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Conserved domains on  [gi|1958774511|ref|XP_038965130|]
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adenine DNA glycosylase isoform X2 [Rattus norvegicus]

Protein Classification

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

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

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

Graphical summary

 Zoom to residue level

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List of domain hits

 Name Accession Description Interval E-value
MutY COG1194
Adenine-specific DNA glycosylase, acts on AG and A-oxoG pairs [Replication, recombination and ...
 62-433 1.50e-122

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: 361.76  E-value: 1.50e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774511  62 ADVTAFRRNLLSWYDQEKRDLPWRKrvkeeanlDRRAYAVWVSEVMLQQTQVATVIDYYTRWMQKWPTLQDLASASLEEV 141
Cdd:COG1194     1 MDMASFAKRLLAWYDRHGRDLPWRQ--------TRDPYRVWLSEIMLQQTQVATVIPYYERFLERFPTVEALAAAPEDEV 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774511 142 NQLWSGLGYYSRGRRLQEGARKVT------------------GV-------------------VDGNVIRVLCRVRAIGA 184
Cdd:COG1194    73 LKLWEGLGYYSRARNLHKAAQQVVeehggvfpdtyeellalpGIgpytaaaiasiafgepapiVDGNVKRVLSRLFAIEG 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774511 185 DPTSSFVSHHLWDLAQQLVDPARPGDFNQAAMELGATVCTPQRPLCSHCPVQSLCRAHQRvgqgqlsalpGSPDieecal 264
Cdd:COG1194   153 PIGSPAAKKELWALAEELLPPERPGDFNQALMDLGATVCTPKKPKCLLCPLQDDCAAFAE----------GRQE------ 216

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774511 265 ntrqcqlclpstnpwdpnmgvvNFPRKASRRPPREEYSATCVVEQPGAtggplILLVQRPNSGLLAGLWEFPSVtlEPSG 344
Cdd:COG1194   217 ----------------------ELPVKKPKKKKPERYGAALVIRDDGR-----VLLEKRPPKGLWGGLWEFPEF--EWEE 267

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774511 345 QHQHKALLQELQHWsAPLPTTPLQHLGEslpptpqVIHVFSHIKLTYQVYSLALEGQTPASttPPGARWLTWEEFRNAAV 424
Cdd:COG1194   268 AEDPEALERWLREE-LGLEVEWLEPLGT-------VRHVFTHFRLHLTVYLARVPAGPPAE--PDGGRWVPLEELAALPL 337


                  ....*....
gi 1958774511 425 STAMKKVFR 433
Cdd:COG1194   338 PAPMRKLLK 346
 
Name Accession Description Interval E-value
MutY COG1194
Adenine-specific DNA glycosylase, acts on AG and A-oxoG pairs [Replication, recombination and ...
 62-433 1.50e-122

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: 361.76  E-value: 1.50e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774511  62 ADVTAFRRNLLSWYDQEKRDLPWRKrvkeeanlDRRAYAVWVSEVMLQQTQVATVIDYYTRWMQKWPTLQDLASASLEEV 141
Cdd:COG1194     1 MDMASFAKRLLAWYDRHGRDLPWRQ--------TRDPYRVWLSEIMLQQTQVATVIPYYERFLERFPTVEALAAAPEDEV 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774511 142 NQLWSGLGYYSRGRRLQEGARKVT------------------GV-------------------VDGNVIRVLCRVRAIGA 184
Cdd:COG1194    73 LKLWEGLGYYSRARNLHKAAQQVVeehggvfpdtyeellalpGIgpytaaaiasiafgepapiVDGNVKRVLSRLFAIEG 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774511 185 DPTSSFVSHHLWDLAQQLVDPARPGDFNQAAMELGATVCTPQRPLCSHCPVQSLCRAHQRvgqgqlsalpGSPDieecal 264
Cdd:COG1194   153 PIGSPAAKKELWALAEELLPPERPGDFNQALMDLGATVCTPKKPKCLLCPLQDDCAAFAE----------GRQE------ 216

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774511 265 ntrqcqlclpstnpwdpnmgvvNFPRKASRRPPREEYSATCVVEQPGAtggplILLVQRPNSGLLAGLWEFPSVtlEPSG 344
Cdd:COG1194   217 ----------------------ELPVKKPKKKKPERYGAALVIRDDGR-----VLLEKRPPKGLWGGLWEFPEF--EWEE 267

