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Conserved domains on  [gi|639187127|ref|WP_024526396|]
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A/G-specific adenine glycosylase [Levilactobacillus brevis]

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 ...
 7-369 4.09e-158

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: 448.05  E-value: 4.09e-158
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639187127   7 ATIREFRQTLLAWYDREGRDLPWRHDQDPYHVWVSEIMLQQTQVQTVIPYYLNFMAMFPTVADLAKAPEEQLLKAWQGLG 86
Cdd:COG1194    1 MDMASFAKRLLAWYDRHGRDLPWRQTRDPYRVWLSEIMLQQTQVATVIPYYERFLERFPTVEALAAAPEDEVLKLWEGLG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639187127  87 YYSRARNLQRAARQLVDDYRGKWPQTAAELLDLTGIGPYTAGAIASIAFGEVVPAVDGNAFRVFSRLLLIDADIAKLQTR 166
Cdd:COG1194   81 YYSRARNLHKAAQQVVEEHGGVFPDTYEELLALPGIGPYTAAAIASIAFGEPAPIVDGNVKRVLSRLFAIEGPIGSPAAK 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639187127 167 KLFEQVIQPIVDPQRPGAFNQAIMDLGSSYMTAKNSDPAHSPVRAFDASYRENCVADFPVKTKAPRPRPVPYYGLIVTSP 246
Cdd:COG1194  161 KELWALAEELLPPERPGDFNQALMDLGATVCTPKKPKCLLCPLQDDCAAFAEGRQEELPVKKPKKKKPERYGAALVIRDD 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639187127 247 AGYLMVQRDATQMLTGYWTFPLIQQADlqdatdqqpatlQTDIAHLEQRFMTDYQLPITLTPLSGqPVSHTYTHQRWQVK 326
Cdd:COG1194  241 GRVLLEKRPPKGLWGGLWEFPEFEWEE------------AEDPEALERWLREELGLEVEWLEPLG-TVRHVFTHFRLHLT 307

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|...
gi 639187127 327 LLVAELSSAADLTFYPGKWVAASTIKTLPLPKVQEKLMTRYQN 369
Cdd:COG1194  308 VYLARVPAGPPAEPDGGRWVPLEELAALPLPAPMRKLLKALLK 350
 
Name Accession Description Interval E-value
MutY COG1194
Adenine-specific DNA glycosylase, acts on AG and A-oxoG pairs [Replication, recombination and ...
 7-369 4.09e-158

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: 448.05  E-value: 4.09e-158
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639187127   7 ATIREFRQTLLAWYDREGRDLPWRHDQDPYHVWVSEIMLQQTQVQTVIPYYLNFMAMFPTVADLAKAPEEQLLKAWQGLG 86
Cdd:COG1194    1 MDMASFAKRLLAWYDRHGRDLPWRQTRDPYRVWLSEIMLQQTQVATVIPYYERFLERFPTVEALAAAPEDEVLKLWEGLG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639187127  87 YYSRARNLQRAARQLVDDYRGKWPQTAAELLDLTGIGPYTAGAIASIAFGEVVPAVDGNAFRVFSRLLLIDADIAKLQTR 166
Cdd:COG1194   81 YYSRARNLHKAAQQVVEEHGGVFPDTYEELLALPGIGPYTAAAIASIAFGEPAPIVDGNVKRVLSRLFAIEGPIGSPAAK 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639187127 167 KLFEQVIQPIVDPQRPGAFNQAIMDLGSSYMTAKNSDPAHSPVRAFDASYRENCVADFPVKTKAPRPRPVPYYGLIVTSP 246
Cdd:COG1194  161 KELWALAEELLPPERPGDFNQALMDLGATVCTPKKPKCLLCPLQDDCAAFAEGRQEELPVKKPKKKKPERYGAALVIRDD 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639187127 247 AGYLMVQRDATQMLTGYWTFPLIQQADlqdatdqqpatlQTDIAHLEQRFMTDYQLPITLTPLSGqPVSHTYTHQRWQVK 326
Cdd:COG1194  241 GRVLLEKRPPKGLWGGLWEFPEFEWEE------------AEDPEALERWLREELGLEVEWLEPLG-TVRHVFTHFRLHLT 307

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|...
gi 639187127 327 LLVAELSSAADLTFYPGKWVAASTIKTLPLPKVQEKLMTRYQN 369
Cdd:COG1194  308 VYLARVPAGPPAEPDGGRWVPLEELAALPLPAPMRKLLKALLK 350
mutY TIGR01084
A/G-specific adenine glycosylase; This equivalog model identifies mutY members of the ...
 11-274 7.40e-102

