|
Name |
Accession |
Description |
Interval |
E-value |
| Ung |
COG0692 |
Uracil-DNA glycosylase [Replication, recombination and repair]; |
1-217 |
6.18e-160 |
|
Uracil-DNA glycosylase [Replication, recombination and repair];
Pssm-ID: 440456 Cd Length: 221 Bit Score: 440.64 E-value: 6.18e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490412626 1 MESWKEALGAEKELPYFRHILETVRAERMQGEVVYPPASDVFNAFKATEFGRVKVVILGQDPYHGPGQAHGLAFSVRPDI 80
Cdd:COG0692 6 EPSWKEALAEEFEKPYFQALGAFLKAEYAAGKTIYPPGEDIFRAFNLTPFDDVKVVILGQDPYHGPGQAHGLSFSVPPGV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490412626 81 QIPPSLKNIYKEMADDIaGFRIPHHGCLQAWAEQGVLLLNTVLTVRAGQAHSHADLGWETFTDKAVRQLAEHREHLVFIL 160
Cdd:COG0692 86 PLPPSLRNIYKELEDDL-GIPIPNHGDLTSWAEQGVLLLNTVLTVRAGQAGSHAGKGWETFTDAVIRALNARKEPVVFLL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 490412626 161 WGSHAQKKGAFIDRNRHLVLTSAHPSPLSAYRGFFGSRPFSKANAYLAAHGQTPIDW 217
Cdd:COG0692 165 WGAYAQKKAALIDASKHLVLESPHPSPLSAHRGFFGSKPFSKANAYLEEQGKTPIDW 221
|
|
| PRK05254 |
PRK05254 |
uracil-DNA glycosylase; Provisional |
1-219 |
1.68e-158 |
|
uracil-DNA glycosylase; Provisional
Pssm-ID: 235376 Cd Length: 224 Bit Score: 437.28 E-value: 1.68e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490412626 1 MESWKEALGAEKELPYFRHILETVRAERMQGEVVYPPASDVFNAFKATEFGRVKVVILGQDPYHGPGQAHGLAFSVRPDI 80
Cdd:PRK05254 7 EPSWKEVLKPEFKKPYFQELLEFLRAERAAGKTIYPPGEDIFRAFNLTPFDDVKVVILGQDPYHGPGQAHGLSFSVPPGV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490412626 81 QIPPSLKNIYKEMADDIaGFRIPHHGCLQAWAEQGVLLLNTVLTVRAGQAHSHADLGWETFTDKAVRQLAEHREHLVFIL 160
Cdd:PRK05254 87 PIPPSLRNIFKELEDDL-GFPIPNHGDLTSWAEQGVLLLNTVLTVEAGQANSHAGKGWETFTDAVIKALNERREPVVFIL 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 490412626 161 WGSHAQKKGAFIDRNRHLVLTSAHPSPLSAYRGFFGSRPFSKANAYLAAHGQTPIDWQL 219
Cdd:PRK05254 166 WGSHAQKKKALIDNSKHLILESPHPSPLSAHRGFFGSKHFSKANALLKQHGKTPIDWQL 224
|
|
| UDG-F1-like |
cd10027 |
Uracil DNA glycosylase family 1 subfamily, includes Human uracil DNA glycosylase and similar ... |
16-217 |
3.92e-136 |
|
Uracil DNA glycosylase family 1 subfamily, includes Human uracil DNA glycosylase and similar proteins; Uracil DNA glycosylase family 1 is the most efficient of all uracil-DNA glycosylases (UDGs, also known as UNGs) and shows a specificity for uracil in DNA. UDG catalyzes the removal of uracil from DNA to initiate the DNA base excision repair pathway. Uracil in DNA can arise as a result of mis-incorporation of dUMP residues by DNA polymerase or deamination of cytosine. Uracil mispaired with guanine in DNA is one of the major pro-mutagenic events, causing G:C->A:T mutations. Thus, UDG is an essential enzyme for maintaining the integrity of genetic information. UDGs have been classified into various families on the basis of their substrate specificity, conserved motifs, and structural similarities. Although these families demonstrate different substrate specificities, often the function of one enzyme can be complemented by the other.