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774511 345 QHQHKALLQELQHWsAPLPTTPLQHLGEslpptpqVIHVFSHIKLTYQVYSLALEGQTPASttPPGARWLTWEEFRNAAV 424
Cdd:COG1194   268 AEDPEALERWLREE-LGLEVEWLEPLGT-------VRHVFTHFRLHLTVYLARVPAGPPAE--PDGGRWVPLEELAALPL 337


                  ....*....
gi 1958774511 425 STAMKKVFR 433
Cdd:COG1194   338 PAPMRKLLK 346
mutY TIGR01084
A/G-specific adenine glycosylase; This equivalog model identifies mutY members of the ...
 66-336 1.65e-79

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: 248.86  E-value: 1.65e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774511  66 AFRRNLLSWYDQEKR-DLPWRkrvkeeanLDRRAYAVWVSEVMLQQTQVATVIDYYTRWMQKWPTLQDLASASLEEVNQL 144
Cdd:TIGR01084   1 QFSEDLLSWYDKYGRkTLPWR--------QNKTPYRVWLSEVMLQQTQVATVIPYFERFLERFPTVQALANAPQDEVLKL 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774511 145 WSGLGYYSRGRRLQEGARKVT------------------GV-------------------VDGNVIRVLCRVRAIGADPT 187
Cdd:TIGR01084  73 WEGLGYYARARNLHKAAQEVVeefggefpqdfedlaalpGVgrytagailsfalnkpypiLDGNVKRVLSRLFAVEGWPG 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774511 188 SSFVSHHLWDLAQQLVDPARPGDFNQAAMELGATVCTPQRPLCSHCPVQSLCRAHQrvgQGQLSALPGspdieecalntr 267
Cdd:TIGR01084 153 KKKVENRLWTLAESLLPKADPEAFNQALMDLGAMICTRKKPKCDLCPLQDFCLAYQ---QGTWEEYPV------------ 217

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958774511 268 qcqlclpstnpwdpnmgvvnfpRKASRRPPREEYSATCVVEQPGAtggplILLVQRPNSGLLAGLWEFP 336
Cdd:TIGR01084 218 ----------------------KKPKAAPPERTTYFLVLQNYDGE-----VLLEQRPEKGLWGGLYCFP 259
PRK10880 PRK10880
adenine DNA glycosylase;
67-389 1.35e-50

adenine DNA glycosylase;


Pssm-ID: 182805 [Multi-domain]  Cd Length: 350  Bit Score: 175.67  E-value: 1.35e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774511  67 FRRNLLSWYDQEKRD-LPWRkrvkeeanLDRRAYAVWVSEVMLQQTQVATVIDYYTRWMQKWPTLQDLASASLEEVNQLW 145
Cdd:PRK10880    6 FSAQVLDWYDKYGRKtLPWQ--------IDKTPYKVWLSEVMLQQTQVATVIPYFERFMARFPTVTDLANAPLDEVLHLW 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774511 146 SGLGYYSRGRRLQEGARKVT------------------GV-------------------VDGNVIRVLCRVRAIGADPTS 188
Cdd:PRK10880   78 TGLGYYARARNLHKAAQQVAtlhggefpetfeevaalpGVgrstagailslslgkhfpiLDGNVKRVLARCYAVSGWPGK 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774511 189 SFVSHHLWDLAQQlVDPARP-GDFNQAAMELGATVCTPQRPLCSHCPVQSLCRAHqrvGQGQLSALPGSPdieecalntr 267
Cdd:PRK10880  158 KEVENRLWQLSEQ-VTPAVGvERFNQAMMDLGAMVCTRSKPKCELCPLQNGCIAY---ANHSWALYPGKK---------- 223

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774511 268 qcqlclpstnpwdpnmgvvnfPRKAsrRPPREEYsatCVVEQPGATggplILLVQRPNSGLLAGLWEFPSVTLEpsgqhq 347
Cdd:PRK10880  224 ---------------------PKQT--LPERTGY---FLLLQHGDE----VWLEQRPPSGLWGGLFCFPQFADE------ 267