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: 302.41  E-value: 7.40e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639187127   11 EFRQTLLAWYDREGR-DLPWRHDQDPYHVWVSEIMLQQTQVQTVIPYYLNFMAMFPTVADLAKAPEEQLLKAWQGLGYYS 89
Cdd:TIGR01084   1 QFSEDLLSWYDKYGRkTLPWRQNKTPYRVWLSEVMLQQTQVATVIPYFERFLERFPTVQALANAPQDEVLKLWEGLGYYA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639187127   90 RARNLQRAARQLVDDYRGKWPQTAAELLDLTGIGPYTAGAIASIAFGEVVPAVDGNAFRVFSRLLLIDADIAKLQTRKLF 169
Cdd:TIGR01084  81 RARNLHKAAQEVVEEFGGEFPQDFEDLAALPGVGRYTAGAILSFALNKPYPILDGNVKRVLSRLFAVEGWPGKKKVENRL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639187127  170 EQVIQPIVDPQRPGAFNQAIMDLGSSYMTAKNSDPAHSPVRAFDASYRENCVADFPVKTKAPRPRPVPYYGLIVTSPAG- 248
Cdd:TIGR01084 161 WTLAESLLPKADPEAFNQALMDLGAMICTRKKPKCDLCPLQDFCLAYQQGTWEEYPVKKPKAAPPERTTYFLVLQNYDGe 240

                         250       260
                  ....*....|....*....|....*.
gi 639187127  249 YLMVQRDATQMLTGYWTFPLIQQADL 274
Cdd:TIGR01084 241 VLLEQRPEKGLWGGLYCFPQFEDEDS 266
PRK10880 PRK10880
adenine DNA glycosylase;
11-294 2.35e-66

adenine DNA glycosylase;


Pssm-ID: 182805 [Multi-domain]  Cd Length: 350  Bit Score: 213.80  E-value: 2.35e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639187127  11 EFRQTLLAWYDREGRD-LPWRHDQDPYHVWVSEIMLQQTQVQTVIPYYLNFMAMFPTVADLAKAPEEQLLKAWQGLGYYS 89
Cdd:PRK10880   5 QFSAQVLDWYDKYGRKtLPWQIDKTPYKVWLSEVMLQQTQVATVIPYFERFMARFPTVTDLANAPLDEVLHLWTGLGYYA 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639187127  90 RARNLQRAARQLVDDYRGKWPQTAAELLDLTGIGPYTAGAIASIAFGEVVPAVDGNAFRVFSRLLLIDADIAKLQTRKLF 169
Cdd:PRK10880  85 RARNLHKAAQQVATLHGGEFPETFEEVAALPGVGRSTAGAILSLSLGKHFPILDGNVKRVLARCYAVSGWPGKKEVENRL 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639187127 170 EQVIQPIVDPQRPGAFNQAIMDLGSsyMTAKNSDPAHS--PVRAFDASYRENCVADFP-VKTKAPRPRPVPYYGLIVTSP 246
Cdd:PRK10880 165 WQLSEQVTPAVGVERFNQAMMDLGA--MVCTRSKPKCElcPLQNGCIAYANHSWALYPgKKPKQTLPERTGYFLLLQHGD 242

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 639187127 247 AGYLMvQRDATQMLTGYWTFPliqQADLQDATDQQPATLQTDIAHLEQ 294
Cdd:PRK10880 243 EVWLE-QRPPSGLWGGLFCFP---QFADEEELRQWLAQRGIAADNLTQ 286
ENDO3c cd00056
endonuclease III; includes endonuclease III (DNA-(apurinic or apyrimidinic site) lyase), ...
 36-193 4.49e-52

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: 170.50  E-value: 4.49e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639187127  36 YHVWVSEIMLQQTQVQTVIPYYLNFMAMF-PTVADLAKAPEEQLLKAWQGLGYYSRARNLQRAARQLVDDYRG---KWPQ 111
Cdd:cd00056    1 FEVLVSEILSQQTTDKAVNKAYERLFERYgPTPEALAAADEEELRELIRSLGYRRKAKYLKELARAIVEGFGGlvlDDPD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639187127 112 TAAELLDLTGIGPYTAGAIASIAFGEVVPAVDGNAFRVFSRLLLidadIAKLQTRKLFEQVIQPIVDPQRPGAFNQAIMD 191
Cdd:cd00056   81 AREELLALPGVGRKTANVVLLFALGPDAFPVDTHVRRVLKRLGL----IPKKKTPEELEELLEELLPKPYWGEANQALMD 156


