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Conserved domains on  [gi|490821070|ref|WP_004683167|]
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MULTISPECIES: A/G-specific adenine glycosylase [Brucella]

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 ...
 1-346 0e+00

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: 509.68  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490821070   1 MDPTTF---LLRWYDRHHRVLPWRVTPvdaakgdvaDPYRVWLSEIMLQQTTVEAVKSYFLRFIERWPTVRAMAKASEDD 77
Cdd:COG1194    1 MDMASFakrLLAWYDRHGRDLPWRQTR---------DPYRVWLSEIMLQQTQVATVIPYYERFLERFPTVEALAAAPEDE 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490821070  78 ILRAWAGLGYYSRARNLKKCADIVVAEHGGEFPKSAAGLKELPGIGDYTSAAIAAIAFGEQVAVVDGNVERVISRLYAID 157
Cdd:COG1194   72 VLKLWEGLGYYSRARNLHKAAQQVVEEHGGVFPDTYEELLALPGIGPYTAAAIASIAFGEPAPIVDGNVKRVLSRLFAIE 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490821070 158 TPL--PVAKAQIRALMGQMTPPDRPGDFAQAMMDLGATICTPRRPACALCPLNKGCIALCERDPEDFPVKAPKAEKPVRT 235
Cdd:COG1194  152 GPIgsPAAKKELWALAEELLPPERPGDFNQALMDLGATVCTPKKPKCLLCPLQDDCAAFAEGRQEELPVKKPKKKKPERY 231

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490821070 236 GAAFIAIAgDGSVYLRKRKGEGLLAGMTEVPGSGWTARIDGDA----TVNAAPFSAAWT-PSGTITHVFTHFELRLSVYR 310
Cdd:COG1194  232 GAALVIRD-DGRVLLEKRPPKGLWGGLWEFPEFEWEEAEDPEAlerwLREELGLEVEWLePLGTVRHVFTHFRLHLTVYL 310

                        330       340       350
                 ....*....|....*....|....*....|....*...
gi 490821070 311 A--SNVRKQAANEGWWSTPEELCGEALPTVMKKAIAAA 346
Cdd:COG1194  311 ArvPAGPPAEPDGGRWVPLEELAALPLPAPMRKLLKAL 348
 
Name Accession Description Interval E-value
MutY COG1194
Adenine-specific DNA glycosylase, acts on AG and A-oxoG pairs [Replication, recombination and ...
 1-346 0e+00

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: 509.68  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490821070   1 MDPTTF---LLRWYDRHHRVLPWRVTPvdaakgdvaDPYRVWLSEIMLQQTTVEAVKSYFLRFIERWPTVRAMAKASEDD 77
Cdd:COG1194    1 MDMASFakrLLAWYDRHGRDLPWRQTR---------DPYRVWLSEIMLQQTQVATVIPYYERFLERFPTVEALAAAPEDE 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490821070  78 ILRAWAGLGYYSRARNLKKCADIVVAEHGGEFPKSAAGLKELPGIGDYTSAAIAAIAFGEQVAVVDGNVERVISRLYAID 157
Cdd:COG1194   72 VLKLWEGLGYYSRARNLHKAAQQVVEEHGGVFPDTYEELLALPGIGPYTAAAIASIAFGEPAPIVDGNVKRVLSRLFAIE 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490821070 158 TPL--PVAKAQIRALMGQMTPPDRPGDFAQAMMDLGATICTPRRPACALCPLNKGCIALCERDPEDFPVKAPKAEKPVRT 235
Cdd:COG1194  152 GPIgsPAAKKELWALAEELLPPERPGDFNQALMDLGATVCTPKKPKCLLCPLQDDCAAFAEGRQEELPVKKPKKKKPERY 231

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490821070 236 GAAFIAIAgDGSVYLRKRKGEGLLAGMTEVPGSGWTARIDGDA----TVNAAPFSAAWT-PSGTITHVFTHFELRLSVYR 310
Cdd:COG1194  232 GAALVIRD-DGRVLLEKRPPKGLWGGLWEFPEFEWEEAEDPEAlerwLREELGLEVEWLePLGTVRHVFTHFRLHLTVYL 310

