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Conserved domains on  [gi|446808878|ref|WP_000886134|]
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A/G-specific adenine glycosylase [Streptococcus oralis]

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 ...
 15-384 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: 526.63  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446808878  15 EKIISFREKLLNWYDENKRDLPWRRSKNPYHIWVSEIMLQQTRVDTVIPYYERFLDWFPTVESLANAPEERLLKAWEGLG 94
Cdd:COG1194    1 MDMASFAKRLLAWYDRHGRDLPWRQTRDPYRVWLSEIMLQQTQVATVIPYYERFLERFPTVEALAAAPEDEVLKLWEGLG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446808878  95 YYSRVRNMQAAAQQIMADFGGQFPNTYEGISSLKGIGPYTAGAISSIAFNLPEPAVDGNVMRVLARLFEVNHDIGVPSNR 174
Cdd:COG1194   81 YYSRARNLHKAAQQVVEEHGGVFPDTYEELLALPGIGPYTAAAIASIAFGEPAPIVDGNVKRVLSRLFAIEGPIGSPAAK 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446808878 175 KIFQAMMEILIDPKRPGDFNQALMDLGSDIEAPVNPRPEESPVKDFSAAYQNGTMGRYPIKEPKKKPLPIYLKALVVRnD 254
Cdd:COG1194  161 KELWALAEELLPPERPGDFNQALMDLGATVCTPKKPKCLLCPLQDDCAAFAEGRQEELPVKKPKKKKPERYGAALVIR-D 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446808878 255 QGQFLLEKNESEKLLAGFWHFPLIEVDDFSSDDnqldlfsqvteesrvfgpSPQENFEQDYDLEVNWSQQvFDQVKHVFS 334
Cdd:COG1194  240 DGRVLLEKRPPKGLWGGLWEFPEFEWEEAEDPE------------------ALERWLREELGLEVEWLEP-LGTVRHVFT 300

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|
gi 446808878 335 HRKWHIQIIAGQVTETKQFSDREIRWVSPQEFSDYPLAKPQQKIWQAYKN 384
Cdd:COG1194  301 HFRLHLTVYLARVPAGPPAEPDGGRWVPLEELAALPLPAPMRKLLKALLK 350
 
Name Accession Description Interval E-value
MutY COG1194
Adenine-specific DNA glycosylase, acts on AG and A-oxoG pairs [Replication, recombination and ...
 15-384 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: 526.63  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446808878  15 EKIISFREKLLNWYDENKRDLPWRRSKNPYHIWVSEIMLQQTRVDTVIPYYERFLDWFPTVESLANAPEERLLKAWEGLG 94
Cdd:COG1194    1 MDMASFAKRLLAWYDRHGRDLPWRQTRDPYRVWLSEIMLQQTQVATVIPYYERFLERFPTVEALAAAPEDEVLKLWEGLG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446808878  95 YYSRVRNMQAAAQQIMADFGGQFPNTYEGISSLKGIGPYTAGAISSIAFNLPEPAVDGNVMRVLARLFEVNHDIGVPSNR 174
Cdd:COG1194   81 YYSRARNLHKAAQQVVEEHGGVFPDTYEELLALPGIGPYTAAAIASIAFGEPAPIVDGNVKRVLSRLFAIEGPIGSPAAK 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446808878 175 KIFQAMMEILIDPKRPGDFNQALMDLGSDIEAPVNPRPEESPVKDFSAAYQNGTMGRYPIKEPKKKPLPIYLKALVVRnD 254
Cdd:COG1194  161 KELWALAEELLPPERPGDFNQALMDLGATVCTPKKPKCLLCPLQDDCAAFAEGRQEELPVKKPKKKKPERYGAALVIR-D 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446808878 255 QGQFLLEKNESEKLLAGFWHFPLIEVDDFSSDDnqldlfsqvteesrvfgpSPQENFEQDYDLEVNWSQQvFDQVKHVFS 334
Cdd:COG1194  240 DGRVLLEKRPPKGLWGGLWEFPEFEWEEAEDPE------------------ALERWLREELGLEVEWLEP-LGTVRHVFT 300

