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Conserved domains on  [gi|488999028|ref|WP_002909706|]
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MULTISPECIES: A/G-specific adenine glycosylase [Streptococcus]

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 ...
 16-382 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: 515.07  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999028  16 KIASFREKLLTWYDENKRDLPWRRTNNPYHIWVSEIMLQQTRVDTVIPYYERFLDWFPTVADLAQAPEDRLLKAWEGLGY 95
Cdd:COG1194    2 DMASFAKRLLAWYDRHGRDLPWRQTRDPYRVWLSEIMLQQTQVATVIPYYERFLERFPTVEALAAAPEDEVLKLWEGLGY 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999028  96 YSRVRNMQKAAQQIMTDFAGKFPDSYEGIASLKGIGPYTAGAIASIAFGLAEPAVDGNVMRVLSRLFEVDLDIGQPSNRK 175
Cdd:COG1194   82 YSRARNLHKAAQQVVEEHGGVFPDTYEELLALPGIGPYTAAAIASIAFGEPAPIVDGNVKRVLSRLFAIEGPIGSPAAKK 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999028 176 VFQAMMEILIDPDRPGDFNQALMDLGSDIEAPVNPHPEDNPVKEFSAAYLHGTMDKYPIKAPKKKPVPVYLQGLIIEnEQ 255
Cdd:COG1194  162 ELWALAEELLPPERPGDFNQALMDLGATVCTPKKPKCLLCPLQDDCAAFAEGRQEELPVKKPKKKKPERYGAALVIR-DD 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999028 256 GQFLLEKNEADGLLSGFWHFPLIEIEEFQTENQMslfevaenqssldlspQESFEQDYDLIVDWQQEsFSKVQHIFSHRK 335
Cdd:COG1194  241 GRVLLEKRPPKGLWGGLWEFPEFEWEEAEDPEAL----------------ERWLREELGLEVEWLEP-LGTVRHVFTHFR 303

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*..
gi 488999028 336 WHIQLVYGRVKDSQHAADGEVLWLHPEDFGNYPFAKPQQKMWEAFQD 382
Cdd:COG1194  304 LHLTVYLARVPAGPPAEPDGGRWVPLEELAALPLPAPMRKLLKALLK 350
 
Name Accession Description Interval E-value
MutY COG1194
Adenine-specific DNA glycosylase, acts on AG and A-oxoG pairs [Replication, recombination and ...
 16-382 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: 515.07  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999028  16 KIASFREKLLTWYDENKRDLPWRRTNNPYHIWVSEIMLQQTRVDTVIPYYERFLDWFPTVADLAQAPEDRLLKAWEGLGY 95
Cdd:COG1194    2 DMASFAKRLLAWYDRHGRDLPWRQTRDPYRVWLSEIMLQQTQVATVIPYYERFLERFPTVEALAAAPEDEVLKLWEGLGY 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999028  96 YSRVRNMQKAAQQIMTDFAGKFPDSYEGIASLKGIGPYTAGAIASIAFGLAEPAVDGNVMRVLSRLFEVDLDIGQPSNRK 175
Cdd:COG1194   82 YSRARNLHKAAQQVVEEHGGVFPDTYEELLALPGIGPYTAAAIASIAFGEPAPIVDGNVKRVLSRLFAIEGPIGSPAAKK 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999028 176 VFQAMMEILIDPDRPGDFNQALMDLGSDIEAPVNPHPEDNPVKEFSAAYLHGTMDKYPIKAPKKKPVPVYLQGLIIEnEQ 255
Cdd:COG1194  162 ELWALAEELLPPERPGDFNQALMDLGATVCTPKKPKCLLCPLQDDCAAFAEGRQEELPVKKPKKKKPERYGAALVIR-DD 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999028 256 GQFLLEKNEADGLLSGFWHFPLIEIEEFQTENQMslfevaenqssldlspQESFEQDYDLIVDWQQEsFSKVQHIFSHRK 335
Cdd:COG1194  241 GRVLLEKRPPKGLWGGLWEFPEFEWEEAEDPEAL----------------ERWLREELGLEVEWLEP-LGTVRHVFTHFR 303