                        330       340       350
                 ....*....|....*....|....*....|....*...
gi 490821070 311 A--SNVRKQAANEGWWSTPEELCGEALPTVMKKAIAAA 346
Cdd:COG1194  311 ArvPAGPPAEPDGGRWVPLEELAALPLPAPMRKLLKAL 348
mutY TIGR01084
A/G-specific adenine glycosylase; This equivalog model identifies mutY members of the ...
 7-266 7.93e-113

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: 329.37  E-value: 7.93e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490821070    7 LLRWYDRHHR-VLPWRVTPvdaakgdvaDPYRVWLSEIMLQQTTVEAVKSYFLRFIERWPTVRAMAKASEDDILRAWAGL 85
Cdd:TIGR01084   6 LLSWYDKYGRkTLPWRQNK---------TPYRVWLSEVMLQQTQVATVIPYFERFLERFPTVQALANAPQDEVLKLWEGL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490821070   86 GYYSRARNLKKCADIVVAEHGGEFPKSAAGLKELPGIGDYTSAAIAAIAFGEQVAVVDGNVERVISRLYAIDTPL--PVA 163
Cdd:TIGR01084  77 GYYARARNLHKAAQEVVEEFGGEFPQDFEDLAALPGVGRYTAGAILSFALNKPYPILDGNVKRVLSRLFAVEGWPgkKKV 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490821070  164 KAQIRALMGQMTPPDRPGDFAQAMMDLGATICTPRRPACALCPLNKGCIALCERDPEDFPVKAPKAEKPVRTGAAFIAIA 243
Cdd:TIGR01084 157 ENRLWTLAESLLPKADPEAFNQALMDLGAMICTRKKPKCDLCPLQDFCLAYQQGTWEEYPVKKPKAAPPERTTYFLVLQN 236

                         250       260
                  ....*....|....*....|...
gi 490821070  244 GDGSVYLRKRKGEGLLAGMTEVP 266
Cdd:TIGR01084 237 YDGEVLLEQRPEKGLWGGLYCFP 259
PRK10880 PRK10880
adenine DNA glycosylase;
7-304 2.88e-82

adenine DNA glycosylase;


Pssm-ID: 182805 [Multi-domain]  Cd Length: 350  Bit Score: 254.25  E-value: 2.88e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490821070   7 LLRWYDRHHR-VLPWRVTPVdaakgdvadPYRVWLSEIMLQQTTVEAVKSYFLRFIERWPTVRAMAKASEDDILRAWAGL 85
Cdd:PRK10880  10 VLDWYDKYGRkTLPWQIDKT---------PYKVWLSEVMLQQTQVATVIPYFERFMARFPTVTDLANAPLDEVLHLWTGL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490821070  86 GYYSRARNLKKCADIVVAEHGGEFPKSAAGLKELPGIGDYTSAAIAAIAFGEQVAVVDGNVERVISRLYAIDTpLPVAK- 164
Cdd:PRK10880  81 GYYARARNLHKAAQQVATLHGGEFPETFEEVAALPGVGRSTAGAILSLSLGKHFPILDGNVKRVLARCYAVSG-WPGKKe 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490821070 165 --AQIRALMGQMTPPDRPGDFAQAMMDLGATICTPRRPACALCPLNKGCIALCERDPEDFPVKAPKAEKPVRTGaAFIAI 242
Cdd:PRK10880 160 veNRLWQLSEQVTPAVGVERFNQAMMDLGAMVCTRSKPKCELCPLQNGCIAYANHSWALYPGKKPKQTLPERTG-YFLLL 238

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490821070 243 AGDGSVYLRKRKGEGLLAGM-------TEVPGSGWTAR--IDGDATVNAAPFSaawtpsgtitHVFTHFEL 304
Cdd:PRK10880 239 QHGDEVWLEQRPPSGLWGGLfcfpqfaDEEELRQWLAQrgIAADNLTQLTAFR----------HTFSHFHL 299
ENDO3c cd00056
endonuclease III; includes endonuclease III (DNA-(apurinic or apyrimidinic site) lyase), ...
 36-191 1.59e-53

