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Conserved domains on  [gi|504758818|ref|WP_014945920|]
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A/G-specific adenine glycosylase [Chlamydia psittaci]

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

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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 ...
 1-356 1.05e-138

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: 398.36  E-value: 1.05e-138
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504758818   1 MTKIAFSERaknfpigkLKQWFTDNKRSFPWRDNPSPYNVWVSEVMLQQTRAEVAVKYFIEWMEKFPTIESLATANEEHV 80
Cdd:COG1194    1 MDMASFAKR--------LLAWYDRHGRDLPWRQTRDPYRVWLSEIMLQQTQVATVIPYYERFLERFPTVEALAAAPEDEV 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504758818  81 MKAWEGLGYYTRARNLLQGARMVMTDFGGKLPDDPLDLMQIKGLGPYTVHAILAFAFKRRTAAVDGNVLRVISRVFLINA 160
Cdd:COG1194   73 LKLWEGLGYYSRARNLHKAAQQVVEEHGGVFPDTYEELLALPGIGPYTAAAIASIAFGEPAPIVDGNVKRVLSRLFAIEG 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504758818 161 SIDLESTKAWVFRIVLSFLPAQDPQVIAEALIELGACICK-RAPKCEICPLNSICGAFKEGRQKSLPVRHARKKTVTLFR 239
Cdd:COG1194  153 PIGSPAAKKELWALAEELLPPERPGDFNQALMDLGATVCTpKKPKCLLCPLQDDCAAFAEGRQEELPVKKPKKKKPERYG 232

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504758818 240 WVAIVLYKGFIVLEQRKPEEMMAGLYEFPYIEVESFDDLSDIDRLIQnmeEYVQAPLVFAGELEEQRHAFTHYKVRLVPK 319
Cdd:COG1194  233 AALVIRDDGRVLLEKRPPKGLWGGLWEFPEFEWEEAEDPEALERWLR---EELGLEVEWLEPLGTVRHVFTHFRLHLTVY 309

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|.
gi 504758818 320 IFHAKSEPKSE----LLYPLDTMDSLPFSSGHRKIKAWLLE 356
Cdd:COG1194  310 LARVPAGPPAEpdggRWVPLEELAALPLPAPMRKLLKALLK 350
 
Name Accession Description Interval E-value
MutY COG1194
Adenine-specific DNA glycosylase, acts on AG and A-oxoG pairs [Replication, recombination and ...
 1-356 1.05e-138

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: 398.36  E-value: 1.05e-138
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504758818   1 MTKIAFSERaknfpigkLKQWFTDNKRSFPWRDNPSPYNVWVSEVMLQQTRAEVAVKYFIEWMEKFPTIESLATANEEHV 80
Cdd:COG1194    1 MDMASFAKR--------LLAWYDRHGRDLPWRQTRDPYRVWLSEIMLQQTQVATVIPYYERFLERFPTVEALAAAPEDEV 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504758818  81 MKAWEGLGYYTRARNLLQGARMVMTDFGGKLPDDPLDLMQIKGLGPYTVHAILAFAFKRRTAAVDGNVLRVISRVFLINA 160
Cdd:COG1194   73 LKLWEGLGYYSRARNLHKAAQQVVEEHGGVFPDTYEELLALPGIGPYTAAAIASIAFGEPAPIVDGNVKRVLSRLFAIEG 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504758818 161 SIDLESTKAWVFRIVLSFLPAQDPQVIAEALIELGACICK-RAPKCEICPLNSICGAFKEGRQKSLPVRHARKKTVTLFR 239
Cdd:COG1194  153 PIGSPAAKKELWALAEELLPPERPGDFNQALMDLGATVCTpKKPKCLLCPLQDDCAAFAEGRQEELPVKKPKKKKPERYG 232

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504758818 240 WVAIVLYKGFIVLEQRKPEEMMAGLYEFPYIEVESFDDLSDIDRLIQnmeEYVQAPLVFAGELEEQRHAFTHYKVRLVPK 319
Cdd:COG1194  233 AALVIRDDGRVLLEKRPPKGLWGGLWEFPEFEWEEAEDPEALERWLR---EELGLEVEWLEPLGTVRHVFTHFRLHLTVY 309

