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Conserved domains on  [gi|490367712|ref|WP_004247375|]
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MULTISPECIES: A/G-specific adenine glycosylase [Proteus]

Protein Classification

A/G-specific adenine glycosylase( domain architecture ID 11485057)

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
PRK10880 PRK10880
adenine DNA glycosylase;
2-346 0e+00

adenine DNA glycosylase;


:

Pssm-ID: 182805 [Multi-domain]  Cd Length: 350  Bit Score: 755.01  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367712   2 MEAQQFSQVVLDWYHKYGRKTLPWQQEKTPYHVWLSEVMLQQTQVATVIPYFERFIARFPNVSALAKAPLDEVLHLWTGL 81
Cdd:PRK10880   1 MQASQFSAQVLDWYDKYGRKTLPWQIDKTPYKVWLSEVMLQQTQVATVIPYFERFMARFPTVTDLANAPLDEVLHLWTGL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367712  82 GYYARARNLHKAAQHIVDKHQGQFPDTFEDVCALPGVGRSTAGAILSLSLKKPYPILDGNVKRVLARCYAVEGWPGKKEV 161
Cdd:PRK10880  81 GYYARARNLHKAAQQVATLHGGEFPETFEEVAALPGVGRSTAGAILSLSLGKHFPILDGNVKRVLARCYAVSGWPGKKEV 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367712 162 ENKLWEISEQVTPTKGVEYFNQAMMDLGAMVCTRTKPKCELCPLNTGCIAYAHHSWADYPGKKPKKAIPEKTTYFLILQY 241
Cdd:PRK10880 161 ENRLWQLSEQVTPAVGVERFNQAMMDLGAMVCTRSKPKCELCPLQNGCIAYANHSWALYPGKKPKQTLPERTGYFLLLQH 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367712 242 DNLVWLDKRPPAGIWGGLFAFPQFETKMLLEQWLTEHGLENNKTEQLISFRHTFSHFHLDIVPICVKLSTFTSLMEAQQG 321
Cdd:PRK10880 241 GDEVWLEQRPPSGLWGGLFCFPQFADEEELRQWLAQRGIAADNLTQLTAFRHTFSHFHLDIVPMWLPVSSFTGCMDEGNG 320
                        330       340
                 ....*....|....*....|....*
gi 490367712 322 LWYNLQTPASVGLAAPVENLLRQLA 346
Cdd:PRK10880 321 LWYNLAQPPSVGLAAPVERLLQQLR 345
 
Name Accession Description Interval E-value
PRK10880 PRK10880
adenine DNA glycosylase;
2-346 0e+00

adenine DNA glycosylase;


