NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|2320295463|ref|WP_263667456|]
View 

A/G-specific adenine glycosylase [Campylobacter sp. CNRCH_2013_0855]

Protein Classification

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

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

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

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
MutY COG1194
Adenine-specific DNA glycosylase, acts on AG and A-oxoG pairs [Replication, recombination and ...
 6-342 4.17e-104

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: 309.38  E-value: 4.17e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320295463   6 MQKIHENILKWYNESGRkSLPWRILHDeykkyakaddleklknidiAYAVYVSEIMLQQTQVKSVLqNYYFQFLAKFPSL 85
Cdd:COG1194     3 MASFAKRLLAWYDRHGR-DLPWRQTRD-------------------PYRVWLSEIMLQQTQVATVI-PYYERFLERFPTV 61

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320295463  86 KALSMVSEDEVLKAWQGLGYYTRARNIHKCAKICTQEFNAKLPSDINELQKLPGIGEYTAGAIACFGFLQAKSFVDANIK 165
Cdd:COG1194    62 EALAAAPEDEVLKLWEGLGYYSRARNLHKAAQQVVEEHGGVFPDTYEELLALPGIGPYTAAAIASIAFGEPAPIVDGNVK 141

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320295463 166 RVLSRFYSLQNPSS-----KLLTQRAKEFLNYDNAFDHNQALLDIGALVCLPKNAKCEICPLKDFCSG--KNEYEKFHV- 237
Cdd:COG1194   142 RVLSRLFAIEGPIGspaakKELWALAEELLPPERPGDFNQALMDLGATVCTPKKPKCLLCPLQDDCAAfaEGRQEELPVk 221

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320295463 238 SKKIQYKNTILKILIVQKNEQFLLIKSQEK-LYFNLYNFLEYKNQKKAKF--------------------IGEFKHSYTK 296
Cdd:COG1194   222 KPKKKKPERYGAALVIRDDGRVLLEKRPPKgLWGGLWEFPEFEWEEAEDPealerwlreelglevewlepLGTVRHVFTH 301

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*....
gi 2320295463 297 YKINAKVYFLKDDDFEDLQAKAFAY---KELEYITLSKLALKAFELFKK 342
Cdd:COG1194   302 FRLHLTVYLARVPAGPPAEPDGGRWvplEELAALPLPAPMRKLLKALLK 350
 
Name Accession Description Interval E-value
MutY COG1194
Adenine-specific DNA glycosylase, acts on AG and A-oxoG pairs [Replication, recombination and ...
 6-342 4.17e-104

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: 309.38  E-value: 4.17e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320295463   6 MQKIHENILKWYNESGRkSLPWRILHDeykkyakaddleklknidiAYAVYVSEIMLQQTQVKSVLqNYYFQFLAKFPSL 85
Cdd:COG1194     3 MASFAKRLLAWYDRHGR-DLPWRQTRD-------------------PYRVWLSEIMLQQTQVATVI-PYYERFLERFPTV 61

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320295463  86 KALSMVSEDEVLKAWQGLGYYTRARNIHKCAKICTQEFNAKLPSDINELQKLPGIGEYTAGAIACFGFLQAKSFVDANIK 165
Cdd:COG1194    62 EALAAAPEDEVLKLWEGLGYYSRARNLHKAAQQVVEEHGGVFPDTYEELLALPGIGPYTAAAIASIAFGEPAPIVDGNVK 141

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320295463 166 RVLSRFYSLQNPSS-----KLLTQRAKEFLNYDNAFDHNQALLDIGALVCLPKNAKCEICPLKDFCSG--KNEYEKFHV- 237
Cdd:COG1194   142 RVLSRLFAIEGPIGspaakKELWALAEELLPPERPGDFNQALMDLGATVCTPKKPKCLLCPLQDDCAAfaEGRQEELPVk 221

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320295463 238 SKKIQYKNTILKILIVQKNEQFLLIKSQEK-LYFNLYNFLEYKNQKKAKF--------------------IGEFKHSYTK 296
Cdd:COG1194   222 KPKKKKPERYGAALVIRDDGRVLLEKRPPKgLWGGLWEFPEFEWEEAEDPealerwlreelglevewlepLGTVRHVFTH 301