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: 173.58  E-value: 1.59e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490821070  36 YRVWLSEIMLQQTTVEAVKSYFLRFIERW-PTVRAMAKASEDDILRAWAGLGYYSRARNLKKCADIVVAEHGGEF---PK 111
Cdd:cd00056    1 FEVLVSEILSQQTTDKAVNKAYERLFERYgPTPEALAAADEEELRELIRSLGYRRKAKYLKELARAIVEGFGGLVlddPD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490821070 112 SAAGLKELPGIGDYTSAAIAAIAFGEQVAVVDGNVERVISRLYAIdtPLPVAKAQIRALMGQMTPPDRPGDFAQAMMDLG 191
Cdd:cd00056   81 AREELLALPGVGRKTANVVLLFALGPDAFPVDTHVRRVLKRLGLI--PKKKTPEELEELLEELLPKPYWGEANQALMDLG 158
ENDO3c smart00478
endonuclease III; includes endonuclease III (DNA-(apurinic or apyrimidinic site) lyase), ...
 44-193 2.71e-41

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: 141.63  E-value: 2.71e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490821070    44 MLQQTTVEAVKSYFLRFIERWPTVRAMAKASEDDILRAWAGLG-YYSRARNLKKCADIVVAEHGGEFPKSAAGLKELPGI 122
Cdd:smart00478   1 LSQQTTDERVNKATERLFEKFPTPEDLAAADEEELEELIRGLGfYRRKARYLIELARILVEEYGGEVPDDREELLKLPGV 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490821070   123 GDYTSAAIAAIAFGEQVAVVDGNVERVISRLYAIDTPLpvAKAQIRALMGQMTPPDRPGDFAQAMMDLGAT 193
Cdd:smart00478  81 GRKTANAVLSFALGKPFIPVDTHVLRIAKRLGLVDKKS--TPEEVEKLLEKLLPEEDWRELNLLLIDFGRT 149
HhH-GPD pfam00730
HhH-GPD superfamily base excision DNA repair protein; This family contains a diverse range of ...
 40-158 6.42e-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: 117.00  E-value: 6.42e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490821070   40 LSEIMLQQTTVEAVKSYFLRFIERW-PTVRAMAKASEDDILRAWAGLGYY-SRARNLKKCADIVVAEHGGEFPKSAAGLK 117
Cdd:pfam00730   1 VSAILSQQTSDKAVNKITERLFEKFfPTPEDLADADEEELRELIRGLGFYrRKAKYLKELARILVEGYGGEVPLDEEELE 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 490821070  118 E-LPGIGDYTSAAIAAIAFG--EQVAVVDGNVERVISRLYAIDT 158
Cdd:pfam00730  81 AlLKGVGRWTAEAVLIFALGrpDPLPVVDTHVRRVLKRLGLIKE 124
 
Name Accession Description Interval E-value
MutY COG1194
Adenine-specific DNA glycosylase, acts on AG and A-oxoG pairs [Replication, recombination and ...
 1-346 0e+00

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: 509.68  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490821070   1 MDPTTF---LLRWYDRHHRVLPWRVTPvdaakgdvaDPYRVWLSEIMLQQTTVEAVKSYFLRFIERWPTVRAMAKASEDD 77
Cdd:COG1194    1 MDMASFakrLLAWYDRHGRDLPWRQTR---------DPYRVWLSEIMLQQTQVATVIPYYERFLERFPTVEALAAAPEDE 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490821070  78 ILRAWAGLGYYSRARNLKKCADIVVAEHGGEFPKSAAGLKELPGIGDYTSAAIAAIAFGEQVAVVDGNVERVISRLYAID 157
Cdd:COG1194   72 VLKLWEGLGYYSRARNLHKAAQQVVEEHGGVFPDTYEELLALPGIGPYTAAAIASIAFGEPAPIVDGNVKRVLSRLFAIE 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490821070 158 TPL--PVAKAQIRALMGQMTPPDRPGDFAQAMMDLGATICTPRRPACALCPLNKGCIALCERDPEDFPVKAPKAEKPVRT 235
Cdd:COG1194  152 GPIgsPAAKKELWALAEELLPPERPGDFNQALMDLGATVCTPKKPKCLLCPLQDDCAAFAEGRQEELPVKKPKKKKPERY 231

