|
Name |
Accession |
Description |
Interval |
E-value |
| Ung |
COG0692 |
Uracil-DNA glycosylase [Replication, recombination and repair]; |
12-224 |
6.11e-124 |
|
Uracil-DNA glycosylase [Replication, recombination and repair];
Pssm-ID: 440456 Cd Length: 221 Bit Score: 350.11 E-value: 6.11e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488909751 12 DWYQHLKPVLGLDYLNQINDFLNKAYTGPLRVFPPEDKIFSAMLYTSLANTKVVIVGQDPYHELGQAQGLSFSVPDNFPA 91
Cdd:COG0692 8 SWKEALAEEFEKPYFQALGAFLKAEYAAGKTIYPPGEDIFRAFNLTPFDDVKVVILGQDPYHGPGQAHGLSFSVPPGVPL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488909751 92 PSSLQNIHKEIASDLGKTRNSH-DLIPWAKQGVLLLNSVLTVEEHKANSHAGMIWEKFTDSVIQLASAEPQPKVFILWGN 170
Cdd:COG0692 88 PPSLRNIYKELEDDLGIPIPNHgDLTSWAEQGVLLLNTVLTVRAGQAGSHAGKGWETFTDAVIRALNARKEPVVFLLWGA 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 488909751 171 FARRKAVLINPKKDLIIQSAHPSGFSANRGFFGSKPFSQTNSWLLSHDRTAIDW 224
Cdd:COG0692 168 YAQKKAALIDASKHLVLESPHPSPLSAHRGFFGSKPFSKANAYLEEQGKTPIDW 221
|
|
| PRK05254 |
PRK05254 |
uracil-DNA glycosylase; Provisional |
7-224 |
2.91e-115 |
|
uracil-DNA glycosylase; Provisional
Pssm-ID: 235376 Cd Length: 224 Bit Score: 328.27 E-value: 2.91e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488909751 7 NLKKTDWYQHLKPVLGLDYLNQINDFLNKAYTGPLRVFPPEDKIFSAMLYTSLANTKVVIVGQDPYHELGQAQGLSFSVP 86
Cdd:PRK05254 4 MLLEPSWKEVLKPEFKKPYFQELLEFLRAERAAGKTIYPPGEDIFRAFNLTPFDDVKVVILGQDPYHGPGQAHGLSFSVP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488909751 87 DNFPAPSSLQNIHKEIASDLGKTRNSH-DLIPWAKQGVLLLNSVLTVEEHKANSHAGMIWEKFTDSVIQLASAEPQPKVF 165
Cdd:PRK05254 84 PGVPIPPSLRNIFKELEDDLGFPIPNHgDLTSWAEQGVLLLNTVLTVEAGQANSHAGKGWETFTDAVIKALNERREPVVF 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 488909751 166 ILWGNFARRKAVLINPKKDLIIQSAHPSGFSANRGFFGSKPFSQTNSWLLSHDRTAIDW 224
Cdd:PRK05254 164 ILWGSHAQKKKALIDNSKHLILESPHPSPLSAHRGFFGSKHFSKANALLKQHGKTPIDW 222
|
|
| UDG-F1-like |
cd10027 |
Uracil DNA glycosylase family 1 subfamily, includes Human uracil DNA glycosylase and similar ... |
25-224 |
9.24e-110 |
|
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: 313.23 E-value: 9.24e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488909751 25 YLNQINDFLNKAYTGPlRVFPPEDKIFSAMLYTSLANTKVVIVGQDPYHELGQAQGLSFSVPDNFPAPSSLQNIHKEIAS 104
Cdd:cd10027 1 YFKKLEAFLEEEYKKK-TIYPPKEDIFRAFELTPLDDVKVVILGQDPYHGPGQAHGLAFSVPPGVKIPPSLRNIFKELKS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488909751 105 DLGKTRNSH-DLIPWAKQGVLLLNSVLTVEEHKANSHAGMIWEKFTDSVIQLASAEPQPKVFILWGNFARRKAVLINPKK 183
Cdd:cd10027 80 DLGIFPPKHgDLSSWAKQGVLLLNTVLTVEAGKPGSHKNIGWETFTDAVIKALSEKNENVVFLLWGNHAQKKKKLIDKKK 159