Pssm-ID: 381678 Cd Length: 200 Bit Score: 379.49 E-value: 3.92e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490412626 16 YFRHILETVRAERmQGEVVYPPASDVFNAFKATEFGRVKVVILGQDPYHGPGQAHGLAFSVRPDIQIPPSLKNIYKEMAD 95
Cdd:cd10027 1 YFKKLEAFLEEEY-KKKTIYPPKEDIFRAFELTPLDDVKVVILGQDPYHGPGQAHGLAFSVPPGVKIPPSLRNIFKELKS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490412626 96 DIAGFrIPHHGCLQAWAEQGVLLLNTVLTVRAGQAHSHADLGWETFTDKAVRQLAEHREHLVFILWGSHAQKKGAFIDRN 175
Cdd:cd10027 80 DLGIF-PPKHGDLSSWAKQGVLLLNTVLTVEAGKPGSHKNIGWETFTDAVIKALSEKNENVVFLLWGNHAQKKKKLIDKK 158
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 490412626 176 RHLVLTSAHPSPLSAYRGFFGSRPFSKANAYLAAHGQTPIDW 217
Cdd:cd10027 159 KHLVLESSHPSPLSAYRGFFGSKHFSKANEYLKKHGKKPIDW 200
|
|
| ung |
TIGR00628 |
uracil-DNA glycosylase; All proteins in this family for which functions are known are ... |
2-212 |
3.65e-125 |
|
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: 352.29 E-value: 3.65e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490412626 2 ESWKEALGAEKELPYFRHILETVRAERmQGEVVYPPASDVFNAFKATEFGRVKVVILGQDPYHGPGQAHGLAFSVRPDIQ 81
Cdd:TIGR00628 2 PSWRAFLQPEFKKPYFQELLAFYKRER-AQETVYPPKEDVFAWTRLCPPEDVKVVILGQDPYHGPGQAHGLAFSVKRGVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490412626 82 IPPSLKNIYKEMADDIAGFRIPHHGCLQAWAEQGVLLLNTVLTVRAGQAHSHADLGWETFTDKAVRQLAEHREHLVFILW 161
Cdd:TIGR00628 81 IPPSLKNIFKELEADYPDFPPPKHGCLEAWARQGVLLLNTVLTVRRGQPGSHSGLGWERFTDAVISRLSERLDGLVFMLW 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 490412626 162 GSHAQKKGAFIDRNRHLVLTSAHPSPLSAYRGFFGSRPFSKANAYLAAHGQ 212
Cdd:TIGR00628 161 GAHAQKKKSLIDAKKHLVLKSPHPSPLSARRGFFGCRHFSKANEYLEKHGK 211
|
|
| UDG |
smart00986 |
Uracil DNA glycosylase superfamily; |
50-207 |
5.39e-31 |
|
Uracil DNA glycosylase superfamily;
Pssm-ID: 214956 Cd Length: 156 Bit Score: 111.32 E-value: 5.39e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490412626 50 FGRVKVVILGQDPYHGPGQ-------AHGLAFSVRP----DIQIPPSLKNIYKEMADDIAgfriphHGCLQAWAEQGVLL 118
Cdd:smart00986 5 DPNAKVLIVGQAPGASEEDrggpfvgAAGLLLSVMLgvagLPRLPPYLTNIVKCRPPDAG------NRRPTSWELQGCLL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490412626 119 lnTVLTVRAGQAHSHADLGWETFTDKAVRQLAEHreHLVFILWGSHAQKKGAfidrnRHLVLTSAHPSPLSAYRgfFGSR 198
Cdd:smart00986 79 --PWLTVELALARPHLILLLGKFAAQALLGLLRR--PLVFGLRGRVAQLKGK-----GHRVLPLPHPSPLNRNF--FPAK 147
|
....*....
gi 490412626 199 PFSKANAYL 207
Cdd:smart00986 148 KFAAWNDLL 156
|
|
| UDG |
pfam03167 |
Uracil DNA glycosylase superfamily; |
53-206 |
1.98e-20 |
|
Uracil DNA glycosylase superfamily;
Pssm-ID: 397331 Cd Length: 154 Bit Score: 83.94 E-value: 1.98e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490412626 53 VKVVILGQDPYHGpGQAHGLAFSVRPDiQIPPSLKNIykemaddiAGFRiphhgcLQAWAEQGVLLLNTVLTVR--AGQA 130
Cdd:pfam03167 8 AKVLIVGEAPGAD-EDATGLPFVGRAG-NLLWKLLNA--------AGLT------RDLFSPQGVYITNVVKCRPgnRRKP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490412626 131 HSHA-DLGWEtFTDKAVRQLAEHrehlVFILWGSHAQKK-----------GAFIDRNRHLVLTSAHPSPLSAYRgffgSR 198
Cdd:pfam03167 72 TSHEiDACWP-YLEAEIELLRPR----VIVLLGKTAAKAllglkkitklrGKLIDLKGIPVLPTPHPSPLLRNK----LN 142
|
....*...