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|.
gi 504758818 320 IFHAKSEPKSE----LLYPLDTMDSLPFSSGHRKIKAWLLE 356
Cdd:COG1194  310 LARVPAGPPAEpdggRWVPLEELAALPLPAPMRKLLKALLK 350
mutY TIGR01084
A/G-specific adenine glycosylase; This equivalog model identifies mutY members of the ...
 18-274 2.04e-109

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: 320.90  E-value: 2.04e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504758818   18 LKQWFTDNKR-SFPWRDNPSPYNVWVSEVMLQQTRAEVAVKYFIEWMEKFPTIESLATANEEHVMKAWEGLGYYTRARNL 96
Cdd:TIGR01084   6 LLSWYDKYGRkTLPWRQNKTPYRVWLSEVMLQQTQVATVIPYFERFLERFPTVQALANAPQDEVLKLWEGLGYYARARNL 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504758818   97 LQGARMVMTDFGGKLPDDPLDLMQIKGLGPYTVHAILAFAFKRRTAAVDGNVLRVISRVFLINASIDLESTKAWVFRIVL 176
Cdd:TIGR01084  86 HKAAQEVVEEFGGEFPQDFEDLAALPGVGRYTAGAILSFALNKPYPILDGNVKRVLSRLFAVEGWPGKKKVENRLWTLAE 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504758818  177 SFLPAQDPQVIAEALIELGACICKRA-PKCEICPLNSICGAFKEGRQKSLPVRH-ARKKTVTLFRWVAIVLYKGFIVLEQ 254
Cdd:TIGR01084 166 SLLPKADPEAFNQALMDLGAMICTRKkPKCDLCPLQDFCLAYQQGTWEEYPVKKpKAAPPERTTYFLVLQNYDGEVLLEQ 245

                         250       260
                  ....*....|....*....|
gi 504758818  255 RKPEEMMAGLYEFPYIEVES 274
Cdd:TIGR01084 246 RPEKGLWGGLYCFPQFEDED 265
PRK10880 PRK10880
adenine DNA glycosylase;
26-318 1.60e-55

adenine DNA glycosylase;


Pssm-ID: 182805 [Multi-domain]  Cd Length: 350  Bit Score: 185.30  E-value: 1.60e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504758818  26 KRSFPWRDNPSPYNVWVSEVMLQQTRAEVAVKYFIEWMEKFPTIESLATANEEHVMKAWEGLGYYTRARNLLQGARMVMT 105
Cdd:PRK10880  19 RKTLPWQIDKTPYKVWLSEVMLQQTQVATVIPYFERFMARFPTVTDLANAPLDEVLHLWTGLGYYARARNLHKAAQQVAT 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504758818 106 DFGGKLPDDPLDLMQIKGLGPYTVHAILAFAFKRRTAAVDGNVLRVISRVFLIN---ASIDLEsTKAWvfRIVLSFLPAQ 182
Cdd:PRK10880  99 LHGGEFPETFEEVAALPGVGRSTAGAILSLSLGKHFPILDGNVKRVLARCYAVSgwpGKKEVE-NRLW--QLSEQVTPAV 175

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504758818 183 DPQVIAEALIELGACICKRA-PKCEICPLNSICGAFKEGR---------QKSLPVRHArkktvtlfrWVAIVLYKGFIVL 252
Cdd:PRK10880 176 GVERFNQAMMDLGAMVCTRSkPKCELCPLQNGCIAYANHSwalypgkkpKQTLPERTG---------YFLLLQHGDEVWL 246

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 504758818 253 EQRKPEEMMAGLYEFPYIEVEsfddlsdidrliQNMEEYVQAPLVFAGELEEQ---RHAFTHYKVRLVP 318
Cdd:PRK10880 247 EQRPPSGLWGGLFCFPQFADE------------EELRQWLAQRGIAADNLTQLtafRHTFSHFHLDIVP 303
ENDO3c cd00056
endonuclease III; includes endonuclease III (DNA-(apurinic or apyrimidinic site) lyase), ...
 38-195 1.26e-46

endonuclease III; includes endonuclease III (DNA-(apurinic or apyrimidinic site) lyase), alkylbase DNA glycosidases (Alka-family) and other DNA glycosidases