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 488909751 184 DLIIQSAHPSGFSANRGFFGSKPFSQTNSWLLSHDRTAIDW 224
Cdd:cd10027 160 HLVLESSHPSPLSAYRGFFGSKHFSKANEYLKKHGKKPIDW 200
|
|
| ung |
TIGR00628 |
uracil-DNA glycosylase; All proteins in this family for which functions are known are ... |
12-219 |
2.86e-89 |
|
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: 261.76 E-value: 2.86e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488909751 12 DWYQHLKPVLGLDYLNQINDFLNKAYTGpLRVFPPEDKIFSAMLYTSLANTKVVIVGQDPYHELGQAQGLSFSVPDNFPA 91
Cdd:TIGR00628 3 SWRAFLQPEFKKPYFQELLAFYKRERAQ-ETVYPPKEDVFAWTRLCPPEDVKVVILGQDPYHGPGQAHGLAFSVKRGVPI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488909751 92 PSSLQNIHKEIASDLGKTR--NSHDLIPWAKQGVLLLNSVLTVEEHKANSHAGMIWEKFTDSVIQLASAEPQPKVFILWG 169
Cdd:TIGR00628 82 PPSLKNIFKELEADYPDFPppKHGCLEAWARQGVLLLNTVLTVRRGQPGSHSGLGWERFTDAVISRLSERLDGLVFMLWG 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 488909751 170 NFARRKAVLINPKKDLIIQSAHPSGFSANRGFFGSKPFSQTNSWLLSHDR 219
Cdd:TIGR00628 162 AHAQKKKSLIDAKKHLVLKSPHPSPLSARRGFFGCRHFSKANEYLEKHGK 211
|
|
| UDG |
smart00986 |
Uracil DNA glycosylase superfamily; |
60-214 |
4.95e-26 |
|
Uracil DNA glycosylase superfamily;
Pssm-ID: 214956 Cd Length: 156 Bit Score: 98.61 E-value: 4.95e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488909751 60 ANTKVVIVGQDPYHELGQAQ-------GLSFSVP----DNFPAPSSLQNIHKEIASDLGKTRNShdliPWAKQGVLLlnS 128
Cdd:smart00986 6 PNAKVLIVGQAPGASEEDRGgpfvgaaGLLLSVMlgvaGLPRLPPYLTNIVKCRPPDAGNRRPT----SWELQGCLL--P 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488909751 129 VLTVEEHKANSHAGMIWEKFTDSVIQLASaePQPKVFILWGNFARRKAVLInpkkdLIIQSAHPSGfsANRGFFGSKPFS 208
Cdd:smart00986 80 WLTVELALARPHLILLLGKFAAQALLGLL--RRPLVFGLRGRVAQLKGKGH-----RVLPLPHPSP--LNRNFFPAKKFA 150
|
....*.
gi 488909751 209 QTNSWL 214
Cdd:smart00986 151 AWNDLL 156
|
|
| UDG |
pfam03167 |
Uracil DNA glycosylase superfamily; |
60-213 |
1.07e-16 |
|
Uracil DNA glycosylase superfamily;
Pssm-ID: 397331 Cd Length: 154 Bit Score: 74.31 E-value: 1.07e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488909751 60 ANTKVVIVGQDPYHElGQAQGLSFSVP--DNFPapsslqnihkEIASDLGKTRNSHdlipwAKQGVLLLNSVLTVEE--H 135
Cdd:pfam03167 6 PNAKVLIVGEAPGAD-EDATGLPFVGRagNLLW----------KLLNAAGLTRDLF-----SPQGVYITNVVKCRPGnrR 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488909751 136 KANSHAGMIWEKFTDSVIQLAsaepQPKVFILWGNFARRKA-----------VLINPKKDLIIQSAHPSGFSANRgffgS 204
Cdd:pfam03167 70 KPTSHEIDACWPYLEAEIELL----RPRVIVLLGKTAAKALlglkkitklrgKLIDLKGIPVLPTPHPSPLLRNK----L 141
|
....*....