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|
gi 446808878 335 HRKWHIQIIAGQVTETKQFSDREIRWVSPQEFSDYPLAKPQQKIWQAYKN 384
Cdd:COG1194  301 HFRLHLTVYLARVPAGPPAEPDGGRWVPLEELAALPLPAPMRKLLKALLK 350
mutY TIGR01084
A/G-specific adenine glycosylase; This equivalog model identifies mutY members of the ...
 20-282 3.69e-124

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: 359.42  E-value: 3.69e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446808878   20 FREKLLNWYDENKR-DLPWRRSKNPYHIWVSEIMLQQTRVDTVIPYYERFLDWFPTVESLANAPEERLLKAWEGLGYYSR 98
Cdd:TIGR01084   2 FSEDLLSWYDKYGRkTLPWRQNKTPYRVWLSEVMLQQTQVATVIPYFERFLERFPTVQALANAPQDEVLKLWEGLGYYAR 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446808878   99 VRNMQAAAQQIMADFGGQFPNTYEGISSLKGIGPYTAGAISSIAFNLPEPAVDGNVMRVLARLFEVNHDIGVPSNRKIFQ 178
Cdd:TIGR01084  82 ARNLHKAAQEVVEEFGGEFPQDFEDLAALPGVGRYTAGAILSFALNKPYPILDGNVKRVLSRLFAVEGWPGKKKVENRLW 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446808878  179 AMMEILIDPKRPGDFNQALMDLGSDIEAPVNPRPEESPVKDFSAAYQNGTMGRYPIKEPKKKPLPIYLKALVVRNDQGQF 258
Cdd:TIGR01084 162 TLAESLLPKADPEAFNQALMDLGAMICTRKKPKCDLCPLQDFCLAYQQGTWEEYPVKKPKAAPPERTTYFLVLQNYDGEV 241

                         250       260
                  ....*....|....*....|....
gi 446808878  259 LLEKNESEKLLAGFWHFPLIEVDD 282
Cdd:TIGR01084 242 LLEQRPEKGLWGGLYCFPQFEDED 265
PRK10880 PRK10880
adenine DNA glycosylase;
20-273 1.70e-70

adenine DNA glycosylase;


Pssm-ID: 182805 [Multi-domain]  Cd Length: 350  Bit Score: 224.97  E-value: 1.70e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446808878  20 FREKLLNWYDENKRD-LPWRRSKNPYHIWVSEIMLQQTRVDTVIPYYERFLDWFPTVESLANAPEERLLKAWEGLGYYSR 98
Cdd:PRK10880   6 FSAQVLDWYDKYGRKtLPWQIDKTPYKVWLSEVMLQQTQVATVIPYFERFMARFPTVTDLANAPLDEVLHLWTGLGYYAR 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446808878  99 VRNMQAAAQQIMADFGGQFPNTYEGISSLKGIGPYTAGAISSIAFNLPEPAVDGNVMRVLARLFEVNhdiGVPSNRKIFQ 178
Cdd:PRK10880  86 ARNLHKAAQQVATLHGGEFPETFEEVAALPGVGRSTAGAILSLSLGKHFPILDGNVKRVLARCYAVS---GWPGKKEVEN 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446808878 179 AMMEIL--IDPKRP-GDFNQALMDLGSDIEAPVNPRPEESPVKDFSAAYQNGTMGRYPIKEPKKKpLPiylkalvvrNDQ 255
Cdd:PRK10880 163 RLWQLSeqVTPAVGvERFNQAMMDLGAMVCTRSKPKCELCPLQNGCIAYANHSWALYPGKKPKQT-LP---------ERT 232

