NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|941355860|ref|NP_001303676|]
View 

adenine DNA glycosylase isoform b [Mus musculus]

Protein Classification

A/G-specific adenine glycosylase( domain architecture ID 11439777)

A/G-specific adenine glycosylase prevents DNA mutations by excising adenine (A) from the oxidatively damaged guanine (7,8-dihydro-8-oxoguanine or 7-oxoG):adenine base pair

EC:  3.2.2.-
Gene Ontology:  GO:0046872|GO:0000701|GO:0006284|GO:0051539
PubMed:  19778963|26673696

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
MutY COG1194
Adenine-specific DNA glycosylase, acts on AG and A-oxoG pairs [Replication, recombination and ...
 63-406 9.74e-116

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: 343.27  E-value: 9.74e-116
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941355860  63 MLKWPKLQDLASASLEEVNQLWSGLGYYSRGRRLQEGARKVVEELGGHMPRTAETLQQLlPGVGRYTAGAIASIAFDQVT 142
Cdd:COG1194   55 LERFPTVEALAAAPEDEVLKLWEGLGYYSRARNLHKAAQQVVEEHGGVFPDTYEELLAL-PGIGPYTAAAIASIAFGEPA 133

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941355860 143 GVVDGNVLRVLCRVRAIGADPTSTLVSHHLWNLAQQLVDPARPGDFNQAAMELGATVCTPQRPLCSHCPVQSLCRAYQRv 222
Cdd:COG1194  134 PIVDGNVKRVLSRLFAIEGPIGSPAAKKELWALAEELLPPERPGDFNQALMDLGATVCTPKKPKCLLCPLQDDCAAFAE- 212

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941355860 223 qrgqlsalpGRPdieecalntrqcqlcltssspwdpsmgvANFPRKASRRPPREEYSATCVVEQPGAiggplVLLVQRPD 302
Cdd:COG1194  213 ---------GRQ----------------------------EELPVKKPKKKKPERYGAALVIRDDGR-----VLLEKRPP 250

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941355860 303 SGLLAGLWEFPSVtlEPSEQHQHKALLQELQRWCGpLPAIRLQHLGEVIHIFSHIKLTYQVYSLALDQAPAStAPPGARW 382
Cdd:COG1194  251 KGLWGGLWEFPEF--EWEEAEDPEALERWLREELG-LEVEWLEPLGTVRHVFTHFRLHLTVYLARVPAGPPA-EPDGGRW 326

                        330       340
                 ....*....|....*....|....
gi 941355860 383 LTWEEFCNAAVSTAMKKVFRMYED 406
Cdd:COG1194  327 VPLEELAALPLPAPMRKLLKALLK 350
 
Name Accession Description Interval E-value
MutY COG1194
Adenine-specific DNA glycosylase, acts on AG and A-oxoG pairs [Replication, recombination and ...
 63-406 9.74e-116

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: 343.27  E-value: 9.74e-116
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941355860  63 MLKWPKLQDLASASLEEVNQLWSGLGYYSRGRRLQEGARKVVEELGGHMPRTAETLQQLlPGVGRYTAGAIASIAFDQVT 142
Cdd:COG1194   55 LERFPTVEALAAAPEDEVLKLWEGLGYYSRARNLHKAAQQVVEEHGGVFPDTYEELLAL-PGIGPYTAAAIASIAFGEPA 133

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941355860 143 GVVDGNVLRVLCRVRAIGADPTSTLVSHHLWNLAQQLVDPARPGDFNQAAMELGATVCTPQRPLCSHCPVQSLCRAYQRv 222
Cdd:COG1194  134 PIVDGNVKRVLSRLFAIEGPIGSPAAKKELWALAEELLPPERPGDFNQALMDLGATVCTPKKPKCLLCPLQDDCAAFAE- 212

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941355860 223 qrgqlsalpGRPdieecalntrqcqlcltssspwdpsmgvANFPRKASRRPPREEYSATCVVEQPGAiggplVLLVQRPD 302
Cdd:COG1194  213 ---------GRQ----------------------------EELPVKKPKKKKPERYGAALVIRDDGR-----VLLEKRPP 250