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490821070 236 GAAFIAIAgDGSVYLRKRKGEGLLAGMTEVPGSGWTARIDGDA----TVNAAPFSAAWT-PSGTITHVFTHFELRLSVYR 310
Cdd:COG1194  232 GAALVIRD-DGRVLLEKRPPKGLWGGLWEFPEFEWEEAEDPEAlerwLREELGLEVEWLePLGTVRHVFTHFRLHLTVYL 310

                        330       340       350
                 ....*....|....*....|....*....|....*...
gi 490821070 311 A--SNVRKQAANEGWWSTPEELCGEALPTVMKKAIAAA 346
Cdd:COG1194  311 ArvPAGPPAEPDGGRWVPLEELAALPLPAPMRKLLKAL 348
mutY TIGR01084
A/G-specific adenine glycosylase; This equivalog model identifies mutY members of the ...
 7-266 7.93e-113

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: 329.37  E-value: 7.93e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490821070    7 LLRWYDRHHR-VLPWRVTPvdaakgdvaDPYRVWLSEIMLQQTTVEAVKSYFLRFIERWPTVRAMAKASEDDILRAWAGL 85
Cdd:TIGR01084   6 LLSWYDKYGRkTLPWRQNK---------TPYRVWLSEVMLQQTQVATVIPYFERFLERFPTVQALANAPQDEVLKLWEGL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490821070   86 GYYSRARNLKKCADIVVAEHGGEFPKSAAGLKELPGIGDYTSAAIAAIAFGEQVAVVDGNVERVISRLYAIDTPL--PVA 163
Cdd:TIGR01084  77 GYYARARNLHKAAQEVVEEFGGEFPQDFEDLAALPGVGRYTAGAILSFALNKPYPILDGNVKRVLSRLFAVEGWPgkKKV 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490821070  164 KAQIRALMGQMTPPDRPGDFAQAMMDLGATICTPRRPACALCPLNKGCIALCERDPEDFPVKAPKAEKPVRTGAAFIAIA 243
Cdd:TIGR01084 157 ENRLWTLAESLLPKADPEAFNQALMDLGAMICTRKKPKCDLCPLQDFCLAYQQGTWEEYPVKKPKAAPPERTTYFLVLQN 236

                         250       260
                  ....*....|....*....|...
gi 490821070  244 GDGSVYLRKRKGEGLLAGMTEVP 266
Cdd:TIGR01084 237 YDGEVLLEQRPEKGLWGGLYCFP 259
PRK10880 PRK10880
adenine DNA glycosylase;
7-304 2.88e-82

adenine DNA glycosylase;


Pssm-ID: 182805 [Multi-domain]  Cd Length: 350  Bit Score: 254.25  E-value: 2.88e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490821070   7 LLRWYDRHHR-VLPWRVTPVdaakgdvadPYRVWLSEIMLQQTTVEAVKSYFLRFIERWPTVRAMAKASEDDILRAWAGL 85
Cdd:PRK10880  10 VLDWYDKYGRkTLPWQIDKT---------PYKVWLSEVMLQQTQVATVIPYFERFMARFPTVTDLANAPLDEVLHLWTGL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490821070  86 GYYSRARNLKKCADIVVAEHGGEFPKSAAGLKELPGIGDYTSAAIAAIAFGEQVAVVDGNVERVISRLYAIDTpLPVAK- 164
Cdd:PRK10880  81 GYYARARNLHKAAQQVATLHGGEFPETFEEVAALPGVGRSTAGAILSLSLGKHFPILDGNVKRVLARCYAVSG-WPGKKe 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490821070 165 --AQIRALMGQMTPPDRPGDFAQAMMDLGATICTPRRPACALCPLNKGCIALCERDPEDFPVKAPKAEKPVRTGaAFIAI 242
Cdd:PRK10880 160 veNRLWQLSEQVTPAVGVERFNQAMMDLGAMVCTRSKPKCELCPLQNGCIAYANHSWALYPGKKPKQTLPERTG-YFLLL 238