                 ..
gi 639187127 192 LG 193
Cdd:cd00056  157 LG 158
ENDO3c smart00478
endonuclease III; includes endonuclease III (DNA-(apurinic or apyrimidinic site) lyase), ...
 44-193 3.00e-44

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: 150.11  E-value: 3.00e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639187127    44 MLQQTQVQTVIPYYLNFMAMFPTVADLAKAPEEQLLKAWQGLG-YYSRARNLQRAARQLVDDYRGKWPQTAAELLDLTGI 122
Cdd:smart00478   1 LSQQTTDERVNKATERLFEKFPTPEDLAAADEEELEELIRGLGfYRRKARYLIELARILVEEYGGEVPDDREELLKLPGV 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 639187127   123 GPYTAGAIASIAFGEVVPAVDGNAFRVFSRLLLIDADIAKLQTRKLFEQviqpIVDPQRPGAFNQAIMDLG 193
Cdd:smart00478  81 GRKTANAVLSFALGKPFIPVDTHVLRIAKRLGLVDKKSTPEEVEKLLEK----LLPEEDWRELNLLLIDFG 147
HhH-GPD pfam00730
HhH-GPD superfamily base excision DNA repair protein; This family contains a diverse range of ...
 40-175 2.19e-41

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: 142.42  E-value: 2.19e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639187127   40 VSEIMLQQTQVQTVIPYYLNFMA-MFPTVADLAKAPEEQLLKAWQGLGYY-SRARNLQRAARQLVDDYRGKWPQTAAELL 117
Cdd:pfam00730   1 VSAILSQQTSDKAVNKITERLFEkFFPTPEDLADADEEELRELIRGLGFYrRKAKYLKELARILVEGYGGEVPLDEEELE 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 639187127  118 D-LTGIGPYTAGAIASIAFG--EVVPAVDGNAFRVFSRLLLIDADIAKLQTRKLFEQVIQP 175
Cdd:pfam00730  81 AlLKGVGRWTAEAVLIFALGrpDPLPVVDTHVRRVLKRLGLIKEKPTPKEVERELEELWPP 141
 
Name Accession Description Interval E-value
MutY COG1194
Adenine-specific DNA glycosylase, acts on AG and A-oxoG pairs [Replication, recombination and ...
 7-369 4.09e-158

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: 448.05  E-value: 4.09e-158
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639187127   7 ATIREFRQTLLAWYDREGRDLPWRHDQDPYHVWVSEIMLQQTQVQTVIPYYLNFMAMFPTVADLAKAPEEQLLKAWQGLG 86
Cdd:COG1194    1 MDMASFAKRLLAWYDRHGRDLPWRQTRDPYRVWLSEIMLQQTQVATVIPYYERFLERFPTVEALAAAPEDEVLKLWEGLG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639187127  87 YYSRARNLQRAARQLVDDYRGKWPQTAAELLDLTGIGPYTAGAIASIAFGEVVPAVDGNAFRVFSRLLLIDADIAKLQTR 166
Cdd:COG1194   81 YYSRARNLHKAAQQVVEEHGGVFPDTYEELLALPGIGPYTAAAIASIAFGEPAPIVDGNVKRVLSRLFAIEGPIGSPAAK 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639187127 167 KLFEQVIQPIVDPQRPGAFNQAIMDLGSSYMTAKNSDPAHSPVRAFDASYRENCVADFPVKTKAPRPRPVPYYGLIVTSP 246
Cdd:COG1194  161 KELWALAEELLPPERPGDFNQALMDLGATVCTPKKPKCLLCPLQDDCAAFAEGRQEELPVKKPKKKKPERYGAALVIRDD 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639187127 247 AGYLMVQRDATQMLTGYWTFPLIQQADlqdatdqqpatlQTDIAHLEQRFMTDYQLPITLTPLSGqPVSHTYTHQRWQVK 326
Cdd:COG1194  241 GRVLLEKRPPKGLWGGLWEFPEFEWEE------------AEDPEALERWLREELGLEVEWLEPLG-TVRHVFTHFRLHLT 307

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|...
gi 639187127 327 LLVAELSSAADLTFYPGKWVAASTIKTLPLPKVQEKLMTRYQN 369
Cdd:COG1194  308 VYLARVPAGPPAEPDGGRWVPLEELAALPLPAPMRKLLKALLK 350
mutY TIGR01084
A/G-specific adenine glycosylase; This equivalog model identifies mutY members of the ...
 11-274 7.40e-102

