NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1183596750|ref|NP_001337579|]
View 

adenine DNA glycosylase isoform 9 [Homo sapiens]

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 ...
 10-356 4.61e-120

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: 352.52  E-value: 4.61e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183596750  10 MLKWPTLQDLASASLEEVNQLWAGLGYYSRGRRLQEGARKVVEELGGHMPRTAETLQQLlPGVGRYTAGAIASIAFGQAT 89
Cdd:COG1194    55 LERFPTVEALAAAPEDEVLKLWEGLGYYSRARNLHKAAQQVVEEHGGVFPDTYEELLAL-PGIGPYTAAAIASIAFGEPA 133

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183596750  90 GVVDGNVARVLCRVRAIGADPSSTLVSQQLWGLAQQLVDPARPGDFNQAAMELGATVCTPQRPLCSQCPVESLCRARQRV 169
Cdd:COG1194   134 PIVDGNVKRVLSRLFAIEGPIGSPAAKKELWALAEELLPPERPGDFNQALMDLGATVCTPKKPKCLLCPLQDDCAAFAEG 213

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183596750 170 EQEQLlasgslsgspdveecapntgqchlclppsepwdqtlgvvnfPRKASRKPPREESSATCVLEQPGalgaQILLVQR 249
Cdd:COG1194   214 RQEEL-----------------------------------------PVKKPKKKKPERYGAALVIRDDG----RVLLEKR 248

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183596750 250 PNSGLLAGLWEFPSVTWEPSEQLQrkALLQELQRWAGpLPATHLRHLGEVVHTFSHIKLTYQVYGLALEGQTPVTtvPPG 329
Cdd:COG1194   249 PPKGLWGGLWEFPEFEWEEAEDPE--ALERWLREELG-LEVEWLEPLGTVRHVFTHFRLHLTVYLARVPAGPPAE--PDG 323

                         330       340
                  ....*....|....*....|....*..
gi 1183596750 330 ARWLTQEEFHTAAVSTAMKKVFRVYQG 356
Cdd:COG1194   324 GRWVPLEELAALPLPAPMRKLLKALLK 350
 
Name Accession Description Interval E-value
MutY COG1194
Adenine-specific DNA glycosylase, acts on AG and A-oxoG pairs [Replication, recombination and ...
 10-356 4.61e-120

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: 352.52  E-value: 4.61e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183596750  10 MLKWPTLQDLASASLEEVNQLWAGLGYYSRGRRLQEGARKVVEELGGHMPRTAETLQQLlPGVGRYTAGAIASIAFGQAT 89
Cdd:COG1194    55 LERFPTVEALAAAPEDEVLKLWEGLGYYSRARNLHKAAQQVVEEHGGVFPDTYEELLAL-PGIGPYTAAAIASIAFGEPA 133

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183596750  90 GVVDGNVARVLCRVRAIGADPSSTLVSQQLWGLAQQLVDPARPGDFNQAAMELGATVCTPQRPLCSQCPVESLCRARQRV 169
Cdd:COG1194   134 PIVDGNVKRVLSRLFAIEGPIGSPAAKKELWALAEELLPPERPGDFNQALMDLGATVCTPKKPKCLLCPLQDDCAAFAEG 213

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183596750 170 EQEQLlasgslsgspdveecapntgqchlclppsepwdqtlgvvnfPRKASRKPPREESSATCVLEQPGalgaQILLVQR 249
Cdd:COG1194   214 RQEEL-----------------------------------------PVKKPKKKKPERYGAALVIRDDG----RVLLEKR 248

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183596750 250 PNSGLLAGLWEFPSVTWEPSEQLQrkALLQELQRWAGpLPATHLRHLGEVVHTFSHIKLTYQVYGLALEGQTPVTtvPPG 329
Cdd:COG1194   249 PPKGLWGGLWEFPEFEWEEAEDPE--ALERWLREELG-LEVEWLEPLGTVRHVFTHFRLHLTVYLARVPAGPPAE--PDG 323

