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Conserved domains on  [gi|495424297|ref|WP_008148994|]
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A/G-specific adenine glycosylase [Parabacteroides johnsonii]

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

 Zoom to residue level

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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 ...
 11-357 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: 506.21  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495424297  11 SRLLRDWYRIHKRELPWRESSDPYIIWISEIILQQTRVVQGMDYFLRFTERFPDVASLASAEEDEVLKYWQGLGYYSRAR 90
Cdd:COG1194    7 AKRLLAWYDRHGRDLPWRQTRDPYRVWLSEIMLQQTQVATVIPYYERFLERFPTVEALAAAPEDEVLKLWEGLGYYSRAR 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495424297  91 NLHAAAKDIMERFDGIFPGRYEDVISLKGIGEYTAAAIVSFVWNQPYPVVDGNVFRVLSRLFAVDTPIDTPRGKKAFTEL 170
Cdd:COG1194   87 NLHKAAQQVVEEHGGVFPDTYEELLALPGIGPYTAAAIASIAFGEPAPIVDGNVKRVLSRLFAIEGPIGSPAAKKELWAL 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495424297 171 AGLVMDPRYAGQHNQAIMELGALQCVPQNPDCEACPLKERCAAYGTGDVQTYPVKQKKTKTRDRYFHYLYIIYKGKTWLA 250
Cdd:COG1194  167 AEELLPPERPGDFNQALMDLGATVCTPKKPKCLLCPLQDDCAAFAEGRQEELPVKKPKKKKPERYGAALVIRDDGRVLLE 246

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495424297 251 RRKGKDIWEGLYEFPLIETDKAMDFAELQttDAFRRLFEGAgwLNVSVDLQGVKHVLSHQILYATFYRIEIEREGD-ALQ 329
Cdd:COG1194  247 KRPPKGLWGGLWEFPEFEWEEAEDPEALE--RWLREELGLE--VEWLEPLGTVRHVFTHFRLHLTVYLARVPAGPPaEPD 322

                        330       340
                 ....*....|....*....|....*...
gi 495424297 330 QFIAVSGKEIEQYAVPRLIQIYLEKIIG 357
Cdd:COG1194  323 GGRWVPLEELAALPLPAPMRKLLKALLK 350
 
Name Accession Description Interval E-value
MutY COG1194
Adenine-specific DNA glycosylase, acts on AG and A-oxoG pairs [Replication, recombination and ...
 11-357 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: 506.21  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495424297  11 SRLLRDWYRIHKRELPWRESSDPYIIWISEIILQQTRVVQGMDYFLRFTERFPDVASLASAEEDEVLKYWQGLGYYSRAR 90
Cdd:COG1194    7 AKRLLAWYDRHGRDLPWRQTRDPYRVWLSEIMLQQTQVATVIPYYERFLERFPTVEALAAAPEDEVLKLWEGLGYYSRAR 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495424297  91 NLHAAAKDIMERFDGIFPGRYEDVISLKGIGEYTAAAIVSFVWNQPYPVVDGNVFRVLSRLFAVDTPIDTPRGKKAFTEL 170
Cdd:COG1194   87 NLHKAAQQVVEEHGGVFPDTYEELLALPGIGPYTAAAIASIAFGEPAPIVDGNVKRVLSRLFAIEGPIGSPAAKKELWAL 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495424297 171 AGLVMDPRYAGQHNQAIMELGALQCVPQNPDCEACPLKERCAAYGTGDVQTYPVKQKKTKTRDRYFHYLYIIYKGKTWLA 250
Cdd:COG1194  167 AEELLPPERPGDFNQALMDLGATVCTPKKPKCLLCPLQDDCAAFAEGRQEELPVKKPKKKKPERYGAALVIRDDGRVLLE 246

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495424297 251 RRKGKDIWEGLYEFPLIETDKAMDFAELQttDAFRRLFEGAgwLNVSVDLQGVKHVLSHQILYATFYRIEIEREGD-ALQ 329
Cdd:COG1194  247 KRPPKGLWGGLWEFPEFEWEEAEDPEALE--RWLREELGLE--VEWLEPLGTVRHVFTHFRLHLTVYLARVPAGPPaEPD 322

