|
Name |
Accession |
Description |
Interval |
E-value |
| Ung |
COG0692 |
Uracil-DNA glycosylase [Replication, recombination and repair]; |
1-220 |
1.06e-156 |
|
Uracil-DNA glycosylase [Replication, recombination and repair];
Pssm-ID: 440456 Cd Length: 221 Bit Score: 432.93 E-value: 1.06e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556311266 1 MTTPLTWHDVLAEEKQQPYFINTLNTVAAERQSGQTIYPPQKDVFNAFRYTELSDVKVVILGQDPYHGPGQAHGLAFSVR 80
Cdd:COG0692 3 VLLEPSWKEALAEEFEKPYFQALGAFLKAEYAAGKTIYPPGEDIFRAFNLTPFDDVKVVILGQDPYHGPGQAHGLSFSVP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556311266 81 PGVAIPPSLLNMYKELEGTVpGFTRPNHGYLESWARQGVLLLNTVLTVRAGQAHSHASLGWETFTDKVISLINEHREGVV 160
Cdd:COG0692 83 PGVPLPPSLRNIYKELEDDL-GIPIPNHGDLTSWAEQGVLLLNTVLTVRAGQAGSHAGKGWETFTDAVIRALNARKEPVV 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 556311266 161 FLLWGSHAQKKGAIIDRQRHHVLKAPHPSPLSAHRGFFGSNHFVLANEWLEKRGETPIDW 220
Cdd:COG0692 162 FLLWGAYAQKKAALIDASKHLVLESPHPSPLSAHRGFFGSKPFSKANAYLEEQGKTPIDW 221
|
|
| PRK05254 |
PRK05254 |
uracil-DNA glycosylase; Provisional |
1-220 |
1.28e-155 |
|
uracil-DNA glycosylase; Provisional
Pssm-ID: 235376 Cd Length: 224 Bit Score: 430.34 E-value: 1.28e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556311266 1 MTTPLTWHDVLAEEKQQPYFINTLNTVAAERQSGQTIYPPQKDVFNAFRYTELSDVKVVILGQDPYHGPGQAHGLAFSVR 80
Cdd:PRK05254 4 MLLEPSWKEVLKPEFKKPYFQELLEFLRAERAAGKTIYPPGEDIFRAFNLTPFDDVKVVILGQDPYHGPGQAHGLSFSVP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556311266 81 PGVAIPPSLLNMYKELEGTVpGFTRPNHGYLESWARQGVLLLNTVLTVRAGQAHSHASLGWETFTDKVISLINEHREGVV 160
Cdd:PRK05254 84 PGVPIPPSLRNIFKELEDDL-GFPIPNHGDLTSWAEQGVLLLNTVLTVEAGQANSHAGKGWETFTDAVIKALNERREPVV 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 556311266 161 FLLWGSHAQKKGAIIDRQRHHVLKAPHPSPLSAHRGFFGSNHFVLANEWLEKRGETPIDW 220
Cdd:PRK05254 163 FILWGSHAQKKKALIDNSKHLILESPHPSPLSAHRGFFGSKHFSKANALLKQHGKTPIDW 222
|
|
| UDG-F1-like |
cd10027 |
Uracil DNA glycosylase family 1 subfamily, includes Human uracil DNA glycosylase and similar ... |
19-220 |
2.28e-135 |
|
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: 378.33 E-value: 2.28e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556311266 19 YFINTLNTVAAERQSgQTIYPPQKDVFNAFRYTELSDVKVVILGQDPYHGPGQAHGLAFSVRPGVAIPPSLLNMYKELEG 98
Cdd:cd10027 1 YFKKLEAFLEEEYKK-KTIYPPKEDIFRAFELTPLDDVKVVILGQDPYHGPGQAHGLAFSVPPGVKIPPSLRNIFKELKS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556311266 99 TVPGFTrPNHGYLESWARQGVLLLNTVLTVRAGQAHSHASLGWETFTDKVISLINEHREGVVFLLWGSHAQKKGAIIDRQ 178
Cdd:cd10027 80 DLGIFP-PKHGDLSSWAKQGVLLLNTVLTVEAGKPGSHKNIGWETFTDAVIKALSEKNENVVFLLWGNHAQKKKKLIDKK 158