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*..
gi 488999028 336 WHIQLVYGRVKDSQHAADGEVLWLHPEDFGNYPFAKPQQKMWEAFQD 382
Cdd:COG1194  304 LHLTVYLARVPAGPPAEPDGGRWVPLEELAALPLPAPMRKLLKALLK 350
mutY TIGR01084
A/G-specific adenine glycosylase; This equivalog model identifies mutY members of the ...
 20-282 3.88e-118

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: 344.01  E-value: 3.88e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999028   20 FREKLLTWYDENKR-DLPWRRTNNPYHIWVSEIMLQQTRVDTVIPYYERFLDWFPTVADLAQAPEDRLLKAWEGLGYYSR 98
Cdd:TIGR01084   2 FSEDLLSWYDKYGRkTLPWRQNKTPYRVWLSEVMLQQTQVATVIPYFERFLERFPTVQALANAPQDEVLKLWEGLGYYAR 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999028   99 VRNMQKAAQQIMTDFAGKFPDSYEGIASLKGIGPYTAGAIASIAFGLAEPAVDGNVMRVLSRLFEVDLDIGQPSNRKVFQ 178
Cdd:TIGR01084  82 ARNLHKAAQEVVEEFGGEFPQDFEDLAALPGVGRYTAGAILSFALNKPYPILDGNVKRVLSRLFAVEGWPGKKKVENRLW 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999028  179 AMMEILIDPDRPGDFNQALMDLGSDIEAPVNPHPEDNPVKEFSAAYLHGTMDKYPIKAPKKKPVPVYLQGLIIENEQGQF 258
Cdd:TIGR01084 162 TLAESLLPKADPEAFNQALMDLGAMICTRKKPKCDLCPLQDFCLAYQQGTWEEYPVKKPKAAPPERTTYFLVLQNYDGEV 241

                         250       260
                  ....*....|....*....|....
gi 488999028  259 LLEKNEADGLLSGFWHFPLIEIEE 282
Cdd:TIGR01084 242 LLEQRPEKGLWGGLYCFPQFEDED 265
PRK10880 PRK10880
adenine DNA glycosylase;
20-360 5.34e-73

adenine DNA glycosylase;


Pssm-ID: 182805 [Multi-domain]  Cd Length: 350  Bit Score: 231.52  E-value: 5.34e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999028  20 FREKLLTWYDENKRD-LPWRRTNNPYHIWVSEIMLQQTRVDTVIPYYERFLDWFPTVADLAQAPEDRLLKAWEGLGYYSR 98
Cdd:PRK10880   6 FSAQVLDWYDKYGRKtLPWQIDKTPYKVWLSEVMLQQTQVATVIPYFERFMARFPTVTDLANAPLDEVLHLWTGLGYYAR 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999028  99 VRNMQKAAQQIMTDFAGKFPDSYEGIASLKGIGPYTAGAIASIAFGLAEPAVDGNVMRVLSRLFEVDldiGQPSNRKVFQ 178
Cdd:PRK10880  86 ARNLHKAAQQVATLHGGEFPETFEEVAALPGVGRSTAGAILSLSLGKHFPILDGNVKRVLARCYAVS---GWPGKKEVEN 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999028 179 AMMEI---LIDPDRPGDFNQALMDLGSDIEAPVNPHPEDNPVKEFSAAYLHGTMDKYPIKAPKKKpVPV---YLqgLIIE 252
Cdd:PRK10880 163 RLWQLseqVTPAVGVERFNQAMMDLGAMVCTRSKPKCELCPLQNGCIAYANHSWALYPGKKPKQT-LPErtgYF--LLLQ 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999028 253 NEQgQFLLEKNEADGLLSGFWHFPlieieEFQTENQMSLFEVAENQSSLDLSPQESFeqdydlivdwqqesfskvQHIFS 332
Cdd:PRK10880 240 HGD-EVWLEQRPPSGLWGGLFCFP-----QFADEEELRQWLAQRGIAADNLTQLTAF------------------RHTFS 295

                        330       340       350
                 ....*....|....*....|....*....|.
gi 488999028 333 HrkWHIQLVYGRVKDSQHAA---DGEVLWLH 360
Cdd:PRK10880 296 H--FHLDIVPMWLPVSSFTGcmdEGNGLWYN 324
ENDO3c cd00056
endonuclease III; includes endonuclease III (DNA-(apurinic or apyrimidinic site) lyase), ...
 44-201 6.30e-53

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: 172.81  E-value: 6.30e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999028  44 YHIWVSEIMLQQTRVDTVIPYYERFLD-WFPTVADLAQAPEDRLLKAWEGLGYYSRVRNMQKAAQQIMTDFAGKF---PD 119
Cdd:cd00056    1 FEVLVSEILSQQTTDKAVNKAYERLFErYGPTPEALAAADEEELRELIRSLGYRRKAKYLKELARAIVEGFGGLVlddPD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999028 120 SYEGIASLKGIGPYTAGAIASIAFGLAEPAVDGNVMRVLSRLFevdlDIGQPSNRKVFQAMMEILIDPDRPGDFNQALMD 199
Cdd:cd00056   81 AREELLALPGVGRKTANVVLLFALGPDAFPVDTHVRRVLKRLG----LIPKKKTPEELEELLEELLPKPYWGEANQALMD 156


                 ..
gi 488999028 200 LG 201
Cdd:cd00056  157 LG 158
ENDO3c smart00478
endonuclease III; includes endonuclease III (DNA-(apurinic or apyrimidinic site) lyase), ...
 52-201 2.75e-40

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: 139.71  E-value: 2.75e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999028    52 MLQQTRVDTVIPYYERFLDWFPTVADLAQAPEDRLLKAWEGLG-YYSRVRNMQKAAQQIMTDFAGKFPDSYEGIASLKGI 130
Cdd:smart00478   1 LSQQTTDERVNKATERLFEKFPTPEDLAAADEEELEELIRGLGfYRRKARYLIELARILVEEYGGEVPDDREELLKLPGV 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488999028   131 GPYTAGAIASIAFGLAEPAVDGNVMRVLSRLFEVDLdigqPSNRKVFQAMMEILIDPDRPGDFNQALMDLG 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 1.23e-34

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: 124.70  E-value: 1.23e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999028   48 VSEIMLQQTRVDTVIPYYERFLD-WFPTVADLAQAPEDRLLKAWEGLGYY-SRVRNMQKAAQQIMTDFAGKFPDSY-EGI 124
Cdd:pfam00730   1 VSAILSQQTSDKAVNKITERLFEkFFPTPEDLADADEEELRELIRGLGFYrRKAKYLKELARILVEGYGGEVPLDEeELE 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488999028  125 ASLKGIGPYTAGAIASIAFGLAE--PAVDGNVMRVLSRLFEVDldiGQPSNRKVFQAMMEIL 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 ...
 16-382 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: 515.07  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999028  16 KIASFREKLLTWYDENKRDLPWRRTNNPYHIWVSEIMLQQTRVDTVIPYYERFLDWFPTVADLAQAPEDRLLKAWEGLGY 95
Cdd:COG1194    2 DMASFAKRLLAWYDRHGRDLPWRQTRDPYRVWLSEIMLQQTQVATVIPYYERFLERFPTVEALAAAPEDEVLKLWEGLGY 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999028  96 YSRVRNMQKAAQQIMTDFAGKFPDSYEGIASLKGIGPYTAGAIASIAFGLAEPAVDGNVMRVLSRLFEVDLDIGQPSNRK 175
Cdd:COG1194   82 YSRARNLHKAAQQVVEEHGGVFPDTYEELLALPGIGPYTAAAIASIAFGEPAPIVDGNVKRVLSRLFAIEGPIGSPAAKK 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999028 176 VFQAMMEILIDPDRPGDFNQALMDLGSDIEAPVNPHPEDNPVKEFSAAYLHGTMDKYPIKAPKKKPVPVYLQGLIIEnEQ 255
Cdd:COG1194  162 ELWALAEELLPPERPGDFNQALMDLGATVCTPKKPKCLLCPLQDDCAAFAEGRQEELPVKKPKKKKPERYGAALVIR-DD 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999028 256 GQFLLEKNEADGLLSGFWHFPLIEIEEFQTENQMslfevaenqssldlspQESFEQDYDLIVDWQQEsFSKVQHIFSHRK 335
Cdd:COG1194  241 GRVLLEKRPPKGLWGGLWEFPEFEWEEAEDPEAL----------------ERWLREELGLEVEWLEP-LGTVRHVFTHFR 303

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*..
gi 488999028 336 WHIQLVYGRVKDSQHAADGEVLWLHPEDFGNYPFAKPQQKMWEAFQD 382
Cdd:COG1194  304 LHLTVYLARVPAGPPAEPDGGRWVPLEELAALPLPAPMRKLLKALLK 350
mutY TIGR01084
A/G-specific adenine glycosylase; This equivalog model identifies mutY members of the ...
 20-282 3.88e-118

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: 344.01  E-value: 3.88e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999028   20 FREKLLTWYDENKR-DLPWRRTNNPYHIWVSEIMLQQTRVDTVIPYYERFLDWFPTVADLAQAPEDRLLKAWEGLGYYSR 98
Cdd:TIGR01084   2 FSEDLLSWYDKYGRkTLPWRQNKTPYRVWLSEVMLQQTQVATVIPYFERFLERFPTVQALANAPQDEVLKLWEGLGYYAR 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999028   99 VRNMQKAAQQIMTDFAGKFPDSYEGIASLKGIGPYTAGAIASIAFGLAEPAVDGNVMRVLSRLFEVDLDIGQPSNRKVFQ 178
Cdd:TIGR01084  82 ARNLHKAAQEVVEEFGGEFPQDFEDLAALPGVGRYTAGAILSFALNKPYPILDGNVKRVLSRLFAVEGWPGKKKVENRLW 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999028  179 AMMEILIDPDRPGDFNQALMDLGSDIEAPVNPHPEDNPVKEFSAAYLHGTMDKYPIKAPKKKPVPVYLQGLIIENEQGQF 258
Cdd:TIGR01084 162 TLAESLLPKADPEAFNQALMDLGAMICTRKKPKCDLCPLQDFCLAYQQGTWEEYPVKKPKAAPPERTTYFLVLQNYDGEV 241

                         250       260
                  ....*....|....*....|....
gi 488999028  259 LLEKNEADGLLSGFWHFPLIEIEE 282
Cdd:TIGR01084 242 LLEQRPEKGLWGGLYCFPQFEDED 265
PRK10880 PRK10880
adenine DNA glycosylase;
20-360 5.34e-73

adenine DNA glycosylase;


Pssm-ID: 182805 [Multi-domain]  Cd Length: 350  Bit Score: 231.52  E-value: 5.34e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999028  20 FREKLLTWYDENKRD-LPWRRTNNPYHIWVSEIMLQQTRVDTVIPYYERFLDWFPTVADLAQAPEDRLLKAWEGLGYYSR 98
Cdd:PRK10880   6 FSAQVLDWYDKYGRKtLPWQIDKTPYKVWLSEVMLQQTQVATVIPYFERFMARFPTVTDLANAPLDEVLHLWTGLGYYAR 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999028  99 VRNMQKAAQQIMTDFAGKFPDSYEGIASLKGIGPYTAGAIASIAFGLAEPAVDGNVMRVLSRLFEVDldiGQPSNRKVFQ 178
Cdd:PRK10880  86 ARNLHKAAQQVATLHGGEFPETFEEVAALPGVGRSTAGAILSLSLGKHFPILDGNVKRVLARCYAVS---GWPGKKEVEN 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999028 179 AMMEI---LIDPDRPGDFNQALMDLGSDIEAPVNPHPEDNPVKEFSAAYLHGTMDKYPIKAPKKKpVPV---YLqgLIIE 252
Cdd:PRK10880 163 RLWQLseqVTPAVGVERFNQAMMDLGAMVCTRSKPKCELCPLQNGCIAYANHSWALYPGKKPKQT-LPErtgYF--LLLQ 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999028 253 NEQgQFLLEKNEADGLLSGFWHFPlieieEFQTENQMSLFEVAENQSSLDLSPQESFeqdydlivdwqqesfskvQHIFS 332
Cdd:PRK10880 240 HGD-EVWLEQRPPSGLWGGLFCFP-----QFADEEELRQWLAQRGIAADNLTQLTAF------------------RHTFS 295

                        330       340       350
                 ....*....|....*....|....*....|.
gi 488999028 333 HrkWHIQLVYGRVKDSQHAA---DGEVLWLH 360
Cdd:PRK10880 296 H--FHLDIVPMWLPVSSFTGcmdEGNGLWYN 324
ENDO3c cd00056
endonuclease III; includes endonuclease III (DNA-(apurinic or apyrimidinic site) lyase), ...
 44-201 6.30e-53

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: 172.81  E-value: 6.30e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999028  44 YHIWVSEIMLQQTRVDTVIPYYERFLD-WFPTVADLAQAPEDRLLKAWEGLGYYSRVRNMQKAAQQIMTDFAGKF---PD 119
Cdd:cd00056    1 FEVLVSEILSQQTTDKAVNKAYERLFErYGPTPEALAAADEEELRELIRSLGYRRKAKYLKELARAIVEGFGGLVlddPD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999028 120 SYEGIASLKGIGPYTAGAIASIAFGLAEPAVDGNVMRVLSRLFevdlDIGQPSNRKVFQAMMEILIDPDRPGDFNQALMD 199
Cdd:cd00056   81 AREELLALPGVGRKTANVVLLFALGPDAFPVDTHVRRVLKRLG----LIPKKKTPEELEELLEELLPKPYWGEANQALMD 156


                 ..
gi 488999028 200 LG 201
Cdd:cd00056  157 LG 158
ENDO3c smart00478
endonuclease III; includes endonuclease III (DNA-(apurinic or apyrimidinic site) lyase), ...
 52-201 2.75e-40

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: 139.71  E-value: 2.75e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999028    52 MLQQTRVDTVIPYYERFLDWFPTVADLAQAPEDRLLKAWEGLG-YYSRVRNMQKAAQQIMTDFAGKFPDSYEGIASLKGI 130
Cdd:smart00478   1 LSQQTTDERVNKATERLFEKFPTPEDLAAADEEELEELIRGLGfYRRKARYLIELARILVEEYGGEVPDDREELLKLPGV 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488999028   131 GPYTAGAIASIAFGLAEPAVDGNVMRVLSRLFEVDLdigqPSNRKVFQAMMEILIDPDRPGDFNQALMDLG 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 1.23e-34

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: 124.70  E-value: 1.23e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999028   48 VSEIMLQQTRVDTVIPYYERFLD-WFPTVADLAQAPEDRLLKAWEGLGYY-SRVRNMQKAAQQIMTDFAGKFPDSY-EGI 124
Cdd:pfam00730   1 VSAILSQQTSDKAVNKITERLFEkFFPTPEDLADADEEELRELIRGLGFYrRKAKYLKELARILVEGYGGEVPLDEeELE 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488999028  125 ASLKGIGPYTAGAIASIAFGLAE--PAVDGNVMRVLSRLFEVDldiGQPSNRKVFQAMMEIL 184
Cdd:pfam00730  81 ALLKGVGRWTAEAVLIFALGRPDplPVVDTHVRRVLKRLGLIK---EKPTPKEVERELEELW 139
PRK13910 PRK13910
DNA glycosylase MutY; Provisional
 52-276 4.57e-29

DNA glycosylase MutY; Provisional


Pssm-ID: 172427 [Multi-domain]  Cd Length: 289  Bit Score: 114.35  E-value: 4.57e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999028  52 MLQQTRVDTVIP-YYERFLDWFPTVADLAQAPEDRLLKAWEGLGYYSRVRNMQKAAQQIMTDFAGKFPDSYEGIASLKGI 130
Cdd:PRK13910   1 MSQQTQINTVVErFYSPFLEAFPTLKDLANAPLEEVLLLWRGLGYYSRAKNLKKSAEICVKEHHSQLPNDYQSLLKLPGI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999028 131 GPYTAGAIASIAFGLAEPAVDGNVMRVLSRLFEVDLDIgqpsNRKVFQAMMEILIDPDRPGDFNQALMDLGSDIEAPvNP 210
Cdd:PRK13910  81 GAYTANAILCFGFREKSACVDANIKRVLLRLFGLDPNI----HAKDLQIKANDFLNLNESFNHNQALIDLGALICSP-KP 155

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488999028 211 HPEDNPVKEFSAAYLHgtMDKYPIKAPKKKPVPVYLQGLIIENEqgQFLLEKNEADgLLSGFWHFP 276
Cdd:PRK13910 156 KCAICPLNPYCLGKNN--PEKHTLKKKQEIVQEERYLGVVIQNN--QIALEKIEQK-LYLGMHHFP 216
NUDIX_DNA_Glycosylase_C-MutY cd03431
C-terminal domain of DNA glycosylase; DNA glycosylase (MutY in bacteria and hMYH in humans) is ...
 241-378 8.81e-26

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: 100.46  E-value: 8.81e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999028 241 PVPVYLQGLIIENEqGQFLLEKNEADGLLSGFWHFPLIEIEEfqtenqmslfevaenqsslDLSPQESFEQDYDLIVDWQ 320
Cdd:cd03431    1 VPERYFTVLVLRDG-GRVLLEKRPEKGLLAGLWEFPLVETEE-------------------EEEEAEALLGLLAEELLLI 60

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 488999028 321 QESFSKVQHIFSHRKWHIQLVYGRVKDSQHAADGEVLWLHPEDFGNYPFAKPQQKMWE 378
Cdd:cd03431   61 LEPLGEVKHVFSHFRLHITVYLVELPEAPPAAPDEGRWVDLEELDEYALPAPMRKLLE 118
Nth COG0177
Endonuclease III [Replication, recombination and repair];
22-220 1.67e-25

Endonuclease III [Replication, recombination and repair];


Pssm-ID: 439947 [Multi-domain]  Cd Length: 198  Bit Score: 102.10  E-value: 1.67e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999028  22 EKLLTWYDENKRDLPWRrtnNPYHIWVSEIMLQQTRVDTVIPYYERFLDWFPTVADLAQAPEDRLLKAWEGLGYY-SRVR 100
Cdd:COG0177    2 ERLKELYPDAKTELDYR---DPFELLVATILSAQTTDERVNKATPRLFARYPTPEALAAADLEELEELIRPIGLYrNKAK 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999028 101 NMQKAAQQIMTDFAGKFPDSYEGIASLKGIGPYTAGAIASIAFGLAEPAVDGNVMRVLSRLfevdldiG--QPSN-RKVF 177
Cdd:COG0177   79 NIIALARILVEKYGGEVPETREELESLPGVGRKTANVVLNFAFGKPAIAVDTHVHRVSNRL-------GlvPGKDpEEVE 151

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 488999028 178 QAMMEIlIDPDRPGDFNQALMDLGSDIEAPVNPHPEDNPVKEF 220
Cdd:COG0177  152 KDLMKL-IPKEYWGDLHHLLILHGRYICKARKPKCEECPLADL 193
NUDIX_4 pfam14815
NUDIX domain;
249-379 8.75e-18

NUDIX domain;


Pssm-ID: 464330 [Multi-domain]  Cd Length: 114  Bit Score: 78.51  E-value: 8.75e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999028  249 LIIENEQGQFLLEKNEADGLLSGFWHFPLIEIEEFQTENQmSLFEVAENQssldlspqesfeqdydlIVDWQQESFSkVQ 328
Cdd:pfam14815   3 LVIRNGDGRVLLRKRPEKGLLGGLWEFPGGKVEPGETLEE-ALARLEELG-----------------IEVEVLEPGT-VK 63

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 488999028  329 HIFSHRKWHIQLVYGRVKDSQHAADGEVLWLHPEDFGNYPFAKPQQKMWEA 379
Cdd:pfam14815  64 HVFTHFRLTLHVYLVREVEGEEEPQQELRWVTPEELDKYALPAAVRKILEA 114
AlkA COG0122
3-methyladenine DNA glycosylase/8-oxoguanine DNA glycosylase [Replication, recombination and ...
 33-182 1.38e-06

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


Pssm-ID: 439892 [Multi-domain]  Cd Length: 255  Bit Score: 49.11  E-value: 1.38e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999028  33 RDLPWRRTNNPYHIWVSEIMLQQ--------------TRVDTVIPYYERFLDWFPTVADLAQAPEDRLLKAweGLGYYsR 98
Cdd:COG0122   74 PGLRLPRRPDPFEALVRAILGQQvsvaaartiwrrlvALFGEPIEGPGGGLYAFPTPEALAAASEEELRAC--GLSRR-K 150

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999028  99 VRNMQKAAQQIMT---DFAGKFPDSYEGIA----SLKGIGPYTAGAIASIAFGLAE--PAVDGNVMRVLSRLFevdlDIG 169
Cdd:COG0122  151 ARYLRALARAVADgelDLEALAGLDDEEAIarltALPGIGPWTAEMVLLFALGRPDafPAGDLGLRRALGRLY----GLG 226

                        170
                 ....*....|...
gi 488999028 170 QPSNRKVFQAMME 182
Cdd:COG0122  227 ERPTPKELRELAE 239
HHH pfam00633
Helix-hairpin-helix motif; The helix-hairpin-helix DNA-binding motif is found to be duplicated ...
 112-141 9.81e-06

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: 42.02  E-value: 9.81e-06
                          10        20        30
                  ....*....|....*....|....*....|
gi 488999028  112 DFAGKFPDSYEGIASLKGIGPYTAGAIASI 141
Cdd:pfam00633   1 SLEGLIPASVEELLALPGVGPKTAEAILSY 30
PRK10702 PRK10702
endonuclease III; Provisional
 78-160 9.26e-05

endonuclease III; Provisional


Pssm-ID: 182661 [Multi-domain]  Cd Length: 211  Bit Score: 43.08  E-value: 9.26e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999028  78 LAQAPEDRLLKAWEGLGYY--------SRVRNMQKAAQQIMTDFAGKFPDSYEGIASLKGIGPYTAGAIASIAFGLAEPA 149
Cdd:PRK10702  57 VANTPAAMLELGVEGVKTYiktiglynSKAENVIKTCRILLEQHNGEVPEDRAALEALPGVGRKTANVVLNTAFGWPTIA 136

                         90
                 ....*....|.
gi 488999028 150 VDGNVMRVLSR 160
Cdd:PRK10702 137 VDTHIFRVCNR 147
PRK10546 PRK10546
pyrimidine (deoxy)nucleoside triphosphate diphosphatase;
250-384 1.05e-03

pyrimidine (deoxy)nucleoside triphosphate diphosphatase;


Pssm-ID: 182536 [Multi-domain]  Cd Length: 135  Bit Score: 38.95  E-value: 1.05e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488999028 250 IIENEqGQFLLEKNEADGLLSGFWHFPLIEIEEFQTENQMSLFEVAEnQSSLDLSPQesfeqdyDLIVDWQQESFSKVQH 329
Cdd:PRK10546  10 IIERD-GKILLAQRPAHSDQAGLWEFAGGKVEPGESQPQALIRELRE-ELGIEATVG-------EYVASHQREVSGRRIH 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 488999028 330 IFShrkWHIQLVYGRVKDSQHAAdgeVLWLHPEDFGNYPFAKPQQKMWEAFQDVR 384
Cdd:PRK10546  81 LHA---WHVPDFHGELQAHEHQA---LVWCTPEEALRYPLAPADIPLLEAFMALR 129
 
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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