|
Name |
Accession |
Description |
Interval |
E-value |
| Ung |
COG0692 |
Uracil-DNA glycosylase [Replication, recombination and repair]; |
87-301 |
9.26e-141 |
|
Uracil-DNA glycosylase [Replication, recombination and repair];
Pssm-ID: 440456 Cd Length: 221 Bit Score: 395.95 E-value: 9.26e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6224979 87 ESWKKHLSGEFGKPYFIKLMGFVAEERK-HYTVYPPPHQVFTWTQMCDIKDVKVVILGQDPYHGPNQAHGLCFSVQRPVP 165
Cdd:COG0692 7 PSWKEALAEEFEKPYFQALGAFLKAEYAaGKTIYPPGEDIFRAFNLTPFDDVKVVILGQDPYHGPGQAHGLSFSVPPGVP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6224979 166 PPPSLENIYKELSTDIeDFVHPGHGDLSGWAKQGVLLLNAVLTVRAHQANSHKERGWEQFTDAVVSWLNQNSNGLVFLLW 245
Cdd:COG0692 87 LPPSLRNIYKELEDDL-GIPIPNHGDLTSWAEQGVLLLNTVLTVRAGQAGSHAGKGWETFTDAVIRALNARKEPVVFLLW 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 6224979 246 GSYAQKKGSAIDRKRHHVLQTAHPSPLSVYRGFFGCRHFSKTNELLQKSGKKPIDW 301
Cdd:COG0692 166 GAYAQKKAALIDASKHLVLESPHPSPLSAHRGFFGSKPFSKANAYLEEQGKTPIDW 221
|
|
| ung |
TIGR00628 |
uracil-DNA glycosylase; All proteins in this family for which functions are known are ... |
87-296 |
5.31e-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: 378.48 E-value: 5.31e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6224979 87 ESWKKHLSGEFGKPYFIKLMGFVAEERKHYTVYPPPHQVFTWTQMCDIKDVKVVILGQDPYHGPNQAHGLCFSVQRPVPP 166
Cdd:TIGR00628 2 PSWRAFLQPEFKKPYFQELLAFYKRERAQETVYPPKEDVFAWTRLCPPEDVKVVILGQDPYHGPGQAHGLAFSVKRGVPI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6224979 167 PPSLENIYKELSTDIEDFVHPGHGDLSGWAKQGVLLLNAVLTVRAHQANSHKERGWEQFTDAVVSWLNQNSNGLVFLLWG 246
Cdd:TIGR00628 82 PPSLKNIFKELEADYPDFPPPKHGCLEAWARQGVLLLNTVLTVRRGQPGSHSGLGWERFTDAVISRLSERLDGLVFMLWG 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 6224979 247 SYAQKKGSAIDRKRHHVLQTAHPSPLSVYRGFFGCRHFSKTNELLQKSGK 296
Cdd:TIGR00628 162 AHAQKKKSLIDAKKHLVLKSPHPSPLSARRGFFGCRHFSKANEYLEKHGK 211
|
|
| PRK05254 |
PRK05254 |
uracil-DNA glycosylase; Provisional |
87-301 |
6.90e-134 |
|
uracil-DNA glycosylase; Provisional
Pssm-ID: 235376 Cd Length: 224 Bit Score: 378.73 E-value: 6.90e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6224979 87 ESWKKHLSGEFGKPYFIKLMGFVAEER-KHYTVYPPPHQVFTWTQMCDIKDVKVVILGQDPYHGPNQAHGLCFSVQRPVP 165