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941355860 303 SGLLAGLWEFPSVtlEPSEQHQHKALLQELQRWCGpLPAIRLQHLGEVIHIFSHIKLTYQVYSLALDQAPAStAPPGARW 382
Cdd:COG1194  251 KGLWGGLWEFPEF--EWEEAEDPEALERWLREELG-LEVEWLEPLGTVRHVFTHFRLHLTVYLARVPAGPPA-EPDGGRW 326

                        330       340
                 ....*....|....*....|....
gi 941355860 383 LTWEEFCNAAVSTAMKKVFRMYED 406
Cdd:COG1194  327 VPLEELAALPLPAPMRKLLKALLK 350
PRK10880 PRK10880
adenine DNA glycosylase;
63-359 1.75e-46

adenine DNA glycosylase;


Pssm-ID: 182805 [Multi-domain]  Cd Length: 350  Bit Score: 164.11  E-value: 1.75e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941355860  63 MLKWPKLQDLASASLEEVNQLWSGLGYYSRGRRLQEGARKVVEELGGHMPRTAETLQQlLPGVGRYTAGAIASIAFDQVT 142
Cdd:PRK10880  56 MARFPTVTDLANAPLDEVLHLWTGLGYYARARNLHKAAQQVATLHGGEFPETFEEVAA-LPGVGRSTAGAILSLSLGKHF 134

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941355860 143 GVVDGNVLRVLCRVRAIGADPTSTLVSHHLWNLAQQlVDPARP-GDFNQAAMELGATVCTPQRPLCSHCPVQSLCRAYqr 221
Cdd:PRK10880 135 PILDGNVKRVLARCYAVSGWPGKKEVENRLWQLSEQ-VTPAVGvERFNQAMMDLGAMVCTRSKPKCELCPLQNGCIAY-- 211

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941355860 222 vqrgqlsalpgrpdieecalntrqcqlcltSSSPWdpsmgvANFPRKASRRPPREEYSATCVVEQpgaigGPLVLLVQRP 301
Cdd:PRK10880 212 ------------------------------ANHSW------ALYPGKKPKQTLPERTGYFLLLQH-----GDEVWLEQRP 250

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 941355860 302 DSGLLAGLWEFPSVTLEpseqhqhkallQELQRWCGP--LPAIRLQHLGEVIHIFSHIKL 359
Cdd:PRK10880 251 PSGLWGGLFCFPQFADE-----------EELRQWLAQrgIAADNLTQLTAFRHTFSHFHL 299
ENDO3c smart00478
endonuclease III; includes endonuclease III (DNA-(apurinic or apyrimidinic site) lyase), ...
 65-198 9.48e-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: 123.91  E-value: 9.48e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941355860    65 KWPKLQDLASASLEEVNQLWSGLG-YYSRGRRLQEGARKVVEELGGHMPRTAETLQQLlPGVGRYTAGAIASIAFDQVTG 143
Cdd:smart00478  20 KFPTPEDLAAADEEELEELIRGLGfYRRKARYLIELARILVEEYGGEVPDDREELLKL-PGVGRKTANAVLSFALGKPFI 98

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 941355860   144 VVDGNVLRVLCRVRAIGADPTstlvSHHLWNLAQQLVDPARPGDFNQAAMELGAT 198
Cdd:smart00478  99 PVDTHVLRIAKRLGLVDKKST----PEEVEKLLEKLLPEEDWRELNLLLIDFGRT 149
ENDO3c cd00056
endonuclease III; includes endonuclease III (DNA-(apurinic or apyrimidinic site) lyase), ...
 67-196 4.73e-33

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: 122.35  E-value: 4.73e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941355860  67 PKLQDLASASLEEVNQLWSGLGYYSRGRRLQEGARKVVEELGG---HMPRTAETLQQLlPGVGRYTAGAIASIAFDQVTG 143
Cdd:cd00056   31 PTPEALAAADEEELRELIRSLGYRRKAKYLKELARAIVEGFGGlvlDDPDAREELLAL-PGVGRKTANVVLLFALGPDAF 109

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 941355860 144 VVDGNVLRVLCRVRAIGADPTstlvSHHLWNLAQQLVDPARPGDFNQAAMELG 196
Cdd:cd00056  110 PVDTHVRRVLKRLGLIPKKKT----PEELEELLEELLPKPYWGEANQALMDLG 158
HhH-GPD pfam00730
HhH-GPD superfamily base excision DNA repair protein; This family contains a diverse range of ...
 66-178 1.11e-30

