|
Name |
Accession |
Description |
Interval |
E-value |
| Ung |
COG0692 |
Uracil-DNA glycosylase [Replication, recombination and repair]; |
89-303 |
3.96e-139 |
|
Uracil-DNA glycosylase [Replication, recombination and repair];
Pssm-ID: 440456 Cd Length: 221 Bit Score: 391.71 E-value: 3.96e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 101943608 89 ESWKQQLCGEFGKPYFVKLMGFVAEER-NHHKVYPPPEQVFTWTQMCDIRDVKVVILGQDPYHGPNQAHGLCFSVQRPVP 167
Cdd:COG0692 7 PSWKEALAEEFEKPYFQALGAFLKAEYaAGKTIYPPGEDIFRAFNLTPFDDVKVVILGQDPYHGPGQAHGLSFSVPPGVP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 101943608 168 PPPSLENIFKELSTDIdGFVHPGHGDLSGWARQGVLLLNAVLTVRAHQANSHKERGWEQFTDAVVSWLNQNLSGLVFLLW 247
Cdd:COG0692 87 LPPSLRNIYKELEDDL-GIPIPNHGDLTSWAEQGVLLLNTVLTVRAGQAGSHAGKGWETFTDAVIRALNARKEPVVFLLW 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 101943608 248 GSYAQKKGSVIDRKRHHVLQTAHPSPLSVHRGFLGCRHFSKANELLQKSGKKPINW 303
Cdd:COG0692 166 GAYAQKKAALIDASKHLVLESPHPSPLSAHRGFFGSKPFSKANAYLEEQGKTPIDW 221
|
|
| ung |
TIGR00628 |
uracil-DNA glycosylase; All proteins in this family for which functions are known are ... |
89-298 |
6.66e-137 |
|
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: 385.80 E-value: 6.66e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 101943608 89 ESWKQQLCGEFGKPYFVKLMGFVAEERNHHKVYPPPEQVFTWTQMCDIRDVKVVILGQDPYHGPNQAHGLCFSVQRPVPP 168
Cdd:TIGR00628 2 PSWRAFLQPEFKKPYFQELLAFYKRERAQETVYPPKEDVFAWTRLCPPEDVKVVILGQDPYHGPGQAHGLAFSVKRGVPI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 101943608 169 PPSLENIFKELSTDIDGFVHPGHGDLSGWARQGVLLLNAVLTVRAHQANSHKERGWEQFTDAVVSWLNQNLSGLVFLLWG 248
Cdd:TIGR00628 82 PPSLKNIFKELEADYPDFPPPKHGCLEAWARQGVLLLNTVLTVRRGQPGSHSGLGWERFTDAVISRLSERLDGLVFMLWG 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 101943608 249 SYAQKKGSVIDRKRHHVLQTAHPSPLSVHRGFLGCRHFSKANELLQKSGK 298
Cdd:TIGR00628 162 AHAQKKKSLIDAKKHLVLKSPHPSPLSARRGFFGCRHFSKANEYLEKHGK 211
|
|
| PRK05254 |
PRK05254 |
uracil-DNA glycosylase; Provisional |
89-303 |
4.02e-133 |
|
uracil-DNA glycosylase; Provisional
Pssm-ID: 235376 Cd Length: 224 Bit Score: 376.80 E-value: 4.02e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 101943608 89 ESWKQQLCGEFGKPYFVKLMGFVAEER-NHHKVYPPPEQVFTWTQMCDIRDVKVVILGQDPYHGPNQAHGLCFSVQRPVP 167
Cdd:PRK05254 8 PSWKEVLKPEFKKPYFQELLEFLRAERaAGKTIYPPGEDIFRAFNLTPFDDVKVVILGQDPYHGPGQAHGLSFSVPPGVP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 101943608 168 PPPSLENIFKELSTDIdGFVHPGHGDLSGWARQGVLLLNAVLTVRAHQANSHKERGWEQFTDAVVSWLNQNLSGLVFLLW 247
