|
Name |
Accession |
Description |
Interval |
E-value |
| Ung |
COG0692 |
Uracil-DNA glycosylase [Replication, recombination and repair]; |
84-300 |
7.26e-138 |
|
Uracil-DNA glycosylase [Replication, recombination and repair];
Pssm-ID: 440456 Cd Length: 221 Bit Score: 388.63 E-value: 7.26e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61557031 84 LGESWKQQLCGEFGKPYFVKLMGFVAEERK-HHKVYPPPEQVFTWTQMCDIRDVKVVILGQDPYHGPNQAHGLCFSVQRP 162
Cdd:COG0692 5 LEPSWKEALAEEFEKPYFQALGAFLKAEYAaGKTIYPPGEDIFRAFNLTPFDDVKVVILGQDPYHGPGQAHGLSFSVPPG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61557031 163 VPPPPSLENIFKELSTDIdGFVHPGHGDLSGWARQGVLLLNAVLTVRAHQANSHKERGWEQFTDAVVSWLNQNLNGLVFL 242
Cdd:COG0692 85 VPLPPSLRNIYKELEDDL-GIPIPNHGDLTSWAEQGVLLLNTVLTVRAGQAGSHAGKGWETFTDAVIRALNARKEPVVFL 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 61557031 243 LWGSYAQKKGSAIDRKRHHVLQTAHPSPLSVYRGFFGCRHFSKANELLQRSGKKPISW 300
Cdd:COG0692 164 LWGAYAQKKAALIDASKHLVLESPHPSPLSAHRGFFGSKPFSKANAYLEEQGKTPIDW 221
|
|
| ung |
TIGR00628 |
uracil-DNA glycosylase; All proteins in this family for which functions are known are ... |
86-295 |
1.23e-135 |
|
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: 382.33 E-value: 1.23e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61557031 86 ESWKQQLCGEFGKPYFVKLMGFVAEERKHHKVYPPPEQVFTWTQMCDIRDVKVVILGQDPYHGPNQAHGLCFSVQRPVPP 165
Cdd:TIGR00628 2 PSWRAFLQPEFKKPYFQELLAFYKRERAQETVYPPKEDVFAWTRLCPPEDVKVVILGQDPYHGPGQAHGLAFSVKRGVPI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61557031 166 PPSLENIFKELSTDIDGFVHPGHGDLSGWARQGVLLLNAVLTVRAHQANSHKERGWEQFTDAVVSWLNQNLNGLVFLLWG 245
Cdd:TIGR00628 82 PPSLKNIFKELEADYPDFPPPKHGCLEAWARQGVLLLNTVLTVRRGQPGSHSGLGWERFTDAVISRLSERLDGLVFMLWG 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 61557031 246 SYAQKKGSAIDRKRHHVLQTAHPSPLSVYRGFFGCRHFSKANELLQRSGK 295
Cdd:TIGR00628 162 AHAQKKKSLIDAKKHLVLKSPHPSPLSARRGFFGCRHFSKANEYLEKHGK 211
|
|
| UDG-F1-like |
cd10027 |
Uracil DNA glycosylase family 1 subfamily, includes Human uracil DNA glycosylase and similar ... |
100-300 |
2.57e-132 |
|
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: 373.71 E-value: 2.57e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61557031 100 YFVKLMGFVAEERKHHKVYPPPEQVFTWTQMCDIRDVKVVILGQDPYHGPNQAHGLCFSVQRPVPPPPSLENIFKELSTD 179
Cdd:cd10027 1 YFKKLEAFLEEEYKKKTIYPPKEDIFRAFELTPLDDVKVVILGQDPYHGPGQAHGLAFSVPPGVKIPPSLRNIFKELKSD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61557031 180 IDGFvHPGHGDLSGWARQGVLLLNAVLTVRAHQANSHKERGWEQFTDAVVSWLNQNLNGLVFLLWGSYAQKKGSAIDRKR 259