Cdd:PRK05254 8 PSWKEVLKPEFKKPYFQELLEFLRAERaAGKTIYPPGEDIFRAFNLTPFDDVKVVILGQDPYHGPGQAHGLSFSVPPGVP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6224979 166 PPPSLENIYKELSTDIeDFVHPGHGDLSGWAKQGVLLLNAVLTVRAHQANSHKERGWEQFTDAVVSWLNQNSNGLVFLLW 245
Cdd:PRK05254 88 IPPSLRNIFKELEDDL-GFPIPNHGDLTSWAEQGVLLLNTVLTVEAGQANSHAGKGWETFTDAVIKALNERREPVVFILW 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 6224979 246 GSYAQKKGSAIDRKRHHVLQTAHPSPLSVYRGFFGCRHFSKTNELLQKSGKKPIDW 301
Cdd:PRK05254 167 GSHAQKKKALIDNSKHLILESPHPSPLSAHRGFFGSKHFSKANALLKQHGKTPIDW 222
|
|
| UDG-F1-like |
cd10027 |
Uracil DNA glycosylase family 1 subfamily, includes Human uracil DNA glycosylase and similar ... |
101-301 |
1.01e-133 |
|
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: 377.17 E-value: 1.01e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6224979 101 YFIKLMGFVAEERKHYTVYPPPHQVFTWTQMCDIKDVKVVILGQDPYHGPNQAHGLCFSVQRPVPPPPSLENIYKELSTD 180
Cdd:cd10027 1 YFKKLEAFLEEEYKKKTIYPPKEDIFRAFELTPLDDVKVVILGQDPYHGPGQAHGLAFSVPPGVKIPPSLRNIFKELKSD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6224979 181 IEDFvHPGHGDLSGWAKQGVLLLNAVLTVRAHQANSHKERGWEQFTDAVVSWLNQNSNGLVFLLWGSYAQKKGSAIDRKR 260
Cdd:cd10027 81 LGIF-PPKHGDLSSWAKQGVLLLNTVLTVEAGKPGSHKNIGWETFTDAVIKALSEKNENVVFLLWGNHAQKKKKLIDKKK 159
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 6224979 261 HHVLQTAHPSPLSVYRGFFGCRHFSKTNELLQKSGKKPIDW 301
Cdd:cd10027 160 HLVLESSHPSPLSAYRGFFGSKHFSKANEYLKKHGKKPIDW 200
|
|
| UDG |
smart00986 |
Uracil DNA glycosylase superfamily; |
135-291 |
2.50e-31 |
|
Uracil DNA glycosylase superfamily;
Pssm-ID: 214956 Cd Length: 156 Bit Score: 114.79 E-value: 2.50e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6224979 135 KDVKVVILGQDPY------HGP-NQAHGLCFSVQRPV----PPPPSLENIYKELSTDiedfvhPGHGDLSGWAKQGVLLl 203
Cdd:smart00986 6 PNAKVLIVGQAPGaseedrGGPfVGAAGLLLSVMLGVaglpRLPPYLTNIVKCRPPD------AGNRRPTSWELQGCLL- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6224979 204 nAVLTVRAHQANSHKERGWEQFTDAVVswLNQNSNGLVFLLWGSYAQKKGsaidrKRHHVLQTAHPSPLSvyRGFFGCRH 283
Cdd:smart00986 79 -PWLTVELALARPHLILLLGKFAAQAL--LGLLRRPLVFGLRGRVAQLKG-----KGHRVLPLPHPSPLN--RNFFPAKK 148
|
....*...