gi 488909751 205 KPFSQTNSW 213
Cdd:pfam03167 142 NPFLKANAW 150
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Ung |
COG0692 |
Uracil-DNA glycosylase [Replication, recombination and repair]; |
12-224 |
6.11e-124 |
|
Uracil-DNA glycosylase [Replication, recombination and repair];
Pssm-ID: 440456 Cd Length: 221 Bit Score: 350.11 E-value: 6.11e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488909751 12 DWYQHLKPVLGLDYLNQINDFLNKAYTGPLRVFPPEDKIFSAMLYTSLANTKVVIVGQDPYHELGQAQGLSFSVPDNFPA 91
Cdd:COG0692 8 SWKEALAEEFEKPYFQALGAFLKAEYAAGKTIYPPGEDIFRAFNLTPFDDVKVVILGQDPYHGPGQAHGLSFSVPPGVPL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488909751 92 PSSLQNIHKEIASDLGKTRNSH-DLIPWAKQGVLLLNSVLTVEEHKANSHAGMIWEKFTDSVIQLASAEPQPKVFILWGN 170
Cdd:COG0692 88 PPSLRNIYKELEDDLGIPIPNHgDLTSWAEQGVLLLNTVLTVRAGQAGSHAGKGWETFTDAVIRALNARKEPVVFLLWGA 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 488909751 171 FARRKAVLINPKKDLIIQSAHPSGFSANRGFFGSKPFSQTNSWLLSHDRTAIDW 224
Cdd:COG0692 168 YAQKKAALIDASKHLVLESPHPSPLSAHRGFFGSKPFSKANAYLEEQGKTPIDW 221
|
|
| PRK05254 |
PRK05254 |
uracil-DNA glycosylase; Provisional |
7-224 |
2.91e-115 |
|
uracil-DNA glycosylase; Provisional
Pssm-ID: 235376 Cd Length: 224 Bit Score: 328.27 E-value: 2.91e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488909751 7 NLKKTDWYQHLKPVLGLDYLNQINDFLNKAYTGPLRVFPPEDKIFSAMLYTSLANTKVVIVGQDPYHELGQAQGLSFSVP 86
Cdd:PRK05254 4 MLLEPSWKEVLKPEFKKPYFQELLEFLRAERAAGKTIYPPGEDIFRAFNLTPFDDVKVVILGQDPYHGPGQAHGLSFSVP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488909751 87 DNFPAPSSLQNIHKEIASDLGKTRNSH-DLIPWAKQGVLLLNSVLTVEEHKANSHAGMIWEKFTDSVIQLASAEPQPKVF 165
Cdd:PRK05254 84 PGVPIPPSLRNIFKELEDDLGFPIPNHgDLTSWAEQGVLLLNTVLTVEAGQANSHAGKGWETFTDAVIKALNERREPVVF 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 488909751 166 ILWGNFARRKAVLINPKKDLIIQSAHPSGFSANRGFFGSKPFSQTNSWLLSHDRTAIDW 224
Cdd:PRK05254 164 ILWGSHAQKKKALIDNSKHLILESPHPSPLSAHRGFFGSKHFSKANALLKQHGKTPIDW 222
|
|
| UDG-F1-like |
cd10027 |
Uracil DNA glycosylase family 1 subfamily, includes Human uracil DNA glycosylase and similar ... |
25-224 |
9.24e-110 |
|
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: 313.23 E-value: 9.24e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488909751 25 YLNQINDFLNKAYTGPlRVFPPEDKIFSAMLYTSLANTKVVIVGQDPYHELGQAQGLSFSVPDNFPAPSSLQNIHKEIAS 104
Cdd:cd10027 1 YFKKLEAFLEEEYKKK-TIYPPKEDIFRAFELTPLDDVKVVILGQDPYHGPGQAHGLAFSVPPGVKIPPSLRNIFKELKS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488909751 105 DLGKTRNSH-DLIPWAKQGVLLLNSVLTVEEHKANSHAGMIWEKFTDSVIQLASAEPQPKVFILWGNFARRKAVLINPKK 183