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*....
gi 2320295463 297 YKINAKVYFLKDDDFEDLQAKAFAY---KELEYITLSKLALKAFELFKK 342
Cdd:COG1194   302 FRLHLTVYLARVPAGPPAEPDGGRWvplEELAALPLPAPMRKLLKALLK 350
mutY TIGR01084
A/G-specific adenine glycosylase; This equivalog model identifies mutY members of the ...
 8-291 1.25e-101

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: 300.48  E-value: 1.25e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320295463   8 KIHENILKWYNESGRKSLPWRILHDEYKkyakaddleklknidiayaVYVSEIMLQQTQVKSVLQnYYFQFLAKFPSLKA 87
Cdd:TIGR01084   1 QFSEDLLSWYDKYGRKTLPWRQNKTPYR-------------------VWLSEVMLQQTQVATVIP-YFERFLERFPTVQA 60

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320295463  88 LSMVSEDEVLKAWQGLGYYTRARNIHKCAKICTQEFNAKLPSDINELQKLPGIGEYTAGAIACFGFLQAKSFVDANIKRV 167
Cdd:TIGR01084  61 LANAPQDEVLKLWEGLGYYARARNLHKAAQEVVEEFGGEFPQDFEDLAALPGVGRYTAGAILSFALNKPYPILDGNVKRV 140

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320295463 168 LSRFYSLQNPSSKLLTQR-----AKEFLNYDNAFDHNQALLDIGALVCLPKNAKCEICPLKDFCSGK--NEYEKFHVSKK 240
Cdd:TIGR01084 141 LSRLFAVEGWPGKKKVENrlwtlAESLLPKADPEAFNQALMDLGAMICTRKKPKCDLCPLQDFCLAYqqGTWEEYPVKKP 220

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2320295463 241 IQYK--NTILKILIVQKNEQFLLIK-SQEKLYFNLYNFLEYKNQKK-AKFIGEFK 291
Cdd:TIGR01084 221 KAAPpeRTTYFLVLQNYDGEVLLEQrPEKGLWGGLYCFPQFEDEDSlAFLLAQRG 275
PRK13910 PRK13910
DNA glycosylase MutY; Provisional
 61-344 1.41e-69

DNA glycosylase MutY; Provisional


Pssm-ID: 172427 [Multi-domain]  Cd Length: 289  Bit Score: 219.12  E-value: 1.41e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320295463  61 MLQQTQVKSVLQNYYFQFLAKFPSLKALSMVSEDEVLKAWQGLGYYTRARNIHKCAKICTQEFNAKLPSDINELQKLPGI 140
Cdd:PRK13910    1 MSQQTQINTVVERFYSPFLEAFPTLKDLANAPLEEVLLLWRGLGYYSRAKNLKKSAEICVKEHHSQLPNDYQSLLKLPGI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320295463 141 GEYTAGAIACFGFLQAKSFVDANIKRVLSRFYSLQ-NPSSKLLTQRAKEFLNYDNAFDHNQALLDIGALVCLPKnAKCEI 219
Cdd:PRK13910   81 GAYTANAILCFGFREKSACVDANIKRVLLRLFGLDpNIHAKDLQIKANDFLNLNESFNHNQALIDLGALICSPK-PKCAI 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320295463 220 CPLKDFCSGKNEYEKFHVSKKIQYKNTILKILIVQKNEQFLLIKSQEKLYFNLYNFLEYKN--QKKAKFIGEFKHSYTKY 297
Cdd:PRK13910  160 CPLNPYCLGKNNPEKHTLKKKQEIVQEERYLGVVIQNNQIALEKIEQKLYLGMHHFPNLKEnlEYKLPFLGAIKHSHTKF 239

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 2320295463 298 KINAKVYFLKDDDFEDlQAKAFAYKELEYITLSKLALKAFELFKKSD 344
Cdd:PRK13910  240 KLNLNLYLAAIKDLKN-PIRFYSLKDLETLPISSMTLKILNFLKQKN 285
ENDO3c cd00056
endonuclease III; includes endonuclease III (DNA-(apurinic or apyrimidinic site) lyase), ...
 53-206 5.04e-42

