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Conserved domains on  [gi|1151266558|gb|OOP87857|]
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adenine-specific DNA glycosylase [Helicobacter pylori]

Protein Classification

A/G-specific adenine glycosylase( domain architecture ID 11486945)

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK13910 PRK13910
DNA glycosylase MutY; Provisional
 40-328 0e+00

DNA glycosylase MutY; Provisional


:

Pssm-ID: 172427 [Multi-domain]  Cd Length: 289  Bit Score: 529.21  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151266558  40 MSQQTQINTVVERFYSPFLEAFPTLKDLANAPLEEVLLLWRGLGYYSRAKNLKKSAEICVKEHHSQLPNDYQSLLKLPGI 119
Cdd:PRK13910    1 MSQQTQINTVVERFYSPFLEAFPTLKDLANAPLEEVLLLWRGLGYYSRAKNLKKSAEICVKEHHSQLPNDYQSLLKLPGI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151266558 120 GTYTANAILCFGFREKTACVDANIKRVLLRLFGLDPNIHAKDLQIKANDFLNPNESFNHNQALIDLGALICSPKPKCAIC 199
Cdd:PRK13910   81 GAYTANAILCFGFREKSACVDANIKRVLLRLFGLDPNIHAKDLQIKANDFLNLNESFNHNQALIDLGALICSPKPKCAIC 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151266558 200 PLNPYCLGKNHPEKHTLKKKQEIIQEERYLGVVIQNNQIALEKIEQKLYLGMHHFPNLKENLEYKLPFLGAIKHSHTKFK 279
Cdd:PRK13910  161 PLNPYCLGKNNPEKHTLKKKQEIVQEERYLGVVIQNNQIALEKIEQKLYLGMHHFPNLKENLEYKLPFLGAIKHSHTKFK 240

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1151266558 280 LNLNLYLAAIKDLKNPIRFYSLKDLETLPISSMTLKILNFLKQKNLFGG 328
Cdd:PRK13910  241 LNLNLYLAAIKDLKNPIRFYSLKDLETLPISSMTLKILNFLKQKNLFGG 289
 
Name Accession Description Interval E-value
PRK13910 PRK13910
DNA glycosylase MutY; Provisional
 40-328 0e+00

DNA glycosylase MutY; Provisional


Pssm-ID: 172427 [Multi-domain]  Cd Length: 289  Bit Score: 529.21  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151266558  40 MSQQTQINTVVERFYSPFLEAFPTLKDLANAPLEEVLLLWRGLGYYSRAKNLKKSAEICVKEHHSQLPNDYQSLLKLPGI 119
Cdd:PRK13910    1 MSQQTQINTVVERFYSPFLEAFPTLKDLANAPLEEVLLLWRGLGYYSRAKNLKKSAEICVKEHHSQLPNDYQSLLKLPGI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151266558 120 GTYTANAILCFGFREKTACVDANIKRVLLRLFGLDPNIHAKDLQIKANDFLNPNESFNHNQALIDLGALICSPKPKCAIC 199
Cdd:PRK13910   81 GAYTANAILCFGFREKSACVDANIKRVLLRLFGLDPNIHAKDLQIKANDFLNLNESFNHNQALIDLGALICSPKPKCAIC 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151266558 200 PLNPYCLGKNHPEKHTLKKKQEIIQEERYLGVVIQNNQIALEKIEQKLYLGMHHFPNLKENLEYKLPFLGAIKHSHTKFK 279
Cdd:PRK13910  161 PLNPYCLGKNNPEKHTLKKKQEIVQEERYLGVVIQNNQIALEKIEQKLYLGMHHFPNLKENLEYKLPFLGAIKHSHTKFK 240

