|
Name |
Accession |
Description |
Interval |
E-value |
| Ung |
COG0692 |
Uracil-DNA glycosylase [Replication, recombination and repair]; |
3-215 |
1.02e-132 |
|
Uracil-DNA glycosylase [Replication, recombination and repair];
Pssm-ID: 440456 Cd Length: 221 Bit Score: 371.68 E-value: 1.02e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039332703 3 HSSWHALIKAQLPEGYFGKINQFMEQVYSQG-IIYPPKEKVFQALLTTLLEEVKVVILGQDPYHGPGQAQGLSFSVPDSI 81
Cdd:COG0692 6 EPSWKEALAEEFEKPYFQALGAFLKAEYAAGkTIYPPGEDIFRAFNLTPFDDVKVVILGQDPYHGPGQAHGLSFSVPPGV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039332703 82 PAPPSLQNILKELSDDIGVK--KSHDLTAWAEQGVLLLNACLTVPAGQANGHAGQIWEPFTDAVIQVVNHLDRPVVFVLW 159
Cdd:COG0692 86 PLPPSLRNIYKELEDDLGIPipNHGDLTSWAEQGVLLLNTVLTVRAGQAGSHAGKGWETFTDAVIRALNARKEPVVFLLW 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2039332703 160 GAYARKKKALVTNPHHLIIESAHPSPLSVYRGFWGSKPFSKANAFLKETGQEPIDW 215
Cdd:COG0692 166 GAYAQKKAALIDASKHLVLESPHPSPLSAHRGFFGSKPFSKANAYLEEQGKTPIDW 221
|
|
| PRK05254 |
PRK05254 |
uracil-DNA glycosylase; Provisional |
1-215 |
3.11e-132 |
|
uracil-DNA glycosylase; Provisional
Pssm-ID: 235376 Cd Length: 224 Bit Score: 370.64 E-value: 3.11e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039332703 1 MEHSSWHALIKAQLPEGYFGKINQFMEQVYSQG-IIYPPKEKVFQALLTTLLEEVKVVILGQDPYHGPGQAQGLSFSVPD 79
Cdd:PRK05254 5 LLEPSWKEVLKPEFKKPYFQELLEFLRAERAAGkTIYPPGEDIFRAFNLTPFDDVKVVILGQDPYHGPGQAHGLSFSVPP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039332703 80 SIPAPPSLQNILKELSDDIGVK--KSHDLTAWAEQGVLLLNACLTVPAGQANGHAGQIWEPFTDAVIQVVNHLDRPVVFV 157
Cdd:PRK05254 85 GVPIPPSLRNIFKELEDDLGFPipNHGDLTSWAEQGVLLLNTVLTVEAGQANSHAGKGWETFTDAVIKALNERREPVVFI 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2039332703 158 LWGAYARKKKALVTNPHHLIIESAHPSPLSVYRGFWGSKPFSKANAFLKETGQEPIDW 215
Cdd:PRK05254 165 LWGSHAQKKKALIDNSKHLILESPHPSPLSAHRGFFGSKHFSKANALLKQHGKTPIDW 222
|
|
| UDG-F1-like |
cd10027 |
Uracil DNA glycosylase family 1 subfamily, includes Human uracil DNA glycosylase and similar ... |
18-215 |
3.22e-121 |
|
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: 341.74 E-value: 3.22e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039332703 18 YFGKINQFMEQVYSQGIIYPPKEKVFQALLTTLLEEVKVVILGQDPYHGPGQAQGLSFSVPDSIPAPPSLQNILKELSDD 97
Cdd:cd10027 1 YFKKLEAFLEEEYKKKTIYPPKEDIFRAFELTPLDDVKVVILGQDPYHGPGQAHGLAFSVPPGVKIPPSLRNIFKELKSD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039332703 98 IGVK--KSHDLTAWAEQGVLLLNACLTVPAGQANGHAGQIWEPFTDAVIQVVNHLDRPVVFVLWGAYARKKKALVTNPHH 175
Cdd:cd10027 81 LGIFppKHGDLSSWAKQGVLLLNTVLTVEAGKPGSHKNIGWETFTDAVIKALSEKNENVVFLLWGNHAQKKKKLIDKKKH 160
