|
Name |
Accession |
Description |
Interval |
E-value |
| Ung |
COG0692 |
Uracil-DNA glycosylase [Replication, recombination and repair]; |
1-214 |
1.08e-136 |
|
Uracil-DNA glycosylase [Replication, recombination and repair];
Pssm-ID: 440456 Cd Length: 221 Bit Score: 382.08 E-value: 1.08e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545346882 1 MHNSWNEVIKNYPKIDELNELIKKID-EKRLTTTIYPPKEQVFRVFDL-ALEDIKVVILGQDPYHNPEQACGLSFSVNDG 78
Cdd:COG0692 5 LEPSWKEALAEEFEKPYFQALGAFLKaEYAAGKTIYPPGEDIFRAFNLtPFDDVKVVILGQDPYHGPGQAHGLSFSVPPG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545346882 79 VPLPKSLINIYKELHDDLGINPAKTGNLESWFNQGVFLLNAVLTVEKNSPASHSKMGWENFTDYIIETISEKNENVVFVL 158
Cdd:COG0692 85 VPLPPSLRNIYKELEDDLGIPIPNHGDLTSWAEQGVLLLNTVLTVRAGQAGSHAGKGWETFTDAVIRALNARKEPVVFLL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1545346882 159 WGAYARSKNKLIDPSKHLIIESAHPSPLSAYRGFFGSKVFSQINDYLDSHGRGNID 214
Cdd:COG0692 165 WGAYAQKKAALIDASKHLVLESPHPSPLSAHRGFFGSKPFSKANAYLEEQGKTPID 220
|
|
| PRK05254 |
PRK05254 |
uracil-DNA glycosylase; Provisional |
1-217 |
5.20e-128 |
|
uracil-DNA glycosylase; Provisional
Pssm-ID: 235376 Cd Length: 224 Bit Score: 360.62 E-value: 5.20e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545346882 1 MHNSWNEVIKNY---PKIDELNELIKKidEKRLTTTIYPPKEQVFRVFDL-ALEDIKVVILGQDPYHNPEQACGLSFSVN 76
Cdd:PRK05254 6 LEPSWKEVLKPEfkkPYFQELLEFLRA--ERAAGKTIYPPGEDIFRAFNLtPFDDVKVVILGQDPYHGPGQAHGLSFSVP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545346882 77 DGVPLPKSLINIYKELHDDLGINPAKTGNLESWFNQGVFLLNAVLTVEKNSPASHSKMGWENFTDYIIETISEKNENVVF 156
Cdd:PRK05254 84 PGVPIPPSLRNIFKELEDDLGFPIPNHGDLTSWAEQGVLLLNTVLTVEAGQANSHAGKGWETFTDAVIKALNERREPVVF 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1545346882 157 VLWGAYARSKNKLIDPSKHLIIESAHPSPLSAYRGFFGSKVFSQINDYLDSHGRGNIDFEL 217
Cdd:PRK05254 164 ILWGSHAQKKKALIDNSKHLILESPHPSPLSAHRGFFGSKHFSKANALLKQHGKTPIDWQL 224
|
|
| UDG-F1-like |
cd10027 |
Uracil DNA glycosylase family 1 subfamily, includes Human uracil DNA glycosylase and similar ... |
18-214 |
2.85e-122 |
|
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: 344.82 E-value: 2.85e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545346882 18 LNELIKKIDEKRLTTTIYPPKEQVFRVFDL-ALEDIKVVILGQDPYHNPEQACGLSFSVNDGVPLPKSLINIYKELHDDL 96
Cdd:cd10027 2 FKKLEAFLEEEYKKKTIYPPKEDIFRAFELtPLDDVKVVILGQDPYHGPGQAHGLAFSVPPGVKIPPSLRNIFKELKSDL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545346882 97 GINPAKTGNLESWFNQGVFLLNAVLTVEKNSPASHSKMGWENFTDYIIETISEKNENVVFVLWGAYARSKNKLIDPSKHL 176
Cdd:cd10027 82 GIFPPKHGDLSSWAKQGVLLLNTVLTVEAGKPGSHKNIGWETFTDAVIKALSEKNENVVFLLWGNHAQKKKKLIDKKKHL 161
|
170 180 190
....*....|....*....|....*....|....*...