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1151266558 280 LNLNLYLAAIKDLKNPIRFYSLKDLETLPISSMTLKILNFLKQKNLFGG 328
Cdd:PRK13910  241 LNLNLYLAAIKDLKNPIRFYSLKDLETLPISSMTLKILNFLKQKNLFGG 289
MutY COG1194
Adenine-specific DNA glycosylase, acts on AG and A-oxoG pairs [Replication, recombination and ...
 1-322 2.89e-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: 339.81  E-value: 2.89e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151266558   1 METLHNALLKWYEEFGRkDLPFRNLKginAPYEVYISEVMSQQTQINTVVErFYSPFLEAFPTLKDLANAPLEEVLLLWR 80
Cdd:COG1194     3 MASFAKRLLAWYDRHGR-DLPWRQTR---DPYRVWLSEIMLQQTQVATVIP-YYERFLERFPTVEALAAAPEDEVLKLWE 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151266558  81 GLGYYSRAKNLKKSAEICVKEHHSQLPNDYQSLLKLPGIGTYTANAILCFGFREKTACVDANIKRVLLRLFGLDPNI--- 157
Cdd:COG1194    78 GLGYYSRARNLHKAAQQVVEEHGGVFPDTYEELLALPGIGPYTAAAIASIAFGEPAPIVDGNVKRVLSRLFAIEGPIgsp 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151266558 158 -HAKDLQIKANDFLNPNESFNHNQALIDLGALICSPK-PKCAICPLNPYCLGKNHPEKHTL---KKKQEIIQEERYLGVV 232
Cdd:COG1194   158 aAKKELWALAEELLPPERPGDFNQALMDLGATVCTPKkPKCLLCPLQDDCAAFAEGRQEELpvkKPKKKKPERYGAALVI 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151266558 233 IQNNQIALEKIEQK-LYLGMHHFPN-----------LKENLEYKLPF-------LGAIKHSHTKFKLNLNLYLAAIKDLK 293
Cdd:COG1194   238 RDDGRVLLEKRPPKgLWGGLWEFPEfeweeaedpeaLERWLREELGLevewlepLGTVRHVFTHFRLHLTVYLARVPAGP 317

                         330       340       350
                  ....*....|....*....|....*....|...
gi 1151266558 294 NP----IRFYSLKDLETLPISSMTLKILNFLKQ 322
Cdd:COG1194   318 PAepdgGRWVPLEELAALPLPAPMRKLLKALLK 350
mutY TIGR01084
A/G-specific adenine glycosylase; This equivalog model identifies mutY members of the ...
 7-258 1.10e-97

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: 289.70  E-value: 1.10e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151266558   7 ALLKWYEEFGRKDLPFRNLKginAPYEVYISEVMSQQTQINTVVErFYSPFLEAFPTLKDLANAPLEEVLLLWRGLGYYS 86
Cdd:TIGR01084   5 DLLSWYDKYGRKTLPWRQNK---TPYRVWLSEVMLQQTQVATVIP-YFERFLERFPTVQALANAPQDEVLKLWEGLGYYA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151266558  87 RAKNLKKSAEICVKEHHSQLPNDYQSLLKLPGIGTYTANAILCFGFREKTACVDANIKRVLLRLFGLDPNIHAKD----L 162
Cdd:TIGR01084  81 RARNLHKAAQEVVEEFGGEFPQDFEDLAALPGVGRYTAGAILSFALNKPYPILDGNVKRVLSRLFAVEGWPGKKKvenrL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151266558 163 QIKANDFLNPNESFNHNQALIDLGALICSPK-PKCAICPLNPYCLGKNH--PEKHTLKKKQ--EIIQEERYLGVVIQNNQ 237
Cdd:TIGR01084 161 WTLAESLLPKADPEAFNQALMDLGAMICTRKkPKCDLCPLQDFCLAYQQgtWEEYPVKKPKaaPPERTTYFLVLQNYDGE 240

                         250       260
                  ....*....|....*....|..
gi 1151266558 238 IALEKIEQK-LYLGMHHFPNLK 258
Cdd:TIGR01084 241 VLLEQRPEKgLWGGLYCFPQFE 262
ENDO3c cd00056
endonuclease III; includes endonuclease III (DNA-(apurinic or apyrimidinic site) lyase), ...
 32-186 3.02e-48