Cdd:PRK05254 88 IPPSLRNIFKELEDDL-GFPIPNHGDLTSWAEQGVLLLNTVLTVEAGQANSHAGKGWETFTDAVIKALNERREPVVFILW 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 101943608 248 GSYAQKKGSVIDRKRHHVLQTAHPSPLSVHRGFLGCRHFSKANELLQKSGKKPINW 303
Cdd:PRK05254 167 GSHAQKKKALIDNSKHLILESPHPSPLSAHRGFFGSKHFSKANALLKQHGKTPIDW 222
|
|
| UDG-F1-like |
cd10027 |
Uracil DNA glycosylase family 1 subfamily, includes Human uracil DNA glycosylase and similar ... |
103-303 |
1.41e-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: 374.48 E-value: 1.41e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 101943608 103 YFVKLMGFVAEERNHHKVYPPPEQVFTWTQMCDIRDVKVVILGQDPYHGPNQAHGLCFSVQRPVPPPPSLENIFKELSTD 182
Cdd:cd10027 1 YFKKLEAFLEEEYKKKTIYPPKEDIFRAFELTPLDDVKVVILGQDPYHGPGQAHGLAFSVPPGVKIPPSLRNIFKELKSD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 101943608 183 IDGFvHPGHGDLSGWARQGVLLLNAVLTVRAHQANSHKERGWEQFTDAVVSWLNQNLSGLVFLLWGSYAQKKGSVIDRKR 262
Cdd:cd10027 81 LGIF-PPKHGDLSSWAKQGVLLLNTVLTVEAGKPGSHKNIGWETFTDAVIKALSEKNENVVFLLWGNHAQKKKKLIDKKK 159
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 101943608 263 HHVLQTAHPSPLSVHRGFLGCRHFSKANELLQKSGKKPINW 303
Cdd:cd10027 160 HLVLESSHPSPLSAYRGFFGSKHFSKANEYLKKHGKKPIDW 200
|
|
| UDG |
smart00986 |
Uracil DNA glycosylase superfamily; |
137-293 |
2.10e-31 |
|
Uracil DNA glycosylase superfamily;
Pssm-ID: 214956 Cd Length: 156 Bit Score: 114.79 E-value: 2.10e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 101943608 137 RDVKVVILGQDPY------HGP-NQAHGLCFSVQRPV----PPPPSLENIFKELSTDidgfvhPGHGDLSGWARQGVLLl 205
Cdd:smart00986 6 PNAKVLIVGQAPGaseedrGGPfVGAAGLLLSVMLGVaglpRLPPYLTNIVKCRPPD------AGNRRPTSWELQGCLL- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 101943608 206 nAVLTVRAHQANSHKERGWEQFTDAVVswLNQNLSGLVFLLWGSYAQKKGsvidrKRHHVLQTAHPSPLSvhRGFLGCRH 285
Cdd:smart00986 79 -PWLTVELALARPHLILLLGKFAAQAL--LGLLRRPLVFGLRGRVAQLKG-----KGHRVLPLPHPSPLN--RNFFPAKK 148
|
....*...
gi 101943608 286 FSKANELL 293
Cdd:smart00986 149 FAAWNDLL 156
|
|
| UDG |
pfam03167 |
Uracil DNA glycosylase superfamily; |
138-292 |
1.12e-19 |
|
Uracil DNA glycosylase superfamily;
Pssm-ID: 397331 Cd Length: 154 Bit Score: 83.55 E-value: 1.12e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 101943608 138 DVKVVILGQDPYHGpNQAHGLCFSVQRPVPPPPSLENIfkELSTDIDgfvhpghgdlsgwARQGVLLLNAVLTVR--AHQ 215
Cdd:pfam03167 7 NAKVLIVGEAPGAD-EDATGLPFVGRAGNLLWKLLNAA--GLTRDLF-------------SPQGVYITNVVKCRPgnRRK 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 101943608 216 ANSHK-ERGWEqFTDAVVSWLNQNlsglVFLLWGSYAQKK-----------GSVIDRKRHHVLQTAHPSPLSVHRgflgC 283
Cdd:pfam03167 71 PTSHEiDACWP-YLEAEIELLRPR----VIVLLGKTAAKAllglkkitklrGKLIDLKGIPVLPTPHPSPLLRNK----L 141
|
....*....