Pssm-ID: 238013 [Multi-domain]  Cd Length: 158  Bit Score: 156.25  E-value: 1.26e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504758818  38 YNVWVSEVMLQQTRAEVAVKYFIEWMEKF-PTIESLATANEEHVMKAWEGLGYYTRARNLLQGARMVMTDFGGKLPDDPL 116
Cdd:cd00056    1 FEVLVSEILSQQTTDKAVNKAYERLFERYgPTPEALAAADEEELRELIRSLGYRRKAKYLKELARAIVEGFGGLVLDDPD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504758818 117 D---LMQIKGLGPYTVHAILAFAFKRRTAAVDGNVLRVISRVFLINAsidlESTKAWVFRIVLSFLPAQDPQVIAEALIE 193
Cdd:cd00056   81 AreeLLALPGVGRKTANVVLLFALGPDAFPVDTHVRRVLKRLGLIPK----KKTPEELEELLEELLPKPYWGEANQALMD 156


                 ..
gi 504758818 194 LG 195
Cdd:cd00056  157 LG 158
ENDO3c smart00478
endonuclease III; includes endonuclease III (DNA-(apurinic or apyrimidinic site) lyase), ...
 46-196 1.71e-42

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: 145.10  E-value: 1.71e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504758818    46 MLQQTRAEVAVKYFIEWMEKFPTIESLATANEEHVMKAWEGLG-YYTRARNLLQGARMVMTDFGGKLPDDPLDLMQIKGL 124
Cdd:smart00478   1 LSQQTTDERVNKATERLFEKFPTPEDLAAADEEELEELIRGLGfYRRKARYLIELARILVEEYGGEVPDDREELLKLPGV 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504758818   125 GPYTVHAILAFAFKRRTAAVDGNVLRVISRVFLinasIDLESTKAWVFRIVLSFLPAQDPQVIAEALIELGA 196
Cdd:smart00478  81 GRKTANAVLSFALGKPFIPVDTHVLRIAKRLGL----VDKKSTPEEVEKLLEKLLPEEDWRELNLLLIDFGR 148
HhH-GPD pfam00730
HhH-GPD superfamily base excision DNA repair protein; This family contains a diverse range of ...
 42-163 8.35e-32

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: 117.00  E-value: 8.35e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504758818   42 VSEVMLQQTRAEVAVKYFIEWMEK-FPTIESLATANEEHVMKAWEGLGYYTR-ARNLLQGARMVMTDFGGKLPDDPLDLM 119
Cdd:pfam00730   1 VSAILSQQTSDKAVNKITERLFEKfFPTPEDLADADEEELRELIRGLGFYRRkAKYLKELARILVEGYGGEVPLDEEELE 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 504758818  120 Q-IKGLGPYTVHAILAFAFKRR--TAAVDGNVLRVISRVFLINASID 163
Cdd:pfam00730  81 AlLKGVGRWTAEAVLIFALGRPdpLPVVDTHVRRVLKRLGLIKEKPT 127
 
Name Accession Description Interval E-value
MutY COG1194
Adenine-specific DNA glycosylase, acts on AG and A-oxoG pairs [Replication, recombination and ...
 1-356 1.05e-138

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: 398.36  E-value: 1.05e-138
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504758818   1 MTKIAFSERaknfpigkLKQWFTDNKRSFPWRDNPSPYNVWVSEVMLQQTRAEVAVKYFIEWMEKFPTIESLATANEEHV 80
Cdd:COG1194    1 MDMASFAKR--------LLAWYDRHGRDLPWRQTRDPYRVWLSEIMLQQTQVATVIPYYERFLERFPTVEALAAAPEDEV 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504758818  81 MKAWEGLGYYTRARNLLQGARMVMTDFGGKLPDDPLDLMQIKGLGPYTVHAILAFAFKRRTAAVDGNVLRVISRVFLINA 160
Cdd:COG1194   73 LKLWEGLGYYSRARNLHKAAQQVVEEHGGVFPDTYEELLALPGIGPYTAAAIASIAFGEPAPIVDGNVKRVLSRLFAIEG 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504758818 161 SIDLESTKAWVFRIVLSFLPAQDPQVIAEALIELGACICK-RAPKCEICPLNSICGAFKEGRQKSLPVRHARKKTVTLFR 239
Cdd:COG1194  153 PIGSPAAKKELWALAEELLPPERPGDFNQALMDLGATVCTpKKPKCLLCPLQDDCAAFAEGRQEELPVKKPKKKKPERYG 232