                        250       260
                 ....*....|....*....|...
gi 446808878 256 GQFLLEKNESEKLLA-----GFW 273
Cdd:PRK10880 233 GYFLLLQHGDEVWLEqrppsGLW 255
ENDO3c cd00056
endonuclease III; includes endonuclease III (DNA-(apurinic or apyrimidinic site) lyase), ...
 44-201 8.98e-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: 8.98e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446808878  44 YHIWVSEIMLQQTRVDTVIPYYERFLD-WFPTVESLANAPEERLLKAWEGLGYYSRVRNMQAAAQQIMADFGG---QFPN 119
Cdd:cd00056    1 FEVLVSEILSQQTTDKAVNKAYERLFErYGPTPEALAAADEEELRELIRSLGYRRKAKYLKELARAIVEGFGGlvlDDPD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446808878 120 TYEGISSLKGIGPYTAGAISSIAFNLPEPAVDGNVMRVLARLFevnhDIGVPSNRKIFQAMMEILIDPKRPGDFNQALMD 199
Cdd:cd00056   81 AREELLALPGVGRKTANVVLLFALGPDAFPVDTHVRRVLKRLG----LIPKKKTPEELEELLEELLPKPYWGEANQALMD 156


                 ..
gi 446808878 200 LG 201
Cdd:cd00056  157 LG 158
ENDO3c smart00478
endonuclease III; includes endonuclease III (DNA-(apurinic or apyrimidinic site) lyase), ...
 52-201 7.25e-42

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: 143.94  E-value: 7.25e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446808878    52 MLQQTRVDTVIPYYERFLDWFPTVESLANAPEERLLKAWEGLG-YYSRVRNMQAAAQQIMADFGGQFPNTYEGISSLKGI 130
Cdd:smart00478   1 LSQQTTDERVNKATERLFEKFPTPEDLAAADEEELEELIRGLGfYRRKARYLIELARILVEEYGGEVPDDREELLKLPGV 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446808878   131 GPYTAGAISSIAFNLPEPAVDGNVMRVLARLFEVNHdigvPSNRKIFQAMMEILIDPKRPGDFNQALMDLG 201
Cdd:smart00478  81 GRKTANAVLSFALGKPFIPVDTHVLRIAKRLGLVDK----KSTPEEVEKLLEKLLPEEDWRELNLLLIDFG 147
HhH-GPD pfam00730
HhH-GPD superfamily base excision DNA repair protein; This family contains a diverse range of ...
 48-184 2.06e-35

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: 126.63  E-value: 2.06e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446808878   48 VSEIMLQQTRVDTVIPYYERFLD-WFPTVESLANAPEERLLKAWEGLGYY-SRVRNMQAAAQQIMADFGGQFPNTY-EGI 124
Cdd:pfam00730   1 VSAILSQQTSDKAVNKITERLFEkFFPTPEDLADADEEELRELIRGLGFYrRKAKYLKELARILVEGYGGEVPLDEeELE 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446808878  125 SSLKGIGPYTAGAISSIAFNLPE--PAVDGNVMRVLARLFEVNhdiGVPSNRKIFQAMMEIL 184
Cdd:pfam00730  81 ALLKGVGRWTAEAVLIFALGRPDplPVVDTHVRRVLKRLGLIK---EKPTPKEVERELEELW 139
 
Name Accession Description Interval E-value
MutY COG1194
Adenine-specific DNA glycosylase, acts on AG and A-oxoG pairs [Replication, recombination and ...
 15-384 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: 526.63  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446808878  15 EKIISFREKLLNWYDENKRDLPWRRSKNPYHIWVSEIMLQQTRVDTVIPYYERFLDWFPTVESLANAPEERLLKAWEGLG 94
Cdd:COG1194    1 MDMASFAKRLLAWYDRHGRDLPWRQTRDPYRVWLSEIMLQQTQVATVIPYYERFLERFPTVEALAAAPEDEVLKLWEGLG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446808878  95 YYSRVRNMQAAAQQIMADFGGQFPNTYEGISSLKGIGPYTAGAISSIAFNLPEPAVDGNVMRVLARLFEVNHDIGVPSNR 174
Cdd:COG1194   81 YYSRARNLHKAAQQVVEEHGGVFPDTYEELLALPGIGPYTAAAIASIAFGEPAPIVDGNVKRVLSRLFAIEGPIGSPAAK 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446808878 175 KIFQAMMEILIDPKRPGDFNQALMDLGSDIEAPVNPRPEESPVKDFSAAYQNGTMGRYPIKEPKKKPLPIYLKALVVRnD 254
Cdd:COG1194  161 KELWALAEELLPPERPGDFNQALMDLGATVCTPKKPKCLLCPLQDDCAAFAEGRQEELPVKKPKKKKPERYGAALVIR-D 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446808878 255 QGQFLLEKNESEKLLAGFWHFPLIEVDDFSSDDnqldlfsqvteesrvfgpSPQENFEQDYDLEVNWSQQvFDQVKHVFS 334
Cdd:COG1194  240 DGRVLLEKRPPKGLWGGLWEFPEFEWEEAEDPE------------------ALERWLREELGLEVEWLEP-LGTVRHVFT 300