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*
gi 1958774511 348 hkallQELQHWsaplpttpLQHLGESLPPTPQVI---HVFSHIKL 389
Cdd:PRK10880  268 -----EELRQW--------LAQRGIAADNLTQLTafrHTFSHFHL 299
ENDO3c cd00056
endonuclease III; includes endonuclease III (DNA-(apurinic or apyrimidinic site) lyase), ...
 99-219 2.59e-29

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: 112.72  E-value: 2.59e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774511  99 YAVWVSEVMLQQTQVATVIDYYTRWMQKW-PTLQDLASASLEEVNQLWSGLGYYSRGRRLQEGARKVT------------ 165
Cdd:cd00056     1 FEVLVSEILSQQTTDKAVNKAYERLFERYgPTPEALAAADEEELRELIRSLGYRRKAKYLKELARAIVegfgglvlddpd 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774511 166 ---------GV-------------------VDGNVIRVLCRVRAIGADPTssfvSHHLWDLAQQLVDPARPGDFNQAAME 217
Cdd:cd00056    81 areellalpGVgrktanvvllfalgpdafpVDTHVRRVLKRLGLIPKKKT----PEELEELLEELLPKPYWGEANQALMD 156


                  ..
gi 1958774511 218 LG 219
Cdd:cd00056   157 LG 158
HhH-GPD pfam00730
HhH-GPD superfamily base excision DNA repair protein; This family contains a diverse range of ...
 103-201 1.22e-21

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: 90.81  E-value: 1.22e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774511 103 VSEVMLQQTQVATVIDYYTRWMQKW-PTLQDLASASLEEVNQLWSGLGYY-SRGRRLQEGARK----------------- 163
Cdd:pfam00730   1 VSAILSQQTSDKAVNKITERLFEKFfPTPEDLADADEEELRELIRGLGFYrRKAKYLKELARIlvegyggevpldeeele 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958774511 164 -----------------------VTGVVDGNVIRVLCRVRAIGADPTSSFVSHHLWDLAQQ 201
Cdd:pfam00730  81 allkgvgrwtaeavlifalgrpdPLPVVDTHVRRVLKRLGLIKEKPTPKEVERELEELWPP 141
FES smart00525
iron-sulpphur binding domain in DNA-(apurinic or apyrimidinic site) lyase (subfamily of ENDO3); ...
 222-241 1.46e-03

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


Pssm-ID: 197771 [Multi-domain]  Cd Length: 21  Bit Score: 35.99  E-value: 1.46e-03
                           10        20
                   ....*....|....*....|
gi 1958774511  222 VCTPQRPLCSHCPVQSLCRA 241
Cdd:smart00525   1 ICTARKPRCDECPLKDLCPA 20
 
Name Accession Description Interval E-value
MutY COG1194
Adenine-specific DNA glycosylase, acts on AG and A-oxoG pairs [Replication, recombination and ...
 62-433 1.50e-122

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: 361.76  E-value: 1.50e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774511  62 ADVTAFRRNLLSWYDQEKRDLPWRKrvkeeanlDRRAYAVWVSEVMLQQTQVATVIDYYTRWMQKWPTLQDLASASLEEV 141
Cdd:COG1194     1 MDMASFAKRLLAWYDRHGRDLPWRQ--------TRDPYRVWLSEIMLQQTQVATVIPYYERFLERFPTVEALAAAPEDEV 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774511 142 NQLWSGLGYYSRGRRLQEGARKVT------------------GV-------------------VDGNVIRVLCRVRAIGA 184
Cdd:COG1194    73 LKLWEGLGYYSRARNLHKAAQQVVeehggvfpdtyeellalpGIgpytaaaiasiafgepapiVDGNVKRVLSRLFAIEG 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774511 185 DPTSSFVSHHLWDLAQQLVDPARPGDFNQAAMELGATVCTPQRPLCSHCPVQSLCRAHQRvgqgqlsalpGSPDieecal 264
Cdd:COG1194   153 PIGSPAAKKELWALAEELLPPERPGDFNQALMDLGATVCTPKKPKCLLCPLQDDCAAFAE----------GRQE------ 216