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: 115.46  E-value: 1.11e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941355860   66 WPKLQDLASASLEEVNQLWSGLGYY-SRGRRLQEGARKVVEELGGHMPRTAETLQQLLPGVGRYTAGAIASIAF--DQVT 142
Cdd:pfam00730  26 FPTPEDLADADEEELRELIRGLGFYrRKAKYLKELARILVEGYGGEVPLDEEELEALLKGVGRWTAEAVLIFALgrPDPL 105

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 941355860  143 GVVDGNVLRVLCRVRAIGADPTSTLVSHHLWNLAQQ 178
Cdd:pfam00730 106 PVVDTHVRRVLKRLGLIKEKPTPKEVERELEELWPP 141
nth TIGR01083
endonuclease III; This equivalog model identifes nth members of the pfam00730 superfamily ...
 65-207 8.46e-20

endonuclease III; This equivalog model identifes nth members of the pfam00730 superfamily (HhH-GPD: Helix-hairpin-helix and Gly/Pro rich loop followed by a conserved aspartate). The major members of the superfamily are nth and mutY. [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 273434 [Multi-domain]  Cd Length: 192  Bit Score: 87.05  E-value: 8.46e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941355860   65 KWPKLQDLASASLEEVNQLWSGLGYY-SRGRRLQEGARKVVEELGGHMPRTAETLQQLlPGVGRYTAGAIASIAFDQVTG 143
Cdd:TIGR01083  55 VYPTPQALAQAGLEELEEYIKSIGLYrNKAKNIIELCRKLVERYGGEVPEDREELVKL-PGVGRKTANVVLNVAFGIPAI 133

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 941355860  144 VVDGNVLRVLCRVR-AIGADPTST------LVSHHLWnlaqqlvdparpGDFNQAAMELGATVCTPQRPLC 207
Cdd:TIGR01083 134 AVDTHVFRVSNRLGlSKGKDPIKVeedlmkLVPREFW------------VKLHHWLILHGRYTCKARKPLC 192
 
Name Accession Description Interval E-value
MutY COG1194
Adenine-specific DNA glycosylase, acts on AG and A-oxoG pairs [Replication, recombination and ...
 63-406 9.74e-116

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: 343.27  E-value: 9.74e-116
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941355860  63 MLKWPKLQDLASASLEEVNQLWSGLGYYSRGRRLQEGARKVVEELGGHMPRTAETLQQLlPGVGRYTAGAIASIAFDQVT 142
Cdd:COG1194   55 LERFPTVEALAAAPEDEVLKLWEGLGYYSRARNLHKAAQQVVEEHGGVFPDTYEELLAL-PGIGPYTAAAIASIAFGEPA 133

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941355860 143 GVVDGNVLRVLCRVRAIGADPTSTLVSHHLWNLAQQLVDPARPGDFNQAAMELGATVCTPQRPLCSHCPVQSLCRAYQRv 222
Cdd:COG1194  134 PIVDGNVKRVLSRLFAIEGPIGSPAAKKELWALAEELLPPERPGDFNQALMDLGATVCTPKKPKCLLCPLQDDCAAFAE- 212

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941355860 223 qrgqlsalpGRPdieecalntrqcqlcltssspwdpsmgvANFPRKASRRPPREEYSATCVVEQPGAiggplVLLVQRPD 302
Cdd:COG1194  213 ---------GRQ----------------------------EELPVKKPKKKKPERYGAALVIRDDGR-----VLLEKRPP 250

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941355860 303 SGLLAGLWEFPSVtlEPSEQHQHKALLQELQRWCGpLPAIRLQHLGEVIHIFSHIKLTYQVYSLALDQAPAStAPPGARW 382
Cdd:COG1194  251 KGLWGGLWEFPEF--EWEEAEDPEALERWLREELG-LEVEWLEPLGTVRHVFTHFRLHLTVYLARVPAGPPA-EPDGGRW 326

                        330       340
                 ....*....|....*....|....
gi 941355860 383 LTWEEFCNAAVSTAMKKVFRMYED 406
Cdd:COG1194  327 VPLEELAALPLPAPMRKLLKALLK 350
PRK10880 PRK10880
adenine DNA glycosylase;
63-359 1.75e-46

adenine DNA glycosylase;