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: 159.33  E-value: 3.02e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151266558  32 YEVYISEVMSQQTQINTVVERFYSPFLEAFPTLKDLANAPLEEVLLLWRGLGYYSRAKNLKKSAEICVKEHHS---QLPN 108
Cdd:cd00056     1 FEVLVSEILSQQTTDKAVNKAYERLFERYGPTPEALAAADEEELRELIRSLGYRRKAKYLKELARAIVEGFGGlvlDDPD 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1151266558 109 DYQSLLKLPGIGTYTANAILCFGFREKTACVDANIKRVLLRLFGLDPNIHAKDLQIKANDFLNPNESFNHNQALIDLG 186
Cdd:cd00056    81 AREELLALPGVGRKTANVVLLFALGPDAFPVDTHVRRVLKRLGLIPKKKTPEELEELLEELLPKPYWGEANQALMDLG 158
ENDO3c smart00478
endonuclease III; includes endonuclease III (DNA-(apurinic or apyrimidinic site) lyase), ...
 40-188 1.99e-43

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: 146.25  E-value: 1.99e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151266558   40 MSQQTQInTVVERFYSPFLEAFPTLKDLANAPLEEVLLLWRGLG-YYSRAKNLKKSAEICVKEHHSQLPNDYQSLLKLPG 118
Cdd:smart00478   1 LSQQTTD-ERVNKATERLFEKFPTPEDLAAADEEELEELIRGLGfYRRKARYLIELARILVEEYGGEVPDDREELLKLPG 79

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151266558  119 IGTYTANAILCFGFREKTACVDANIKRVLLRLFGLDPNIHAKDLQIKANDFLNPNESFNHNQALIDLGAL 188
Cdd:smart00478  80 VGRKTANAVLSFALGKPFIPVDTHVLRIAKRLGLVDKKSTPEEVEKLLEKLLPEEDWRELNLLLIDFGRT 149
HhH-GPD pfam00730
HhH-GPD superfamily base excision DNA repair protein; This family contains a diverse range of ...
 36-172 5.04e-39

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: 134.72  E-value: 5.04e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151266558  36 ISEVMSQQTQ---INTVVERFYSPFleaFPTLKDLANAPLEEVLLLWRGLGYY-SRAKNLKKSAEICVKEHHSQLPNDYQ 111
Cdd:pfam00730   1 VSAILSQQTSdkaVNKITERLFEKF---FPTPEDLADADEEELRELIRGLGFYrRKAKYLKELARILVEGYGGEVPLDEE 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1151266558 112 SLLK-LPGIGTYTANAILCFGFR--EKTACVDANIKRVLLRLFGLDPNIHAKDLQIKANDFLNP 172
Cdd:pfam00730  78 ELEAlLKGVGRWTAEAVLIFALGrpDPLPVVDTHVRRVLKRLGLIKEKPTPKEVERELEELWPP 141
 
Name Accession Description Interval E-value
PRK13910 PRK13910
DNA glycosylase MutY; Provisional
 40-328 0e+00

DNA glycosylase MutY; Provisional


Pssm-ID: 172427 [Multi-domain]  Cd Length: 289  Bit Score: 529.21  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151266558  40 MSQQTQINTVVERFYSPFLEAFPTLKDLANAPLEEVLLLWRGLGYYSRAKNLKKSAEICVKEHHSQLPNDYQSLLKLPGI 119
Cdd:PRK13910    1 MSQQTQINTVVERFYSPFLEAFPTLKDLANAPLEEVLLLWRGLGYYSRAKNLKKSAEICVKEHHSQLPNDYQSLLKLPGI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151266558 120 GTYTANAILCFGFREKTACVDANIKRVLLRLFGLDPNIHAKDLQIKANDFLNPNESFNHNQALIDLGALICSPKPKCAIC 199
Cdd:PRK13910   81 GAYTANAILCFGFREKSACVDANIKRVLLRLFGLDPNIHAKDLQIKANDFLNLNESFNHNQALIDLGALICSPKPKCAIC 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151266558 200 PLNPYCLGKNHPEKHTLKKKQEIIQEERYLGVVIQNNQIALEKIEQKLYLGMHHFPNLKENLEYKLPFLGAIKHSHTKFK 279
Cdd:PRK13910  161 PLNPYCLGKNNPEKHTLKKKQEIVQEERYLGVVIQNNQIALEKIEQKLYLGMHHFPNLKENLEYKLPFLGAIKHSHTKFK 240