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 556311266 179 RHHVLKAPHPSPLSAHRGFFGSNHFVLANEWLEKRGETPIDW 220
Cdd:cd10027 159 KHLVLESSHPSPLSAYRGFFGSKHFSKANEYLKKHGKKPIDW 200
|
|
| ung |
TIGR00628 |
uracil-DNA glycosylase; All proteins in this family for which functions are known are ... |
7-215 |
4.87e-129 |
|
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: 362.69 E-value: 4.87e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556311266 7 WHDVLAEEKQQPYFINTLNTVAAERQSgQTIYPPQKDVFNAFRYTELSDVKVVILGQDPYHGPGQAHGLAFSVRPGVAIP 86
Cdd:TIGR00628 4 WRAFLQPEFKKPYFQELLAFYKRERAQ-ETVYPPKEDVFAWTRLCPPEDVKVVILGQDPYHGPGQAHGLAFSVKRGVPIP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556311266 87 PSLLNMYKELEGTVPGFTRPNHGYLESWARQGVLLLNTVLTVRAGQAHSHASLGWETFTDKVISLINEHREGVVFLLWGS 166
Cdd:TIGR00628 83 PSLKNIFKELEADYPDFPPPKHGCLEAWARQGVLLLNTVLTVRRGQPGSHSGLGWERFTDAVISRLSERLDGLVFMLWGA 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 556311266 167 HAQKKGAIIDRQRHHVLKAPHPSPLSAHRGFFGSNHFVLANEWLEKRGE 215
Cdd:TIGR00628 163 HAQKKKSLIDAKKHLVLKSPHPSPLSARRGFFGCRHFSKANEYLEKHGK 211
|
|
| UDG |
smart00986 |
Uracil DNA glycosylase superfamily; |
54-210 |
2.28e-35 |
|
Uracil DNA glycosylase superfamily;
Pssm-ID: 214956 Cd Length: 156 Bit Score: 122.88 E-value: 2.28e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556311266 54 SDVKVVILGQDPYHGPGQ-------AHGLAFSVRPGVA----IPPSLLNMYKELEGTvpgftrPNHGYLESWARQGVLLl 122
Cdd:smart00986 6 PNAKVLIVGQAPGASEEDrggpfvgAAGLLLSVMLGVAglprLPPYLTNIVKCRPPD------AGNRRPTSWELQGCLL- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556311266 123 nTVLTVRAGQAHSHASLGWETFTDKVISLINEHRegVVFLLWGSHAQKKGAiidrqRHHVLKAPHPSPLSAHRgfFGSNH 202
Cdd:smart00986 79 -PWLTVELALARPHLILLLGKFAAQALLGLLRRP--LVFGLRGRVAQLKGK-----GHRVLPLPHPSPLNRNF--FPAKK 148
|
....*...
gi 556311266 203 FVLANEWL 210
Cdd:smart00986 149 FAAWNDLL 156
|
|
| UDG |
pfam03167 |
Uracil DNA glycosylase superfamily; |
55-211 |
8.45e-25 |
|
Uracil DNA glycosylase superfamily;
Pssm-ID: 397331 Cd Length: 154 Bit Score: 95.49 E-value: 8.45e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556311266 55 DVKVVILGQDPYHGpGQAHGLAFSVRPGvAIPPSLLNMYkelegtvpGFTRPNHgyleswARQGVLLLNTVLTVR--AGQ 132
Cdd:pfam03167 7 NAKVLIVGEAPGAD-EDATGLPFVGRAG-NLLWKLLNAA--------GLTRDLF------SPQGVYITNVVKCRPgnRRK 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556311266 133 AHSHA-SLGWEtFTDKVISLINEHregvVFLLWGSHAQKK-----------GAIIDRQRHHVLKAPHPSPLSAHRgffgS 200
Cdd:pfam03167 71 PTSHEiDACWP-YLEAEIELLRPR----VIVLLGKTAAKAllglkkitklrGKLIDLKGIPVLPTPHPSPLLRNK----L 141
|
170
....*....|.