Pssm-ID: 182805 [Multi-domain]  Cd Length: 350  Bit Score: 164.11  E-value: 1.75e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941355860  63 MLKWPKLQDLASASLEEVNQLWSGLGYYSRGRRLQEGARKVVEELGGHMPRTAETLQQlLPGVGRYTAGAIASIAFDQVT 142
Cdd:PRK10880  56 MARFPTVTDLANAPLDEVLHLWTGLGYYARARNLHKAAQQVATLHGGEFPETFEEVAA-LPGVGRSTAGAILSLSLGKHF 134

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941355860 143 GVVDGNVLRVLCRVRAIGADPTSTLVSHHLWNLAQQlVDPARP-GDFNQAAMELGATVCTPQRPLCSHCPVQSLCRAYqr 221
Cdd:PRK10880 135 PILDGNVKRVLARCYAVSGWPGKKEVENRLWQLSEQ-VTPAVGvERFNQAMMDLGAMVCTRSKPKCELCPLQNGCIAY-- 211

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941355860 222 vqrgqlsalpgrpdieecalntrqcqlcltSSSPWdpsmgvANFPRKASRRPPREEYSATCVVEQpgaigGPLVLLVQRP 301
Cdd:PRK10880 212 ------------------------------ANHSW------ALYPGKKPKQTLPERTGYFLLLQH-----GDEVWLEQRP 250

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 941355860 302 DSGLLAGLWEFPSVTLEpseqhqhkallQELQRWCGP--LPAIRLQHLGEVIHIFSHIKL 359
Cdd:PRK10880 251 PSGLWGGLFCFPQFADE-----------EELRQWLAQrgIAADNLTQLTAFRHTFSHFHL 299
ENDO3c smart00478
endonuclease III; includes endonuclease III (DNA-(apurinic or apyrimidinic site) lyase), ...
 65-198 9.48e-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: 123.91  E-value: 9.48e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941355860    65 KWPKLQDLASASLEEVNQLWSGLG-YYSRGRRLQEGARKVVEELGGHMPRTAETLQQLlPGVGRYTAGAIASIAFDQVTG 143
Cdd:smart00478  20 KFPTPEDLAAADEEELEELIRGLGfYRRKARYLIELARILVEEYGGEVPDDREELLKL-PGVGRKTANAVLSFALGKPFI 98

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 941355860   144 VVDGNVLRVLCRVRAIGADPTstlvSHHLWNLAQQLVDPARPGDFNQAAMELGAT 198
Cdd:smart00478  99 PVDTHVLRIAKRLGLVDKKST----PEEVEKLLEKLLPEEDWRELNLLLIDFGRT 149
ENDO3c cd00056
endonuclease III; includes endonuclease III (DNA-(apurinic or apyrimidinic site) lyase), ...
 67-196 4.73e-33

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: 122.35  E-value: 4.73e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941355860  67 PKLQDLASASLEEVNQLWSGLGYYSRGRRLQEGARKVVEELGG---HMPRTAETLQQLlPGVGRYTAGAIASIAFDQVTG 143
Cdd:cd00056   31 PTPEALAAADEEELRELIRSLGYRRKAKYLKELARAIVEGFGGlvlDDPDAREELLAL-PGVGRKTANVVLLFALGPDAF 109

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 941355860 144 VVDGNVLRVLCRVRAIGADPTstlvSHHLWNLAQQLVDPARPGDFNQAAMELG 196
Cdd:cd00056  110 PVDTHVRRVLKRLGLIPKKKT----PEELEELLEELLPKPYWGEANQALMDLG 158
HhH-GPD pfam00730
HhH-GPD superfamily base excision DNA repair protein; This family contains a diverse range of ...
 66-178 1.11e-30

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: 115.46  E-value: 1.11e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941355860   66 WPKLQDLASASLEEVNQLWSGLGYY-SRGRRLQEGARKVVEELGGHMPRTAETLQQLLPGVGRYTAGAIASIAF--DQVT 142
Cdd:pfam00730  26 FPTPEDLADADEEELRELIRGLGFYrRKAKYLKELARILVEGYGGEVPLDEEELEALLKGVGRWTAEAVLIFALgrPDPL 105

