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Conserved domains on  [gi|1080949418|gb|OFR08558|]
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A/G-specific adenine glycosylase [Staphylococcus sp. HMSC078E07]

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

CATH:  3.90.79.10|1.10.340.30|1.10.1670.10
EC:  3.2.2.31
Gene Ontology:  GO:0046872|GO:0000701|GO:0006284|GO:0051539|GO:0019104|GO:0016798
PubMed:  21764637|19778963|2682664
SCOP:  4001144|4001553

Graphical summary

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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 ...
 3-345 4.67e-165

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: 464.23  E-value: 4.67e-165
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080949418   3 NETTFKNNIVTWFEKNQREMPWRETTNPYYIWLSEVMLQQTQVKTVIDYYNKFIHRFPTVKALSEAEEDEVLKYWEGLGY 82
Cdd:COG1194     2 DMASFAKRLLAWYDRHGRDLPWRQTRDPYRVWLSEIMLQQTQVATVIPYYERFLERFPTVEALAAAPEDEVLKLWEGLGY 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080949418  83 YSRARNFHTAIKEVHHNYNGEVPSSPKVFGELKGVGPYTQAAVMSIAFNRPLATVDGNVFRVWTRLNNDYRDIKLQSTRK 162
Cdd:COG1194    82 YSRARNLHKAAQQVVEEHGGVFPDTYEELLALPGIGPYTAAAIASIAFGEPAPIVDGNVKRVLSRLFAIEGPIGSPAAKK 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080949418 163 SFEKELQPFV-QEEAGTFNQSMMELGATICTPKNPLCLFCPVQENCEAFRKGTTLELPIKTKKQAKKIINQEVFLVRnQK 241
Cdd:COG1194   162 ELWALAEELLpPERPGDFNQALMDLGATVCTPKKPKCLLCPLQDDCAAFAEGRQEELPVKKPKKKKPERYGAALVIR-DD 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080949418 242 GQYLIEKRQEK-LLNGMWQFPMFESPNGI--QKLEYKLNQSLTLAENAIFQL---KHQFTHKTWNLNVYSVieDINIDSA 315
Cdd:COG1194   241 GRVLLEKRPPKgLWGGLWEFPEFEWEEAEdpEALERWLREELGLEVEWLEPLgtvRHVFTHFRLHLTVYLA--RVPAGPP 318

                         330       340       350
                  ....*....|....*....|....*....|
gi 1080949418 316 QLPDFMEWFDLENRDDYSFPVSMSKIYEFI 345
Cdd:COG1194   319 AEPDGGRWVPLEELAALPLPAPMRKLLKAL 348
 
Name Accession Description Interval E-value
MutY COG1194
Adenine-specific DNA glycosylase, acts on AG and A-oxoG pairs [Replication, recombination and ...
 3-345 4.67e-165

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: 464.23  E-value: 4.67e-165
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080949418   3 NETTFKNNIVTWFEKNQREMPWRETTNPYYIWLSEVMLQQTQVKTVIDYYNKFIHRFPTVKALSEAEEDEVLKYWEGLGY 82
Cdd:COG1194     2 DMASFAKRLLAWYDRHGRDLPWRQTRDPYRVWLSEIMLQQTQVATVIPYYERFLERFPTVEALAAAPEDEVLKLWEGLGY 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080949418  83 YSRARNFHTAIKEVHHNYNGEVPSSPKVFGELKGVGPYTQAAVMSIAFNRPLATVDGNVFRVWTRLNNDYRDIKLQSTRK 162
Cdd:COG1194    82 YSRARNLHKAAQQVVEEHGGVFPDTYEELLALPGIGPYTAAAIASIAFGEPAPIVDGNVKRVLSRLFAIEGPIGSPAAKK 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080949418 163 SFEKELQPFV-QEEAGTFNQSMMELGATICTPKNPLCLFCPVQENCEAFRKGTTLELPIKTKKQAKKIINQEVFLVRnQK 241
Cdd:COG1194   162 ELWALAEELLpPERPGDFNQALMDLGATVCTPKKPKCLLCPLQDDCAAFAEGRQEELPVKKPKKKKPERYGAALVIR-DD 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080949418 242 GQYLIEKRQEK-LLNGMWQFPMFESPNGI--QKLEYKLNQSLTLAENAIFQL---KHQFTHKTWNLNVYSVieDINIDSA 315
Cdd:COG1194   241 GRVLLEKRPPKgLWGGLWEFPEFEWEEAEdpEALERWLREELGLEVEWLEPLgtvRHVFTHFRLHLTVYLA--RVPAGPP 318