Cdd:cd10027 81 LGIF-PPKHGDLSSWAKQGVLLLNTVLTVEAGKPGSHKNIGWETFTDAVIKALSEKNENVVFLLWGNHAQKKKKLIDKKK 159
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 61557031 260 HHVLQTAHPSPLSVYRGFFGCRHFSKANELLQRSGKKPISW 300
Cdd:cd10027 160 HLVLESSHPSPLSAYRGFFGSKHFSKANEYLKKHGKKPIDW 200
|
|
| PRK05254 |
PRK05254 |
uracil-DNA glycosylase; Provisional |
84-300 |
1.73e-131 |
|
uracil-DNA glycosylase; Provisional
Pssm-ID: 235376 Cd Length: 224 Bit Score: 372.56 E-value: 1.73e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61557031 84 LGESWKQQLCGEFGKPYFVKLMGFVAEER-KHHKVYPPPEQVFTWTQMCDIRDVKVVILGQDPYHGPNQAHGLCFSVQRP 162
Cdd:PRK05254 6 LEPSWKEVLKPEFKKPYFQELLEFLRAERaAGKTIYPPGEDIFRAFNLTPFDDVKVVILGQDPYHGPGQAHGLSFSVPPG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61557031 163 VPPPPSLENIFKELSTDIdGFVHPGHGDLSGWARQGVLLLNAVLTVRAHQANSHKERGWEQFTDAVVSWLNQNLNGLVFL 242
Cdd:PRK05254 86 VPIPPSLRNIFKELEDDL-GFPIPNHGDLTSWAEQGVLLLNTVLTVEAGQANSHAGKGWETFTDAVIKALNERREPVVFI 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 61557031 243 LWGSYAQKKGSAIDRKRHHVLQTAHPSPLSVYRGFFGCRHFSKANELLQRSGKKPISW 300
Cdd:PRK05254 165 LWGSHAQKKKALIDNSKHLILESPHPSPLSAHRGFFGSKHFSKANALLKQHGKTPIDW 222
|
|
| UDG |
smart00986 |
Uracil DNA glycosylase superfamily; |
134-290 |
1.63e-30 |
|
Uracil DNA glycosylase superfamily;
Pssm-ID: 214956 Cd Length: 156 Bit Score: 112.48 E-value: 1.63e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61557031 134 RDVKVVILGQDPY------HGP-NQAHGLCFSVQRPV----PPPPSLENIFKELSTDidgfvhPGHGDLSGWARQGVLLl 202
Cdd:smart00986 6 PNAKVLIVGQAPGaseedrGGPfVGAAGLLLSVMLGVaglpRLPPYLTNIVKCRPPD------AGNRRPTSWELQGCLL- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61557031 203 nAVLTVRAHQANSHKERGWEQFTDAVVswLNQNLNGLVFLLWGSYAQKKGsaidrKRHHVLQTAHPSPLSvyRGFFGCRH 282
Cdd:smart00986 79 -PWLTVELALARPHLILLLGKFAAQAL--LGLLRRPLVFGLRGRVAQLKG-----KGHRVLPLPHPSPLN--RNFFPAKK 148
|
....*...
gi 61557031 283 FSKANELL 290
Cdd:smart00986 149 FAAWNDLL 156
|
|
| UDG |
pfam03167 |
Uracil DNA glycosylase superfamily; |
135-289 |
8.43e-18 |
|
Uracil DNA glycosylase superfamily;
Pssm-ID: 397331 Cd Length: 154 Bit Score: 78.54 E-value: 8.43e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61557031 135 DVKVVILGQDPYHGpNQAHGLCFSVQRPVPPPPSLENIfkELSTDIDgfvhpghgdlsgwARQGVLLLNAVLTVR--AHQ 212
Cdd:pfam03167 7 NAKVLIVGEAPGAD-EDATGLPFVGRAGNLLWKLLNAA--GLTRDLF-------------SPQGVYITNVVKCRPgnRRK 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61557031 213 ANSHKERGWEQFTDAVVSWLNQNlnglVFLLWGSYAQKK-----------GSAIDRKRHHVLQTAHPSPLSVYRgffgCR 281
Cdd:pfam03167 71 PTSHEIDACWPYLEAEIELLRPR----VIVLLGKTAAKAllglkkitklrGKLIDLKGIPVLPTPHPSPLLRNK----LN 142
|
....*...