Cdd:cd10027 80 DLGIFPPKHgDLSSWAKQGVLLLNTVLTVEAGKPGSHKNIGWETFTDAVIKALSEKNENVVFLLWGNHAQKKKKLIDKKK 159
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 488909751 184 DLIIQSAHPSGFSANRGFFGSKPFSQTNSWLLSHDRTAIDW 224
Cdd:cd10027 160 HLVLESSHPSPLSAYRGFFGSKHFSKANEYLKKHGKKPIDW 200
|
|
| ung |
TIGR00628 |
uracil-DNA glycosylase; All proteins in this family for which functions are known are ... |
12-219 |
2.86e-89 |
|
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: 261.76 E-value: 2.86e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488909751 12 DWYQHLKPVLGLDYLNQINDFLNKAYTGpLRVFPPEDKIFSAMLYTSLANTKVVIVGQDPYHELGQAQGLSFSVPDNFPA 91
Cdd:TIGR00628 3 SWRAFLQPEFKKPYFQELLAFYKRERAQ-ETVYPPKEDVFAWTRLCPPEDVKVVILGQDPYHGPGQAHGLAFSVKRGVPI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488909751 92 PSSLQNIHKEIASDLGKTR--NSHDLIPWAKQGVLLLNSVLTVEEHKANSHAGMIWEKFTDSVIQLASAEPQPKVFILWG 169
Cdd:TIGR00628 82 PPSLKNIFKELEADYPDFPppKHGCLEAWARQGVLLLNTVLTVRRGQPGSHSGLGWERFTDAVISRLSERLDGLVFMLWG 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 488909751 170 NFARRKAVLINPKKDLIIQSAHPSGFSANRGFFGSKPFSQTNSWLLSHDR 219
Cdd:TIGR00628 162 AHAQKKKSLIDAKKHLVLKSPHPSPLSARRGFFGCRHFSKANEYLEKHGK 211
|
|
| PHA03347 |
PHA03347 |
uracil DNA glycosylase; Provisional |
26-224 |
6.98e-58 |
|
uracil DNA glycosylase; Provisional
Pssm-ID: 177588 Cd Length: 252 Bit Score: 183.33 E-value: 6.98e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488909751 26 LNQINDFLNKAYtgplrVFPPEDKIFSAMLYTSLANTKVVIVGQDPYHElGQAQGLSFSVPDNFPAPSSLQNIHKEIA-S 104
Cdd:PHA03347 48 LNCVRELRKQTV-----IYPPEDRIMAWSYLCDPEDIKVVILGQDPYHG-GQANGLAFSVAYGFPVPPSLRNIFAELHrS 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488909751 105 DLGKTRNSHD-LIPWAKQGVLLLNSVLTVEEHKANSHAGMIWEKFTDSVIQLASAEPQPKVFILWGNFARRKAVLINPKK 183
Cdd:PHA03347 122 VPDFSPPDHGcLDAWARQGVLLLNTILTVEKGKPGSHSDLGWAWFTDYIISSLSEKLKACVFMLWGSKAIDKASLINSQK 201
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 488909751 184 DLIIQSAHPSGFSANRG-------FFGSKPFSQTNSWLLSHDRTAIDW 224
Cdd:PHA03347 202 HLVLKAQHPSPLAANSTrsstwpkFLGCNHFVLANKYLTQHGKGPIDW 249
|
|
| PHA03200 |
PHA03200 |
uracil DNA glycosylase; Provisional |
12-224 |
1.17e-43 |
|
uracil DNA glycosylase; Provisional
Pssm-ID: 165467 Cd Length: 255 Bit Score: 147.18 E-value: 1.17e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488909751 12 DWYQHLK-PVLGLDYLNQINDFLNKAYTgPLRVFPPEDKIFSAMLYTSLANTKVVIVGQDPYHElGQAQGLSFSVPDNFP 90
Cdd:PHA03200 35 DWLRFLNlSDHDISQLRRIVDAVDRDRQ-RLTVYPPPEDVHRWSRLCSPEDVKVVIVGQDPYHD-GSACGLAFGTVRGRS 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488909751 91 APSSLQNIHKEIASDLGKTR--NSHDLIPWAKQGVLLLNSVLTVEEHKANSHAGMIWEKFTDSVIQLASAEPQPKVFILW 168