gi 556311266 201 NHFVLANEWLE 211
Cdd:pfam03167 142 NPFLKANAWED 152
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| Ung |
COG0692 |
Uracil-DNA glycosylase [Replication, recombination and repair]; |
1-220 |
1.06e-156 |
|
Uracil-DNA glycosylase [Replication, recombination and repair];
Pssm-ID: 440456 Cd Length: 221 Bit Score: 432.93 E-value: 1.06e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556311266 1 MTTPLTWHDVLAEEKQQPYFINTLNTVAAERQSGQTIYPPQKDVFNAFRYTELSDVKVVILGQDPYHGPGQAHGLAFSVR 80
Cdd:COG0692 3 VLLEPSWKEALAEEFEKPYFQALGAFLKAEYAAGKTIYPPGEDIFRAFNLTPFDDVKVVILGQDPYHGPGQAHGLSFSVP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556311266 81 PGVAIPPSLLNMYKELEGTVpGFTRPNHGYLESWARQGVLLLNTVLTVRAGQAHSHASLGWETFTDKVISLINEHREGVV 160
Cdd:COG0692 83 PGVPLPPSLRNIYKELEDDL-GIPIPNHGDLTSWAEQGVLLLNTVLTVRAGQAGSHAGKGWETFTDAVIRALNARKEPVV 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 556311266 161 FLLWGSHAQKKGAIIDRQRHHVLKAPHPSPLSAHRGFFGSNHFVLANEWLEKRGETPIDW 220
Cdd:COG0692 162 FLLWGAYAQKKAALIDASKHLVLESPHPSPLSAHRGFFGSKPFSKANAYLEEQGKTPIDW 221
|
|
| PRK05254 |
PRK05254 |
uracil-DNA glycosylase; Provisional |
1-220 |
1.28e-155 |
|
uracil-DNA glycosylase; Provisional
Pssm-ID: 235376 Cd Length: 224 Bit Score: 430.34 E-value: 1.28e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556311266 1 MTTPLTWHDVLAEEKQQPYFINTLNTVAAERQSGQTIYPPQKDVFNAFRYTELSDVKVVILGQDPYHGPGQAHGLAFSVR 80
Cdd:PRK05254 4 MLLEPSWKEVLKPEFKKPYFQELLEFLRAERAAGKTIYPPGEDIFRAFNLTPFDDVKVVILGQDPYHGPGQAHGLSFSVP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556311266 81 PGVAIPPSLLNMYKELEGTVpGFTRPNHGYLESWARQGVLLLNTVLTVRAGQAHSHASLGWETFTDKVISLINEHREGVV 160
Cdd:PRK05254 84 PGVPIPPSLRNIFKELEDDL-GFPIPNHGDLTSWAEQGVLLLNTVLTVEAGQANSHAGKGWETFTDAVIKALNERREPVV 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 556311266 161 FLLWGSHAQKKGAIIDRQRHHVLKAPHPSPLSAHRGFFGSNHFVLANEWLEKRGETPIDW 220
Cdd:PRK05254 163 FILWGSHAQKKKALIDNSKHLILESPHPSPLSAHRGFFGSKHFSKANALLKQHGKTPIDW 222
|
|
| UDG-F1-like |
cd10027 |
Uracil DNA glycosylase family 1 subfamily, includes Human uracil DNA glycosylase and similar ... |
19-220 |
2.28e-135 |
|
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: 378.33 E-value: 2.28e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556311266 19 YFINTLNTVAAERQSgQTIYPPQKDVFNAFRYTELSDVKVVILGQDPYHGPGQAHGLAFSVRPGVAIPPSLLNMYKELEG 98
Cdd:cd10027 1 YFKKLEAFLEEEYKK-KTIYPPKEDIFRAFELTPLDDVKVVILGQDPYHGPGQAHGLAFSVPPGVKIPPSLRNIFKELKS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556311266 99 TVPGFTrPNHGYLESWARQGVLLLNTVLTVRAGQAHSHASLGWETFTDKVISLINEHREGVVFLLWGSHAQKKGAIIDRQ 178
Cdd:cd10027 80 DLGIFP-PKHGDLSSWAKQGVLLLNTVLTVEAGKPGSHKNIGWETFTDAVIKALSEKNENVVFLLWGNHAQKKKKLIDKK 158