Pssm-ID: 182805 [Multi-domain]  Cd Length: 350  Bit Score: 755.01  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367712   2 MEAQQFSQVVLDWYHKYGRKTLPWQQEKTPYHVWLSEVMLQQTQVATVIPYFERFIARFPNVSALAKAPLDEVLHLWTGL 81
Cdd:PRK10880   1 MQASQFSAQVLDWYDKYGRKTLPWQIDKTPYKVWLSEVMLQQTQVATVIPYFERFMARFPTVTDLANAPLDEVLHLWTGL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367712  82 GYYARARNLHKAAQHIVDKHQGQFPDTFEDVCALPGVGRSTAGAILSLSLKKPYPILDGNVKRVLARCYAVEGWPGKKEV 161
Cdd:PRK10880  81 GYYARARNLHKAAQQVATLHGGEFPETFEEVAALPGVGRSTAGAILSLSLGKHFPILDGNVKRVLARCYAVSGWPGKKEV 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367712 162 ENKLWEISEQVTPTKGVEYFNQAMMDLGAMVCTRTKPKCELCPLNTGCIAYAHHSWADYPGKKPKKAIPEKTTYFLILQY 241
Cdd:PRK10880 161 ENRLWQLSEQVTPAVGVERFNQAMMDLGAMVCTRSKPKCELCPLQNGCIAYANHSWALYPGKKPKQTLPERTGYFLLLQH 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367712 242 DNLVWLDKRPPAGIWGGLFAFPQFETKMLLEQWLTEHGLENNKTEQLISFRHTFSHFHLDIVPICVKLSTFTSLMEAQQG 321
Cdd:PRK10880 241 GDEVWLEQRPPSGLWGGLFCFPQFADEEELRQWLAQRGIAADNLTQLTAFRHTFSHFHLDIVPMWLPVSSFTGCMDEGNG 320
                        330       340
                 ....*....|....*....|....*
gi 490367712 322 LWYNLQTPASVGLAAPVENLLRQLA 346
Cdd:PRK10880 321 LWYNLAQPPSVGLAAPVERLLQQLR 345
MutY COG1194
Adenine-specific DNA glycosylase, acts on AG and A-oxoG pairs [Replication, recombination and ...
2-346 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: 563.22  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367712   2 MEAQQFSQVVLDWYHKYGRkTLPWQQEKTPYHVWLSEVMLQQTQVATVIPYFERFIARFPNVSALAKAPLDEVLHLWTGL 81
Cdd:COG1194    1 MDMASFAKRLLAWYDRHGR-DLPWRQTRDPYRVWLSEIMLQQTQVATVIPYYERFLERFPTVEALAAAPEDEVLKLWEGL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367712  82 GYYARARNLHKAAQHIVDKHQGQFPDTFEDVCALPGVGRSTAGAILSLSLKKPYPILDGNVKRVLARCYAVEGWPGKKEV 161
Cdd:COG1194   80 GYYSRARNLHKAAQQVVEEHGGVFPDTYEELLALPGIGPYTAAAIASIAFGEPAPIVDGNVKRVLSRLFAIEGPIGSPAA 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367712 162 ENKLWEISEQVTPTKGVEYFNQAMMDLGAMVCTRTKPKCELCPLNTGCIAYAHHSWADYPGKKPKKAIPEKTTYFLILQY 241
Cdd:COG1194  160 KKELWALAEELLPPERPGDFNQALMDLGATVCTPKKPKCLLCPLQDDCAAFAEGRQEELPVKKPKKKKPERYGAALVIRD 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367712 242 DNLVWLDKRPPAGIWGGLFAFPQFETK-----MLLEQWLTEH-GLENNKTEQLISFRHTFSHFHLDIVPICVKLSTFTSL 315
Cdd:COG1194  240 DGRVLLEKRPPKGLWGGLWEFPEFEWEeaedpEALERWLREElGLEVEWLEPLGTVRHVFTHFRLHLTVYLARVPAGPPA 319
                        330       340       350
                 ....*....|....*....|....*....|.
gi 490367712 316 mEAQQGLWYNLQTPASVGLAAPVENLLRQLA 346
Cdd:COG1194  320 -EPDGGRWVPLEELAALPLPAPMRKLLKALL 349
mutY TIGR01084
A/G-specific adenine glycosylase; This equivalog model identifies mutY members of the ...
6-279 9.28e-173

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: 480.75  E-value: 9.28e-173
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367712    6 QFSQVVLDWYHKYGRKTLPWQQEKTPYHVWLSEVMLQQTQVATVIPYFERFIARFPNVSALAKAPLDEVLHLWTGLGYYA 85
Cdd:TIGR01084   1 QFSEDLLSWYDKYGRKTLPWRQNKTPYRVWLSEVMLQQTQVATVIPYFERFLERFPTVQALANAPQDEVLKLWEGLGYYA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367712   86 RARNLHKAAQHIVDKHQGQFPDTFEDVCALPGVGRSTAGAILSLSLKKPYPILDGNVKRVLARCYAVEGWPGKKEVENKL 165
Cdd:TIGR01084  81 RARNLHKAAQEVVEEFGGEFPQDFEDLAALPGVGRYTAGAILSFALNKPYPILDGNVKRVLSRLFAVEGWPGKKKVENRL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367712  166 WEISEQVTPTKGVEYFNQAMMDLGAMVCTRTKPKCELCPLNTGCIAYAHHSWADYPGKKPKKAIPEKTTYFLILQ-YDNL 244
Cdd:TIGR01084 161 WTLAESLLPKADPEAFNQALMDLGAMICTRKKPKCDLCPLQDFCLAYQQGTWEEYPVKKPKAAPPERTTYFLVLQnYDGE 240
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 490367712  245 VWLDKRPPAGIWGGLFAFPQFETKMLLEQWLTEHG 279
Cdd:TIGR01084 241 VLLEQRPEKGLWGGLYCFPQFEDEDSLAFLLAQRG 275
ENDO3c cd00056
endonuclease III; includes endonuclease III (DNA-(apurinic or apyrimidinic site) lyase), ...
32-189 2.91e-55