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1151266558 280 LNLNLYLAAIKDLKNPIRFYSLKDLETLPISSMTLKILNFLKQKNLFGG 328
Cdd:PRK13910  241 LNLNLYLAAIKDLKNPIRFYSLKDLETLPISSMTLKILNFLKQKNLFGG 289
MutY COG1194
Adenine-specific DNA glycosylase, acts on AG and A-oxoG pairs [Replication, recombination and ...
 1-322 2.89e-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: 339.81  E-value: 2.89e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151266558   1 METLHNALLKWYEEFGRkDLPFRNLKginAPYEVYISEVMSQQTQINTVVErFYSPFLEAFPTLKDLANAPLEEVLLLWR 80
Cdd:COG1194     3 MASFAKRLLAWYDRHGR-DLPWRQTR---DPYRVWLSEIMLQQTQVATVIP-YYERFLERFPTVEALAAAPEDEVLKLWE 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151266558  81 GLGYYSRAKNLKKSAEICVKEHHSQLPNDYQSLLKLPGIGTYTANAILCFGFREKTACVDANIKRVLLRLFGLDPNI--- 157
Cdd:COG1194    78 GLGYYSRARNLHKAAQQVVEEHGGVFPDTYEELLALPGIGPYTAAAIASIAFGEPAPIVDGNVKRVLSRLFAIEGPIgsp 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151266558 158 -HAKDLQIKANDFLNPNESFNHNQALIDLGALICSPK-PKCAICPLNPYCLGKNHPEKHTL---KKKQEIIQEERYLGVV 232
Cdd:COG1194   158 aAKKELWALAEELLPPERPGDFNQALMDLGATVCTPKkPKCLLCPLQDDCAAFAEGRQEELpvkKPKKKKPERYGAALVI 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151266558 233 IQNNQIALEKIEQK-LYLGMHHFPN-----------LKENLEYKLPF-------LGAIKHSHTKFKLNLNLYLAAIKDLK 293
Cdd:COG1194   238 RDDGRVLLEKRPPKgLWGGLWEFPEfeweeaedpeaLERWLREELGLevewlepLGTVRHVFTHFRLHLTVYLARVPAGP 317

                         330       340       350
                  ....*....|....*....|....*....|...
gi 1151266558 294 NP----IRFYSLKDLETLPISSMTLKILNFLKQ 322
Cdd:COG1194   318 PAepdgGRWVPLEELAALPLPAPMRKLLKALLK 350
mutY TIGR01084
A/G-specific adenine glycosylase; This equivalog model identifies mutY members of the ...
 7-258 1.10e-97