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774511 265 ntrqcqlclpstnpwdpnmgvvNFPRKASRRPPREEYSATCVVEQPGAtggplILLVQRPNSGLLAGLWEFPSVtlEPSG 344
Cdd:COG1194   217 ----------------------ELPVKKPKKKKPERYGAALVIRDDGR-----VLLEKRPPKGLWGGLWEFPEF--EWEE 267

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774511 345 QHQHKALLQELQHWsAPLPTTPLQHLGEslpptpqVIHVFSHIKLTYQVYSLALEGQTPASttPPGARWLTWEEFRNAAV 424
Cdd:COG1194   268 AEDPEALERWLREE-LGLEVEWLEPLGT-------VRHVFTHFRLHLTVYLARVPAGPPAE--PDGGRWVPLEELAALPL 337


                  ....*....
gi 1958774511 425 STAMKKVFR 433
Cdd:COG1194   338 PAPMRKLLK 346
mutY TIGR01084
A/G-specific adenine glycosylase; This equivalog model identifies mutY members of the ...
 66-336 1.65e-79

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: 248.86  E-value: 1.65e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774511  66 AFRRNLLSWYDQEKR-DLPWRkrvkeeanLDRRAYAVWVSEVMLQQTQVATVIDYYTRWMQKWPTLQDLASASLEEVNQL 144
Cdd:TIGR01084   1 QFSEDLLSWYDKYGRkTLPWR--------QNKTPYRVWLSEVMLQQTQVATVIPYFERFLERFPTVQALANAPQDEVLKL 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774511 145 WSGLGYYSRGRRLQEGARKVT------------------GV-------------------VDGNVIRVLCRVRAIGADPT 187
Cdd:TIGR01084  73 WEGLGYYARARNLHKAAQEVVeefggefpqdfedlaalpGVgrytagailsfalnkpypiLDGNVKRVLSRLFAVEGWPG 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774511 188 SSFVSHHLWDLAQQLVDPARPGDFNQAAMELGATVCTPQRPLCSHCPVQSLCRAHQrvgQGQLSALPGspdieecalntr 267
Cdd:TIGR01084 153 KKKVENRLWTLAESLLPKADPEAFNQALMDLGAMICTRKKPKCDLCPLQDFCLAYQ---QGTWEEYPV------------ 217

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958774511 268 qcqlclpstnpwdpnmgvvnfpRKASRRPPREEYSATCVVEQPGAtggplILLVQRPNSGLLAGLWEFP 336
Cdd:TIGR01084 218 ----------------------KKPKAAPPERTTYFLVLQNYDGE-----VLLEQRPEKGLWGGLYCFP 259
PRK10880 PRK10880
adenine DNA glycosylase;
67-389 1.35e-50

adenine DNA glycosylase;


Pssm-ID: 182805 [Multi-domain]  Cd Length: 350  Bit Score: 175.67  E-value: 1.35e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774511  67 FRRNLLSWYDQEKRD-LPWRkrvkeeanLDRRAYAVWVSEVMLQQTQVATVIDYYTRWMQKWPTLQDLASASLEEVNQLW 145
Cdd:PRK10880    6 FSAQVLDWYDKYGRKtLPWQ--------IDKTPYKVWLSEVMLQQTQVATVIPYFERFMARFPTVTDLANAPLDEVLHLW 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774511 146 SGLGYYSRGRRLQEGARKVT------------------GV-------------------VDGNVIRVLCRVRAIGADPTS 188
Cdd:PRK10880   78 TGLGYYARARNLHKAAQQVAtlhggefpetfeevaalpGVgrstagailslslgkhfpiLDGNVKRVLARCYAVSGWPGK 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774511 189 SFVSHHLWDLAQQlVDPARP-GDFNQAAMELGATVCTPQRPLCSHCPVQSLCRAHqrvGQGQLSALPGSPdieecalntr 267
Cdd:PRK10880  158 KEVENRLWQLSEQ-VTPAVGvERFNQAMMDLGAMVCTRSKPKCELCPLQNGCIAY---ANHSWALYPGKK---------- 223

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774511 268 qcqlclpstnpwdpnmgvvnfPRKAsrRPPREEYsatCVVEQPGATggplILLVQRPNSGLLAGLWEFPSVTLEpsgqhq 347
Cdd:PRK10880  224 ---------------------PKQT--LPERTGY---FLLLQHGDE----VWLEQRPPSGLWGGLFCFPQFADE------ 267