gi 1545346882 177 IIESAHPSPLSAYRGFFGSKVFSQINDYLDSHGRGNID 214
Cdd:cd10027 162 VLESSHPSPLSAYRGFFGSKHFSKANEYLKKHGKKPID 199
|
|
| ung |
TIGR00628 |
uracil-DNA glycosylase; All proteins in this family for which functions are known are ... |
2-210 |
4.83e-107 |
|
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: 306.83 E-value: 4.83e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545346882 2 HNSWNEVIKNYPKIDELNELIKKIDEKRLTTTIYPPKEQVFRVFDL-ALEDIKVVILGQDPYHNPEQACGLSFSVNDGVP 80
Cdd:TIGR00628 1 SPSWRAFLQPEFKKPYFQELLAFYKRERAQETVYPPKEDVFAWTRLcPPEDVKVVILGQDPYHGPGQAHGLAFSVKRGVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545346882 81 LPKSLINIYKELHDDLG-INPAKTGNLESWFNQGVFLLNAVLTVEKNSPASHSKMGWENFTDYIIETISEKNENVVFVLW 159
Cdd:TIGR00628 81 IPPSLKNIFKELEADYPdFPPPKHGCLEAWARQGVLLLNTVLTVRRGQPGSHSGLGWERFTDAVISRLSERLDGLVFMLW 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1545346882 160 GAYARSKNKLIDPSKHLIIESAHPSPLSAYRGFFGSKVFSQINDYLDSHGR 210
Cdd:TIGR00628 161 GAHAQKKKSLIDAKKHLVLKSPHPSPLSARRGFFGCRHFSKANEYLEKHGK 211
|
|
| UDG |
smart00986 |
Uracil DNA glycosylase superfamily; |
45-205 |
4.24e-27 |
|
Uracil DNA glycosylase superfamily;
Pssm-ID: 214956 Cd Length: 156 Bit Score: 101.31 E-value: 4.24e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545346882 45 FDLALEDIKVVILGQDPYHNPEQ-------ACGLSFSVNDGV----PLPKSLINIYKELHDDLGinpakTGNLESWFNQG 113
Cdd:smart00986 1 PGTGDPNAKVLIVGQAPGASEEDrggpfvgAAGLLLSVMLGVaglpRLPPYLTNIVKCRPPDAG-----NRRPTSWELQG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545346882 114 VFLlnAVLTVEKNSPASHSKMGWENFTDYIIETISEKneNVVFVLWGAYARSKNKLidpskHLIIESAHPSPLSAYRgfF 193
Cdd:smart00986 76 CLL--PWLTVELALARPHLILLLGKFAAQALLGLLRR--PLVFGLRGRVAQLKGKG-----HRVLPLPHPSPLNRNF--F 144
|
170
....*....|..
gi 1545346882 194 GSKVFSQINDYL 205
Cdd:smart00986 145 PAKKFAAWNDLL 156
|
|
| UDG |
pfam03167 |
Uracil DNA glycosylase superfamily; |
45-197 |
6.17e-22 |
|
Uracil DNA glycosylase superfamily;
Pssm-ID: 397331 Cd Length: 154 Bit Score: 87.79 E-value: 6.17e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545346882 45 FDLALEDIKVVILGQDPYHNpEQACGLSFSVNDGVPLPKSLINIykelhddlGINPaktgnlESWFNQGVFLLNAVLTV- 123
Cdd:pfam03167 1 PGFGPPNAKVLIVGEAPGAD-EDATGLPFVGRAGNLLWKLLNAA--------GLTR------DLFSPQGVYITNVVKCRp 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545346882 124 -EKNSPASHS-KMGWEnFTDYIIETISEKnenvVFVLWGAYA-----------RSKNKLIDPSKHLIIESAHPSPLSAYR 190
Cdd:pfam03167 66 gNRRKPTSHEiDACWP-YLEAEIELLRPR----VIVLLGKTAakallglkkitKLRGKLIDLKGIPVLPTPHPSPLLRNK 140
|
....*..