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504758818 240 WVAIVLYKGFIVLEQRKPEEMMAGLYEFPYIEVESFDDLSDIDRLIQnmeEYVQAPLVFAGELEEQRHAFTHYKVRLVPK 319
Cdd:COG1194  233 AALVIRDDGRVLLEKRPPKGLWGGLWEFPEFEWEEAEDPEALERWLR---EELGLEVEWLEPLGTVRHVFTHFRLHLTVY 309

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|.
gi 504758818 320 IFHAKSEPKSE----LLYPLDTMDSLPFSSGHRKIKAWLLE 356
Cdd:COG1194  310 LARVPAGPPAEpdggRWVPLEELAALPLPAPMRKLLKALLK 350
mutY TIGR01084
A/G-specific adenine glycosylase; This equivalog model identifies mutY members of the ...
 18-274 2.04e-109

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: 320.90  E-value: 2.04e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504758818   18 LKQWFTDNKR-SFPWRDNPSPYNVWVSEVMLQQTRAEVAVKYFIEWMEKFPTIESLATANEEHVMKAWEGLGYYTRARNL 96
Cdd:TIGR01084   6 LLSWYDKYGRkTLPWRQNKTPYRVWLSEVMLQQTQVATVIPYFERFLERFPTVQALANAPQDEVLKLWEGLGYYARARNL 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504758818   97 LQGARMVMTDFGGKLPDDPLDLMQIKGLGPYTVHAILAFAFKRRTAAVDGNVLRVISRVFLINASIDLESTKAWVFRIVL 176
Cdd:TIGR01084  86 HKAAQEVVEEFGGEFPQDFEDLAALPGVGRYTAGAILSFALNKPYPILDGNVKRVLSRLFAVEGWPGKKKVENRLWTLAE 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504758818  177 SFLPAQDPQVIAEALIELGACICKRA-PKCEICPLNSICGAFKEGRQKSLPVRH-ARKKTVTLFRWVAIVLYKGFIVLEQ 254
Cdd:TIGR01084 166 SLLPKADPEAFNQALMDLGAMICTRKkPKCDLCPLQDFCLAYQQGTWEEYPVKKpKAAPPERTTYFLVLQNYDGEVLLEQ 245

                         250       260
                  ....*....|....*....|
gi 504758818  255 RKPEEMMAGLYEFPYIEVES 274
Cdd:TIGR01084 246 RPEKGLWGGLYCFPQFEDED 265
PRK10880 PRK10880
adenine DNA glycosylase;
26-318 1.60e-55

adenine DNA glycosylase;


Pssm-ID: 182805 [Multi-domain]  Cd Length: 350  Bit Score: 185.30  E-value: 1.60e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504758818  26 KRSFPWRDNPSPYNVWVSEVMLQQTRAEVAVKYFIEWMEKFPTIESLATANEEHVMKAWEGLGYYTRARNLLQGARMVMT 105
Cdd:PRK10880  19 RKTLPWQIDKTPYKVWLSEVMLQQTQVATVIPYFERFMARFPTVTDLANAPLDEVLHLWTGLGYYARARNLHKAAQQVAT 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504758818 106 DFGGKLPDDPLDLMQIKGLGPYTVHAILAFAFKRRTAAVDGNVLRVISRVFLIN---ASIDLEsTKAWvfRIVLSFLPAQ 182
Cdd:PRK10880  99 LHGGEFPETFEEVAALPGVGRSTAGAILSLSLGKHFPILDGNVKRVLARCYAVSgwpGKKEVE-NRLW--QLSEQVTPAV 175

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504758818 183 DPQVIAEALIELGACICKRA-PKCEICPLNSICGAFKEGR---------QKSLPVRHArkktvtlfrWVAIVLYKGFIVL 252
Cdd:PRK10880 176 GVERFNQAMMDLGAMVCTRSkPKCELCPLQNGCIAYANHSwalypgkkpKQTLPERTG---------YFLLLQHGDEVWL 246