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490821070 243 AGDGSVYLRKRKGEGLLAGM-------TEVPGSGWTAR--IDGDATVNAAPFSaawtpsgtitHVFTHFEL 304
Cdd:PRK10880 239 QHGDEVWLEQRPPSGLWGGLfcfpqfaDEEELRQWLAQrgIAADNLTQLTAFR----------HTFSHFHL 299
ENDO3c cd00056
endonuclease III; includes endonuclease III (DNA-(apurinic or apyrimidinic site) lyase), ...
 36-191 1.59e-53

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: 173.58  E-value: 1.59e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490821070  36 YRVWLSEIMLQQTTVEAVKSYFLRFIERW-PTVRAMAKASEDDILRAWAGLGYYSRARNLKKCADIVVAEHGGEF---PK 111
Cdd:cd00056    1 FEVLVSEILSQQTTDKAVNKAYERLFERYgPTPEALAAADEEELRELIRSLGYRRKAKYLKELARAIVEGFGGLVlddPD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490821070 112 SAAGLKELPGIGDYTSAAIAAIAFGEQVAVVDGNVERVISRLYAIdtPLPVAKAQIRALMGQMTPPDRPGDFAQAMMDLG 191
Cdd:cd00056   81 AREELLALPGVGRKTANVVLLFALGPDAFPVDTHVRRVLKRLGLI--PKKKTPEELEELLEELLPKPYWGEANQALMDLG 158
ENDO3c smart00478
endonuclease III; includes endonuclease III (DNA-(apurinic or apyrimidinic site) lyase), ...
 44-193 2.71e-41

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: 141.63  E-value: 2.71e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490821070    44 MLQQTTVEAVKSYFLRFIERWPTVRAMAKASEDDILRAWAGLG-YYSRARNLKKCADIVVAEHGGEFPKSAAGLKELPGI 122
Cdd:smart00478   1 LSQQTTDERVNKATERLFEKFPTPEDLAAADEEELEELIRGLGfYRRKARYLIELARILVEEYGGEVPDDREELLKLPGV 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490821070   123 GDYTSAAIAAIAFGEQVAVVDGNVERVISRLYAIDTPLpvAKAQIRALMGQMTPPDRPGDFAQAMMDLGAT 193
Cdd:smart00478  81 GRKTANAVLSFALGKPFIPVDTHVLRIAKRLGLVDKKS--TPEEVEKLLEKLLPEEDWRELNLLLIDFGRT 149
PRK13910 PRK13910
DNA glycosylase MutY; Provisional
 44-312 7.10e-41

DNA glycosylase MutY; Provisional


Pssm-ID: 172427 [Multi-domain]  Cd Length: 289  Bit Score: 145.16  E-value: 7.10e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490821070  44 MLQQTTVEAV-KSYFLRFIERWPTVRAMAKASEDDILRAWAGLGYYSRARNLKKCADIVVAEHGGEFPKSAAGLKELPGI 122
Cdd:PRK13910   1 MSQQTQINTVvERFYSPFLEAFPTLKDLANAPLEEVLLLWRGLGYYSRAKNLKKSAEICVKEHHSQLPNDYQSLLKLPGI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490821070 123 GDYTSAAIAAIAFGEQVAVVDGNVERVISRLYAIDTPLPVAKAQIRAlmGQMTPPDRPGDFAQAMMDLGATICTPrRPAC 202
Cdd:PRK13910  81 GAYTANAILCFGFREKSACVDANIKRVLLRLFGLDPNIHAKDLQIKA--NDFLNLNESFNHNQALIDLGALICSP-KPKC 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490821070 203 ALCPLNKGCIAlcERDPEDFPVKapKAEKPVRTGAAFIAIAGDGSVYLRKRKgEGLLAGMTEVPGSGWTARIDgdatvna 282
Cdd:PRK13910 158 AICPLNPYCLG--KNNPEKHTLK--KKQEIVQEERYLGVVIQNNQIALEKIE-QKLYLGMHHFPNLKENLEYK------- 225

                        250       260       270
                 ....*....|....*....|....*....|
gi 490821070 283 APFsaawtpSGTITHVFTHFELRLSVYRAS 312
Cdd:PRK13910 226 LPF------LGAIKHSHTKFKLNLNLYLAA 249
Nth COG0177
Endonuclease III [Replication, recombination and repair];
34-211 6.09e-36

