|
Name |
Accession |
Description |
Interval |
E-value |
| Ung |
COG0692 |
Uracil-DNA glycosylase [Replication, recombination and repair]; |
9-222 |
1.24e-157 |
|
Uracil-DNA glycosylase [Replication, recombination and repair];
Pssm-ID: 440456 Cd Length: 221 Bit Score: 435.24 E-value: 1.24e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492167823 9 TWQTVLGEEKQEPYFQEILDFVKKERKAGKIIYPPQKDIFNALKLTPYEAVKVVILGQDPYHGPNQAHGLAFSVRPGVPA 88
Cdd:COG0692 8 SWKEALAEEFEKPYFQALGAFLKAEYAAGKTIYPPGEDIFRAFNLTPFDDVKVVILGQDPYHGPGQAHGLSFSVPPGVPL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492167823 89 PPSLQNIFKELHADLGVSIPSHGFLEKWAKQGVLLLNAALTVEAGKPQSHANIGWHRFTDKVIESLNDHPEGIVFLLWGS 168
Cdd:COG0692 88 PPSLRNIYKELEDDLGIPIPNHGDLTSWAEQGVLLLNTVLTVRAGQAGSHAGKGWETFTDAVIRALNARKEPVVFLLWGA 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 492167823 169 YAQKKSQLITNLRHRILKAPHPSPLSAARGFLGCRHFSKANQLLHEMGRGEIDW 222
Cdd:COG0692 168 YAQKKAALIDASKHLVLESPHPSPLSAHRGFFGSKPFSKANAYLEEQGKTPIDW 221
|
|
| PRK05254 |
PRK05254 |
uracil-DNA glycosylase; Provisional |
1-224 |
4.20e-154 |
|
uracil-DNA glycosylase; Provisional
Pssm-ID: 235376 Cd Length: 224 Bit Score: 426.49 E-value: 4.20e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492167823 1 MTTMAETQTWQTVLGEEKQEPYFQEILDFVKKERKAGKIIYPPQKDIFNALKLTPYEAVKVVILGQDPYHGPNQAHGLAF 80
Cdd:PRK05254 1 PMKMLLEPSWKEVLKPEFKKPYFQELLEFLRAERAAGKTIYPPGEDIFRAFNLTPFDDVKVVILGQDPYHGPGQAHGLSF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492167823 81 SVRPGVPAPPSLQNIFKELHADLGVSIPSHGFLEKWAKQGVLLLNAALTVEAGKPQSHANIGWHRFTDKVIESLNDHPEG 160
Cdd:PRK05254 81 SVPPGVPIPPSLRNIFKELEDDLGFPIPNHGDLTSWAEQGVLLLNTVLTVEAGQANSHAGKGWETFTDAVIKALNERREP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 492167823 161 IVFLLWGSYAQKKSQLITNLRHRILKAPHPSPLSAARGFLGCRHFSKANQLLHEMGRGEIDWAL 224
Cdd:PRK05254 161 VVFILWGSHAQKKKALIDNSKHLILESPHPSPLSAHRGFFGSKHFSKANALLKQHGKTPIDWQL 224
|
|
| UDG-F1-like |
cd10027 |
Uracil DNA glycosylase family 1 subfamily, includes Human uracil DNA glycosylase and similar ... |
22-222 |
2.46e-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: 380.64 E-value: 2.46e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492167823 22 YFQEILDFVKKERKAgKIIYPPQKDIFNALKLTPYEAVKVVILGQDPYHGPNQAHGLAFSVRPGVPAPPSLQNIFKELHA 101
Cdd:cd10027 1 YFKKLEAFLEEEYKK-KTIYPPKEDIFRAFELTPLDDVKVVILGQDPYHGPGQAHGLAFSVPPGVKIPPSLRNIFKELKS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492167823 102 DLGVSIPSHGFLEKWAKQGVLLLNAALTVEAGKPQSHANIGWHRFTDKVIESLNDHPEGIVFLLWGSYAQKKSQLITNLR 181
Cdd:cd10027 80 DLGIFPPKHGDLSSWAKQGVLLLNTVLTVEAGKPGSHKNIGWETFTDAVIKALSEKNENVVFLLWGNHAQKKKKLIDKKK 159