                         330       340
                  ....*....|....*....|....*..
gi 1183596750 330 ARWLTQEEFHTAAVSTAMKKVFRVYQG 356
Cdd:COG1194   324 GRWVPLEELAALPLPAPMRKLLKALLK 350
PRK10880 PRK10880
adenine DNA glycosylase;
10-308 4.49e-50

adenine DNA glycosylase;


Pssm-ID: 182805 [Multi-domain]  Cd Length: 350  Bit Score: 172.20  E-value: 4.49e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183596750  10 MLKWPTLQDLASASLEEVNQLWAGLGYYSRGRRLQEGARKVVEELGGHMPRTAETLQQlLPGVGRYTAGAIASIAFGQAT 89
Cdd:PRK10880   56 MARFPTVTDLANAPLDEVLHLWTGLGYYARARNLHKAAQQVATLHGGEFPETFEEVAA-LPGVGRSTAGAILSLSLGKHF 134

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183596750  90 GVVDGNVARVLCRVRAIGADPSSTLVSQQLWGLAQQlVDPARP-GDFNQAAMELGATVCTPQRPLCSQCPVESLCRARqr 168
Cdd:PRK10880  135 PILDGNVKRVLARCYAVSGWPGKKEVENRLWQLSEQ-VTPAVGvERFNQAMMDLGAMVCTRSKPKCELCPLQNGCIAY-- 211

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183596750 169 veqeqllASGSlsgspdveecapntgqchlclppsepWDQtlgvvnFPRKASRKPPREESSATCVLEQpgalGAQILLVQ 248
Cdd:PRK10880  212 -------ANHS--------------------------WAL------YPGKKPKQTLPERTGYFLLLQH----GDEVWLEQ 248

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1183596750 249 RPNSGLLAGLWEFPSVTWEpseqlqrkallQELQRW--AGPLPATHLRHLGEVVHTFSHIKL 308
Cdd:PRK10880  249 RPPSGLWGGLFCFPQFADE-----------EELRQWlaQRGIAADNLTQLTAFRHTFSHFHL 299
ENDO3c smart00478
endonuclease III; includes endonuclease III (DNA-(apurinic or apyrimidinic site) lyase), ...
 12-145 5.64e-35

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: 126.22  E-value: 5.64e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183596750   12 KWPTLQDLASASLEEVNQLWAGLG-YYSRGRRLQEGARKVVEELGGHMPRTAETLQQLlPGVGRYTAGAIASIAFGQATG 90
Cdd:smart00478  20 KFPTPEDLAAADEEELEELIRGLGfYRRKARYLIELARILVEEYGGEVPDDREELLKL-PGVGRKTANAVLSFALGKPFI 98

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1183596750   91 VVDGNVARVLCRVRAIGAdpssTLVSQQLWGLAQQLVDPARPGDFNQAAMELGAT 145
Cdd:smart00478  99 PVDTHVLRIAKRLGLVDK----KSTPEEVEKLLEKLLPEEDWRELNLLLIDFGRT 149
ENDO3c cd00056
endonuclease III; includes endonuclease III (DNA-(apurinic or apyrimidinic site) lyase), ...
 14-143 2.35e-34

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: 125.05  E-value: 2.35e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183596750  14 PTLQDLASASLEEVNQLWAGLGYYSRGRRLQEGARKVVEELGG---HMPRTAETLQQlLPGVGRYTAGAIASIAFGQATG 90
Cdd:cd00056    31 PTPEALAAADEEELRELIRSLGYRRKAKYLKELARAIVEGFGGlvlDDPDAREELLA-LPGVGRKTANVVLLFALGPDAF 109

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1183596750  91 VVDGNVARVLCRVRAIGADPSstlvSQQLWGLAQQLVDPARPGDFNQAAMELG 143
Cdd:cd00056   110 PVDTHVRRVLKRLGLIPKKKT----PEELEELLEELLPKPYWGEANQALMDLG 158
HhH-GPD pfam00730
HhH-GPD superfamily base excision DNA repair protein; This family contains a diverse range of ...
 13-125 6.73e-32

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: 117.77  E-value: 6.73e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183596750  13 WPTLQDLASASLEEVNQLWAGLGYY-SRGRRLQEGARKVVEELGGHMPRTAETLQQLLPGVGRYTAGAIASIAFG--QAT 89
Cdd:pfam00730  26 FPTPEDLADADEEELRELIRGLGFYrRKAKYLKELARILVEGYGGEVPLDEEELEALLKGVGRWTAEAVLIFALGrpDPL 105