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 941355860  143 GVVDGNVLRVLCRVRAIGADPTSTLVSHHLWNLAQQ 178
Cdd:pfam00730 106 PVVDTHVRRVLKRLGLIKEKPTPKEVERELEELWPP 141
NUDIX_DNA_Glycosylase_C-MutY cd03431
C-terminal domain of DNA glycosylase; DNA glycosylase (MutY in bacteria and hMYH in humans) is ...
 274-401 2.47e-30

C-terminal domain of DNA glycosylase; DNA glycosylase (MutY in bacteria and hMYH in humans) is responsible for repairing misread A*oxoG residues to C*G by removing the inappropriately paired adenine base from the DNA backbone. It belongs to the NUDIX hydrolase superfamily and is important for the repair of various genotoxic lesions. Enzymes belonging to this superfamily requires a divalent cation, such as Mg2+ or Mn2+ for their activity. They are also recognized by a highly conserved 23-residue NUDIX motif (GX5EX7REUXEEXGU, where U = I, L or V). However, DNA glycosylase does not seem to contain this signature motif. DNA glycosylase consists of 2 domains: the N-terminal domain contains the catalytic properties of the enzyme and the C-terminal domain affects substrate (oxoG) binding and enzymatic turnover. The C-terminal domain is highly similar to MutT, based on secondary structure and topology, despite low sequence identity. MutT sanitizes the nucleotide precursor pool by hydrolyzing oxo-dGTP to oxo-dGMO and inorganic pyrophosphate. The similarity strongly suggests that the two proteins share a common evolutionary origin.


Pssm-ID: 467537 [Multi-domain]  Cd Length: 118  Bit Score: 113.55  E-value: 2.47e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941355860 274 PREEYSATCVVEQPGAiggplVLLVQRPDSGLLAGLWEFPSVTLEPSEQhqhkaLLQELQRWCGPLPAIRLQHLGEVIHI 353
Cdd:cd03431    1 VPERYFTVLVLRDGGR-----VLLEKRPEKGLLAGLWEFPLVETEEEEE-----EAEALLGLLAEELLLILEPLGEVKHV 70

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 941355860 354 FSHIKLTYQVYSLALDQAPAsTAPPGARWLTWEEFCNAAVSTAMKKVF 401
Cdd:cd03431   71 FSHFRLHITVYLVELPEAPP-AAPDEGRWVDLEELDEYALPAPMRKLL 117
Nth COG0177
Endonuclease III [Replication, recombination and repair];
65-220 1.04e-27

Endonuclease III [Replication, recombination and repair];


Pssm-ID: 439947 [Multi-domain]  Cd Length: 198  Bit Score: 109.03  E-value: 1.04e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941355860  65 KWPKLQDLASASLEEVNQLWSGLGYY-SRGRRLQEGARKVVEELGGHMPRTAETLQQLlPGVGRYTAGAIASIAFDQVTG 143
Cdd:COG0177   48 RYPTPEALAAADLEELEELIRPIGLYrNKAKNIIALARILVEKYGGEVPETREELESL-PGVGRKTANVVLNFAFGKPAI 126

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 941355860 144 VVDGNVLRVLCRvraIG-ADPTSTL-VSHHLwnlaQQLVDPARPGDFNQAAMELGATVCTPQRPLCSHCPVQSLCRAYQ 220
Cdd:COG0177  127 AVDTHVHRVSNR---LGlVPGKDPEeVEKDL----MKLIPKEYWGDLHHLLILHGRYICKARKPKCEECPLADLCPYYG 198
PRK13910 PRK13910
DNA glycosylase MutY; Provisional
 62-227 3.15e-27

DNA glycosylase MutY; Provisional


Pssm-ID: 172427 [Multi-domain]  Cd Length: 289  Bit Score: 110.50  E-value: 3.15e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941355860  62 PMLK-WPKLQDLASASLEEVNQLWSGLGYYSRGRRLQEGARKVVEELGGHMPRTAETLQQlLPGVGRYTAGAIASIAFDQ 140
Cdd:PRK13910  17 PFLEaFPTLKDLANAPLEEVLLLWRGLGYYSRAKNLKKSAEICVKEHHSQLPNDYQSLLK-LPGIGAYTANAILCFGFRE 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941355860 141 VTGVVDGNVLRVLCRVraIGADPTSTlvSHHLWNLAQQLVDPARPGDFNQAAMELGATVCTPqRPLCSHCPVQSLCRAYQ 220
Cdd:PRK13910  96 KSACVDANIKRVLLRL--FGLDPNIH--AKDLQIKANDFLNLNESFNHNQALIDLGALICSP-KPKCAICPLNPYCLGKN 170


