPHPSPLSAHRGFFGSKPFSKANAYLEEQGKTPIDW 221
|
|
| ung |
TIGR00628 |
uracil-DNA glycosylase; All proteins in this family for which functions are known are ... |
96-305 |
1.27e-134 |
|
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: 380.41 E-value: 1.27e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19718751 96 ESWKKHLSGEFGKPYFIKLMGFVAEERKHYTVYPPPHQVFTWTQMCDIKDVKVVILGQDPYHGPNQAHGLCFSVQRPVPP 175
Cdd:TIGR00628 2 PSWRAFLQPEFKKPYFQELLAFYKRERAQETVYPPKEDVFAWTRLCPPEDVKVVILGQDPYHGPGQAHGLAFSVKRGVPI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19718751 176 PPSLENIYKELSTDIEDFVHPGHGDLSGWAKQGVLLLNAVLTVRAHQANSHKERGWEQFTDAVVSWLNQNSNGLVFLLWG 255
Cdd:TIGR00628 82 PPSLKNIFKELEADYPDFPPPKHGCLEAWARQGVLLLNTVLTVRRGQPGSHSGLGWERFTDAVISRLSERLDGLVFMLWG 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 19718751 256 SYAQKKGSAIDRKRHHVLQTAHPSPLSVYRGFFGCRHFSKTNELLQKSGK 305
Cdd:TIGR00628 162 AHAQKKKSLIDAKKHLVLKSPHPSPLSARRGFFGCRHFSKANEYLEKHGK 211
|
|
| UDG-F1-like |
cd10027 |
Uracil DNA glycosylase family 1 subfamily, includes Human uracil DNA glycosylase and similar ... |
110-310 |
2.87e-134 |
|
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: 379.10 E-value: 2.87e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19718751 110 YFIKLMGFVAEERKHYTVYPPPHQVFTWTQMCDIKDVKVVILGQDPYHGPNQAHGLCFSVQRPVPPPPSLENIYKELSTD 189
Cdd:cd10027 1 YFKKLEAFLEEEYKKKTIYPPKEDIFRAFELTPLDDVKVVILGQDPYHGPGQAHGLAFSVPPGVKIPPSLRNIFKELKSD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19718751 190 IEDFvHPGHGDLSGWAKQGVLLLNAVLTVRAHQANSHKERGWEQFTDAVVSWLNQNSNGLVFLLWGSYAQKKGSAIDRKR 269
Cdd:cd10027 81 LGIF-PPKHGDLSSWAKQGVLLLNTVLTVEAGKPGSHKNIGWETFTDAVIKALSEKNENVVFLLWGNHAQKKKKLIDKKK 159
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 19718751 270 HHVLQTAHPSPLSVYRGFFGCRHFSKTNELLQKSGKKPIDW 310
Cdd:cd10027 160 HLVLESSHPSPLSAYRGFFGSKHFSKANEYLKKHGKKPIDW 200
|
|
| PRK05254 |
PRK05254 |
uracil-DNA glycosylase; Provisional |
96-310 |
3.83e-134 |
|
uracil-DNA glycosylase; Provisional
Pssm-ID: 235376 Cd Length: 224 Bit Score: 379.50 E-value: 3.83e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19718751 96 ESWKKHLSGEFGKPYFIKLMGFVAEER-KHYTVYPPPHQVFTWTQMCDIKDVKVVILGQDPYHGPNQAHGLCFSVQRPVP 174
Cdd:PRK05254 8 PSWKEVLKPEFKKPYFQELLEFLRAERaAGKTIYPPGEDIFRAFNLTPFDDVKVVILGQDPYHGPGQAHGLSFSVPPGVP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19718751 175 PPPSLENIYKELSTDIeDFVHPGHGDLSGWAKQGVLLLNAVLTVRAHQANSHKERGWEQFTDAVVSWLNQNSNGLVFLLW 254
Cdd:PRK05254 88 IPPSLRNIFKELEDDL-GFPIPNHGDLTSWAEQGVLLLNTVLTVEAGQANSHAGKGWETFTDAVIKALNERREPVVFILW 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 19718751 255 GSYAQKKGSAIDRKRHHVLQTAHPSPLSVYRGFFGCRHFSKTNELLQKSGKKPIDW 310
Cdd:PRK05254 167 GSHAQKKKALIDNSKHLILESPHPSPLSAHRGFFGSKHFSKANALLKQHGKTPIDW 222
|
|
| UDG |
smart00986 |
Uracil DNA glycosylase superfamily; |
144-300 |
4.27e-32 |
|
Uracil DNA glycosylase superfamily;
Pssm-ID: 214956 Cd Length: 156 Bit Score: 116.72 E-value: 4.27e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19718751 144 KDVKVVILGQDPY------HGP-NQAHGLCFSVQRPV----PPPPSLENIYKELSTDiedfvhPGHGDLSGWAKQGVLLl 212
Cdd:smart00986 6 PNAKVLIVGQAPGaseedrGGPfVGAAGLLLSVMLGVaglpRLPPYLTNIVKCRPPD------AGNRRPTSWELQGCLL- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19718751 213 nAVLTVRAHQANSHKERGWEQFTDAVVswLNQNSNGLVFLLWGSYAQKKGsaidrKRHHVLQTAHPSPLSvyRGFFGCRH 292
Cdd:smart00986 79 -PWLTVELALARPHLILLLGKFAAQAL--LGLLRRPLVFGLRGRVAQLKG-----KGHRVLPLPHPSPLN--RNFFPAKK 148
|
....*...