gi 490412626 199 PFSKANAY 206
Cdd:pfam03167 143 PFLKANAW 150
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| Ung |
COG0692 |
Uracil-DNA glycosylase [Replication, recombination and repair]; |
1-217 |
6.18e-160 |
|
Uracil-DNA glycosylase [Replication, recombination and repair];
Pssm-ID: 440456 Cd Length: 221 Bit Score: 440.64 E-value: 6.18e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490412626 1 MESWKEALGAEKELPYFRHILETVRAERMQGEVVYPPASDVFNAFKATEFGRVKVVILGQDPYHGPGQAHGLAFSVRPDI 80
Cdd:COG0692 6 EPSWKEALAEEFEKPYFQALGAFLKAEYAAGKTIYPPGEDIFRAFNLTPFDDVKVVILGQDPYHGPGQAHGLSFSVPPGV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490412626 81 QIPPSLKNIYKEMADDIaGFRIPHHGCLQAWAEQGVLLLNTVLTVRAGQAHSHADLGWETFTDKAVRQLAEHREHLVFIL 160
Cdd:COG0692 86 PLPPSLRNIYKELEDDL-GIPIPNHGDLTSWAEQGVLLLNTVLTVRAGQAGSHAGKGWETFTDAVIRALNARKEPVVFLL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 490412626 161 WGSHAQKKGAFIDRNRHLVLTSAHPSPLSAYRGFFGSRPFSKANAYLAAHGQTPIDW 217
Cdd:COG0692 165 WGAYAQKKAALIDASKHLVLESPHPSPLSAHRGFFGSKPFSKANAYLEEQGKTPIDW 221
|
|
| PRK05254 |
PRK05254 |
uracil-DNA glycosylase; Provisional |
1-219 |
1.68e-158 |
|
uracil-DNA glycosylase; Provisional
Pssm-ID: 235376 Cd Length: 224 Bit Score: 437.28 E-value: 1.68e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490412626 1 MESWKEALGAEKELPYFRHILETVRAERMQGEVVYPPASDVFNAFKATEFGRVKVVILGQDPYHGPGQAHGLAFSVRPDI 80
Cdd:PRK05254 7 EPSWKEVLKPEFKKPYFQELLEFLRAERAAGKTIYPPGEDIFRAFNLTPFDDVKVVILGQDPYHGPGQAHGLSFSVPPGV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490412626 81 QIPPSLKNIYKEMADDIaGFRIPHHGCLQAWAEQGVLLLNTVLTVRAGQAHSHADLGWETFTDKAVRQLAEHREHLVFIL 160
Cdd:PRK05254 87 PIPPSLRNIFKELEDDL-GFPIPNHGDLTSWAEQGVLLLNTVLTVEAGQANSHAGKGWETFTDAVIKALNERREPVVFIL 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 490412626 161 WGSHAQKKGAFIDRNRHLVLTSAHPSPLSAYRGFFGSRPFSKANAYLAAHGQTPIDWQL 219
Cdd:PRK05254 166 WGSHAQKKKALIDNSKHLILESPHPSPLSAHRGFFGSKHFSKANALLKQHGKTPIDWQL 224
|
|
| UDG-F1-like |
cd10027 |
Uracil DNA glycosylase family 1 subfamily, includes Human uracil DNA glycosylase and similar ... |
16-217 |
3.92e-136 |
|
Uracil DNA glycosylase family 1 subfamily, includes Human uracil DNA glycosylase and similar proteins; Uracil DNA glycosylase family 1 is the most efficient of all uracil-DNA glycosylases (UDGs, also known as UNGs) and shows a specificity for uracil in DNA. UDG catalyzes the removal of uracil from DNA to initiate the DNA base excision repair pathway. Uracil in DNA can arise as a result of mis-incorporation of dUMP residues by DNA polymerase or deamination of cytosine. Uracil mispaired with guanine in DNA is one of the major pro-mutagenic events, causing G:C->A:T mutations. Thus, UDG is an essential enzyme for maintaining the integrity of genetic information. UDGs have been classified into various families on the basis of their substrate specificity, conserved motifs, and structural similarities. Although these families demonstrate different substrate specificities, often the function of one enzyme can be complemented by the other.