                        330       340
                 ....*....|....*....|....*...
gi 495424297 330 QFIAVSGKEIEQYAVPRLIQIYLEKIIG 357
Cdd:COG1194  323 GGRWVPLEELAALPLPAPMRKLLKALLK 350
mutY TIGR01084
A/G-specific adenine glycosylase; This equivalog model identifies mutY members of the ...
 11-279 1.10e-112

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: 328.99  E-value: 1.10e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495424297   11 SRLLRDWYRIHKRE-LPWRESSDPYIIWISEIILQQTRVVQGMDYFLRFTERFPDVASLASAEEDEVLKYWQGLGYYSRA 89
Cdd:TIGR01084   3 SEDLLSWYDKYGRKtLPWRQNKTPYRVWLSEVMLQQTQVATVIPYFERFLERFPTVQALANAPQDEVLKLWEGLGYYARA 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495424297   90 RNLHAAAKDIMERFDGIFPGRYEDVISLKGIGEYTAAAIVSFVWNQPYPVVDGNVFRVLSRLFAVDTPIDTPRGKKAFTE 169
Cdd:TIGR01084  83 RNLHKAAQEVVEEFGGEFPQDFEDLAALPGVGRYTAGAILSFALNKPYPILDGNVKRVLSRLFAVEGWPGKKKVENRLWT 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495424297  170 LAGLVMDPRYAGQHNQAIMELGALQCVPQNPDCEACPLKERCAAYGTGDVQTYPVKQKKTKTRDRYFHYLYI-IYKGKTW 248
Cdd:TIGR01084 163 LAESLLPKADPEAFNQALMDLGAMICTRKKPKCDLCPLQDFCLAYQQGTWEEYPVKKPKAAPPERTTYFLVLqNYDGEVL 242

                         250       260       270
                  ....*....|....*....|....*....|.
gi 495424297  249 LARRKGKDIWEGLYEFPLIETDKAMDFAELQ 279
Cdd:TIGR01084 243 LEQRPEKGLWGGLYCFPQFEDEDSLAFLLAQ 273
PRK10880 PRK10880
adenine DNA glycosylase;
11-288 2.67e-83

adenine DNA glycosylase;


Pssm-ID: 182805 [Multi-domain]  Cd Length: 350  Bit Score: 256.95  E-value: 2.67e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495424297  11 SRLLRDWYRIHKRE-LPWRESSDPYIIWISEIILQQTRVVQGMDYFLRFTERFPDVASLASAEEDEVLKYWQGLGYYSRA 89
Cdd:PRK10880   7 SAQVLDWYDKYGRKtLPWQIDKTPYKVWLSEVMLQQTQVATVIPYFERFMARFPTVTDLANAPLDEVLHLWTGLGYYARA 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495424297  90 RNLHAAAKDIMERFDGIFPGRYEDVISLKGIGEYTAAAIVSFVWNQPYPVVDGNVFRVLSRLFAVDT-PidtprGKKAFT 168
Cdd:PRK10880  87 RNLHKAAQQVATLHGGEFPETFEEVAALPGVGRSTAGAILSLSLGKHFPILDGNVKRVLARCYAVSGwP-----GKKEVE 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495424297 169 ----ELAGLVMDPRYAGQHNQAIMELGALQCVPQNPDCEACPLKERCAAYGTGDVQTYPVKQKKTKTRDRYFHYLYIIYK 244
Cdd:PRK10880 162 nrlwQLSEQVTPAVGVERFNQAMMDLGAMVCTRSKPKCELCPLQNGCIAYANHSWALYPGKKPKQTLPERTGYFLLLQHG 241

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 495424297 245 GKTWLARRKGKDIWEGLYEFPLIET---------DKAMDFAELQTTDAFRRLF 288
Cdd:PRK10880 242 DEVWLEQRPPSGLWGGLFCFPQFADeeelrqwlaQRGIAADNLTQLTAFRHTF 294
ENDO3c cd00056
endonuclease III; includes endonuclease III (DNA-(apurinic or apyrimidinic site) lyase), ...
 34-191 1.40e-46