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1183596750  90 GVVDGNVARVLCRVRAIGADPSSTLVSQQLWGLAQQ 125
Cdd:pfam00730 106 PVVDTHVRRVLKRLGLIKEKPTPKEVERELEELWPP 141
nth TIGR01083
endonuclease III; This equivalog model identifes nth members of the pfam00730 superfamily ...
 12-154 5.44e-22

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: 92.44  E-value: 5.44e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183596750  12 KWPTLQDLASASLEEVNQLWAGLGYY-SRGRRLQEGARKVVEELGGHMPRTAETLQQLlPGVGRYTAGAIASIAFGQATG 90
Cdd:TIGR01083  55 VYPTPQALAQAGLEELEEYIKSIGLYrNKAKNIIELCRKLVERYGGEVPEDREELVKL-PGVGRKTANVVLNVAFGIPAI 133

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1183596750  91 VVDGNVARVLCRVR-AIGADPSST------LVSQQLWglaqqlvdparpGDFNQAAMELGATVCTPQRPLC 154
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 ...
 10-356 4.61e-120

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: 352.52  E-value: 4.61e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183596750  10 MLKWPTLQDLASASLEEVNQLWAGLGYYSRGRRLQEGARKVVEELGGHMPRTAETLQQLlPGVGRYTAGAIASIAFGQAT 89
Cdd:COG1194    55 LERFPTVEALAAAPEDEVLKLWEGLGYYSRARNLHKAAQQVVEEHGGVFPDTYEELLAL-PGIGPYTAAAIASIAFGEPA 133

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183596750  90 GVVDGNVARVLCRVRAIGADPSSTLVSQQLWGLAQQLVDPARPGDFNQAAMELGATVCTPQRPLCSQCPVESLCRARQRV 169
Cdd:COG1194   134 PIVDGNVKRVLSRLFAIEGPIGSPAAKKELWALAEELLPPERPGDFNQALMDLGATVCTPKKPKCLLCPLQDDCAAFAEG 213

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183596750 170 EQEQLlasgslsgspdveecapntgqchlclppsepwdqtlgvvnfPRKASRKPPREESSATCVLEQPGalgaQILLVQR 249
Cdd:COG1194   214 RQEEL-----------------------------------------PVKKPKKKKPERYGAALVIRDDG----RVLLEKR 248

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183596750 250 PNSGLLAGLWEFPSVTWEPSEQLQrkALLQELQRWAGpLPATHLRHLGEVVHTFSHIKLTYQVYGLALEGQTPVTtvPPG 329
Cdd:COG1194   249 PPKGLWGGLWEFPEFEWEEAEDPE--ALERWLREELG-LEVEWLEPLGTVRHVFTHFRLHLTVYLARVPAGPPAE--PDG 323

                         330       340
                  ....*....|....*....|....*..
gi 1183596750 330 ARWLTQEEFHTAAVSTAMKKVFRVYQG 356
Cdd:COG1194   324 GRWVPLEELAALPLPAPMRKLLKALLK 350
PRK10880 PRK10880
adenine DNA glycosylase;
10-308 4.49e-50

adenine DNA glycosylase;


Pssm-ID: 182805 [Multi-domain]  Cd Length: 350  Bit Score: 172.20  E-value: 4.49e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183596750  10 MLKWPTLQDLASASLEEVNQLWAGLGYYSRGRRLQEGARKVVEELGGHMPRTAETLQQlLPGVGRYTAGAIASIAFGQAT 89
Cdd:PRK10880   56 MARFPTVTDLANAPLDEVLHLWTGLGYYARARNLHKAAQQVATLHGGEFPETFEEVAA-LPGVGRSTAGAILSLSLGKHF 134

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183596750  90 GVVDGNVARVLCRVRAIGADPSSTLVSQQLWGLAQQlVDPARP-GDFNQAAMELGATVCTPQRPLCSQCPVESLCRARqr 168
Cdd:PRK10880  135 PILDGNVKRVLARCYAVSGWPGKKEVENRLWQLSEQ-VTPAVGvERFNQAMMDLGAMVCTRSKPKCELCPLQNGCIAY-- 211