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 504758818 253 EQRKPEEMMAGLYEFPYIEVEsfddlsdidrliQNMEEYVQAPLVFAGELEEQ---RHAFTHYKVRLVP 318
Cdd:PRK10880 247 EQRPPSGLWGGLFCFPQFADE------------EELRQWLAQRGIAADNLTQLtafRHTFSHFHLDIVP 303
ENDO3c cd00056
endonuclease III; includes endonuclease III (DNA-(apurinic or apyrimidinic site) lyase), ...
 38-195 1.26e-46

endonuclease III; includes endonuclease III (DNA-(apurinic or apyrimidinic site) lyase), alkylbase DNA glycosidases (Alka-family) and other DNA glycosidases


Pssm-ID: 238013 [Multi-domain]  Cd Length: 158  Bit Score: 156.25  E-value: 1.26e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504758818  38 YNVWVSEVMLQQTRAEVAVKYFIEWMEKF-PTIESLATANEEHVMKAWEGLGYYTRARNLLQGARMVMTDFGGKLPDDPL 116
Cdd:cd00056    1 FEVLVSEILSQQTTDKAVNKAYERLFERYgPTPEALAAADEEELRELIRSLGYRRKAKYLKELARAIVEGFGGLVLDDPD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504758818 117 D---LMQIKGLGPYTVHAILAFAFKRRTAAVDGNVLRVISRVFLINAsidlESTKAWVFRIVLSFLPAQDPQVIAEALIE 193
Cdd:cd00056   81 AreeLLALPGVGRKTANVVLLFALGPDAFPVDTHVRRVLKRLGLIPK----KKTPEELEELLEELLPKPYWGEANQALMD 156


                 ..
gi 504758818 194 LG 195
Cdd:cd00056  157 LG 158
ENDO3c smart00478
endonuclease III; includes endonuclease III (DNA-(apurinic or apyrimidinic site) lyase), ...
 46-196 1.71e-42

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: 145.10  E-value: 1.71e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504758818    46 MLQQTRAEVAVKYFIEWMEKFPTIESLATANEEHVMKAWEGLG-YYTRARNLLQGARMVMTDFGGKLPDDPLDLMQIKGL 124
Cdd:smart00478   1 LSQQTTDERVNKATERLFEKFPTPEDLAAADEEELEELIRGLGfYRRKARYLIELARILVEEYGGEVPDDREELLKLPGV 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504758818   125 GPYTVHAILAFAFKRRTAAVDGNVLRVISRVFLinasIDLESTKAWVFRIVLSFLPAQDPQVIAEALIELGA 196
Cdd:smart00478  81 GRKTANAVLSFALGKPFIPVDTHVLRIAKRLGL----VDKKSTPEEVEKLLEKLLPEEDWRELNLLLIDFGR 148
PRK13910 PRK13910
DNA glycosylase MutY; Provisional
 46-354 3.01e-41

DNA glycosylase MutY; Provisional


Pssm-ID: 172427 [Multi-domain]  Cd Length: 289  Bit Score: 146.32  E-value: 3.01e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504758818  46 MLQQTRAEVAV-KYFIEWMEKFPTIESLATANEEHVMKAWEGLGYYTRARNLLQGARMVMTDFGGKLPDDPLDLMQIKGL 124
Cdd:PRK13910   1 MSQQTQINTVVeRFYSPFLEAFPTLKDLANAPLEEVLLLWRGLGYYSRAKNLKKSAEICVKEHHSQLPNDYQSLLKLPGI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504758818 125 GPYTVHAILAFAFKRRTAAVDGNVLRVISRVFLINASIDLESTKawvfRIVLSFLPAQDPQVIAEALIELGACICKRAPK 204
Cdd:PRK13910  81 GAYTANAILCFGFREKSACVDANIKRVLLRLFGLDPNIHAKDLQ----IKANDFLNLNESFNHNQALIDLGALICSPKPK 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504758818 205 CEICPLNSICGAfkegrqKSLPVRHARKKTVTLF---RWVAIVLYKGFIVLEQRKpEEMMAGLYEFPyievesfddlsdi 281
Cdd:PRK13910 157 CAICPLNPYCLG------KNNPEKHTLKKKQEIVqeeRYLGVVIQNNQIALEKIE-QKLYLGMHHFP------------- 216