                         330       340       350
                  ....*....|....*....|....*....|
gi 1080949418 316 QLPDFMEWFDLENRDDYSFPVSMSKIYEFI 345
Cdd:COG1194   319 AEPDGGRWVPLEELAALPLPAPMRKLLKAL 348
mutY TIGR01084
A/G-specific adenine glycosylase; This equivalog model identifies mutY members of the ...
 7-276 1.43e-108

A/G-specific adenine glycosylase; This equivalog model identifies mutY 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: 130156  Cd Length: 275  Bit Score: 318.20  E-value: 1.43e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080949418   7 FKNNIVTWFEKNQRE-MPWRETTNPYYIWLSEVMLQQTQVKTVIDYYNKFIHRFPTVKALSEAEEDEVLKYWEGLGYYSR 85
Cdd:TIGR01084   2 FSEDLLSWYDKYGRKtLPWRQNKTPYRVWLSEVMLQQTQVATVIPYFERFLERFPTVQALANAPQDEVLKLWEGLGYYAR 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080949418  86 ARNFHTAIKEVHHNYNGEVPSSPKVFGELKGVGPYTQAAVMSIAFNRPLATVDGNVFRVWTRLnndyRDIKLQSTRKSFE 165
Cdd:TIGR01084  82 ARNLHKAAQEVVEEFGGEFPQDFEDLAALPGVGRYTAGAILSFALNKPYPILDGNVKRVLSRL----FAVEGWPGKKKVE 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080949418 166 KELQPFVQE-----EAGTFNQSMMELGATICTPKNPLCLFCPVQENCEAFRKGTTLELPIKTKKQAKKIINQEVFLVRNQ 240
Cdd:TIGR01084 158 NRLWTLAESllpkaDPEAFNQALMDLGAMICTRKKPKCDLCPLQDFCLAYQQGTWEEYPVKKPKAAPPERTTYFLVLQNY 237

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1080949418 241 KGQYLIEKRQEK-LLNGMWQFPMFESPNGIQKLEYKL 276
Cdd:TIGR01084 238 DGEVLLEQRPEKgLWGGLYCFPQFEDEDSLAFLLAQR 274
PRK10880 PRK10880
adenine DNA glycosylase;
7-296 6.00e-66

adenine DNA glycosylase;


Pssm-ID: 182805 [Multi-domain]  Cd Length: 350  Bit Score: 211.88  E-value: 6.00e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080949418   7 FKNNIVTWFEKNQRE-MPWRETTNPYYIWLSEVMLQQTQVKTVIDYYNKFIHRFPTVKALSEAEEDEVLKYWEGLGYYSR 85
Cdd:PRK10880    6 FSAQVLDWYDKYGRKtLPWQIDKTPYKVWLSEVMLQQTQVATVIPYFERFMARFPTVTDLANAPLDEVLHLWTGLGYYAR 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080949418  86 ARNFHTAIKEVHHNYNGEVPSSPKVFGELKGVGPYTQAAVMSIAFNRPLATVDGNVFRVWTRlnndYRDIKLQSTRKSFE 165
Cdd:PRK10880   86 ARNLHKAAQQVATLHGGEFPETFEEVAALPGVGRSTAGAILSLSLGKHFPILDGNVKRVLAR----CYAVSGWPGKKEVE 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080949418 166 KELQPFVQE-----EAGTFNQSMMELGATICTPKNPLCLFCPVQENCEAFRKGTTLELPiktKKQAKKIINQEV--FLVR 238
Cdd:PRK10880  162 NRLWQLSEQvtpavGVERFNQAMMDLGAMVCTRSKPKCELCPLQNGCIAYANHSWALYP---GKKPKQTLPERTgyFLLL 238

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1080949418 239 NQKGQYLIEKRQEK-LLNGMWQFPMFESPngiQKLEYKLNQSlTLAENAIFQL---KHQFTH 296
Cdd:PRK10880  239 QHGDEVWLEQRPPSgLWGGLFCFPQFADE---EELRQWLAQR-GIAADNLTQLtafRHTFSH 296
ENDO3c cd00056
endonuclease III; includes endonuclease III (DNA-(apurinic or apyrimidinic site) lyase), ...
 31-187 8.55e-45