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183596750 169 veqeqllASGSlsgspdveecapntgqchlclppsepWDQtlgvvnFPRKASRKPPREESSATCVLEQpgalGAQILLVQ 248
Cdd:PRK10880  212 -------ANHS--------------------------WAL------YPGKKPKQTLPERTGYFLLLQH----GDEVWLEQ 248

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1183596750 249 RPNSGLLAGLWEFPSVTWEpseqlqrkallQELQRW--AGPLPATHLRHLGEVVHTFSHIKL 308
Cdd:PRK10880  249 RPPSGLWGGLFCFPQFADE-----------EELRQWlaQRGIAADNLTQLTAFRHTFSHFHL 299
ENDO3c smart00478
endonuclease III; includes endonuclease III (DNA-(apurinic or apyrimidinic site) lyase), ...
 12-145 5.64e-35

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: 126.22  E-value: 5.64e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183596750   12 KWPTLQDLASASLEEVNQLWAGLG-YYSRGRRLQEGARKVVEELGGHMPRTAETLQQLlPGVGRYTAGAIASIAFGQATG 90
Cdd:smart00478  20 KFPTPEDLAAADEEELEELIRGLGfYRRKARYLIELARILVEEYGGEVPDDREELLKL-PGVGRKTANAVLSFALGKPFI 98

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1183596750   91 VVDGNVARVLCRVRAIGAdpssTLVSQQLWGLAQQLVDPARPGDFNQAAMELGAT 145
Cdd:smart00478  99 PVDTHVLRIAKRLGLVDK----KSTPEEVEKLLEKLLPEEDWRELNLLLIDFGRT 149
ENDO3c cd00056
endonuclease III; includes endonuclease III (DNA-(apurinic or apyrimidinic site) lyase), ...
 14-143 2.35e-34

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: 125.05  E-value: 2.35e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183596750  14 PTLQDLASASLEEVNQLWAGLGYYSRGRRLQEGARKVVEELGG---HMPRTAETLQQlLPGVGRYTAGAIASIAFGQATG 90
Cdd:cd00056    31 PTPEALAAADEEELRELIRSLGYRRKAKYLKELARAIVEGFGGlvlDDPDAREELLA-LPGVGRKTANVVLLFALGPDAF 109

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1183596750  91 VVDGNVARVLCRVRAIGADPSstlvSQQLWGLAQQLVDPARPGDFNQAAMELG 143
Cdd:cd00056   110 PVDTHVRRVLKRLGLIPKKKT----PEELEELLEELLPKPYWGEANQALMDLG 158
HhH-GPD pfam00730
HhH-GPD superfamily base excision DNA repair protein; This family contains a diverse range of ...
 13-125 6.73e-32

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: 117.77  E-value: 6.73e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183596750  13 WPTLQDLASASLEEVNQLWAGLGYY-SRGRRLQEGARKVVEELGGHMPRTAETLQQLLPGVGRYTAGAIASIAFG--QAT 89
Cdd:pfam00730  26 FPTPEDLADADEEELRELIRGLGFYrRKAKYLKELARILVEGYGGEVPLDEEELEALLKGVGRWTAEAVLIFALGrpDPL 105

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1183596750  90 GVVDGNVARVLCRVRAIGADPSSTLVSQQLWGLAQQ 125
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 ...
 224-351 7.49e-31

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: 114.32  E-value: 7.49e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183596750 224 PREESSATCVLEQPGalgaQILLVQRPNSGLLAGLWEFPSVTWEPSEQlqrkaLLQELQRWAGPLPATHLRHLGEVVHTF 303
Cdd:cd03431     1 VPERYFTVLVLRDGG----RVLLEKRPEKGLLAGLWEFPLVETEEEEE-----EAEALLGLLAEELLLILEPLGEVKHVF 71