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: 177.82  E-value: 2.91e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367712  32 YHVWLSEVMLQQTQVATVIPYFERFIARF-PNVSALAKAPLDEVLHLWTGLGYYARARNLHKAAQHIVDKHQG---QFPD 107
Cdd:cd00056    1 FEVLVSEILSQQTTDKAVNKAYERLFERYgPTPEALAAADEEELRELIRSLGYRRKAKYLKELARAIVEGFGGlvlDDPD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367712 108 TFEDVCALPGVGRSTAGAILSLSLKKPYPILDGNVKRVLARCyaveGWPGKKEVENKLWEISEQVTPTKGVEYFNQAMMD 187
Cdd:cd00056   81 AREELLALPGVGRKTANVVLLFALGPDAFPVDTHVRRVLKRL----GLIPKKKTPEELEELLEELLPKPYWGEANQALMD 156

                 ..
gi 490367712 188 LG 189
Cdd:cd00056  157 LG 158
ENDO3c smart00478
endonuclease III; includes endonuclease III (DNA-(apurinic or apyrimidinic site) lyase), ...
40-191 1.53e-48

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: 160.12  E-value: 1.53e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367712    40 MLQQTQVATVIPYFERFIARFPNVSALAKAPLDEVLHLWTGLG-YYARARNLHKAAQHIVDKHQGQFPDTFEDVCALPGV 118
Cdd:smart00478   1 LSQQTTDERVNKATERLFEKFPTPEDLAAADEEELEELIRGLGfYRRKARYLIELARILVEEYGGEVPDDREELLKLPGV 80
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490367712   119 GRSTAGAILSLSLKKPYPILDGNVKRVLARCYavegWPGKKEVENKLWEISEQVTPTKGVEYFNQAMMDLGAM 191
Cdd:smart00478  81 GRKTANAVLSFALGKPFIPVDTHVLRIAKRLG----LVDKKSTPEEVEKLLEKLLPEEDWRELNLLLIDFGRT 149
HhH-GPD pfam00730
HhH-GPD superfamily base excision DNA repair protein; This family contains a diverse range of ...
36-171 1.88e-43

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: 146.66  E-value: 1.88e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367712   36 LSEVMLQQTQVATVIPYFERFIAR-FPNVSALAKAPLDEVLHLWTGLGYYAR-ARNLHKAAQHIVDKHQGQFPDTF-EDV 112
Cdd:pfam00730   1 VSAILSQQTSDKAVNKITERLFEKfFPTPEDLADADEEELRELIRGLGFYRRkAKYLKELARILVEGYGGEVPLDEeELE 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490367712  113 CALPGVGRSTAGAILSLSL--KKPYPILDGNVKRVLARCYAVEGWPGKKEVENKLWEISEQ 171
Cdd:pfam00730  81 ALLKGVGRWTAEAVLIFALgrPDPLPVVDTHVRRVLKRLGLIKEKPTPKEVERELEELWPP 141
 
Name Accession Description Interval E-value
PRK10880 PRK10880
adenine DNA glycosylase;
2-346 0e+00

adenine DNA glycosylase;