gi 61557031 282 HFSKANEL 289
Cdd:pfam03167 143 PFLKANAW 150
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Ung |
COG0692 |
Uracil-DNA glycosylase [Replication, recombination and repair]; |
84-300 |
7.26e-138 |
|
Uracil-DNA glycosylase [Replication, recombination and repair];
Pssm-ID: 440456 Cd Length: 221 Bit Score: 388.63 E-value: 7.26e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61557031 84 LGESWKQQLCGEFGKPYFVKLMGFVAEERK-HHKVYPPPEQVFTWTQMCDIRDVKVVILGQDPYHGPNQAHGLCFSVQRP 162
Cdd:COG0692 5 LEPSWKEALAEEFEKPYFQALGAFLKAEYAaGKTIYPPGEDIFRAFNLTPFDDVKVVILGQDPYHGPGQAHGLSFSVPPG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61557031 163 VPPPPSLENIFKELSTDIdGFVHPGHGDLSGWARQGVLLLNAVLTVRAHQANSHKERGWEQFTDAVVSWLNQNLNGLVFL 242
Cdd:COG0692 85 VPLPPSLRNIYKELEDDL-GIPIPNHGDLTSWAEQGVLLLNTVLTVRAGQAGSHAGKGWETFTDAVIRALNARKEPVVFL 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 61557031 243 LWGSYAQKKGSAIDRKRHHVLQTAHPSPLSVYRGFFGCRHFSKANELLQRSGKKPISW 300
Cdd:COG0692 164 LWGAYAQKKAALIDASKHLVLESPHPSPLSAHRGFFGSKPFSKANAYLEEQGKTPIDW 221
|
|
| ung |
TIGR00628 |
uracil-DNA glycosylase; All proteins in this family for which functions are known are ... |
86-295 |
1.23e-135 |
|
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: 382.33 E-value: 1.23e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61557031 86 ESWKQQLCGEFGKPYFVKLMGFVAEERKHHKVYPPPEQVFTWTQMCDIRDVKVVILGQDPYHGPNQAHGLCFSVQRPVPP 165
Cdd:TIGR00628 2 PSWRAFLQPEFKKPYFQELLAFYKRERAQETVYPPKEDVFAWTRLCPPEDVKVVILGQDPYHGPGQAHGLAFSVKRGVPI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61557031 166 PPSLENIFKELSTDIDGFVHPGHGDLSGWARQGVLLLNAVLTVRAHQANSHKERGWEQFTDAVVSWLNQNLNGLVFLLWG 245
Cdd:TIGR00628 82 PPSLKNIFKELEADYPDFPPPKHGCLEAWARQGVLLLNTVLTVRRGQPGSHSGLGWERFTDAVISRLSERLDGLVFMLWG 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 61557031 246 SYAQKKGSAIDRKRHHVLQTAHPSPLSVYRGFFGCRHFSKANELLQRSGK 295
Cdd:TIGR00628 162 AHAQKKKSLIDAKKHLVLKSPHPSPLSARRGFFGCRHFSKANEYLEKHGK 211
|
|
| UDG-F1-like |
cd10027 |
Uracil DNA glycosylase family 1 subfamily, includes Human uracil DNA glycosylase and similar ... |
100-300 |
2.57e-132 |
|
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: 373.71 E-value: 2.57e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61557031 100 YFVKLMGFVAEERKHHKVYPPPEQVFTWTQMCDIRDVKVVILGQDPYHGPNQAHGLCFSVQRPVPPPPSLENIFKELSTD 179
Cdd:cd10027 1 YFKKLEAFLEEEYKKKTIYPPKEDIFRAFELTPLDDVKVVILGQDPYHGPGQAHGLAFSVPPGVKIPPSLRNIFKELKSD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61557031 180 IDGFvHPGHGDLSGWARQGVLLLNAVLTVRAHQANSHKERGWEQFTDAVVSWLNQNLNGLVFLLWGSYAQKKGSAIDRKR 259
Cdd:cd10027 81 LGIF-PPKHGDLSSWAKQGVLLLNTVLTVEAGKPGSHKNIGWETFTDAVIKALSEKNENVVFLLWGNHAQKKKKLIDKKK 159