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1183596750 304 SHIKLTYQVYGLALEGQTPVTtvPPGARWLTQEEFHTAAVSTAMKKVF 351
Cdd:cd03431    72 SHFRLHITVYLVELPEAPPAA--PDEGRWVDLEELDEYALPAPMRKLL 117
Nth COG0177
Endonuclease III [Replication, recombination and repair];
12-167 8.38e-31

Endonuclease III [Replication, recombination and repair];


Pssm-ID: 439947 [Multi-domain]  Cd Length: 198  Bit Score: 116.73  E-value: 8.38e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183596750  12 KWPTLQDLASASLEEVNQLWAGLGYY-SRGRRLQEGARKVVEELGGHMPRTAETLQQLlPGVGRYTAGAIASIAFGQATG 90
Cdd:COG0177    48 RYPTPEALAAADLEELEELIRPIGLYrNKAKNIIALARILVEKYGGEVPETREELESL-PGVGRKTANVVLNFAFGKPAI 126

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1183596750  91 VVDGNVARVLCRvraIG-ADPSSTL-VSQQLwglaQQLVDPARPGDFNQAAMELGATVCTPQRPLCSQCPVESLCRARQ 167
Cdd:COG0177   127 AVDTHVHRVSNR---LGlVPGKDPEeVEKDL----MKLIPKEYWGDLHHLLILHGRYICKARKPKCEECPLADLCPYYG 198
PRK13910 PRK13910
DNA glycosylase MutY; Provisional
 13-174 7.92e-30

DNA glycosylase MutY; Provisional


Pssm-ID: 172427 [Multi-domain]  Cd Length: 289  Bit Score: 116.66  E-value: 7.92e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183596750  13 WPTLQDLASASLEEVNQLWAGLGYYSRGRRLQEGARKVVEELGGHMPRTAETLQQlLPGVGRYTAGAIASIAFGQATGVV 92
Cdd:PRK13910   22 FPTLKDLANAPLEEVLLLWRGLGYYSRAKNLKKSAEICVKEHHSQLPNDYQSLLK-LPGIGAYTANAILCFGFREKSACV 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183596750  93 DGNVARVLCRVraIGADPSSTlvSQQLWGLAQQLVDPARPGDFNQAAMELGATVCTPqRPLCSQCPVESLCRARQRVEQE 172
Cdd:PRK13910  101 DANIKRVLLRL--FGLDPNIH--AKDLQIKANDFLNLNESFNHNQALIDLGALICSP-KPKCAICPLNPYCLGKNNPEKH 175


                  ..
gi 1183596750 173 QL 174
Cdd:PRK13910  176 TL 177
NUDIX_4 pfam14815
NUDIX domain;
243-352 3.33e-23

NUDIX domain;


Pssm-ID: 464330 [Multi-domain]  Cd Length: 114  Bit Score: 93.53  E-value: 3.33e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183596750 243 QILLVQRPNSGLLAGLWEFPSVTWEPSEQLQRKalLQELQRWAgpLPATHLRHlGEVVHTFSHIKLTYQVYGLALEGQTP 322
Cdd:pfam14815  11 RVLLRKRPEKGLLGGLWEFPGGKVEPGETLEEA--LARLEELG--IEVEVLEP-GTVKHVFTHFRLTLHVYLVREVEGEE 85

                          90       100       110
                  ....*....|....*....|....*....|
gi 1183596750 323 vtTVPPGARWLTQEEFHTAAVSTAMKKVFR 352
Cdd:pfam14815  86 --EPQQELRWVTPEELDKYALPAAVRKILE 113
nth TIGR01083
endonuclease III; This equivalog model identifes nth members of the pfam00730 superfamily ...
 12-154 5.44e-22

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: 92.44  E-value: 5.44e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183596750  12 KWPTLQDLASASLEEVNQLWAGLGYY-SRGRRLQEGARKVVEELGGHMPRTAETLQQLlPGVGRYTAGAIASIAFGQATG 90
Cdd:TIGR01083  55 VYPTPQALAQAGLEELEEYIKSIGLYrNKAKNIIELCRKLVERYGGEVPEDREELVKL-PGVGRKTANVVLNVAFGIPAI 133