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: 143.54  E-value: 5.04e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320295463  53 YAVYVSEIMLQQTQVKSVLQnYYFQFLAKF-PSLKALSMVSEDEVLKAWQGLGYYTRARNIHKCAKICTQEFN---AKLP 128
Cdd:cd00056     1 FEVLVSEILSQQTTDKAVNK-AYERLFERYgPTPEALAAADEEELRELIRSLGYRRKAKYLKELARAIVEGFGglvLDDP 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2320295463 129 SDINELQKLPGIGEYTAGAIACFGFLQAKSFVDANIKRVLSRFYSLQNPSS-KLLTQRAKEFLNYDNAFDHNQALLDIG 206
Cdd:cd00056    80 DAREELLALPGVGRKTANVVLLFALGPDAFPVDTHVRRVLKRLGLIPKKKTpEELEELLEELLPKPYWGEANQALMDLG 158
ENDO3c smart00478
endonuclease III; includes endonuclease III (DNA-(apurinic or apyrimidinic site) lyase), ...
 61-208 2.71e-33

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: 120.45  E-value: 2.71e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320295463   61 MLQQTQVKSVlQNYYFQFLAKFPSLKALSMVSEDEVLKAWQGLG-YYTRARNIHKCAKICTQEFNAKLPSDINELQKLPG 139
Cdd:smart00478   1 LSQQTTDERV-NKATERLFEKFPTPEDLAAADEEELEELIRGLGfYRRKARYLIELARILVEEYGGEVPDDREELLKLPG 79

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320295463  140 IGEYTAGAIACFGFLQAKSFVDANIKRVLSRFYSLQNPSSKLLTQR-AKEFLNYDNAFDHNQALLDIGAL 208
Cdd:smart00478  80 VGRKTANAVLSFALGKPFIPVDTHVLRIAKRLGLVDKKSTPEEVEKlLEKLLPEEDWRELNLLLIDFGRT 149
HhH-GPD pfam00730
HhH-GPD superfamily base excision DNA repair protein; This family contains a diverse range of ...
 57-191 9.72e-30

HhH-GPD superfamily base excision DNA repair protein; This family contains a diverse range of structurally related DNA repair proteins. The superfamily is called the HhH-GPD family after its hallmark Helix-hairpin-helix and Gly/Pro rich loop followed by a conserved aspartate. This includes endonuclease III, EC:4.2.99.18 and MutY an A/G-specific adenine glycosylase, both have a C terminal 4Fe-4S cluster. The family also includes 8-oxoguanine DNA glycosylases. The methyl-CPG binding protein MBD4 also contains a related domain that is a thymine DNA glycosylase. The family also includes DNA-3-methyladenine glycosylase II EC:3.2.2.21 and other members of the AlkA family.


Pssm-ID: 425841 [Multi-domain]  Cd Length: 141  Bit Score: 110.84  E-value: 9.72e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320295463  57 VSEIMLQQTQVKSVLQnYYFQFLAK-FPSLKALSMVSEDEVLKAWQGLGYYTR-ARNIHKCAKICTQEFNAKLPSDINEL 134
Cdd:pfam00730   1 VSAILSQQTSDKAVNK-ITERLFEKfFPTPEDLADADEEELRELIRGLGFYRRkAKYLKELARILVEGYGGEVPLDEEEL 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2320295463 135 QK-LPGIGEYTAGAIACFGFLQAKSF--VDANIKRVLSRFYSL-QNPSSKLLTQRAKEFLN 191
Cdd:pfam00730  80 EAlLKGVGRWTAEAVLIFALGRPDPLpvVDTHVRRVLKRLGLIkEKPTPKEVERELEELWP 140
 
Name Accession Description Interval E-value
MutY COG1194
Adenine-specific DNA glycosylase, acts on AG and A-oxoG pairs [Replication, recombination and ...
 6-342 4.17e-104