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: 289.70  E-value: 1.10e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151266558   7 ALLKWYEEFGRKDLPFRNLKginAPYEVYISEVMSQQTQINTVVErFYSPFLEAFPTLKDLANAPLEEVLLLWRGLGYYS 86
Cdd:TIGR01084   5 DLLSWYDKYGRKTLPWRQNK---TPYRVWLSEVMLQQTQVATVIP-YFERFLERFPTVQALANAPQDEVLKLWEGLGYYA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151266558  87 RAKNLKKSAEICVKEHHSQLPNDYQSLLKLPGIGTYTANAILCFGFREKTACVDANIKRVLLRLFGLDPNIHAKD----L 162
Cdd:TIGR01084  81 RARNLHKAAQEVVEEFGGEFPQDFEDLAALPGVGRYTAGAILSFALNKPYPILDGNVKRVLSRLFAVEGWPGKKKvenrL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151266558 163 QIKANDFLNPNESFNHNQALIDLGALICSPK-PKCAICPLNPYCLGKNH--PEKHTLKKKQ--EIIQEERYLGVVIQNNQ 237
Cdd:TIGR01084 161 WTLAESLLPKADPEAFNQALMDLGAMICTRKkPKCDLCPLQDFCLAYQQgtWEEYPVKKPKaaPPERTTYFLVLQNYDGE 240

                         250       260
                  ....*....|....*....|..
gi 1151266558 238 IALEKIEQK-LYLGMHHFPNLK 258
Cdd:TIGR01084 241 VLLEQRPEKgLWGGLYCFPQFE 262
PRK10880 PRK10880
adenine DNA glycosylase;
7-282 2.81e-62

adenine DNA glycosylase;


Pssm-ID: 182805 [Multi-domain]  Cd Length: 350  Bit Score: 201.86  E-value: 2.81e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151266558   7 ALLKWYEEFGRKDLPFRNLKginAPYEVYISEVMSQQTQINTVVERFySPFLEAFPTLKDLANAPLEEVLLLWRGLGYYS 86
Cdd:PRK10880    9 QVLDWYDKYGRKTLPWQIDK---TPYKVWLSEVMLQQTQVATVIPYF-ERFMARFPTVTDLANAPLDEVLHLWTGLGYYA 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151266558  87 RAKNLKKSAEICVKEHHSQLPNDYQSLLKLPGIGTYTANAILCFGFREKTACVDANIKRVLLRLFGLDPNIHAKDLQIKA 166
Cdd:PRK10880   85 RARNLHKAAQQVATLHGGEFPETFEEVAALPGVGRSTAGAILSLSLGKHFPILDGNVKRVLARCYAVSGWPGKKEVENRL 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151266558 167 NDF------LNPNESFnhNQALIDLGALICS-PKPKCAICPLNPYCLG-KNH-----PEKhtlKKKQEIIQEERYLGVVI 233
Cdd:PRK10880  165 WQLseqvtpAVGVERF--NQAMMDLGAMVCTrSKPKCELCPLQNGCIAyANHswalyPGK---KPKQTLPERTGYFLLLQ 239

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1151266558 234 QNNQIALekiEQK----LYLGMHHFPNL--KENLEY----------KLPFLGAIKHSHTKFKLNL 282
Cdd:PRK10880  240 HGDEVWL---EQRppsgLWGGLFCFPQFadEEELRQwlaqrgiaadNLTQLTAFRHTFSHFHLDI 301
ENDO3c cd00056
endonuclease III; includes endonuclease III (DNA-(apurinic or apyrimidinic site) lyase), ...
 32-186 3.02e-48

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: 159.33  E-value: 3.02e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151266558  32 YEVYISEVMSQQTQINTVVERFYSPFLEAFPTLKDLANAPLEEVLLLWRGLGYYSRAKNLKKSAEICVKEHHS---QLPN 108
Cdd:cd00056     1 FEVLVSEILSQQTTDKAVNKAYERLFERYGPTPEALAAADEEELRELIRSLGYRRKAKYLKELARAIVEGFGGlvlDDPD 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1151266558 109 DYQSLLKLPGIGTYTANAILCFGFREKTACVDANIKRVLLRLFGLDPNIHAKDLQIKANDFLNPNESFNHNQALIDLG 186
Cdd:cd00056    81 AREELLALPGVGRKTANVVLLFALGPDAFPVDTHVRRVLKRLGLIPKKKTPEELEELLEELLPKPYWGEANQALMDLG 158
ENDO3c smart00478
endonuclease III; includes endonuclease III (DNA-(apurinic or apyrimidinic site) lyase), ...
 40-188 1.99e-43