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 504758818 282 drliqNMEEYVQAPLVFAGELeeqRHAFTHYKVRLVPKIFHAKSEPKSELLYPLDTMDSLPFSSGHRKIKAWL 354
Cdd:PRK13910 217 -----NLKENLEYKLPFLGAI---KHSHTKFKLNLNLYLAAIKDLKNPIRFYSLKDLETLPISSMTLKILNFL 281
HhH-GPD pfam00730
HhH-GPD superfamily base excision DNA repair protein; This family contains a diverse range of ...
 42-163 8.35e-32

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: 117.00  E-value: 8.35e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504758818   42 VSEVMLQQTRAEVAVKYFIEWMEK-FPTIESLATANEEHVMKAWEGLGYYTR-ARNLLQGARMVMTDFGGKLPDDPLDLM 119
Cdd:pfam00730   1 VSAILSQQTSDKAVNKITERLFEKfFPTPEDLADADEEELRELIRGLGFYRRkAKYLKELARILVEGYGGEVPLDEEELE 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 504758818  120 Q-IKGLGPYTVHAILAFAFKRR--TAAVDGNVLRVISRVFLINASID 163
Cdd:pfam00730  81 AlLKGVGRWTAEAVLIFALGRPdpLPVVDTHVRRVLKRLGLIKEKPT 127
Nth COG0177
Endonuclease III [Replication, recombination and repair];
17-214 1.01e-30

Endonuclease III [Replication, recombination and repair];


Pssm-ID: 439947 [Multi-domain]  Cd Length: 198  Bit Score: 115.58  E-value: 1.01e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504758818  17 KLKQWFTDNKRSFPWRDnpsPYNVWVSEVMLQQTRAEVAVKYFIEWMEKFPTIESLATANEEHVMKAWEGLGYY-TRARN 95
Cdd:COG0177    3 RLKELYPDAKTELDYRD---PFELLVATILSAQTTDERVNKATPRLFARYPTPEALAAADLEELEELIRPIGLYrNKAKN 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504758818  96 LLQGARMVMTDFGGKLPDDPLDLMQIKGLGPYTVHAILAFAFKRRTAAVDGNVLRVISRVFLINASiDLESTKawvfRIV 175
Cdd:COG0177   80 IIALARILVEKYGGEVPETREELESLPGVGRKTANVVLNFAFGKPAIAVDTHVHRVSNRLGLVPGK-DPEEVE----KDL 154

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 504758818 176 LSFLPAQDPQVIAEALIELGACICK-RAPKCEICPLNSIC 214
Cdd:COG0177  155 MKLIPKEYWGDLHHLLILHGRYICKaRKPKCEECPLADLC 194
NUDIX_DNA_Glycosylase_C-MutY cd03431
C-terminal domain of DNA glycosylase; DNA glycosylase (MutY in bacteria and hMYH in humans) is ...
 236-350 1.01e-17

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: 78.11  E-value: 1.01e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504758818 236 TLFRWVAIVLYKGFIVLEQRKPEEMMAGLYEFPYIEVESFDDLSDIDRLIQNMEeyvqaPLVFAGELEEQRHAFTHYKVR 315
Cdd:cd03431    3 ERYFTVLVLRDGGRVLLEKRPEKGLLAGLWEFPLVETEEEEEEAEALLGLLAEE-----LLLILEPLGEVKHVFSHFRLH 77

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 504758818 316 LVPKIFHAKSEPKSE----LLYPLDTMDSLPFSSGHRKI 350
Cdd:cd03431   78 ITVYLVELPEAPPAApdegRWVDLEELDEYALPAPMRKL 116
HP0602 COG2231
3-Methyladenine DNA glycosylase, HhH-GPD/Endo3 superfamily [Replication, recombination and ...
 36-214 2.12e-13