Pssm-ID: 182805 [Multi-domain]  Cd Length: 350  Bit Score: 755.01  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367712   2 MEAQQFSQVVLDWYHKYGRKTLPWQQEKTPYHVWLSEVMLQQTQVATVIPYFERFIARFPNVSALAKAPLDEVLHLWTGL 81
Cdd:PRK10880   1 MQASQFSAQVLDWYDKYGRKTLPWQIDKTPYKVWLSEVMLQQTQVATVIPYFERFMARFPTVTDLANAPLDEVLHLWTGL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367712  82 GYYARARNLHKAAQHIVDKHQGQFPDTFEDVCALPGVGRSTAGAILSLSLKKPYPILDGNVKRVLARCYAVEGWPGKKEV 161
Cdd:PRK10880  81 GYYARARNLHKAAQQVATLHGGEFPETFEEVAALPGVGRSTAGAILSLSLGKHFPILDGNVKRVLARCYAVSGWPGKKEV 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367712 162 ENKLWEISEQVTPTKGVEYFNQAMMDLGAMVCTRTKPKCELCPLNTGCIAYAHHSWADYPGKKPKKAIPEKTTYFLILQY 241
Cdd:PRK10880 161 ENRLWQLSEQVTPAVGVERFNQAMMDLGAMVCTRSKPKCELCPLQNGCIAYANHSWALYPGKKPKQTLPERTGYFLLLQH 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367712 242 DNLVWLDKRPPAGIWGGLFAFPQFETKMLLEQWLTEHGLENNKTEQLISFRHTFSHFHLDIVPICVKLSTFTSLMEAQQG 321
Cdd:PRK10880 241 GDEVWLEQRPPSGLWGGLFCFPQFADEEELRQWLAQRGIAADNLTQLTAFRHTFSHFHLDIVPMWLPVSSFTGCMDEGNG 320
                        330       340
                 ....*....|....*....|....*
gi 490367712 322 LWYNLQTPASVGLAAPVENLLRQLA 346
Cdd:PRK10880 321 LWYNLAQPPSVGLAAPVERLLQQLR 345
MutY COG1194
Adenine-specific DNA glycosylase, acts on AG and A-oxoG pairs [Replication, recombination and ...
2-346 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: 563.22  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367712   2 MEAQQFSQVVLDWYHKYGRkTLPWQQEKTPYHVWLSEVMLQQTQVATVIPYFERFIARFPNVSALAKAPLDEVLHLWTGL 81
Cdd:COG1194    1 MDMASFAKRLLAWYDRHGR-DLPWRQTRDPYRVWLSEIMLQQTQVATVIPYYERFLERFPTVEALAAAPEDEVLKLWEGL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367712  82 GYYARARNLHKAAQHIVDKHQGQFPDTFEDVCALPGVGRSTAGAILSLSLKKPYPILDGNVKRVLARCYAVEGWPGKKEV 161
Cdd:COG1194   80 GYYSRARNLHKAAQQVVEEHGGVFPDTYEELLALPGIGPYTAAAIASIAFGEPAPIVDGNVKRVLSRLFAIEGPIGSPAA 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367712 162 ENKLWEISEQVTPTKGVEYFNQAMMDLGAMVCTRTKPKCELCPLNTGCIAYAHHSWADYPGKKPKKAIPEKTTYFLILQY 241
Cdd:COG1194  160 KKELWALAEELLPPERPGDFNQALMDLGATVCTPKKPKCLLCPLQDDCAAFAEGRQEELPVKKPKKKKPERYGAALVIRD 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367712 242 DNLVWLDKRPPAGIWGGLFAFPQFETK-----MLLEQWLTEH-GLENNKTEQLISFRHTFSHFHLDIVPICVKLSTFTSL 315
Cdd:COG1194  240 DGRVLLEKRPPKGLWGGLWEFPEFEWEeaedpEALERWLREElGLEVEWLEPLGTVRHVFTHFRLHLTVYLARVPAGPPA 319
                        330       340       350
                 ....*....|....*....|....*....|.
gi 490367712 316 mEAQQGLWYNLQTPASVGLAAPVENLLRQLA 346
Cdd:COG1194  320 -EPDGGRWVPLEELAALPLPAPMRKLLKALL 349
mutY TIGR01084
A/G-specific adenine glycosylase; This equivalog model identifies mutY members of the ...
6-279 9.28e-173