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|
gi 446808878 335 HRKWHIQIIAGQVTETKQFSDREIRWVSPQEFSDYPLAKPQQKIWQAYKN 384
Cdd:COG1194  301 HFRLHLTVYLARVPAGPPAEPDGGRWVPLEELAALPLPAPMRKLLKALLK 350
mutY TIGR01084
A/G-specific adenine glycosylase; This equivalog model identifies mutY members of the ...
 20-282 3.69e-124

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: 359.42  E-value: 3.69e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446808878   20 FREKLLNWYDENKR-DLPWRRSKNPYHIWVSEIMLQQTRVDTVIPYYERFLDWFPTVESLANAPEERLLKAWEGLGYYSR 98
Cdd:TIGR01084   2 FSEDLLSWYDKYGRkTLPWRQNKTPYRVWLSEVMLQQTQVATVIPYFERFLERFPTVQALANAPQDEVLKLWEGLGYYAR 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446808878   99 VRNMQAAAQQIMADFGGQFPNTYEGISSLKGIGPYTAGAISSIAFNLPEPAVDGNVMRVLARLFEVNHDIGVPSNRKIFQ 178
Cdd:TIGR01084  82 ARNLHKAAQEVVEEFGGEFPQDFEDLAALPGVGRYTAGAILSFALNKPYPILDGNVKRVLSRLFAVEGWPGKKKVENRLW 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446808878  179 AMMEILIDPKRPGDFNQALMDLGSDIEAPVNPRPEESPVKDFSAAYQNGTMGRYPIKEPKKKPLPIYLKALVVRNDQGQF 258
Cdd:TIGR01084 162 TLAESLLPKADPEAFNQALMDLGAMICTRKKPKCDLCPLQDFCLAYQQGTWEEYPVKKPKAAPPERTTYFLVLQNYDGEV 241

                         250       260
                  ....*....|....*....|....
gi 446808878  259 LLEKNESEKLLAGFWHFPLIEVDD 282
Cdd:TIGR01084 242 LLEQRPEKGLWGGLYCFPQFEDED 265
PRK10880 PRK10880
adenine DNA glycosylase;
20-273 1.70e-70

adenine DNA glycosylase;


Pssm-ID: 182805 [Multi-domain]  Cd Length: 350  Bit Score: 224.97  E-value: 1.70e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446808878  20 FREKLLNWYDENKRD-LPWRRSKNPYHIWVSEIMLQQTRVDTVIPYYERFLDWFPTVESLANAPEERLLKAWEGLGYYSR 98
Cdd:PRK10880   6 FSAQVLDWYDKYGRKtLPWQIDKTPYKVWLSEVMLQQTQVATVIPYFERFMARFPTVTDLANAPLDEVLHLWTGLGYYAR 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446808878  99 VRNMQAAAQQIMADFGGQFPNTYEGISSLKGIGPYTAGAISSIAFNLPEPAVDGNVMRVLARLFEVNhdiGVPSNRKIFQ 178
Cdd:PRK10880  86 ARNLHKAAQQVATLHGGEFPETFEEVAALPGVGRSTAGAILSLSLGKHFPILDGNVKRVLARCYAVS---GWPGKKEVEN 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446808878 179 AMMEIL--IDPKRP-GDFNQALMDLGSDIEAPVNPRPEESPVKDFSAAYQNGTMGRYPIKEPKKKpLPiylkalvvrNDQ 255
Cdd:PRK10880 163 RLWQLSeqVTPAVGvERFNQAMMDLGAMVCTRSKPKCELCPLQNGCIAYANHSWALYPGKKPKQT-LP---------ERT 232