                 ....*..
gi 941355860 221 RVQRGQL 227
Cdd:PRK13910 171 NPEKHTL 177
NUDIX_4 pfam14815
NUDIX domain;
295-403 1.87e-22

NUDIX domain;


Pssm-ID: 464330 [Multi-domain]  Cd Length: 114  Bit Score: 91.99  E-value: 1.87e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941355860  295 VLLVQRPDSGLLAGLWEFPSVTLEPSEqhqhkALLQELQRWCGPLPAIRLQHLGEVIHIFSHIKLTYQVYsLALDQAPAS 374
Cdd:pfam14815  12 VLLRKRPEKGLLGGLWEFPGGKVEPGE-----TLEEALARLEELGIEVEVLEPGTVKHVFTHFRLTLHVY-LVREVEGEE 85

                          90       100
                  ....*....|....*....|....*....
gi 941355860  375 TAPPGARWLTWEEFCNAAVSTAMKKVFRM 403
Cdd:pfam14815  86 EPQQELRWVTPEELDKYALPAAVRKILEA 114
nth TIGR01083
endonuclease III; This equivalog model identifes nth members of the pfam00730 superfamily ...
 65-207 8.46e-20

endonuclease III; This equivalog model identifes nth members of the pfam00730 superfamily (HhH-GPD: Helix-hairpin-helix and Gly/Pro rich loop followed by a conserved aspartate). The major members of the superfamily are nth and mutY. [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 273434 [Multi-domain]  Cd Length: 192  Bit Score: 87.05  E-value: 8.46e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941355860   65 KWPKLQDLASASLEEVNQLWSGLGYY-SRGRRLQEGARKVVEELGGHMPRTAETLQQLlPGVGRYTAGAIASIAFDQVTG 143
Cdd:TIGR01083  55 VYPTPQALAQAGLEELEEYIKSIGLYrNKAKNIIELCRKLVERYGGEVPEDREELVKL-PGVGRKTANVVLNVAFGIPAI 133

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 941355860  144 VVDGNVLRVLCRVR-AIGADPTST------LVSHHLWnlaqqlvdparpGDFNQAAMELGATVCTPQRPLC 207
Cdd:TIGR01083 134 AVDTHVFRVSNRLGlSKGKDPIKVeedlmkLVPREFW------------VKLHHWLILHGRYTCKARKPLC 192
HP0602 COG2231
3-Methyladenine DNA glycosylase, HhH-GPD/Endo3 superfamily [Replication, recombination and ...
 69-222 2.74e-07

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


Pssm-ID: 441832 [Multi-domain]  Cd Length: 220  Bit Score: 51.00  E-value: 2.74e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941355860  69 LQDLASASLEEVNQLWSGLGYYSR-GRRLQEGARKVVEELGGHMPR-----TAETLQQLL--PGVGRYTAGAIASIAFDQ 140
Cdd:COG2231   62 PEALAALDPEELAELIRPSGFYNQkAKRLKNLARWLVERYGGGLEKlkalpTEELREELLslKGIGPETADSILLYAFNR 141

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941355860 141 VTGVVDGNVLRVLCRVrAIGADPTStlvshhlWNLAQQLVDPARPGDFNQA----AM--ELGATVCTPqRPLCSHCPVQS 214
Cdd:COG2231  142 PVFVVDAYTRRIFSRL-GLIEEDAS-------YDELQRLFEENLPPDVALYnefhALivEHGKEYCKK-KPKCEECPLRD 212


                 ....*...
gi 941355860 215 LCRAYQRV 222
Cdd:COG2231  213 LCPYGGQE 220
PRK10702 PRK10702
endonuclease III; Provisional
 89-222 5.78e-06

endonuclease III; Provisional


Pssm-ID: 182661 [Multi-domain]  Cd Length: 211  Bit Score: 47.32  E-value: 5.78e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941355860  89 YYSRGRRLQEGARKVVEELGGHMPRTAETLQQLlPGVGRYTAGAIASIAFDQVTGVVDGNVLRVLCRVR-AIGAD----- 162
Cdd:PRK10702  82 YNSKAENVIKTCRILLEQHNGEVPEDRAALEAL-PGVGRKTANVVLNTAFGWPTIAVDTHIFRVCNRTQfAPGKNveqve 160