gi 101943608 284 RHFSKANEL 292
Cdd:pfam03167 142 NPFLKANAW 150
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Ung |
COG0692 |
Uracil-DNA glycosylase [Replication, recombination and repair]; |
89-303 |
3.96e-139 |
|
Uracil-DNA glycosylase [Replication, recombination and repair];
Pssm-ID: 440456 Cd Length: 221 Bit Score: 391.71 E-value: 3.96e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 101943608 89 ESWKQQLCGEFGKPYFVKLMGFVAEER-NHHKVYPPPEQVFTWTQMCDIRDVKVVILGQDPYHGPNQAHGLCFSVQRPVP 167
Cdd:COG0692 7 PSWKEALAEEFEKPYFQALGAFLKAEYaAGKTIYPPGEDIFRAFNLTPFDDVKVVILGQDPYHGPGQAHGLSFSVPPGVP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 101943608 168 PPPSLENIFKELSTDIdGFVHPGHGDLSGWARQGVLLLNAVLTVRAHQANSHKERGWEQFTDAVVSWLNQNLSGLVFLLW 247
Cdd:COG0692 87 LPPSLRNIYKELEDDL-GIPIPNHGDLTSWAEQGVLLLNTVLTVRAGQAGSHAGKGWETFTDAVIRALNARKEPVVFLLW 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 101943608 248 GSYAQKKGSVIDRKRHHVLQTAHPSPLSVHRGFLGCRHFSKANELLQKSGKKPINW 303
Cdd:COG0692 166 GAYAQKKAALIDASKHLVLESPHPSPLSAHRGFFGSKPFSKANAYLEEQGKTPIDW 221
|
|
| ung |
TIGR00628 |
uracil-DNA glycosylase; All proteins in this family for which functions are known are ... |
89-298 |
6.66e-137 |
|
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: 385.80 E-value: 6.66e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 101943608 89 ESWKQQLCGEFGKPYFVKLMGFVAEERNHHKVYPPPEQVFTWTQMCDIRDVKVVILGQDPYHGPNQAHGLCFSVQRPVPP 168
Cdd:TIGR00628 2 PSWRAFLQPEFKKPYFQELLAFYKRERAQETVYPPKEDVFAWTRLCPPEDVKVVILGQDPYHGPGQAHGLAFSVKRGVPI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 101943608 169 PPSLENIFKELSTDIDGFVHPGHGDLSGWARQGVLLLNAVLTVRAHQANSHKERGWEQFTDAVVSWLNQNLSGLVFLLWG 248
Cdd:TIGR00628 82 PPSLKNIFKELEADYPDFPPPKHGCLEAWARQGVLLLNTVLTVRRGQPGSHSGLGWERFTDAVISRLSERLDGLVFMLWG 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 101943608 249 SYAQKKGSVIDRKRHHVLQTAHPSPLSVHRGFLGCRHFSKANELLQKSGK 298
Cdd:TIGR00628 162 AHAQKKKSLIDAKKHLVLKSPHPSPLSARRGFFGCRHFSKANEYLEKHGK 211
|
|
| PRK05254 |
PRK05254 |
uracil-DNA glycosylase; Provisional |
89-303 |
4.02e-133 |
|
uracil-DNA glycosylase; Provisional
Pssm-ID: 235376 Cd Length: 224 Bit Score: 376.80 E-value: 4.02e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 101943608 89 ESWKQQLCGEFGKPYFVKLMGFVAEER-NHHKVYPPPEQVFTWTQMCDIRDVKVVILGQDPYHGPNQAHGLCFSVQRPVP 167
Cdd:PRK05254 8 PSWKEVLKPEFKKPYFQELLEFLRAERaAGKTIYPPGEDIFRAFNLTPFDDVKVVILGQDPYHGPGQAHGLSFSVPPGVP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 101943608 168 PPPSLENIFKELSTDIdGFVHPGHGDLSGWARQGVLLLNAVLTVRAHQANSHKERGWEQFTDAVVSWLNQNLSGLVFLLW 247
Cdd:PRK05254 88 IPPSLRNIFKELEDDL-GFPIPNHGDLTSWAEQGVLLLNTVLTVEAGQANSHAGKGWETFTDAVIKALNERREPVVFILW 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 101943608 248 GSYAQKKGSVIDRKRHHVLQTAHPSPLSVHRGFLGCRHFSKANELLQKSGKKPINW 303