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: 146.25  E-value: 1.99e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151266558   40 MSQQTQInTVVERFYSPFLEAFPTLKDLANAPLEEVLLLWRGLG-YYSRAKNLKKSAEICVKEHHSQLPNDYQSLLKLPG 118
Cdd:smart00478   1 LSQQTTD-ERVNKATERLFEKFPTPEDLAAADEEELEELIRGLGfYRRKARYLIELARILVEEYGGEVPDDREELLKLPG 79

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151266558  119 IGTYTANAILCFGFREKTACVDANIKRVLLRLFGLDPNIHAKDLQIKANDFLNPNESFNHNQALIDLGAL 188
Cdd:smart00478  80 VGRKTANAVLSFALGKPFIPVDTHVLRIAKRLGLVDKKSTPEEVEKLLEKLLPEEDWRELNLLLIDFGRT 149
HhH-GPD pfam00730
HhH-GPD superfamily base excision DNA repair protein; This family contains a diverse range of ...
 36-172 5.04e-39

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: 134.72  E-value: 5.04e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151266558  36 ISEVMSQQTQ---INTVVERFYSPFleaFPTLKDLANAPLEEVLLLWRGLGYY-SRAKNLKKSAEICVKEHHSQLPNDYQ 111
Cdd:pfam00730   1 VSAILSQQTSdkaVNKITERLFEKF---FPTPEDLADADEEELRELIRGLGFYrRKAKYLKELARILVEGYGGEVPLDEE 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1151266558 112 SLLK-LPGIGTYTANAILCFGFR--EKTACVDANIKRVLLRLFGLDPNIHAKDLQIKANDFLNP 172
Cdd:pfam00730  78 ELEAlLKGVGRWTAEAVLIFALGrpDPLPVVDTHVRRVLKRLGLIKEKPTPKEVERELEELWPP 141
Nth COG0177
Endonuclease III [Replication, recombination and repair];
5-205 4.03e-36

Endonuclease III [Replication, recombination and repair];


Pssm-ID: 439947 [Multi-domain]  Cd Length: 198  Bit Score: 129.06  E-value: 4.03e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151266558   5 HNALLKWYEEFgRKDLPFRNlkginaPYEVYISEVMSQQT---QINTVVERFYspflEAFPTLKDLANAPLEEVLLLWRG 81
Cdd:COG0177     1 LERLKELYPDA-KTELDYRD------PFELLVATILSAQTtdeRVNKATPRLF----ARYPTPEALAAADLEELEELIRP 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151266558  82 LGYY-SRAKNLKKSAEICVKEHHSQLPNDYQSLLKLPGIGTYTANAILCFGFREKTACVDANIKRVLLRLfGL----DPN 156
Cdd:COG0177    70 IGLYrNKAKNIIALARILVEKYGGEVPETREELESLPGVGRKTANVVLNFAFGKPAIAVDTHVHRVSNRL-GLvpgkDPE 148

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1151266558 157 IHAKDLQikanDFLNPNESFNHNQALIDLGALICSP-KPKCAICPLNPYC 205
Cdd:COG0177   149 EVEKDLM----KLIPKEYWGDLHHLLILHGRYICKArKPKCEECPLADLC 194
nth TIGR01083
endonuclease III; This equivalog model identifes nth members of the pfam00730 superfamily ...
 29-196 1.60e-21

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: 90.13  E-value: 1.60e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151266558  29 NAPYEVYISEVMSQQTQiNTVVERFYSPFLEAFPTLKDLANAPLEEVLLLWRGLGYY-SRAKNLKKSAEICVKEHHSQLP 107
Cdd:TIGR01083  25 NNPFELLVATILSAQAT-DKRVNKATPKLFEVYPTPQALAQAGLEELEEYIKSIGLYrNKAKNIIELCRKLVERYGGEVP 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151266558 108 NDYQSLLKLPGIGTYTANAILCFGFREKTACVDANIKRVLLRLfGL----DPNIHAKDLQ-IKANDFLNPnesFNHnqAL 182
Cdd:TIGR01083 104 EDREELVKLPGVGRKTANVVLNVAFGIPAIAVDTHVFRVSNRL-GLskgkDPIKVEEDLMkLVPREFWVK---LHH--WL 177