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2039332703 176 LIIESAHPSPLSVYRGFWGSKPFSKANAFLKETGQEPIDW 215
Cdd:cd10027 161 LVLESSHPSPLSAYRGFFGSKHFSKANEYLKKHGKKPIDW 200
|
|
| ung |
TIGR00628 |
uracil-DNA glycosylase; All proteins in this family for which functions are known are ... |
3-210 |
6.85e-112 |
|
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: 318.77 E-value: 6.85e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039332703 3 HSSWHALIKAQLPEGYFGKINQFMEQVYSQGIIYPPKEKVFQALLTTLLEEVKVVILGQDPYHGPGQAQGLSFSVPDSIP 82
Cdd:TIGR00628 1 SPSWRAFLQPEFKKPYFQELLAFYKRERAQETVYPPKEDVFAWTRLCPPEDVKVVILGQDPYHGPGQAHGLAFSVKRGVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039332703 83 APPSLQNILKELSDDIG---VKKSHDLTAWAEQGVLLLNACLTVPAGQANGHAGQIWEPFTDAVIQVVNHLDRPVVFVLW 159
Cdd:TIGR00628 81 IPPSLKNIFKELEADYPdfpPPKHGCLEAWARQGVLLLNTVLTVRRGQPGSHSGLGWERFTDAVISRLSERLDGLVFMLW 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2039332703 160 GAYARKKKALVTNPHHLIIESAHPSPLSVYRGFWGSKPFSKANAFLKETGQ 210
Cdd:TIGR00628 161 GAHAQKKKSLIDAKKHLVLKSPHPSPLSARRGFFGCRHFSKANEYLEKHGK 211
|
|
| UDG |
smart00986 |
Uracil DNA glycosylase superfamily; |
49-205 |
5.73e-27 |
|
Uracil DNA glycosylase superfamily;
Pssm-ID: 214956 Cd Length: 156 Bit Score: 100.92 E-value: 5.73e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039332703 49 TLLEEVKVVILGQDPYHGPGQAQ-------GLSFSVP----DSIPAPPSLQNILKELSDDIGVKkshDLTAWAEQGVLLl 117
Cdd:smart00986 3 TGDPNAKVLIVGQAPGASEEDRGgpfvgaaGLLLSVMlgvaGLPRLPPYLTNIVKCRPPDAGNR---RPTSWELQGCLL- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039332703 118 nACLTVPAGQANGHAGQIWEPFTDAVIqvVNHLDRPVVFVLWGAYARKKkalvtNPHHLIIESAHPSPLSvyRGFWGSKP 197
Cdd:smart00986 79 -PWLTVELALARPHLILLLGKFAAQAL--LGLLRRPLVFGLRGRVAQLK-----GKGHRVLPLPHPSPLN--RNFFPAKK 148
|
....*...
gi 2039332703 198 FSKANAFL 205
Cdd:smart00986 149 FAAWNDLL 156
|
|
| UDG |
pfam03167 |
Uracil DNA glycosylase superfamily; |
52-204 |
1.84e-21 |
|
Uracil DNA glycosylase superfamily;
Pssm-ID: 397331 Cd Length: 154 Bit Score: 86.25 E-value: 1.84e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039332703 52 EEVKVVILGQDPYHGpGQAQGLSFSVPDSipappslqNILKELSDDIGVKKSHDltawAEQGVLLLNACLTVP--AGQAN 129
Cdd:pfam03167 6 PNAKVLIVGEAPGAD-EDATGLPFVGRAG--------NLLWKLLNAAGLTRDLF----SPQGVYITNVVKCRPgnRRKPT 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039332703 130 GHAGQIWEPFTDAVIQVVnhldRPVVFVLWGAYARKK-----------KALVTNPHHLIIESAHPSPLSVyrgfWGSKPF 198
Cdd:pfam03167 73 SHEIDACWPYLEAEIELL----RPRVIVLLGKTAAKAllglkkitklrGKLIDLKGIPVLPTPHPSPLLR----NKLNPF 144
|
....*.