gi 19718751 293 FSKTNELL 300
Cdd:smart00986 149 FAAWNDLL 156
|
|
| UDG |
pfam03167 |
Uracil DNA glycosylase superfamily; |
144-299 |
2.86e-18 |
|
Uracil DNA glycosylase superfamily;
Pssm-ID: 397331 Cd Length: 154 Bit Score: 80.08 E-value: 2.86e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19718751 144 KDVKVVILGQDPYHGpNQAHGLCFSVQRPVPPPPSLENIykELSTDIEDFvhpghgdlsgwakQGVLLLNAVLTVR--AH 221
Cdd:pfam03167 6 PNAKVLIVGEAPGAD-EDATGLPFVGRAGNLLWKLLNAA--GLTRDLFSP-------------QGVYITNVVKCRPgnRR 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19718751 222 QANSHK-ERGWEqFTDAVVSWLNQNsnglVFLLWGSYAQKK-----------GSAIDRKRHHVLQTAHPSPLSVYRgffg 289
Cdd:pfam03167 70 KPTSHEiDACWP-YLEAEIELLRPR----VIVLLGKTAAKAllglkkitklrGKLIDLKGIPVLPTPHPSPLLRNK---- 140
|
170
....*....|
gi 19718751 290 CRHFSKTNEL 299
Cdd:pfam03167 141 LNPFLKANAW 150
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Ung |
COG0692 |
Uracil-DNA glycosylase [Replication, recombination and repair]; |
96-310 |
5.81e-141 |
|
Uracil-DNA glycosylase [Replication, recombination and repair];
Pssm-ID: 440456 Cd Length: 221 Bit Score: 396.72 E-value: 5.81e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19718751 96 ESWKKHLSGEFGKPYFIKLMGFVAEERK-HYTVYPPPHQVFTWTQMCDIKDVKVVILGQDPYHGPNQAHGLCFSVQRPVP 174
Cdd:COG0692 7 PSWKEALAEEFEKPYFQALGAFLKAEYAaGKTIYPPGEDIFRAFNLTPFDDVKVVILGQDPYHGPGQAHGLSFSVPPGVP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19718751 175 PPPSLENIYKELSTDIeDFVHPGHGDLSGWAKQGVLLLNAVLTVRAHQANSHKERGWEQFTDAVVSWLNQNSNGLVFLLW 254
Cdd:COG0692 87 LPPSLRNIYKELEDDL-GIPIPNHGDLTSWAEQGVLLLNTVLTVRAGQAGSHAGKGWETFTDAVIRALNARKEPVVFLLW 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 19718751 255 GSYAQKKGSAIDRKRHHVLQTAHPSPLSVYRGFFGCRHFSKTNELLQKSGKKPIDW 310
Cdd:COG0692 166 GAYAQKKAALIDASKHLVLESPHPSPLSAHRGFFGSKPFSKANAYLEEQGKTPIDW 221
|
|
| ung |
TIGR00628 |
uracil-DNA glycosylase; All proteins in this family for which functions are known are ... |
96-305 |
1.27e-134 |
|
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: 380.41 E-value: 1.27e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19718751 96 ESWKKHLSGEFGKPYFIKLMGFVAEERKHYTVYPPPHQVFTWTQMCDIKDVKVVILGQDPYHGPNQAHGLCFSVQRPVPP 175
Cdd:TIGR00628 2 PSWRAFLQPEFKKPYFQELLAFYKRERAQETVYPPKEDVFAWTRLCPPEDVKVVILGQDPYHGPGQAHGLAFSVKRGVPI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19718751 176 PPSLENIYKELSTDIEDFVHPGHGDLSGWAKQGVLLLNAVLTVRAHQANSHKERGWEQFTDAVVSWLNQNSNGLVFLLWG 255
Cdd:TIGR00628 82 PPSLKNIFKELEADYPDFPPPKHGCLEAWARQGVLLLNTVLTVRRGQPGSHSGLGWERFTDAVISRLSERLDGLVFMLWG 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 19718751 256 SYAQKKGSAIDRKRHHVLQTAHPSPLSVYRGFFGCRHFSKTNELLQKSGK 305