                         170
                  ....*....|....*
gi 1151266558 183 IDLGALICSP-KPKC 196
Cdd:TIGR01083 178 ILHGRYTCKArKPLC 192
HP0602 COG2231
3-Methyladenine DNA glycosylase, HhH-GPD/Endo3 superfamily [Replication, recombination and ...
 63-211 1.46e-17

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


Pssm-ID: 441832 [Multi-domain]  Cd Length: 220  Bit Score: 79.89  E-value: 1.46e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151266558  63 TLKDLANAPLEEVLLLWRGLGYYSR-AKNLKKSAEICVKEHHSQLPN--------DYQSLLKLPGIGTYTANAILCFGFR 133
Cdd:COG2231    61 DPEALAALDPEELAELIRPSGFYNQkAKRLKNLARWLVERYGGGLEKlkalpteeLREELLSLKGIGPETADSILLYAFN 140

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151266558 134 EKTACVDANIKRVLLRLFGLDPNIHAKDLQIKANDFLNPN-ESFNHNQALID-LGALICSPKPKCAICPLNPYCLGKNHP 211
Cdd:COG2231   141 RPVFVVDAYTRRIFSRLGLIEEDASYDELQRLFEENLPPDvALYNEFHALIVeHGKEYCKKKPKCEECPLRDLCPYGGQE 220
PRK10702 PRK10702
endonuclease III; Provisional
 29-205 4.46e-12

endonuclease III; Provisional


Pssm-ID: 182661 [Multi-domain]  Cd Length: 211  Bit Score: 64.27  E-value: 4.46e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151266558  29 NAPYEVYISEVMSQQT---QINTVVERFYSpfleafptlkdLANAPLEEVLLLWRGLGYY--------SRAKNLKKSAEI 97
Cdd:PRK10702   27 SSPFELLIAVLLSAQAtdvSVNKATAKLYP-----------VANTPAAMLELGVEGVKTYiktiglynSKAENVIKTCRI 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151266558  98 CVKEHHSQLPNDYQSLLKLPGIGTYTANAILCFGFREKTACVDANIKRVLLRLfGLDPNIHAKDLQIKANDFLNPNESFN 177
Cdd:PRK10702   96 LLEQHNGEVPEDRAALEALPGVGRKTANVVLNTAFGWPTIAVDTHIFRVCNRT-QFAPGKNVEQVEEKLLKVVPAEFKVD 174

                         170       180
                  ....*....|....*....|....*....
gi 1151266558 178 HNQALIDLGALIC-SPKPKCAICPLNPYC 205
Cdd:PRK10702  175 CHHWLILHGRYTCiARKPRCGSCIIEDLC 203
AlkA COG0122
3-methyladenine DNA glycosylase/8-oxoguanine DNA glycosylase [Replication, recombination and ...
 31-169 3.87e-09

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


Pssm-ID: 439892 [Multi-domain]  Cd Length: 255  Bit Score: 56.43  E-value: 3.87e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151266558  31 PYEVYISEVMSQQ-------TQINTVVERFYSPF------LEAFPTLKDLANAPLEEvlllWRGLGY-YSRAKNLKKSAE 96
Cdd:COG0122    84 PFEALVRAILGQQvsvaaarTIWRRLVALFGEPIegpgggLYAFPTPEALAAASEEE----LRACGLsRRKARYLRALAR 159

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151266558  97 ICVK-----EHHSQLPND--YQSLLKLPGIGTYTANAILCFGFREKTA--CVDANIKRVLLRLFGLDPNIHAKDLQIKAN 167
Cdd:COG0122   160 AVADgeldlEALAGLDDEeaIARLTALPGIGPWTAEMVLLFALGRPDAfpAGDLGLRRALGRLYGLGERPTPKELRELAE 239