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 941355860 163 -------PTSTLVSHHLWNLAQqlvdparpgdfnqaamelGATVCTPQRPLCSHCPVQSLCRAYQRV 222
Cdd:PRK10702 161 ekllkvvPAEFKVDCHHWLILH------------------GRYTCIARKPRCGSCIIEDLCEYKEKV 209
PRK10546 PRK10546
pyrimidine (deoxy)nucleoside triphosphate diphosphatase;
283-333 2.91e-05

pyrimidine (deoxy)nucleoside triphosphate diphosphatase;


Pssm-ID: 182536 [Multi-domain]  Cd Length: 135  Bit Score: 43.58  E-value: 2.91e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 941355860 283 VVEQPGAIggplvLLVQRPDSGLLAGLWEFPSVTLEPSEQhQHKALLQELQ 333
Cdd:PRK10546  10 IIERDGKI-----LLAQRPAHSDQAGLWEFAGGKVEPGES-QPQALIRELR 54
HHH pfam00633
Helix-hairpin-helix motif; The helix-hairpin-helix DNA-binding motif is found to be duplicated ...
 106-136 8.67e-05

Helix-hairpin-helix motif; The helix-hairpin-helix DNA-binding motif is found to be duplicated in the central domain of RuvA. The HhH domain of DisA, a bacterial checkpoint control protein, is a DNA-binding domain.


Pssm-ID: 425789 [Multi-domain]  Cd Length: 30  Bit Score: 39.32  E-value: 8.67e-05
                          10        20        30
                  ....*....|....*....|....*....|.
gi 941355860  106 ELGGHMPRTAETLQQLlPGVGRYTAGAIASI 136
Cdd:pfam00633   1 SLEGLIPASVEELLAL-PGVGPKTAEAILSY 30
NUDIX_MutT_NudA_like cd03425
MutT pyrophosphohydrolase; The MutT pyrophosphohydrolase is a prototypical NUDIX hydrolase ...
 295-387 3.03e-04

MutT pyrophosphohydrolase; The MutT pyrophosphohydrolase is a prototypical NUDIX hydrolase that catalyzes the hydrolysis of nucleoside and deoxynucleoside triphosphates (NTPs and dNTPs) by substitution at a beta-phosphorus to yield a nucleotide monophosphate (NMP) and inorganic pyrophosphate (PPi). This enzyme requires two divalent cations for activity; one coordinates the phosphoryl groups of the NTP/dNTP substrate, and the other coordinates to the enzyme. It also contains the NUDIX motif, a highly conserved 23-residue block (GX5EX7REUXEEXGU, where U = I, L or V), that functions as metal binding and catalytic site. MutT pyrophosphohydrolase is important in preventing errors in DNA replication by hydrolyzing mutagenic nucleotides such as 8-oxo-dGTP (a product of oxidative damage), which can mispair with template adenine during DNA replication, to guanine nucleotides.


Pssm-ID: 467531 [Multi-domain]  Cd Length: 123  Bit Score: 40.51  E-value: 3.03e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941355860 295 VLLVQRPDSGLLAGLWEFPSVTLEPSEQHQHkALLQELQRWCGpLPAIRLQHLGEVIHIFSHIKLTYQVYS-LALDQAPA 373
Cdd:cd03425   14 VLIAQRPEGKHLAGLWEFPGGKVEPGETPEQ-ALVRELREELG-IEVEVGEPLGTVEHDYPDFHVRLHVYLcTLWSGEPQ 91

                         90
                 ....*....|....
gi 941355860 374 STAPPGARWLTWEE 387
Cdd:cd03425   92 LLEHQELRWVTPEE 105
FES smart00525
iron-sulpphur binding domain in DNA-(apurinic or apyrimidinic site) lyase (subfamily of ENDO3); ...
 199-219 3.75e-04

iron-sulpphur binding domain in DNA-(apurinic or apyrimidinic site) lyase (subfamily of ENDO3);