Cdd:PHA03200 113 APPSLKNVFRELERTVPNFSrpDSGCLDSWCRQGVLLLNTVFTVVHGQPGSHEALGWQTLSDRVISRLSEKREHLVFMLW 192
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 488909751 169 GNFARRKAVLINPKKDLIIQSAHPS--GFSANRGFFGSKPFSQTNSWLLSHDRTAIDW 224
Cdd:PHA03200 193 GAQAQKLEYLIDSRKHLILKSAHPSprVKGARTPFIGNNHFVLANEYLSTHGKRPIDW 250
|
|
| PHA03202 |
PHA03202 |
uracil DNA glycosylase; Provisional |
43-225 |
3.34e-40 |
|
uracil DNA glycosylase; Provisional
Pssm-ID: 165469 Cd Length: 313 Bit Score: 139.83 E-value: 3.34e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488909751 43 VFPPEDKIFSAMLYTSLANTKVVIVGQDPYHELGQAQGLSFSVPDNFPAPSSLQNIHKEIASDLGKTRN-SHDLIP-WAK 120
Cdd:PHA03202 129 VFPPKEDIFAWTRFSPPEKVRVVIVGQDPYHAPGQAHGLAFSVRKGVPVPPSLRNIYSAVQKSYPSFRPpMHGFLEkWAE 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488909751 121 QGVLLLNSVLTVEEHKANSHAGMIWEKFTDSVIQLASAEPQPKVFILWGNFArRKAVLINPKKDLIIQSAHPSGFSanRG 200
Cdd:PHA03202 209 QGVLLINTTLTVARGKPGSHATLGWHRLVRAVIDRLCTTSQGLVFMLWGAHA-QKSCSPNRQHHLVLTYGHPSPLS--RV 285
|
170 180
....*....|....*....|....*.
gi 488909751 201 FFGSKP-FSQTNSWLLSHDRTAIDWL 225
Cdd:PHA03202 286 NFRDCPhFLEANAYLTKTGRKPVDWQ 311
|
|
| PHA03201 |
PHA03201 |
uracil DNA glycosylase; Provisional |
43-224 |
1.02e-39 |
|
uracil DNA glycosylase; Provisional
Pssm-ID: 165468 Cd Length: 318 Bit Score: 138.87 E-value: 1.02e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488909751 43 VFPPEDKIFSAMLYTSLANTKVVIVGQDPYHELGQAQGLSFSVPDNFPAPSSLQNIHKEIASDLGKTRNSHD--LIPWAK 120
Cdd:PHA03201 135 VLPPREDVFSWTRYCTPDEVRVVIIGQDPYHQPGQAHGLAFSVRPGTPAPPSLRNILAAVRNCCPDARMSGHgcLEKWAR 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488909751 121 QGVLLLNSVLTVEEHKANSHAGMIWEKFTDSVIQLASAEPQPKVFILWGNFArRKAVLINPKKDLIIQSAHPSGFSanRG 200
Cdd:PHA03201 215 GGVLLLNTTLTVRRGEPASHAKIGWDRFVGSVVRRLAASRPGLVFMLWGAHA-QNAIRPDPRVHRVLTYSHPSPLS--KV 291
|
170 180
....*....|....*....|....*
gi 488909751 201 FFGS-KPFSQTNSWLLSHDRTAIDW 224
Cdd:PHA03201 292 PFGScRHFCLANQYLRERSLAPIDW 316
|
|
| UDG-F1-like |
cd19371 |
Uracil DNA glycosylase family 1, includes Human uracil DNA glycosylase, Vaccinia virus protein ... |
64-196 |
3.38e-39 |
|
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: 131.69 E-value: 3.38e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488909751 64 VVIVGQDPYHELGQAQGLSFSVPDNFPAPSSLQNIHKEIASDLG--KTRNSHDLIPWAKQGVLLLNSVLTVEEHKANSHa 141
Cdd:cd19371 1 VVIIGQDPYPSPGHAGGLAFSVTSEVPPPKSLRNIYKELERDYSsfLPPGNGTLEFWARQGVLLLNAALTCESGKPKSH- 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 488909751 142 GMIWEKFTDSVIQLASAEPQPKVFILWGNFARRKAVLINPKKDLIIQSAHPSGFS 196