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


Pssm-ID: 441832 [Multi-domain]  Cd Length: 220  Bit Score: 68.72  E-value: 2.12e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504758818  36 SPYNVWVSEVMLQQTRAEVaVKYFIEWMEKFP--TIESLATANEEHVMKAWEGLGYYTR-ARNLLQGARMVMTDFGG--- 109
Cdd:COG2231   28 TPFEVIVGAILTQNTSWKN-VEKAIANLKEAGllDPEALAALDPEELAELIRPSGFYNQkAKRLKNLARWLVERYGGgle 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504758818 110 ---KLPDDPL--DLMQIKGLGPYTVHAILAFAFKRRTAAVDGNVLRVISRVFLINASIDLESTKAWVFRIvlsfLPAqDP 184
Cdd:COG2231  107 klkALPTEELreELLSLKGIGPETADSILLYAFNRPVFVVDAYTRRIFSRLGLIEEDASYDELQRLFEEN----LPP-DV 181

                        170       180       190
                 ....*....|....*....|....*....|...
gi 504758818 185 QVIAE--ALI-ELGACICKRAPKCEICPLNSIC 214
Cdd:COG2231  182 ALYNEfhALIvEHGKEYCKKKPKCEECPLRDLC 214
NUDIX_4 pfam14815
NUDIX domain;
240-350 3.95e-12

NUDIX domain;


Pssm-ID: 464330 [Multi-domain]  Cd Length: 114  Bit Score: 62.33  E-value: 3.95e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504758818  240 WVAIVLYKGFIVLEQRKPEEMMAGLYEFPyiEVESFDDLSDIDRLIQNMEeyvQAPLVFAGELEEQRHAFTHYKVRL--- 316
Cdd:pfam14815   2 VLVIRNGDGRVLLRKRPEKGLLGGLWEFP--GGKVEPGETLEEALARLEE---LGIEVEVLEPGTVKHVFTHFRLTLhvy 76

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 504758818  317 -VPKIFHAKSEPKSELLYPLDTMDSLPFSSGHRKI 350
Cdd:pfam14815  77 lVREVEGEEEPQQELRWVTPEELDKYALPAAVRKI 111
PRK10702 PRK10702
endonuclease III; Provisional
 89-219 9.51e-09

endonuclease III; Provisional


Pssm-ID: 182661 [Multi-domain]  Cd Length: 211  Bit Score: 55.02  E-value: 9.51e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504758818  89 YYTRARNLLQGARMVMTDFGGKLPDDPLDLMQIKGLGPYTVHAILAFAFKRRTAAVDGNVLRVISRVFLINASiDLESTK 168
Cdd:PRK10702  82 YNSKAENVIKTCRILLEQHNGEVPEDRAALEALPGVGRKTANVVLNTAFGWPTIAVDTHIFRVCNRTQFAPGK-NVEQVE 160

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 504758818 169 AWVFRIVlsflPAQDPQVIAEALIELGACIC-KRAPKCEICPLNSICgAFKE 219
Cdd:PRK10702 161 EKLLKVV----PAEFKVDCHHWLILHGRYTCiARKPRCGSCIIEDLC-EYKE 207
HHH pfam00633
Helix-hairpin-helix motif; The helix-hairpin-helix DNA-binding motif is found to be duplicated ...
 106-135 3.06e-03

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: 34.70  E-value: 3.06e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 504758818  106 DFGGKLPDDPLDLMQIKGLGPYTVHAILAF 135
Cdd:pfam00633   1 SLEGLIPASVEELLALPGVGPKTAEAILSY 30
EndIII_4Fe-2S pfam10576
Iron-sulfur binding domain of endonuclease III; Escherichia coli endonuclease III (EC 4.2.99. ...
 199-214 3.13e-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: 3.13e-03
                          10
                  ....*....|....*..
gi 504758818  199 CK-RAPKCEICPLNSIC 214
Cdd:pfam10576   1 CTaRKPKCEECPLADLC 17
FES smart00525
iron-sulpphur binding domain in DNA-(apurinic or apyrimidinic site) lyase (subfamily of ENDO3); ...
 198-217 3.72e-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: 34.45  E-value: 3.72e-03
                           10        20
                   ....*....|....*....|.
gi 504758818   198 ICK-RAPKCEICPLNSICGAF 217
Cdd:smart00525   1 ICTaRKPRCDECPLKDLCPAY 21
 
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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