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 61557031 260 HHVLQTAHPSPLSVYRGFFGCRHFSKANELLQRSGKKPISW 300
Cdd:cd10027 160 HLVLESSHPSPLSAYRGFFGSKHFSKANEYLKKHGKKPIDW 200
|
|
| PRK05254 |
PRK05254 |
uracil-DNA glycosylase; Provisional |
84-300 |
1.73e-131 |
|
uracil-DNA glycosylase; Provisional
Pssm-ID: 235376 Cd Length: 224 Bit Score: 372.56 E-value: 1.73e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61557031 84 LGESWKQQLCGEFGKPYFVKLMGFVAEER-KHHKVYPPPEQVFTWTQMCDIRDVKVVILGQDPYHGPNQAHGLCFSVQRP 162
Cdd:PRK05254 6 LEPSWKEVLKPEFKKPYFQELLEFLRAERaAGKTIYPPGEDIFRAFNLTPFDDVKVVILGQDPYHGPGQAHGLSFSVPPG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61557031 163 VPPPPSLENIFKELSTDIdGFVHPGHGDLSGWARQGVLLLNAVLTVRAHQANSHKERGWEQFTDAVVSWLNQNLNGLVFL 242
Cdd:PRK05254 86 VPIPPSLRNIFKELEDDL-GFPIPNHGDLTSWAEQGVLLLNTVLTVEAGQANSHAGKGWETFTDAVIKALNERREPVVFI 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 61557031 243 LWGSYAQKKGSAIDRKRHHVLQTAHPSPLSVYRGFFGCRHFSKANELLQRSGKKPISW 300
Cdd:PRK05254 165 LWGSHAQKKKALIDNSKHLILESPHPSPLSAHRGFFGSKHFSKANALLKQHGKTPIDW 222
|
|
| PHA03347 |
PHA03347 |
uracil DNA glycosylase; Provisional |
96-300 |
8.69e-79 |
|
uracil DNA glycosylase; Provisional
Pssm-ID: 177588 Cd Length: 252 Bit Score: 239.95 E-value: 8.69e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61557031 96 FGKPYFVKLMGFVAEERKHHKVYPPPEQVFTWTQMCDIRDVKVVILGQDPYHGpNQAHGLCFSVQRPVPPPPSLENIFKE 175
Cdd:PHA03347 39 FLKQKLLALLNCVRELRKQTVIYPPEDRIMAWSYLCDPEDIKVVILGQDPYHG-GQANGLAFSVAYGFPVPPSLRNIFAE 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61557031 176 LSTDIDGFVHPGHGDLSGWARQGVLLLNAVLTVRAHQANSHKERGWEQFTDAVVSWLNQNLNGLVFLLWGSYAQKKGSAI 255
Cdd:PHA03347 118 LHRSVPDFSPPDHGCLDAWARQGVLLLNTILTVEKGKPGSHSDLGWAWFTDYIISSLSEKLKACVFMLWGSKAIDKASLI 197
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 61557031 256 DRKRHHVLQTAHPSPL---SVYRG----FFGCRHFSKANELLQRSGKKPISW 300
Cdd:PHA03347 198 NSQKHLVLKAQHPSPLaanSTRSStwpkFLGCNHFVLANKYLTQHGKGPIDW 249
|
|
| PHA03200 |
PHA03200 |
uracil DNA glycosylase; Provisional |
108-303 |
2.85e-74 |
|
uracil DNA glycosylase; Provisional
Pssm-ID: 165467 Cd Length: 255 Bit Score: 228.46 E-value: 2.85e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61557031 108 VAEERKHHKVYPPPEQVFTWTQMCDIRDVKVVILGQDPYHGpNQAHGLCFSVQRPVPPPPSLENIFKELSTDIDGFVHPG 187
Cdd:PHA03200 57 VDRDRQRLTVYPPPEDVHRWSRLCSPEDVKVVIVGQDPYHD-GSACGLAFGTVRGRSAPPSLKNVFRELERTVPNFSRPD 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61557031 188 HGDLSGWARQGVLLLNAVLTVRAHQANSHKERGWEQFTDAVVSWLNQNLNGLVFLLWGSYAQKKGSAIDRKRHHVLQTAH 267
Cdd:PHA03200 136 SGCLDSWCRQGVLLLNTVFTVVHGQPGSHEALGWQTLSDRVISRLSEKREHLVFMLWGAQAQKLEYLIDSRKHLILKSAH 215
|
170 180 190
....*....|....*....|....*....|....*...
