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Conserved domains on  [gi|1958774515|ref|XP_038965132|]
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adenine DNA glycosylase isoform X5 [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

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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 ...
 1-348 9.50e-116

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: 341.35  E-value: 9.50e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774515   1 MQKWPTLQDLASASLEEVNQLWSGLGYYSRGRRLQEGARKVVEELGGHVPRTAETLQQLlPGVGRYTAGAIASIAFDQVT 80
Cdd:COG1194    55 LERFPTVEALAAAPEDEVLKLWEGLGYYSRARNLHKAAQQVVEEHGGVFPDTYEELLAL-PGIGPYTAAAIASIAFGEPA 133

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774515  81 GVVDGNVIRVLCRVRAIGADPTSSFVSHHLWDLAQQLVDPARPGDFNQAAMELGATVCTPQRPLCSHCPVQSLCRAHQRv 160
Cdd:COG1194   134 PIVDGNVKRVLSRLFAIEGPIGSPAAKKELWALAEELLPPERPGDFNQALMDLGATVCTPKKPKCLLCPLQDDCAAFAE- 212

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774515 161 gqgqlsalpGSPDieecalntrqcqlclpstnpwdpnmgvvNFPRKASRRPPREEYSATCVVEQPGAtggplILLVQRPN 240
Cdd:COG1194   213 ---------GRQE----------------------------ELPVKKPKKKKPERYGAALVIRDDGR-----VLLEKRPP 250

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774515 241 SGLLAGLWEFPSVtlEPSGQHQHKALLQELQHWsAPLPTTPLQHLGEslpptpqVIHVFSHIKLTYQVYSLALEGQTPAS 320
Cdd:COG1194   251 KGLWGGLWEFPEF--EWEEAEDPEALERWLREE-LGLEVEWLEPLGT-------VRHVFTHFRLHLTVYLARVPAGPPAE 320

                         330       340
                  ....*....|....*....|....*...
gi 1958774515 321 ttPPGARWLTWEEFRNAAVSTAMKKVFR 348
Cdd:COG1194   321 --PDGGRWVPLEELAALPLPAPMRKLLK 346
 
Name Accession Description Interval E-value
MutY COG1194
Adenine-specific DNA glycosylase, acts on AG and A-oxoG pairs [Replication, recombination and ...
 1-348 9.50e-116

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: 341.35  E-value: 9.50e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774515   1 MQKWPTLQDLASASLEEVNQLWSGLGYYSRGRRLQEGARKVVEELGGHVPRTAETLQQLlPGVGRYTAGAIASIAFDQVT 80
Cdd:COG1194    55 LERFPTVEALAAAPEDEVLKLWEGLGYYSRARNLHKAAQQVVEEHGGVFPDTYEELLAL-PGIGPYTAAAIASIAFGEPA 133

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774515  81 GVVDGNVIRVLCRVRAIGADPTSSFVSHHLWDLAQQLVDPARPGDFNQAAMELGATVCTPQRPLCSHCPVQSLCRAHQRv 160
Cdd:COG1194   134 PIVDGNVKRVLSRLFAIEGPIGSPAAKKELWALAEELLPPERPGDFNQALMDLGATVCTPKKPKCLLCPLQDDCAAFAE- 212

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774515 161 gqgqlsalpGSPDieecalntrqcqlclpstnpwdpnmgvvNFPRKASRRPPREEYSATCVVEQPGAtggplILLVQRPN 240
Cdd:COG1194   213 ---------GRQE----------------------------ELPVKKPKKKKPERYGAALVIRDDGR-----VLLEKRPP 250

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774515 241 SGLLAGLWEFPSVtlEPSGQHQHKALLQELQHWsAPLPTTPLQHLGEslpptpqVIHVFSHIKLTYQVYSLALEGQTPAS 320
Cdd:COG1194   251 KGLWGGLWEFPEF--EWEEAEDPEALERWLREE-LGLEVEWLEPLGT-------VRHVFTHFRLHLTVYLARVPAGPPAE 320

                         330       340
                  ....*....|....*....|....*...
gi 1958774515 321 ttPPGARWLTWEEFRNAAVSTAMKKVFR 348
Cdd:COG1194   321 --PDGGRWVPLEELAALPLPAPMRKLLK 346
PRK10880 PRK10880
adenine DNA glycosylase;
1-304 1.99e-45

adenine DNA glycosylase;