Endonuclease III [Replication, recombination and repair];


Pssm-ID: 439947 [Multi-domain]  Cd Length: 198  Bit Score: 129.45  E-value: 6.09e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490821070  34 DPYRVWLSEIMLQQTTVEAVKSYFLRFIERWPTVRAMAKASEDDILRAWAGLGYY-SRARNLKKCADIVVAEHGGEFPKS 112
Cdd:COG0177   19 DPFELLVATILSAQTTDERVNKATPRLFARYPTPEALAAADLEELEELIRPIGLYrNKAKNIIALARILVEKYGGEVPET 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490821070 113 AAGLKELPGIGDYTSAAIAAIAFGEQVAVVDGNVERVISRLYAID--TPLPVAKaqirALMgQMTPPDRPGDFAQAMMDL 190
Cdd:COG0177   99 REELESLPGVGRKTANVVLNFAFGKPAIAVDTHVHRVSNRLGLVPgkDPEEVEK----DLM-KLIPKEYWGDLHHLLILH 173

                        170       180
                 ....*....|....*....|.
gi 490821070 191 GATICTPRRPACALCPLNKGC 211
Cdd:COG0177  174 GRYICKARKPKCEECPLADLC 194
HhH-GPD pfam00730
HhH-GPD superfamily base excision DNA repair protein; This family contains a diverse range of ...
 40-158 6.42e-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: 117.00  E-value: 6.42e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490821070   40 LSEIMLQQTTVEAVKSYFLRFIERW-PTVRAMAKASEDDILRAWAGLGYY-SRARNLKKCADIVVAEHGGEFPKSAAGLK 117
Cdd:pfam00730   1 VSAILSQQTSDKAVNKITERLFEKFfPTPEDLADADEEELRELIRGLGFYrRKAKYLKELARILVEGYGGEVPLDEEELE 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 490821070  118 E-LPGIGDYTSAAIAAIAFG--EQVAVVDGNVERVISRLYAIDT 158
Cdd:pfam00730  81 AlLKGVGRWTAEAVLIFALGrpDPLPVVDTHVRRVLKRLGLIKE 124
NUDIX_DNA_Glycosylase_C-MutY cd03431
C-terminal domain of DNA glycosylase; DNA glycosylase (MutY in bacteria and hMYH in humans) is ...
 231-344 8.92e-25

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: 97.37  E-value: 8.92e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490821070 231 KPVRTGAAFIAIAGdGSVYLRKRKGEGLLAGMTEVPGSGWTARIDGD---ATVNAAPFSAAWTPSGTITHVFTHFELRLS 307
Cdd:cd03431    1 VPERYFTVLVLRDG-GRVLLEKRPEKGLLAGLWEFPLVETEEEEEEAealLGLLAEELLLILEPLGEVKHVFSHFRLHIT 79

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 490821070 308 VYRA--SNVRKQAANEGWWSTPEELCGEALPTVMKKAIA 344
Cdd:cd03431   80 VYLVelPEAPPAAPDEGRWVDLEELDEYALPAPMRKLLE 118
NUDIX_4 pfam14815
NUDIX domain;
237-345 1.12e-22

NUDIX domain;


Pssm-ID: 464330 [Multi-domain]  Cd Length: 114  Bit Score: 91.61  E-value: 1.12e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490821070  237 AAFIAIAGDGSVYLRKRKGEGLLAGMTEVPGSGWtarIDGDATVNAAPFSAAW------TPSGTITHVFTHFELRLSVYR 310
Cdd:pfam14815   1 AVLVIRNGDGRVLLRKRPEKGLLGGLWEFPGGKV---EPGETLEEALARLEELgievevLEPGTVKHVFTHFRLTLHVYL 77