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: 480.75  E-value: 9.28e-173
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367712    6 QFSQVVLDWYHKYGRKTLPWQQEKTPYHVWLSEVMLQQTQVATVIPYFERFIARFPNVSALAKAPLDEVLHLWTGLGYYA 85
Cdd:TIGR01084   1 QFSEDLLSWYDKYGRKTLPWRQNKTPYRVWLSEVMLQQTQVATVIPYFERFLERFPTVQALANAPQDEVLKLWEGLGYYA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367712   86 RARNLHKAAQHIVDKHQGQFPDTFEDVCALPGVGRSTAGAILSLSLKKPYPILDGNVKRVLARCYAVEGWPGKKEVENKL 165
Cdd:TIGR01084  81 RARNLHKAAQEVVEEFGGEFPQDFEDLAALPGVGRYTAGAILSFALNKPYPILDGNVKRVLSRLFAVEGWPGKKKVENRL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367712  166 WEISEQVTPTKGVEYFNQAMMDLGAMVCTRTKPKCELCPLNTGCIAYAHHSWADYPGKKPKKAIPEKTTYFLILQ-YDNL 244
Cdd:TIGR01084 161 WTLAESLLPKADPEAFNQALMDLGAMICTRKKPKCDLCPLQDFCLAYQQGTWEEYPVKKPKAAPPERTTYFLVLQnYDGE 240
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 490367712  245 VWLDKRPPAGIWGGLFAFPQFETKMLLEQWLTEHG 279
Cdd:TIGR01084 241 VLLEQRPEKGLWGGLYCFPQFEDEDSLAFLLAQRG 275
ENDO3c cd00056
endonuclease III; includes endonuclease III (DNA-(apurinic or apyrimidinic site) lyase), ...
32-189 2.91e-55

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: 177.82  E-value: 2.91e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367712  32 YHVWLSEVMLQQTQVATVIPYFERFIARF-PNVSALAKAPLDEVLHLWTGLGYYARARNLHKAAQHIVDKHQG---QFPD 107
Cdd:cd00056    1 FEVLVSEILSQQTTDKAVNKAYERLFERYgPTPEALAAADEEELRELIRSLGYRRKAKYLKELARAIVEGFGGlvlDDPD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367712 108 TFEDVCALPGVGRSTAGAILSLSLKKPYPILDGNVKRVLARCyaveGWPGKKEVENKLWEISEQVTPTKGVEYFNQAMMD 187
Cdd:cd00056   81 AREELLALPGVGRKTANVVLLFALGPDAFPVDTHVRRVLKRL----GLIPKKKTPEELEELLEELLPKPYWGEANQALMD 156

                 ..
gi 490367712 188 LG 189
Cdd:cd00056  157 LG 158
ENDO3c smart00478
endonuclease III; includes endonuclease III (DNA-(apurinic or apyrimidinic site) lyase), ...
40-191 1.53e-48

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: 160.12  E-value: 1.53e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367712    40 MLQQTQVATVIPYFERFIARFPNVSALAKAPLDEVLHLWTGLG-YYARARNLHKAAQHIVDKHQGQFPDTFEDVCALPGV 118
Cdd:smart00478   1 LSQQTTDERVNKATERLFEKFPTPEDLAAADEEELEELIRGLGfYRRKARYLIELARILVEEYGGEVPDDREELLKLPGV 80
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490367712   119 GRSTAGAILSLSLKKPYPILDGNVKRVLARCYavegWPGKKEVENKLWEISEQVTPTKGVEYFNQAMMDLGAM 191
Cdd:smart00478  81 GRKTANAVLSFALGKPFIPVDTHVLRIAKRLG----LVDKKSTPEEVEKLLEKLLPEEDWRELNLLLIDFGRT 149
HhH-GPD pfam00730
HhH-GPD superfamily base excision DNA repair protein; This family contains a diverse range of ...
36-171 1.88e-43

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: 146.66  E-value: 1.88e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367712   36 LSEVMLQQTQVATVIPYFERFIAR-FPNVSALAKAPLDEVLHLWTGLGYYAR-ARNLHKAAQHIVDKHQGQFPDTF-EDV 112
Cdd:pfam00730   1 VSAILSQQTSDKAVNKITERLFEKfFPTPEDLADADEEELRELIRGLGFYRRkAKYLKELARILVEGYGGEVPLDEeELE 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490367712  113 CALPGVGRSTAGAILSLSL--KKPYPILDGNVKRVLARCYAVEGWPGKKEVENKLWEISEQ 171
Cdd:pfam00730  81 ALLKGVGRWTAEAVLIFALgrPDPLPVVDTHVRRVLKRLGLIKEKPTPKEVERELEELWPP 141
PRK13910 PRK13910
DNA glycosylase MutY; Provisional
40-269 1.26e-37