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1183596750  91 VVDGNVARVLCRVR-AIGADPSST------LVSQQLWglaqqlvdparpGDFNQAAMELGATVCTPQRPLC 154
Cdd:TIGR01083 134 AVDTHVFRVSNRLGlSKGKDPIKVeedlmkLVPREFW------------VKLHHWLILHGRYTCKARKPLC 192
PRK10702 PRK10702
endonuclease III; Provisional
 36-169 1.23e-08

endonuclease III; Provisional


Pssm-ID: 182661 [Multi-domain]  Cd Length: 211  Bit Score: 55.02  E-value: 1.23e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183596750  36 YYSRGRRLQEGARKVVEELGGHMPRTAETLQQLlPGVGRYTAGAIASIAFGQATGVVDGNVARVLCRVraiGADPSSTLv 115
Cdd:PRK10702   82 YNSKAENVIKTCRILLEQHNGEVPEDRAALEAL-PGVGRKTANVVLNTAFGWPTIAVDTHIFRVCNRT---QFAPGKNV- 156

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1183596750 116 sQQLWGLAQQLVDPARPGDFNQAAMELGATVCTPQRPLCSQCPVESLCRARQRV 169
Cdd:PRK10702  157 -EQVEEKLLKVVPAEFKVDCHHWLILHGRYTCIARKPRCGSCIIEDLCEYKEKV 209
HP0602 COG2231
3-Methyladenine DNA glycosylase, HhH-GPD/Endo3 superfamily [Replication, recombination and ...
 15-169 1.10e-06

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


Pssm-ID: 441832 [Multi-domain]  Cd Length: 220  Bit Score: 49.07  E-value: 1.10e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183596750  15 TLQDLASASLEEVNQLWAGLGYYSR-GRRLQEGARKVVEELGGHMPR-----TAETLQQLL--PGVGRYTAGAIASIAFG 86
Cdd:COG2231    61 DPEALAALDPEELAELIRPSGFYNQkAKRLKNLARWLVERYGGGLEKlkalpTEELREELLslKGIGPETADSILLYAFN 140

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183596750  87 QATGVVDGNVARVLCRVrAIGADPSStlvsqqlWGLAQQLVDPARPGDFNQA----AM--ELGATVCTPqRPLCSQCPVE 160
Cdd:COG2231   141 RPVFVVDAYTRRIFSRL-GLIEEDAS-------YDELQRLFEENLPPDVALYnefhALivEHGKEYCKK-KPKCEECPLR 211


                  ....*....
gi 1183596750 161 SLCRARQRV 169
Cdd:COG2231   212 DLCPYGGQE 220
NUDIX_MutT_NudA_like cd03425
MutT pyrophosphohydrolase; The MutT pyrophosphohydrolase is a prototypical NUDIX hydrolase ...
 233-340 2.14e-05

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: 43.59  E-value: 2.14e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183596750 233 VLEQPGalgaQILLVQRPNSGLLAGLWEFP--SVtwEPSEQLQrKALLQELQ---RWAgplpATHLRHLGEVVHTFSHIK 307
Cdd:cd03425     7 IIVDDG----RVLIAQRPEGKHLAGLWEFPggKV--EPGETPE-QALVRELReelGIE----VEVGEPLGTVEHDYPDFH 75

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1183596750 308 LTYQVYGLALEGQTPVTTVPPGARWLTQEEFHT 340
Cdd:cd03425    76 VRLHVYLCTLWSGEPQLLEHQELRWVTPEELDD 108
PRK10546 PRK10546
pyrimidine (deoxy)nucleoside triphosphate diphosphatase;
233-282 2.16e-05

pyrimidine (deoxy)nucleoside triphosphate diphosphatase;


Pssm-ID: 182536 [Multi-domain]  Cd Length: 135  Bit Score: 43.96  E-value: 2.16e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1183596750 233 VLEQPGalgaQILLVQRPNSGLLAGLWEFPSVTWEPSEQlQRKALLQELQ 282
Cdd:PRK10546   10 IIERDG----KILLAQRPAHSDQAGLWEFAGGKVEPGES-QPQALIRELR 54
FES smart00525
iron-sulpphur binding domain in DNA-(apurinic or apyrimidinic site) lyase (subfamily of ENDO3); ...
 146-166 5.00e-05

