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Conserved domains on  [gi|503252921|ref|WP_013487582|]
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A/G-specific adenine glycosylase [Evansella cellulosilytica]

Protein Classification

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

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

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

Graphical summary

 Zoom to residue level

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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 ...
 10-360 7.56e-168

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: 471.93  E-value: 7.56e-168
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503252921  10 PAEDFQANLLHWYEENKRDLPWRRERDPYKIWVSEIMLQQTKVDTVIPYYERFISLFPSAKALAEAEEETVLKAWEGLGY 89
Cdd:COG1194    2 DMASFAKRLLAWYDRHGRDLPWRQTRDPYRVWLSEIMLQQTQVATVIPYYERFLERFPTVEALAAAPEDEVLKLWEGLGY 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503252921  90 YSRARNLHAAVKEVNEVYGGMVPNNKAEISRLRGVGPYTAGAILSIAYNIPAPAVDGNVMRVVTRLLLMYDDISKVTTRK 169
Cdd:COG1194   82 YSRARNLHKAAQQVVEEHGGVFPDTYEELLALPGIGPYTAAAIASIAFGEPAPIVDGNVKRVLSRLFAIEGPIGSPAAKK 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503252921 170 KIEAIIEQIISEQHPSEFNQALMELGALICTPRNPACLICPVQLQCRAREEGVQETLPVKAKKAKPKQKNMLALVVKnKA 249
Cdd:COG1194  162 ELWALAEELLPPERPGDFNQALMDLGATVCTPKKPKCLLCPLQDDCAAFAEGRQEELPVKKPKKKKPERYGAALVIR-DD 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503252921 250 GQVLIQKRPETGLLANLWQFPNVE---ADNIEAIVNYMKETAQLEVDVNVTVKQhVKHVFTHLIWEIDVYsgeVGEWGEE 326
Cdd:COG1194  241 GRVLLEKRPPKGLWGGLWEFPEFEweeAEDPEALERWLREELGLEVEWLEPLGT-VRHVFTHFRLHLTVY---LARVPAG 316

                        330       340       350
                 ....*....|....*....|....*....|....
gi 503252921 327 TDLESSSFKFVDKEDIDWYPFPVSHQKIIDRMVK 360
Cdd:COG1194  317 PPAEPDGGRWVPLEELAALPLPAPMRKLLKALLK 350
 
Name Accession Description Interval E-value
MutY COG1194
Adenine-specific DNA glycosylase, acts on AG and A-oxoG pairs [Replication, recombination and ...
 10-360 7.56e-168

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: 471.93  E-value: 7.56e-168
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503252921  10 PAEDFQANLLHWYEENKRDLPWRRERDPYKIWVSEIMLQQTKVDTVIPYYERFISLFPSAKALAEAEEETVLKAWEGLGY 89
Cdd:COG1194    2 DMASFAKRLLAWYDRHGRDLPWRQTRDPYRVWLSEIMLQQTQVATVIPYYERFLERFPTVEALAAAPEDEVLKLWEGLGY 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503252921  90 YSRARNLHAAVKEVNEVYGGMVPNNKAEISRLRGVGPYTAGAILSIAYNIPAPAVDGNVMRVVTRLLLMYDDISKVTTRK 169
Cdd:COG1194   82 YSRARNLHKAAQQVVEEHGGVFPDTYEELLALPGIGPYTAAAIASIAFGEPAPIVDGNVKRVLSRLFAIEGPIGSPAAKK 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503252921 170 KIEAIIEQIISEQHPSEFNQALMELGALICTPRNPACLICPVQLQCRAREEGVQETLPVKAKKAKPKQKNMLALVVKnKA 249
Cdd:COG1194  162 ELWALAEELLPPERPGDFNQALMDLGATVCTPKKPKCLLCPLQDDCAAFAEGRQEELPVKKPKKKKPERYGAALVIR-DD 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503252921 250 GQVLIQKRPETGLLANLWQFPNVE---ADNIEAIVNYMKETAQLEVDVNVTVKQhVKHVFTHLIWEIDVYsgeVGEWGEE 326
Cdd:COG1194  241 GRVLLEKRPPKGLWGGLWEFPEFEweeAEDPEALERWLREELGLEVEWLEPLGT-VRHVFTHFRLHLTVY---LARVPAG 316