Cdd:TIGR00628 162 AHAQKKKSLIDAKKHLVLKSPHPSPLSARRGFFGCRHFSKANEYLEKHGK 211
|
|
| UDG-F1-like |
cd10027 |
Uracil DNA glycosylase family 1 subfamily, includes Human uracil DNA glycosylase and similar ... |
110-310 |
2.87e-134 |
|
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: 379.10 E-value: 2.87e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19718751 110 YFIKLMGFVAEERKHYTVYPPPHQVFTWTQMCDIKDVKVVILGQDPYHGPNQAHGLCFSVQRPVPPPPSLENIYKELSTD 189
Cdd:cd10027 1 YFKKLEAFLEEEYKKKTIYPPKEDIFRAFELTPLDDVKVVILGQDPYHGPGQAHGLAFSVPPGVKIPPSLRNIFKELKSD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19718751 190 IEDFvHPGHGDLSGWAKQGVLLLNAVLTVRAHQANSHKERGWEQFTDAVVSWLNQNSNGLVFLLWGSYAQKKGSAIDRKR 269
Cdd:cd10027 81 LGIF-PPKHGDLSSWAKQGVLLLNTVLTVEAGKPGSHKNIGWETFTDAVIKALSEKNENVVFLLWGNHAQKKKKLIDKKK 159
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 19718751 270 HHVLQTAHPSPLSVYRGFFGCRHFSKTNELLQKSGKKPIDW 310
Cdd:cd10027 160 HLVLESSHPSPLSAYRGFFGSKHFSKANEYLKKHGKKPIDW 200
|
|
| PRK05254 |
PRK05254 |
uracil-DNA glycosylase; Provisional |
96-310 |
3.83e-134 |
|
uracil-DNA glycosylase; Provisional
Pssm-ID: 235376 Cd Length: 224 Bit Score: 379.50 E-value: 3.83e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19718751 96 ESWKKHLSGEFGKPYFIKLMGFVAEER-KHYTVYPPPHQVFTWTQMCDIKDVKVVILGQDPYHGPNQAHGLCFSVQRPVP 174
Cdd:PRK05254 8 PSWKEVLKPEFKKPYFQELLEFLRAERaAGKTIYPPGEDIFRAFNLTPFDDVKVVILGQDPYHGPGQAHGLSFSVPPGVP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19718751 175 PPPSLENIYKELSTDIeDFVHPGHGDLSGWAKQGVLLLNAVLTVRAHQANSHKERGWEQFTDAVVSWLNQNSNGLVFLLW 254
Cdd:PRK05254 88 IPPSLRNIFKELEDDL-GFPIPNHGDLTSWAEQGVLLLNTVLTVEAGQANSHAGKGWETFTDAVIKALNERREPVVFILW 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 19718751 255 GSYAQKKGSAIDRKRHHVLQTAHPSPLSVYRGFFGCRHFSKTNELLQKSGKKPIDW 310
Cdd:PRK05254 167 GSHAQKKKALIDNSKHLILESPHPSPLSAHRGFFGSKHFSKANALLKQHGKTPIDW 222
|
|
| PHA03347 |
PHA03347 |
uracil DNA glycosylase; Provisional |
96-310 |
1.66e-77 |
|
uracil DNA glycosylase; Provisional
Pssm-ID: 177588 Cd Length: 252 Bit Score: 236.87 E-value: 1.66e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19718751 96 ESWKKHLS-GEFGKPYFIKLMGFVAEERKHYTVYPPPHQVFTWTQMCDIKDVKVVILGQDPYHGpNQAHGLCFSVQRPVP 174
Cdd:PHA03347 28 DPWLDFLQlSPFLKQKLLALLNCVRELRKQTVIYPPEDRIMAWSYLCDPEDIKVVILGQDPYHG-GQANGLAFSVAYGFP 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19718751 175 PPPSLENIYKELSTDIEDFVHPGHGDLSGWAKQGVLLLNAVLTVRAHQANSHKERGWEQFTDAVVSWLNQNSNGLVFLLW 254