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*
gi 1958774511 348 hkallQELQHWsaplpttpLQHLGESLPPTPQVI---HVFSHIKL 389
Cdd:PRK10880  268 -----EELRQW--------LAQRGIAADNLTQLTafrHTFSHFHL 299
ENDO3c cd00056
endonuclease III; includes endonuclease III (DNA-(apurinic or apyrimidinic site) lyase), ...
 99-219 2.59e-29

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: 112.72  E-value: 2.59e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774511  99 YAVWVSEVMLQQTQVATVIDYYTRWMQKW-PTLQDLASASLEEVNQLWSGLGYYSRGRRLQEGARKVT------------ 165
Cdd:cd00056     1 FEVLVSEILSQQTTDKAVNKAYERLFERYgPTPEALAAADEEELRELIRSLGYRRKAKYLKELARAIVegfgglvlddpd 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774511 166 ---------GV-------------------VDGNVIRVLCRVRAIGADPTssfvSHHLWDLAQQLVDPARPGDFNQAAME 217
Cdd:cd00056    81 areellalpGVgrktanvvllfalgpdafpVDTHVRRVLKRLGLIPKKKT----PEELEELLEELLPKPYWGEANQALMD 156


                  ..
gi 1958774511 218 LG 219
Cdd:cd00056   157 LG 158
NUDIX_DNA_Glycosylase_C-MutY cd03431
C-terminal domain of DNA glycosylase; DNA glycosylase (MutY in bacteria and hMYH in humans) is ...
 297-432 6.10e-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: 102.00  E-value: 6.10e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774511 297 PREEYSATCVVEQPGAtggplILLVQRPNSGLLAGLWEFPSVTLEPSGQhqhkaLLQELQHWSAPLPTTPLQHLGEslpp 376
Cdd:cd03431     1 VPERYFTVLVLRDGGR-----VLLEKRPEKGLLAGLWEFPLVETEEEEE-----EAEALLGLLAEELLLILEPLGE---- 66

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1958774511 377 tpqVIHVFSHIKLTYQVYSLALEGQTPASttPPGARWLTWEEFRNAAVSTAMKKVF 432
Cdd:cd03431    67 ---VKHVFSHFRLHITVYLVELPEAPPAA--PDEGRWVDLEELDEYALPAPMRKLL 117
HhH-GPD pfam00730
HhH-GPD superfamily base excision DNA repair protein; This family contains a diverse range of ...
 103-201 1.22e-21

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: 90.81  E-value: 1.22e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774511 103 VSEVMLQQTQVATVIDYYTRWMQKW-PTLQDLASASLEEVNQLWSGLGYY-SRGRRLQEGARK----------------- 163
Cdd:pfam00730   1 VSAILSQQTSDKAVNKITERLFEKFfPTPEDLADADEEELRELIRGLGFYrRKAKYLKELARIlvegyggevpldeeele 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958774511 164 -----------------------VTGVVDGNVIRVLCRVRAIGADPTSSFVSHHLWDLAQQ 201
Cdd:pfam00730  81 allkgvgrwtaeavlifalgrpdPLPVVDTHVRRVLKRLGLIKEKPTPKEVERELEELWPP 141
PRK13910 PRK13910
DNA glycosylase MutY; Provisional
 107-239 2.30e-19

DNA glycosylase MutY; Provisional


Pssm-ID: 172427 [Multi-domain]  Cd Length: 289  Bit Score: 88.16  E-value: 2.30e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774511 107 MLQQTQVATVID-YYTRWMQKWPTLQDLASASLEEVNQLWSGLGYYSRGRRLQEGA------------------------ 161
Cdd:PRK13910    1 MSQQTQINTVVErFYSPFLEAFPTLKDLANAPLEEVLLLWRGLGYYSRAKNLKKSAeicvkehhsqlpndyqsllklpgi 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774511 162 -------------RKVTGVVDGNVIRVLCRVraIGADPtsSFVSHHLWDLAQQLVDPARPGDFNQAAMELGATVCTPqRP 228
Cdd:PRK13910   81 gaytanailcfgfREKSACVDANIKRVLLRL--FGLDP--NIHAKDLQIKANDFLNLNESFNHNQALIDLGALICSP-KP 155