Pssm-ID: 381678 Cd Length: 200 Bit Score: 379.49 E-value: 3.92e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490412626 16 YFRHILETVRAERmQGEVVYPPASDVFNAFKATEFGRVKVVILGQDPYHGPGQAHGLAFSVRPDIQIPPSLKNIYKEMAD 95
Cdd:cd10027 1 YFKKLEAFLEEEY-KKKTIYPPKEDIFRAFELTPLDDVKVVILGQDPYHGPGQAHGLAFSVPPGVKIPPSLRNIFKELKS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490412626 96 DIAGFrIPHHGCLQAWAEQGVLLLNTVLTVRAGQAHSHADLGWETFTDKAVRQLAEHREHLVFILWGSHAQKKGAFIDRN 175
Cdd:cd10027 80 DLGIF-PPKHGDLSSWAKQGVLLLNTVLTVEAGKPGSHKNIGWETFTDAVIKALSEKNENVVFLLWGNHAQKKKKLIDKK 158
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 490412626 176 RHLVLTSAHPSPLSAYRGFFGSRPFSKANAYLAAHGQTPIDW 217
Cdd:cd10027 159 KHLVLESSHPSPLSAYRGFFGSKHFSKANEYLKKHGKKPIDW 200
|
|
| ung |
TIGR00628 |
uracil-DNA glycosylase; All proteins in this family for which functions are known are ... |
2-212 |
3.65e-125 |
|
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: 352.29 E-value: 3.65e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490412626 2 ESWKEALGAEKELPYFRHILETVRAERmQGEVVYPPASDVFNAFKATEFGRVKVVILGQDPYHGPGQAHGLAFSVRPDIQ 81
Cdd:TIGR00628 2 PSWRAFLQPEFKKPYFQELLAFYKRER-AQETVYPPKEDVFAWTRLCPPEDVKVVILGQDPYHGPGQAHGLAFSVKRGVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490412626 82 IPPSLKNIYKEMADDIAGFRIPHHGCLQAWAEQGVLLLNTVLTVRAGQAHSHADLGWETFTDKAVRQLAEHREHLVFILW 161
Cdd:TIGR00628 81 IPPSLKNIFKELEADYPDFPPPKHGCLEAWARQGVLLLNTVLTVRRGQPGSHSGLGWERFTDAVISRLSERLDGLVFMLW 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 490412626 162 GSHAQKKGAFIDRNRHLVLTSAHPSPLSAYRGFFGSRPFSKANAYLAAHGQ 212
Cdd:TIGR00628 161 GAHAQKKKSLIDAKKHLVLKSPHPSPLSARRGFFGCRHFSKANEYLEKHGK 211
|
|
| PHA03347 |
PHA03347 |
uracil DNA glycosylase; Provisional |
15-219 |
2.23e-85 |
|
uracil DNA glycosylase; Provisional
Pssm-ID: 177588 Cd Length: 252 Bit Score: 253.05 E-value: 2.23e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490412626 15 PYFRH----ILETVRAERMQgEVVYPPASDVFNAFKATEFGRVKVVILGQDPYHGpGQAHGLAFSVRPDIQIPPSLKNIY 90
Cdd:PHA03347 38 PFLKQkllaLLNCVRELRKQ-TVIYPPEDRIMAWSYLCDPEDIKVVILGQDPYHG-GQANGLAFSVAYGFPVPPSLRNIF 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490412626 91 KEMADDIAGFRIPHHGCLQAWAEQGVLLLNTVLTVRAGQAHSHADLGWETFTDKAVRQLAEHREHLVFILWGSHAQKKGA 170
Cdd:PHA03347 116 AELHRSVPDFSPPDHGCLDAWARQGVLLLNTILTVEKGKPGSHSDLGWAWFTDYIISSLSEKLKACVFMLWGSKAIDKAS 195
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 490412626 171 FIDRNRHLVLTSAHPSPLSA---YRG----FFGSRPFSKANAYLAAHGQTPIDWQL 219
Cdd:PHA03347 196 LINSQKHLVLKAQHPSPLAAnstRSStwpkFLGCNHFVLANKYLTQHGKGPIDWNL 251
|
|
| PHA03200 |
PHA03200 |
uracil DNA glycosylase; Provisional |
11-219 |
3.03e-85 |
|
uracil DNA glycosylase; Provisional
Pssm-ID: 165467 Cd Length: 255 Bit Score: 253.11 E-value: 3.03e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490412626 11 EKELPYFRHILETVRAERmQGEVVYPPASDVFNAFKATEFGRVKVVILGQDPYHGpGQAHGLAFSVRPDIQIPPSLKNIY 90