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: 302.41  E-value: 7.40e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639187127   11 EFRQTLLAWYDREGR-DLPWRHDQDPYHVWVSEIMLQQTQVQTVIPYYLNFMAMFPTVADLAKAPEEQLLKAWQGLGYYS 89
Cdd:TIGR01084   1 QFSEDLLSWYDKYGRkTLPWRQNKTPYRVWLSEVMLQQTQVATVIPYFERFLERFPTVQALANAPQDEVLKLWEGLGYYA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639187127   90 RARNLQRAARQLVDDYRGKWPQTAAELLDLTGIGPYTAGAIASIAFGEVVPAVDGNAFRVFSRLLLIDADIAKLQTRKLF 169
Cdd:TIGR01084  81 RARNLHKAAQEVVEEFGGEFPQDFEDLAALPGVGRYTAGAILSFALNKPYPILDGNVKRVLSRLFAVEGWPGKKKVENRL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639187127  170 EQVIQPIVDPQRPGAFNQAIMDLGSSYMTAKNSDPAHSPVRAFDASYRENCVADFPVKTKAPRPRPVPYYGLIVTSPAG- 248
Cdd:TIGR01084 161 WTLAESLLPKADPEAFNQALMDLGAMICTRKKPKCDLCPLQDFCLAYQQGTWEEYPVKKPKAAPPERTTYFLVLQNYDGe 240

                         250       260
                  ....*....|....*....|....*.
gi 639187127  249 YLMVQRDATQMLTGYWTFPLIQQADL 274
Cdd:TIGR01084 241 VLLEQRPEKGLWGGLYCFPQFEDEDS 266
PRK10880 PRK10880
adenine DNA glycosylase;
11-294 2.35e-66

adenine DNA glycosylase;


Pssm-ID: 182805 [Multi-domain]  Cd Length: 350  Bit Score: 213.80  E-value: 2.35e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639187127  11 EFRQTLLAWYDREGRD-LPWRHDQDPYHVWVSEIMLQQTQVQTVIPYYLNFMAMFPTVADLAKAPEEQLLKAWQGLGYYS 89
Cdd:PRK10880   5 QFSAQVLDWYDKYGRKtLPWQIDKTPYKVWLSEVMLQQTQVATVIPYFERFMARFPTVTDLANAPLDEVLHLWTGLGYYA 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639187127  90 RARNLQRAARQLVDDYRGKWPQTAAELLDLTGIGPYTAGAIASIAFGEVVPAVDGNAFRVFSRLLLIDADIAKLQTRKLF 169
Cdd:PRK10880  85 RARNLHKAAQQVATLHGGEFPETFEEVAALPGVGRSTAGAILSLSLGKHFPILDGNVKRVLARCYAVSGWPGKKEVENRL 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639187127 170 EQVIQPIVDPQRPGAFNQAIMDLGSsyMTAKNSDPAHS--PVRAFDASYRENCVADFP-VKTKAPRPRPVPYYGLIVTSP 246
Cdd:PRK10880 165 WQLSEQVTPAVGVERFNQAMMDLGA--MVCTRSKPKCElcPLQNGCIAYANHSWALYPgKKPKQTLPERTGYFLLLQHGD 242

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 639187127 247 AGYLMvQRDATQMLTGYWTFPliqQADLQDATDQQPATLQTDIAHLEQ 294
Cdd:PRK10880 243 EVWLE-QRPPSGLWGGLFCFP---QFADEEELRQWLAQRGIAADNLTQ 286
ENDO3c cd00056
endonuclease III; includes endonuclease III (DNA-(apurinic or apyrimidinic site) lyase), ...
 36-193 4.49e-52

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: 170.50  E-value: 4.49e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639187127  36 YHVWVSEIMLQQTQVQTVIPYYLNFMAMF-PTVADLAKAPEEQLLKAWQGLGYYSRARNLQRAARQLVDDYRG---KWPQ 111
Cdd:cd00056    1 FEVLVSEILSQQTTDKAVNKAYERLFERYgPTPEALAAADEEELRELIRSLGYRRKAKYLKELARAIVEGFGGlvlDDPD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639187127 112 TAAELLDLTGIGPYTAGAIASIAFGEVVPAVDGNAFRVFSRLLLidadIAKLQTRKLFEQVIQPIVDPQRPGAFNQAIMD 191
Cdd:cd00056   81 AREELLALPGVGRKTANVVLLFALGPDAFPVDTHVRRVLKRLGL----IPKKKTPEELEELLEELLPKPYWGEANQALMD 156