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 492167823 182 HRILKAPHPSPLSAARGFLGCRHFSKANQLLHEMGRGEIDW 222
Cdd:cd10027 160 HLVLESSHPSPLSAYRGFFGSKHFSKANEYLKKHGKKPIDW 200
|
|
| ung |
TIGR00628 |
uracil-DNA glycosylase; All proteins in this family for which functions are known are ... |
10-217 |
4.20e-121 |
|
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: 342.66 E-value: 4.20e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492167823 10 WQTVLGEEKQEPYFQEILDFVKKERkAGKIIYPPQKDIFNALKLTPYEAVKVVILGQDPYHGPNQAHGLAFSVRPGVPAP 89
Cdd:TIGR00628 4 WRAFLQPEFKKPYFQELLAFYKRER-AQETVYPPKEDVFAWTRLCPPEDVKVVILGQDPYHGPGQAHGLAFSVKRGVPIP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492167823 90 PSLQNIFKELHADLG-VSIPSHGFLEKWAKQGVLLLNAALTVEAGKPQSHANIGWHRFTDKVIESLNDHPEGIVFLLWGS 168
Cdd:TIGR00628 83 PSLKNIFKELEADYPdFPPPKHGCLEAWARQGVLLLNTVLTVRRGQPGSHSGLGWERFTDAVISRLSERLDGLVFMLWGA 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 492167823 169 YAQKKSQLITNLRHRILKAPHPSPLSAARGFLGCRHFSKANQLLHEMGR 217
Cdd:TIGR00628 163 HAQKKKSLIDAKKHLVLKSPHPSPLSARRGFFGCRHFSKANEYLEKHGK 211
|
|
| UDG |
smart00986 |
Uracil DNA glycosylase superfamily; |
53-212 |
2.14e-35 |
|
Uracil DNA glycosylase superfamily;
Pssm-ID: 214956 Cd Length: 156 Bit Score: 122.88 E-value: 2.14e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492167823 53 LTPYEAVKVVILGQDPY------HGP-NQAHGLAFSVRPGV----PAPPSLQNIFKELHADlgvsiPSHGFLEKWAKQGV 121
Cdd:smart00986 2 GTGDPNAKVLIVGQAPGaseedrGGPfVGAAGLLLSVMLGVaglpRLPPYLTNIVKCRPPD-----AGNRRPTSWELQGC 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492167823 122 LLlnAALTVEAGKPQSHANIGWHRFTDKVIESLNDHPegIVFLLWGSYAQKKSQLitnlrHRILKAPHPSPLSAARgfLG 201
Cdd:smart00986 77 LL--PWLTVELALARPHLILLLGKFAAQALLGLLRRP--LVFGLRGRVAQLKGKG-----HRVLPLPHPSPLNRNF--FP 145
|
170
....*....|.
gi 492167823 202 CRHFSKANQLL 212
Cdd:smart00986 146 AKKFAAWNDLL 156
|
|
| UDG |
pfam03167 |
Uracil DNA glycosylase superfamily; |
57-209 |
1.01e-20 |
|
Uracil DNA glycosylase superfamily;
Pssm-ID: 397331 Cd Length: 154 Bit Score: 84.71 E-value: 1.01e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492167823 57 EAVKVVILGQDPYHGpNQAHGLAFSVRPGvpappslqNIFKELHADLGVSIPSHgflekwAKQGVLLLNAALTV--EAGK 134
Cdd:pfam03167 6 PNAKVLIVGEAPGAD-EDATGLPFVGRAG--------NLLWKLLNAAGLTRDLF------SPQGVYITNVVKCRpgNRRK 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492167823 135 PQSHA-NIGWhRFTDKVIESLNDHpegiVFLLWGSYAQK---KSQLITNLR--------HRILKAPHPSPLSAARgflgC 202
Cdd:pfam03167 71 PTSHEiDACW-PYLEAEIELLRPR----VIVLLGKTAAKallGLKKITKLRgklidlkgIPVLPTPHPSPLLRNK----L 141
|
....*..