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: 309.38  E-value: 4.17e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320295463   6 MQKIHENILKWYNESGRkSLPWRILHDeykkyakaddleklknidiAYAVYVSEIMLQQTQVKSVLqNYYFQFLAKFPSL 85
Cdd:COG1194     3 MASFAKRLLAWYDRHGR-DLPWRQTRD-------------------PYRVWLSEIMLQQTQVATVI-PYYERFLERFPTV 61

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320295463  86 KALSMVSEDEVLKAWQGLGYYTRARNIHKCAKICTQEFNAKLPSDINELQKLPGIGEYTAGAIACFGFLQAKSFVDANIK 165
Cdd:COG1194    62 EALAAAPEDEVLKLWEGLGYYSRARNLHKAAQQVVEEHGGVFPDTYEELLALPGIGPYTAAAIASIAFGEPAPIVDGNVK 141

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320295463 166 RVLSRFYSLQNPSS-----KLLTQRAKEFLNYDNAFDHNQALLDIGALVCLPKNAKCEICPLKDFCSG--KNEYEKFHV- 237
Cdd:COG1194   142 RVLSRLFAIEGPIGspaakKELWALAEELLPPERPGDFNQALMDLGATVCTPKKPKCLLCPLQDDCAAfaEGRQEELPVk 221

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320295463 238 SKKIQYKNTILKILIVQKNEQFLLIKSQEK-LYFNLYNFLEYKNQKKAKF--------------------IGEFKHSYTK 296
Cdd:COG1194   222 KPKKKKPERYGAALVIRDDGRVLLEKRPPKgLWGGLWEFPEFEWEEAEDPealerwlreelglevewlepLGTVRHVFTH 301

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*....
gi 2320295463 297 YKINAKVYFLKDDDFEDLQAKAFAY---KELEYITLSKLALKAFELFKK 342
Cdd:COG1194   302 FRLHLTVYLARVPAGPPAEPDGGRWvplEELAALPLPAPMRKLLKALLK 350
mutY TIGR01084
A/G-specific adenine glycosylase; This equivalog model identifies mutY members of the ...
 8-291 1.25e-101

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: 300.48  E-value: 1.25e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320295463   8 KIHENILKWYNESGRKSLPWRILHDEYKkyakaddleklknidiayaVYVSEIMLQQTQVKSVLQnYYFQFLAKFPSLKA 87
Cdd:TIGR01084   1 QFSEDLLSWYDKYGRKTLPWRQNKTPYR-------------------VWLSEVMLQQTQVATVIP-YFERFLERFPTVQA 60

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320295463  88 LSMVSEDEVLKAWQGLGYYTRARNIHKCAKICTQEFNAKLPSDINELQKLPGIGEYTAGAIACFGFLQAKSFVDANIKRV 167
Cdd:TIGR01084  61 LANAPQDEVLKLWEGLGYYARARNLHKAAQEVVEEFGGEFPQDFEDLAALPGVGRYTAGAILSFALNKPYPILDGNVKRV 140

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320295463 168 LSRFYSLQNPSSKLLTQR-----AKEFLNYDNAFDHNQALLDIGALVCLPKNAKCEICPLKDFCSGK--NEYEKFHVSKK 240
Cdd:TIGR01084 141 LSRLFAVEGWPGKKKVENrlwtlAESLLPKADPEAFNQALMDLGAMICTRKKPKCDLCPLQDFCLAYqqGTWEEYPVKKP 220

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2320295463 241 IQYK--NTILKILIVQKNEQFLLIK-SQEKLYFNLYNFLEYKNQKK-AKFIGEFK 291
Cdd:TIGR01084 221 KAAPpeRTTYFLVLQNYDGEVLLEQrPEKGLWGGLYCFPQFEDEDSlAFLLAQRG 275
PRK13910 PRK13910
DNA glycosylase MutY; Provisional
 61-344 1.41e-69