DNA glycosylase MutY; Provisional


Pssm-ID: 172427 [Multi-domain]  Cd Length: 289  Bit Score: 136.31  E-value: 1.26e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367712  40 MLQQTQVATVIP-YFERFIARFPNVSALAKAPLDEVLHLWTGLGYYARARNLHKAAQHIVDKHQGQFPDTFEDVCALPGV 118
Cdd:PRK13910   1 MSQQTQINTVVErFYSPFLEAFPTLKDLANAPLEEVLLLWRGLGYYSRAKNLKKSAEICVKEHHSQLPNDYQSLLKLPGI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367712 119 GRSTAGAILSLSLKKPYPILDGNVKRVLARCYAVEGWPGKKEVE---NKLWEISEQVTptkgveyFNQAMMDLGAMVCTr 195
Cdd:PRK13910  81 GAYTANAILCFGFREKSACVDANIKRVLLRLFGLDPNIHAKDLQikaNDFLNLNESFN-------HNQALIDLGALICS- 152
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490367712 196 TKPKCELCPLNTGCIAYAHhswADYPGKKPKKAIPEKTTYFLILQYDNLVWLDKRPPAgIWGGLFAFPQFETKM 269
Cdd:PRK13910 153 PKPKCAICPLNPYCLGKNN---PEKHTLKKKQEIVQEERYLGVVIQNNQIALEKIEQK-LYLGMHHFPNLKENL 222
Nth COG0177
Endonuclease III [Replication, recombination and repair];
29-209 1.18e-34

Endonuclease III [Replication, recombination and repair];


Pssm-ID: 439947 [Multi-domain]  Cd Length: 198  Bit Score: 125.59  E-value: 1.18e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367712  29 KTPYHVWLSEVMLQQTQVATVIPYFERFIARFPNVSALAKAPLDEVLHLWTGLGYY-ARARNLHKAAQHIVDKHQGQFPD 107
Cdd:COG0177   18 RDPFELLVATILSAQTTDERVNKATPRLFARYPTPEALAAADLEELEELIRPIGLYrNKAKNIIALARILVEKYGGEVPE 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367712 108 TFEDVCALPGVGRSTAGAILSLSLKKPYPILDGNVKRVLARCyaveGW-PGK--KEVENKLweisEQVTPTKGVEYFNQA 184
Cdd:COG0177   98 TREELESLPGVGRKTANVVLNFAFGKPAIAVDTHVHRVSNRL----GLvPGKdpEEVEKDL----MKLIPKEYWGDLHHL 169
                        170       180
                 ....*....|....*....|....*
gi 490367712 185 MMDLGAMVCTRTKPKCELCPLNTGC 209
Cdd:COG0177  170 LILHGRYICKARKPKCEECPLADLC 194
NUDIX_DNA_Glycosylase_C-MutY cd03431
C-terminal domain of DNA glycosylase; DNA glycosylase (MutY in bacteria and hMYH in humans) is ...
229-342 7.38e-30