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 556311266 179 RHHVLKAPHPSPLSAHRGFFGSNHFVLANEWLEKRGETPIDW 220
Cdd:cd10027 159 KHLVLESSHPSPLSAYRGFFGSKHFSKANEYLKKHGKKPIDW 200
|
|
| ung |
TIGR00628 |
uracil-DNA glycosylase; All proteins in this family for which functions are known are ... |
7-215 |
4.87e-129 |
|
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: 362.69 E-value: 4.87e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556311266 7 WHDVLAEEKQQPYFINTLNTVAAERQSgQTIYPPQKDVFNAFRYTELSDVKVVILGQDPYHGPGQAHGLAFSVRPGVAIP 86
Cdd:TIGR00628 4 WRAFLQPEFKKPYFQELLAFYKRERAQ-ETVYPPKEDVFAWTRLCPPEDVKVVILGQDPYHGPGQAHGLAFSVKRGVPIP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556311266 87 PSLLNMYKELEGTVPGFTRPNHGYLESWARQGVLLLNTVLTVRAGQAHSHASLGWETFTDKVISLINEHREGVVFLLWGS 166
Cdd:TIGR00628 83 PSLKNIFKELEADYPDFPPPKHGCLEAWARQGVLLLNTVLTVRRGQPGSHSGLGWERFTDAVISRLSERLDGLVFMLWGA 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 556311266 167 HAQKKGAIIDRQRHHVLKAPHPSPLSAHRGFFGSNHFVLANEWLEKRGE 215
Cdd:TIGR00628 163 HAQKKKSLIDAKKHLVLKSPHPSPLSARRGFFGCRHFSKANEYLEKHGK 211
|
|
| PHA03347 |
PHA03347 |
uracil DNA glycosylase; Provisional |
22-220 |
2.42e-91 |
|
uracil DNA glycosylase; Provisional
Pssm-ID: 177588 Cd Length: 252 Bit Score: 268.84 E-value: 2.42e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556311266 22 NTLNTVAAERQSgQTIYPPQKDVFNAFRYTELSDVKVVILGQDPYHGpGQAHGLAFSVRPGVAIPPSLLNMYKELEGTVP 101
Cdd:PHA03347 46 ALLNCVRELRKQ-TVIYPPEDRIMAWSYLCDPEDIKVVILGQDPYHG-GQANGLAFSVAYGFPVPPSLRNIFAELHRSVP 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556311266 102 GFTRPNHGYLESWARQGVLLLNTVLTVRAGQAHSHASLGWETFTDKVISLINEHREGVVFLLWGSHAQKKGAIIDRQRHH 181
Cdd:PHA03347 124 DFSPPDHGCLDAWARQGVLLLNTILTVEKGKPGSHSDLGWAWFTDYIISSLSEKLKACVFMLWGSKAIDKASLINSQKHL 203
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 556311266 182 VLKAPHPSPLSAHRG-------FFGSNHFVLANEWLEKRGETPIDW 220
Cdd:PHA03347 204 VLKAQHPSPLAANSTrsstwpkFLGCNHFVLANKYLTQHGKGPIDW 249
|
|
| PHA03200 |
PHA03200 |
uracil DNA glycosylase; Provisional |
22-220 |
1.25e-83 |
|
uracil DNA glycosylase; Provisional
Pssm-ID: 165467 Cd Length: 255 Bit Score: 249.26 E-value: 1.25e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556311266 22 NTLNTVAAERQSGqTIYPPQKDVFNAFRYTELSDVKVVILGQDPYHGpGQAHGLAFSVRPGVAIPPSLLNMYKELEGTVP 101
Cdd:PHA03200 52 RIVDAVDRDRQRL-TVYPPPEDVHRWSRLCSPEDVKVVIVGQDPYHD-GSACGLAFGTVRGRSAPPSLKNVFRELERTVP 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556311266 102 GFTRPNHGYLESWARQGVLLLNTVLTVRAGQAHSHASLGWETFTDKVISLINEHREGVVFLLWGSHAQKKGAIIDRQRHH 181
Cdd:PHA03200 130 NFSRPDSGCLDSWCRQGVLLLNTVFTVVHGQPGSHEALGWQTLSDRVISRLSEKREHLVFMLWGAQAQKLEYLIDSRKHL 209