Pssm-ID: 182805 [Multi-domain]  Cd Length: 350  Bit Score: 159.88  E-value: 1.99e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774515   1 MQKWPTLQDLASASLEEVNQLWSGLGYYSRGRRLQEGARKVVEELGGHVPRTAETLQQlLPGVGRYTAGAIASIAFDQVT 80
Cdd:PRK10880   56 MARFPTVTDLANAPLDEVLHLWTGLGYYARARNLHKAAQQVATLHGGEFPETFEEVAA-LPGVGRSTAGAILSLSLGKHF 134

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774515  81 GVVDGNVIRVLCRVRAIGADPTSSFVSHHLWDLAQQlVDPARP-GDFNQAAMELGATVCTPQRPLCSHCPVQSLCRAHqr 159
Cdd:PRK10880  135 PILDGNVKRVLARCYAVSGWPGKKEVENRLWQLSEQ-VTPAVGvERFNQAMMDLGAMVCTRSKPKCELCPLQNGCIAY-- 211

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774515 160 vGQGQLSALPGSPdieecalntrqcqlclpstnpwdpnmgvvnfPRKAsrRPPREEYsatCVVEQPGATggplILLVQRP 239
Cdd:PRK10880  212 -ANHSWALYPGKK-------------------------------PKQT--LPERTGY---FLLLQHGDE----VWLEQRP 250

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958774515 240 NSGLLAGLWEFPSVTLEpsgqhqhkallQELQHWsaplpttpLQHLGESLPPTPQVI---HVFSHIKL 304
Cdd:PRK10880  251 PSGLWGGLFCFPQFADE-----------EELRQW--------LAQRGIAADNLTQLTafrHTFSHFHL 299
ENDO3c smart00478
endonuclease III; includes endonuclease III (DNA-(apurinic or apyrimidinic site) lyase), ...
 1-136 9.37e-36

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: 128.15  E-value: 9.37e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774515    1 MQKWPTLQDLASASLEEVNQLWSGLG-YYSRGRRLQEGARKVVEELGGHVPRTAETLQQLlPGVGRYTAGAIASIAFDQV 79
Cdd:smart00478  18 FEKFPTPEDLAAADEEELEELIRGLGfYRRKARYLIELARILVEEYGGEVPDDREELLKL-PGVGRKTANAVLSFALGKP 96

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1958774515   80 TGVVDGNVIRVLCRVRAIGADPTSSfvshHLWDLAQQLVDPARPGDFNQAAMELGAT 136
Cdd:smart00478  97 FIPVDTHVLRIAKRLGLVDKKSTPE----EVEKLLEKLLPEEDWRELNLLLIDFGRT 149
ENDO3c cd00056
endonuclease III; includes endonuclease III (DNA-(apurinic or apyrimidinic site) lyase), ...
 1-134 1.51e-35

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: 128.13  E-value: 1.51e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774515   1 MQKW-PTLQDLASASLEEVNQLWSGLGYYSRGRRLQEGARKVVEELGGHVPRTAETLQQL--LPGVGRYTAGAIASIAFD 77
Cdd:cd00056    26 FERYgPTPEALAAADEEELRELIRSLGYRRKAKYLKELARAIVEGFGGLVLDDPDAREELlaLPGVGRKTANVVLLFALG 105

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1958774515  78 QVTGVVDGNVIRVLCRVRAIGADPTssfvSHHLWDLAQQLVDPARPGDFNQAAMELG 134
Cdd:cd00056   106 PDAFPVDTHVRRVLKRLGLIPKKKT----PEELEELLEELLPKPYWGEANQALMDLG 158
HhH-GPD pfam00730
HhH-GPD superfamily base excision DNA repair protein; This family contains a diverse range of ...
 4-116 1.53e-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: 119.31  E-value: 1.53e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774515   4 WPTLQDLASASLEEVNQLWSGLGYY-SRGRRLQEGARKVVEELGGHVPRTAETLQQLLPGVGRYTAGAIASIAF--DQVT 80
Cdd:pfam00730  26 FPTPEDLADADEEELRELIRGLGFYrRKAKYLKELARILVEGYGGEVPLDEEELEALLKGVGRWTAEAVLIFALgrPDPL 105

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1958774515  81 GVVDGNVIRVLCRVRAIGADPTSSFVSHHLWDLAQQ 116
Cdd:pfam00730 106 PVVDTHVRRVLKRLGLIKEKPTPKEVERELEELWPP 141
nth TIGR01083
endonuclease III; This equivalog model identifes nth members of the pfam00730 superfamily ...
 2-145 2.84e-21