                        250       260
                 ....*....|....*....|...
gi 446808878 256 GQFLLEKNESEKLLA-----GFW 273
Cdd:PRK10880 233 GYFLLLQHGDEVWLEqrppsGLW 255
ENDO3c cd00056
endonuclease III; includes endonuclease III (DNA-(apurinic or apyrimidinic site) lyase), ...
 44-201 8.98e-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: 8.98e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446808878  44 YHIWVSEIMLQQTRVDTVIPYYERFLD-WFPTVESLANAPEERLLKAWEGLGYYSRVRNMQAAAQQIMADFGG---QFPN 119
Cdd:cd00056    1 FEVLVSEILSQQTTDKAVNKAYERLFErYGPTPEALAAADEEELRELIRSLGYRRKAKYLKELARAIVEGFGGlvlDDPD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446808878 120 TYEGISSLKGIGPYTAGAISSIAFNLPEPAVDGNVMRVLARLFevnhDIGVPSNRKIFQAMMEILIDPKRPGDFNQALMD 199
Cdd:cd00056   81 AREELLALPGVGRKTANVVLLFALGPDAFPVDTHVRRVLKRLG----LIPKKKTPEELEELLEELLPKPYWGEANQALMD 156


                 ..
gi 446808878 200 LG 201
Cdd:cd00056  157 LG 158
ENDO3c smart00478
endonuclease III; includes endonuclease III (DNA-(apurinic or apyrimidinic site) lyase), ...
 52-201 7.25e-42

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: 143.94  E-value: 7.25e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446808878    52 MLQQTRVDTVIPYYERFLDWFPTVESLANAPEERLLKAWEGLG-YYSRVRNMQAAAQQIMADFGGQFPNTYEGISSLKGI 130
Cdd:smart00478   1 LSQQTTDERVNKATERLFEKFPTPEDLAAADEEELEELIRGLGfYRRKARYLIELARILVEEYGGEVPDDREELLKLPGV 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446808878   131 GPYTAGAISSIAFNLPEPAVDGNVMRVLARLFEVNHdigvPSNRKIFQAMMEILIDPKRPGDFNQALMDLG 201
Cdd:smart00478  81 GRKTANAVLSFALGKPFIPVDTHVLRIAKRLGLVDK----KSTPEEVEKLLEKLLPEEDWRELNLLLIDFG 147
HhH-GPD pfam00730
HhH-GPD superfamily base excision DNA repair protein; This family contains a diverse range of ...
 48-184 2.06e-35

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: 126.63  E-value: 2.06e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446808878   48 VSEIMLQQTRVDTVIPYYERFLD-WFPTVESLANAPEERLLKAWEGLGYY-SRVRNMQAAAQQIMADFGGQFPNTY-EGI 124
Cdd:pfam00730   1 VSAILSQQTSDKAVNKITERLFEkFFPTPEDLADADEEELRELIRGLGFYrRKAKYLKELARILVEGYGGEVPLDEeELE 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446808878  125 SSLKGIGPYTAGAISSIAFNLPE--PAVDGNVMRVLARLFEVNhdiGVPSNRKIFQAMMEIL 184
Cdd:pfam00730  81 ALLKGVGRWTAEAVLIFALGRPDplPVVDTHVRRVLKRLGLIK---EKPTPKEVERELEELW 139
PRK13910 PRK13910
DNA glycosylase MutY; Provisional
 52-276 3.10e-29

DNA glycosylase MutY; Provisional


Pssm-ID: 172427 [Multi-domain]  Cd Length: 289  Bit Score: 114.73  E-value: 3.10e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446808878  52 MLQQTRVDTVIP-YYERFLDWFPTVESLANAPEERLLKAWEGLGYYSRVRNMQAAAQQIMADFGGQFPNTYEGISSLKGI 130
Cdd:PRK13910   1 MSQQTQINTVVErFYSPFLEAFPTLKDLANAPLEEVLLLWRGLGYYSRAKNLKKSAEICVKEHHSQLPNDYQSLLKLPGI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446808878 131 GPYTAGAISSIAFNLPEPAVDGNVMRVLARLFEVNHDIgvpsNRKIFQAMMEILIDPKRPGDFNQALMDLGSDIEAPvNP 210
Cdd:PRK13910  81 GAYTANAILCFGFREKSACVDANIKRVLLRLFGLDPNI----HAKDLQIKANDFLNLNESFNHNQALIDLGALICSP-KP 155