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: 110.47  E-value: 7.38e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367712 229 IPEKTTYFLILQYDNLVWLDKRPPAGIWGGLFAFPQFETKMLLEQWLTEHGLE----NNKTEQLISFRHTFSHFHLDIVP 304
Cdd:cd03431    1 VPERYFTVLVLRDGGRVLLEKRPEKGLLAGLWEFPLVETEEEEEEAEALLGLLaeelLLILEPLGEVKHVFSHFRLHITV 80
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 490367712 305 ICVKLSTfTSLMEAQQGLWYNLQTPASVGLAAPVENLL 342
Cdd:cd03431   81 YLVELPE-APPAAPDEGRWVDLEELDEYALPAPMRKLL 117
nth TIGR01083
endonuclease III; This equivalog model identifes nth members of the pfam00730 superfamily ...
29-200 4.06e-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: 89.36  E-value: 4.06e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367712   29 KTPYHVWLSEVMLQQTQVATVIPYFERFIARFPNVSALAKAPLDEVLHLWTGLGYY-ARARNLHKAAQHIVDKHQGQFPD 107
Cdd:TIGR01083  25 NNPFELLVATILSAQATDKRVNKATPKLFEVYPTPQALAQAGLEELEEYIKSIGLYrNKAKNIIELCRKLVERYGGEVPE 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367712  108 TFEDVCALPGVGRSTAGAILSLSLKKPYPILDGNVKRVLARCyaveGW-PGK--KEVENKLWEiseqVTPTKGVEYFNQA 184
Cdd:TIGR01083 105 DREELVKLPGVGRKTANVVLNVAFGIPAIAVDTHVFRVSNRL----GLsKGKdpIKVEEDLMK----LVPREFWVKLHHW 176
                         170
                  ....*....|....*.
gi 490367712  185 MMDLGAMVCTRTKPKC 200
Cdd:TIGR01083 177 LILHGRYTCKARKPLC 192
NUDIX_4 pfam14815
NUDIX domain;
234-344 3.55e-20

NUDIX domain;


Pssm-ID: 464330 [Multi-domain]  Cd Length: 114  Bit Score: 84.67  E-value: 3.55e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367712  234 TYFLILQYDNLVWLDKRPPAGIWGGLFAFPQF--ETKMLLEQWL---TEHGLENNKTEQlISFRHTFSHFHLDI-VPICV 307
Cdd:pfam14815   1 AVLVIRNGDGRVLLRKRPEKGLLGGLWEFPGGkvEPGETLEEALarlEELGIEVEVLEP-GTVKHVFTHFRLTLhVYLVR 79
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 490367712  308 KLSTFTSlmEAQQGLWYNLQTPASVGLAAPVENLLRQ 344
Cdd:pfam14815  80 EVEGEEE--PQQELRWVTPEELDKYALPAAVRKILEA 114
PRK10702 PRK10702
endonuclease III; Provisional
83-209 1.31e-10

endonuclease III; Provisional


Pssm-ID: 182661 [Multi-domain]  Cd Length: 211  Bit Score: 60.42  E-value: 1.31e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367712  83 YYARARNLHKAAQHIVDKHQGQFPDTFEDVCALPGVGRSTAGAILSLSLKKPYPILDGNVKRVlarCYAVEGWPGK--KE 160
Cdd:PRK10702  82 YNSKAENVIKTCRILLEQHNGEVPEDRAALEALPGVGRKTANVVLNTAFGWPTIAVDTHIFRV---CNRTQFAPGKnvEQ 158
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 490367712 161 VENKLWeiseQVTPTKGVEYFNQAMMDLGAMVCTRTKPKCELCPLNTGC 209
Cdd:PRK10702 159 VEEKLL----KVVPAEFKVDCHHWLILHGRYTCIARKPRCGSCIIEDLC 203
HP0602 COG2231
3-Methyladenine DNA glycosylase, HhH-GPD/Endo3 superfamily [Replication, recombination and ...
1-216 1.75e-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: 1.75e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367712   1 MMEAQQFSQVVLDWYHKYGRktLPWQQEKTPYHVWLSEVMLQQTQVATVipyfERFIARFPN-----VSALAKAPLDEVL 75
Cdd:COG2231    1 MNTKEDLLEIYERLLEHYGP--QHWWPAETPFEVIVGAILTQNTSWKNV----EKAIANLKEaglldPEALAALDPEELA 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367712  76 HLWTGLGYYAR-ARNLHKAAQHIVDKHQGQFPDTF--------EDVCALPGVGRSTAGAILSLSLKKPYPILDGNVKRVL 146
Cdd:COG2231   75 ELIRPSGFYNQkAKRLKNLARWLVERYGGGLEKLKalpteelrEELLSLKGIGPETADSILLYAFNRPVFVVDAYTRRIF 154
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490367712 147 ARCYAVEGWPGKKEVENKLweisEQVTPtKGVEYFNQ--AMMD-LGAMVCtRTKPKCELCPLNTGCiAYAHHS 216
Cdd:COG2231  155 SRLGLIEEDASYDELQRLF----EENLP-PDVALYNEfhALIVeHGKEYC-KKKPKCEECPLRDLC-PYGGQE 220
AlkA COG0122
3-methyladenine DNA glycosylase/8-oxoguanine DNA glycosylase [Replication, recombination and ...
48-162 2.53e-07