Cdd:PHA03347 107 VPPSLRNIFAELHRSVPDFSPPDHGCLDAWARQGVLLLNTILTVEKGKPGSHSDLGWAWFTDYIISSLSEKLKACVFMLW 186
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 19718751 255 GSYAQKKGSAIDRKRHHVLQTAHPSPL---SVYRG----FFGCRHFSKTNELLQKSGKKPIDW 310
Cdd:PHA03347 187 GSKAIDKASLINSQKHLVLKAQHPSPLaanSTRSStwpkFLGCNHFVLANKYLTQHGKGPIDW 249
|
|
| PHA03200 |
PHA03200 |
uracil DNA glycosylase; Provisional |
118-313 |
1.78e-72 |
|
uracil DNA glycosylase; Provisional
Pssm-ID: 165467 Cd Length: 255 Bit Score: 224.22 E-value: 1.78e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19718751 118 VAEERKHYTVYPPPHQVFTWTQMCDIKDVKVVILGQDPYHGpNQAHGLCFSVQRPVPPPPSLENIYKELSTDIEDFVHPG 197
Cdd:PHA03200 57 VDRDRQRLTVYPPPEDVHRWSRLCSPEDVKVVIVGQDPYHD-GSACGLAFGTVRGRSAPPSLKNVFRELERTVPNFSRPD 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19718751 198 HGDLSGWAKQGVLLLNAVLTVRAHQANSHKERGWEQFTDAVVSWLNQNSNGLVFLLWGSYAQKKGSAIDRKRHHVLQTAH 277
Cdd:PHA03200 136 SGCLDSWCRQGVLLLNTVFTVVHGQPGSHEALGWQTLSDRVISRLSEKREHLVFMLWGAQAQKLEYLIDSRKHLILKSAH 215
|
170 180 190
....*....|....*....|....*....|....*...
gi 19718751 278 PSP--LSVYRGFFGCRHFSKTNELLQKSGKKPIDWKEL 313
Cdd:PHA03200 216 PSPrvKGARTPFIGNNHFVLANEYLSTHGKRPIDWNIL 253
|
|
| PHA03202 |
PHA03202 |
uracil DNA glycosylase; Provisional |
97-311 |
7.28e-68 |
|
uracil DNA glycosylase; Provisional
Pssm-ID: 165469 Cd Length: 313 Bit Score: 214.56 E-value: 7.28e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19718751 97 SWKKHLSGEFGKPYFIKLMGFVAEERKHYTVYPPPHQVFTWTQMCDIKDVKVVILGQDPYHGPNQAHGLCFSVQRPVPPP 176
Cdd:PHA03202 99 SWRPILEREMQQPYVRLLLNEYKLRCAREEVFPPKEDIFAWTRFSPPEKVRVVIVGQDPYHAPGQAHGLAFSVRKGVPVP 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19718751 177 PSLENIYKELSTDIEDFVHPGHGDLSGWAKQGVLLLNAVLTVRAHQANSHKERGWEQFTDAVVSWLNQNSNGLVFLLWGS 256
Cdd:PHA03202 179 PSLRNIYSAVQKSYPSFRPPMHGFLEKWAEQGVLLINTTLTVARGKPGSHATLGWHRLVRAVIDRLCTTSQGLVFMLWGA 258
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 19718751 257 YAQKKGSAiDRKRHHVLQTAHPSPLSVYrGFFGCRHFSKTNELLQKSGKKPIDWK 311
Cdd:PHA03202 259 HAQKSCSP-NRQHHLVLTYGHPSPLSRV-NFRDCPHFLEANAYLTKTGRKPVDWQ 311
|
|
| PHA03201 |
PHA03201 |
uracil DNA glycosylase; Provisional |
95-310 |
9.03e-60 |
|
uracil DNA glycosylase; Provisional
Pssm-ID: 165468 Cd Length: 318 Bit Score: 193.57 E-value: 9.03e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19718751 95 GESWKKHLSGEFGKPYFIKLMGFVAEERKHYTVYPPPHQVFTWTQMCDIKDVKVVILGQDPYHGPNQAHGLCFSVQRPVP 174
Cdd:PHA03201 103 GDAWRPLLEPELANPLTARLMAEYERRCRTEEVLPPREDVFSWTRYCTPDEVRVVIIGQDPYHQPGQAHGLAFSVRPGTP 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19718751 175 PPPSLENIYKELSTDIEDFVHPGHGDLSGWAKQGVLLLNAVLTVRAHQANSHKERGWEQFTDAVVSWLNQNSNGLVFLLW 254