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: 150.85  E-value: 8.55e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080949418  31 YYIWLSEVMLQQTQVKTVIDYYNKFIHRF-PTVKALSEAEEDEVLKYWEGLGYYSRARNFHTAIKEVHHNYNGEVPSSPK 109
Cdd:cd00056     1 FEVLVSEILSQQTTDKAVNKAYERLFERYgPTPEALAAADEEELRELIRSLGYRRKAKYLKELARAIVEGFGGLVLDDPD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080949418 110 VFGEL---KGVGPYTQAAVMSIAFNRPLATVDGNVFRVWTRLNndyrDIKLQSTRKSFEKELQPFV-QEEAGTFNQSMME 185
Cdd:cd00056    81 AREELlalPGVGRKTANVVLLFALGPDAFPVDTHVRRVLKRLG----LIPKKKTPEELEELLEELLpKPYWGEANQALMD 156


                  ..
gi 1080949418 186 LG 187
Cdd:cd00056   157 LG 158
ENDO3c smart00478
endonuclease III; includes endonuclease III (DNA-(apurinic or apyrimidinic site) lyase), ...
 39-189 8.41e-36

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: 126.99  E-value: 8.41e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080949418   39 MLQQTQVKTVIDYYNKFIHRFPTVKALSEAEEDEVLKYWEGLG-YYSRARNFHTAIKEVHHNYNGEVPSSPKVFGELKGV 117
Cdd:smart00478   1 LSQQTTDERVNKATERLFEKFPTPEDLAAADEEELEELIRGLGfYRRKARYLIELARILVEEYGGEVPDDREELLKLPGV 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1080949418  118 GPYTQAAVMSIAFNRPLATVDGNVFRVWTRLNNdyrdIKLQSTRKSFEKELQPFVQEE-AGTFNQSMMELGAT 189
Cdd:smart00478  81 GRKTANAVLSFALGKPFIPVDTHVLRIAKRLGL----VDKKSTPEEVEKLLEKLLPEEdWRELNLLLIDFGRT 149
HhH-GPD pfam00730
HhH-GPD superfamily base excision DNA repair protein; This family contains a diverse range of ...
 35-170 2.17e-28

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: 107.37  E-value: 2.17e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080949418  35 LSEVMLQQTQVKTVIDYYNKFIHR-FPTVKALSEAEEDEVLKYWEGLGYY-SRARNFHTAIKEVHHNYNGEVPSSPKVFG 112
Cdd:pfam00730   1 VSAILSQQTSDKAVNKITERLFEKfFPTPEDLADADEEELRELIRGLGFYrRKAKYLKELARILVEGYGGEVPLDEEELE 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1080949418 113 E-LKGVGPYTQAAVMSIAFNRPLAT--VDGNVFRVWTRLNNDYRDIKLQSTRKSFEKELQP 170
Cdd:pfam00730  81 AlLKGVGRWTAEAVLIFALGRPDPLpvVDTHVRRVLKRLGLIKEKPTPKEVERELEELWPP 141
 
Name Accession Description Interval E-value
MutY COG1194
Adenine-specific DNA glycosylase, acts on AG and A-oxoG pairs [Replication, recombination and ...
 3-345 4.67e-165

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: 464.23  E-value: 4.67e-165
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080949418   3 NETTFKNNIVTWFEKNQREMPWRETTNPYYIWLSEVMLQQTQVKTVIDYYNKFIHRFPTVKALSEAEEDEVLKYWEGLGY 82
Cdd:COG1194     2 DMASFAKRLLAWYDRHGRDLPWRQTRDPYRVWLSEIMLQQTQVATVIPYYERFLERFPTVEALAAAPEDEVLKLWEGLGY 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080949418  83 YSRARNFHTAIKEVHHNYNGEVPSSPKVFGELKGVGPYTQAAVMSIAFNRPLATVDGNVFRVWTRLNNDYRDIKLQSTRK 162
Cdd:COG1194    82 YSRARNLHKAAQQVVEEHGGVFPDTYEELLALPGIGPYTAAAIASIAFGEPAPIVDGNVKRVLSRLFAIEGPIGSPAAKK 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080949418 163 SFEKELQPFV-QEEAGTFNQSMMELGATICTPKNPLCLFCPVQENCEAFRKGTTLELPIKTKKQAKKIINQEVFLVRnQK 241
Cdd:COG1194   162 ELWALAEELLpPERPGDFNQALMDLGATVCTPKKPKCLLCPLQDDCAAFAEGRQEELPVKKPKKKKPERYGAALVIR-DD 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080949418 242 GQYLIEKRQEK-LLNGMWQFPMFESPNGI--QKLEYKLNQSLTLAENAIFQL---KHQFTHKTWNLNVYSVieDINIDSA 315
Cdd:COG1194   241 GRVLLEKRPPKgLWGGLWEFPEFEWEEAEdpEALERWLREELGLEVEWLEPLgtvRHVFTHFRLHLTVYLA--RVPAGPP 318