gi 6224979 284 FSKTNELL 291
Cdd:smart00986 149 FAAWNDLL 156
|
|
| UDG |
pfam03167 |
Uracil DNA glycosylase superfamily; |
135-290 |
7.87e-18 |
|
Uracil DNA glycosylase superfamily;
Pssm-ID: 397331 Cd Length: 154 Bit Score: 78.54 E-value: 7.87e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6224979 135 KDVKVVILGQDPYHGpNQAHGLCFSVQRPVPPPPSLENIykELSTDIEDFvhpghgdlsgwakQGVLLLNAVLTVR--AH 212
Cdd:pfam03167 6 PNAKVLIVGEAPGAD-EDATGLPFVGRAGNLLWKLLNAA--GLTRDLFSP-------------QGVYITNVVKCRPgnRR 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6224979 213 QANSHK-ERGWEqFTDAVVSWLNQNsnglVFLLWGSYAQKK-----------GSAIDRKRHHVLQTAHPSPLSVYRgffg 280
Cdd:pfam03167 70 KPTSHEiDACWP-YLEAEIELLRPR----VIVLLGKTAAKAllglkkitklrGKLIDLKGIPVLPTPHPSPLLRNK---- 140
|
170
....*....|
gi 6224979 281 CRHFSKTNEL 290
Cdd:pfam03167 141 LNPFLKANAW 150
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Ung |
COG0692 |
Uracil-DNA glycosylase [Replication, recombination and repair]; |
87-301 |
9.26e-141 |
|
Uracil-DNA glycosylase [Replication, recombination and repair];
Pssm-ID: 440456 Cd Length: 221 Bit Score: 395.95 E-value: 9.26e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6224979 87 ESWKKHLSGEFGKPYFIKLMGFVAEERK-HYTVYPPPHQVFTWTQMCDIKDVKVVILGQDPYHGPNQAHGLCFSVQRPVP 165
Cdd:COG0692 7 PSWKEALAEEFEKPYFQALGAFLKAEYAaGKTIYPPGEDIFRAFNLTPFDDVKVVILGQDPYHGPGQAHGLSFSVPPGVP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6224979 166 PPPSLENIYKELSTDIeDFVHPGHGDLSGWAKQGVLLLNAVLTVRAHQANSHKERGWEQFTDAVVSWLNQNSNGLVFLLW 245
Cdd:COG0692 87 LPPSLRNIYKELEDDL-GIPIPNHGDLTSWAEQGVLLLNTVLTVRAGQAGSHAGKGWETFTDAVIRALNARKEPVVFLLW 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 6224979 246 GSYAQKKGSAIDRKRHHVLQTAHPSPLSVYRGFFGCRHFSKTNELLQKSGKKPIDW 301
Cdd:COG0692 166 GAYAQKKAALIDASKHLVLESPHPSPLSAHRGFFGSKPFSKANAYLEEQGKTPIDW 221
|
|
| ung |
TIGR00628 |
uracil-DNA glycosylase; All proteins in this family for which functions are known are ... |
87-296 |
5.31e-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: 378.48 E-value: 5.31e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6224979 87 ESWKKHLSGEFGKPYFIKLMGFVAEERKHYTVYPPPHQVFTWTQMCDIKDVKVVILGQDPYHGPNQAHGLCFSVQRPVPP 166
Cdd:TIGR00628 2 PSWRAFLQPEFKKPYFQELLAFYKRERAQETVYPPKEDVFAWTRLCPPEDVKVVILGQDPYHGPGQAHGLAFSVKRGVPI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6224979 167 PPSLENIYKELSTDIEDFVHPGHGDLSGWAKQGVLLLNAVLTVRAHQANSHKERGWEQFTDAVVSWLNQNSNGLVFLLWG 246
Cdd:TIGR00628 82 PPSLKNIFKELEADYPDFPPPKHGCLEAWARQGVLLLNTVLTVRRGQPGSHSGLGWERFTDAVISRLSERLDGLVFMLWG 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 6224979 247 SYAQKKGSAIDRKRHHVLQTAHPSPLSVYRGFFGCRHFSKTNELLQKSGK 296
Cdd:TIGR00628 162 AHAQKKKSLIDAKKHLVLKSPHPSPLSARRGFFGCRHFSKANEYLEKHGK 211
|
|
| PRK05254 |
PRK05254 |
uracil-DNA glycosylase; Provisional |
87-301 |
6.90e-134 |
|
uracil-DNA glycosylase; Provisional
Pssm-ID: 235376 Cd Length: 224 Bit Score: 378.73 E-value: 6.90e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6224979 87 ESWKKHLSGEFGKPYFIKLMGFVAEER-KHYTVYPPPHQVFTWTQMCDIKDVKVVILGQDPYHGPNQAHGLCFSVQRPVP 165