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


Pssm-ID: 439892 [Multi-domain]  Cd Length: 255  Bit Score: 51.04  E-value: 2.53e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367712  48 TVIPYFERFIARFPNVSALAKAPLDEVLHLwtGLGYYaRARNLHKAAQHIVDK--HQGQFPD-TFEDV----CALPGVGR 120
Cdd:COG0122  115 EPIEGPGGGLYAFPTPEALAAASEEELRAC--GLSRR-KARYLRALARAVADGelDLEALAGlDDEEAiarlTALPGIGP 191
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 490367712 121 STAGAILSLSLKKP--YPILDGNVKRVLARCYAVEGWPGKKEVE 162
Cdd:COG0122  192 WTAEMVLLFALGRPdaFPAGDLGLRRALGRLYGLGERPTPKELR 235
HHH pfam00633
Helix-hairpin-helix motif; The helix-hairpin-helix DNA-binding motif is found to be duplicated ...
100-128 3.54e-07

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: 45.87  E-value: 3.54e-07
                          10        20
                  ....*....|....*....|....*....
gi 490367712  100 KHQGQFPDTFEDVCALPGVGRSTAGAILS 128
Cdd:pfam00633   1 SLEGLIPASVEELLALPGVGPKTAEAILS 29
FES smart00525
iron-sulpphur binding domain in DNA-(apurinic or apyrimidinic site) lyase (subfamily of ENDO3); ...
192-212 8.51e-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: 39.07  E-value: 8.51e-05
                           10        20
                   ....*....|....*....|.
gi 490367712   192 VCTRTKPKCELCPLNTGCIAY 212
Cdd:smart00525   1 ICTARKPRCDECPLKDLCPAY 21
EndIII_4Fe-2S pfam10576
Iron-sulfur binding domain of endonuclease III; Escherichia coli endonuclease III (EC 4.2.99. ...
193-209 1.45e-03

Iron-sulfur binding domain of endonuclease III; Escherichia coli endonuclease III (EC 4.2.99.18) is a DNA repair enzyme that acts both as a DNA N-glycosylase, removing oxidized pyrimidines from DNA, and as an apurinic/apyrimidinic (AP) endonuclease, introducing a single-strand nick at the site from which the damaged base was removed. Endonuclease III is an iron-sulfur protein that binds a single 4Fe-4S cluster. The 4Fe-4S cluster does not seem to be important for catalytic activity, but is probably involved in the proper positioning of the enzyme along the DNA strand. The 4Fe-4S cluster is bound by four cysteines which are all located in a 17 amino acid region at the C-terminal end of endonuclease III. A similar region is also present in the central section of mutY and in the C-terminus of ORF-10 and of the Micro-coccus UV endonuclease.


Pssm-ID: 463153 [Multi-domain]  Cd Length: 17  Bit Score: 35.44  E-value: 1.45e-03
                          10
                  ....*....|....*..
gi 490367712  193 CTRTKPKCELCPLNTGC 209
Cdd:pfam10576   1 CTARKPKCEECPLADLC 17
ogg TIGR00588
8-oxoguanine DNA-glycosylase (ogg); All proteins in this family for which functions are known ...
60-150 8.71e-03

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: 37.58  E-value: 8.71e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367712   60 FPNVSALAKAPLDEVLHLwTGLGYyaRARNLHKAAQHIVDKHQG----------QFPDTFEDVCALPGVGRSTAGAILSL 129
Cdd:TIGR00588 163 FPSLHALTGPEAEAHLRK-LGLGY--RARYIRETARALLEEQGGrawlqqirgaSYEDAREALCELPGVGPKVADCICLM 239
                          90       100
                  ....*....|....*....|...
gi 490367712  130 SLKKP--YPIlDGNVKRVLARCY 150
Cdd:TIGR00588 240 GLDKPqaVPV-DVHVWRIANRDY 261
 
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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