gi 2039332703 199 SKANAF 204
Cdd:pfam03167 145 LKANAW 150
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Ung |
COG0692 |
Uracil-DNA glycosylase [Replication, recombination and repair]; |
3-215 |
1.02e-132 |
|
Uracil-DNA glycosylase [Replication, recombination and repair];
Pssm-ID: 440456 Cd Length: 221 Bit Score: 371.68 E-value: 1.02e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039332703 3 HSSWHALIKAQLPEGYFGKINQFMEQVYSQG-IIYPPKEKVFQALLTTLLEEVKVVILGQDPYHGPGQAQGLSFSVPDSI 81
Cdd:COG0692 6 EPSWKEALAEEFEKPYFQALGAFLKAEYAAGkTIYPPGEDIFRAFNLTPFDDVKVVILGQDPYHGPGQAHGLSFSVPPGV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039332703 82 PAPPSLQNILKELSDDIGVK--KSHDLTAWAEQGVLLLNACLTVPAGQANGHAGQIWEPFTDAVIQVVNHLDRPVVFVLW 159
Cdd:COG0692 86 PLPPSLRNIYKELEDDLGIPipNHGDLTSWAEQGVLLLNTVLTVRAGQAGSHAGKGWETFTDAVIRALNARKEPVVFLLW 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2039332703 160 GAYARKKKALVTNPHHLIIESAHPSPLSVYRGFWGSKPFSKANAFLKETGQEPIDW 215
Cdd:COG0692 166 GAYAQKKAALIDASKHLVLESPHPSPLSAHRGFFGSKPFSKANAYLEEQGKTPIDW 221
|
|
| PRK05254 |
PRK05254 |
uracil-DNA glycosylase; Provisional |
1-215 |
3.11e-132 |
|
uracil-DNA glycosylase; Provisional
Pssm-ID: 235376 Cd Length: 224 Bit Score: 370.64 E-value: 3.11e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039332703 1 MEHSSWHALIKAQLPEGYFGKINQFMEQVYSQG-IIYPPKEKVFQALLTTLLEEVKVVILGQDPYHGPGQAQGLSFSVPD 79
Cdd:PRK05254 5 LLEPSWKEVLKPEFKKPYFQELLEFLRAERAAGkTIYPPGEDIFRAFNLTPFDDVKVVILGQDPYHGPGQAHGLSFSVPP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039332703 80 SIPAPPSLQNILKELSDDIGVK--KSHDLTAWAEQGVLLLNACLTVPAGQANGHAGQIWEPFTDAVIQVVNHLDRPVVFV 157
Cdd:PRK05254 85 GVPIPPSLRNIFKELEDDLGFPipNHGDLTSWAEQGVLLLNTVLTVEAGQANSHAGKGWETFTDAVIKALNERREPVVFI 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2039332703 158 LWGAYARKKKALVTNPHHLIIESAHPSPLSVYRGFWGSKPFSKANAFLKETGQEPIDW 215
Cdd:PRK05254 165 LWGSHAQKKKALIDNSKHLILESPHPSPLSAHRGFFGSKHFSKANALLKQHGKTPIDW 222
|
|
| UDG-F1-like |
cd10027 |
Uracil DNA glycosylase family 1 subfamily, includes Human uracil DNA glycosylase and similar ... |
18-215 |
3.22e-121 |
|
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: 341.74 E-value: 3.22e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039332703 18 YFGKINQFMEQVYSQGIIYPPKEKVFQALLTTLLEEVKVVILGQDPYHGPGQAQGLSFSVPDSIPAPPSLQNILKELSDD 97