Cdd:PRK05254 8 PSWKEVLKPEFKKPYFQELLEFLRAERaAGKTIYPPGEDIFRAFNLTPFDDVKVVILGQDPYHGPGQAHGLSFSVPPGVP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6224979 166 PPPSLENIYKELSTDIeDFVHPGHGDLSGWAKQGVLLLNAVLTVRAHQANSHKERGWEQFTDAVVSWLNQNSNGLVFLLW 245
Cdd:PRK05254 88 IPPSLRNIFKELEDDL-GFPIPNHGDLTSWAEQGVLLLNTVLTVEAGQANSHAGKGWETFTDAVIKALNERREPVVFILW 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 6224979 246 GSYAQKKGSAIDRKRHHVLQTAHPSPLSVYRGFFGCRHFSKTNELLQKSGKKPIDW 301
Cdd:PRK05254 167 GSHAQKKKALIDNSKHLILESPHPSPLSAHRGFFGSKHFSKANALLKQHGKTPIDW 222
|
|
| UDG-F1-like |
cd10027 |
Uracil DNA glycosylase family 1 subfamily, includes Human uracil DNA glycosylase and similar ... |
101-301 |
1.01e-133 |
|
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: 377.17 E-value: 1.01e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6224979 101 YFIKLMGFVAEERKHYTVYPPPHQVFTWTQMCDIKDVKVVILGQDPYHGPNQAHGLCFSVQRPVPPPPSLENIYKELSTD 180
Cdd:cd10027 1 YFKKLEAFLEEEYKKKTIYPPKEDIFRAFELTPLDDVKVVILGQDPYHGPGQAHGLAFSVPPGVKIPPSLRNIFKELKSD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6224979 181 IEDFvHPGHGDLSGWAKQGVLLLNAVLTVRAHQANSHKERGWEQFTDAVVSWLNQNSNGLVFLLWGSYAQKKGSAIDRKR 260
Cdd:cd10027 81 LGIF-PPKHGDLSSWAKQGVLLLNTVLTVEAGKPGSHKNIGWETFTDAVIKALSEKNENVVFLLWGNHAQKKKKLIDKKK 159
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 6224979 261 HHVLQTAHPSPLSVYRGFFGCRHFSKTNELLQKSGKKPIDW 301
Cdd:cd10027 160 HLVLESSHPSPLSAYRGFFGSKHFSKANEYLKKHGKKPIDW 200
|
|
| PHA03347 |
PHA03347 |
uracil DNA glycosylase; Provisional |
87-301 |
6.59e-77 |
|
uracil DNA glycosylase; Provisional
Pssm-ID: 177588 Cd Length: 252 Bit Score: 234.94 E-value: 6.59e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6224979 87 ESWKKHLS-GEFGKPYFIKLMGFVAEERKHYTVYPPPHQVFTWTQMCDIKDVKVVILGQDPYHGpNQAHGLCFSVQRPVP 165
Cdd:PHA03347 28 DPWLDFLQlSPFLKQKLLALLNCVRELRKQTVIYPPEDRIMAWSYLCDPEDIKVVILGQDPYHG-GQANGLAFSVAYGFP 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6224979 166 PPPSLENIYKELSTDIEDFVHPGHGDLSGWAKQGVLLLNAVLTVRAHQANSHKERGWEQFTDAVVSWLNQNSNGLVFLLW 245
Cdd:PHA03347 107 VPPSLRNIFAELHRSVPDFSPPDHGCLDAWARQGVLLLNTILTVEKGKPGSHSDLGWAWFTDYIISSLSEKLKACVFMLW 186
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6224979 246 GSYAQKKGSAIDRKRHHVLQTAHPSPL---SVYRG----FFGCRHFSKTNELLQKSGKKPIDW 301
Cdd:PHA03347 187 GSKAIDKASLINSQKHLVLKAQHPSPLaanSTRSStwpkFLGCNHFVLANKYLTQHGKGPIDW 249
|
|
| PHA03200 |
PHA03200 |
uracil DNA glycosylase; Provisional |
109-304 |
4.21e-72 |
|
uracil DNA glycosylase; Provisional
Pssm-ID: 165467 Cd Length: 255 Bit Score: 223.07 E-value: 4.21e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6224979 109 VAEERKHYTVYPPPHQVFTWTQMCDIKDVKVVILGQDPYHGpNQAHGLCFSVQRPVPPPPSLENIYKELSTDIEDFVHPG 188
Cdd:PHA03200 57 VDRDRQRLTVYPPPEDVHRWSRLCSPEDVKVVIVGQDPYHD-GSACGLAFGTVRGRSAPPSLKNVFRELERTVPNFSRPD 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6224979 189 HGDLSGWAKQGVLLLNAVLTVRAHQANSHKERGWEQFTDAVVSWLNQNSNGLVFLLWGSYAQKKGSAIDRKRHHVLQTAH 268
Cdd:PHA03200 136 SGCLDSWCRQGVLLLNTVFTVVHGQPGSHEALGWQTLSDRVISRLSEKREHLVFMLWGAQAQKLEYLIDSRKHLILKSAH 215
|
170 180 190
....*....|....*....|....*....|....*...