gi 1545346882 191 GFFGSKV 197
Cdd:pfam03167 141 LNPFLKA 147
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Ung |
COG0692 |
Uracil-DNA glycosylase [Replication, recombination and repair]; |
1-214 |
1.08e-136 |
|
Uracil-DNA glycosylase [Replication, recombination and repair];
Pssm-ID: 440456 Cd Length: 221 Bit Score: 382.08 E-value: 1.08e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545346882 1 MHNSWNEVIKNYPKIDELNELIKKID-EKRLTTTIYPPKEQVFRVFDL-ALEDIKVVILGQDPYHNPEQACGLSFSVNDG 78
Cdd:COG0692 5 LEPSWKEALAEEFEKPYFQALGAFLKaEYAAGKTIYPPGEDIFRAFNLtPFDDVKVVILGQDPYHGPGQAHGLSFSVPPG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545346882 79 VPLPKSLINIYKELHDDLGINPAKTGNLESWFNQGVFLLNAVLTVEKNSPASHSKMGWENFTDYIIETISEKNENVVFVL 158
Cdd:COG0692 85 VPLPPSLRNIYKELEDDLGIPIPNHGDLTSWAEQGVLLLNTVLTVRAGQAGSHAGKGWETFTDAVIRALNARKEPVVFLL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1545346882 159 WGAYARSKNKLIDPSKHLIIESAHPSPLSAYRGFFGSKVFSQINDYLDSHGRGNID 214
Cdd:COG0692 165 WGAYAQKKAALIDASKHLVLESPHPSPLSAHRGFFGSKPFSKANAYLEEQGKTPID 220
|
|
| PRK05254 |
PRK05254 |
uracil-DNA glycosylase; Provisional |
1-217 |
5.20e-128 |
|
uracil-DNA glycosylase; Provisional
Pssm-ID: 235376 Cd Length: 224 Bit Score: 360.62 E-value: 5.20e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545346882 1 MHNSWNEVIKNY---PKIDELNELIKKidEKRLTTTIYPPKEQVFRVFDL-ALEDIKVVILGQDPYHNPEQACGLSFSVN 76
Cdd:PRK05254 6 LEPSWKEVLKPEfkkPYFQELLEFLRA--ERAAGKTIYPPGEDIFRAFNLtPFDDVKVVILGQDPYHGPGQAHGLSFSVP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545346882 77 DGVPLPKSLINIYKELHDDLGINPAKTGNLESWFNQGVFLLNAVLTVEKNSPASHSKMGWENFTDYIIETISEKNENVVF 156
Cdd:PRK05254 84 PGVPIPPSLRNIFKELEDDLGFPIPNHGDLTSWAEQGVLLLNTVLTVEAGQANSHAGKGWETFTDAVIKALNERREPVVF 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1545346882 157 VLWGAYARSKNKLIDPSKHLIIESAHPSPLSAYRGFFGSKVFSQINDYLDSHGRGNIDFEL 217
Cdd:PRK05254 164 ILWGSHAQKKKALIDNSKHLILESPHPSPLSAHRGFFGSKHFSKANALLKQHGKTPIDWQL 224
|
|
| UDG-F1-like |
cd10027 |
Uracil DNA glycosylase family 1 subfamily, includes Human uracil DNA glycosylase and similar ... |
18-214 |
2.85e-122 |
|
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: 344.82 E-value: 2.85e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545346882 18 LNELIKKIDEKRLTTTIYPPKEQVFRVFDL-ALEDIKVVILGQDPYHNPEQACGLSFSVNDGVPLPKSLINIYKELHDDL 96
Cdd:cd10027 2 FKKLEAFLEEEYKKKTIYPPKEDIFRAFELtPLDDVKVVILGQDPYHGPGQAHGLAFSVPPGVKIPPSLRNIFKELKSDL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545346882 97 GINPAKTGNLESWFNQGVFLLNAVLTVEKNSPASHSKMGWENFTDYIIETISEKNENVVFVLWGAYARSKNKLIDPSKHL 176
Cdd:cd10027 82 GIFPPKHGDLSSWAKQGVLLLNTVLTVEAGKPGSHKNIGWETFTDAVIKALSEKNENVVFLLWGNHAQKKKKLIDKKKHL 161
|
170 180 190
....*....|....*....|....*....|....*...