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 556311266 182 VLKAPHPSP--LSAHRGFFGSNHFVLANEWLEKRGETPIDW 220
Cdd:PHA03200 210 ILKSAHPSPrvKGARTPFIGNNHFVLANEYLSTHGKRPIDW 250
|
|
| PHA03202 |
PHA03202 |
uracil DNA glycosylase; Provisional |
6-221 |
1.91e-77 |
|
uracil DNA glycosylase; Provisional
Pssm-ID: 165469 Cd Length: 313 Bit Score: 235.75 E-value: 1.91e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556311266 6 TWHDVLAEEKQQPYFINTLNTVAAeRQSGQTIYPPQKDVFNAFRYTELSDVKVVILGQDPYHGPGQAHGLAFSVRPGVAI 85
Cdd:PHA03202 99 SWRPILEREMQQPYVRLLLNEYKL-RCAREEVFPPKEDIFAWTRFSPPEKVRVVIVGQDPYHAPGQAHGLAFSVRKGVPV 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556311266 86 PPSLLNMYKELEGTVPGFTRPNHGYLESWARQGVLLLNTVLTVRAGQAHSHASLGWETFTDKVISLINEHREGVVFLLWG 165
Cdd:PHA03202 178 PPSLRNIYSAVQKSYPSFRPPMHGFLEKWAEQGVLLINTTLTVARGKPGSHATLGWHRLVRAVIDRLCTTSQGLVFMLWG 257
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 556311266 166 SHAQKKGAiIDRQRHHVLKAPHPSPLSaHRGFFGSNHFVLANEWLEKRGETPIDWM 221
Cdd:PHA03202 258 AHAQKSCS-PNRQHHLVLTYGHPSPLS-RVNFRDCPHFLEANAYLTKTGRKPVDWQ 311
|
|
| PHA03199 |
PHA03199 |
uracil DNA glycosylase; Provisional |
7-220 |
1.86e-69 |
|
uracil DNA glycosylase; Provisional
Pssm-ID: 165466 Cd Length: 304 Bit Score: 214.87 E-value: 1.86e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556311266 7 WHDVLAEEKQQPYFINTLNTVAAERQSGQTIYPPQKDVFNAFRYTELSDVKVVILGQDPYHGPGQAHGLAFSVRPGVAIP 86
Cdd:PHA03199 91 WHDLLRDEFEEPYAKGIFEEYNQLLNNGEEIFPIKGDIFAWTRFCGPEKIRVVIIGQDPYHGAGHAHGLAFSVKRGIPIP 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556311266 87 PSLLNMYKELEGTVPGFTRPNHGYLESWARQGVLLLNTVLTVRAGQAHSHASLGWETFTDKVISLINEHREGVVFLLWGS 166
Cdd:PHA03199 171 PSLKNIFAALMESYPHLPLPTHGCLDNWARQGVLLLNTTLTVKRGTPGSHFYLGWDMLIKRMLKRLCENRTGLVFMLWGA 250
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 556311266 167 HAQKKGAIIDRQrHHVLKAPHPSPLSaHRGFFGSNHFVLANEWLEKRGETPIDW 220
Cdd:PHA03199 251 HAQKTIQPNPRC-HLVLTHAHPSPLS-RSEFRNCKHFLQANEYFLKKGEPEIDW 302
|
|
| PHA03201 |
PHA03201 |
uracil DNA glycosylase; Provisional |
31-220 |
2.16e-68 |
|
uracil DNA glycosylase; Provisional
Pssm-ID: 165468 Cd Length: 318 Bit Score: 212.83 E-value: 2.16e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556311266 31 RQSGQTIYPPQKDVFNAFRYTELSDVKVVILGQDPYHGPGQAHGLAFSVRPGVAIPPSLLNMYKELEGTVPGFTRPNHGY 110
Cdd:PHA03201 129 RCRTEEVLPPREDVFSWTRYCTPDEVRVVIIGQDPYHQPGQAHGLAFSVRPGTPAPPSLRNILAAVRNCCPDARMSGHGC 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556311266 111 LESWARQGVLLLNTVLTVRAGQAHSHASLGWETFTDKVISLINEHREGVVFLLWGSHAQKkgAI-IDRQRHHVLKAPHPS 189
Cdd:PHA03201 209 LEKWARGGVLLLNTTLTVRRGEPASHAKIGWDRFVGSVVRRLAASRPGLVFMLWGAHAQN--AIrPDPRVHRVLTYSHPS 286
|
170 180 190
....*....|....*....|....*....|..