gi 6224979 269 PSP--LSVYRGFFGCRHFSKTNELLQKSGKKPIDWKEL 304
Cdd:PHA03200 216 PSPrvKGARTPFIGNNHFVLANEYLSTHGKRPIDWNIL 253
|
|
| PHA03202 |
PHA03202 |
uracil DNA glycosylase; Provisional |
88-302 |
7.58e-69 |
|
uracil DNA glycosylase; Provisional
Pssm-ID: 165469 Cd Length: 313 Bit Score: 216.49 E-value: 7.58e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6224979 88 SWKKHLSGEFGKPYFIKLMGFVAEERKHYTVYPPPHQVFTWTQMCDIKDVKVVILGQDPYHGPNQAHGLCFSVQRPVPPP 167
Cdd:PHA03202 99 SWRPILEREMQQPYVRLLLNEYKLRCAREEVFPPKEDIFAWTRFSPPEKVRVVIVGQDPYHAPGQAHGLAFSVRKGVPVP 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6224979 168 PSLENIYKELSTDIEDFVHPGHGDLSGWAKQGVLLLNAVLTVRAHQANSHKERGWEQFTDAVVSWLNQNSNGLVFLLWGS 247
Cdd:PHA03202 179 PSLRNIYSAVQKSYPSFRPPMHGFLEKWAEQGVLLINTTLTVARGKPGSHATLGWHRLVRAVIDRLCTTSQGLVFMLWGA 258
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 6224979 248 YAQKKGSAiDRKRHHVLQTAHPSPLSVYrGFFGCRHFSKTNELLQKSGKKPIDWK 302
Cdd:PHA03202 259 HAQKSCSP-NRQHHLVLTYGHPSPLSRV-NFRDCPHFLEANAYLTKTGRKPVDWQ 311
|
|
| PHA03201 |
PHA03201 |
uracil DNA glycosylase; Provisional |
86-301 |
1.46e-60 |
|
uracil DNA glycosylase; Provisional
Pssm-ID: 165468 Cd Length: 318 Bit Score: 195.50 E-value: 1.46e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6224979 86 GESWKKHLSGEFGKPYFIKLMGFVAEERKHYTVYPPPHQVFTWTQMCDIKDVKVVILGQDPYHGPNQAHGLCFSVQRPVP 165
Cdd:PHA03201 103 GDAWRPLLEPELANPLTARLMAEYERRCRTEEVLPPREDVFSWTRYCTPDEVRVVIIGQDPYHQPGQAHGLAFSVRPGTP 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6224979 166 PPPSLENIYKELSTDIEDFVHPGHGDLSGWAKQGVLLLNAVLTVRAHQANSHKERGWEQFTDAVVSWLNQNSNGLVFLLW 245
Cdd:PHA03201 183 APPSLRNILAAVRNCCPDARMSGHGCLEKWARGGVLLLNTTLTVRRGEPASHAKIGWDRFVGSVVRRLAASRPGLVFMLW 262
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 6224979 246 GSYAQkkgSAI--DRKRHHVLQTAHPSPLSvyRGFFG-CRHFSKTNELLQKSGKKPIDW 301
Cdd:PHA03201 263 GAHAQ---NAIrpDPRVHRVLTYSHPSPLS--KVPFGsCRHFCLANQYLRERSLAPIDW 316
|
|
| PHA03204 |
PHA03204 |
uracil DNA glycosylase; Provisional |
87-301 |
2.15e-59 |
|
uracil DNA glycosylase; Provisional
Pssm-ID: 165471 Cd Length: 322 Bit Score: 192.48 E-value: 2.15e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6224979 87 ESWKKHLSGEFGKPYFIKLMGFVAEERKHYTVYPPPHQVFTWTQMCDIKDVKVVILGQDPYHGPNQAHGLCFSVQRPVPP 166