gi 492167823 203 RHFSKAN 209
Cdd:pfam03167 142 NPFLKAN 148
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| Ung |
COG0692 |
Uracil-DNA glycosylase [Replication, recombination and repair]; |
9-222 |
1.24e-157 |
|
Uracil-DNA glycosylase [Replication, recombination and repair];
Pssm-ID: 440456 Cd Length: 221 Bit Score: 435.24 E-value: 1.24e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492167823 9 TWQTVLGEEKQEPYFQEILDFVKKERKAGKIIYPPQKDIFNALKLTPYEAVKVVILGQDPYHGPNQAHGLAFSVRPGVPA 88
Cdd:COG0692 8 SWKEALAEEFEKPYFQALGAFLKAEYAAGKTIYPPGEDIFRAFNLTPFDDVKVVILGQDPYHGPGQAHGLSFSVPPGVPL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492167823 89 PPSLQNIFKELHADLGVSIPSHGFLEKWAKQGVLLLNAALTVEAGKPQSHANIGWHRFTDKVIESLNDHPEGIVFLLWGS 168
Cdd:COG0692 88 PPSLRNIYKELEDDLGIPIPNHGDLTSWAEQGVLLLNTVLTVRAGQAGSHAGKGWETFTDAVIRALNARKEPVVFLLWGA 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 492167823 169 YAQKKSQLITNLRHRILKAPHPSPLSAARGFLGCRHFSKANQLLHEMGRGEIDW 222
Cdd:COG0692 168 YAQKKAALIDASKHLVLESPHPSPLSAHRGFFGSKPFSKANAYLEEQGKTPIDW 221
|
|
| PRK05254 |
PRK05254 |
uracil-DNA glycosylase; Provisional |
1-224 |
4.20e-154 |
|
uracil-DNA glycosylase; Provisional
Pssm-ID: 235376 Cd Length: 224 Bit Score: 426.49 E-value: 4.20e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492167823 1 MTTMAETQTWQTVLGEEKQEPYFQEILDFVKKERKAGKIIYPPQKDIFNALKLTPYEAVKVVILGQDPYHGPNQAHGLAF 80
Cdd:PRK05254 1 PMKMLLEPSWKEVLKPEFKKPYFQELLEFLRAERAAGKTIYPPGEDIFRAFNLTPFDDVKVVILGQDPYHGPGQAHGLSF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492167823 81 SVRPGVPAPPSLQNIFKELHADLGVSIPSHGFLEKWAKQGVLLLNAALTVEAGKPQSHANIGWHRFTDKVIESLNDHPEG 160
Cdd:PRK05254 81 SVPPGVPIPPSLRNIFKELEDDLGFPIPNHGDLTSWAEQGVLLLNTVLTVEAGQANSHAGKGWETFTDAVIKALNERREP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 492167823 161 IVFLLWGSYAQKKSQLITNLRHRILKAPHPSPLSAARGFLGCRHFSKANQLLHEMGRGEIDWAL 224
Cdd:PRK05254 161 VVFILWGSHAQKKKALIDNSKHLILESPHPSPLSAHRGFFGSKHFSKANALLKQHGKTPIDWQL 224
|
|
| UDG-F1-like |
cd10027 |
Uracil DNA glycosylase family 1 subfamily, includes Human uracil DNA glycosylase and similar ... |
22-222 |
2.46e-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: 380.64 E-value: 2.46e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492167823 22 YFQEILDFVKKERKAgKIIYPPQKDIFNALKLTPYEAVKVVILGQDPYHGPNQAHGLAFSVRPGVPAPPSLQNIFKELHA 101
Cdd:cd10027 1 YFKKLEAFLEEEYKK-KTIYPPKEDIFRAFELTPLDDVKVVILGQDPYHGPGQAHGLAFSVPPGVKIPPSLRNIFKELKS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492167823 102 DLGVSIPSHGFLEKWAKQGVLLLNAALTVEAGKPQSHANIGWHRFTDKVIESLNDHPEGIVFLLWGSYAQKKSQLITNLR 181
Cdd:cd10027 80 DLGIFPPKHGDLSSWAKQGVLLLNTVLTVEAGKPGSHKNIGWETFTDAVIKALSEKNENVVFLLWGNHAQKKKKLIDKKK 159