gi 1545346882 177 IIESAHPSPLSAYRGFFGSKVFSQINDYLDSHGRGNID 214
Cdd:cd10027 162 VLESSHPSPLSAYRGFFGSKHFSKANEYLKKHGKKPID 199
|
|
| ung |
TIGR00628 |
uracil-DNA glycosylase; All proteins in this family for which functions are known are ... |
2-210 |
4.83e-107 |
|
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: 306.83 E-value: 4.83e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545346882 2 HNSWNEVIKNYPKIDELNELIKKIDEKRLTTTIYPPKEQVFRVFDL-ALEDIKVVILGQDPYHNPEQACGLSFSVNDGVP 80
Cdd:TIGR00628 1 SPSWRAFLQPEFKKPYFQELLAFYKRERAQETVYPPKEDVFAWTRLcPPEDVKVVILGQDPYHGPGQAHGLAFSVKRGVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545346882 81 LPKSLINIYKELHDDLG-INPAKTGNLESWFNQGVFLLNAVLTVEKNSPASHSKMGWENFTDYIIETISEKNENVVFVLW 159
Cdd:TIGR00628 81 IPPSLKNIFKELEADYPdFPPPKHGCLEAWARQGVLLLNTVLTVRRGQPGSHSGLGWERFTDAVISRLSERLDGLVFMLW 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1545346882 160 GAYARSKNKLIDPSKHLIIESAHPSPLSAYRGFFGSKVFSQINDYLDSHGR 210
Cdd:TIGR00628 161 GAHAQKKKSLIDAKKHLVLKSPHPSPLSARRGFFGCRHFSKANEYLEKHGK 211
|
|
| PHA03347 |
PHA03347 |
uracil DNA glycosylase; Provisional |
18-217 |
7.33e-79 |
|
uracil DNA glycosylase; Provisional
Pssm-ID: 177588 Cd Length: 252 Bit Score: 236.87 E-value: 7.33e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545346882 18 LNELIKKIDEKRLTTTIYPPKEQVFR-VFDLALEDIKVVILGQDPYHNPeQACGLSFSVNDGVPLPKSLINIYKELHD-D 95
Cdd:PHA03347 44 LLALLNCVRELRKQTVIYPPEDRIMAwSYLCDPEDIKVVILGQDPYHGG-QANGLAFSVAYGFPVPPSLRNIFAELHRsV 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545346882 96 LGINPAKTGNLESWFNQGVFLLNAVLTVEKNSPASHSKMGWENFTDYIIETISEKNENVVFVLWGAYARSKNKLIDPSKH 175
Cdd:PHA03347 123 PDFSPPDHGCLDAWARQGVLLLNTILTVEKGKPGSHSDLGWAWFTDYIISSLSEKLKACVFMLWGSKAIDKASLINSQKH 202
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1545346882 176 LIIESAHPSPLSA---YRG----FFGSKVFSQINDYLDSHGRGNIDFEL 217
Cdd:PHA03347 203 LVLKAQHPSPLAAnstRSStwpkFLGCNHFVLANKYLTQHGKGPIDWNL 251
|
|
| PHA03200 |
PHA03200 |
uracil DNA glycosylase; Provisional |
15-217 |
1.21e-65 |
|
uracil DNA glycosylase; Provisional
Pssm-ID: 165467 Cd Length: 255 Bit Score: 203.42 E-value: 1.21e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545346882 15 IDELNELIKKIDEKRLTTTIYPPKEQVFR-VFDLALEDIKVVILGQDPYHNpEQACGLSFSVNDGVPLPKSLINIYKELH 93
Cdd:PHA03200 47 ISQLRRIVDAVDRDRQRLTVYPPPEDVHRwSRLCSPEDVKVVIVGQDPYHD-GSACGLAFGTVRGRSAPPSLKNVFRELE 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545346882 94 DDL-GINPAKTGNLESWFNQGVFLLNAVLTVEKNSPASHSKMGWENFTDYIIETISEKNENVVFVLWGAYARSKNKLIDP 172
Cdd:PHA03200 126 RTVpNFSRPDSGCLDSWCRQGVLLLNTVFTVVHGQPGSHEALGWQTLSDRVISRLSEKREHLVFMLWGAQAQKLEYLIDS 205