Cdd:PHA03204 104 CRWKEILLPELCCPTGSKILAEYERRARYEEVYPPKSDIFAWTRYCAPDHVKVVIVGQDPYANPGQAHGLAFSVKPGSPI 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6224979 167 PPSLENIYKELSTDIEDFVHPGHGDLSGWAKQGVLLLNAVLTVRAHQANSHKERGWEQFTDAVVSWLNQNSNGLVFLLWG 246
Cdd:PHA03204 184 PPSLKNILAAVKACYPSIELGSHGCLEDWAKRGVLLLNSVLTVKRGDPGSHHSVGWQILVRNVLRRLSQSTRGIVFMLWG 263
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 6224979 247 SYAQKKGSAIDRK-RHHVLQTAHPSPLSvYRGFFGCRHFSKTNELLQKSGKKPIDW 301
Cdd:PHA03204 264 AQAQTMYFQTDNDdRHLVLKYSHPSPLS-RKPFAHCTHFKDANEFLCKMGKGAIDW 318
|
|
| UDG-F1-like |
cd19371 |
Uracil DNA glycosylase family 1, includes Human uracil DNA glycosylase, Vaccinia virus protein ... |
139-273 |
1.17e-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: 1.17e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6224979 139 VVILGQDPYHGPNQAHGLCFSVQRPVPPPPSLENIYKELSTDIEDFVHPGHGDLSGWAKQGVLLLNAVLTVRAHQANSHk 218
Cdd:cd19371 1 VVIIGQDPYPSPGHAGGLAFSVTSEVPPPKSLRNIYKELERDYSSFLPPGNGTLEFWARQGVLLLNAALTCESGKPKSH- 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 6224979 219 ERGWEQFTDAVVSWLNQNSNGLVFLLWGSYAQKKGSAIDRKRHHVLQTAHPSPLS 273
Cdd:cd19371 80 YLLWEPFIKAFIRYISAHNKGLVFLLFGSDAQKLRKKINGRNVHVFKADHPSPAD 134
|
|
| PHA03199 |
PHA03199 |
uracil DNA glycosylase; Provisional |
89-301 |
7.27e-58 |
|
uracil DNA glycosylase; Provisional
Pssm-ID: 165466 Cd Length: 304 Bit Score: 187.91 E-value: 7.27e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6224979 89 WKKHLSGEFGKPYfikLMGFVAEERKHYT----VYPPPHQVFTWTQMCDIKDVKVVILGQDPYHGPNQAHGLCFSVQRPV 164
Cdd:PHA03199 91 WHDLLRDEFEEPY---AKGIFEEYNQLLNngeeIFPIKGDIFAWTRFCGPEKIRVVIIGQDPYHGAGHAHGLAFSVKRGI 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6224979 165 PPPPSLENIYKELSTDIEDFVHPGHGDLSGWAKQGVLLLNAVLTVRAHQANSHKERGWEQFTDAVVSWLNQNSNGLVFLL 244
Cdd:PHA03199 168 PIPPSLKNIFAALMESYPHLPLPTHGCLDNWARQGVLLLNTTLTVKRGTPGSHFYLGWDMLIKRMLKRLCENRTGLVFML 247
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 6224979 245 WGSYAQKKGSAIDRKrHHVLQTAHPSPLSVYRgFFGCRHFSKTNELLQKSGKKPIDW 301
Cdd:PHA03199 248 WGAHAQKTIQPNPRC-HLVLTHAHPSPLSRSE-FRNCKHFLQANEYFLKKGEPEIDW 302
|
|
| UDG |
smart00986 |