                        330       340       350
                 ....*....|....*....|....*....|....
gi 503252921 327 TDLESSSFKFVDKEDIDWYPFPVSHQKIIDRMVK 360
Cdd:COG1194  317 PPAEPDGGRWVPLEELAALPLPAPMRKLLKALLK 350
mutY TIGR01084
A/G-specific adenine glycosylase; This equivalog model identifies mutY members of the ...
 14-276 5.16e-117

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: 340.16  E-value: 5.16e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503252921   14 FQANLLHWYEENKR-DLPWRRERDPYKIWVSEIMLQQTKVDTVIPYYERFISLFPSAKALAEAEEETVLKAWEGLGYYSR 92
Cdd:TIGR01084   2 FSEDLLSWYDKYGRkTLPWRQNKTPYRVWLSEVMLQQTQVATVIPYFERFLERFPTVQALANAPQDEVLKLWEGLGYYAR 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503252921   93 ARNLHAAVKEVNEVYGGMVPNNKAEISRLRGVGPYTAGAILSIAYNIPAPAVDGNVMRVVTRLLLMYDDISKVTTRKKIE 172
Cdd:TIGR01084  82 ARNLHKAAQEVVEEFGGEFPQDFEDLAALPGVGRYTAGAILSFALNKPYPILDGNVKRVLSRLFAVEGWPGKKKVENRLW 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503252921  173 AIIEQIISEQHPSEFNQALMELGALICTPRNPACLICPVQLQCRAREEGVQETLPVKAKKAKPKQKNMLALVVKNKAGQV 252
Cdd:TIGR01084 162 TLAESLLPKADPEAFNQALMDLGAMICTRKKPKCDLCPLQDFCLAYQQGTWEEYPVKKPKAAPPERTTYFLVLQNYDGEV 241

                         250       260
                  ....*....|....*....|....
gi 503252921  253 LIQKRPETGLLANLWQFPNVEADN 276
Cdd:TIGR01084 242 LLEQRPEKGLWGGLYCFPQFEDED 265
PRK10880 PRK10880
adenine DNA glycosylase;
11-270 1.65e-68

adenine DNA glycosylase;


Pssm-ID: 182805 [Multi-domain]  Cd Length: 350  Bit Score: 218.81  E-value: 1.65e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503252921  11 AEDFQANLLHWYEENKRD-LPWRRERDPYKIWVSEIMLQQTKVDTVIPYYERFISLFPSAKALAEAEEETVLKAWEGLGY 89
Cdd:PRK10880   3 ASQFSAQVLDWYDKYGRKtLPWQIDKTPYKVWLSEVMLQQTQVATVIPYFERFMARFPTVTDLANAPLDEVLHLWTGLGY 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503252921  90 YSRARNLHAAVKEVNEVYGGMVPNNKAEISRLRGVGPYTAGAILSIAYNIPAPAVDGNVMRVVTRLLLMYDDISKVTTRK 169
Cdd:PRK10880  83 YARARNLHKAAQQVATLHGGEFPETFEEVAALPGVGRSTAGAILSLSLGKHFPILDGNVKRVLARCYAVSGWPGKKEVEN 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503252921 170 KIEAIIEQIISEQHPSEFNQALMELGALICTPRNPACLICPVQLQCRAREEGVQETLPVKAKKAKPKQKNMLALVVKNkA 249
Cdd:PRK10880 163 RLWQLSEQVTPAVGVERFNQAMMDLGAMVCTRSKPKCELCPLQNGCIAYANHSWALYPGKKPKQTLPERTGYFLLLQH-G 241