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: 90.52  E-value: 2.84e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774515   2 QKWPTLQDLASASLEEVNQLWSGLGYY-SRGRRLQEGARKVVEELGGHVPRTAETLQQLlPGVGRYTAGAIASIAFDQVT 80
Cdd:TIGR01083  54 EVYPTPQALAQAGLEELEEYIKSIGLYrNKAKNIIELCRKLVERYGGEVPEDREELVKL-PGVGRKTANVVLNVAFGIPA 132

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958774515  81 GVVDGNVIRVLCRVR-AIGADPTSsfVSHHLwdlaQQLVDPARPGDFNQAAMELGATVCTPQRPLC 145
Cdd:TIGR01083 133 IAVDTHVFRVSNRLGlSKGKDPIK--VEEDL----MKLVPREFWVKLHHWLILHGRYTCKARKPLC 192
 
Name Accession Description Interval E-value
MutY COG1194
Adenine-specific DNA glycosylase, acts on AG and A-oxoG pairs [Replication, recombination and ...
 1-348 9.50e-116

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: 341.35  E-value: 9.50e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774515   1 MQKWPTLQDLASASLEEVNQLWSGLGYYSRGRRLQEGARKVVEELGGHVPRTAETLQQLlPGVGRYTAGAIASIAFDQVT 80
Cdd:COG1194    55 LERFPTVEALAAAPEDEVLKLWEGLGYYSRARNLHKAAQQVVEEHGGVFPDTYEELLAL-PGIGPYTAAAIASIAFGEPA 133

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774515  81 GVVDGNVIRVLCRVRAIGADPTSSFVSHHLWDLAQQLVDPARPGDFNQAAMELGATVCTPQRPLCSHCPVQSLCRAHQRv 160
Cdd:COG1194   134 PIVDGNVKRVLSRLFAIEGPIGSPAAKKELWALAEELLPPERPGDFNQALMDLGATVCTPKKPKCLLCPLQDDCAAFAE- 212

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774515 161 gqgqlsalpGSPDieecalntrqcqlclpstnpwdpnmgvvNFPRKASRRPPREEYSATCVVEQPGAtggplILLVQRPN 240
Cdd:COG1194   213 ---------GRQE----------------------------ELPVKKPKKKKPERYGAALVIRDDGR-----VLLEKRPP 250

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774515 241 SGLLAGLWEFPSVtlEPSGQHQHKALLQELQHWsAPLPTTPLQHLGEslpptpqVIHVFSHIKLTYQVYSLALEGQTPAS 320
Cdd:COG1194   251 KGLWGGLWEFPEF--EWEEAEDPEALERWLREE-LGLEVEWLEPLGT-------VRHVFTHFRLHLTVYLARVPAGPPAE 320

                         330       340
                  ....*....|....*....|....*...
gi 1958774515 321 ttPPGARWLTWEEFRNAAVSTAMKKVFR 348
Cdd:COG1194   321 --PDGGRWVPLEELAALPLPAPMRKLLK 346
PRK10880 PRK10880
adenine DNA glycosylase;
1-304 1.99e-45

adenine DNA glycosylase;


Pssm-ID: 182805 [Multi-domain]  Cd Length: 350  Bit Score: 159.88  E-value: 1.99e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774515   1 MQKWPTLQDLASASLEEVNQLWSGLGYYSRGRRLQEGARKVVEELGGHVPRTAETLQQlLPGVGRYTAGAIASIAFDQVT 80
Cdd:PRK10880   56 MARFPTVTDLANAPLDEVLHLWTGLGYYARARNLHKAAQQVATLHGGEFPETFEEVAA-LPGVGRSTAGAILSLSLGKHF 134

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774515  81 GVVDGNVIRVLCRVRAIGADPTSSFVSHHLWDLAQQlVDPARP-GDFNQAAMELGATVCTPQRPLCSHCPVQSLCRAHqr 159
Cdd:PRK10880  135 PILDGNVKRVLARCYAVSGWPGKKEVENRLWQLSEQ-VTPAVGvERFNQAMMDLGAMVCTRSKPKCELCPLQNGCIAY-- 211

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774515 160 vGQGQLSALPGSPdieecalntrqcqlclpstnpwdpnmgvvnfPRKAsrRPPREEYsatCVVEQPGATggplILLVQRP 239
Cdd:PRK10880  212 -ANHSWALYPGKK-------------------------------PKQT--LPERTGY---FLLLQHGDE----VWLEQRP 250

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958774515 240 NSGLLAGLWEFPSVTLEpsgqhqhkallQELQHWsaplpttpLQHLGESLPPTPQVI---HVFSHIKL 304
Cdd:PRK10880  251 PSGLWGGLFCFPQFADE-----------EELRQW--------LAQRGIAADNLTQLTafrHTFSHFHL 299
ENDO3c smart00478
endonuclease III; includes endonuclease III (DNA-(apurinic or apyrimidinic site) lyase), ...
 1-136 9.37e-36

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: 128.15  E-value: 9.37e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774515    1 MQKWPTLQDLASASLEEVNQLWSGLG-YYSRGRRLQEGARKVVEELGGHVPRTAETLQQLlPGVGRYTAGAIASIAFDQV 79
Cdd:smart00478  18 FEKFPTPEDLAAADEEELEELIRGLGfYRRKARYLIELARILVEEYGGEVPDDREELLKL-PGVGRKTANAVLSFALGKP 96

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1958774515   80 TGVVDGNVIRVLCRVRAIGADPTSSfvshHLWDLAQQLVDPARPGDFNQAAMELGAT 136
Cdd:smart00478  97 FIPVDTHVLRIAKRLGLVDKKSTPE----EVEKLLEKLLPEEDWRELNLLLIDFGRT 149
ENDO3c cd00056
endonuclease III; includes endonuclease III (DNA-(apurinic or apyrimidinic site) lyase), ...
 1-134 1.51e-35

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: 128.13  E-value: 1.51e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774515   1 MQKW-PTLQDLASASLEEVNQLWSGLGYYSRGRRLQEGARKVVEELGGHVPRTAETLQQL--LPGVGRYTAGAIASIAFD 77
Cdd:cd00056    26 FERYgPTPEALAAADEEELRELIRSLGYRRKAKYLKELARAIVEGFGGLVLDDPDAREELlaLPGVGRKTANVVLLFALG 105

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1958774515  78 QVTGVVDGNVIRVLCRVRAIGADPTssfvSHHLWDLAQQLVDPARPGDFNQAAMELG 134
Cdd:cd00056   106 PDAFPVDTHVRRVLKRLGLIPKKKT----PEELEELLEELLPKPYWGEANQALMDLG 158
HhH-GPD pfam00730
HhH-GPD superfamily base excision DNA repair protein; This family contains a diverse range of ...
 4-116 1.53e-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: 119.31  E-value: 1.53e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774515   4 WPTLQDLASASLEEVNQLWSGLGYY-SRGRRLQEGARKVVEELGGHVPRTAETLQQLLPGVGRYTAGAIASIAF--DQVT 80
Cdd:pfam00730  26 FPTPEDLADADEEELRELIRGLGFYrRKAKYLKELARILVEGYGGEVPLDEEELEALLKGVGRWTAEAVLIFALgrPDPL 105

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1958774515  81 GVVDGNVIRVLCRVRAIGADPTSSFVSHHLWDLAQQ 116
Cdd:pfam00730 106 PVVDTHVRRVLKRLGLIKEKPTPKEVERELEELWPP 141
Nth COG0177
Endonuclease III [Replication, recombination and repair];
2-155 2.00e-29

Endonuclease III [Replication, recombination and repair];


Pssm-ID: 439947 [Multi-domain]  Cd Length: 198  Bit Score: 112.88  E-value: 2.00e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774515   2 QKWPTLQDLASASLEEVNQLWSGLGYY-SRGRRLQEGARKVVEELGGHVPRTAETLQQLlPGVGRYTAGAIASIAFDQVT 80
Cdd:COG0177    47 ARYPTPEALAAADLEELEELIRPIGLYrNKAKNIIALARILVEKYGGEVPETREELESL-PGVGRKTANVVLNFAFGKPA 125

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958774515  81 GVVDGNVIRVLCRVR-AIGADPTSsfVSHHLwdlaQQLVDPARPGDFNQAAMELGATVCTPQRPLCSHCPVQSLCR 155
Cdd:COG0177   126 IAVDTHVHRVSNRLGlVPGKDPEE--VEKDL----MKLIPKEYWGDLHHLLILHGRYICKARKPKCEECPLADLCP 195
PRK13910 PRK13910
DNA glycosylase MutY; Provisional
 1-154 2.73e-27

DNA glycosylase MutY; Provisional


Pssm-ID: 172427 [Multi-domain]  Cd Length: 289  Bit Score: 109.73  E-value: 2.73e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774515   1 MQKWPTLQDLASASLEEVNQLWSGLGYYSRGRRLQEGARKVVEELGGHVPRTAETLQQlLPGVGRYTAGAIASIAFDQVT 80
Cdd:PRK13910   19 LEAFPTLKDLANAPLEEVLLLWRGLGYYSRAKNLKKSAEICVKEHHSQLPNDYQSLLK-LPGIGAYTANAILCFGFREKS 97