DNA glycosylase MutY; Provisional


Pssm-ID: 172427 [Multi-domain]  Cd Length: 289  Bit Score: 219.12  E-value: 1.41e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320295463  61 MLQQTQVKSVLQNYYFQFLAKFPSLKALSMVSEDEVLKAWQGLGYYTRARNIHKCAKICTQEFNAKLPSDINELQKLPGI 140
Cdd:PRK13910    1 MSQQTQINTVVERFYSPFLEAFPTLKDLANAPLEEVLLLWRGLGYYSRAKNLKKSAEICVKEHHSQLPNDYQSLLKLPGI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320295463 141 GEYTAGAIACFGFLQAKSFVDANIKRVLSRFYSLQ-NPSSKLLTQRAKEFLNYDNAFDHNQALLDIGALVCLPKnAKCEI 219
Cdd:PRK13910   81 GAYTANAILCFGFREKSACVDANIKRVLLRLFGLDpNIHAKDLQIKANDFLNLNESFNHNQALIDLGALICSPK-PKCAI 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320295463 220 CPLKDFCSGKNEYEKFHVSKKIQYKNTILKILIVQKNEQFLLIKSQEKLYFNLYNFLEYKN--QKKAKFIGEFKHSYTKY 297
Cdd:PRK13910  160 CPLNPYCLGKNNPEKHTLKKKQEIVQEERYLGVVIQNNQIALEKIEQKLYLGMHHFPNLKEnlEYKLPFLGAIKHSHTKF 239

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 2320295463 298 KINAKVYFLKDDDFEDlQAKAFAYKELEYITLSKLALKAFELFKKSD 344
Cdd:PRK13910  240 KLNLNLYLAAIKDLKN-PIRFYSLKDLETLPISSMTLKILNFLKQKN 285
PRK10880 PRK10880
adenine DNA glycosylase;
7-226 3.15e-55

adenine DNA glycosylase;


Pssm-ID: 182805 [Multi-domain]  Cd Length: 350  Bit Score: 184.14  E-value: 3.15e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320295463   7 QKIHENILKWYNESGRKSLPWRilhdeykkyakaddLEKlknidIAYAVYVSEIMLQQTQVKSVLQnyYFQ-FLAKFPSL 85
Cdd:PRK10880    4 SQFSAQVLDWYDKYGRKTLPWQ--------------IDK-----TPYKVWLSEVMLQQTQVATVIP--YFErFMARFPTV 62

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320295463  86 KALSMVSEDEVLKAWQGLGYYTRARNIHKCAKICTQEFNAKLPSDINELQKLPGIGEYTAGAIACFGFLQAKSFVDANIK 165
Cdd:PRK10880   63 TDLANAPLDEVLHLWTGLGYYARARNLHKAAQQVATLHGGEFPETFEEVAALPGVGRSTAGAILSLSLGKHFPILDGNVK 142

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2320295463 166 RVLSRFYSLQN-PSSKLLTQR----AKEFLNYDNAFDHNQALLDIGALVCLPKNAKCEICPLKDFC 226
Cdd:PRK10880  143 RVLARCYAVSGwPGKKEVENRlwqlSEQVTPAVGVERFNQAMMDLGAMVCTRSKPKCELCPLQNGC 208
ENDO3c cd00056
endonuclease III; includes endonuclease III (DNA-(apurinic or apyrimidinic site) lyase), ...
 53-206 5.04e-42

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: 143.54  E-value: 5.04e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320295463  53 YAVYVSEIMLQQTQVKSVLQnYYFQFLAKF-PSLKALSMVSEDEVLKAWQGLGYYTRARNIHKCAKICTQEFN---AKLP 128
Cdd:cd00056     1 FEVLVSEILSQQTTDKAVNK-AYERLFERYgPTPEALAAADEEELRELIRSLGYRRKAKYLKELARAIVEGFGglvLDDP 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2320295463 129 SDINELQKLPGIGEYTAGAIACFGFLQAKSFVDANIKRVLSRFYSLQNPSS-KLLTQRAKEFLNYDNAFDHNQALLDIG 206
Cdd:cd00056    80 DAREELLALPGVGRKTANVVLLFALGPDAFPVDTHVRRVLKRLGLIPKKKTpEELEELLEELLPKPYWGEANQALMDLG 158
ENDO3c smart00478
endonuclease III; includes endonuclease III (DNA-(apurinic or apyrimidinic site) lyase), ...
 61-208 2.71e-33