                        250       260
                 ....*....|....*....|.
gi 503252921 250 GQVLIQKRPETGLLANLWQFP 270
Cdd:PRK10880 242 DEVWLEQRPPSGLWGGLFCFP 262
ENDO3c cd00056
endonuclease III; includes endonuclease III (DNA-(apurinic or apyrimidinic site) lyase), ...
 38-195 4.27e-45

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: 152.01  E-value: 4.27e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503252921  38 YKIWVSEIMLQQTKVDTVIPYYERFISLF-PSAKALAEAEEETVLKAWEGLGYYSRARNLHAAVKEVNEVYGGMV---PN 113
Cdd:cd00056    1 FEVLVSEILSQQTTDKAVNKAYERLFERYgPTPEALAAADEEELRELIRSLGYRRKAKYLKELARAIVEGFGGLVlddPD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503252921 114 NKAEISRLRGVGPYTAGAILSIAYNIPAPAVDGNVMRVVTRLLLmyddISKVTTRKKIEAIIEQIISEQHPSEFNQALME 193
Cdd:cd00056   81 AREELLALPGVGRKTANVVLLFALGPDAFPVDTHVRRVLKRLGL----IPKKKTPEELEELLEELLPKPYWGEANQALMD 156


                 ..
gi 503252921 194 LG 195
Cdd:cd00056  157 LG 158
ENDO3c smart00478
endonuclease III; includes endonuclease III (DNA-(apurinic or apyrimidinic site) lyase), ...
 46-197 5.07e-39

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: 135.85  E-value: 5.07e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503252921    46 MLQQTKVDTVIPYYERFISLFPSAKALAEAEEETVLKAWEGLG-YYSRARNLHAAVKEVNEVYGGMVPNNKAEISRLRGV 124
Cdd:smart00478   1 LSQQTTDERVNKATERLFEKFPTPEDLAAADEEELEELIRGLGfYRRKARYLIELARILVEEYGGEVPDDREELLKLPGV 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 503252921   125 GPYTAGAILSIAYNIPAPAVDGNVMRVVTRLLLmyddISKVTTRKKIEAIIEQIISEQHPSEFNQALMELGAL 197
Cdd:smart00478  81 GRKTANAVLSFALGKPFIPVDTHVLRIAKRLGL----VDKKSTPEEVEKLLEKLLPEEDWRELNLLLIDFGRT 149
HhH-GPD pfam00730
HhH-GPD superfamily base excision DNA repair protein; This family contains a diverse range of ...
 42-177 9.14e-29

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: 108.53  E-value: 9.14e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503252921   42 VSEIMLQQTKVDTVIPYYERFISL-FPSAKALAEAEEETVLKAWEGLGYY-SRARNLHAAVKEVNEVYGGMVPNNKAEI- 118
Cdd:pfam00730   1 VSAILSQQTSDKAVNKITERLFEKfFPTPEDLADADEEELRELIRGLGFYrRKAKYLKELARILVEGYGGEVPLDEEELe 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 503252921  119 SRLRGVGPYTAGAILSIA--YNIPAPAVDGNVMRVVTRLLLMYDDISKVTTRKKIEAIIEQ 177
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 ...
 10-360 7.56e-168

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: 471.93  E-value: 7.56e-168
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503252921  10 PAEDFQANLLHWYEENKRDLPWRRERDPYKIWVSEIMLQQTKVDTVIPYYERFISLFPSAKALAEAEEETVLKAWEGLGY 89
Cdd:COG1194    2 DMASFAKRLLAWYDRHGRDLPWRQTRDPYRVWLSEIMLQQTQVATVIPYYERFLERFPTVEALAAAPEDEVLKLWEGLGY 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503252921  90 YSRARNLHAAVKEVNEVYGGMVPNNKAEISRLRGVGPYTAGAILSIAYNIPAPAVDGNVMRVVTRLLLMYDDISKVTTRK 169
Cdd:COG1194   82 YSRARNLHKAAQQVVEEHGGVFPDTYEELLALPGIGPYTAAAIASIAFGEPAPIVDGNVKRVLSRLFAIEGPIGSPAAKK 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503252921 170 KIEAIIEQIISEQHPSEFNQALMELGALICTPRNPACLICPVQLQCRAREEGVQETLPVKAKKAKPKQKNMLALVVKnKA 249
Cdd:COG1194  162 ELWALAEELLPPERPGDFNQALMDLGATVCTPKKPKCLLCPLQDDCAAFAEGRQEELPVKKPKKKKPERYGAALVIR-DD 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503252921 250 GQVLIQKRPETGLLANLWQFPNVE---ADNIEAIVNYMKETAQLEVDVNVTVKQhVKHVFTHLIWEIDVYsgeVGEWGEE 326
Cdd:COG1194  241 GRVLLEKRPPKGLWGGLWEFPEFEweeAEDPEALERWLREELGLEVEWLEPLGT-VRHVFTHFRLHLTVY---LARVPAG 316