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


Pssm-ID: 197771 [Multi-domain]  Cd Length: 21  Bit Score: 39.84  E-value: 5.00e-05
                           10        20
                   ....*....|....*....|.
gi 1183596750  146 VCTPQRPLCSQCPVESLCRAR 166
Cdd:smart00525   1 ICTARKPRCDECPLKDLCPAY 21
HHH pfam00633
Helix-hairpin-helix motif; The helix-hairpin-helix DNA-binding motif is found to be duplicated ...
 53-83 7.77e-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: 7.77e-05
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1183596750  53 ELGGHMPRTAETLQQLlPGVGRYTAGAIASI 83
Cdd:pfam00633   1 SLEGLIPASVEELLAL-PGVGPKTAEAILSY 30
PRK10776 PRK10776
8-oxo-dGTP diphosphatase MutT;
243-337 1.60e-04

8-oxo-dGTP diphosphatase MutT;


Pssm-ID: 182721 [Multi-domain]  Cd Length: 129  Bit Score: 41.12  E-value: 1.60e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183596750 243 QILLVQRPNSGLLAGLWEFPSVTWEPSEQLQrKALLQELQRWAGpLPATHLRHLGEVVHTFS--HIKLTY--------QV 312
Cdd:PRK10776   17 EIFITRRAADAHMAGKWEFPGGKIEAGETPE-QALIRELQEEVG-ITVQHATLFEKLEYEFPdrHITLWFwlveswegEP 94

                          90       100
                  ....*....|....*....|....*
gi 1183596750 313 YGlaLEGQtpvttvpPGaRWLTQEE 337
Cdd:PRK10776   95 WG--KEGQ-------PG-RWVSQVA 109
PRK08999 PRK08999
Nudix family hydrolase;
243-338 2.81e-03

Nudix family hydrolase;


Pssm-ID: 236361 [Multi-domain]  Cd Length: 312  Bit Score: 39.47  E-value: 2.81e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183596750 243 QILLVQRPNSGLLAGLWEFPSVTWEPSEQLqRKALLQELQRWAGpLPATHLRHLGEVVHTFSHIKLT---YQVYG----- 314
Cdd:PRK08999   18 RILLARRPEGKHQGGLWEFPGGKVEPGETV-EQALARELQEELG-IEVTAARPLITVRHDYPDKRVRldvRRVTAwqgep 95

                          90       100
                  ....*....|....*....|....
gi 1183596750 315 LALEGQtPVTTVPPgaRWLTQEEF 338
Cdd:PRK08999   96 HGREGQ-PLAWVAP--DELAVYPF 116
EndIII_4Fe-2S pfam10576
Iron-sulfur binding domain of endonuclease III; Escherichia coli endonuclease III (EC 4.2.99. ...
 147-163 3.35e-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: 34.67  E-value: 3.35e-03
                          10
                  ....*....|....*..
gi 1183596750 147 CTPQRPLCSQCPVESLC 163
Cdd:pfam10576   1 CTARKPKCEECPLADLC 17
YjhB COG1051
ADP-ribose pyrophosphatase YjhB, NUDIX family [Nucleotide transport and metabolism];
229-352 7.22e-03

ADP-ribose pyrophosphatase YjhB, NUDIX family [Nucleotide transport and metabolism];


Pssm-ID: 440671 [Multi-domain]  Cd Length: 125  Bit Score: 36.49  E-value: 7.22e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183596750 229 SATCVLEQPGAlgaQILLVQRPNsGLLAGLWEFPSVTWEPSEQLqRKALLQELqrW--AGpLPATHLRHLGEVVHTFSHI 306
Cdd:COG1051     8 AVDAVIFRKDG---RVLLVRRAD-EPGKGLWALPGGKVEPGETP-EEAALREL--ReeTG-LEVEVLELLGVFDHPDRGH 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1183596750 307 KLTYQVYGLALEGQTPVTTVPPGARWLTQEEFHTAAVSTAMKKVFR 352
Cdd:COG1051    80 VVSVAFLAEVLSGEPRADDEIDEARWFPLDELPELAFTPADHEILE 125
 
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