Cdd:cd10027 1 YFKKLEAFLEEEYKKKTIYPPKEDIFRAFELTPLDDVKVVILGQDPYHGPGQAHGLAFSVPPGVKIPPSLRNIFKELKSD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039332703 98 IGVK--KSHDLTAWAEQGVLLLNACLTVPAGQANGHAGQIWEPFTDAVIQVVNHLDRPVVFVLWGAYARKKKALVTNPHH 175
Cdd:cd10027 81 LGIFppKHGDLSSWAKQGVLLLNTVLTVEAGKPGSHKNIGWETFTDAVIKALSEKNENVVFLLWGNHAQKKKKLIDKKKH 160
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2039332703 176 LIIESAHPSPLSVYRGFWGSKPFSKANAFLKETGQEPIDW 215
Cdd:cd10027 161 LVLESSHPSPLSAYRGFFGSKHFSKANEYLKKHGKKPIDW 200
|
|
| ung |
TIGR00628 |
uracil-DNA glycosylase; All proteins in this family for which functions are known are ... |
3-210 |
6.85e-112 |
|
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: 318.77 E-value: 6.85e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039332703 3 HSSWHALIKAQLPEGYFGKINQFMEQVYSQGIIYPPKEKVFQALLTTLLEEVKVVILGQDPYHGPGQAQGLSFSVPDSIP 82
Cdd:TIGR00628 1 SPSWRAFLQPEFKKPYFQELLAFYKRERAQETVYPPKEDVFAWTRLCPPEDVKVVILGQDPYHGPGQAHGLAFSVKRGVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039332703 83 APPSLQNILKELSDDIG---VKKSHDLTAWAEQGVLLLNACLTVPAGQANGHAGQIWEPFTDAVIQVVNHLDRPVVFVLW 159
Cdd:TIGR00628 81 IPPSLKNIFKELEADYPdfpPPKHGCLEAWARQGVLLLNTVLTVRRGQPGSHSGLGWERFTDAVISRLSERLDGLVFMLW 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2039332703 160 GAYARKKKALVTNPHHLIIESAHPSPLSVYRGFWGSKPFSKANAFLKETGQ 210
Cdd:TIGR00628 161 GAHAQKKKSLIDAKKHLVLKSPHPSPLSARRGFFGCRHFSKANEYLEKHGK 211
|
|
| PHA03347 |
PHA03347 |
uracil DNA glycosylase; Provisional |
32-215 |
1.30e-55 |
|
uracil DNA glycosylase; Provisional
Pssm-ID: 177588 Cd Length: 252 Bit Score: 177.55 E-value: 1.30e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039332703 32 QGIIYPPKEKVFQALLTTLLEEVKVVILGQDPYHGpGQAQGLSFSVPDSIPAPPSLQNILKEL--SDDIGVKKSHD-LTA 108
Cdd:PHA03347 57 QTVIYPPEDRIMAWSYLCDPEDIKVVILGQDPYHG-GQANGLAFSVAYGFPVPPSLRNIFAELhrSVPDFSPPDHGcLDA 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039332703 109 WAEQGVLLLNACLTVPAGQANGHAGQIWEPFTDAVIQVV-NHLDRpVVFVLWGAYARKKKALVTNPHHLIIESAHPSPL- 186
Cdd:PHA03347 136 WARQGVLLLNTILTVEKGKPGSHSDLGWAWFTDYIISSLsEKLKA-CVFMLWGSKAIDKASLINSQKHLVLKAQHPSPLa 214
|
170 180 190
....*....|....*....|....*....|....*
gi 2039332703 187 --SVYRGFW----GSKPFSKANAFLKETGQEPIDW 215
Cdd:PHA03347 215 anSTRSSTWpkflGCNHFVLANKYLTQHGKGPIDW 249
|
|
| PHA03202 |
PHA03202 |
uracil DNA glycosylase; Provisional |
5-216 |
2.08e-52 |
|
uracil DNA glycosylase; Provisional