                 ..
gi 639187127 192 LG 193
Cdd:cd00056  157 LG 158
ENDO3c smart00478
endonuclease III; includes endonuclease III (DNA-(apurinic or apyrimidinic site) lyase), ...
 44-193 3.00e-44

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: 150.11  E-value: 3.00e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639187127    44 MLQQTQVQTVIPYYLNFMAMFPTVADLAKAPEEQLLKAWQGLG-YYSRARNLQRAARQLVDDYRGKWPQTAAELLDLTGI 122
Cdd:smart00478   1 LSQQTTDERVNKATERLFEKFPTPEDLAAADEEELEELIRGLGfYRRKARYLIELARILVEEYGGEVPDDREELLKLPGV 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 639187127   123 GPYTAGAIASIAFGEVVPAVDGNAFRVFSRLLLIDADIAKLQTRKLFEQviqpIVDPQRPGAFNQAIMDLG 193
Cdd:smart00478  81 GRKTANAVLSFALGKPFIPVDTHVLRIAKRLGLVDKKSTPEEVEKLLEK----LLPEEDWRELNLLLIDFG 147
HhH-GPD pfam00730
HhH-GPD superfamily base excision DNA repair protein; This family contains a diverse range of ...
 40-175 2.19e-41

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: 142.42  E-value: 2.19e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639187127   40 VSEIMLQQTQVQTVIPYYLNFMA-MFPTVADLAKAPEEQLLKAWQGLGYY-SRARNLQRAARQLVDDYRGKWPQTAAELL 117
Cdd:pfam00730   1 VSAILSQQTSDKAVNKITERLFEkFFPTPEDLADADEEELRELIRGLGFYrRKAKYLKELARILVEGYGGEVPLDEEELE 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 639187127  118 D-LTGIGPYTAGAIASIAFG--EVVPAVDGNAFRVFSRLLLIDADIAKLQTRKLFEQVIQP 175
Cdd:pfam00730  81 AlLKGVGRWTAEAVLIFALGrpDPLPVVDTHVRRVLKRLGLIKEKPTPKEVERELEELWPP 141
Nth COG0177
Endonuclease III [Replication, recombination and repair];
28-212 1.36e-27

Endonuclease III [Replication, recombination and repair];


Pssm-ID: 439947 [Multi-domain]  Cd Length: 198  Bit Score: 107.49  E-value: 1.36e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639187127  28 PWRHDQDPYHVWVSEIMLQQTQVQTVIPYYLNFMAMFPTVADLAKAPEEQLLKAWQGLGYY-SRARNLQRAARQLVDDYR 106
Cdd:COG0177   13 TELDYRDPFELLVATILSAQTTDERVNKATPRLFARYPTPEALAAADLEELEELIRPIGLYrNKAKNIIALARILVEKYG 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639187127 107 GKWPQTAAELLDLTGIGPYTAGAIASIAFGEVVPAVDGNAFRVFSRLLLIDADIAkLQTrklfEQVIQPIVDPQRPGAFN 186
Cdd:COG0177   93 GEVPETREELESLPGVGRKTANVVLNFAFGKPAIAVDTHVHRVSNRLGLVPGKDP-EEV----EKDLMKLIPKEYWGDLH 167

                        170       180
                 ....*....|....*....|....*.
gi 639187127 187 QAIMDLGSSYMTAKNSDPAHSPVRAF 212
Cdd:COG0177  168 HLLILHGRYICKARKPKCEECPLADL 193
PRK13910 PRK13910
DNA glycosylase MutY; Provisional
 44-194 9.78e-26

DNA glycosylase MutY; Provisional


Pssm-ID: 172427 [Multi-domain]  Cd Length: 289  Bit Score: 105.10  E-value: 9.78e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639187127  44 MLQQTQVQTVIP-YYLNFMAMFPTVADLAKAPEEQLLKAWQGLGYYSRARNLQRAARQLVDDYRGKWPQTAAELLDLTGI 122
Cdd:PRK13910   1 MSQQTQINTVVErFYSPFLEAFPTLKDLANAPLEEVLLLWRGLGYYSRAKNLKKSAEICVKEHHSQLPNDYQSLLKLPGI 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 639187127 123 GPYTAGAIASIAFGEVVPAVDGNAFRVFSRLLLIDADIaklqTRKLFEQVIQPIVDPQRPGAFNQAIMDLGS 194
Cdd:PRK13910  81 GAYTANAILCFGFREKSACVDANIKRVLLRLFGLDPNI----HAKDLQIKANDFLNLNESFNHNQALIDLGA 148
NUDIX_DNA_Glycosylase_C-MutY cd03431
C-terminal domain of DNA glycosylase; DNA glycosylase (MutY in bacteria and hMYH in humans) is ...
 233-364 7.66e-19