Cdd:cd19371 80 YLLWEPFIKAFIRYISAHNKGLVFLLFGSDAQKLRKKINGRNVHVFKADHPSPAD 134
|
|
| PHA03204 |
PHA03204 |
uracil DNA glycosylase; Provisional |
43-224 |
2.57e-37 |
|
uracil DNA glycosylase; Provisional
Pssm-ID: 165471 Cd Length: 322 Bit Score: 132.39 E-value: 2.57e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488909751 43 VFPPEDKIFSAMLYTSLANTKVVIVGQDPYHELGQAQGLSFSVPDNFPAPSSLQNIHKEI-----ASDLGktrNSHDLIP 117
Cdd:PHA03204 135 VYPPKSDIFAWTRYCAPDHVKVVIVGQDPYANPGQAHGLAFSVKPGSPIPPSLKNILAAVkacypSIELG---SHGCLED 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488909751 118 WAKQGVLLLNSVLTVEEHKANSHAGMIWEKFTDSVIQLASAEPQPKVFILWGnfARRKAVLINPKKD---LIIQSAHPSG 194
Cdd:PHA03204 212 WAKRGVLLLNSVLTVKRGDPGSHHSVGWQILVRNVLRRLSQSTRGIVFMLWG--AQAQTMYFQTDNDdrhLVLKYSHPSP 289
|
170 180 190
....*....|....*....|....*....|
gi 488909751 195 FSaNRGFFGSKPFSQTNSWLLSHDRTAIDW 224
Cdd:PHA03204 290 LS-RKPFAHCTHFKDANEFLCKMGKGAIDW 318
|
|
| PHA03199 |
PHA03199 |
uracil DNA glycosylase; Provisional |
12-224 |
2.21e-34 |
|
uracil DNA glycosylase; Provisional
Pssm-ID: 165466 Cd Length: 304 Bit Score: 124.35 E-value: 2.21e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488909751 12 DWYQHLKPVLGLDYLNQINDFLNKAYTGPLRVFPPEDKIFSAMLYTSLANTKVVIVGQDPYHELGQAQGLSFSVPDNFPA 91
Cdd:PHA03199 90 EWHDLLRDEFEEPYAKGIFEEYNQLLNNGEEIFPIKGDIFAWTRFCGPEKIRVVIIGQDPYHGAGHAHGLAFSVKRGIPI 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488909751 92 PSSLQNIHKEI-ASDLGKTRNSHD-LIPWAKQGVLLLNSVLTVEEHKANSHAGMIWEKFTDSVIQLASAEPQPKVFILWG 169
Cdd:PHA03199 170 PPSLKNIFAALmESYPHLPLPTHGcLDNWARQGVLLLNTTLTVKRGTPGSHFYLGWDMLIKRMLKRLCENRTGLVFMLWG 249
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 488909751 170 NFARRkAVLINPKKDLIIQSAHPSGFSANRgFFGSKPFSQTNSWLLSHDRTAIDW 224
Cdd:PHA03199 250 AHAQK-TIQPNPRCHLVLTHAHPSPLSRSE-FRNCKHFLQANEYFLKKGEPEIDW 302
|
|
| UDG |
smart00986 |
Uracil DNA glycosylase superfamily; |
60-214 |
4.95e-26 |
|
Uracil DNA glycosylase superfamily;
Pssm-ID: 214956 Cd Length: 156 Bit Score: 98.61 E-value: 4.95e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488909751 60 ANTKVVIVGQDPYHELGQAQ-------GLSFSVP----DNFPAPSSLQNIHKEIASDLGKTRNShdliPWAKQGVLLlnS 128
Cdd:smart00986 6 PNAKVLIVGQAPGASEEDRGgpfvgaaGLLLSVMlgvaGLPRLPPYLTNIVKCRPPDAGNRRPT----SWELQGCLL--P 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488909751 129 VLTVEEHKANSHAGMIWEKFTDSVIQLASaePQPKVFILWGNFARRKAVLInpkkdLIIQSAHPSGfsANRGFFGSKPFS 208
Cdd:smart00986 80 WLTVELALARPHLILLLGKFAAQALLGLL--RRPLVFGLRGRVAQLKGKGH-----RVLPLPHPSP--LNRNFFPAKKFA 150
|
....*.