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1545346882 173 SKHLIIESAHPSP--LSAYRGFFGSKVFSQINDYLDSHGRGNIDFEL 217
Cdd:PHA03200 206 RKHLILKSAHPSPrvKGARTPFIGNNHFVLANEYLSTHGKRPIDWNI 252
|
|
| PHA03202 |
PHA03202 |
uracil DNA glycosylase; Provisional |
1-218 |
3.14e-48 |
|
uracil DNA glycosylase; Provisional
Pssm-ID: 165469 Cd Length: 313 Bit Score: 160.63 E-value: 3.14e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545346882 1 MHNSWNEVIKNYPKIDELNELIKK----------IDEKRLTTT---IYPPKEQVFRVFDLAL-EDIKVVILGQDPYHNPE 66
Cdd:PHA03202 83 CQSSWEDVEREFNIAPSWRPILERemqqpyvrllLNEYKLRCAreeVFPPKEDIFAWTRFSPpEKVRVVIVGQDPYHAPG 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545346882 67 QACGLSFSVNDGVPLPKSLINIYKELHDDL-GINPAKTGNLESWFNQGVFLLNAVLTVEKNSPASHSKMGWENFTDYIIE 145
Cdd:PHA03202 163 QAHGLAFSVRKGVPVPPSLRNIYSAVQKSYpSFRPPMHGFLEKWAEQGVLLINTTLTVARGKPGSHATLGWHRLVRAVID 242
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1545346882 146 TISEKNENVVFVLWGAYARsknKLIDPSK--HLIIESAHPSPLSAYrGFFGSKVFSQINDYLDSHGRGNIDFELK 218
Cdd:PHA03202 243 RLCTTSQGLVFMLWGAHAQ---KSCSPNRqhHLVLTYGHPSPLSRV-NFRDCPHFLEANAYLTKTGRKPVDWQIE 313
|
|
| PHA03204 |
PHA03204 |
uracil DNA glycosylase; Provisional |
1-217 |
1.22e-47 |
|
uracil DNA glycosylase; Provisional
Pssm-ID: 165471 Cd Length: 322 Bit Score: 159.35 E-value: 1.22e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545346882 1 MHNSWNEVIknYPKIDELN--ELIKKIDEKRLTTTIYPPKEQVFR-VFDLALEDIKVVILGQDPYHNPEQACGLSFSVND 77
Cdd:PHA03204 102 IDCRWKEIL--LPELCCPTgsKILAEYERRARYEEVYPPKSDIFAwTRYCAPDHVKVVIVGQDPYANPGQAHGLAFSVKP 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545346882 78 GVPLPKSLINIYKELHD-----DLGinpaKTGNLESWFNQGVFLLNAVLTVEKNSPASHSKMGWENFTDYIIETISEKNE 152
Cdd:PHA03204 180 GSPIPPSLKNILAAVKAcypsiELG----SHGCLEDWAKRGVLLLNSVLTVKRGDPGSHHSVGWQILVRNVLRRLSQSTR 255
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1545346882 153 NVVFVLWGAYARSKNKLID-PSKHLIIESAHPSPLSAyRGFFGSKVFSQINDYLDSHGRGNIDFEL 217
Cdd:PHA03204 256 GIVFMLWGAQAQTMYFQTDnDDRHLVLKYSHPSPLSR-KPFAHCTHFKDANEFLCKMGKGAIDWSL 320
|
|
| UDG-F1-like |
cd19371 |
Uracil DNA glycosylase family 1, includes Human uracil DNA glycosylase, Vaccinia virus protein ... |
54-187 |
1.23e-45 |
|
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: 148.25 E-value: 1.23e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545346882 54 VVILGQDPYHNPEQACGLSFSVNDGVPLPKSLINIYKELHDDLG-INPAKTGNLESWFNQGVFLLNAVLTVEKNSPASHS 132