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: 81.20  E-value: 7.66e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639187127 233 PRPVPYYGLIVTSPAGYLMVQRDATQMLTGYWTFPLIQQADLQDATDQQPATLQTDIAHLEQRFMtdyqlpitltplsgq 312
Cdd:cd03431    1 VPERYFTVLVLRDGGRVLLEKRPEKGLLAGLWEFPLVETEEEEEEAEALLGLLAEELLLILEPLG--------------- 65

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 639187127 313 PVSHTYTHQRWQVKLLVAELSSAADLTFYPGKWVAASTIKTLPLPKVQEKLM 364
Cdd:cd03431   66 EVKHVFSHFRLHITVYLVELPEAPPAAPDEGRWVDLEELDEYALPAPMRKLL 117
NUDIX_4 pfam14815
NUDIX domain;
238-366 5.22e-11

NUDIX domain;


Pssm-ID: 464330 [Multi-domain]  Cd Length: 114  Bit Score: 59.25  E-value: 5.22e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639187127  238 YYGLIVTSPAGYLMVQRDATQMLTGYWTFPLIQQADlqdatdqqPATLQTDIAHLEQrfmtdyqLPITLTPLSGQPVSHT 317
Cdd:pfam14815   1 AVLVIRNGDGRVLLRKRPEKGLLGGLWEFPGGKVEP--------GETLEEALARLEE-------LGIEVEVLEPGTVKHV 65

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 639187127  318 YTHQRWQVKLLVAELSSAADLTFYPGKWVAASTIKTLPLPKVQEKLMTR 366
Cdd:pfam14815  66 FTHFRLTLHVYLVREVEGEEEPQQELRWVTPEELDKYALPAAVRKILEA 114
HP0602 COG2231
3-Methyladenine DNA glycosylase, HhH-GPD/Endo3 superfamily [Replication, recombination and ...
 66-175 1.52e-10

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


Pssm-ID: 441832 [Multi-domain]  Cd Length: 220  Bit Score: 60.24  E-value: 1.52e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639187127  66 TVADLAKAPEEQLLKAWQGLGYYSR-ARNLQRAARQLVDDYRG------KWPQTA--AELLDLTGIGPYTAGAIASIAFG 136
Cdd:COG2231   61 DPEALAALDPEELAELIRPSGFYNQkAKRLKNLARWLVERYGGgleklkALPTEElrEELLSLKGIGPETADSILLYAFN 140

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 639187127 137 EVVPAVDGNAFRVFSRLLLIDADIAKLQTRKLFEQVIQP 175
Cdd:COG2231  141 RPVFVVDAYTRRIFSRLGLIEEDASYDELQRLFEENLPP 179
PRK10702 PRK10702
endonuclease III; Provisional
 70-152 8.58e-06

endonuclease III; Provisional


Pssm-ID: 182661 [Multi-domain]  Cd Length: 211  Bit Score: 46.16  E-value: 8.58e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639187127  70 LAKAPEEQLLKAWQGLGYY--------SRARNLQRAARQLVDDYRGKWPQTAAELLDLTGIGPYTAGAIASIAFGEVVPA 141
Cdd:PRK10702  57 VANTPAAMLELGVEGVKTYiktiglynSKAENVIKTCRILLEQHNGEVPEDRAALEALPGVGRKTANVVLNTAFGWPTIA 136

                         90
                 ....*....|.
gi 639187127 142 VDGNAFRVFSR 152
Cdd:PRK10702 137 VDTHIFRVCNR 147
HHH pfam00633
Helix-hairpin-helix motif; The helix-hairpin-helix DNA-binding motif is found to be duplicated ...
 104-133 5.18e-04

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: 37.01  E-value: 5.18e-04
                          10        20        30
                  ....*....|....*....|....*....|
gi 639187127  104 DYRGKWPQTAAELLDLTGIGPYTAGAIASI 133
Cdd:pfam00633   1 SLEGLIPASVEELLALPGVGPKTAEAILSY 30
 
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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