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: 155.86  E-value: 1.40e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495424297  34 YIIWISEIILQQTRVVQGMDYFLRFTERF-PDVASLASAEEDEVLKYWQGLGYYSRARNLHAAAKDIMERFDGIF---PG 109
Cdd:cd00056    1 FEVLVSEILSQQTTDKAVNKAYERLFERYgPTPEALAAADEEELRELIRSLGYRRKAKYLKELARAIVEGFGGLVlddPD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495424297 110 RYEDVISLKGIGEYTAAAIVSFVWNQPYPVVDGNVFRVLSRLFAVDTPIDtprgKKAFTELAGLVMDPRYAGQHNQAIME 189
Cdd:cd00056   81 AREELLALPGVGRKTANVVLLFALGPDAFPVDTHVRRVLKRLGLIPKKKT----PEELEELLEELLPKPYWGEANQALMD 156


                 ..
gi 495424297 190 LG 191
Cdd:cd00056  157 LG 158
ENDO3c smart00478
endonuclease III; includes endonuclease III (DNA-(apurinic or apyrimidinic site) lyase), ...
 42-193 1.39e-34

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: 124.30  E-value: 1.39e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495424297    42 ILQQTRVVQGMDYFLRFTERFPDVASLASAEEDEVLKYWQGLG-YYSRARNLHAAAKDIMERFDGIFPGRYEDVISLKGI 120
Cdd:smart00478   1 LSQQTTDERVNKATERLFEKFPTPEDLAAADEEELEELIRGLGfYRRKARYLIELARILVEEYGGEVPDDREELLKLPGV 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495424297   121 GEYTAAAIVSFVWNQPYPVVDGNVFRVLSRLFAVDTpIDTPrgkKAFTELAGLVMDPRYAGQHNQAIMELGAL 193
Cdd:smart00478  81 GRKTANAVLSFALGKPFIPVDTHVLRIAKRLGLVDK-KSTP---EEVEKLLEKLLPEEDWRELNLLLIDFGRT 149
HhH-GPD pfam00730
HhH-GPD superfamily base excision DNA repair protein; This family contains a diverse range of ...
 38-174 5.99e-31

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: 114.30  E-value: 5.99e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495424297   38 ISEIILQQTRVVQGMDYFLRFTER-FPDVASLASAEEDEVLKYWQGLGYY-SRARNLHAAAKDIMERFDGIFPGRY-EDV 114
Cdd:pfam00730   1 VSAILSQQTSDKAVNKITERLFEKfFPTPEDLADADEEELRELIRGLGFYrRKAKYLKELARILVEGYGGEVPLDEeELE 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 495424297  115 ISLKGIGEYTAAAIVSFVW--NQPYPVVDGNVFRVLSRLFAVDTpIDTPrgKKAFTELAGLV 174
Cdd:pfam00730  81 ALLKGVGRWTAEAVLIFALgrPDPLPVVDTHVRRVLKRLGLIKE-KPTP--KEVERELEELW 139
 
Name Accession Description Interval E-value
MutY COG1194
Adenine-specific DNA glycosylase, acts on AG and A-oxoG pairs [Replication, recombination and ...
 11-357 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: 506.21  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495424297  11 SRLLRDWYRIHKRELPWRESSDPYIIWISEIILQQTRVVQGMDYFLRFTERFPDVASLASAEEDEVLKYWQGLGYYSRAR 90
Cdd:COG1194    7 AKRLLAWYDRHGRDLPWRQTRDPYRVWLSEIMLQQTQVATVIPYYERFLERFPTVEALAAAPEDEVLKLWEGLGYYSRAR 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495424297  91 NLHAAAKDIMERFDGIFPGRYEDVISLKGIGEYTAAAIVSFVWNQPYPVVDGNVFRVLSRLFAVDTPIDTPRGKKAFTEL 170
Cdd:COG1194   87 NLHKAAQQVVEEHGGVFPDTYEELLALPGIGPYTAAAIASIAFGEPAPIVDGNVKRVLSRLFAIEGPIGSPAAKKELWAL 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495424297 171 AGLVMDPRYAGQHNQAIMELGALQCVPQNPDCEACPLKERCAAYGTGDVQTYPVKQKKTKTRDRYFHYLYIIYKGKTWLA 250
Cdd:COG1194  167 AEELLPPERPGDFNQALMDLGATVCTPKKPKCLLCPLQDDCAAFAEGRQEELPVKKPKKKKPERYGAALVIRDDGRVLLE 246