                  ..
gi 1151266558 168 DF 169
Cdd:COG0122   240 PW 241
NUDIX_DNA_Glycosylase_C-MutY cd03431
C-terminal domain of DNA glycosylase; DNA glycosylase (MutY in bacteria and hMYH in humans) is ...
 222-318 3.72e-06

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: 45.37  E-value: 3.72e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151266558 222 IIQEERYLGVVIQNNQIALEKIEQKLYL-GMHHFPNL----------------KENLEYKLPFLGAIKH--SHtkFKLNL 282
Cdd:cd03431     1 VPERYFTVLVLRDGGRVLLEKRPEKGLLaGLWEFPLVeteeeeeeaeallgllAEELLLILEPLGEVKHvfSH--FRLHI 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1151266558 283 NLYLAAIKD----LKNPIRFYSLKDLETLPISSMTLKILN 318
Cdd:cd03431    79 TVYLVELPEappaAPDEGRWVDLEELDEYALPAPMRKLLE 118
ogg TIGR00588
8-oxoguanine DNA-glycosylase (ogg); All proteins in this family for which functions are known ...
 31-165 6.44e-06

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: 47.21  E-value: 6.44e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151266558  31 PYEVYISEVMSQQ---TQINTVVERFYSPF-----------LEAFPTLKDLANAPLEEVLllwRGLGYYSRAKNLKKSAE 96
Cdd:TIGR00588 119 PFECLISFICSSNnniARITRMVERLCQAFgprlitldgvtYHGFPSLHALTGPEAEAHL---RKLGLGYRARYIRETAR 195

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151266558  97 ICVKEH----------HSQLPNDYQSLLKLPGIGTYTANAILCFGFREKTAC-VDANIKRVLLRLFGldpnIHAKDLQIK 165
Cdd:TIGR00588 196 ALLEEQggrawlqqirGASYEDAREALCELPGVGPKVADCICLMGLDKPQAVpVDVHVWRIANRDYP----WHPKTSRAK 271
HHH pfam00633
Helix-hairpin-helix motif; The helix-hairpin-helix DNA-binding motif is found to be duplicated ...
 101-130 1.54e-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: 41.25  E-value: 1.54e-05
                          10        20        30
                  ....*....|....*....|....*....|
gi 1151266558 101 EHHSQLPNDYQSLLKLPGIGTYTANAILCF 130
Cdd:pfam00633   1 SLEGLIPASVEELLALPGVGPKTAEAILSY 30
NUDIX_4 pfam14815
NUDIX domain;
228-318 1.50e-03

NUDIX domain;


Pssm-ID: 464330 [Multi-domain]  Cd Length: 114  Bit Score: 37.68  E-value: 1.50e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151266558 228 YLGVVIQNNQIALEKIEQKLYL-GMHHFPNLK----ENLEYKLPFL------------GAIKHSHTKFKLNLNLY----L 286
Cdd:pfam14815   2 VLVIRNGDGRVLLRKRPEKGLLgGLWEFPGGKvepgETLEEALARLeelgievevlepGTVKHVFTHFRLTLHVYlvreV 81

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1151266558 287 AAIKDLKNPIRFYSLKDLETLPISSMTLKILN 318
Cdd:pfam14815  82 EGEEEPQQELRWVTPEELDKYALPAAVRKILE 113
FES smart00525
iron-sulpphur binding domain in DNA-(apurinic or apyrimidinic site) lyase (subfamily of ENDO3); ...
 189-208 9.09e-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: 33.29  E-value: 9.09e-03
                           10        20
                   ....*....|....*....|.
gi 1151266558  189 ICSP-KPKCAICPLNPYCLGK 208
Cdd:smart00525   1 ICTArKPRCDECPLKDLCPAY 21
 
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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