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446808878 211 RPEESPVKDFsaayqngTMGR-YPIKEPKKKPLPI-----YLkALVVRNDqgQFLLEKNEsEKLLAGFWHFP 276
Cdd:PRK13910 156 KCAICPLNPY-------CLGKnNPEKHTLKKKQEIvqeerYL-GVVIQNN--QIALEKIE-QKLYLGMHHFP 216
Nth COG0177
Endonuclease III [Replication, recombination and repair];
22-220 4.28e-29

Endonuclease III [Replication, recombination and repair];


Pssm-ID: 439947 [Multi-domain]  Cd Length: 198  Bit Score: 111.73  E-value: 4.28e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446808878  22 EKLLNWYDENKRDLPWRrskNPYHIWVSEIMLQQTRVDTVIPYYERFLDWFPTVESLANAPEERLLKAWEGLGYY-SRVR 100
Cdd:COG0177    2 ERLKELYPDAKTELDYR---DPFELLVATILSAQTTDERVNKATPRLFARYPTPEALAAADLEELEELIRPIGLYrNKAK 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446808878 101 NMQAAAQQIMADFGGQFPNTYEGISSLKGIGPYTAGAISSIAFNLPEPAVDGNVMRVLARLfevnhdiG-VPSN--RKIF 177
Cdd:COG0177   79 NIIALARILVEKYGGEVPETREELESLPGVGRKTANVVLNFAFGKPAIAVDTHVHRVSNRL-------GlVPGKdpEEVE 151

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 446808878 178 QAMMEIlIDPKRPGDFNQALMDLGSDIEAPVNPRPEESPVKDF 220
Cdd:COG0177  152 KDLMKL-IPKEYWGDLHHLLILHGRYICKARKPKCEECPLADL 193
NUDIX_DNA_Glycosylase_C-MutY cd03431
C-terminal domain of DNA glycosylase; DNA glycosylase (MutY in bacteria and hMYH in humans) is ...
 243-380 2.56e-27

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: 104.31  E-value: 2.56e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446808878 243 PIYLKALVVRnDQGQFLLEKNESEKLLAGFWHFPLIEVDDfssddnqldlfsqvteesrvfGPSPQENFEQDYDLEVNWS 322
Cdd:cd03431    3 ERYFTVLVLR-DGGRVLLEKRPEKGLLAGLWEFPLVETEE---------------------EEEEAEALLGLLAEELLLI 60

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 446808878 323 QQVFDQVKHVFSHRKWHIQIIAGQVTETKQFSDREIRWVSPQEFSDYPLAKPQQKIWQ 380
Cdd:cd03431   61 LEPLGEVKHVFSHFRLHITVYLVELPEAPPAAPDEGRWVDLEELDEYALPAPMRKLLE 118
NUDIX_4 pfam14815
NUDIX domain;
248-381 4.80e-19

NUDIX domain;


Pssm-ID: 464330 [Multi-domain]  Cd Length: 114  Bit Score: 81.98  E-value: 4.80e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446808878  248 ALVVRNDQGQFLLEKNESEKLLAGFWHFPLIEVDDfssddnqldlfsqvteesrvfGPSPQENFEQDYDLEVNWSQQVFD 327
Cdd:pfam14815   2 VLVIRNGDGRVLLRKRPEKGLLGGLWEFPGGKVEP---------------------GETLEEALARLEELGIEVEVLEPG 60

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 446808878  328 QVKHVFSHRKWHIQIIAGQVTETKQFSDREIRWVSPQEFSDYPLAKPQQKIWQA 381
Cdd:pfam14815  61 TVKHVFTHFRLTLHVYLVREVEGEEEPQQELRWVTPEELDKYALPAAVRKILEA 114
HP0602 COG2231
3-Methyladenine DNA glycosylase, HhH-GPD/Endo3 superfamily [Replication, recombination and ...
 19-226 2.98e-06