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 492167823 182 HRILKAPHPSPLSAARGFLGCRHFSKANQLLHEMGRGEIDW 222
Cdd:cd10027 160 HLVLESSHPSPLSAYRGFFGSKHFSKANEYLKKHGKKPIDW 200
|
|
| ung |
TIGR00628 |
uracil-DNA glycosylase; All proteins in this family for which functions are known are ... |
10-217 |
4.20e-121 |
|
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: 342.66 E-value: 4.20e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492167823 10 WQTVLGEEKQEPYFQEILDFVKKERkAGKIIYPPQKDIFNALKLTPYEAVKVVILGQDPYHGPNQAHGLAFSVRPGVPAP 89
Cdd:TIGR00628 4 WRAFLQPEFKKPYFQELLAFYKRER-AQETVYPPKEDVFAWTRLCPPEDVKVVILGQDPYHGPGQAHGLAFSVKRGVPIP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492167823 90 PSLQNIFKELHADLG-VSIPSHGFLEKWAKQGVLLLNAALTVEAGKPQSHANIGWHRFTDKVIESLNDHPEGIVFLLWGS 168
Cdd:TIGR00628 83 PSLKNIFKELEADYPdFPPPKHGCLEAWARQGVLLLNTVLTVRRGQPGSHSGLGWERFTDAVISRLSERLDGLVFMLWGA 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 492167823 169 YAQKKSQLITNLRHRILKAPHPSPLSAARGFLGCRHFSKANQLLHEMGR 217
Cdd:TIGR00628 163 HAQKKKSLIDAKKHLVLKSPHPSPLSARRGFFGCRHFSKANEYLEKHGK 211
|
|
| PHA03347 |
PHA03347 |
uracil DNA glycosylase; Provisional |
24-225 |
1.93e-85 |
|
uracil DNA glycosylase; Provisional
Pssm-ID: 177588 Cd Length: 252 Bit Score: 253.82 E-value: 1.93e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492167823 24 QEILDFVKKERKAgKIIYPPQKDIFNALKLTPYEAVKVVILGQDPYHGpNQAHGLAFSVRPGVPAPPSLQNIFKELHA-D 102
Cdd:PHA03347 45 LALLNCVRELRKQ-TVIYPPEDRIMAWSYLCDPEDIKVVILGQDPYHG-GQANGLAFSVAYGFPVPPSLRNIFAELHRsV 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492167823 103 LGVSIPSHGFLEKWAKQGVLLLNAALTVEAGKPQSHANIGWHRFTDKVIESLNDHPEGIVFLLWGSYAQKKSQLITNLRH 182
Cdd:PHA03347 123 PDFSPPDHGCLDAWARQGVLLLNTILTVEKGKPGSHSDLGWAWFTDYIISSLSEKLKACVFMLWGSKAIDKASLINSQKH 202
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 492167823 183 RILKAPHPSPLSAARG-------FLGCRHFSKANQLLHEMGRGEIDWALD 225
Cdd:PHA03347 203 LVLKAQHPSPLAANSTrsstwpkFLGCNHFVLANKYLTQHGKGPIDWNLE 252
|
|
| PHA03202 |
PHA03202 |
uracil DNA glycosylase; Provisional |
9-225 |
5.08e-78 |
|
uracil DNA glycosylase; Provisional
Pssm-ID: 165469 Cd Length: 313 Bit Score: 237.29 E-value: 5.08e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492167823 9 TWQTVLGEEKQEPYFQEILDFVKKeRKAGKIIYPPQKDIFNALKLTPYEAVKVVILGQDPYHGPNQAHGLAFSVRPGVPA 88
Cdd:PHA03202 99 SWRPILEREMQQPYVRLLLNEYKL-RCAREEVFPPKEDIFAWTRFSPPEKVRVVIVGQDPYHAPGQAHGLAFSVRKGVPV 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492167823 89 PPSLQNIFKELHADL-GVSIPSHGFLEKWAKQGVLLLNAALTVEAGKPQSHANIGWHRFTDKVIESLNDHPEGIVFLLWG 167
Cdd:PHA03202 178 PPSLRNIYSAVQKSYpSFRPPMHGFLEKWAEQGVLLINTTLTVARGKPGSHATLGWHRLVRAVIDRLCTTSQGLVFMLWG 257
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 492167823 168 SYAQKKSQlITNLRHRILKAPHPSPLSAArGFLGCRHFSKANQLLHEMGRGEIDWALD 225
Cdd:PHA03202 258 AHAQKSCS-PNRQHHLVLTYGHPSPLSRV-NFRDCPHFLEANAYLTKTGRKPVDWQIE 313
|
|
| PHA03200 |
PHA03200 |
uracil DNA glycosylase; Provisional |
24-225 |
7.06e-69 |
|
uracil DNA glycosylase; Provisional
Pssm-ID: 165467 Cd Length: 255 Bit Score: 211.89 E-value: 7.06e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492167823 24 QEILDFVKKERKAGkIIYPPQKDIFNALKLTPYEAVKVVILGQDPYHGpNQAHGLAFSVRPGVPAPPSLQNIFKELHADL 103
Cdd:PHA03200 51 RRIVDAVDRDRQRL-TVYPPPEDVHRWSRLCSPEDVKVVIVGQDPYHD-GSACGLAFGTVRGRSAPPSLKNVFRELERTV 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492167823 104 -GVSIPSHGFLEKWAKQGVLLLNAALTVEAGKPQSHANIGWHRFTDKVIESLNDHPEGIVFLLWGSYAQKKSQLITNLRH 182
Cdd:PHA03200 129 pNFSRPDSGCLDSWCRQGVLLLNTVFTVVHGQPGSHEALGWQTLSDRVISRLSEKREHLVFMLWGAQAQKLEYLIDSRKH 208
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 492167823 183 RILKAPHPSP--LSAARGFLGCRHFSKANQLLHEMGRGEIDWALD 225
Cdd:PHA03200 209 LILKSAHPSPrvKGARTPFIGNNHFVLANEYLSTHGKRPIDWNIL 253
|
|
| PHA03199 |
PHA03199 |
uracil DNA glycosylase; Provisional |
10-224 |
4.99e-68 |
|
uracil DNA glycosylase; Provisional
Pssm-ID: 165466 Cd Length: 304 Bit Score: 211.40 E-value: 4.99e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492167823 10 WQTVLGEEKQEPYFQEILDFVKKERKAGKIIYPPQKDIFNALKLTPYEAVKVVILGQDPYHGPNQAHGLAFSVRPGVPAP 89
Cdd:PHA03199 91 WHDLLRDEFEEPYAKGIFEEYNQLLNNGEEIFPIKGDIFAWTRFCGPEKIRVVIIGQDPYHGAGHAHGLAFSVKRGIPIP 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492167823 90 PSLQNIFKELHADL-GVSIPSHGFLEKWAKQGVLLLNAALTVEAGKPQSHANIGWHRFTDKVIESLNDHPEGIVFLLWGS 168
Cdd:PHA03199 171 PSLKNIFAALMESYpHLPLPTHGCLDNWARQGVLLLNTTLTVKRGTPGSHFYLGWDMLIKRMLKRLCENRTGLVFMLWGA 250
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 492167823 169 YAQKKSQliTNLR-HRILKAPHPSPLSAARgFLGCRHFSKANQLLHEMGRGEIDWAL 224
Cdd:PHA03199 251 HAQKTIQ--PNPRcHLVLTHAHPSPLSRSE-FRNCKHFLQANEYFLKKGEPEIDWSI 304
|
|
| PHA03204 |
PHA03204 |
uracil DNA glycosylase; Provisional |
10-224 |
8.52e-68 |
|
uracil DNA glycosylase; Provisional
Pssm-ID: 165471 Cd Length: 322 Bit Score: 211.36 E-value: 8.52e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492167823 10 WQTVLGEEKQEPYFQEILdfVKKERKAG-KIIYPPQKDIFNALKLTPYEAVKVVILGQDPYHGPNQAHGLAFSVRPGVPA 88
Cdd:PHA03204 106 WKEILLPELCCPTGSKIL--AEYERRARyEEVYPPKSDIFAWTRYCAPDHVKVVIVGQDPYANPGQAHGLAFSVKPGSPI 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492167823 89 PPSLQNIFKELHADL-GVSIPSHGFLEKWAKQGVLLLNAALTVEAGKPQSHANIGWHRFTDKVIESLNDHPEGIVFLLWG 167
Cdd:PHA03204 184 PPSLKNILAAVKACYpSIELGSHGCLEDWAKRGVLLLNSVLTVKRGDPGSHHSVGWQILVRNVLRRLSQSTRGIVFMLWG 263
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 492167823 168 SYAQKKS-QLITNLRHRILKAPHPSPLSaARGFLGCRHFSKANQLLHEMGRGEIDWAL 224
Cdd:PHA03204 264 AQAQTMYfQTDNDDRHLVLKYSHPSPLS-RKPFAHCTHFKDANEFLCKMGKGAIDWSL 320
|
|
| PHA03201 |
PHA03201 |
uracil DNA glycosylase; Provisional |
10-223 |
4.61e-64 |
|
uracil DNA glycosylase; Provisional
Pssm-ID: 165468 Cd Length: 318 Bit Score: 201.66 E-value: 4.61e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492167823 10 WQTVLGEEKQEPYFQEILDFVKKERKAGKIIyPPQKDIFNALKLTPYEAVKVVILGQDPYHGPNQAHGLAFSVRPGVPAP 89
Cdd:PHA03201 106 WRPLLEPELANPLTARLMAEYERRCRTEEVL-PPREDVFSWTRYCTPDEVRVVIIGQDPYHQPGQAHGLAFSVRPGTPAP 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492167823 90 PSLQNIF---KELHADLGVSipSHGFLEKWAKQGVLLLNAALTVEAGKPQSHANIGWHRFTDKVIESLNDHPEGIVFLLW 166
Cdd:PHA03201 185 PSLRNILaavRNCCPDARMS--GHGCLEKWARGGVLLLNTTLTVRRGEPASHAKIGWDRFVGSVVRRLAASRPGLVFMLW 262
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 492167823 167 GSYAQkkSQLITNLR-HRILKAPHPSPLSAARgFLGCRHFSKANQLLHEMGRGEIDWA 223
Cdd:PHA03201 263 GAHAQ--NAIRPDPRvHRVLTYSHPSPLSKVP-FGSCRHFCLANQYLRERSLAPIDWS 317
|
|
| UDG-F1-like |
cd19371 |
Uracil DNA glycosylase family 1, includes Human uracil DNA glycosylase, Vaccinia virus protein ... |
61-194 |
1.02e-54 |
|
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: 171.36 E-value: 1.02e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492167823 61 VVILGQDPYHGPNQAHGLAFSVRPGVPAPPSLQNIFKELHADLGV-SIPSHGFLEKWAKQGVLLLNAALTVEAGKPQSHA 139
Cdd:cd19371 1 VVIIGQDPYPSPGHAGGLAFSVTSEVPPPKSLRNIYKELERDYSSfLPPGNGTLEFWARQGVLLLNAALTCESGKPKSHY 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 492167823 140 nIGWHRFTDKVIESLNDHPEGIVFLLWGSYAQKKSQLITNLRHRILKAPHPSPLS 194
Cdd:cd19371 81 -LLWEPFIKAFIRYISAHNKGLVFLLFGSDAQKLRKKINGRNVHVFKADHPSPAD 134
|
|
| UDG |
smart00986 |
Uracil DNA glycosylase superfamily; |
53-212 |
2.14e-35 |
|
Uracil DNA glycosylase superfamily;
Pssm-ID: 214956 Cd Length: 156 Bit Score: 122.88 E-value: 2.14e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492167823 53 LTPYEAVKVVILGQDPY------HGP-NQAHGLAFSVRPGV----PAPPSLQNIFKELHADlgvsiPSHGFLEKWAKQGV 121
Cdd:smart00986 2 GTGDPNAKVLIVGQAPGaseedrGGPfVGAAGLLLSVMLGVaglpRLPPYLTNIVKCRPPD-----AGNRRPTSWELQGC 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492167823 122 LLlnAALTVEAGKPQSHANIGWHRFTDKVIESLNDHPegIVFLLWGSYAQKKSQLitnlrHRILKAPHPSPLSAARgfLG 201
Cdd:smart00986 77 LL--PWLTVELALARPHLILLLGKFAAQALLGLLRRP--LVFGLRGRVAQLKGKG-----HRVLPLPHPSPLNRNF--FP 145
|
170
....*....|.
gi 492167823 202 CRHFSKANQLL 212
Cdd:smart00986 146 AKKFAAWNDLL 156
|
|
| UDG |
pfam03167 |
Uracil DNA glycosylase superfamily; |
57-209 |
1.01e-20 |
|
Uracil DNA glycosylase superfamily;
Pssm-ID: 397331 Cd Length: 154 Bit Score: 84.71 E-value: 1.01e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492167823 57 EAVKVVILGQDPYHGpNQAHGLAFSVRPGvpappslqNIFKELHADLGVSIPSHgflekwAKQGVLLLNAALTV--EAGK 134
Cdd:pfam03167 6 PNAKVLIVGEAPGAD-EDATGLPFVGRAG--------NLLWKLLNAAGLTRDLF------SPQGVYITNVVKCRpgNRRK 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492167823 135 PQSHA-NIGWhRFTDKVIESLNDHpegiVFLLWGSYAQK---KSQLITNLR--------HRILKAPHPSPLSAARgflgC 202
Cdd:pfam03167 71 PTSHEiDACW-PYLEAEIELLRPR----VIVLLGKTAAKallGLKKITKLRgklidlkgIPVLPTPHPSPLLRNK----L 141
|
....*..
gi 492167823 203 RHFSKAN 209
Cdd:pfam03167 142 NPFLKAN 148
|
|
| UDG-like |
cd09593 |
uracil-DNA glycosylases (UDG) and related enzymes; Uracil-DNA glycosylases (UDGs) initiate ... |
61-195 |
8.51e-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: 78.97 E-value: 8.51e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492167823 61 VVILGQDPYHGPNQAHglafsvrpGVPAPPSLQNIFKELHADlgvsipshGFLEKWAKQGVLLLNAALTVEAGKPQSHaN 140
Cdd:cd09593 1 VLIVGQNPGPHGARAG--------GVPPGPSGNRLWRLLAAA--------GGTPRLFRYGVGLTNTVPRGPPGAAAGS-E 63
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 492167823 141 IGWHRFTDKVIESLNDHPEGIVFLLWGSYAQKK-------SQLITNLRHRILKAPHPSPLSA 195
Cdd:cd09593 64 KKELRFCGRWLRKLLELLNPRVVVLLGKKAQEAylavltsSKGAPGKGTEVLVLPHPSPRNR 125
|
|
| UDG-F1_NsUNG-like |
cd19373 |
Uracil DNA glycosylase family 1 subfamily, includes Nitratifractor salsuginis UNG and similar ... |
62-190 |
2.81e-05 |
|
Uracil DNA glycosylase family 1 subfamily, includes 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. Nitratifractor salsuginis UNG (NsaUNG) only exhibits robust enzymatic activity on uracil-containing DNAs, in particular double-stranded uracil-containing substrates, and does not act on hypoxanthine- and xanthine-containing substrates. NsUNG is not inhibited by Ugi protein that specifically inhibits conventional family 1 UDGs. 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.
Pssm-ID: 381688 Cd Length: 174 Bit Score: 43.28 E-value: 2.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492167823 62 VILGQDPYHGPNQAHGLAF---SVRP---------GVPAPPSLQNIFKELhadlgvsIPSHGFL---------------- 113
Cdd:cd19373 2 ILFGQDPYPREKSATGYAFidgAVKEifspkglskEVNRATSLRNFIKMA-------LVARGSLdpddlsqeaiakldks 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492167823 114 ----------EKWAKQGVLLLNAALTVEA-GKPQSHANiGWHRFTDKVIESLNDHpeGIVFLLWGSYAQKKSQLITNLRH 182
Cdd:cd19373 75 llvdtidelrENFEKSGVLLLNAALLFTSkEESNRHAR-AWRPFIEKLLEGLEAY--GPELILFGAHAKEIKKLKSARGF 151
|
....*...
gi 492167823 183 RILKAPHP 190
Cdd:cd19373 152 PQVELEHP 159
|
|
|