Cdd:PRK05254 167 GSHAQKKKALIDNSKHLILESPHPSPLSAHRGFFGSKHFSKANALLKQHGKTPIDW 222
|
|
| UDG-F1-like |
cd10027 |
Uracil DNA glycosylase family 1 subfamily, includes Human uracil DNA glycosylase and similar ... |
103-303 |
1.41e-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: 374.48 E-value: 1.41e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 101943608 103 YFVKLMGFVAEERNHHKVYPPPEQVFTWTQMCDIRDVKVVILGQDPYHGPNQAHGLCFSVQRPVPPPPSLENIFKELSTD 182
Cdd:cd10027 1 YFKKLEAFLEEEYKKKTIYPPKEDIFRAFELTPLDDVKVVILGQDPYHGPGQAHGLAFSVPPGVKIPPSLRNIFKELKSD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 101943608 183 IDGFvHPGHGDLSGWARQGVLLLNAVLTVRAHQANSHKERGWEQFTDAVVSWLNQNLSGLVFLLWGSYAQKKGSVIDRKR 262
Cdd:cd10027 81 LGIF-PPKHGDLSSWAKQGVLLLNTVLTVEAGKPGSHKNIGWETFTDAVIKALSEKNENVVFLLWGNHAQKKKKLIDKKK 159
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 101943608 263 HHVLQTAHPSPLSVHRGFLGCRHFSKANELLQKSGKKPINW 303
Cdd:cd10027 160 HLVLESSHPSPLSAYRGFFGSKHFSKANEYLKKHGKKPIDW 200
|
|
| PHA03347 |
PHA03347 |
uracil DNA glycosylase; Provisional |
99-303 |
3.07e-79 |
|
uracil DNA glycosylase; Provisional
Pssm-ID: 177588 Cd Length: 252 Bit Score: 241.11 E-value: 3.07e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 101943608 99 FGKPYFVKLMGFVAEERNHHKVYPPPEQVFTWTQMCDIRDVKVVILGQDPYHGpNQAHGLCFSVQRPVPPPPSLENIFKE 178
Cdd:PHA03347 39 FLKQKLLALLNCVRELRKQTVIYPPEDRIMAWSYLCDPEDIKVVILGQDPYHG-GQANGLAFSVAYGFPVPPSLRNIFAE 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 101943608 179 LSTDIDGFVHPGHGDLSGWARQGVLLLNAVLTVRAHQANSHKERGWEQFTDAVVSWLNQNLSGLVFLLWGSYAQKKGSVI 258
Cdd:PHA03347 118 LHRSVPDFSPPDHGCLDAWARQGVLLLNTILTVEKGKPGSHSDLGWAWFTDYIISSLSEKLKACVFMLWGSKAIDKASLI 197
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 101943608 259 DRKRHHVLQTAHPSPLSVHRG-------FLGCRHFSKANELLQKSGKKPINW 303
Cdd:PHA03347 198 NSQKHLVLKAQHPSPLAANSTrsstwpkFLGCNHFVLANKYLTQHGKGPIDW 249
|
|
| PHA03200 |
PHA03200 |
uracil DNA glycosylase; Provisional |
111-306 |
1.21e-76 |
|
uracil DNA glycosylase; Provisional
Pssm-ID: 165467 Cd Length: 255 Bit Score: 234.62 E-value: 1.21e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 101943608 111 VAEERNHHKVYPPPEQVFTWTQMCDIRDVKVVILGQDPYHGpNQAHGLCFSVQRPVPPPPSLENIFKELSTDIDGFVHPG 190
Cdd:PHA03200 57 VDRDRQRLTVYPPPEDVHRWSRLCSPEDVKVVIVGQDPYHD-GSACGLAFGTVRGRSAPPSLKNVFRELERTVPNFSRPD 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 101943608 191 HGDLSGWARQGVLLLNAVLTVRAHQANSHKERGWEQFTDAVVSWLNQNLSGLVFLLWGSYAQKKGSVIDRKRHHVLQTAH 270
Cdd:PHA03200 136 SGCLDSWCRQGVLLLNTVFTVVHGQPGSHEALGWQTLSDRVISRLSEKREHLVFMLWGAQAQKLEYLIDSRKHLILKSAH 215
|
170 180 190
....*....|....*....|....*....|....*...
gi 101943608 271 PSP--LSVHRGFLGCRHFSKANELLQKSGKKPINWKEL 306
Cdd:PHA03200 216 PSPrvKGARTPFIGNNHFVLANEYLSTHGKRPIDWNIL 253
|
|
| PHA03202 |
PHA03202 |
uracil DNA glycosylase; Provisional |
90-304 |
1.82e-68 |
|
uracil DNA glycosylase; Provisional
Pssm-ID: 165469 Cd Length: 313 Bit Score: 215.71 E-value: 1.82e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 101943608 90 SWKQQLCGEFGKPYFVKLMGFVAEERNHHKVYPPPEQVFTWTQMCDIRDVKVVILGQDPYHGPNQAHGLCFSVQRPVPPP 169
Cdd:PHA03202 99 SWRPILEREMQQPYVRLLLNEYKLRCAREEVFPPKEDIFAWTRFSPPEKVRVVIVGQDPYHAPGQAHGLAFSVRKGVPVP 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 101943608 170 PSLENIFKELSTDIDGFVHPGHGDLSGWARQGVLLLNAVLTVRAHQANSHKERGWEQFTDAVVSWLNQNLSGLVFLLWGS 249
Cdd:PHA03202 179 PSLRNIYSAVQKSYPSFRPPMHGFLEKWAEQGVLLINTTLTVARGKPGSHATLGWHRLVRAVIDRLCTTSQGLVFMLWGA 258
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 101943608 250 YAQKKGSViDRKRHHVLQTAHPSPLSvHRGFLGCRHFSKANELLQKSGKKPINWK 304
Cdd:PHA03202 259 HAQKSCSP-NRQHHLVLTYGHPSPLS-RVNFRDCPHFLEANAYLTKTGRKPVDWQ 311
|
|
| PHA03201 |
PHA03201 |
uracil DNA glycosylase; Provisional |
12-303 |
6.50e-61 |
|
uracil DNA glycosylase; Provisional
Pssm-ID: 165468 Cd Length: 318 Bit Score: 196.27 E-value: 6.50e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 101943608 12 SPTPTGKRTTR-SPE------PVPGSGVAAEIGGdavASPAKKARVEQNEQGSPLSAEQLVRIQRNKAAALLRLAARNVP 84
Cdd:PHA03201 17 PPRPTPPRSPDaSPEetppspPGPGAEPPPGRAA---GPAAPRRRPRGCPAGVTFSSSAPPRPPLGLDDAPAATPPPLDW 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 101943608 85 AGF------GESWKQQLCGEFGKPYFVKLMGFVAEERNHHKVYPPPEQVFTWTQMCDIRDVKVVILGQDPYHGPNQAHGL 158
Cdd:PHA03201 94 TEFrrrflvGDAWRPLLEPELANPLTARLMAEYERRCRTEEVLPPREDVFSWTRYCTPDEVRVVIIGQDPYHQPGQAHGL 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 101943608 159 CFSVQRPVPPPPSLENIFKELSTDIDGFVHPGHGDLSGWARQGVLLLNAVLTVRAHQANSHKERGWEQFTDAVVSWLNQN 238
Cdd:PHA03201 174 AFSVRPGTPAPPSLRNILAAVRNCCPDARMSGHGCLEKWARGGVLLLNTTLTVRRGEPASHAKIGWDRFVGSVVRRLAAS 253
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 101943608 239 LSGLVFLLWGSYAQkkgSVI--DRKRHHVLQTAHPSPLSvHRGFLGCRHFSKANELLQKSGKKPINW 303
Cdd:PHA03201 254 RPGLVFMLWGAHAQ---NAIrpDPRVHRVLTYSHPSPLS-KVPFGSCRHFCLANQYLRERSLAPIDW 316
|
|
| PHA03204 |
PHA03204 |
uracil DNA glycosylase; Provisional |
89-303 |
7.02e-61 |
|
uracil DNA glycosylase; Provisional
Pssm-ID: 165471 Cd Length: 322 Bit Score: 196.33 E-value: 7.02e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 101943608 89 ESWKQQLCGEFGKPYFVKLMGFVAEERNHHKVYPPPEQVFTWTQMCDIRDVKVVILGQDPYHGPNQAHGLCFSVQRPVPP 168
Cdd:PHA03204 104 CRWKEILLPELCCPTGSKILAEYERRARYEEVYPPKSDIFAWTRYCAPDHVKVVIVGQDPYANPGQAHGLAFSVKPGSPI 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 101943608 169 PPSLENIFKELSTDIDGFVHPGHGDLSGWARQGVLLLNAVLTVRAHQANSHKERGWEQFTDAVVSWLNQNLSGLVFLLWG 248
Cdd:PHA03204 184 PPSLKNILAAVKACYPSIELGSHGCLEDWAKRGVLLLNSVLTVKRGDPGSHHSVGWQILVRNVLRRLSQSTRGIVFMLWG 263
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 101943608 249 SYAQKKGSVIDRK-RHHVLQTAHPSPLSvHRGFLGCRHFSKANELLQKSGKKPINW 303
Cdd:PHA03204 264 AQAQTMYFQTDNDdRHLVLKYSHPSPLS-RKPFAHCTHFKDANEFLCKMGKGAIDW 318
|
|
| PHA03199 |
PHA03199 |
uracil DNA glycosylase; Provisional |
91-303 |
4.98e-60 |
|
uracil DNA glycosylase; Provisional
Pssm-ID: 165466 Cd Length: 304 Bit Score: 193.68 E-value: 4.98e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 101943608 91 WKQQLCGEFGKPYfvkLMGFVAEER----NHHKVYPPPEQVFTWTQMCDIRDVKVVILGQDPYHGPNQAHGLCFSVQRPV 166
Cdd:PHA03199 91 WHDLLRDEFEEPY---AKGIFEEYNqllnNGEEIFPIKGDIFAWTRFCGPEKIRVVIIGQDPYHGAGHAHGLAFSVKRGI 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 101943608 167 PPPPSLENIFKELSTDIDGFVHPGHGDLSGWARQGVLLLNAVLTVRAHQANSHKERGWEQFTDAVVSWLNQNLSGLVFLL 246
Cdd:PHA03199 168 PIPPSLKNIFAALMESYPHLPLPTHGCLDNWARQGVLLLNTTLTVKRGTPGSHFYLGWDMLIKRMLKRLCENRTGLVFML 247
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 101943608 247 WGSYAQKKGSVIDRKrHHVLQTAHPSPLSvHRGFLGCRHFSKANELLQKSGKKPINW 303
Cdd:PHA03199 248 WGAHAQKTIQPNPRC-HLVLTHAHPSPLS-RSEFRNCKHFLQANEYFLKKGEPEIDW 302
|
|
| UDG-F1-like |
cd19371 |
Uracil DNA glycosylase family 1, includes Human uracil DNA glycosylase, Vaccinia virus protein ... |
141-275 |
2.87e-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: 183.31 E-value: 2.87e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 101943608 141 VVILGQDPYHGPNQAHGLCFSVQRPVPPPPSLENIFKELSTDIDGFVHPGHGDLSGWARQGVLLLNAVLTVRAHQANSHk 220
Cdd:cd19371 1 VVIIGQDPYPSPGHAGGLAFSVTSEVPPPKSLRNIYKELERDYSSFLPPGNGTLEFWARQGVLLLNAALTCESGKPKSH- 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 101943608 221 ERGWEQFTDAVVSWLNQNLSGLVFLLWGSYAQKKGSVIDRKRHHVLQTAHPSPLS 275
Cdd:cd19371 80 YLLWEPFIKAFIRYISAHNKGLVFLLFGSDAQKLRKKINGRNVHVFKADHPSPAD 134
|
|
| UDG |
smart00986 |
Uracil DNA glycosylase superfamily; |
137-293 |
2.10e-31 |
|
Uracil DNA glycosylase superfamily;
Pssm-ID: 214956 Cd Length: 156 Bit Score: 114.79 E-value: 2.10e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 101943608 137 RDVKVVILGQDPY------HGP-NQAHGLCFSVQRPV----PPPPSLENIFKELSTDidgfvhPGHGDLSGWARQGVLLl 205
Cdd:smart00986 6 PNAKVLIVGQAPGaseedrGGPfVGAAGLLLSVMLGVaglpRLPPYLTNIVKCRPPD------AGNRRPTSWELQGCLL- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 101943608 206 nAVLTVRAHQANSHKERGWEQFTDAVVswLNQNLSGLVFLLWGSYAQKKGsvidrKRHHVLQTAHPSPLSvhRGFLGCRH 285
Cdd:smart00986 79 -PWLTVELALARPHLILLLGKFAAQAL--LGLLRRPLVFGLRGRVAQLKG-----KGHRVLPLPHPSPLN--RNFFPAKK 148
|
....*...