                         330       340       350
                  ....*....|....*....|....*....|
gi 1080949418 316 QLPDFMEWFDLENRDDYSFPVSMSKIYEFI 345
Cdd:COG1194   319 AEPDGGRWVPLEELAALPLPAPMRKLLKAL 348
mutY TIGR01084
A/G-specific adenine glycosylase; This equivalog model identifies mutY members of the ...
 7-276 1.43e-108

A/G-specific adenine glycosylase; This equivalog model identifies mutY 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: 130156  Cd Length: 275  Bit Score: 318.20  E-value: 1.43e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080949418   7 FKNNIVTWFEKNQRE-MPWRETTNPYYIWLSEVMLQQTQVKTVIDYYNKFIHRFPTVKALSEAEEDEVLKYWEGLGYYSR 85
Cdd:TIGR01084   2 FSEDLLSWYDKYGRKtLPWRQNKTPYRVWLSEVMLQQTQVATVIPYFERFLERFPTVQALANAPQDEVLKLWEGLGYYAR 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080949418  86 ARNFHTAIKEVHHNYNGEVPSSPKVFGELKGVGPYTQAAVMSIAFNRPLATVDGNVFRVWTRLnndyRDIKLQSTRKSFE 165
Cdd:TIGR01084  82 ARNLHKAAQEVVEEFGGEFPQDFEDLAALPGVGRYTAGAILSFALNKPYPILDGNVKRVLSRL----FAVEGWPGKKKVE 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080949418 166 KELQPFVQE-----EAGTFNQSMMELGATICTPKNPLCLFCPVQENCEAFRKGTTLELPIKTKKQAKKIINQEVFLVRNQ 240
Cdd:TIGR01084 158 NRLWTLAESllpkaDPEAFNQALMDLGAMICTRKKPKCDLCPLQDFCLAYQQGTWEEYPVKKPKAAPPERTTYFLVLQNY 237

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1080949418 241 KGQYLIEKRQEK-LLNGMWQFPMFESPNGIQKLEYKL 276
Cdd:TIGR01084 238 DGEVLLEQRPEKgLWGGLYCFPQFEDEDSLAFLLAQR 274
PRK10880 PRK10880
adenine DNA glycosylase;
7-296 6.00e-66

adenine DNA glycosylase;


Pssm-ID: 182805 [Multi-domain]  Cd Length: 350  Bit Score: 211.88  E-value: 6.00e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080949418   7 FKNNIVTWFEKNQRE-MPWRETTNPYYIWLSEVMLQQTQVKTVIDYYNKFIHRFPTVKALSEAEEDEVLKYWEGLGYYSR 85
Cdd:PRK10880    6 FSAQVLDWYDKYGRKtLPWQIDKTPYKVWLSEVMLQQTQVATVIPYFERFMARFPTVTDLANAPLDEVLHLWTGLGYYAR 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080949418  86 ARNFHTAIKEVHHNYNGEVPSSPKVFGELKGVGPYTQAAVMSIAFNRPLATVDGNVFRVWTRlnndYRDIKLQSTRKSFE 165
Cdd:PRK10880   86 ARNLHKAAQQVATLHGGEFPETFEEVAALPGVGRSTAGAILSLSLGKHFPILDGNVKRVLAR----CYAVSGWPGKKEVE 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080949418 166 KELQPFVQE-----EAGTFNQSMMELGATICTPKNPLCLFCPVQENCEAFRKGTTLELPiktKKQAKKIINQEV--FLVR 238
Cdd:PRK10880  162 NRLWQLSEQvtpavGVERFNQAMMDLGAMVCTRSKPKCELCPLQNGCIAYANHSWALYP---GKKPKQTLPERTgyFLLL 238