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: 120.45  E-value: 2.71e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320295463   61 MLQQTQVKSVlQNYYFQFLAKFPSLKALSMVSEDEVLKAWQGLG-YYTRARNIHKCAKICTQEFNAKLPSDINELQKLPG 139
Cdd:smart00478   1 LSQQTTDERV-NKATERLFEKFPTPEDLAAADEEELEELIRGLGfYRRKARYLIELARILVEEYGGEVPDDREELLKLPG 79

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320295463  140 IGEYTAGAIACFGFLQAKSFVDANIKRVLSRFYSLQNPSSKLLTQR-AKEFLNYDNAFDHNQALLDIGAL 208
Cdd:smart00478  80 VGRKTANAVLSFALGKPFIPVDTHVLRIAKRLGLVDKKSTPEEVEKlLEKLLPEEDWRELNLLLIDFGRT 149
HhH-GPD pfam00730
HhH-GPD superfamily base excision DNA repair protein; This family contains a diverse range of ...
 57-191 9.72e-30

HhH-GPD superfamily base excision DNA repair protein; This family contains a diverse range of structurally related DNA repair proteins. The superfamily is called the HhH-GPD family after its hallmark Helix-hairpin-helix and Gly/Pro rich loop followed by a conserved aspartate. This includes endonuclease III, EC:4.2.99.18 and MutY an A/G-specific adenine glycosylase, both have a C terminal 4Fe-4S cluster. The family also includes 8-oxoguanine DNA glycosylases. The methyl-CPG binding protein MBD4 also contains a related domain that is a thymine DNA glycosylase. The family also includes DNA-3-methyladenine glycosylase II EC:3.2.2.21 and other members of the AlkA family.


Pssm-ID: 425841 [Multi-domain]  Cd Length: 141  Bit Score: 110.84  E-value: 9.72e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320295463  57 VSEIMLQQTQVKSVLQnYYFQFLAK-FPSLKALSMVSEDEVLKAWQGLGYYTR-ARNIHKCAKICTQEFNAKLPSDINEL 134
Cdd:pfam00730   1 VSAILSQQTSDKAVNK-ITERLFEKfFPTPEDLADADEEELRELIRGLGFYRRkAKYLKELARILVEGYGGEVPLDEEEL 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2320295463 135 QK-LPGIGEYTAGAIACFGFLQAKSF--VDANIKRVLSRFYSL-QNPSSKLLTQRAKEFLN 191
Cdd:pfam00730  80 EAlLKGVGRWTAEAVLIFALGRPDPLpvVDTHVRRVLKRLGLIkEKPTPKEVERELEELWP 140
Nth COG0177
Endonuclease III [Replication, recombination and repair];
57-226 4.47e-23

Endonuclease III [Replication, recombination and repair];


Pssm-ID: 439947 [Multi-domain]  Cd Length: 198  Bit Score: 94.78  E-value: 4.47e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320295463  57 VSEIMLQQTQVKSVLQNYyFQFLAKFPSLKALSMVSEDEVLKAWQGLGYY-TRARNIHKCAKICTQEFNAKLPSDINELQ 135
Cdd:COG0177    25 VATILSAQTTDERVNKAT-PRLFARYPTPEALAAADLEELEELIRPIGLYrNKAKNIIALARILVEKYGGEVPETREELE 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320295463 136 KLPGIGEYTAGAIACFGFLQAkSF-VDANIKRVLSRFySLQNPSSKLLTQRA------KEFLNydnafDHNQALLDIGAL 208
Cdd:COG0177   104 SLPGVGRKTANVVLNFAFGKP-AIaVDTHVHRVSNRL-GLVPGKDPEEVEKDlmklipKEYWG-----DLHHLLILHGRY 176

                         170
                  ....*....|....*...
gi 2320295463 209 VCLPKNAKCEICPLKDFC 226
Cdd:COG0177   177 ICKARKPKCEECPLADLC 194
HP0602 COG2231
3-Methyladenine DNA glycosylase, HhH-GPD/Endo3 superfamily [Replication, recombination and ...
 84-226 1.65e-08