Pssm-ID: 165469 Cd Length: 313 Bit Score: 171.03 E-value: 2.08e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039332703 5 SWHALIKAQLPEGYFGKI-NQFMEQVYSQGIiYPPKEKVFQALLTTLLEEVKVVILGQDPYHGPGQAQGLSFSVPDSIPA 83
Cdd:PHA03202 99 SWRPILEREMQQPYVRLLlNEYKLRCAREEV-FPPKEDIFAWTRFSPPEKVRVVIVGQDPYHAPGQAHGLAFSVRKGVPV 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039332703 84 PPSLQNILKelsddiGVKKSHD---------LTAWAEQGVLLLNACLTVPAGQANGHAGQIWEPFTDAVIQVVNHLDRPV 154
Cdd:PHA03202 178 PPSLRNIYS------AVQKSYPsfrppmhgfLEKWAEQGVLLINTTLTVARGKPGSHATLGWHRLVRAVIDRLCTTSQGL 251
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2039332703 155 VFVLWGAYARKKKAlVTNPHHLIIESAHPSPLSVYrGFWGSKPFSKANAFLKETGQEPIDWL 216
Cdd:PHA03202 252 VFMLWGAHAQKSCS-PNRQHHLVLTYGHPSPLSRV-NFRDCPHFLEANAYLTKTGRKPVDWQ 311
|
|
| PHA03200 |
PHA03200 |
uracil DNA glycosylase; Provisional |
33-215 |
8.36e-50 |
|
uracil DNA glycosylase; Provisional
Pssm-ID: 165467 Cd Length: 255 Bit Score: 162.59 E-value: 8.36e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039332703 33 GIIYPPKEKVFQALLTTLLEEVKVVILGQDPYHGpGQAQGLSFSVPDSIPAPPSLQNILKELS---DDIGVKKSHDLTAW 109
Cdd:PHA03200 64 LTVYPPPEDVHRWSRLCSPEDVKVVIVGQDPYHD-GSACGLAFGTVRGRSAPPSLKNVFRELErtvPNFSRPDSGCLDSW 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039332703 110 AEQGVLLLNACLTVPAGQANGHAGQIWEPFTDAVIQVVNHLDRPVVFVLWGAYARKKKALVTNPHHLIIESAHPSP--LS 187
Cdd:PHA03200 143 CRQGVLLLNTVFTVVHGQPGSHEALGWQTLSDRVISRLSEKREHLVFMLWGAQAQKLEYLIDSRKHLILKSAHPSPrvKG 222
|
170 180
....*....|....*....|....*...
gi 2039332703 188 VYRGFWGSKPFSKANAFLKETGQEPIDW 215
Cdd:PHA03200 223 ARTPFIGNNHFVLANEYLSTHGKRPIDW 250
|
|
| PHA03204 |
PHA03204 |
uracil DNA glycosylase; Provisional |
35-215 |
3.52e-44 |
|
uracil DNA glycosylase; Provisional
Pssm-ID: 165471 Cd Length: 322 Bit Score: 150.11 E-value: 3.52e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039332703 35 IYPPKEKVFQALLTTLLEEVKVVILGQDPYHGPGQAQGLSFSVPDSIPAPPSLQNILKEL-----SDDIGvkkSHD-LTA 108
Cdd:PHA03204 135 VYPPKSDIFAWTRYCAPDHVKVVIVGQDPYANPGQAHGLAFSVKPGSPIPPSLKNILAAVkacypSIELG---SHGcLED 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039332703 109 WAEQGVLLLNACLTVPAGQANGHAGQIWEPFTDAVIQVVNHLDRPVVFVLWGAYARKKKALVTNP-HHLIIESAHPSPLS 187
Cdd:PHA03204 212 WAKRGVLLLNSVLTVKRGDPGSHHSVGWQILVRNVLRRLSQSTRGIVFMLWGAQAQTMYFQTDNDdRHLVLKYSHPSPLS 291
|
170 180
....*....|....*....|....*...