gi 556311266 190 PLSahRGFFGS-NHFVLANEWLEKRGETPIDW 220
Cdd:PHA03201 287 PLS--KVPFGScRHFCLANQYLRERSLAPIDW 316
|
|
| PHA03204 |
PHA03204 |
uracil DNA glycosylase; Provisional |
7-220 |
2.52e-64 |
|
uracil DNA glycosylase; Provisional
Pssm-ID: 165471 Cd Length: 322 Bit Score: 202.50 E-value: 2.52e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556311266 7 WHDVLAEEKQQPyfinTLNTVAAE---RQSGQTIYPPQKDVFNAFRYTELSDVKVVILGQDPYHGPGQAHGLAFSVRPGV 83
Cdd:PHA03204 106 WKEILLPELCCP----TGSKILAEyerRARYEEVYPPKSDIFAWTRYCAPDHVKVVIVGQDPYANPGQAHGLAFSVKPGS 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556311266 84 AIPPSLLNMYKELEGTVPGFTRPNHGYLESWARQGVLLLNTVLTVRAGQAHSHASLGWETFTDKVISLINEHREGVVFLL 163
Cdd:PHA03204 182 PIPPSLKNILAAVKACYPSIELGSHGCLEDWAKRGVLLLNSVLTVKRGDPGSHHSVGWQILVRNVLRRLSQSTRGIVFML 261
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 556311266 164 WGSHAQKKGAIIDRQ-RHHVLKAPHPSPLSaHRGFFGSNHFVLANEWLEKRGETPIDW 220
Cdd:PHA03204 262 WGAQAQTMYFQTDNDdRHLVLKYSHPSPLS-RKPFAHCTHFKDANEFLCKMGKGAIDW 318
|
|
| UDG-F1-like |
cd19371 |
Uracil DNA glycosylase family 1, includes Human uracil DNA glycosylase, Vaccinia virus protein ... |
58-192 |
6.85e-60 |
|
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: 184.85 E-value: 6.85e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556311266 58 VVILGQDPYHGPGQAHGLAFSVRPGVAIPPSLLNMYKELEGTVPGFTRPNHGYLESWARQGVLLLNTVLTVRAGQAHSHa 137
Cdd:cd19371 1 VVIIGQDPYPSPGHAGGLAFSVTSEVPPPKSLRNIYKELERDYSSFLPPGNGTLEFWARQGVLLLNAALTCESGKPKSH- 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 556311266 138 SLGWETFTDKVISLINEHREGVVFLLWGSHAQKKGAIIDRQRHHVLKAPHPSPLS 192
Cdd:cd19371 80 YLLWEPFIKAFIRYISAHNKGLVFLLFGSDAQKLRKKINGRNVHVFKADHPSPAD 134
|
|
| UDG |
smart00986 |
Uracil DNA glycosylase superfamily; |
54-210 |
2.28e-35 |
|
Uracil DNA glycosylase superfamily;
Pssm-ID: 214956 Cd Length: 156 Bit Score: 122.88 E-value: 2.28e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556311266 54 SDVKVVILGQDPYHGPGQ-------AHGLAFSVRPGVA----IPPSLLNMYKELEGTvpgftrPNHGYLESWARQGVLLl 122
Cdd:smart00986 6 PNAKVLIVGQAPGASEEDrggpfvgAAGLLLSVMLGVAglprLPPYLTNIVKCRPPD------AGNRRPTSWELQGCLL- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556311266 123 nTVLTVRAGQAHSHASLGWETFTDKVISLINEHRegVVFLLWGSHAQKKGAiidrqRHHVLKAPHPSPLSAHRgfFGSNH 202
Cdd:smart00986 79 -PWLTVELALARPHLILLLGKFAAQALLGLLRRP--LVFGLRGRVAQLKGK-----GHRVLPLPHPSPLNRNF--FPAKK 148
|
....*...
gi 556311266 203 FVLANEWL 210
Cdd:smart00986 149 FAAWNDLL 156
|
|
| UDG |
pfam03167 |
Uracil DNA glycosylase superfamily; |
55-211 |
8.45e-25 |
|
Uracil DNA glycosylase superfamily;
Pssm-ID: 397331 Cd Length: 154 Bit Score: 95.49 E-value: 8.45e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556311266 55 DVKVVILGQDPYHGpGQAHGLAFSVRPGvAIPPSLLNMYkelegtvpGFTRPNHgyleswARQGVLLLNTVLTVR--AGQ 132
Cdd:pfam03167 7 NAKVLIVGEAPGAD-EDATGLPFVGRAG-NLLWKLLNAA--------GLTRDLF------SPQGVYITNVVKCRPgnRRK 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556311266 133 AHSHA-SLGWEtFTDKVISLINEHregvVFLLWGSHAQKK-----------GAIIDRQRHHVLKAPHPSPLSAHRgffgS 200
Cdd:pfam03167 71 PTSHEiDACWP-YLEAEIELLRPR----VIVLLGKTAAKAllglkkitklrGKLIDLKGIPVLPTPHPSPLLRNK----L 141
|
170
....*....|.
gi 556311266 201 NHFVLANEWLE 211
Cdd:pfam03167 142 NPFLKANAWED 152
|
|
| UDG-like |
cd09593 |
uracil-DNA glycosylases (UDG) and related enzymes; Uracil-DNA glycosylases (UDGs) initiate ... |
58-193 |
3.80e-18 |
|
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: 77.04 E-value: 3.80e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556311266 58 VVILGQDPYHGPGQAHGLAFsvrpgvaiPPSLLNMYKELEgtVPGFTrpnhgylESWARQGVLLLNTVLTVRAGQAHSHA 137
Cdd:cd09593 1 VLIVGQNPGPHGARAGGVPP--------GPSGNRLWRLLA--AAGGT-------PRLFRYGVGLTNTVPRGPPGAAAGSE 63
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 556311266 138 SlGWETFTDKVISLINEHREGVVFLLWGSHAQKKG-------AIIDRQRHHVLKAPHPSPLSA 193
Cdd:cd09593 64 K-KELRFCGRWLRKLLELLNPRVVVLLGKKAQEAYlavltssKGAPGKGTEVLVLPHPSPRNR 125
|
|
| UDG_F1_VAVC_D4-like |
cd19372 |
Uracil DNA glycosylase family 1 subfamily, includes Vaccinia virus protein D4 and similar ... |
39-220 |
9.03e-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: 42.04 E-value: 9.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556311266 39 PPQKDVFNAFRyTELSDVKVVILGQDPYhgPGQAHGLAF-----SVRPGVAIPPSLLNMYKelegtVPGFTRPNHGYLEs 113
Cdd:cd19372 26 PIPENFFKQLK-QPLRDKRVCICGIDPY--PTDATGVPFespdfSKKTIRAIAEAISRRTG-----VSLYKGYNFALVE- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556311266 114 warqGVLLLNTVLTVRAGQAHSHAsLGWETFTDKVISLINEHREgVVFLLWGSHAQKKGAIIDRQRhHVLKAPHPSplSA 193
Cdd:cd19372 97 ----GVLAWNYYLSCREGETKSHA-IHWERISKLLLQHIAKYVS-VLYCLGKTDFSNVRARLEVPV-TVVVGYHPA--AR 167
|
170 180
....*....|....*....|....*..
gi 556311266 194 HRGFFGSNHFVLANEWLEKRGETPIDW 220
Cdd:cd19372 168 DGQFDKERAFEIVNVLLELNGKPPVNW 194
|
|
|