Cdd:cd19371 1 VVIIGQDPYPSPGHAGGLAFSVTSEVPPPKSLRNIYKELERDYSsFLPPGNGTLEFWARQGVLLLNAALTCESGKPKSHY 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1545346882 133 kMGWENFTDYIIETISEKNENVVFVLWGAYARSKNKLIDPSKHLIIESAHPSPLS 187
Cdd:cd19371 81 -LLWEPFIKAFIRYISAHNKGLVFLLFGSDAQKLRKKINGRNVHVFKADHPSPAD 134
|
|
| PHA03201 |
PHA03201 |
uracil DNA glycosylase; Provisional |
21-215 |
3.53e-44 |
|
uracil DNA glycosylase; Provisional
Pssm-ID: 165468 Cd Length: 318 Bit Score: 150.43 E-value: 3.53e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545346882 21 LIKKIDEKRLTTTIYPPKEQVFRVFDL-ALEDIKVVILGQDPYHNPEQACGLSFSVNDGVPLPKSLINIYKELHDdlgIN 99
Cdd:PHA03201 122 LMAEYERRCRTEEVLPPREDVFSWTRYcTPDEVRVVIIGQDPYHQPGQAHGLAFSVRPGTPAPPSLRNILAAVRN---CC 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545346882 100 PAKT----GNLESWFNQGVFLLNAVLTVEKNSPASHSKMGWENFTDYIIETISEKNENVVFVLWGAYARSKNKlIDPSKH 175
Cdd:PHA03201 199 PDARmsghGCLEKWARGGVLLLNTTLTVRRGEPASHAKIGWDRFVGSVVRRLAASRPGLVFMLWGAHAQNAIR-PDPRVH 277
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1545346882 176 LIIESAHPSPLSayRGFFGS-KVFSQINDYLDSHGRGNIDF 215
Cdd:PHA03201 278 RVLTYSHPSPLS--KVPFGScRHFCLANQYLRERSLAPIDW 316
|
|
| PHA03199 |
PHA03199 |
uracil DNA glycosylase; Provisional |
50-217 |
8.13e-44 |
|
uracil DNA glycosylase; Provisional
Pssm-ID: 165466 Cd Length: 304 Bit Score: 149.00 E-value: 8.13e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545346882 50 EDIKVVILGQDPYHNPEQACGLSFSVNDGVPLPKSLINIYKELHDDL-GINPAKTGNLESWFNQGVFLLNAVLTVEKNSP 128
Cdd:PHA03199 138 EKIRVVIIGQDPYHGAGHAHGLAFSVKRGIPIPPSLKNIFAALMESYpHLPLPTHGCLDNWARQGVLLLNTTLTVKRGTP 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545346882 129 ASHSKMGWENFTDYIIETISEKNENVVFVLWGAYARsKNKLIDPSKHLIIESAHPSPLSAYRgFFGSKVFSQINDYLDSH 208
Cdd:PHA03199 218 GSHFYLGWDMLIKRMLKRLCENRTGLVFMLWGAHAQ-KTIQPNPRCHLVLTHAHPSPLSRSE-FRNCKHFLQANEYFLKK 295
|
....*....
gi 1545346882 209 GRGNIDFEL 217
Cdd:PHA03199 296 GEPEIDWSI 304
|
|
| UDG |
smart00986 |
Uracil DNA glycosylase superfamily; |
45-205 |
4.24e-27 |
|
Uracil DNA glycosylase superfamily;
Pssm-ID: 214956 Cd Length: 156 Bit Score: 101.31 E-value: 4.24e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545346882 45 FDLALEDIKVVILGQDPYHNPEQ-------ACGLSFSVNDGV----PLPKSLINIYKELHDDLGinpakTGNLESWFNQG 113
Cdd:smart00986 1 PGTGDPNAKVLIVGQAPGASEEDrggpfvgAAGLLLSVMLGVaglpRLPPYLTNIVKCRPPDAG-----NRRPTSWELQG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545346882 114 VFLlnAVLTVEKNSPASHSKMGWENFTDYIIETISEKneNVVFVLWGAYARSKNKLidpskHLIIESAHPSPLSAYRgfF 193
Cdd:smart00986 76 CLL--PWLTVELALARPHLILLLGKFAAQALLGLLRR--PLVFGLRGRVAQLKGKG-----HRVLPLPHPSPLNRNF--F 144
|
170
....*....|..