                        330       340       350
                 ....*....|....*....|....*....|....
gi 503252921 327 TDLESSSFKFVDKEDIDWYPFPVSHQKIIDRMVK 360
Cdd:COG1194  317 PPAEPDGGRWVPLEELAALPLPAPMRKLLKALLK 350
mutY TIGR01084
A/G-specific adenine glycosylase; This equivalog model identifies mutY members of the ...
 14-276 5.16e-117

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: 340.16  E-value: 5.16e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503252921   14 FQANLLHWYEENKR-DLPWRRERDPYKIWVSEIMLQQTKVDTVIPYYERFISLFPSAKALAEAEEETVLKAWEGLGYYSR 92
Cdd:TIGR01084   2 FSEDLLSWYDKYGRkTLPWRQNKTPYRVWLSEVMLQQTQVATVIPYFERFLERFPTVQALANAPQDEVLKLWEGLGYYAR 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503252921   93 ARNLHAAVKEVNEVYGGMVPNNKAEISRLRGVGPYTAGAILSIAYNIPAPAVDGNVMRVVTRLLLMYDDISKVTTRKKIE 172
Cdd:TIGR01084  82 ARNLHKAAQEVVEEFGGEFPQDFEDLAALPGVGRYTAGAILSFALNKPYPILDGNVKRVLSRLFAVEGWPGKKKVENRLW 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503252921  173 AIIEQIISEQHPSEFNQALMELGALICTPRNPACLICPVQLQCRAREEGVQETLPVKAKKAKPKQKNMLALVVKNKAGQV 252
Cdd:TIGR01084 162 TLAESLLPKADPEAFNQALMDLGAMICTRKKPKCDLCPLQDFCLAYQQGTWEEYPVKKPKAAPPERTTYFLVLQNYDGEV 241

                         250       260
                  ....*....|....*....|....
gi 503252921  253 LIQKRPETGLLANLWQFPNVEADN 276
Cdd:TIGR01084 242 LLEQRPEKGLWGGLYCFPQFEDED 265
PRK10880 PRK10880
adenine DNA glycosylase;
11-270 1.65e-68

adenine DNA glycosylase;


Pssm-ID: 182805 [Multi-domain]  Cd Length: 350  Bit Score: 218.81  E-value: 1.65e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503252921  11 AEDFQANLLHWYEENKRD-LPWRRERDPYKIWVSEIMLQQTKVDTVIPYYERFISLFPSAKALAEAEEETVLKAWEGLGY 89
Cdd:PRK10880   3 ASQFSAQVLDWYDKYGRKtLPWQIDKTPYKVWLSEVMLQQTQVATVIPYFERFMARFPTVTDLANAPLDEVLHLWTGLGY 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503252921  90 YSRARNLHAAVKEVNEVYGGMVPNNKAEISRLRGVGPYTAGAILSIAYNIPAPAVDGNVMRVVTRLLLMYDDISKVTTRK 169
Cdd:PRK10880  83 YARARNLHKAAQQVATLHGGEFPETFEEVAALPGVGRSTAGAILSLSLGKHFPILDGNVKRVLARCYAVSGWPGKKEVEN 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503252921 170 KIEAIIEQIISEQHPSEFNQALMELGALICTPRNPACLICPVQLQCRAREEGVQETLPVKAKKAKPKQKNMLALVVKNkA 249
Cdd:PRK10880 163 RLWQLSEQVTPAVGVERFNQAMMDLGAMVCTRSKPKCELCPLQNGCIAYANHSWALYPGKKPKQTLPERTGYFLLLQH-G 241

                        250       260
                 ....*....|....*....|.
gi 503252921 250 GQVLIQKRPETGLLANLWQFP 270
Cdd:PRK10880 242 DEVWLEQRPPSGLWGGLFCFP 262
ENDO3c cd00056
endonuclease III; includes endonuclease III (DNA-(apurinic or apyrimidinic site) lyase), ...
 38-195 4.27e-45

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: 152.01  E-value: 4.27e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503252921  38 YKIWVSEIMLQQTKVDTVIPYYERFISLF-PSAKALAEAEEETVLKAWEGLGYYSRARNLHAAVKEVNEVYGGMV---PN 113
Cdd:cd00056    1 FEVLVSEILSQQTTDKAVNKAYERLFERYgPTPEALAAADEEELRELIRSLGYRRKAKYLKELARAIVEGFGGLVlddPD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503252921 114 NKAEISRLRGVGPYTAGAILSIAYNIPAPAVDGNVMRVVTRLLLmyddISKVTTRKKIEAIIEQIISEQHPSEFNQALME 193
Cdd:cd00056   81 AREELLALPGVGRKTANVVLLFALGPDAFPVDTHVRRVLKRLGL----IPKKKTPEELEELLEELLPKPYWGEANQALMD 156


                 ..
gi 503252921 194 LG 195
Cdd:cd00056  157 LG 158
ENDO3c smart00478
endonuclease III; includes endonuclease III (DNA-(apurinic or apyrimidinic site) lyase), ...
 46-197 5.07e-39

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: 135.85  E-value: 5.07e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503252921    46 MLQQTKVDTVIPYYERFISLFPSAKALAEAEEETVLKAWEGLG-YYSRARNLHAAVKEVNEVYGGMVPNNKAEISRLRGV 124
Cdd:smart00478   1 LSQQTTDERVNKATERLFEKFPTPEDLAAADEEELEELIRGLGfYRRKARYLIELARILVEEYGGEVPDDREELLKLPGV 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 503252921   125 GPYTAGAILSIAYNIPAPAVDGNVMRVVTRLLLmyddISKVTTRKKIEAIIEQIISEQHPSEFNQALMELGAL 197
Cdd:smart00478  81 GRKTANAVLSFALGKPFIPVDTHVLRIAKRLGL----VDKKSTPEEVEKLLEKLLPEEDWRELNLLLIDFGRT 149
Nth COG0177
Endonuclease III [Replication, recombination and repair];
18-216 3.16e-31

Endonuclease III [Replication, recombination and repair];


Pssm-ID: 439947 [Multi-domain]  Cd Length: 198  Bit Score: 117.12  E-value: 3.16e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503252921  18 LLHWYEENKRDLPWRrerDPYKIWVSEIMLQQTKVDTVIPYYERFISLFPSAKALAEAEEETVLKAWEGLGYY-SRARNL 96
Cdd:COG0177    4 LKELYPDAKTELDYR---DPFELLVATILSAQTTDERVNKATPRLFARYPTPEALAAADLEELEELIRPIGLYrNKAKNI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503252921  97 HAAVKEVNEVYGGMVPNNKAEISRLRGVGPYTAGAILSIAYNIPAPAVDGNVMRVVTRLllmydDISKVTTRKKIEAIIE 176
Cdd:COG0177   81 IALARILVEKYGGEVPETREELESLPGVGRKTANVVLNFAFGKPAIAVDTHVHRVSNRL-----GLVPGKDPEEVEKDLM 155

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 503252921 177 QIISEQHPSEFNQALMELGALICTPRNPACLICPVQLQCR 216
Cdd:COG0177  156 KLIPKEYWGDLHHLLILHGRYICKARKPKCEECPLADLCP 195
NUDIX_DNA_Glycosylase_C-MutY cd03431
C-terminal domain of DNA glycosylase; DNA glycosylase (MutY in bacteria and hMYH in humans) is ...
 240-356 9.01e-31

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: 113.17  E-value: 9.01e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503252921 240 MLALVVKNKaGQVLIQKRPETGLLANLWQFPNVEADNIEAIVNYMKETAQLEVDVNVTVKQHVKHVFTHLIWEIDVYsge 319
Cdd:cd03431    6 FTVLVLRDG-GRVLLEKRPEKGLLAGLWEFPLVETEEEEEEAEALLGLLAEELLLILEPLGEVKHVFSHFRLHITVY--- 81

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 503252921 320 VGEWGEETDLESSSFKFVDKEDIDWYPFPVSHQKIID 356
Cdd:cd03431   82 LVELPEAPPAAPDEGRWVDLEELDEYALPAPMRKLLE 118
PRK13910 PRK13910
DNA glycosylase MutY; Provisional
 46-278 4.80e-29

DNA glycosylase MutY; Provisional


Pssm-ID: 172427 [Multi-domain]  Cd Length: 289  Bit Score: 113.58  E-value: 4.80e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503252921  46 MLQQTKVDTVIP-YYERFISLFPSAKALAEAEEETVLKAWEGLGYYSRARNLHAAVKEVNEVYGGMVPNNKAEISRLRGV 124
Cdd:PRK13910   1 MSQQTQINTVVErFYSPFLEAFPTLKDLANAPLEEVLLLWRGLGYYSRAKNLKKSAEICVKEHHSQLPNDYQSLLKLPGI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503252921 125 GPYTAGAILSIAYNIPAPAVDGNVMRVVTRLLLMYDDISKVTTRKKIEAIIEQIISEQHpsefNQALMELGALICTPRnP 204
Cdd:PRK13910  81 GAYTANAILCFGFREKSACVDANIKRVLLRLFGLDPNIHAKDLQIKANDFLNLNESFNH----NQALIDLGALICSPK-P 155

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 503252921 205 ACLICPVQLQCRAREEGVQETLpvKAKKAKPKQKNMLALVVKNKagQVLIQKrPETGLLANLWQFPNVEaDNIE 278
Cdd:PRK13910 156 KCAICPLNPYCLGKNNPEKHTL--KKKQEIVQEERYLGVVIQNN--QIALEK-IEQKLYLGMHHFPNLK-ENLE 223
HhH-GPD pfam00730
HhH-GPD superfamily base excision DNA repair protein; This family contains a diverse range of ...
 42-177 9.14e-29

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: 108.53  E-value: 9.14e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503252921   42 VSEIMLQQTKVDTVIPYYERFISL-FPSAKALAEAEEETVLKAWEGLGYY-SRARNLHAAVKEVNEVYGGMVPNNKAEI- 118
Cdd:pfam00730   1 VSAILSQQTSDKAVNKITERLFEKfFPTPEDLADADEEELRELIRGLGFYrRKAKYLKELARILVEGYGGEVPLDEEELe 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 503252921  119 SRLRGVGPYTAGAILSIA--YNIPAPAVDGNVMRVVTRLLLMYDDISKVTTRKKIEAIIEQ 177
Cdd:pfam00730  81 ALLKGVGRWTAEAVLIFAlgRPDPLPVVDTHVRRVLKRLGLIKEKPTPKEVERELEELWPP 141
NUDIX_4 pfam14815
NUDIX domain;
242-357 1.88e-26

NUDIX domain;


Pssm-ID: 464330 [Multi-domain]  Cd Length: 114  Bit Score: 101.62  E-value: 1.88e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503252921  242 ALVVKNKAGQVLIQKRPETGLLANLWQFPNVEADNIEAIVNYMKETAQLEVDVNVTVKQHVKHVFTHLIWEIDVYsgEVG 321
Cdd:pfam14815   2 VLVIRNGDGRVLLRKRPEKGLLGGLWEFPGGKVEPGETLEEALARLEELGIEVEVLEPGTVKHVFTHFRLTLHVY--LVR 79

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 503252921  322 EWgEETDLESSSFKFVDKEDIDWYPFPVSHQKIIDR 357
Cdd:pfam14815  80 EV-EGEEEPQQELRWVTPEELDKYALPAAVRKILEA 114
nth TIGR01083
endonuclease III; This equivalog model identifes nth members of the pfam00730 superfamily ...
 88-206 9.08e-20

endonuclease III; This equivalog model identifes nth members of the pfam00730 superfamily (HhH-GPD: Helix-hairpin-helix and Gly/Pro rich loop followed by a conserved aspartate). The major members of the superfamily are nth and mutY. [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 273434 [Multi-domain]  Cd Length: 192  Bit Score: 85.89  E-value: 9.08e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503252921   88 GYY-SRARNLHAAVKEVNEVYGGMVPNNKAEISRLRGVGPYTAGAILSIAYNIPAPAVDGNVMRVVTRLllmydDISKVT 166
Cdd:TIGR01083  78 GLYrNKAKNIIELCRKLVERYGGEVPEDREELVKLPGVGRKTANVVLNVAFGIPAIAVDTHVFRVSNRL-----GLSKGK 152

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 503252921  167 TRKKIEAIIEQIISEQHPSEFNQALMELGALICTPRNPAC 206
Cdd:TIGR01083 153 DPIKVEEDLMKLVPREFWVKLHHWLILHGRYTCKARKPLC 192
PRK10702 PRK10702
endonuclease III; Provisional
 89-220 3.99e-10

endonuclease III; Provisional


Pssm-ID: 182661 [Multi-domain]  Cd Length: 211  Bit Score: 58.88  E-value: 3.99e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503252921  89 YYSRARNLHAAVKEVNEVYGGMVPNNKAEISRLRGVGPYTAGAILSIAYNIPAPAVDGNVMRVVTRlllmyddiSKVTTR 168
Cdd:PRK10702  82 YNSKAENVIKTCRILLEQHNGEVPEDRAALEALPGVGRKTANVVLNTAFGWPTIAVDTHIFRVCNR--------TQFAPG 153

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 503252921 169 KKIEAIIEQIIsEQHPSEF----NQALMELGALICTPRNPACLICPVQLQCRAREE 220
Cdd:PRK10702 154 KNVEQVEEKLL-KVVPAEFkvdcHHWLILHGRYTCIARKPRCGSCIIEDLCEYKEK 208
NUDIX_MutT_NudA_like cd03425
MutT pyrophosphohydrolase; The MutT pyrophosphohydrolase is a prototypical NUDIX hydrolase ...
 242-357 7.12e-07

MutT pyrophosphohydrolase; The MutT pyrophosphohydrolase is a prototypical NUDIX hydrolase that catalyzes the hydrolysis of nucleoside and deoxynucleoside triphosphates (NTPs and dNTPs) by substitution at a beta-phosphorus to yield a nucleotide monophosphate (NMP) and inorganic pyrophosphate (PPi). This enzyme requires two divalent cations for activity; one coordinates the phosphoryl groups of the NTP/dNTP substrate, and the other coordinates to the enzyme. It also contains the NUDIX motif, a highly conserved 23-residue block (GX5EX7REUXEEXGU, where U = I, L or V), that functions as metal binding and catalytic site. MutT pyrophosphohydrolase is important in preventing errors in DNA replication by hydrolyzing mutagenic nucleotides such as 8-oxo-dGTP (a product of oxidative damage), which can mispair with template adenine during DNA replication, to guanine nucleotides.


Pssm-ID: 467531 [Multi-domain]  Cd Length: 123  Bit Score: 47.45  E-value: 7.12e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503252921 242 ALVVKNkaGQVLIQKRPETGLLANLWQFP--NVEAD--NIEAIVNYMKEtaqlEVDVNVTVKQH---VKHVFTHLIWEID 314
Cdd:cd03425    6 AIIVDD--GRVLIAQRPEGKHLAGLWEFPggKVEPGetPEQALVRELRE----ELGIEVEVGEPlgtVEHDYPDFHVRLH 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 503252921 315 VYSGEVGEwGEETDLESSSFKFVDKEDIDWYPFPVSHQKIIDR 357
Cdd:cd03425   80 VYLCTLWS-GEPQLLEHQELRWVTPEELDDLDWLPADIPIVEA 121
HP0602 COG2231
3-Methyladenine DNA glycosylase, HhH-GPD/Endo3 superfamily [Replication, recombination and ...
 88-218 1.08e-06

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


Pssm-ID: 441832 [Multi-domain]  Cd Length: 220  Bit Score: 49.07  E-value: 1.08e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503252921  88 GYYSR-ARNLHAAVKEVNEVYGGMVPN-NKAEISRLR-------GVGPYTAGAILSIAYNIPAPAVDGNVMRVVTRLLLM 158
Cdd:COG2231   81 GFYNQkAKRLKNLARWLVERYGGGLEKlKALPTEELReellslkGIGPETADSILLYAFNRPVFVVDAYTRRIFSRLGLI 160

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 503252921 159 YDDISKVTTRKKIEAIIEQiiseqHPSEFNQ--ALM-ELGALICTPRnPACLICPVQLQCRAR 218
Cdd:COG2231  161 EEDASYDELQRLFEENLPP-----DVALYNEfhALIvEHGKEYCKKK-PKCEECPLRDLCPYG 217
PRK08999 PRK08999
Nudix family hydrolase;
242-355 1.15e-04

Nudix family hydrolase;


Pssm-ID: 236361 [Multi-domain]  Cd Length: 312  Bit Score: 43.32  E-value: 1.15e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503252921 242 ALVVKNKAGQVLIQKRPETGLLANLWQFP--NVEADN--IEAIVNYMKETAQLEVDVNVTVKQhVKHVFTHLIWEIDVYs 317
Cdd:PRK08999   9 AGVIRDADGRILLARRPEGKHQGGLWEFPggKVEPGEtvEQALARELQEELGIEVTAARPLIT-VRHDYPDKRVRLDVR- 86

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 503252921 318 gEVGEW-GEETDLESSSFKFVDKEDIDWYPFPVSHQKII 355
Cdd:PRK08999  87 -RVTAWqGEPHGREGQPLAWVAPDELAVYPFPPANQPIV 124
HHH pfam00633
Helix-hairpin-helix motif; The helix-hairpin-helix DNA-binding motif is found to be duplicated ...
 107-135 3.16e-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: 37.40  E-value: 3.16e-04
                          10        20
                  ....*....|....*....|....*....
gi 503252921  107 YGGMVPNNKAEISRLRGVGPYTAGAILSI 135
Cdd:pfam00633   2 LEGLIPASVEELLALPGVGPKTAEAILSY 30
FES smart00525
iron-sulpphur binding domain in DNA-(apurinic or apyrimidinic site) lyase (subfamily of ENDO3); ...
 198-218 3.44e-04

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


Pssm-ID: 197771 [Multi-domain]  Cd Length: 21  Bit Score: 37.53  E-value: 3.44e-04
                           10        20
                   ....*....|....*....|.
gi 503252921   198 ICTPRNPACLICPVQLQCRAR 218
Cdd:smart00525   1 ICTARKPRCDECPLKDLCPAY 21
EndIII_4Fe-2S pfam10576
Iron-sulfur binding domain of endonuclease III; Escherichia coli endonuclease III (EC 4.2.99. ...
 199-215 6.36e-04

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


Pssm-ID: 463153 [Multi-domain]  Cd Length: 17  Bit Score: 36.60  E-value: 6.36e-04
                          10
                  ....*....|....*..
gi 503252921  199 CTPRNPACLICPVQLQC 215
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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