gi 61557031 268 PSP--LSVYRGFFGCRHFSKANELLQRSGKKPISWKEL 303
Cdd:PHA03200 216 PSPrvKGARTPFIGNNHFVLANEYLSTHGKRPIDWNIL 253
|
|
| PHA03202 |
PHA03202 |
uracil DNA glycosylase; Provisional |
84-301 |
4.16e-66 |
|
uracil DNA glycosylase; Provisional
Pssm-ID: 165469 Cd Length: 313 Bit Score: 209.55 E-value: 4.16e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61557031 84 LGESWKQQLCGEFGKPYFVKLMGFVAEERKHHKVYPPPEQVFTWTQMCDIRDVKVVILGQDPYHGPNQAHGLCFSVQRPV 163
Cdd:PHA03202 96 IAPSWRPILEREMQQPYVRLLLNEYKLRCAREEVFPPKEDIFAWTRFSPPEKVRVVIVGQDPYHAPGQAHGLAFSVRKGV 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61557031 164 PPPPSLENIFKELSTDIDGFVHPGHGDLSGWARQGVLLLNAVLTVRAHQANSHKERGWEQFTDAVVSWLNQNLNGLVFLL 243
Cdd:PHA03202 176 PVPPSLRNIYSAVQKSYPSFRPPMHGFLEKWAEQGVLLINTTLTVARGKPGSHATLGWHRLVRAVIDRLCTTSQGLVFML 255
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 61557031 244 WGSYAQKKGSAiDRKRHHVLQTAHPSPLSVYrGFFGCRHFSKANELLQRSGKKPISWK 301
Cdd:PHA03202 256 WGAHAQKSCSP-NRQHHLVLTYGHPSPLSRV-NFRDCPHFLEANAYLTKTGRKPVDWQ 311
|
|
| PHA03204 |
PHA03204 |
uracil DNA glycosylase; Provisional |
86-300 |
5.91e-59 |
|
uracil DNA glycosylase; Provisional
Pssm-ID: 165471 Cd Length: 322 Bit Score: 191.33 E-value: 5.91e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61557031 86 ESWKQQLCGEFGKPYFVKLMGFVAEERKHHKVYPPPEQVFTWTQMCDIRDVKVVILGQDPYHGPNQAHGLCFSVQRPVPP 165
Cdd:PHA03204 104 CRWKEILLPELCCPTGSKILAEYERRARYEEVYPPKSDIFAWTRYCAPDHVKVVIVGQDPYANPGQAHGLAFSVKPGSPI 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61557031 166 PPSLENIFKELSTDIDGFVHPGHGDLSGWARQGVLLLNAVLTVRAHQANSHKERGWEQFTDAVVSWLNQNLNGLVFLLWG 245
Cdd:PHA03204 184 PPSLKNILAAVKACYPSIELGSHGCLEDWAKRGVLLLNSVLTVKRGDPGSHHSVGWQILVRNVLRRLSQSTRGIVFMLWG 263
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 61557031 246 SYAQKKGSAIDRK-RHHVLQTAHPSPLSvYRGFFGCRHFSKANELLQRSGKKPISW 300
Cdd:PHA03204 264 AQAQTMYFQTDNDdRHLVLKYSHPSPLS-RKPFAHCTHFKDANEFLCKMGKGAIDW 318
|
|
| UDG-F1-like |
cd19371 |
Uracil DNA glycosylase family 1, includes Human uracil DNA glycosylase, Vaccinia virus protein ... |
138-272 |
4.76e-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: 182.53 E-value: 4.76e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61557031 138 VVILGQDPYHGPNQAHGLCFSVQRPVPPPPSLENIFKELSTDIDGFVHPGHGDLSGWARQGVLLLNAVLTVRAHQANSHk 217
Cdd:cd19371 1 VVIIGQDPYPSPGHAGGLAFSVTSEVPPPKSLRNIYKELERDYSSFLPPGNGTLEFWARQGVLLLNAALTCESGKPKSH- 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 61557031 218 ERGWEQFTDAVVSWLNQNLNGLVFLLWGSYAQKKGSAIDRKRHHVLQTAHPSPLS 272