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


Pssm-ID: 441832 [Multi-domain]  Cd Length: 220  Bit Score: 47.92  E-value: 2.98e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446808878  19 SFREKLLNWYDENKR---DLPWRRSKNPYHIWVSEIMLQQTR---VDTVIpyyERF-----LDwfptVESLANAPEERLL 87
Cdd:COG2231    2 NTKEDLLEIYERLLEhygPQHWWPAETPFEVIVGAILTQNTSwknVEKAI---ANLkeaglLD----PEALAALDPEELA 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446808878  88 KAWEGLGYY----SRVRNMqaaAQQIMADFGGQFPNTYEG--------ISSLKGIGPYTAGAISSIAFNLPEPAVDGNVM 155
Cdd:COG2231   75 ELIRPSGFYnqkaKRLKNL---ARWLVERYGGGLEKLKALpteelreeLLSLKGIGPETADSILLYAFNRPVFVVDAYTR 151

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446808878 156 RVLARLFEVNHDIGVPSNRKIFqamMEILidPKRPGDFNQ--ALMD-LGSDIEAPvNPRPEESPVKDFSAAYQN 226
Cdd:COG2231  152 RIFSRLGLIEEDASYDELQRLF---EENL--PPDVALYNEfhALIVeHGKEYCKK-KPKCEECPLRDLCPYGGQ 219
AlkA COG0122
3-methyladenine DNA glycosylase/8-oxoguanine DNA glycosylase [Replication, recombination and ...
 33-182 3.57e-06

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


Pssm-ID: 439892 [Multi-domain]  Cd Length: 255  Bit Score: 47.96  E-value: 3.57e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446808878  33 RDLPWRRSKNPYHIWVSEIMLQQ--------------TRVDTVIPYYERFLDWFPTVESLANAPEERLLKAweGLGYYsR 98
Cdd:COG0122   74 PGLRLPRRPDPFEALVRAILGQQvsvaaartiwrrlvALFGEPIEGPGGGLYAFPTPEALAAASEEELRAC--GLSRR-K 150

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446808878  99 VRNMQAAAQQIMA---DFGGQFPNTYEGI----SSLKGIGPYTAG--AIssiaFNL--PE--PAVDGNVMRVLARLFevn 165
Cdd:COG0122  151 ARYLRALARAVADgelDLEALAGLDDEEAiarlTALPGIGPWTAEmvLL----FALgrPDafPAGDLGLRRALGRLY--- 223

                        170
                 ....*....|....*..
gi 446808878 166 hDIGVPSNRKIFQAMME 182
Cdd:COG0122  224 -GLGERPTPKELRELAE 239
PRK10702 PRK10702
endonuclease III; Provisional
 78-160 3.08e-05

endonuclease III; Provisional


Pssm-ID: 182661 [Multi-domain]  Cd Length: 211  Bit Score: 44.62  E-value: 3.08e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446808878  78 LANAPEERLLKAWEGLGYY--------SRVRNMQAAAQQIMADFGGQFPNTYEGISSLKGIGPYTAGAISSIAFNLPEPA 149
Cdd:PRK10702  57 VANTPAAMLELGVEGVKTYiktiglynSKAENVIKTCRILLEQHNGEVPEDRAALEALPGVGRKTANVVLNTAFGWPTIA 136

                         90
                 ....*....|.
gi 446808878 150 VDGNVMRVLAR 160
Cdd:PRK10702 137 VDTHIFRVCNR 147
HHH pfam00633
Helix-hairpin-helix motif; The helix-hairpin-helix DNA-binding motif is found to be duplicated ...
 112-141 3.09e-05

Helix-hairpin-helix motif; The helix-hairpin-helix DNA-binding motif is found to be duplicated in the central domain of RuvA. The HhH domain of DisA, a bacterial checkpoint control protein, is a DNA-binding domain.


Pssm-ID: 425789 [Multi-domain]  Cd Length: 30  Bit Score: 40.48  E-value: 3.09e-05
                          10        20        30
                  ....*....|....*....|....*....|
gi 446808878  112 DFGGQFPNTYEGISSLKGIGPYTAGAISSI 141
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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