gi 488909751 209 QTNSWL 214
Cdd:smart00986 151 AWNDLL 156
|
|
| UDG |
pfam03167 |
Uracil DNA glycosylase superfamily; |
60-213 |
1.07e-16 |
|
Uracil DNA glycosylase superfamily;
Pssm-ID: 397331 Cd Length: 154 Bit Score: 74.31 E-value: 1.07e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488909751 60 ANTKVVIVGQDPYHElGQAQGLSFSVP--DNFPapsslqnihkEIASDLGKTRNSHdlipwAKQGVLLLNSVLTVEE--H 135
Cdd:pfam03167 6 PNAKVLIVGEAPGAD-EDATGLPFVGRagNLLW----------KLLNAAGLTRDLF-----SPQGVYITNVVKCRPGnrR 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488909751 136 KANSHAGMIWEKFTDSVIQLAsaepQPKVFILWGNFARRKA-----------VLINPKKDLIIQSAHPSGFSANRgffgS 204
Cdd:pfam03167 70 KPTSHEIDACWPYLEAEIELL----RPRVIVLLGKTAAKALlglkkitklrgKLIDLKGIPVLPTPHPSPLLRNK----L 141
|
....*....
gi 488909751 205 KPFSQTNSW 213
Cdd:pfam03167 142 NPFLKANAW 150
|
|
| UDG-like |
cd09593 |
uracil-DNA glycosylases (UDG) and related enzymes; Uracil-DNA glycosylases (UDGs) initiate ... |
64-197 |
1.79e-11 |
|
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: 59.32 E-value: 1.79e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488909751 64 VVIVGQDPYHELGQAQGlsfsvpdnFPAPSSLQNIHKEIASDLGKTRnshdlipWAKQGVLLLNSVLTVE-EHKANSHAG 142
Cdd:cd09593 1 VLIVGQNPGPHGARAGG--------VPPGPSGNRLWRLLAAAGGTPR-------LFRYGVGLTNTVPRGPpGAAAGSEKK 65
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488909751 143 miWEKFTDSVIQLASAEPQPKVFILWGNFAR------RKAVLINPKKDL-IIQSAHPSGFSA 197
Cdd:cd09593 66 --ELRFCGRWLRKLLELLNPRVVVLLGKKAQeaylavLTSSKGAPGKGTeVLVLPHPSPRNR 125
|
|
| UDG_F1_VAVC_D4-like |
cd19372 |
Uracil DNA glycosylase family 1 subfamily, includes Vaccinia virus protein D4 and similar ... |
26-226 |
8.39e-08 |
|
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: 50.90 E-value: 8.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488909751 26 LNQINDFLNKAYTGPLR--VFPPEDKIFsAMLYTSLANTKVVIVGQDPYHElgQAQGLSFSVPDnfpapSSLQNIhKEIA 103
Cdd:cd19372 5 INQLVDEYTEVAPWLLRdeTSPIPENFF-KQLKQPLRDKRVCICGIDPYPT--DATGVPFESPD-----FSKKTI-RAIA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488909751 104 SDLGKTRNSHDLIPW---AKQGVLLLNSVLTVEEHKANSHAgMIWEKFTDSVIQLASAepQPKVFILWG--NFARRKAVL 178
Cdd:cd19372 76 EAISRRTGVSLYKGYnfaLVEGVLAWNYYLSCREGETKSHA-IHWERISKLLLQHIAK--YVSVLYCLGktDFSNVRARL 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 488909751 179 INPKKdlIIQSAHPSgfSANRGFFGSKPFSQTNSWLLSHDRTAIDWLK 226
Cdd:cd19372 153 EVPVT--VVVGYHPA--ARDGQFDKERAFEIVNVLLELNGKPPVNWAQ 196
|
|
| |