Uracil DNA glycosylase superfamily; |
135-291 |
2.50e-31 |
|
Uracil DNA glycosylase superfamily;
Pssm-ID: 214956 Cd Length: 156 Bit Score: 114.79 E-value: 2.50e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6224979 135 KDVKVVILGQDPY------HGP-NQAHGLCFSVQRPV----PPPPSLENIYKELSTDiedfvhPGHGDLSGWAKQGVLLl 203
Cdd:smart00986 6 PNAKVLIVGQAPGaseedrGGPfVGAAGLLLSVMLGVaglpRLPPYLTNIVKCRPPD------AGNRRPTSWELQGCLL- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6224979 204 nAVLTVRAHQANSHKERGWEQFTDAVVswLNQNSNGLVFLLWGSYAQKKGsaidrKRHHVLQTAHPSPLSvyRGFFGCRH 283
Cdd:smart00986 79 -PWLTVELALARPHLILLLGKFAAQAL--LGLLRRPLVFGLRGRVAQLKG-----KGHRVLPLPHPSPLN--RNFFPAKK 148
|
....*...
gi 6224979 284 FSKTNELL 291
Cdd:smart00986 149 FAAWNDLL 156
|
|
| UDG-like |
cd09593 |
uracil-DNA glycosylases (UDG) and related enzymes; Uracil-DNA glycosylases (UDGs) initiate ... |
139-273 |
2.33e-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: 100.54 E-value: 2.33e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6224979 139 VVILGQDPYHGPNQAHGlcfsvqrpVPPPPSLENIYKELSTDIEDFVhpghgdlsgWAKQGVLLLNAVLTVRAHQANSHk 218
Cdd:cd09593 1 VLIVGQNPGPHGARAGG--------VPPGPSGNRLWRLLAAAGGTPR---------LFRYGVGLTNTVPRGPPGAAAGS- 62
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6224979 219 ERGWEQFTDAVVSWLNQNSNGLVFLLWGSYAQKKGSAID-------RKRHHVLQTAHPSPLS 273
Cdd:cd09593 63 EKKELRFCGRWLRKLLELLNPRVVVLLGKKAQEAYLAVLtsskgapGKGTEVLVLPHPSPRN 124
|
|
| UDG |
pfam03167 |
Uracil DNA glycosylase superfamily; |
135-290 |
7.87e-18 |
|
Uracil DNA glycosylase superfamily;
Pssm-ID: 397331 Cd Length: 154 Bit Score: 78.54 E-value: 7.87e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6224979 135 KDVKVVILGQDPYHGpNQAHGLCFSVQRPVPPPPSLENIykELSTDIEDFvhpghgdlsgwakQGVLLLNAVLTVR--AH 212
Cdd:pfam03167 6 PNAKVLIVGEAPGAD-EDATGLPFVGRAGNLLWKLLNAA--GLTRDLFSP-------------QGVYITNVVKCRPgnRR 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6224979 213 QANSHK-ERGWEqFTDAVVSWLNQNsnglVFLLWGSYAQKK-----------GSAIDRKRHHVLQTAHPSPLSVYRgffg 280
Cdd:pfam03167 70 KPTSHEiDACWP-YLEAEIELLRPR----VIVLLGKTAAKAllglkkitklrGKLIDLKGIPVLPTPHPSPLLRNK---- 140
|
170
....*....|
gi 6224979 281 CRHFSKTNEL 290
Cdd:pfam03167 141 LNPFLKANAW 150
|
|
| |