Cdd:PHA03200 44 DHDISQLRRIVDAVDRDR-QRLTVYPPPEDVHRWSRLCSPEDVKVVIVGQDPYHD-GSACGLAFGTVRGRSAPPSLKNVF 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490412626 91 KEMADDIAGFRIPHHGCLQAWAEQGVLLLNTVLTVRAGQAHSHADLGWETFTDKAVRQLAEHREHLVFILWGSHAQKKGA 170
Cdd:PHA03200 122 RELERTVPNFSRPDSGCLDSWCRQGVLLLNTVFTVVHGQPGSHEALGWQTLSDRVISRLSEKREHLVFMLWGAQAQKLEY 201
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 490412626 171 FIDRNRHLVLTSAHPSP--LSAYRGFFGSRPFSKANAYLAAHGQTPIDWQL 219
Cdd:PHA03200 202 LIDSRKHLILKSAHPSPrvKGARTPFIGNNHFVLANEYLSTHGKRPIDWNI 252
|
|
| PHA03202 |
PHA03202 |
uracil DNA glycosylase; Provisional |
3-219 |
3.72e-76 |
|
uracil DNA glycosylase; Provisional
Pssm-ID: 165469 Cd Length: 313 Bit Score: 231.89 E-value: 3.72e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490412626 3 SWKEALGAEKELPYFRHILETVRAeRMQGEVVYPPASDVFNAFKATEFGRVKVVILGQDPYHGPGQAHGLAFSVRPDIQI 82
Cdd:PHA03202 99 SWRPILEREMQQPYVRLLLNEYKL-RCAREEVFPPKEDIFAWTRFSPPEKVRVVIVGQDPYHAPGQAHGLAFSVRKGVPV 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490412626 83 PPSLKNIYKEMADDIAGFRIPHHGCLQAWAEQGVLLLNTVLTVRAGQAHSHADLGWETFTDKAVRQLAEHREHLVFILWG 162
Cdd:PHA03202 178 PPSLRNIYSAVQKSYPSFRPPMHGFLEKWAEQGVLLINTTLTVARGKPGSHATLGWHRLVRAVIDRLCTTSQGLVFMLWG 257
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 490412626 163 SHAQKKGAfIDRNRHLVLTSAHPSPLSayRGFFGSRP-FSKANAYLAAHGQTPIDWQL 219
Cdd:PHA03202 258 AHAQKSCS-PNRQHHLVLTYGHPSPLS--RVNFRDCPhFLEANAYLTKTGRKPVDWQI 312
|
|
| PHA03199 |
PHA03199 |
uracil DNA glycosylase; Provisional |
4-219 |
3.43e-68 |
|
uracil DNA glycosylase; Provisional
Pssm-ID: 165466 Cd Length: 304 Bit Score: 211.40 E-value: 3.43e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490412626 4 WKEALGAEKELPYFRHILETVRAERMQGEVVYPPASDVFNAFKATEFGRVKVVILGQDPYHGPGQAHGLAFSVRPDIQIP 83
Cdd:PHA03199 91 WHDLLRDEFEEPYAKGIFEEYNQLLNNGEEIFPIKGDIFAWTRFCGPEKIRVVIIGQDPYHGAGHAHGLAFSVKRGIPIP 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490412626 84 PSLKNIYKEMADDIAGFRIPHHGCLQAWAEQGVLLLNTVLTVRAGQAHSHADLGWETFTDKAVRQLAEHREHLVFILWGS 163
Cdd:PHA03199 171 PSLKNIFAALMESYPHLPLPTHGCLDNWARQGVLLLNTTLTVKRGTPGSHFYLGWDMLIKRMLKRLCENRTGLVFMLWGA 250
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 490412626 164 HAQKKgafIDRN--RHLVLTSAHPSPLSAYRgFFGSRPFSKANAYLAAHGQTPIDWQL 219
Cdd:PHA03199 251 HAQKT---IQPNprCHLVLTHAHPSPLSRSE-FRNCKHFLQANEYFLKKGEPEIDWSI 304
|
|
| PHA03201 |
PHA03201 |
uracil DNA glycosylase; Provisional |
2-217 |
3.75e-66 |
|
uracil DNA glycosylase; Provisional
Pssm-ID: 165468 Cd Length: 318 Bit Score: 206.67 E-value: 3.75e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490412626 2 ESWKEALGAEKELPYFRHIL-ETVRaeRMQGEVVYPPASDVFNAFKATEFGRVKVVILGQDPYHGPGQAHGLAFSVRPDI 80