Cdd:PHA03201 183 APPSLRNILAAVRNCCPDARMSGHGCLEKWARGGVLLLNTTLTVRRGEPASHAKIGWDRFVGSVVRRLAASRPGLVFMLW 262
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 19718751 255 GSYAQkkgSAI--DRKRHHVLQTAHPSPLSvyRGFFG-CRHFSKTNELLQKSGKKPIDW 310
Cdd:PHA03201 263 GAHAQ---NAIrpDPRVHRVLTYSHPSPLS--KVPFGsCRHFCLANQYLRERSLAPIDW 316
|
|
| PHA03204 |
PHA03204 |
uracil DNA glycosylase; Provisional |
96-310 |
4.24e-59 |
|
uracil DNA glycosylase; Provisional
Pssm-ID: 165471 Cd Length: 322 Bit Score: 192.10 E-value: 4.24e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19718751 96 ESWKKHLSGEFGKPYFIKLMGFVAEERKHYTVYPPPHQVFTWTQMCDIKDVKVVILGQDPYHGPNQAHGLCFSVQRPVPP 175
Cdd:PHA03204 104 CRWKEILLPELCCPTGSKILAEYERRARYEEVYPPKSDIFAWTRYCAPDHVKVVIVGQDPYANPGQAHGLAFSVKPGSPI 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19718751 176 PPSLENIYKELSTDIEDFVHPGHGDLSGWAKQGVLLLNAVLTVRAHQANSHKERGWEQFTDAVVSWLNQNSNGLVFLLWG 255
Cdd:PHA03204 184 PPSLKNILAAVKACYPSIELGSHGCLEDWAKRGVLLLNSVLTVKRGDPGSHHSVGWQILVRNVLRRLSQSTRGIVFMLWG 263
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 19718751 256 SYAQKKGSAIDRK-RHHVLQTAHPSPLSvYRGFFGCRHFSKTNELLQKSGKKPIDW 310
Cdd:PHA03204 264 AQAQTMYFQTDNDdRHLVLKYSHPSPLS-RKPFAHCTHFKDANEFLCKMGKGAIDW 318
|
|
| UDG-F1-like |
cd19371 |
Uracil DNA glycosylase family 1, includes Human uracil DNA glycosylase, Vaccinia virus protein ... |
148-282 |
1.23e-58 |
|
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: 184.46 E-value: 1.23e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19718751 148 VVILGQDPYHGPNQAHGLCFSVQRPVPPPPSLENIYKELSTDIEDFVHPGHGDLSGWAKQGVLLLNAVLTVRAHQANSHk 227
Cdd:cd19371 1 VVIIGQDPYPSPGHAGGLAFSVTSEVPPPKSLRNIYKELERDYSSFLPPGNGTLEFWARQGVLLLNAALTCESGKPKSH- 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 19718751 228 ERGWEQFTDAVVSWLNQNSNGLVFLLWGSYAQKKGSAIDRKRHHVLQTAHPSPLS 282
Cdd:cd19371 80 YLLWEPFIKAFIRYISAHNKGLVFLLFGSDAQKLRKKINGRNVHVFKADHPSPAD 134
|
|
| PHA03199 |
PHA03199 |
uracil DNA glycosylase; Provisional |
98-310 |
1.70e-57 |
|
uracil DNA glycosylase; Provisional
Pssm-ID: 165466 Cd Length: 304 Bit Score: 187.52 E-value: 1.70e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19718751 98 WKKHLSGEFGKPYfikLMGFVAEERKHYT----VYPPPHQVFTWTQMCDIKDVKVVILGQDPYHGPNQAHGLCFSVQRPV 173
Cdd:PHA03199 91 WHDLLRDEFEEPY---AKGIFEEYNQLLNngeeIFPIKGDIFAWTRFCGPEKIRVVIIGQDPYHGAGHAHGLAFSVKRGI 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19718751 174 PPPPSLENIYKELSTDIEDFVHPGHGDLSGWAKQGVLLLNAVLTVRAHQANSHKERGWEQFTDAVVSWLNQNSNGLVFLL 253