gi 101943608 286 FSKANELL 293
Cdd:smart00986 149 FAAWNDLL 156
|
|
| UDG-like |
cd09593 |
uracil-DNA glycosylases (UDG) and related enzymes; Uracil-DNA glycosylases (UDGs) initiate ... |
141-275 |
2.17e-24 |
|
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: 95.53 E-value: 2.17e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 101943608 141 VVILGQDPYHGPNQAHGlcfsvqrpVPPPPSLENIFKELSTDIDGFVhpghgdlsgWARQGVLLLNAVLTVRAHQANSHk 220
Cdd:cd09593 1 VLIVGQNPGPHGARAGG--------VPPGPSGNRLWRLLAAAGGTPR---------LFRYGVGLTNTVPRGPPGAAAGS- 62
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 101943608 221 ERGWEQFTDAVVSWLNQNLSGLVFLLWGSYAQKKGS-------VIDRKRHHVLQTAHPSPLS 275
Cdd:cd09593 63 EKKELRFCGRWLRKLLELLNPRVVVLLGKKAQEAYLavltsskGAPGKGTEVLVLPHPSPRN 124
|
|
| UDG |
pfam03167 |
Uracil DNA glycosylase superfamily; |
138-292 |
1.12e-19 |
|
Uracil DNA glycosylase superfamily;
Pssm-ID: 397331 Cd Length: 154 Bit Score: 83.55 E-value: 1.12e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 101943608 138 DVKVVILGQDPYHGpNQAHGLCFSVQRPVPPPPSLENIfkELSTDIDgfvhpghgdlsgwARQGVLLLNAVLTVR--AHQ 215
Cdd:pfam03167 7 NAKVLIVGEAPGAD-EDATGLPFVGRAGNLLWKLLNAA--GLTRDLF-------------SPQGVYITNVVKCRPgnRRK 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 101943608 216 ANSHK-ERGWEqFTDAVVSWLNQNlsglVFLLWGSYAQKK-----------GSVIDRKRHHVLQTAHPSPLSVHRgflgC 283
Cdd:pfam03167 71 PTSHEiDACWP-YLEAEIELLRPR----VIVLLGKTAAKAllglkkitklrGKLIDLKGIPVLPTPHPSPLLRNK----L 141
|
....*....
gi 101943608 284 RHFSKANEL 292
Cdd:pfam03167 142 NPFLKANAW 150
|
|
| UDG_F1_VAVC_D4-like |
cd19372 |
Uracil DNA glycosylase family 1 subfamily, includes Vaccinia virus protein D4 and similar ... |
118-305 |
4.81e-05 |
|
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: 43.58 E-value: 4.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 101943608 118 HKVYPPPEQVFTWTQMcDIRDVKVVILGQDPYhgPNQAHGLCFsvQRPVPPPPSLENIFKELS--TDIDGFvhpGHGDLS 195
Cdd:cd19372 22 DETSPIPENFFKQLKQ-PLRDKRVCICGIDPY--PTDATGVPF--ESPDFSKKTIRAIAEAISrrTGVSLY---KGYNFA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 101943608 196 gwARQGVLLLNAVLTVRAHQANSHKERgWEQFTDAVVSWLNQNLSGLVFLLWGSYAQKKgSVIDrKRHHVLQTAHPSplS 275
Cdd:cd19372 94 --LVEGVLAWNYYLSCREGETKSHAIH-WERISKLLLQHIAKYVSVLYCLGKTDFSNVR-ARLE-VPVTVVVGYHPA--A 166
|
170 180 190
....*....|....*....|....*....|
gi 101943608 276 VHRGFLGCRHFSKANELLQKSGKKPINWKE 305
Cdd:cd19372 167 RDGQFDKERAFEIVNVLLELNGKPPVNWAQ 196
|
|
| |