gi 1545346882 194 GSKVFSQINDYL 205
Cdd:smart00986 145 PAKKFAAWNDLL 156
|
|
| UDG |
pfam03167 |
Uracil DNA glycosylase superfamily; |
45-197 |
6.17e-22 |
|
Uracil DNA glycosylase superfamily;
Pssm-ID: 397331 Cd Length: 154 Bit Score: 87.79 E-value: 6.17e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545346882 45 FDLALEDIKVVILGQDPYHNpEQACGLSFSVNDGVPLPKSLINIykelhddlGINPaktgnlESWFNQGVFLLNAVLTV- 123
Cdd:pfam03167 1 PGFGPPNAKVLIVGEAPGAD-EDATGLPFVGRAGNLLWKLLNAA--------GLTR------DLFSPQGVYITNVVKCRp 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545346882 124 -EKNSPASHS-KMGWEnFTDYIIETISEKnenvVFVLWGAYA-----------RSKNKLIDPSKHLIIESAHPSPLSAYR 190
Cdd:pfam03167 66 gNRRKPTSHEiDACWP-YLEAEIELLRPR----VIVLLGKTAakallglkkitKLRGKLIDLKGIPVLPTPHPSPLLRNK 140
|
....*..
gi 1545346882 191 GFFGSKV 197
Cdd:pfam03167 141 LNPFLKA 147
|
|
| UDG-like |
cd09593 |
uracil-DNA glycosylases (UDG) and related enzymes; Uracil-DNA glycosylases (UDGs) initiate ... |
54-188 |
8.63e-14 |
|
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: 65.49 E-value: 8.63e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545346882 54 VVILGQDPYHNPEQAcglsfsvnDGVPLPKSLINIYKELHDDlGINPaktgnleSWFNQGVFLLNAVLTVEKNSpASHSK 133
Cdd:cd09593 1 VLIVGQNPGPHGARA--------GGVPPGPSGNRLWRLLAAA-GGTP-------RLFRYGVGLTNTVPRGPPGA-AAGSE 63
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1545346882 134 MGWENFTDyiiETISEKNENV---VFVLWGAYA-------RSKNKLIDPSKHLIIESAHPSPLSA 188
Cdd:cd09593 64 KKELRFCG---RWLRKLLELLnprVVVLLGKKAqeaylavLTSSKGAPGKGTEVLVLPHPSPRNR 125
|
|
| UDG_F1_VAVC_D4-like |
cd19372 |
Uracil DNA glycosylase family 1 subfamily, includes Vaccinia virus protein D4 and similar ... |
13-216 |
1.58e-04 |
|
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: 41.27 E-value: 1.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545346882 13 PKIDELNELIKKIDEKRLTTTIYPPKEQVFRVFDLALEDIKVVILGQDPYhnPEQACGLSFSVNDGVplPKSLINIYKEL 92
Cdd:cd19372 3 PVINQLVDEYTEVAPWLLRDETSPIPENFFKQLKQPLRDKRVCICGIDPY--PTDATGVPFESPDFS--KKTIRAIAEAI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1545346882 93 HDDLGINPAKTGNLEswFNQGVFLLNAVLTVEKNSPASHSkMGWENFTDYIIETISeKNENVVFVLWGA-YARSKNKLID 171
Cdd:cd19372 79 SRRTGVSLYKGYNFA--LVEGVLAWNYYLSCREGETKSHA-IHWERISKLLLQHIA-KYVSVLYCLGKTdFSNVRARLEV 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1545346882 172 PSKhlIIESAHPSPLSayRGFFGSKVFSQINDYLDSHGRGNIDFE 216
Cdd:cd19372 155 PVT--VVVGYHPAARD--GQFDKERAFEIVNVLLELNGKPPVNWA 195
|
|
| |