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495424297 251 RRKGKDIWEGLYEFPLIETDKAMDFAELQttDAFRRLFEGAgwLNVSVDLQGVKHVLSHQILYATFYRIEIEREGD-ALQ 329
Cdd:COG1194  247 KRPPKGLWGGLWEFPEFEWEEAEDPEALE--RWLREELGLE--VEWLEPLGTVRHVFTHFRLHLTVYLARVPAGPPaEPD 322

                        330       340
                 ....*....|....*....|....*...
gi 495424297 330 QFIAVSGKEIEQYAVPRLIQIYLEKIIG 357
Cdd:COG1194  323 GGRWVPLEELAALPLPAPMRKLLKALLK 350
mutY TIGR01084
A/G-specific adenine glycosylase; This equivalog model identifies mutY members of the ...
 11-279 1.10e-112

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: 328.99  E-value: 1.10e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495424297   11 SRLLRDWYRIHKRE-LPWRESSDPYIIWISEIILQQTRVVQGMDYFLRFTERFPDVASLASAEEDEVLKYWQGLGYYSRA 89
Cdd:TIGR01084   3 SEDLLSWYDKYGRKtLPWRQNKTPYRVWLSEVMLQQTQVATVIPYFERFLERFPTVQALANAPQDEVLKLWEGLGYYARA 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495424297   90 RNLHAAAKDIMERFDGIFPGRYEDVISLKGIGEYTAAAIVSFVWNQPYPVVDGNVFRVLSRLFAVDTPIDTPRGKKAFTE 169
Cdd:TIGR01084  83 RNLHKAAQEVVEEFGGEFPQDFEDLAALPGVGRYTAGAILSFALNKPYPILDGNVKRVLSRLFAVEGWPGKKKVENRLWT 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495424297  170 LAGLVMDPRYAGQHNQAIMELGALQCVPQNPDCEACPLKERCAAYGTGDVQTYPVKQKKTKTRDRYFHYLYI-IYKGKTW 248
Cdd:TIGR01084 163 LAESLLPKADPEAFNQALMDLGAMICTRKKPKCDLCPLQDFCLAYQQGTWEEYPVKKPKAAPPERTTYFLVLqNYDGEVL 242

                         250       260       270
                  ....*....|....*....|....*....|.
gi 495424297  249 LARRKGKDIWEGLYEFPLIETDKAMDFAELQ 279
Cdd:TIGR01084 243 LEQRPEKGLWGGLYCFPQFEDEDSLAFLLAQ 273
PRK10880 PRK10880
adenine DNA glycosylase;
11-288 2.67e-83

adenine DNA glycosylase;


Pssm-ID: 182805 [Multi-domain]  Cd Length: 350  Bit Score: 256.95  E-value: 2.67e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495424297  11 SRLLRDWYRIHKRE-LPWRESSDPYIIWISEIILQQTRVVQGMDYFLRFTERFPDVASLASAEEDEVLKYWQGLGYYSRA 89
Cdd:PRK10880   7 SAQVLDWYDKYGRKtLPWQIDKTPYKVWLSEVMLQQTQVATVIPYFERFMARFPTVTDLANAPLDEVLHLWTGLGYYARA 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495424297  90 RNLHAAAKDIMERFDGIFPGRYEDVISLKGIGEYTAAAIVSFVWNQPYPVVDGNVFRVLSRLFAVDT-PidtprGKKAFT 168
Cdd:PRK10880  87 RNLHKAAQQVATLHGGEFPETFEEVAALPGVGRSTAGAILSLSLGKHFPILDGNVKRVLARCYAVSGwP-----GKKEVE 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495424297 169 ----ELAGLVMDPRYAGQHNQAIMELGALQCVPQNPDCEACPLKERCAAYGTGDVQTYPVKQKKTKTRDRYFHYLYIIYK 244
Cdd:PRK10880 162 nrlwQLSEQVTPAVGVERFNQAMMDLGAMVCTRSKPKCELCPLQNGCIAYANHSWALYPGKKPKQTLPERTGYFLLLQHG 241

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 495424297 245 GKTWLARRKGKDIWEGLYEFPLIET---------DKAMDFAELQTTDAFRRLF 288
Cdd:PRK10880 242 DEVWLEQRPPSGLWGGLFCFPQFADeeelrqwlaQRGIAADNLTQLTAFRHTF 294
ENDO3c cd00056
endonuclease III; includes endonuclease III (DNA-(apurinic or apyrimidinic site) lyase), ...
 34-191 1.40e-46

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: 155.86  E-value: 1.40e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495424297  34 YIIWISEIILQQTRVVQGMDYFLRFTERF-PDVASLASAEEDEVLKYWQGLGYYSRARNLHAAAKDIMERFDGIF---PG 109
Cdd:cd00056    1 FEVLVSEILSQQTTDKAVNKAYERLFERYgPTPEALAAADEEELRELIRSLGYRRKAKYLKELARAIVEGFGGLVlddPD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495424297 110 RYEDVISLKGIGEYTAAAIVSFVWNQPYPVVDGNVFRVLSRLFAVDTPIDtprgKKAFTELAGLVMDPRYAGQHNQAIME 189
Cdd:cd00056   81 AREELLALPGVGRKTANVVLLFALGPDAFPVDTHVRRVLKRLGLIPKKKT----PEELEELLEELLPKPYWGEANQALMD 156


                 ..
gi 495424297 190 LG 191
Cdd:cd00056  157 LG 158
ENDO3c smart00478
endonuclease III; includes endonuclease III (DNA-(apurinic or apyrimidinic site) lyase), ...
 42-193 1.39e-34

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: 124.30  E-value: 1.39e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495424297    42 ILQQTRVVQGMDYFLRFTERFPDVASLASAEEDEVLKYWQGLG-YYSRARNLHAAAKDIMERFDGIFPGRYEDVISLKGI 120
Cdd:smart00478   1 LSQQTTDERVNKATERLFEKFPTPEDLAAADEEELEELIRGLGfYRRKARYLIELARILVEEYGGEVPDDREELLKLPGV 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495424297   121 GEYTAAAIVSFVWNQPYPVVDGNVFRVLSRLFAVDTpIDTPrgkKAFTELAGLVMDPRYAGQHNQAIMELGAL 193
Cdd:smart00478  81 GRKTANAVLSFALGKPFIPVDTHVLRIAKRLGLVDK-KSTP---EEVEKLLEKLLPEEDWRELNLLLIDFGRT 149
Nth COG0177
Endonuclease III [Replication, recombination and repair];
12-215 4.52e-34

Endonuclease III [Replication, recombination and repair];


Pssm-ID: 439947 [Multi-domain]  Cd Length: 198  Bit Score: 124.44  E-value: 4.52e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495424297  12 RLLRDWYRIHKRELPWRessDPYIIWISEIILQQT---RVVQGmdyFLRFTERFPDVASLASAEEDEVLKYWQGLGYY-S 87
Cdd:COG0177    2 ERLKELYPDAKTELDYR---DPFELLVATILSAQTtdeRVNKA---TPRLFARYPTPEALAAADLEELEELIRPIGLYrN 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495424297  88 RARNLHAAAKDIMERFDGIFPGRYEDVISLKGIGEYTAAAIVSFVWNQPYPVVDGNVFRVLSRLFAVDTpiDTPRgkKAF 167
Cdd:COG0177   76 KAKNIIALARILVEKYGGEVPETREELESLPGVGRKTANVVLNFAFGKPAIAVDTHVHRVSNRLGLVPG--KDPE--EVE 151

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 495424297 168 TELAGLVmDPRYAGQHNQAIMELGALQCVPQNPDCEACPLKERCAAYG 215
Cdd:COG0177  152 KDLMKLI-PKEYWGDLHHLLILHGRYICKARKPKCEECPLADLCPYYG 198
PRK13910 PRK13910
DNA glycosylase MutY; Provisional
 44-265 4.82e-33

DNA glycosylase MutY; Provisional


Pssm-ID: 172427 [Multi-domain]  Cd Length: 289  Bit Score: 124.36  E-value: 4.82e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495424297  44 QQTRVVQGMD-YFLRFTERFPDVASLASAEEDEVLKYWQGLGYYSRARNLHAAAKDIMERFDGIFPGRYEDVISLKGIGE 122
Cdd:PRK13910   3 QQTQINTVVErFYSPFLEAFPTLKDLANAPLEEVLLLWRGLGYYSRAKNLKKSAEICVKEHHSQLPNDYQSLLKLPGIGA 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495424297 123 YTAAAIVSFVWNQPYPVVDGNVFRVLSRLFAVDTPIDTprgkKAFTELAGLVMDPRYAGQHNQAIMELGALQCVPQnPDC 202
Cdd:PRK13910  83 YTANAILCFGFREKSACVDANIKRVLLRLFGLDPNIHA----KDLQIKANDFLNLNESFNHNQALIDLGALICSPK-PKC 157

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495424297 203 EACPLKERCaaYGTGDVQTYPVKQKKTKTRDRyfHYLYIIYKGKTWLARRKGKDIWEGLYEFP 265
Cdd:PRK13910 158 AICPLNPYC--LGKNNPEKHTLKKKQEIVQEE--RYLGVVIQNNQIALEKIEQKLYLGMHHFP 216
HhH-GPD pfam00730
HhH-GPD superfamily base excision DNA repair protein; This family contains a diverse range of ...
 38-174 5.99e-31

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: 114.30  E-value: 5.99e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495424297   38 ISEIILQQTRVVQGMDYFLRFTER-FPDVASLASAEEDEVLKYWQGLGYY-SRARNLHAAAKDIMERFDGIFPGRY-EDV 114
Cdd:pfam00730   1 VSAILSQQTSDKAVNKITERLFEKfFPTPEDLADADEEELRELIRGLGFYrRKAKYLKELARILVEGYGGEVPLDEeELE 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 495424297  115 ISLKGIGEYTAAAIVSFVW--NQPYPVVDGNVFRVLSRLFAVDTpIDTPrgKKAFTELAGLV 174
Cdd:pfam00730  81 ALLKGVGRWTAEAVLIFALgrPDPLPVVDTHVRRVLKRLGLIKE-KPTP--KEVERELEELW 139
NUDIX_DNA_Glycosylase_C-MutY cd03431
C-terminal domain of DNA glycosylase; DNA glycosylase (MutY in bacteria and hMYH in humans) is ...
 232-353 2.61e-29

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: 109.32  E-value: 2.61e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495424297 232 RDRYFHYLYIIYKGKTWLARRKGKDIWEGLYEFPLIETDKAMDFAELQttdafrRLFEGAGWLNVSVDLQGVKHVLSHQI 311
Cdd:cd03431    2 PERYFTVLVLRDGGRVLLEKRPEKGLLAGLWEFPLVETEEEEEEAEAL------LGLLAEELLLILEPLGEVKHVFSHFR 75

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 495424297 312 LYATFYRIEIEREGDAL-QQFIAVSGKEIEQYAVPRLIQIYLE 353
Cdd:cd03431   76 LHITVYLVELPEAPPAApDEGRWVDLEELDEYALPAPMRKLLE 118
NUDIX_4 pfam14815
NUDIX domain;
237-354 3.21e-18

NUDIX domain;


Pssm-ID: 464330 [Multi-domain]  Cd Length: 114  Bit Score: 79.28  E-value: 3.21e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495424297  237 HYLYIIYK-GKTWLARRKGKDIWEGLYEFPLIEtdkamDFAELQTTDAFRRLfEGAGWLNVSVDLQGVKHVLSHQILYAT 315
Cdd:pfam14815   1 AVLVIRNGdGRVLLRKRPEKGLLGGLWEFPGGK-----VEPGETLEEALARL-EELGIEVEVLEPGTVKHVFTHFRLTLH 74

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 495424297  316 FYRIEIEREGDALQQ-FIAVSGKEIEQYAVPRLIQIYLEK 354
Cdd:pfam14815  75 VYLVREVEGEEEPQQeLRWVTPEELDKYALPAAVRKILEA 114
HP0602 COG2231
3-Methyladenine DNA glycosylase, HhH-GPD/Endo3 superfamily [Replication, recombination and ...
 64-215 2.13e-09

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


Pssm-ID: 441832 [Multi-domain]  Cd Length: 220  Bit Score: 56.78  E-value: 2.13e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495424297  64 DVASLASAEEDEVLKYWQGLGYYSR-ARNLHAAAKDIMERFDG----IFPGRYEDV----ISLKGIGEYTAAAIVSFVWN 134
Cdd:COG2231   61 DPEALAALDPEELAELIRPSGFYNQkAKRLKNLARWLVERYGGglekLKALPTEELreelLSLKGIGPETADSILLYAFN 140

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495424297 135 QPYPVVDGNVFRVLSRLFAVDTPIDTPRGKKAFTELagLVMDPRYAGQ-HNQaIMELGALQCVPQnPDCEACPLKERCAA 213
Cdd:COG2231  141 RPVFVVDAYTRRIFSRLGLIEEDASYDELQRLFEEN--LPPDVALYNEfHAL-IVEHGKEYCKKK-PKCEECPLRDLCPY 216


                 ..
gi 495424297 214 YG 215
Cdd:COG2231  217 GG 218
AlkA COG0122
3-methyladenine DNA glycosylase/8-oxoguanine DNA glycosylase [Replication, recombination and ...
 62-171 7.82e-07

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


Pssm-ID: 439892 [Multi-domain]  Cd Length: 255  Bit Score: 49.88  E-value: 7.82e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495424297  62 FPDVASLASAEEDEvlkyWQGLGY-YSRARNLHAAAKDIME---RFDGIFPGRYEDVI----SLKGIGEYTAAAIVSFVW 133
Cdd:COG0122  127 FPTPEALAAASEEE----LRACGLsRRKARYLRALARAVADgelDLEALAGLDDEEAIarltALPGIGPWTAEMVLLFAL 202

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 495424297 134 NQP--YPVVDGNVFRVLSRLFAVDTPIDtprgKKAFTELA 171
Cdd:COG0122  203 GRPdaFPAGDLGLRRALGRLYGLGERPT----PKELRELA 238
HHH pfam00633
Helix-hairpin-helix motif; The helix-hairpin-helix DNA-binding motif is found to be duplicated ...
 102-131 1.82e-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: 40.86  E-value: 1.82e-05
                          10        20        30
                  ....*....|....*....|....*....|
gi 495424297  102 RFDGIFPGRYEDVISLKGIGEYTAAAIVSF 131
Cdd:pfam00633   1 SLEGLIPASVEELLALPGVGPKTAEAILSY 30
PRK10702 PRK10702
endonuclease III; Provisional
 74-211 2.82e-05

endonuclease III; Provisional


Pssm-ID: 182661 [Multi-domain]  Cd Length: 211  Bit Score: 44.62  E-value: 2.82e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495424297  74 DEVLKYWQGLGYY-SRARNLHAAAKDIMERFDGIFPGRYEDVISLKGIGEYTAAAIVSFVWNQPYPVVDGNVFRVLSRL- 151
Cdd:PRK10702  70 EGVKTYIKTIGLYnSKAENVIKTCRILLEQHNGEVPEDRAALEALPGVGRKTANVVLNTAFGWPTIAVDTHIFRVCNRTq 149

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 495424297 152 FAVDTPIDTPRGKkafteLAGLVMDPRYAGQHNQAIMElGALQCVPQNPDCEACPLKERC 211
Cdd:PRK10702 150 FAPGKNVEQVEEK-----LLKVVPAEFKVDCHHWLILH-GRYTCIARKPRCGSCIIEDLC 203
FES smart00525
iron-sulpphur binding domain in DNA-(apurinic or apyrimidinic site) lyase (subfamily of ENDO3); ...
 195-214 5.56e-05

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


Pssm-ID: 197771 [Multi-domain]  Cd Length: 21  Bit Score: 39.46  E-value: 5.56e-05
                           10        20
                   ....*....|....*....|
gi 495424297   195 CVPQNPDCEACPLKERCAAY 214
Cdd:smart00525   2 CTARKPRCDECPLKDLCPAY 21
EndIII_4Fe-2S pfam10576
Iron-sulfur binding domain of endonuclease III; Escherichia coli endonuclease III (EC 4.2.99. ...
 195-211 2.00e-04

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


Pssm-ID: 463153 [Multi-domain]  Cd Length: 17  Bit Score: 38.14  E-value: 2.00e-04
                          10
                  ....*....|....*..
gi 495424297  195 CVPQNPDCEACPLKERC 211
Cdd:pfam10576   1 CTARKPKCEECPLADLC 17
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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