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 490821070  311 ASNV--RKQAANEGWWSTPEELCGEALPTVMKKAIAA 345
Cdd:pfam14815  78 VREVegEEEPQQELRWVTPEELDKYALPAAVRKILEA 114
PRK10702 PRK10702
endonuclease III; Provisional
 35-211 3.75e-10

endonuclease III; Provisional


Pssm-ID: 182661 [Multi-domain]  Cd Length: 211  Bit Score: 58.88  E-value: 3.75e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490821070  35 PYRVWLSEIMLQQTTVEAVKSYFLRFIERWPTVRAMAKASEDDILRAWAGLGYY-SRARNLKKCADIVVAEHGGEFPKSA 113
Cdd:PRK10702  29 PFELLIAVLLSAQATDVSVNKATAKLYPVANTPAAMLELGVEGVKTYIKTIGLYnSKAENVIKTCRILLEQHNGEVPEDR 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490821070 114 AGLKELPGIGDYTSAAIAAIAFGEQVAVVDGNVERVISRlyaidTPLPVAK--AQIRALMGQMTPPDRPGDFAQAMMDLG 191
Cdd:PRK10702 109 AALEALPGVGRKTANVVLNTAFGWPTIAVDTHIFRVCNR-----TQFAPGKnvEQVEEKLLKVVPAEFKVDCHHWLILHG 183

                        170       180
                 ....*....|....*....|
gi 490821070 192 ATICTPRRPACALCPLNKGC 211
Cdd:PRK10702 184 RYTCIARKPRCGSCIIEDLC 203
HP0602 COG2231
3-Methyladenine DNA glycosylase, HhH-GPD/Endo3 superfamily [Replication, recombination and ...
 66-211 3.45e-08

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


Pssm-ID: 441832 [Multi-domain]  Cd Length: 220  Bit Score: 53.31  E-value: 3.45e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490821070  66 TVRAMAKASEDDILRAWAGLGYYSR-ARNLKKCADIVVAEHGGEFPKSAAG--------LKELPGIGDYTSAAIAAIAFG 136
Cdd:COG2231   61 DPEALAALDPEELAELIRPSGFYNQkAKRLKNLARWLVERYGGGLEKLKALpteelreeLLSLKGIGPETADSILLYAFN 140

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490821070 137 EQVAVVDGNVERVISRLYAIDtpLPVAKAQIRALMGQMTPPDrPGDFAQ--AMMD-LGATICTPRrPACALCPLNKGC 211
Cdd:COG2231  141 RPVFVVDAYTRRIFSRLGLIE--EDASYDELQRLFEENLPPD-VALYNEfhALIVeHGKEYCKKK-PKCEECPLRDLC 214
FES smart00525
iron-sulpphur binding domain in DNA-(apurinic or apyrimidinic site) lyase (subfamily of ENDO3); ...
 194-213 5.83e-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: 39.46  E-value: 5.83e-05
                           10        20
                   ....*....|....*....|
gi 490821070   194 ICTPRRPACALCPLNKGCIA 213
Cdd:smart00525   1 ICTARKPRCDECPLKDLCPA 20
AlkA COG0122
3-methyladenine DNA glycosylase/8-oxoguanine DNA glycosylase [Replication, recombination and ...
 46-171 5.07e-04

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


Pssm-ID: 439892 [Multi-domain]  Cd Length: 255  Bit Score: 41.02  E-value: 5.07e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490821070  46 QQTTVEAVKSYFLRFIERW--------------PTVRAMAKASEDDiLRAwAGLGYYsRARNLKKCADiVVAEHGGEFPK 111
Cdd:COG0122   95 QQVSVAAARTIWRRLVALFgepiegpggglyafPTPEALAAASEEE-LRA-CGLSRR-KARYLRALAR-AVADGELDLEA 170

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490821070 112 SAAG--------LKELPGIGDYTSAAIAAIAFG--EQVAVVDGNVERVISRLYAIDTplPVAKAQIRALM 171
Cdd:COG0122  171 LAGLddeeaiarLTALPGIGPWTAEMVLLFALGrpDAFPAGDLGLRRALGRLYGLGE--RPTPKELRELA 238
EndIII_4Fe-2S pfam10576
Iron-sulfur binding domain of endonuclease III; Escherichia coli endonuclease III (EC 4.2.99. ...
 195-211 5.63e-04

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: 36.60  E-value: 5.63e-04
                          10
                  ....*....|....*..
gi 490821070  195 CTPRRPACALCPLNKGC 211
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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