Cdd:PHA03201 104 DAWRPLLEPELANPLTARLMaEYER--RCRTEEVLPPREDVFSWTRYCTPDEVRVVIIGQDPYHQPGQAHGLAFSVRPGT 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490412626 81 QIPPSLKNIYKEMADDIAGFRIPHHGCLQAWAEQGVLLLNTVLTVRAGQAHSHADLGWETFTDKAVRQLAEHREHLVFIL 160
Cdd:PHA03201 182 PAPPSLRNILAAVRNCCPDARMSGHGCLEKWARGGVLLLNTTLTVRRGEPASHAKIGWDRFVGSVVRRLAASRPGLVFML 261
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 490412626 161 WGSHAQkKGAFIDRNRHLVLTSAHPSPLSayRGFFGS-RPFSKANAYLAAHGQTPIDW 217
Cdd:PHA03201 262 WGAHAQ-NAIRPDPRVHRVLTYSHPSPLS--KVPFGScRHFCLANQYLRERSLAPIDW 316
|
|
| PHA03204 |
PHA03204 |
uracil DNA glycosylase; Provisional |
2-219 |
5.33e-63 |
|
uracil DNA glycosylase; Provisional
Pssm-ID: 165471 Cd Length: 322 Bit Score: 198.65 E-value: 5.33e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490412626 2 ESWKEALGAEKELPYFRHIL-ETVRaeRMQGEVVYPPASDVFNAFKATEFGRVKVVILGQDPYHGPGQAHGLAFSVRPDI 80
Cdd:PHA03204 104 CRWKEILLPELCCPTGSKILaEYER--RARYEEVYPPKSDIFAWTRYCAPDHVKVVIVGQDPYANPGQAHGLAFSVKPGS 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490412626 81 QIPPSLKNIYKEMADDIAGFRIPHHGCLQAWAEQGVLLLNTVLTVRAGQAHSHADLGWETFTDKAVRQLAEHREHLVFIL 160
Cdd:PHA03204 182 PIPPSLKNILAAVKACYPSIELGSHGCLEDWAKRGVLLLNSVLTVKRGDPGSHHSVGWQILVRNVLRRLSQSTRGIVFML 261
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 490412626 161 WGSHAQKKGAFIDRN-RHLVLTSAHPSPLSAyRGFFGSRPFSKANAYLAAHGQTPIDWQL 219
Cdd:PHA03204 262 WGAQAQTMYFQTDNDdRHLVLKYSHPSPLSR-KPFAHCTHFKDANEFLCKMGKGAIDWSL 320
|
|
| UDG-F1-like |
cd19371 |
Uracil DNA glycosylase family 1, includes Human uracil DNA glycosylase, Vaccinia virus protein ... |
55-189 |
7.13e-55 |
|
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: 171.75 E-value: 7.13e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490412626 55 VVILGQDPYHGPGQAHGLAFSVRPDIQIPPSLKNIYKEMADDIAGFRIPHHGCLQAWAEQGVLLLNTVLTVRAGQAHSHA 134
Cdd:cd19371 1 VVIIGQDPYPSPGHAGGLAFSVTSEVPPPKSLRNIYKELERDYSSFLPPGNGTLEFWARQGVLLLNAALTCESGKPKSHY 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 490412626 135 DLgWETFTDKAVRQLAEHREHLVFILWGSHAQKKGAFIDRNRHLVLTSAHPSPLS 189
Cdd:cd19371 81 LL-WEPFIKAFIRYISAHNKGLVFLLFGSDAQKLRKKINGRNVHVFKADHPSPAD 134
|
|
| UDG |
smart00986 |
Uracil DNA glycosylase superfamily; |
50-207 |
5.39e-31 |
|
Uracil DNA glycosylase superfamily;
Pssm-ID: 214956 Cd Length: 156 Bit Score: 111.32 E-value: 5.39e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490412626 50 FGRVKVVILGQDPYHGPGQ-------AHGLAFSVRP----DIQIPPSLKNIYKEMADDIAgfriphHGCLQAWAEQGVLL 118
Cdd:smart00986 5 DPNAKVLIVGQAPGASEEDrggpfvgAAGLLLSVMLgvagLPRLPPYLTNIVKCRPPDAG------NRRPTSWELQGCLL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490412626 119 lnTVLTVRAGQAHSHADLGWETFTDKAVRQLAEHreHLVFILWGSHAQKKGAfidrnRHLVLTSAHPSPLSAYRgfFGSR 198
Cdd:smart00986 79 --PWLTVELALARPHLILLLGKFAAQALLGLLRR--PLVFGLRGRVAQLKGK-----GHRVLPLPHPSPLNRNF--FPAK 147
|
....*....