                         170
                  ....*....|.
gi 1958774511 229 LCSHCPVQSLC 239
Cdd:PRK13910  156 KCAICPLNPYC 166
NUDIX_4 pfam14815
NUDIX domain;
318-433 4.80e-19

NUDIX domain;


Pssm-ID: 464330 [Multi-domain]  Cd Length: 114  Bit Score: 82.36  E-value: 4.80e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774511 318 ILLVQRPNSGLLAGLWEFPSVTLEPSGQHQHKALLQELQHwsapLPTTPLQHLgeslpptpQVIHVFSHIKLTYQVYSLA 397
Cdd:pfam14815  12 VLLRKRPEKGLLGGLWEFPGGKVEPGETLEEALARLEELG----IEVEVLEPG--------TVKHVFTHFRLTLHVYLVR 79

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1958774511 398 LEGQTPASttPPGARWLTWEEFRNAAVSTAMKKVFR 433
Cdd:pfam14815  80 EVEGEEEP--QQELRWVTPEELDKYALPAAVRKILE 113
Nth COG0177
Endonuclease III [Replication, recombination and repair];
125-240 1.55e-10

Endonuclease III [Replication, recombination and repair];


Pssm-ID: 439947 [Multi-domain]  Cd Length: 198  Bit Score: 60.49  E-value: 1.55e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774511 125 QKWPTLQDLASASLEEVNQLWSGLGYY-SRGRRLQEGARKVT------------------GV------------------ 167
Cdd:COG0177    47 ARYPTPEALAAADLEELEELIRPIGLYrNKAKNIIALARILVekyggevpetreeleslpGVgrktanvvlnfafgkpai 126

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958774511 168 -VDGNVIRVLCRVR-AIGADPTSsfVSHHLwdlaQQLVDPARPGDFNQAAMELGATVCTPQRPLCSHCPVQSLCR 240
Cdd:COG0177   127 aVDTHVHRVSNRLGlVPGKDPEE--VEKDL----MKLIPKEYWGDLHHLLILHGRYICKARKPKCEECPLADLCP 195
PRK10546 PRK10546
pyrimidine (deoxy)nucleoside triphosphate diphosphatase;
306-356 2.88e-05

pyrimidine (deoxy)nucleoside triphosphate diphosphatase;


Pssm-ID: 182536 [Multi-domain]  Cd Length: 135  Bit Score: 43.96  E-value: 2.88e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1958774511 306 VVEQPGAtggplILLVQRPNSGLLAGLWEFPSVTLEPsGQHQHKALLQELQ 356
Cdd:PRK10546   10 IIERDGK-----ILLAQRPAHSDQAGLWEFAGGKVEP-GESQPQALIRELR 54
FES smart00525
iron-sulpphur binding domain in DNA-(apurinic or apyrimidinic site) lyase (subfamily of ENDO3); ...
 222-241 1.46e-03

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


Pssm-ID: 197771 [Multi-domain]  Cd Length: 21  Bit Score: 35.99  E-value: 1.46e-03
                           10        20
                   ....*....|....*....|
gi 1958774511  222 VCTPQRPLCSHCPVQSLCRA 241
Cdd:smart00525   1 ICTARKPRCDECPLKDLCPA 20
EndIII_4Fe-2S pfam10576
Iron-sulfur binding domain of endonuclease III; Escherichia coli endonuclease III (EC 4.2.99. ...
 223-239 2.61e-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: 35.05  E-value: 2.61e-03
                          10
                  ....*....|....*..
gi 1958774511 223 CTPQRPLCSHCPVQSLC 239
Cdd:pfam10576   1 CTARKPKCEECPLADLC 17
NUDIX_MutT_NudA_like cd03425
MutT pyrophosphohydrolase; The MutT pyrophosphohydrolase is a prototypical NUDIX hydrolase ...
 318-336 5.95e-03

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: 36.66  E-value: 5.95e-03
                          10
                  ....*....|....*....
gi 1958774511 318 ILLVQRPNSGLLAGLWEFP 336
Cdd:cd03425    14 VLIAQRPEGKHLAGLWEFP 32
 
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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