Cdd:PHA03199 168 PIPPSLKNIFAALMESYPHLPLPTHGCLDNWARQGVLLLNTTLTVKRGTPGSHFYLGWDMLIKRMLKRLCENRTGLVFML 247
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 19718751 254 WGSYAQKKGSAIDRKrHHVLQTAHPSPLSVYRgFFGCRHFSKTNELLQKSGKKPIDW 310
Cdd:PHA03199 248 WGAHAQKTIQPNPRC-HLVLTHAHPSPLSRSE-FRNCKHFLQANEYFLKKGEPEIDW 302
|
|
| UDG |
smart00986 |
Uracil DNA glycosylase superfamily; |
144-300 |
4.27e-32 |
|
Uracil DNA glycosylase superfamily;
Pssm-ID: 214956 Cd Length: 156 Bit Score: 116.72 E-value: 4.27e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19718751 144 KDVKVVILGQDPY------HGP-NQAHGLCFSVQRPV----PPPPSLENIYKELSTDiedfvhPGHGDLSGWAKQGVLLl 212
Cdd:smart00986 6 PNAKVLIVGQAPGaseedrGGPfVGAAGLLLSVMLGVaglpRLPPYLTNIVKCRPPD------AGNRRPTSWELQGCLL- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19718751 213 nAVLTVRAHQANSHKERGWEQFTDAVVswLNQNSNGLVFLLWGSYAQKKGsaidrKRHHVLQTAHPSPLSvyRGFFGCRH 292
Cdd:smart00986 79 -PWLTVELALARPHLILLLGKFAAQAL--LGLLRRPLVFGLRGRVAQLKG-----KGHRVLPLPHPSPLN--RNFFPAKK 148
|
....*...
gi 19718751 293 FSKTNELL 300
Cdd:smart00986 149 FAAWNDLL 156
|
|
| UDG-like |
cd09593 |
uracil-DNA glycosylases (UDG) and related enzymes; Uracil-DNA glycosylases (UDGs) initiate ... |
148-282 |
1.39e-26 |
|
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: 101.31 E-value: 1.39e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19718751 148 VVILGQDPYHGPNQAHGlcfsvqrpVPPPPSLENIYKELSTDIEDFVhpghgdlsgWAKQGVLLLNAVLTVRAHQANSHk 227
Cdd:cd09593 1 VLIVGQNPGPHGARAGG--------VPPGPSGNRLWRLLAAAGGTPR---------LFRYGVGLTNTVPRGPPGAAAGS- 62
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19718751 228 ERGWEQFTDAVVSWLNQNSNGLVFLLWGSYAQKKGSAID-------RKRHHVLQTAHPSPLS 282
Cdd:cd09593 63 EKKELRFCGRWLRKLLELLNPRVVVLLGKKAQEAYLAVLtsskgapGKGTEVLVLPHPSPRN 124
|
|
| UDG |
pfam03167 |
Uracil DNA glycosylase superfamily; |
144-299 |
2.86e-18 |
|
Uracil DNA glycosylase superfamily;
Pssm-ID: 397331 Cd Length: 154 Bit Score: 80.08 E-value: 2.86e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19718751 144 KDVKVVILGQDPYHGpNQAHGLCFSVQRPVPPPPSLENIykELSTDIEDFvhpghgdlsgwakQGVLLLNAVLTVR--AH 221
Cdd:pfam03167 6 PNAKVLIVGEAPGAD-EDATGLPFVGRAGNLLWKLLNAA--GLTRDLFSP-------------QGVYITNVVKCRPgnRR 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19718751 222 QANSHK-ERGWEqFTDAVVSWLNQNsnglVFLLWGSYAQKK-----------GSAIDRKRHHVLQTAHPSPLSVYRgffg 289
Cdd:pfam03167 70 KPTSHEiDACWP-YLEAEIELLRPR----VIVLLGKTAAKAllglkkitklrGKLIDLKGIPVLPTPHPSPLLRNK---- 140
|
170
....*....|
gi 19718751 290 CRHFSKTNEL 299
Cdd:pfam03167 141 LNPFLKANAW 150
|
|
| |