Cdd:cd19371 80 YLLWEPFIKAFIRYISAHNKGLVFLLFGSDAQKLRKKINGRNVHVFKADHPSPAD 134
|
|
| PHA03199 |
PHA03199 |
uracil DNA glycosylase; Provisional |
88-300 |
4.84e-58 |
|
uracil DNA glycosylase; Provisional
Pssm-ID: 165466 Cd Length: 304 Bit Score: 188.68 E-value: 4.84e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61557031 88 WKQQLCGEFGKPYfvkLMGFVAEERKH----HKVYPPPEQVFTWTQMCDIRDVKVVILGQDPYHGPNQAHGLCFSVQRPV 163
Cdd:PHA03199 91 WHDLLRDEFEEPY---AKGIFEEYNQLlnngEEIFPIKGDIFAWTRFCGPEKIRVVIIGQDPYHGAGHAHGLAFSVKRGI 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61557031 164 PPPPSLENIFKELSTDIDGFVHPGHGDLSGWARQGVLLLNAVLTVRAHQANSHKERGWEQFTDAVVSWLNQNLNGLVFLL 243
Cdd:PHA03199 168 PIPPSLKNIFAALMESYPHLPLPTHGCLDNWARQGVLLLNTTLTVKRGTPGSHFYLGWDMLIKRMLKRLCENRTGLVFML 247
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 61557031 244 WGSYAQKKGSAIDRKrHHVLQTAHPSPLSVYRgFFGCRHFSKANELLQRSGKKPISW 300
Cdd:PHA03199 248 WGAHAQKTIQPNPRC-HLVLTHAHPSPLSRSE-FRNCKHFLQANEYFLKKGEPEIDW 302
|
|
| PHA03201 |
PHA03201 |
uracil DNA glycosylase; Provisional |
84-300 |
5.02e-58 |
|
uracil DNA glycosylase; Provisional
Pssm-ID: 165468 Cd Length: 318 Bit Score: 188.95 E-value: 5.02e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61557031 84 LGESWKQQLCGEFGKPYFVKLMGFVAEERKHHKVYPPPEQVFTWTQMCDIRDVKVVILGQDPYHGPNQAHGLCFSVQRPV 163
Cdd:PHA03201 102 VGDAWRPLLEPELANPLTARLMAEYERRCRTEEVLPPREDVFSWTRYCTPDEVRVVIIGQDPYHQPGQAHGLAFSVRPGT 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61557031 164 PPPPSLENIFKELSTDIDGFVHPGHGDLSGWARQGVLLLNAVLTVRAHQANSHKERGWEQFTDAVVSWLNQNLNGLVFLL 243
Cdd:PHA03201 182 PAPPSLRNILAAVRNCCPDARMSGHGCLEKWARGGVLLLNTTLTVRRGEPASHAKIGWDRFVGSVVRRLAASRPGLVFML 261
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 61557031 244 WGSYAQkkgSAI--DRKRHHVLQTAHPSPLSvyRGFFG-CRHFSKANELLQRSGKKPISW 300
Cdd:PHA03201 262 WGAHAQ---NAIrpDPRVHRVLTYSHPSPLS--KVPFGsCRHFCLANQYLRERSLAPIDW 316
|
|
| UDG |
smart00986 |
Uracil DNA glycosylase superfamily; |
134-290 |
1.63e-30 |
|
Uracil DNA glycosylase superfamily;
Pssm-ID: 214956 Cd Length: 156 Bit Score: 112.48 E-value: 1.63e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61557031 134 RDVKVVILGQDPY------HGP-NQAHGLCFSVQRPV----PPPPSLENIFKELSTDidgfvhPGHGDLSGWARQGVLLl 202
Cdd:smart00986 6 PNAKVLIVGQAPGaseedrGGPfVGAAGLLLSVMLGVaglpRLPPYLTNIVKCRPPD------AGNRRPTSWELQGCLL- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61557031 203 nAVLTVRAHQANSHKERGWEQFTDAVVswLNQNLNGLVFLLWGSYAQKKGsaidrKRHHVLQTAHPSPLSvyRGFFGCRH 282
Cdd:smart00986 79 -PWLTVELALARPHLILLLGKFAAQAL--LGLLRRPLVFGLRGRVAQLKG-----KGHRVLPLPHPSPLN--RNFFPAKK 148
|
....*...