gi 2039332703 188 vYRGFWGSKPFSKANAFLKETGQEPIDW 215
Cdd:PHA03204 292 -RKPFAHCTHFKDANEFLCKMGKGAIDW 318
|
|
| UDG-F1-like |
cd19371 |
Uracil DNA glycosylase family 1, includes Human uracil DNA glycosylase, Vaccinia virus protein ... |
56-187 |
6.24e-44 |
|
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: 143.63 E-value: 6.24e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039332703 56 VVILGQDPYHGPGQAQGLSFSVPDSIPAPPSLQNILKELSDDIGVKKS---HDLTAWAEQGVLLLNACLTVPAGQANGHa 132
Cdd:cd19371 1 VVIIGQDPYPSPGHAGGLAFSVTSEVPPPKSLRNIYKELERDYSSFLPpgnGTLEFWARQGVLLLNAALTCESGKPKSH- 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 2039332703 133 GQIWEPFTDAVIQVVNHLDRPVVFVLWGAYARKKKALVTNPHHLIIESAHPSPLS 187
Cdd:cd19371 80 YLLWEPFIKAFIRYISAHNKGLVFLLFGSDAQKLRKKINGRNVHVFKADHPSPAD 134
|
|
| PHA03201 |
PHA03201 |
uracil DNA glycosylase; Provisional |
35-215 |
9.82e-43 |
|
uracil DNA glycosylase; Provisional
Pssm-ID: 165468 Cd Length: 318 Bit Score: 146.19 E-value: 9.82e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039332703 35 IYPPKEKVFQALLTTLLEEVKVVILGQDPYHGPGQAQGLSFSVPDSIPAPPSLQNIL---KELSDDIGVKKSHDLTAWAE 111
Cdd:PHA03201 135 VLPPREDVFSWTRYCTPDEVRVVIIGQDPYHQPGQAHGLAFSVRPGTPAPPSLRNILaavRNCCPDARMSGHGCLEKWAR 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039332703 112 QGVLLLNACLTVPAGQANGHAGQIWEPFTDAVIQVVNhLDRP-VVFVLWGAYArkKKALVTNPH-HLIIESAHPSPLSVY 189
Cdd:PHA03201 215 GGVLLLNTTLTVRRGEPASHAKIGWDRFVGSVVRRLA-ASRPgLVFMLWGAHA--QNAIRPDPRvHRVLTYSHPSPLSKV 291
|
170 180
....*....|....*....|....*.
gi 2039332703 190 RgFWGSKPFSKANAFLKETGQEPIDW 215
Cdd:PHA03201 292 P-FGSCRHFCLANQYLRERSLAPIDW 316
|
|
| PHA03199 |
PHA03199 |
uracil DNA glycosylase; Provisional |
6-215 |
1.05e-41 |
|
uracil DNA glycosylase; Provisional
Pssm-ID: 165466 Cd Length: 304 Bit Score: 143.22 E-value: 1.05e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039332703 6 WHALIKAQLPEGYFGKI-NQFMEQVYSQGIIYPPKEKVFQALLTTLLEEVKVVILGQDPYHGPGQAQGLSFSVPDSIPAP 84
Cdd:PHA03199 91 WHDLLRDEFEEPYAKGIfEEYNQLLNNGEEIFPIKGDIFAWTRFCGPEKIRVVIIGQDPYHGAGHAHGLAFSVKRGIPIP 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039332703 85 PSLQNI---LKELSDDIGVKKSHDLTAWAEQGVLLLNACLTVPAGQANGHAGQIWEPFTDAVIQVVNHLDRPVVFVLWGA 161
Cdd:PHA03199 171 PSLKNIfaaLMESYPHLPLPTHGCLDNWARQGVLLLNTTLTVKRGTPGSHFYLGWDMLIKRMLKRLCENRTGLVFMLWGA 250
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2039332703 162 YArkKKALVTNPH-HLIIESAHPSPLSVYRgFWGSKPFSKANAFLKETGQEPIDW 215
Cdd:PHA03199 251 HA--QKTIQPNPRcHLVLTHAHPSPLSRSE-FRNCKHFLQANEYFLKKGEPEIDW 302
|
|
| UDG |
smart00986 |
Uracil DNA glycosylase superfamily; |
49-205 |
5.73e-27 |
|
Uracil DNA glycosylase superfamily;
Pssm-ID: 214956 Cd Length: 156 Bit Score: 100.92 E-value: 5.73e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039332703 49 TLLEEVKVVILGQDPYHGPGQAQ-------GLSFSVP----DSIPAPPSLQNILKELSDDIGVKkshDLTAWAEQGVLLl 117
Cdd:smart00986 3 TGDPNAKVLIVGQAPGASEEDRGgpfvgaaGLLLSVMlgvaGLPRLPPYLTNIVKCRPPDAGNR---RPTSWELQGCLL- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039332703 118 nACLTVPAGQANGHAGQIWEPFTDAVIqvVNHLDRPVVFVLWGAYARKKkalvtNPHHLIIESAHPSPLSvyRGFWGSKP 197
Cdd:smart00986 79 -PWLTVELALARPHLILLLGKFAAQAL--LGLLRRPLVFGLRGRVAQLK-----GKGHRVLPLPHPSPLN--RNFFPAKK 148
|
....*...