gi 490412626 199 PFSKANAYL 207
Cdd:smart00986 148 KFAAWNDLL 156
|
|
| UDG |
pfam03167 |
Uracil DNA glycosylase superfamily; |
53-206 |
1.98e-20 |
|
Uracil DNA glycosylase superfamily;
Pssm-ID: 397331 Cd Length: 154 Bit Score: 83.94 E-value: 1.98e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490412626 53 VKVVILGQDPYHGpGQAHGLAFSVRPDiQIPPSLKNIykemaddiAGFRiphhgcLQAWAEQGVLLLNTVLTVR--AGQA 130
Cdd:pfam03167 8 AKVLIVGEAPGAD-EDATGLPFVGRAG-NLLWKLLNA--------AGLT------RDLFSPQGVYITNVVKCRPgnRRKP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490412626 131 HSHA-DLGWEtFTDKAVRQLAEHrehlVFILWGSHAQKK-----------GAFIDRNRHLVLTSAHPSPLSAYRgffgSR 198
Cdd:pfam03167 72 TSHEiDACWP-YLEAEIELLRPR----VIVLLGKTAAKAllglkkitklrGKLIDLKGIPVLPTPHPSPLLRNK----LN 142
|
....*...
gi 490412626 199 PFSKANAY 206
Cdd:pfam03167 143 PFLKANAW 150
|
|
| UDG-like |
cd09593 |
uracil-DNA glycosylases (UDG) and related enzymes; Uracil-DNA glycosylases (UDGs) initiate ... |
55-190 |
9.69e-19 |
|
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: 78.58 E-value: 9.69e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490412626 55 VVILGQDPYHGPGQAHGlafsvrpdIQIPPSLKNIYKEMADDIAGFRiphhgclqaWAEQGVLLLNTVLTVRAGQAHSHA 134
Cdd:cd09593 1 VLIVGQNPGPHGARAGG--------VPPGPSGNRLWRLLAAAGGTPR---------LFRYGVGLTNTVPRGPPGAAAGSE 63
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490412626 135 DlGWETFTDKAVRQLAEHREHLVFILWGSHAQKKG-------AFIDRNRHLVLTSAHPSPLSA 190
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 ... |
54-217 |
5.57e-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: 42.42 E-value: 5.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490412626 54 KVVILGQDPYhgPGQAHGLAFsvrpdiQIPPSLKNIYKEMADDIA-GFRIPHHGCLQAWAEQGVLLLNTVLTVRAGQAHS 132
Cdd:cd19372 43 RVCICGIDPY--PTDATGVPF------ESPDFSKKTIRAIAEAISrRTGVSLYKGYNFALVEGVLAWNYYLSCREGETKS 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490412626 133 HAdLGWETFTDKAVRQLAEHREHLVFiLWGSHAQKKGAFIDRNRHLVLtSAHPsplsAYRG--FFGSRPFSKANAYLAAH 210
Cdd:cd19372 115 HA-IHWERISKLLLQHIAKYVSVLYC-LGKTDFSNVRARLEVPVTVVV-GYHP----AARDgqFDKERAFEIVNVLLELN 187
|
....*..
gi 490412626 211 GQTPIDW 217
Cdd:cd19372 188 GKPPVNW 194
|
|
|