gi 61557031 283 FSKANELL 290
Cdd:smart00986 149 FAAWNDLL 156
|
|
| UDG-like |
cd09593 |
uracil-DNA glycosylases (UDG) and related enzymes; Uracil-DNA glycosylases (UDGs) initiate ... |
138-272 |
1.74e-25 |
|
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: 98.23 E-value: 1.74e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61557031 138 VVILGQDPYHGPNQAHGlcfsvqrpVPPPPSLENIFKELSTDIDGFVhpghgdlsgWARQGVLLLNAVLTVRAHQANSHk 217
Cdd:cd09593 1 VLIVGQNPGPHGARAGG--------VPPGPSGNRLWRLLAAAGGTPR---------LFRYGVGLTNTVPRGPPGAAAGS- 62
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 61557031 218 ERGWEQFTDAVVSWLNQNLNGLVFLLWGSYAQKKGSAID-------RKRHHVLQTAHPSPLS 272
Cdd:cd09593 63 EKKELRFCGRWLRKLLELLNPRVVVLLGKKAQEAYLAVLtsskgapGKGTEVLVLPHPSPRN 124
|
|
| UDG |
pfam03167 |
Uracil DNA glycosylase superfamily; |
135-289 |
8.43e-18 |
|
Uracil DNA glycosylase superfamily;
Pssm-ID: 397331 Cd Length: 154 Bit Score: 78.54 E-value: 8.43e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61557031 135 DVKVVILGQDPYHGpNQAHGLCFSVQRPVPPPPSLENIfkELSTDIDgfvhpghgdlsgwARQGVLLLNAVLTVR--AHQ 212
Cdd:pfam03167 7 NAKVLIVGEAPGAD-EDATGLPFVGRAGNLLWKLLNAA--GLTRDLF-------------SPQGVYITNVVKCRPgnRRK 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61557031 213 ANSHKERGWEQFTDAVVSWLNQNlnglVFLLWGSYAQKK-----------GSAIDRKRHHVLQTAHPSPLSVYRgffgCR 281
Cdd:pfam03167 71 PTSHEIDACWPYLEAEIELLRPR----VIVLLGKTAAKAllglkkitklrGKLIDLKGIPVLPTPHPSPLLRNK----LN 142
|
....*...
gi 61557031 282 HFSKANEL 289
Cdd:pfam03167 143 PFLKANAW 150
|
|
| UDG_F1_VAVC_D4-like |
cd19372 |
Uracil DNA glycosylase family 1 subfamily, includes Vaccinia virus protein D4 and similar ... |
115-302 |
1.12e-03 |
|
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: 39.34 E-value: 1.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61557031 115 HKVYPPPEQVFTWTQMcDIRDVKVVILGQDPYhgPNQAHGLCFsvQRPVPPPPSLENIFKELS--TDIDGFvhpGHGDLS 192
Cdd:cd19372 22 DETSPIPENFFKQLKQ-PLRDKRVCICGIDPY--PTDATGVPF--ESPDFSKKTIRAIAEAISrrTGVSLY---KGYNFA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61557031 193 gwARQGVLLLNAVLTVRAHQANSHKERgWEQFTDAVVSWLNQNLNGLVFLLWGSYAQKKgsAIDRKRHHVLQTAHPSPLS 272
Cdd:cd19372 94 --LVEGVLAWNYYLSCREGETKSHAIH-WERISKLLLQHIAKYVSVLYCLGKTDFSNVR--ARLEVPVTVVVGYHPAARD 168
|
170 180 190
....*....|....*....|....*....|
gi 61557031 273 vyRGFFGCRHFSKANELLQRSGKKPISWKE 302
Cdd:cd19372 169 --GQFDKERAFEIVNVLLELNGKPPVNWAQ 196
|
|
| |