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


Pssm-ID: 441832 [Multi-domain]  Cd Length: 220  Bit Score: 54.08  E-value: 1.65e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320295463  84 SLKALSMVSEDEVLKAWQGLGYYTR-ARNIHKCAKICTQEFN------AKLPSDI--NELQKLPGIGEYTAGAIACFGFL 154
Cdd:COG2231    61 DPEALAALDPEELAELIRPSGFYNQkAKRLKNLARWLVERYGggleklKALPTEElrEELLSLKGIGPETADSILLYAFN 140

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2320295463 155 QaKSFV-DANIKRVLSRFYSLQNPSSKlltQRAKEFLNYDNAFDHNQ-----ALLD-IGALVCLPKnAKCEICPLKDFC 226
Cdd:COG2231   141 R-PVFVvDAYTRRIFSRLGLIEEDASY---DELQRLFEENLPPDVALynefhALIVeHGKEYCKKK-PKCEECPLRDLC 214
AlkA COG0122
3-methyladenine DNA glycosylase/8-oxoguanine DNA glycosylase [Replication, recombination and ...
 82-189 7.25e-08

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


Pssm-ID: 439892 [Multi-domain]  Cd Length: 255  Bit Score: 52.58  E-value: 7.25e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320295463  82 FPSLKALSMVSEDEVLKAwqGLGYYtRARNIHKCAKICTQ-----EFNAKLPSD--INELQKLPGIGEYTAGAIA--CFG 152
Cdd:COG0122   127 FPTPEALAAASEEELRAC--GLSRR-KARYLRALARAVADgeldlEALAGLDDEeaIARLTALPGIGPWTAEMVLlfALG 203

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2320295463 153 FLQAKSFVDANIKRVLSRFYSL-QNPSSKLLTQRAKEF 189
Cdd:COG0122   204 RPDAFPAGDLGLRRALGRLYGLgERPTPKELRELAEPW 241
PRK10702 PRK10702
endonuclease III; Provisional
 105-231 2.77e-07

endonuclease III; Provisional


Pssm-ID: 182661 [Multi-domain]  Cd Length: 211  Bit Score: 50.40  E-value: 2.77e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320295463 105 YYTRARNIHKCAKICTQEFNAKLPSDINELQKLPGIGEYTAGAIACFGFLQAKSFVDANIKRVLSRF-----YSLQNPSS 179
Cdd:PRK10702   82 YNSKAENVIKTCRILLEQHNGEVPEDRAALEALPGVGRKTANVVLNTAFGWPTIAVDTHIFRVCNRTqfapgKNVEQVEE 161

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2320295463 180 KLLTQRAKEFlnydnAFDHNQALLDIGALVCLPKNAKCEICPLKDFCSGKNE 231
Cdd:PRK10702  162 KLLKVVPAEF-----KVDCHHWLILHGRYTCIARKPRCGSCIIEDLCEYKEK 208
HHH pfam00633
Helix-hairpin-helix motif; The helix-hairpin-helix DNA-binding motif is found to be duplicated ...
 122-151 5.16e-06

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: 42.40  E-value: 5.16e-06
                          10        20        30
                  ....*....|....*....|....*....|
gi 2320295463 122 EFNAKLPSDINELQKLPGIGEYTAGAIACF 151
Cdd:pfam00633   1 SLEGLIPASVEELLALPGVGPKTAEAILSY 30
FES smart00525
iron-sulpphur binding domain in DNA-(apurinic or apyrimidinic site) lyase (subfamily of ENDO3); ...
 209-229 1.92e-04

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


Pssm-ID: 197771 [Multi-domain]  Cd Length: 21  Bit Score: 37.92  E-value: 1.92e-04
                           10        20
                   ....*....|....*....|.
gi 2320295463  209 VCLPKNAKCEICPLKDFCSGK 229
Cdd:smart00525   1 ICTARKPRCDECPLKDLCPAY 21
EndIII_4Fe-2S pfam10576
Iron-sulfur binding domain of endonuclease III; Escherichia coli endonuclease III (EC 4.2.99. ...
 210-226 6.27e-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: 6.27e-04
                          10
                  ....*....|....*..
gi 2320295463 210 CLPKNAKCEICPLKDFC 226
Cdd:pfam10576   1 CTARKPKCEECPLADLC 17
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH