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Conserved domains on  [gi|187960092|ref|NP_035087|]
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N-glycosylase/DNA lyase isoform 1 [Mus musculus]

Protein Classification

N-glycosylase/DNA lyase( domain architecture ID 11489366)

N-glycosylase/DNA lyase specifically removes oxidatively damaged form of guanine (7,8-dihydro-8-oxoguanine or 7-oxoG) from DNA

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
ogg TIGR00588
8-oxoguanine DNA-glycosylase (ogg); All proteins in this family for which functions are known ...
11-328 0e+00

8-oxoguanine DNA-glycosylase (ogg); All proteins in this family for which functions are known are 8-oxo-guanaine 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). This family is distantly realted to the Nth-MutY superfamily. [DNA metabolism, DNA replication, recombination, and repair]


:

Pssm-ID: 211589 [Multi-domain]  Cd Length: 310  Bit Score: 546.05  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187960092   11 MRHRtlssspalWASIPCPRSELRLDLVLASGQSFRWK-EQSPAHWSG--VLADQ-VWTLTQTEDQLYCTVYRGDDsqvs 86
Cdd:TIGR00588   1 MGHR--------WASIPIPRSELRLDLVLRSGQSFRWRwEESPAHWSGllVIADQpVWTLTQTEEQLLCTVYRGDK---- 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187960092   87 rPTLEELET-LHKYFQLDVSLAQLYSHWASVDSHFQRVAQKFQGVRLLRQDPTECLFSFICSSNNNIARITGMVERLCQA 165
Cdd:TIGR00588  69 -PTQDELETkLEKYFQLDVSLAQLYTHWGSVDKHFQYVAQKFQGVRLLRQDPFECLISFICSSNNNIARITRMVERLCQA 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187960092  166 FGPRLIQLDDVTYHGFPNLHALAGPEAETHLRKLGLGYRARYVRASAKAILEEQGGPAWLQQLRVAPYEEAHKALCTLPG 245
Cdd:TIGR00588 148 FGPRLITLDGVTYHGFPSLHALTGPEAEAHLRKLGLGYRARYIRETARALLEEQGGRAWLQQIRGASYEDAREALCELPG 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187960092  246 VGAKVADCICLMALDKPQAVPVDVHVWQIAHRDYGWHPKTSQAKGPSPLANKELGNFFRNLWGPYAGWAQAVLFSADLRQ 325
Cdd:TIGR00588 228 VGPKVADCICLMGLDKPQAVPVDVHVWRIANRDYPWHPKTSRAKGPSPFARKELGNFFRSLWGPYAGWAQAVLFSADLRQ 307

                  ...
gi 187960092  326 PSL 328
Cdd:TIGR00588 308 GSH 310
 
Name Accession Description Interval E-value
ogg TIGR00588
8-oxoguanine DNA-glycosylase (ogg); All proteins in this family for which functions are known ...
11-328 0e+00

8-oxoguanine DNA-glycosylase (ogg); All proteins in this family for which functions are known are 8-oxo-guanaine 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). This family is distantly realted to the Nth-MutY superfamily. [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 211589 [Multi-domain]  Cd Length: 310  Bit Score: 546.05  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187960092   11 MRHRtlssspalWASIPCPRSELRLDLVLASGQSFRWK-EQSPAHWSG--VLADQ-VWTLTQTEDQLYCTVYRGDDsqvs 86
Cdd:TIGR00588   1 MGHR--------WASIPIPRSELRLDLVLRSGQSFRWRwEESPAHWSGllVIADQpVWTLTQTEEQLLCTVYRGDK---- 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187960092   87 rPTLEELET-LHKYFQLDVSLAQLYSHWASVDSHFQRVAQKFQGVRLLRQDPTECLFSFICSSNNNIARITGMVERLCQA 165
Cdd:TIGR00588  69 -PTQDELETkLEKYFQLDVSLAQLYTHWGSVDKHFQYVAQKFQGVRLLRQDPFECLISFICSSNNNIARITRMVERLCQA 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187960092  166 FGPRLIQLDDVTYHGFPNLHALAGPEAETHLRKLGLGYRARYVRASAKAILEEQGGPAWLQQLRVAPYEEAHKALCTLPG 245
Cdd:TIGR00588 148 FGPRLITLDGVTYHGFPSLHALTGPEAEAHLRKLGLGYRARYIRETARALLEEQGGRAWLQQIRGASYEDAREALCELPG 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187960092  246 VGAKVADCICLMALDKPQAVPVDVHVWQIAHRDYGWHPKTSQAKGPSPLANKELGNFFRNLWGPYAGWAQAVLFSADLRQ 325
Cdd:TIGR00588 228 VGPKVADCICLMGLDKPQAVPVDVHVWRIANRDYPWHPKTSRAKGPSPFARKELGNFFRSLWGPYAGWAQAVLFSADLRQ 307

                  ...
gi 187960092  326 PSL 328
Cdd:TIGR00588 308 GSH 310
AlkA COG0122
3-methyladenine DNA glycosylase/8-oxoguanine DNA glycosylase [Replication, recombination and ...
52-319 1.46e-46

3-methyladenine DNA glycosylase/8-oxoguanine DNA glycosylase [Replication, recombination and repair];


Pssm-ID: 439892 [Multi-domain]  Cd Length: 255  Bit Score: 158.51  E-value: 1.46e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187960092  52 PAHWSGVLADQVWTltQTEDQLYCTVYRGDDSQVSRPTLEELETLHKYFQLDVSLAQLYsHWASVDSHFQRVAQKFQGVR 131
Cdd:COG0122    1 PFDLDATLDDGTWR--RLPDGPGVVRMRPGGDALEVELAEAVARLRRLLDLDDDLEAIA-ALAARDPVLAPLIERYPGLR 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187960092 132 LLR-QDPTECLFSFICSSNNNIARITGMVERLCQAFGPRlIQLDDVTYHGFPNLHALAG-PEAEthLRKLGLG-YRARYV 208
Cdd:COG0122   78 LPRrPDPFEALVRAILGQQVSVAAARTIWRRLVALFGEP-IEGPGGGLYAFPTPEALAAaSEEE--LRACGLSrRKARYL 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187960092 209 RASAKAILEeqgGPAWLQQLRVAPYEEAHKALCTLPGVGAKVADCICLMALDKPQAVPV-DVHVWQIAHRDYGWHPKTSQ 287
Cdd:COG0122  155 RALARAVAD---GELDLEALAGLDDEEAIARLTALPGIGPWTAEMVLLFALGRPDAFPAgDLGLRRALGRLYGLGERPTP 231
                        250       260       270
                 ....*....|....*....|....*....|..
gi 187960092 288 akgpsplanKELGNFFRNlWGPYAGWAQAVLF 319
Cdd:COG0122  232 ---------KELRELAEP-WRPYRSYAARYLW 253
OGG_N pfam07934
8-oxoguanine DNA glycosylase, N-terminal domain; The presence of 8-oxoguanine residues in DNA ...
25-141 2.14e-45

8-oxoguanine DNA glycosylase, N-terminal domain; The presence of 8-oxoguanine residues in DNA can give rise to G-C to T-A transversion mutations. This enzyme is found in archaeal, bacterial and eukaryotic species, and is specifically responsible for the process which leads to the removal of 8-oxoguanine residues. It has DNA glycosylase activity (EC:3.2.2.23) and DNA lyase activity (EC:4.2.99.18). The region featured in this family is the N-terminal domain, which is organized into a single copy of a TBP-like fold. The domain contributes residues to the 8-oxoguanine binding pocket.


Pssm-ID: 429744  Cd Length: 115  Bit Score: 150.85  E-value: 2.14e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187960092   25 SIPCPRSELRLDLVLASGQSFRWKEQSPAHWSGVLADQVWTLTQTEDQLYCTVYRGDDSQVSRPTLEELetLHKYFQLDV 104
Cdd:pfam07934   1 KLLISKEELDLKKTLLCGQSFRWKRTENTSYTGVIGGRVVELKQDEDDLIYRCVNDSDPLLKEEDFESI--LSDYFDLDV 78
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 187960092  105 SLAQLYSHWASVDSHFQRVAQKFQGVRLLRQDPTECL 141
Cdd:pfam07934  79 DLEKLYEDWSKKDPLFKKAADKFTGIRILRQDPWETL 115
ENDO3c cd00056
endonuclease III; includes endonuclease III (DNA-(apurinic or apyrimidinic site) lyase), ...
139-319 1.68e-35

endonuclease III; includes endonuclease III (DNA-(apurinic or apyrimidinic site) lyase), alkylbase DNA glycosidases (Alka-family) and other DNA glycosidases


Pssm-ID: 238013 [Multi-domain]  Cd Length: 158  Bit Score: 126.59  E-value: 1.68e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187960092 139 ECLFSFICSSNNNIARITGMVERLCQAFGPrliqlddvtyhgfpNLHALAGPEAEtHLRKLGLG----YRARYVRASAKA 214
Cdd:cd00056    2 EVLVSEILSQQTTDKAVNKAYERLFERYGP--------------TPEALAAADEE-ELRELIRSlgyrRKAKYLKELARA 66
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187960092 215 ILEEQGGpawlqqlRVAPYEEAHKALCTLPGVGAKVADCICLMALDKPqAVPVDVHVWQIAHRdYGWHPKTSQAkgpspl 294
Cdd:cd00056   67 IVEGFGG-------LVLDDPDAREELLALPGVGRKTANVVLLFALGPD-AFPVDTHVRRVLKR-LGLIPKKKTP------ 131
                        170       180
                 ....*....|....*....|....*..
gi 187960092 295 anKELGNFFRNLWGP--YAGWAQAVLF 319
Cdd:cd00056  132 --EELEELLEELLPKpyWGEANQALMD 156
ENDO3c smart00478
endonuclease III; includes endonuclease III (DNA-(apurinic or apyrimidinic site) lyase), ...
146-315 1.02e-34

endonuclease III; includes endonuclease III (DNA-(apurinic or apyrimidinic site) lyase), alkylbase DNA glycosidases (Alka-family) and other DNA glycosidases


Pssm-ID: 214684 [Multi-domain]  Cd Length: 149  Bit Score: 124.30  E-value: 1.02e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187960092   146 CSSNNNIARITGMVERLCQAFGPrliqlddvtyhgFPNLHALAGPEAETHLRKLGLGY-RARYVRASAKAILEEQGGPaw 224
Cdd:smart00478   1 LSQQTTDERVNKATERLFEKFPT------------PEDLAAADEEELEELIRGLGFYRrKARYLIELARILVEEYGGE-- 66
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187960092   225 lqqlrvapYEEAHKALCTLPGVGAKVADCICLMALDKPqAVPVDVHVWQIAHRdYGWHPKTSQAKGPSPLANKELG-NFF 303
Cdd:smart00478  67 --------VPDDREELLKLPGVGRKTANAVLSFALGKP-FIPVDTHVLRIAKR-LGLVDKKSTPEEVEKLLEKLLPeEDW 136
                          170
                   ....*....|..
gi 187960092   304 RNLWGPYAGWAQ 315
Cdd:smart00478 137 RELNLLLIDFGR 148
 
Name Accession Description Interval E-value
ogg TIGR00588
8-oxoguanine DNA-glycosylase (ogg); All proteins in this family for which functions are known ...
11-328 0e+00

8-oxoguanine DNA-glycosylase (ogg); All proteins in this family for which functions are known are 8-oxo-guanaine 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). This family is distantly realted to the Nth-MutY superfamily. [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 211589 [Multi-domain]  Cd Length: 310  Bit Score: 546.05  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187960092   11 MRHRtlssspalWASIPCPRSELRLDLVLASGQSFRWK-EQSPAHWSG--VLADQ-VWTLTQTEDQLYCTVYRGDDsqvs 86
Cdd:TIGR00588   1 MGHR--------WASIPIPRSELRLDLVLRSGQSFRWRwEESPAHWSGllVIADQpVWTLTQTEEQLLCTVYRGDK---- 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187960092   87 rPTLEELET-LHKYFQLDVSLAQLYSHWASVDSHFQRVAQKFQGVRLLRQDPTECLFSFICSSNNNIARITGMVERLCQA 165
Cdd:TIGR00588  69 -PTQDELETkLEKYFQLDVSLAQLYTHWGSVDKHFQYVAQKFQGVRLLRQDPFECLISFICSSNNNIARITRMVERLCQA 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187960092  166 FGPRLIQLDDVTYHGFPNLHALAGPEAETHLRKLGLGYRARYVRASAKAILEEQGGPAWLQQLRVAPYEEAHKALCTLPG 245
Cdd:TIGR00588 148 FGPRLITLDGVTYHGFPSLHALTGPEAEAHLRKLGLGYRARYIRETARALLEEQGGRAWLQQIRGASYEDAREALCELPG 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187960092  246 VGAKVADCICLMALDKPQAVPVDVHVWQIAHRDYGWHPKTSQAKGPSPLANKELGNFFRNLWGPYAGWAQAVLFSADLRQ 325
Cdd:TIGR00588 228 VGPKVADCICLMGLDKPQAVPVDVHVWRIANRDYPWHPKTSRAKGPSPFARKELGNFFRSLWGPYAGWAQAVLFSADLRQ 307

                  ...
gi 187960092  326 PSL 328
Cdd:TIGR00588 308 GSH 310
AlkA COG0122
3-methyladenine DNA glycosylase/8-oxoguanine DNA glycosylase [Replication, recombination and ...
52-319 1.46e-46

3-methyladenine DNA glycosylase/8-oxoguanine DNA glycosylase [Replication, recombination and repair];


Pssm-ID: 439892 [Multi-domain]  Cd Length: 255  Bit Score: 158.51  E-value: 1.46e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187960092  52 PAHWSGVLADQVWTltQTEDQLYCTVYRGDDSQVSRPTLEELETLHKYFQLDVSLAQLYsHWASVDSHFQRVAQKFQGVR 131
Cdd:COG0122    1 PFDLDATLDDGTWR--RLPDGPGVVRMRPGGDALEVELAEAVARLRRLLDLDDDLEAIA-ALAARDPVLAPLIERYPGLR 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187960092 132 LLR-QDPTECLFSFICSSNNNIARITGMVERLCQAFGPRlIQLDDVTYHGFPNLHALAG-PEAEthLRKLGLG-YRARYV 208
Cdd:COG0122   78 LPRrPDPFEALVRAILGQQVSVAAARTIWRRLVALFGEP-IEGPGGGLYAFPTPEALAAaSEEE--LRACGLSrRKARYL 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187960092 209 RASAKAILEeqgGPAWLQQLRVAPYEEAHKALCTLPGVGAKVADCICLMALDKPQAVPV-DVHVWQIAHRDYGWHPKTSQ 287
Cdd:COG0122  155 RALARAVAD---GELDLEALAGLDDEEAIARLTALPGIGPWTAEMVLLFALGRPDAFPAgDLGLRRALGRLYGLGERPTP 231
                        250       260       270
                 ....*....|....*....|....*....|..
gi 187960092 288 akgpsplanKELGNFFRNlWGPYAGWAQAVLF 319
Cdd:COG0122  232 ---------KELRELAEP-WRPYRSYAARYLW 253
OGG_N pfam07934
8-oxoguanine DNA glycosylase, N-terminal domain; The presence of 8-oxoguanine residues in DNA ...
25-141 2.14e-45

8-oxoguanine DNA glycosylase, N-terminal domain; The presence of 8-oxoguanine residues in DNA can give rise to G-C to T-A transversion mutations. This enzyme is found in archaeal, bacterial and eukaryotic species, and is specifically responsible for the process which leads to the removal of 8-oxoguanine residues. It has DNA glycosylase activity (EC:3.2.2.23) and DNA lyase activity (EC:4.2.99.18). The region featured in this family is the N-terminal domain, which is organized into a single copy of a TBP-like fold. The domain contributes residues to the 8-oxoguanine binding pocket.


Pssm-ID: 429744  Cd Length: 115  Bit Score: 150.85  E-value: 2.14e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187960092   25 SIPCPRSELRLDLVLASGQSFRWKEQSPAHWSGVLADQVWTLTQTEDQLYCTVYRGDDSQVSRPTLEELetLHKYFQLDV 104
Cdd:pfam07934   1 KLLISKEELDLKKTLLCGQSFRWKRTENTSYTGVIGGRVVELKQDEDDLIYRCVNDSDPLLKEEDFESI--LSDYFDLDV 78
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 187960092  105 SLAQLYSHWASVDSHFQRVAQKFQGVRLLRQDPTECL 141
Cdd:pfam07934  79 DLEKLYEDWSKKDPLFKKAADKFTGIRILRQDPWETL 115
ENDO3c cd00056
endonuclease III; includes endonuclease III (DNA-(apurinic or apyrimidinic site) lyase), ...
139-319 1.68e-35

endonuclease III; includes endonuclease III (DNA-(apurinic or apyrimidinic site) lyase), alkylbase DNA glycosidases (Alka-family) and other DNA glycosidases


Pssm-ID: 238013 [Multi-domain]  Cd Length: 158  Bit Score: 126.59  E-value: 1.68e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187960092 139 ECLFSFICSSNNNIARITGMVERLCQAFGPrliqlddvtyhgfpNLHALAGPEAEtHLRKLGLG----YRARYVRASAKA 214
Cdd:cd00056    2 EVLVSEILSQQTTDKAVNKAYERLFERYGP--------------TPEALAAADEE-ELRELIRSlgyrRKAKYLKELARA 66
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187960092 215 ILEEQGGpawlqqlRVAPYEEAHKALCTLPGVGAKVADCICLMALDKPqAVPVDVHVWQIAHRdYGWHPKTSQAkgpspl 294
Cdd:cd00056   67 IVEGFGG-------LVLDDPDAREELLALPGVGRKTANVVLLFALGPD-AFPVDTHVRRVLKR-LGLIPKKKTP------ 131
                        170       180
                 ....*....|....*....|....*..
gi 187960092 295 anKELGNFFRNLWGP--YAGWAQAVLF 319
Cdd:cd00056  132 --EELEELLEELLPKpyWGEANQALMD 156
ENDO3c smart00478
endonuclease III; includes endonuclease III (DNA-(apurinic or apyrimidinic site) lyase), ...
146-315 1.02e-34

endonuclease III; includes endonuclease III (DNA-(apurinic or apyrimidinic site) lyase), alkylbase DNA glycosidases (Alka-family) and other DNA glycosidases


Pssm-ID: 214684 [Multi-domain]  Cd Length: 149  Bit Score: 124.30  E-value: 1.02e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187960092   146 CSSNNNIARITGMVERLCQAFGPrliqlddvtyhgFPNLHALAGPEAETHLRKLGLGY-RARYVRASAKAILEEQGGPaw 224
Cdd:smart00478   1 LSQQTTDERVNKATERLFEKFPT------------PEDLAAADEEELEELIRGLGFYRrKARYLIELARILVEEYGGE-- 66
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187960092   225 lqqlrvapYEEAHKALCTLPGVGAKVADCICLMALDKPqAVPVDVHVWQIAHRdYGWHPKTSQAKGPSPLANKELG-NFF 303
Cdd:smart00478  67 --------VPDDREELLKLPGVGRKTANAVLSFALGKP-FIPVDTHVLRIAKR-LGLVDKKSTPEEVEKLLEKLLPeEDW 136
                          170
                   ....*....|..
gi 187960092   304 RNLWGPYAGWAQ 315
Cdd:smart00478 137 RELNLLLIDFGR 148
HhH-GPD pfam00730
HhH-GPD superfamily base excision DNA repair protein; This family contains a diverse range of ...
143-286 8.78e-24

HhH-GPD superfamily base excision DNA repair protein; This family contains a diverse range of structurally related DNA repair proteins. The superfamily is called the HhH-GPD family after its hallmark Helix-hairpin-helix and Gly/Pro rich loop followed by a conserved aspartate. This includes endonuclease III, EC:4.2.99.18 and MutY an A/G-specific adenine glycosylase, both have a C terminal 4Fe-4S cluster. The family also includes 8-oxoguanine DNA glycosylases. The methyl-CPG binding protein MBD4 also contains a related domain that is a thymine DNA glycosylase. The family also includes DNA-3-methyladenine glycosylase II EC:3.2.2.21 and other members of the AlkA family.


Pssm-ID: 425841 [Multi-domain]  Cd Length: 141  Bit Score: 95.04  E-value: 8.78e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187960092  143 SFICSSNNNIARITGMVERLCQAFgprliqlddvtyhgFPNLHALAGPEaETHLRKL--GLGY---RARYVRASAKAILE 217
Cdd:pfam00730   2 SAILSQQTSDKAVNKITERLFEKF--------------FPTPEDLADAD-EEELRELirGLGFyrrKAKYLKELARILVE 66
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187960092  218 EQGGpawlqqlRVAPYEEAHKALctLPGVGAKVADCICLMALDKPQAVP-VDVHVWQIAHRDYGWHPKTS 286
Cdd:pfam00730  67 GYGG-------EVPLDEEELEAL--LKGVGRWTAEAVLIFALGRPDPLPvVDTHVRRVLKRLGLIKEKPT 127
Nth COG0177
Endonuclease III [Replication, recombination and repair];
181-277 1.04e-14

Endonuclease III [Replication, recombination and repair];


Pssm-ID: 439947 [Multi-domain]  Cd Length: 198  Bit Score: 71.67  E-value: 1.04e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187960092 181 FPNLHAL--AGPEA-ETHLRKLGLgYR--ARYVRASAKAILEEQGGPAwlqqlrvapyEEAHKALCTLPGVGAKVADCIC 255
Cdd:COG0177   49 YPTPEALaaADLEElEELIRPIGL-YRnkAKNIIALARILVEKYGGEV----------PETREELESLPGVGRKTANVVL 117
                         90       100
                 ....*....|....*....|..
gi 187960092 256 LMALDKPqAVPVDVHVWQIAHR 277
Cdd:COG0177  118 NFAFGKP-AIAVDTHVHRVSNR 138
MutY COG1194
Adenine-specific DNA glycosylase, acts on AG and A-oxoG pairs [Replication, recombination and ...
181-268 8.32e-05

Adenine-specific DNA glycosylase, acts on AG and A-oxoG pairs [Replication, recombination and repair];


Pssm-ID: 440807 [Multi-domain]  Cd Length: 350  Bit Score: 43.97  E-value: 8.32e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187960092 181 FPNLHALAG-PEAEthLRKL--GLGY--RARYVRASAKAILEEQGG--PawlqqlrvapyeEAHKALCTLPGVGAKVADC 253
Cdd:COG1194   58 FPTVEALAAaPEDE--VLKLweGLGYysRARNLHKAAQQVVEEHGGvfP------------DTYEELLALPGIGPYTAAA 123
                         90
                 ....*....|....*
gi 187960092 254 ICLMALDKPQAVpVD 268
Cdd:COG1194  124 IASIAFGEPAPI-VD 137
HP0602 COG2231
3-Methyladenine DNA glycosylase, HhH-GPD/Endo3 superfamily [Replication, recombination and ...
203-262 8.63e-04

3-Methyladenine DNA glycosylase, HhH-GPD/Endo3 superfamily [Replication, recombination and repair];


Pssm-ID: 441832 [Multi-domain]  Cd Length: 220  Bit Score: 40.21  E-value: 8.63e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 187960092 203 YR--ARYVRASAKAILEEQGGPawLQQLRVAPYEEAHKALCTLPGVGAKVADCICLMALDKP 262
Cdd:COG2231   83 YNqkAKRLKNLARWLVERYGGG--LEKLKALPTEELREELLSLKGIGPETADSILLYAFNRP 142
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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