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1080949418 239 NQKGQYLIEKRQEK-LLNGMWQFPMFESPngiQKLEYKLNQSlTLAENAIFQL---KHQFTH 296
Cdd:PRK10880  239 QHGDEVWLEQRPPSgLWGGLFCFPQFADE---EELRQWLAQR-GIAADNLTQLtafRHTFSH 296
ENDO3c cd00056
endonuclease III; includes endonuclease III (DNA-(apurinic or apyrimidinic site) lyase), ...
 31-187 8.55e-45

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: 150.85  E-value: 8.55e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080949418  31 YYIWLSEVMLQQTQVKTVIDYYNKFIHRF-PTVKALSEAEEDEVLKYWEGLGYYSRARNFHTAIKEVHHNYNGEVPSSPK 109
Cdd:cd00056     1 FEVLVSEILSQQTTDKAVNKAYERLFERYgPTPEALAAADEEELRELIRSLGYRRKAKYLKELARAIVEGFGGLVLDDPD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080949418 110 VFGEL---KGVGPYTQAAVMSIAFNRPLATVDGNVFRVWTRLNndyrDIKLQSTRKSFEKELQPFV-QEEAGTFNQSMME 185
Cdd:cd00056    81 AREELlalPGVGRKTANVVLLFALGPDAFPVDTHVRRVLKRLG----LIPKKKTPEELEELLEELLpKPYWGEANQALMD 156


                  ..
gi 1080949418 186 LG 187
Cdd:cd00056   157 LG 158
ENDO3c smart00478
endonuclease III; includes endonuclease III (DNA-(apurinic or apyrimidinic site) lyase), ...
 39-189 8.41e-36

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: 126.99  E-value: 8.41e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080949418   39 MLQQTQVKTVIDYYNKFIHRFPTVKALSEAEEDEVLKYWEGLG-YYSRARNFHTAIKEVHHNYNGEVPSSPKVFGELKGV 117
Cdd:smart00478   1 LSQQTTDERVNKATERLFEKFPTPEDLAAADEEELEELIRGLGfYRRKARYLIELARILVEEYGGEVPDDREELLKLPGV 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1080949418  118 GPYTQAAVMSIAFNRPLATVDGNVFRVWTRLNNdyrdIKLQSTRKSFEKELQPFVQEE-AGTFNQSMMELGAT 189
Cdd:smart00478  81 GRKTANAVLSFALGKPFIPVDTHVLRIAKRLGL----VDKKSTPEEVEKLLEKLLPEEdWRELNLLLIDFGRT 149
PRK13910 PRK13910
DNA glycosylase MutY; Provisional
 39-304 7.49e-34

DNA glycosylase MutY; Provisional


Pssm-ID: 172427 [Multi-domain]  Cd Length: 289  Bit Score: 126.29  E-value: 7.49e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080949418  39 MLQQTQVKTVID-YYNKFIHRFPTVKALSEAEEDEVLKYWEGLGYYSRARNFHTAIKEVHHNYNGEVPSSPKVFGELKGV 117
Cdd:PRK13910    1 MSQQTQINTVVErFYSPFLEAFPTLKDLANAPLEEVLLLWRGLGYYSRAKNLKKSAEICVKEHHSQLPNDYQSLLKLPGI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080949418 118 GPYTQAAVMSIAFNRPLATVDGNVFRVWTRLNNDYRDIklqsTRKSFEKELQPFVQ-EEAGTFNQSMMELGATICTPKnP 196
Cdd:PRK13910   81 GAYTANAILCFGFREKSACVDANIKRVLLRLFGLDPNI----HAKDLQIKANDFLNlNESFNHNQALIDLGALICSPK-P 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080949418 197 LCLFCPVQENCEAFRkgttlELPIKTKKQAKKIINQEVFL-VRNQKGQYLIEKRQEKLLNGMWQFpmfesPNGIQKLEYK 275
Cdd:PRK13910  156 KCAICPLNPYCLGKN-----NPEKHTLKKKQEIVQEERYLgVVIQNNQIALEKIEQKLYLGMHHF-----PNLKENLEYK 225

                         250       260
                  ....*....|....*....|....*....
gi 1080949418 276 LnqsltlaeNAIFQLKHQFTHKTWNLNVY 304
Cdd:PRK13910  226 L--------PFLGAIKHSHTKFKLNLNLY 246
Nth COG0177
Endonuclease III [Replication, recombination and repair];
23-211 3.38e-29

Endonuclease III [Replication, recombination and repair];


Pssm-ID: 439947 [Multi-domain]  Cd Length: 198  Bit Score: 111.34  E-value: 3.38e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080949418  23 PWRETTNPYYIWLSEVMLQQTQVKTVIDYYNKFIHRFPTVKALSEAEEDEVLKYWEGLGYY-SRARNFHTAIKEVHHNYN 101
Cdd:COG0177    13 TELDYRDPFELLVATILSAQTTDERVNKATPRLFARYPTPEALAAADLEELEELIRPIGLYrNKAKNIIALARILVEKYG 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080949418 102 GEVPSSPKVFGELKGVGPYTQAAVMSIAFNRPLATVDGNVFRVWTRL----NNDYRDIklqstrksfEKELQPFV-QEEA 176
Cdd:COG0177    93 GEVPETREELESLPGVGRKTANVVLNFAFGKPAIAVDTHVHRVSNRLglvpGKDPEEV---------EKDLMKLIpKEYW 163

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1080949418 177 GTFNQSMMELGATICTPKNPLCLFCPVQENCEAFR 211
Cdd:COG0177   164 GDLHHLLILHGRYICKARKPKCEECPLADLCPYYG 198
HhH-GPD pfam00730
HhH-GPD superfamily base excision DNA repair protein; This family contains a diverse range of ...
 35-170 2.17e-28

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: 107.37  E-value: 2.17e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080949418  35 LSEVMLQQTQVKTVIDYYNKFIHR-FPTVKALSEAEEDEVLKYWEGLGYY-SRARNFHTAIKEVHHNYNGEVPSSPKVFG 112
Cdd:pfam00730   1 VSAILSQQTSDKAVNKITERLFEKfFPTPEDLADADEEELRELIRGLGFYrRKAKYLKELARILVEGYGGEVPLDEEELE 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1080949418 113 E-LKGVGPYTQAAVMSIAFNRPLAT--VDGNVFRVWTRLNNDYRDIKLQSTRKSFEKELQP 170
Cdd:pfam00730  81 AlLKGVGRWTAEAVLIFALGRPDPLpvVDTHVRRVLKRLGLIKEKPTPKEVERELEELWPP 141
NUDIX_DNA_Glycosylase_C-MutY cd03431
C-terminal domain of DNA glycosylase; DNA glycosylase (MutY in bacteria and hMYH in humans) is ...
 227-343 3.64e-24

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: 95.45  E-value: 3.64e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080949418 227 KKIINQEVFLVRNQkGQYLIEKRQEK-LLNGMWQFPMFESPNGIQKLEYKLNQSLTLAENAIFQL---KHQFTHKTWNLN 302
Cdd:cd03431     1 VPERYFTVLVLRDG-GRVLLEKRPEKgLLAGLWEFPLVETEEEEEEAEALLGLLAEELLLILEPLgevKHVFSHFRLHIT 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1080949418 303 VYSVieDINIDSAQLPDFMEWFDLENRDDYSFPVSMSKIYE 343
Cdd:cd03431    80 VYLV--ELPEAPPAAPDEGRWVDLEELDEYALPAPMRKLLE 118
nth TIGR01083
endonuclease III; This equivalog model identifes nth members of the pfam00730 superfamily ...
 28-198 1.54e-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: 87.82  E-value: 1.54e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080949418  28 TNPYYIWLSEVMLQQTQVKTVIDYYNKFIHRFPTVKALSEAEEDEVLKYWEGLGYY-SRARNFHTAIKEVHHNYNGEVPS 106
Cdd:TIGR01083  25 NNPFELLVATILSAQATDKRVNKATPKLFEVYPTPQALAQAGLEELEEYIKSIGLYrNKAKNIIELCRKLVERYGGEVPE 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080949418 107 SPKVFGELKGVGPYTQAAVMSIAFNRPLATVDGNVFRVWTRLNndyrdIKLQSTRKSFEKELQPFV-QEEAGTFNQSMME 185
Cdd:TIGR01083 105 DREELVKLPGVGRKTANVVLNVAFGIPAIAVDTHVFRVSNRLG-----LSKGKDPIKVEEDLMKLVpREFWVKLHHWLIL 179

                         170
                  ....*....|...
gi 1080949418 186 LGATICTPKNPLC 198
Cdd:TIGR01083 180 HGRYTCKARKPLC 192
NUDIX_4 pfam14815
NUDIX domain;
234-343 1.24e-19

NUDIX domain;


Pssm-ID: 464330 [Multi-domain]  Cd Length: 114  Bit Score: 83.13  E-value: 1.24e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080949418 234 VFLVRNQKGQYLIEKRQEK-LLNGMWQFP---MFESPNGIQKLEYKLNQSLTLAENAIFQLKHQFTHKTWNLNVYSVIED 309
Cdd:pfam14815   2 VLVIRNGDGRVLLRKRPEKgLLGGLWEFPggkVEPGETLEEALARLEELGIEVEVLEPGTVKHVFTHFRLTLHVYLVREV 81

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1080949418 310 INIDSAQLPdfMEWFDLENRDDYSFPVSMSKIYE 343
Cdd:pfam14815  82 EGEEEPQQE--LRWVTPEELDKYALPAAVRKILE 113
PRK10702 PRK10702
endonuclease III; Provisional
 28-208 4.16e-07

endonuclease III; Provisional


Pssm-ID: 182661 [Multi-domain]  Cd Length: 211  Bit Score: 50.02  E-value: 4.16e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080949418  28 TNPYYIWLSEVMLQQTQVKTVIDYYNKFIHRFPTVKALSEAEEDEVLKYWEGLGYY-SRARNFHTAIKEVHHNYNGEVPS 106
Cdd:PRK10702   27 SSPFELLIAVLLSAQATDVSVNKATAKLYPVANTPAAMLELGVEGVKTYIKTIGLYnSKAENVIKTCRILLEQHNGEVPE 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080949418 107 SPKVFGELKGVGPYTQAAVMSIAFNRPLATVDGNVFRVWTRLNndyrdIKLQSTRKSFEKELQPFVQEEAGTFNQSMMEL 186
Cdd:PRK10702  107 DRAALEALPGVGRKTANVVLNTAFGWPTIAVDTHIFRVCNRTQ-----FAPGKNVEQVEEKLLKVVPAEFKVDCHHWLIL 181

                         170       180
                  ....*....|....*....|...
gi 1080949418 187 -GATICTPKNPLCLFCPVQENCE 208
Cdd:PRK10702  182 hGRYTCIARKPRCGSCIIEDLCE 204
HP0602 COG2231
3-Methyladenine DNA glycosylase, HhH-GPD/Endo3 superfamily [Replication, recombination and ...
 61-208 3.52e-06

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


Pssm-ID: 441832 [Multi-domain]  Cd Length: 220  Bit Score: 47.15  E-value: 3.52e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080949418  61 TVKALSEAEEDEVLKYWEGLGYYSR-ARNFHTAIKEVHHNYNGEVP-----SSPKVFGEL---KGVGPYTQAAVMSIAFN 131
Cdd:COG2231    61 DPEALAALDPEELAELIRPSGFYNQkAKRLKNLARWLVERYGGGLEklkalPTEELREELlslKGIGPETADSILLYAFN 140

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080949418 132 RPLATVDGNVFRVWTRLNNDYRDIKLQSTRKSFEKELQPfvqeEAGTFNQ---SMMELGATICTPKnPLCLFCPVQENCE 208
Cdd:COG2231   141 RPVFVVDAYTRRIFSRLGLIEEDASYDELQRLFEENLPP----DVALYNEfhaLIVEHGKEYCKKK-PKCEECPLRDLCP 215
FES smart00525
iron-sulpphur binding domain in DNA-(apurinic or apyrimidinic site) lyase (subfamily of ENDO3); ...
 190-210 3.02e-03

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


Pssm-ID: 197771 [Multi-domain]  Cd Length: 21  Bit Score: 34.45  E-value: 3.02e-03
                           10        20
                   ....*....|....*....|.
gi 1080949418  190 ICTPKNPLCLFCPVQENCEAF 210
Cdd:smart00525   1 ICTARKPRCDECPLKDLCPAY 21
EndIII_4Fe-2S pfam10576
Iron-sulfur binding domain of endonuclease III; Escherichia coli endonuclease III (EC 4.2.99. ...
 191-207 4.11e-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: 4.11e-03
                          10
                  ....*....|....*..
gi 1080949418 191 CTPKNPLCLFCPVQENC 207
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.
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