gi 2039332703 198 FSKANAFL 205
Cdd:smart00986 149 FAAWNDLL 156
|
|
| UDG |
pfam03167 |
Uracil DNA glycosylase superfamily; |
52-204 |
1.84e-21 |
|
Uracil DNA glycosylase superfamily;
Pssm-ID: 397331 Cd Length: 154 Bit Score: 86.25 E-value: 1.84e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039332703 52 EEVKVVILGQDPYHGpGQAQGLSFSVPDSipappslqNILKELSDDIGVKKSHDltawAEQGVLLLNACLTVP--AGQAN 129
Cdd:pfam03167 6 PNAKVLIVGEAPGAD-EDATGLPFVGRAG--------NLLWKLLNAAGLTRDLF----SPQGVYITNVVKCRPgnRRKPT 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039332703 130 GHAGQIWEPFTDAVIQVVnhldRPVVFVLWGAYARKK-----------KALVTNPHHLIIESAHPSPLSVyrgfWGSKPF 198
Cdd:pfam03167 73 SHEIDACWPYLEAEIELL----RPRVIVLLGKTAAKAllglkkitklrGKLIDLKGIPVLPTPHPSPLLR----NKLNPF 144
|
....*.
gi 2039332703 199 SKANAF 204
Cdd:pfam03167 145 LKANAW 150
|
|
| UDG-like |
cd09593 |
uracil-DNA glycosylases (UDG) and related enzymes; Uracil-DNA glycosylases (UDGs) initiate ... |
56-187 |
3.86e-17 |
|
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: 74.35 E-value: 3.86e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039332703 56 VVILGQDPYHGPGQAQGlsfsvpdsIPAPPSLQNILKELSDDIGVKKshdltaWAEQGVLLLNACLTVPAGQANGHAGQi 135
Cdd:cd09593 1 VLIVGQNPGPHGARAGG--------VPPGPSGNRLWRLLAAAGGTPR------LFRYGVGLTNTVPRGPPGAAAGSEKK- 65
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 2039332703 136 WEPFTDAVIQVVNHLDRPVVFVLWGAYARK--KKALVTNPH-----HLIIESAHPSPLS 187
Cdd:cd09593 66 ELRFCGRWLRKLLELLNPRVVVLLGKKAQEayLAVLTSSKGapgkgTEVLVLPHPSPRN 124
|
|
| UDG_F1_VAVC_D4-like |
cd19372 |
Uracil DNA glycosylase family 1 subfamily, includes Vaccinia virus protein D4 and similar ... |
37-217 |
5.28e-06 |
|
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: 45.51 E-value: 5.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039332703 37 PPKEKVFqALLTTLLEEVKVVILGQDPYhgPGQAQGLSFSVPDSipAPPSLQNILKELSDDIGVK--KSHDLTAwaEQGV 114
Cdd:cd19372 26 PIPENFF-KQLKQPLRDKRVCICGIDPY--PTDATGVPFESPDF--SKKTIRAIAEAISRRTGVSlyKGYNFAL--VEGV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039332703 115 LLLNACLTVPAGQANGHAgQIWEPFTDAVIQvvnHLDR--PVVFVLWGAYARKKKALVTNPHHLIIeSAHPSPLSvyRGF 192
Cdd:cd19372 99 LAWNYYLSCREGETKSHA-IHWERISKLLLQ---HIAKyvSVLYCLGKTDFSNVRARLEVPVTVVV-GYHPAARD--GQF 171
|
170 180
....*....|....*....|....*
gi 2039332703 193 WGSKPFSKANAFLKETGQEPIDWLR 217
Cdd:cd19372 172 DKERAFEIVNVLLELNGKPPVNWAQ 196
|
|
| |