Pssm-ID: 197771 [Multi-domain]  Cd Length: 21  Bit Score: 37.53  E-value: 3.75e-04
                           10        20
                   ....*....|....*....|.
gi 941355860   199 VCTPQRPLCSHCPVQSLCRAY 219
Cdd:smart00525   1 ICTARKPRCDECPLKDLCPAY 21
MutT COG0494
8-oxo-dGTP pyrophosphatase MutT and related house-cleaning NTP pyrophosphohydrolases, NUDIX ...
 295-400 2.86e-03

8-oxo-dGTP pyrophosphatase MutT and related house-cleaning NTP pyrophosphohydrolases, NUDIX family [Defense mechanisms];


Pssm-ID: 440260 [Multi-domain]  Cd Length: 143  Bit Score: 38.09  E-value: 2.86e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941355860 295 VLLVQRPDSGLLAGLWEFPSVTLEPSEQHQHkALLQELQ----------RWCGPLPAIRlqHLGEVIHIFsHIKLTYQVY 364
Cdd:COG0494   27 VLLVRRYRYGVGPGLWEFPGGKIEPGESPEE-AALRELReetgltaedlELLGELPSPG--YTDEKVHVF-LARGLGPGE 102

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 941355860 365 SLALDQAPASTAppgARWLTWEEFCNAAVSTAMKKV 400
Cdd:COG0494  103 EVGLDDEDEFIE---VRWVPLDEALALVTAGEIAKT 135
ogg TIGR00588
8-oxoguanine DNA-glycosylase (ogg); All proteins in this family for which functions are known ...
 27-155 3.17e-03

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: 39.51  E-value: 3.17e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 941355860   27 MSQLSEATCSAGMTKRSVTSLGETWQKKRPTRTGGPMLKWPKLQDLASASLE-EVNQLwsGLGYysRGRRLQEGARKVVE 105
Cdd:TIGR00588 124 ISFICSSNNNIARITRMVERLCQAFGPRLITLDGVTYHGFPSLHALTGPEAEaHLRKL--GLGY--RARYIRETARALLE 199

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 941355860  106 ELGGhmprtAETLQQL--------------LPGVGRYTAGAIASIAFDQVTGV-VDGNVLRVLCR 155
Cdd:TIGR00588 200 EQGG-----RAWLQQIrgasyedarealceLPGVGPKVADCICLMGLDKPQAVpVDVHVWRIANR 259
PRK10776 PRK10776
8-oxo-dGTP diphosphatase MutT;
299-359 3.69e-03

8-oxo-dGTP diphosphatase MutT;


Pssm-ID: 182721 [Multi-domain]  Cd Length: 129  Bit Score: 37.27  E-value: 3.69e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 941355860 299 QRPDSGLLAGLWEFPSVTLEPSEQHQhKALLQELQRWCGpLPAIRLQHLGEVIHIFS--HIKL 359
Cdd:PRK10776  22 RRAADAHMAGKWEFPGGKIEAGETPE-QALIRELQEEVG-ITVQHATLFEKLEYEFPdrHITL 82
EndIII_4Fe-2S pfam10576
Iron-sulfur binding domain of endonuclease III; Escherichia coli endonuclease III (EC 4.2.99. ...
 200-216 5.15e-03

Iron-sulfur binding domain of endonuclease III; Escherichia coli endonuclease III (EC 4.2.99.18) is a DNA repair enzyme that acts both as a DNA N-glycosylase, removing oxidized pyrimidines from DNA, and as an apurinic/apyrimidinic (AP) endonuclease, introducing a single-strand nick at the site from which the damaged base was removed. Endonuclease III is an iron-sulfur protein that binds a single 4Fe-4S cluster. The 4Fe-4S cluster does not seem to be important for catalytic activity, but is probably involved in the proper positioning of the enzyme along the DNA strand. The 4Fe-4S cluster is bound by four cysteines which are all located in a 17 amino acid region at the C-terminal end of endonuclease III. A similar region is also present in the central section of mutY and in the C-terminus of ORF-10 and of the Micro-coccus UV endonuclease.


Pssm-ID: 463153 [Multi-domain]  Cd Length: 17  Bit Score: 34.28  E-value: 5.15e-03
                          10
                  ....*....|....*..
gi 941355860  200 CTPQRPLCSHCPVQSLC 216
Cdd:pfam10576   1 CTARKPKCEECPLADLC 17
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH