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Conserved domains on  [gi|1758688337|gb|KAB2470543|]
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A/G-specific adenine glycosylase [Bacillus cereus]

Protein Classification

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

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

CATH:  3.90.79.10|1.10.340.30|1.10.1670.10
EC:  3.2.2.31
Gene Ontology:  GO:0046872|GO:0000701|GO:0006284|GO:0051539|GO:0019104|GO:0016798
PubMed:  21764637|19778963|2682664
SCOP:  4001144|4001553

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
MutY COG1194
Adenine-specific DNA glycosylase, acts on AG and A-oxoG pairs [Replication, recombination and ...
 9-356 0e+00

Adenine-specific DNA glycosylase, acts on AG and A-oxoG pairs [Replication, recombination and repair];


:

Pssm-ID: 440807 [Multi-domain]  Cd Length: 350  Bit Score: 526.63  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758688337   9 FNIEQFQNDLIGWFEEEQRDLPWRKNKDPYRVWVSEIMLQQTRVEAVKPYYANFMGKFPTLEALANADDEEVLKAWEGLG 88
Cdd:COG1194     1 MDMASFAKRLLAWYDRHGRDLPWRQTRDPYRVWLSEIMLQQTQVATVIPYYERFLERFPTVEALAAAPEDEVLKLWEGLG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758688337  89 YYSRARNLHAAVKEVKEVYGGVVPSDVKKIEKLKGVGPYTKGAILSIAYGIPEPAVDGNVMRVLSRILSVWDDIAKPKTR 168
Cdd:COG1194    81 YYSRARNLHKAAQQVVEEHGGVFPDTYEELLALPGIGPYTAAAIASIAFGEPAPIVDGNVKRVLSRLFAIEGPIGSPAAK 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758688337 169 KVFEEIVREIISVENPSYFNQGLMELGALICIPKNPSCLLCPVREHCRGYAEGVQKELPVKSKAKAPKMVPIVAGVLQtE 248
Cdd:COG1194   161 KELWALAEELLPPERPGDFNQALMDLGATVCTPKKPKCLLCPLQDDCAAFAEGRQEELPVKKPKKKKPERYGAALVIR-D 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758688337 249 DGRYVINKRPSTGLLANMWEFPNAELGEGIrnQKEQLIDYMKEKFELAVSIDEYAMNVQHTFTHRTWDIFVFYGKVTGNI 328
Cdd:COG1194   240 DGRVLLEKRPPKGLWGGLWEFPEFEWEEAE--DPEALERWLREELGLEVEWLEPLGTVRHVFTHFRLHLTVYLARVPAGP 317

                         330       340
                  ....*....|....*....|....*....
gi 1758688337 329 -VDTDTLKFVSKEAFEQLPFSKSHRTIYE 356
Cdd:COG1194   318 pAEPDGGRWVPLEELAALPLPAPMRKLLK 346
 
Name Accession Description Interval E-value
MutY COG1194
Adenine-specific DNA glycosylase, acts on AG and A-oxoG pairs [Replication, recombination and ...
 9-356 0e+00

Adenine-specific DNA glycosylase, acts on AG and A-oxoG pairs [Replication, recombination and repair];


Pssm-ID: 440807 [Multi-domain]  Cd Length: 350  Bit Score: 526.63  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758688337   9 FNIEQFQNDLIGWFEEEQRDLPWRKNKDPYRVWVSEIMLQQTRVEAVKPYYANFMGKFPTLEALANADDEEVLKAWEGLG 88
Cdd:COG1194     1 MDMASFAKRLLAWYDRHGRDLPWRQTRDPYRVWLSEIMLQQTQVATVIPYYERFLERFPTVEALAAAPEDEVLKLWEGLG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758688337  89 YYSRARNLHAAVKEVKEVYGGVVPSDVKKIEKLKGVGPYTKGAILSIAYGIPEPAVDGNVMRVLSRILSVWDDIAKPKTR 168
Cdd:COG1194    81 YYSRARNLHKAAQQVVEEHGGVFPDTYEELLALPGIGPYTAAAIASIAFGEPAPIVDGNVKRVLSRLFAIEGPIGSPAAK 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758688337 169 KVFEEIVREIISVENPSYFNQGLMELGALICIPKNPSCLLCPVREHCRGYAEGVQKELPVKSKAKAPKMVPIVAGVLQtE 248
Cdd:COG1194   161 KELWALAEELLPPERPGDFNQALMDLGATVCTPKKPKCLLCPLQDDCAAFAEGRQEELPVKKPKKKKPERYGAALVIR-D 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758688337 249 DGRYVINKRPSTGLLANMWEFPNAELGEGIrnQKEQLIDYMKEKFELAVSIDEYAMNVQHTFTHRTWDIFVFYGKVTGNI 328
Cdd:COG1194   240 DGRVLLEKRPPKGLWGGLWEFPEFEWEEAE--DPEALERWLREELGLEVEWLEPLGTVRHVFTHFRLHLTVYLARVPAGP 317

                         330       340
                  ....*....|....*....|....*....
gi 1758688337 329 -VDTDTLKFVSKEAFEQLPFSKSHRTIYE 356
Cdd:COG1194   318 pAEPDGGRWVPLEELAALPLPAPMRKLLK 346
mutY TIGR01084
A/G-specific adenine glycosylase; This equivalog model identifies mutY members of the ...
 13-279 7.03e-139

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: 395.63  E-value: 7.03e-139
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758688337  13 QFQNDLIGWFEEEQR-DLPWRKNKDPYRVWVSEIMLQQTRVEAVKPYYANFMGKFPTLEALANADDEEVLKAWEGLGYYS 91
Cdd:TIGR01084   1 QFSEDLLSWYDKYGRkTLPWRQNKTPYRVWLSEVMLQQTQVATVIPYFERFLERFPTVQALANAPQDEVLKLWEGLGYYA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758688337  92 RARNLHAAVKEVKEVYGGVVPSDVKKIEKLKGVGPYTKGAILSIAYGIPEPAVDGNVMRVLSRILSVWDDIAKPKTRKVF 171
Cdd:TIGR01084  81 RARNLHKAAQEVVEEFGGEFPQDFEDLAALPGVGRYTAGAILSFALNKPYPILDGNVKRVLSRLFAVEGWPGKKKVENRL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758688337 172 EEIVREIISVENPSYFNQGLMELGALICIPKNPSCLLCPVREHCRGYAEGVQKELPVKSKAKAPKMVPIVAGVLQTEDGR 251
Cdd:TIGR01084 161 WTLAESLLPKADPEAFNQALMDLGAMICTRKKPKCDLCPLQDFCLAYQQGTWEEYPVKKPKAAPPERTTYFLVLQNYDGE 240

                         250       260
                  ....*....|....*....|....*...
gi 1758688337 252 YVINKRPSTGLLANMWEFPNAELGEGIR 279
Cdd:TIGR01084 241 VLLEQRPEKGLWGGLYCFPQFEDEDSLA 268
PRK10880 PRK10880
adenine DNA glycosylase;
12-317 4.15e-73

adenine DNA glycosylase;


Pssm-ID: 182805 [Multi-domain]  Cd Length: 350  Bit Score: 230.75  E-value: 4.15e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758688337  12 EQFQNDLIGWFEEEQRD-LPWRKNKDPYRVWVSEIMLQQTRVEAVKPYYANFMGKFPTLEALANADDEEVLKAWEGLGYY 90
Cdd:PRK10880    4 SQFSAQVLDWYDKYGRKtLPWQIDKTPYKVWLSEVMLQQTQVATVIPYFERFMARFPTVTDLANAPLDEVLHLWTGLGYY 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758688337  91 SRARNLHAAVKEVKEVYGGVVPSDVKKIEKLKGVGPYTKGAILSIAYGIPEPAVDGNVMRVLSRILSV--WDdiAKPKTR 168
Cdd:PRK10880   84 ARARNLHKAAQQVATLHGGEFPETFEEVAALPGVGRSTAGAILSLSLGKHFPILDGNVKRVLARCYAVsgWP--GKKEVE 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758688337 169 KVFEEIVREIISVENPSYFNQGLMELGALICIPKNPSCLLCPVREHCRGYAEGVQKELPVKskaKAPKMVPIVAG--VLQ 246
Cdd:PRK10880  162 NRLWQLSEQVTPAVGVERFNQAMMDLGAMVCTRSKPKCELCPLQNGCIAYANHSWALYPGK---KPKQTLPERTGyfLLL 238

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1758688337 247 TEDGRYVINKRPSTGLLANMWEFPNAElgegirnQKEQLIDYMKEKfELAVSIDEYAMNVQHTFTHRTWDI 317
Cdd:PRK10880  239 QHGDEVWLEQRPPSGLWGGLFCFPQFA-------DEEELRQWLAQR-GIAADNLTQLTAFRHTFSHFHLDI 301
ENDO3c cd00056
endonuclease III; includes endonuclease III (DNA-(apurinic or apyrimidinic site) lyase), ...
 38-195 9.24e-58

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: 184.75  E-value: 9.24e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758688337  38 YRVWVSEIMLQQTRVEAVKPYYANFMGKF-PTLEALANADDEEVLKAWEGLGYYSRARNLHAAVKEVKEVYGGVV---PS 113
Cdd:cd00056     1 FEVLVSEILSQQTTDKAVNKAYERLFERYgPTPEALAAADEEELRELIRSLGYRRKAKYLKELARAIVEGFGGLVlddPD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758688337 114 DVKKIEKLKGVGPYTKGAILSIAYGIPEPAVDGNVMRVLSRilsvWDDIAKPKTRKVFEEIVREIISVENPSYFNQGLME 193
Cdd:cd00056    81 AREELLALPGVGRKTANVVLLFALGPDAFPVDTHVRRVLKR----LGLIPKKKTPEELEELLEELLPKPYWGEANQALMD 156


                  ..
gi 1758688337 194 LG 195
Cdd:cd00056   157 LG 158
ENDO3c smart00478
endonuclease III; includes endonuclease III (DNA-(apurinic or apyrimidinic site) lyase), ...
 46-197 2.52e-47

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: 157.43  E-value: 2.52e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758688337   46 MLQQTRVEAVKPYYANFMGKFPTLEALANADDEEVLKAWEGLG-YYSRARNLHAAVKEVKEVYGGVVPSDVKKIEKLKGV 124
Cdd:smart00478   1 LSQQTTDERVNKATERLFEKFPTPEDLAAADEEELEELIRGLGfYRRKARYLIELARILVEEYGGEVPDDREELLKLPGV 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1758688337  125 GPYTKGAILSIAYGIPEPAVDGNVMRVLSRILSVWddiaKPKTRKVFEEIVREIISVENPSYFNQGLMELGAL 197
Cdd:smart00478  81 GRKTANAVLSFALGKPFIPVDTHVLRIAKRLGLVD----KKSTPEEVEKLLEKLLPEEDWRELNLLLIDFGRT 149
HhH-GPD pfam00730
HhH-GPD superfamily base excision DNA repair protein; This family contains a diverse range of ...
 42-177 8.21e-41

HhH-GPD superfamily base excision DNA repair protein; This family contains a diverse range of structurally related DNA repair proteins. The superfamily is called the HhH-GPD family after its hallmark Helix-hairpin-helix and Gly/Pro rich loop followed by a conserved aspartate. This includes endonuclease III, EC:4.2.99.18 and MutY an A/G-specific adenine glycosylase, both have a C terminal 4Fe-4S cluster. The family also includes 8-oxoguanine DNA glycosylases. The methyl-CPG binding protein MBD4 also contains a related domain that is a thymine DNA glycosylase. The family also includes DNA-3-methyladenine glycosylase II EC:3.2.2.21 and other members of the AlkA family.


Pssm-ID: 425841 [Multi-domain]  Cd Length: 141  Bit Score: 140.50  E-value: 8.21e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758688337  42 VSEIMLQQTRVEAVKPYYANFMGK-FPTLEALANADDEEVLKAWEGLGYY-SRARNLHAAVKEVKEVYGGVVPSDVKKIE 119
Cdd:pfam00730   1 VSAILSQQTSDKAVNKITERLFEKfFPTPEDLADADEEELRELIRGLGFYrRKAKYLKELARILVEGYGGEVPLDEEELE 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1758688337 120 K-LKGVGPYTKGAILSIAYGIPE--PAVDGNVMRVLSRILSVWDDIAKPKTRKVFEEIVRE 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 ...
 9-356 0e+00

Adenine-specific DNA glycosylase, acts on AG and A-oxoG pairs [Replication, recombination and repair];


Pssm-ID: 440807 [Multi-domain]  Cd Length: 350  Bit Score: 526.63  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758688337   9 FNIEQFQNDLIGWFEEEQRDLPWRKNKDPYRVWVSEIMLQQTRVEAVKPYYANFMGKFPTLEALANADDEEVLKAWEGLG 88
Cdd:COG1194     1 MDMASFAKRLLAWYDRHGRDLPWRQTRDPYRVWLSEIMLQQTQVATVIPYYERFLERFPTVEALAAAPEDEVLKLWEGLG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758688337  89 YYSRARNLHAAVKEVKEVYGGVVPSDVKKIEKLKGVGPYTKGAILSIAYGIPEPAVDGNVMRVLSRILSVWDDIAKPKTR 168
Cdd:COG1194    81 YYSRARNLHKAAQQVVEEHGGVFPDTYEELLALPGIGPYTAAAIASIAFGEPAPIVDGNVKRVLSRLFAIEGPIGSPAAK 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758688337 169 KVFEEIVREIISVENPSYFNQGLMELGALICIPKNPSCLLCPVREHCRGYAEGVQKELPVKSKAKAPKMVPIVAGVLQtE 248
Cdd:COG1194   161 KELWALAEELLPPERPGDFNQALMDLGATVCTPKKPKCLLCPLQDDCAAFAEGRQEELPVKKPKKKKPERYGAALVIR-D 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758688337 249 DGRYVINKRPSTGLLANMWEFPNAELGEGIrnQKEQLIDYMKEKFELAVSIDEYAMNVQHTFTHRTWDIFVFYGKVTGNI 328
Cdd:COG1194   240 DGRVLLEKRPPKGLWGGLWEFPEFEWEEAE--DPEALERWLREELGLEVEWLEPLGTVRHVFTHFRLHLTVYLARVPAGP 317

                         330       340
                  ....*....|....*....|....*....
gi 1758688337 329 -VDTDTLKFVSKEAFEQLPFSKSHRTIYE 356
Cdd:COG1194   318 pAEPDGGRWVPLEELAALPLPAPMRKLLK 346
mutY TIGR01084
A/G-specific adenine glycosylase; This equivalog model identifies mutY members of the ...
 13-279 7.03e-139

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: 395.63  E-value: 7.03e-139
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758688337  13 QFQNDLIGWFEEEQR-DLPWRKNKDPYRVWVSEIMLQQTRVEAVKPYYANFMGKFPTLEALANADDEEVLKAWEGLGYYS 91
Cdd:TIGR01084   1 QFSEDLLSWYDKYGRkTLPWRQNKTPYRVWLSEVMLQQTQVATVIPYFERFLERFPTVQALANAPQDEVLKLWEGLGYYA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758688337  92 RARNLHAAVKEVKEVYGGVVPSDVKKIEKLKGVGPYTKGAILSIAYGIPEPAVDGNVMRVLSRILSVWDDIAKPKTRKVF 171
Cdd:TIGR01084  81 RARNLHKAAQEVVEEFGGEFPQDFEDLAALPGVGRYTAGAILSFALNKPYPILDGNVKRVLSRLFAVEGWPGKKKVENRL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758688337 172 EEIVREIISVENPSYFNQGLMELGALICIPKNPSCLLCPVREHCRGYAEGVQKELPVKSKAKAPKMVPIVAGVLQTEDGR 251
Cdd:TIGR01084 161 WTLAESLLPKADPEAFNQALMDLGAMICTRKKPKCDLCPLQDFCLAYQQGTWEEYPVKKPKAAPPERTTYFLVLQNYDGE 240

                         250       260
                  ....*....|....*....|....*...
gi 1758688337 252 YVINKRPSTGLLANMWEFPNAELGEGIR 279
Cdd:TIGR01084 241 VLLEQRPEKGLWGGLYCFPQFEDEDSLA 268
PRK10880 PRK10880
adenine DNA glycosylase;
12-317 4.15e-73

adenine DNA glycosylase;


Pssm-ID: 182805 [Multi-domain]  Cd Length: 350  Bit Score: 230.75  E-value: 4.15e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758688337  12 EQFQNDLIGWFEEEQRD-LPWRKNKDPYRVWVSEIMLQQTRVEAVKPYYANFMGKFPTLEALANADDEEVLKAWEGLGYY 90
Cdd:PRK10880    4 SQFSAQVLDWYDKYGRKtLPWQIDKTPYKVWLSEVMLQQTQVATVIPYFERFMARFPTVTDLANAPLDEVLHLWTGLGYY 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758688337  91 SRARNLHAAVKEVKEVYGGVVPSDVKKIEKLKGVGPYTKGAILSIAYGIPEPAVDGNVMRVLSRILSV--WDdiAKPKTR 168
Cdd:PRK10880   84 ARARNLHKAAQQVATLHGGEFPETFEEVAALPGVGRSTAGAILSLSLGKHFPILDGNVKRVLARCYAVsgWP--GKKEVE 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758688337 169 KVFEEIVREIISVENPSYFNQGLMELGALICIPKNPSCLLCPVREHCRGYAEGVQKELPVKskaKAPKMVPIVAG--VLQ 246
Cdd:PRK10880  162 NRLWQLSEQVTPAVGVERFNQAMMDLGAMVCTRSKPKCELCPLQNGCIAYANHSWALYPGK---KPKQTLPERTGyfLLL 238

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1758688337 247 TEDGRYVINKRPSTGLLANMWEFPNAElgegirnQKEQLIDYMKEKfELAVSIDEYAMNVQHTFTHRTWDI 317
Cdd:PRK10880  239 QHGDEVWLEQRPPSGLWGGLFCFPQFA-------DEEELRQWLAQR-GIAADNLTQLTAFRHTFSHFHLDI 301
ENDO3c cd00056
endonuclease III; includes endonuclease III (DNA-(apurinic or apyrimidinic site) lyase), ...
 38-195 9.24e-58

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: 184.75  E-value: 9.24e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758688337  38 YRVWVSEIMLQQTRVEAVKPYYANFMGKF-PTLEALANADDEEVLKAWEGLGYYSRARNLHAAVKEVKEVYGGVV---PS 113
Cdd:cd00056     1 FEVLVSEILSQQTTDKAVNKAYERLFERYgPTPEALAAADEEELRELIRSLGYRRKAKYLKELARAIVEGFGGLVlddPD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758688337 114 DVKKIEKLKGVGPYTKGAILSIAYGIPEPAVDGNVMRVLSRilsvWDDIAKPKTRKVFEEIVREIISVENPSYFNQGLME 193
Cdd:cd00056    81 AREELLALPGVGRKTANVVLLFALGPDAFPVDTHVRRVLKR----LGLIPKKKTPEELEELLEELLPKPYWGEANQALMD 156


                  ..
gi 1758688337 194 LG 195
Cdd:cd00056   157 LG 158
ENDO3c smart00478
endonuclease III; includes endonuclease III (DNA-(apurinic or apyrimidinic site) lyase), ...
 46-197 2.52e-47

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: 157.43  E-value: 2.52e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758688337   46 MLQQTRVEAVKPYYANFMGKFPTLEALANADDEEVLKAWEGLG-YYSRARNLHAAVKEVKEVYGGVVPSDVKKIEKLKGV 124
Cdd:smart00478   1 LSQQTTDERVNKATERLFEKFPTPEDLAAADEEELEELIRGLGfYRRKARYLIELARILVEEYGGEVPDDREELLKLPGV 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1758688337  125 GPYTKGAILSIAYGIPEPAVDGNVMRVLSRILSVWddiaKPKTRKVFEEIVREIISVENPSYFNQGLMELGAL 197
Cdd:smart00478  81 GRKTANAVLSFALGKPFIPVDTHVLRIAKRLGLVD----KKSTPEEVEKLLEKLLPEEDWRELNLLLIDFGRT 149
HhH-GPD pfam00730
HhH-GPD superfamily base excision DNA repair protein; This family contains a diverse range of ...
 42-177 8.21e-41

HhH-GPD superfamily base excision DNA repair protein; This family contains a diverse range of structurally related DNA repair proteins. The superfamily is called the HhH-GPD family after its hallmark Helix-hairpin-helix and Gly/Pro rich loop followed by a conserved aspartate. This includes endonuclease III, EC:4.2.99.18 and MutY an A/G-specific adenine glycosylase, both have a C terminal 4Fe-4S cluster. The family also includes 8-oxoguanine DNA glycosylases. The methyl-CPG binding protein MBD4 also contains a related domain that is a thymine DNA glycosylase. The family also includes DNA-3-methyladenine glycosylase II EC:3.2.2.21 and other members of the AlkA family.


Pssm-ID: 425841 [Multi-domain]  Cd Length: 141  Bit Score: 140.50  E-value: 8.21e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758688337  42 VSEIMLQQTRVEAVKPYYANFMGK-FPTLEALANADDEEVLKAWEGLGYY-SRARNLHAAVKEVKEVYGGVVPSDVKKIE 119
Cdd:pfam00730   1 VSAILSQQTSDKAVNKITERLFEKfFPTPEDLADADEEELRELIRGLGFYrRKAKYLKELARILVEGYGGEVPLDEEELE 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1758688337 120 K-LKGVGPYTKGAILSIAYGIPE--PAVDGNVMRVLSRILSVWDDIAKPKTRKVFEEIVRE 177
Cdd:pfam00730  81 AlLKGVGRWTAEAVLIFALGRPDplPVVDTHVRRVLKRLGLIKEKPTPKEVERELEELWPP 141
Nth COG0177
Endonuclease III [Replication, recombination and repair];
30-216 8.87e-39

Endonuclease III [Replication, recombination and repair];


Pssm-ID: 439947 [Multi-domain]  Cd Length: 198  Bit Score: 136.76  E-value: 8.87e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758688337  30 PWRKNKDPYRVWVSEIMLQQTRVEAVKPYYANFMGKFPTLEALANADDEEVLKAWEGLGYY-SRARNLHAAVKEVKEVYG 108
Cdd:COG0177    13 TELDYRDPFELLVATILSAQTTDERVNKATPRLFARYPTPEALAAADLEELEELIRPIGLYrNKAKNIIALARILVEKYG 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758688337 109 GVVPSDVKKIEKLKGVGPYTKGAILSIAYGIPEPAVDGNVMRVLSRIlsvwdDIAKPKT-RKVfEEIVREIISVENPSYF 187
Cdd:COG0177    93 GEVPETREELESLPGVGRKTANVVLNFAFGKPAIAVDTHVHRVSNRL-----GLVPGKDpEEV-EKDLMKLIPKEYWGDL 166

                         170       180
                  ....*....|....*....|....*....
gi 1758688337 188 NQGLMELGALICIPKNPSCLLCPVREHCR 216
Cdd:COG0177   167 HHLLILHGRYICKARKPKCEECPLADLCP 195
PRK13910 PRK13910
DNA glycosylase MutY; Provisional
 46-217 3.36e-30

DNA glycosylase MutY; Provisional


Pssm-ID: 172427 [Multi-domain]  Cd Length: 289  Bit Score: 117.05  E-value: 3.36e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758688337  46 MLQQTRVEAV-KPYYANFMGKFPTLEALANADDEEVLKAWEGLGYYSRARNLHAAVKEVKEVYGGVVPSDVKKIEKLKGV 124
Cdd:PRK13910    1 MSQQTQINTVvERFYSPFLEAFPTLKDLANAPLEEVLLLWRGLGYYSRAKNLKKSAEICVKEHHSQLPNDYQSLLKLPGI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758688337 125 GPYTKGAILSIAYGIPEPAVDGNVMRVLSRILSVWDDIakpkTRKVFEEIVREIISVENPSYFNQGLMELGALICIPKnP 204
Cdd:PRK13910   81 GAYTANAILCFGFREKSACVDANIKRVLLRLFGLDPNI----HAKDLQIKANDFLNLNESFNHNQALIDLGALICSPK-P 155

                         170
                  ....*....|...
gi 1758688337 205 SCLLCPVREHCRG 217
Cdd:PRK13910  156 KCAICPLNPYCLG 168
nth TIGR01083
endonuclease III; This equivalog model identifes nth members of the pfam00730 superfamily ...
 35-206 1.69e-26

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: 104.38  E-value: 1.69e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758688337  35 KDPYRVWVSEIMLQQTRVEAVKPYYANFMGKFPTLEALANADDEEVLKAWEGLGYY-SRARNLHAAVKEVKEVYGGVVPS 113
Cdd:TIGR01083  25 NNPFELLVATILSAQATDKRVNKATPKLFEVYPTPQALAQAGLEELEEYIKSIGLYrNKAKNIIELCRKLVERYGGEVPE 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758688337 114 DVKKIEKLKGVGPYTKGAILSIAYGIPEPAVDGNVMRVLSRI-LSVWDDIakpktRKVfEEIVREIISVENPSYFNQGLM 192
Cdd:TIGR01083 105 DREELVKLPGVGRKTANVVLNVAFGIPAIAVDTHVFRVSNRLgLSKGKDP-----IKV-EEDLMKLVPREFWVKLHHWLI 178

                         170
                  ....*....|....
gi 1758688337 193 ELGALICIPKNPSC 206
Cdd:TIGR01083 179 LHGRYTCKARKPLC 192
NUDIX_DNA_Glycosylase_C-MutY cd03431
C-terminal domain of DNA glycosylase; DNA glycosylase (MutY in bacteria and hMYH in humans) is ...
 241-356 2.32e-25

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: 98.91  E-value: 2.32e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758688337 241 VAGVLQTEdGRYVINKRPSTGLLANMWEFPNAELGEGIRNQKEQLidymKEKFELAVSIDEYAMNVQHTFTHRTWDIFVF 320
Cdd:cd03431     7 TVLVLRDG-GRVLLEKRPEKGLLAGLWEFPLVETEEEEEEAEALL----GLLAEELLLILEPLGEVKHVFSHFRLHITVY 81

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1758688337 321 YGKVTGNI-VDTDTLKFVSKEAFEQLPFSKSHRTIYE 356
Cdd:cd03431    82 LVELPEAPpAAPDEGRWVDLEELDEYALPAPMRKLLE 118
NUDIX_4 pfam14815
NUDIX domain;
241-356 6.45e-23

NUDIX domain;


Pssm-ID: 464330 [Multi-domain]  Cd Length: 114  Bit Score: 91.99  E-value: 6.45e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758688337 241 VAGVLQTEDGRYVINKRPSTGLLANMWEFPNAELGEGirnqkEQLIDYMKEKFELAVSIDEYA-MNVQHTFTHRTWDIFV 319
Cdd:pfam14815   1 AVLVIRNGDGRVLLRKRPEKGLLGGLWEFPGGKVEPG-----ETLEEALARLEELGIEVEVLEpGTVKHVFTHFRLTLHV 75

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1758688337 320 FY-GKVTGNIVDTDTLKFVSKEAFEQLPFSKSHRTIYE 356
Cdd:pfam14815  76 YLvREVEGEEEPQQELRWVTPEELDKYALPAAVRKILE 113
HP0602 COG2231
3-Methyladenine DNA glycosylase, HhH-GPD/Endo3 superfamily [Replication, recombination and ...
 37-220 5.05e-11

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


Pssm-ID: 441832 [Multi-domain]  Cd Length: 220  Bit Score: 61.78  E-value: 5.05e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758688337  37 PYRVWVSEIMLQQTRVEAVKPYYANF--MGKFpTLEALANADDEEVLKAWEGLGYYSR-ARNLHAAVKEVKEVYGGvvps 113
Cdd:COG2231    29 PFEVIVGAILTQNTSWKNVEKAIANLkeAGLL-DPEALAALDPEELAELIRPSGFYNQkAKRLKNLARWLVERYGG---- 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758688337 114 DVKKIEK------------LKGVGPYTKGAILSIAYGIPEPAVDGNVMRVLSRILSVWDDIAKPKTRKVFEEIVREiisv 181
Cdd:COG2231   104 GLEKLKAlpteelreellsLKGIGPETADSILLYAFNRPVFVVDAYTRRIFSRLGLIEEDASYDELQRLFEENLPP---- 179

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1758688337 182 eNPSYFNQ---GLMELGALICIPKnPSCLLCPVREHCRGYAE 220
Cdd:COG2231   180 -DVALYNEfhaLIVEHGKEYCKKK-PKCEECPLRDLCPYGGQ 219
PRK10702 PRK10702
endonuclease III; Provisional
 37-222 1.61e-10

endonuclease III; Provisional


Pssm-ID: 182661 [Multi-domain]  Cd Length: 211  Bit Score: 60.03  E-value: 1.61e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758688337  37 PYRVWVSEIMLQQTRVEAVKPYYANFMGKFPTLEALANADDEEVLKAWEGLGYY-SRARNLHAAVKEVKEVYGGVVPSDV 115
Cdd:PRK10702   29 PFELLIAVLLSAQATDVSVNKATAKLYPVANTPAAMLELGVEGVKTYIKTIGLYnSKAENVIKTCRILLEQHNGEVPEDR 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758688337 116 KKIEKLKGVGPYTKGAILSIAYGIPEPAVDGNVMRVLSRIlsvwdDIAKPKTRKVFEEIVREIISVENPSYFNQGLMELG 195
Cdd:PRK10702  109 AALEALPGVGRKTANVVLNTAFGWPTIAVDTHIFRVCNRT-----QFAPGKNVEQVEEKLLKVVPAEFKVDCHHWLILHG 183

                         170       180
                  ....*....|....*....|....*..
gi 1758688337 196 ALICIPKNPSCLLCPVREHCRgYAEGV 222
Cdd:PRK10702  184 RYTCIARKPRCGSCIIEDLCE-YKEKV 209
NUDIX_MutT_NudA_like cd03425
MutT pyrophosphohydrolase; The MutT pyrophosphohydrolase is a prototypical NUDIX hydrolase ...
 238-347 2.31e-05

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: 43.21  E-value: 2.31e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758688337 238 VPIVAGVLQtEDGRYVINKRPSTGLLANMWEFP--NAELGEgirNQKEQLIDYMKEKFELAVSIDEYAMNVQHTFTHRTW 315
Cdd:cd03425     1 IEVVAAIIV-DDGRVLIAQRPEGKHLAGLWEFPggKVEPGE---TPEQALVRELREELGIEVEVGEPLGTVEHDYPDFHV 76

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1758688337 316 DIFVFYGK-VTGNIVDT--DTLKFVSKEAFEQLPF 347
Cdd:cd03425    77 RLHVYLCTlWSGEPQLLehQELRWVTPEELDDLDW 111
PRK08999 PRK08999
Nudix family hydrolase;
234-314 6.75e-05

Nudix family hydrolase;


Pssm-ID: 236361 [Multi-domain]  Cd Length: 312  Bit Score: 44.09  E-value: 6.75e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758688337 234 APKMVPIVAGVLQTEDGRYVINKRPSTGLLANMWEFPNA--ELGEGIrnqkEQ-LIDYMKEkfELAVSIDEYA--MNVQH 308
Cdd:PRK08999    1 SMKRIHVAAGVIRDADGRILLARRPEGKHQGGLWEFPGGkvEPGETV----EQaLARELQE--ELGIEVTAARplITVRH 74


                  ....*.
gi 1758688337 309 TFTHRT 314
Cdd:PRK08999   75 DYPDKR 80
FES smart00525
iron-sulpphur binding domain in DNA-(apurinic or apyrimidinic site) lyase (subfamily of ENDO3); ...
 198-218 7.51e-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: 39.07  E-value: 7.51e-05
                           10        20
                   ....*....|....*....|.
gi 1758688337  198 ICIPKNPSCLLCPVREHCRGY 218
Cdd:smart00525   1 ICTARKPRCDECPLKDLCPAY 21
AlkA COG0122
3-methyladenine DNA glycosylase/8-oxoguanine DNA glycosylase [Replication, recombination and ...
 24-174 1.84e-04

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


Pssm-ID: 439892 [Multi-domain]  Cd Length: 255  Bit Score: 42.56  E-value: 1.84e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758688337  24 EEQRDLPWRKNKDPYRVWVSEIMLQQTRVEAVK--------------PYYANFMGKFPTLEALANADDEEVLKAweGLGY 89
Cdd:COG0122    71 ERYPGLRLPRRPDPFEALVRAILGQQVSVAAARtiwrrlvalfgepiEGPGGGLYAFPTPEALAAASEEELRAC--GLSR 148

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1758688337  90 YsRARNLHAAVKEVKEvyGGVVPSD---------VKKIEKLKGVGPYTKGAILSIAYGIPE--PAVDGNVMRVLSRILsv 158
Cdd:COG0122   149 R-KARYLRALARAVAD--GELDLEAlaglddeeaIARLTALPGIGPWTAEMVLLFALGRPDafPAGDLGLRRALGRLY-- 223

                         170
                  ....*....|....*.
gi 1758688337 159 wdDIAKPKTRKVFEEI 174
Cdd:COG0122   224 --GLGERPTPKELREL 237
HHH pfam00633
Helix-hairpin-helix motif; The helix-hairpin-helix DNA-binding motif is found to be duplicated ...
 107-135 2.80e-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: 37.78  E-value: 2.80e-04
                          10        20
                  ....*....|....*....|....*....
gi 1758688337 107 YGGVVPSDVKKIEKLKGVGPYTKGAILSI 135
Cdd:pfam00633   2 LEGLIPASVEELLALPGVGPKTAEAILSY 30
EndIII_4Fe-2S pfam10576
Iron-sulfur binding domain of endonuclease III; Escherichia coli endonuclease III (EC 4.2.99. ...
 199-215 3.06e-03

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: 34.67  E-value: 3.06e-03
                          10
                  ....*....|....*..
gi 1758688337 199 CIPKNPSCLLCPVREHC 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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