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958774515  81 GVVDGNVIRVLCRVraIGADPtsSFVSHHLWDLAQQLVDPARPGDFNQAAMELGATVCTPqRPLCSHCPVQSLC 154
Cdd:PRK13910   98 ACVDANIKRVLLRL--FGLDP--NIHAKDLQIKANDFLNLNESFNHNQALIDLGALICSP-KPKCAICPLNPYC 166
NUDIX_DNA_Glycosylase_C-MutY cd03431
C-terminal domain of DNA glycosylase; DNA glycosylase (MutY in bacteria and hMYH in humans) is ...
 212-347 1.78e-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: 102.38  E-value: 1.78e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774515 212 PREEYSATCVVEQPGAtggplILLVQRPNSGLLAGLWEFPSVTLEPSGQhqhkaLLQELQHWSAPLPTTPLQHLGEslpp 291
Cdd:cd03431     1 VPERYFTVLVLRDGGR-----VLLEKRPEKGLLAGLWEFPLVETEEEEE-----EAEALLGLLAEELLLILEPLGE---- 66

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1958774515 292 tpqVIHVFSHIKLTYQVYSLALEGQTPASttPPGARWLTWEEFRNAAVSTAMKKVF 347
Cdd:cd03431    67 ---VKHVFSHFRLHITVYLVELPEAPPAA--PDEGRWVDLEELDEYALPAPMRKLL 117
nth TIGR01083
endonuclease III; This equivalog model identifes nth members of the pfam00730 superfamily ...
 2-145 2.84e-21

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: 90.52  E-value: 2.84e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774515   2 QKWPTLQDLASASLEEVNQLWSGLGYY-SRGRRLQEGARKVVEELGGHVPRTAETLQQLlPGVGRYTAGAIASIAFDQVT 80
Cdd:TIGR01083  54 EVYPTPQALAQAGLEELEEYIKSIGLYrNKAKNIIELCRKLVERYGGEVPEDREELVKL-PGVGRKTANVVLNVAFGIPA 132

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958774515  81 GVVDGNVIRVLCRVR-AIGADPTSsfVSHHLwdlaQQLVDPARPGDFNQAAMELGATVCTPQRPLC 145
Cdd:TIGR01083 133 IAVDTHVFRVSNRLGlSKGKDPIK--VEEDL----MKLVPREFWVKLHHWLILHGRYTCKARKPLC 192
NUDIX_4 pfam14815
NUDIX domain;
233-348 3.73e-19

NUDIX domain;


Pssm-ID: 464330 [Multi-domain]  Cd Length: 114  Bit Score: 82.36  E-value: 3.73e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774515 233 ILLVQRPNSGLLAGLWEFPSVTLEPSGQHQHKALLQELQHwsapLPTTPLQHLgeslpptpQVIHVFSHIKLTYQVYSLA 312
Cdd:pfam14815  12 VLLRKRPEKGLLGGLWEFPGGKVEPGETLEEALARLEELG----IEVEVLEPG--------TVKHVFTHFRLTLHVYLVR 79

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1958774515 313 LEGQTPASttPPGARWLTWEEFRNAAVSTAMKKVFR 348
Cdd:pfam14815  80 EVEGEEEP--QQELRWVTPEELDKYALPAAVRKILE 113
HP0602 COG2231
3-Methyladenine DNA glycosylase, HhH-GPD/Endo3 superfamily [Replication, recombination and ...
 6-160 2.18e-08

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


Pssm-ID: 441832 [Multi-domain]  Cd Length: 220  Bit Score: 54.08  E-value: 2.18e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774515   6 TLQDLASASLEEVNQLWSGLGYYSR-GRRLQEGARKVVEELGGHVPR-----TAETLQQLL--PGVGRYTAGAIASIAFD 77
Cdd:COG2231    61 DPEALAALDPEELAELIRPSGFYNQkAKRLKNLARWLVERYGGGLEKlkalpTEELREELLslKGIGPETADSILLYAFN 140

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774515  78 QVTGVVDGNVIRVLcrVRAIGADPTSSFvshhlwDLAQQLVDPARPGDFNQA----AM--ELGATVCTPqRPLCSHCPVQ 151
Cdd:COG2231   141 RPVFVVDAYTRRIF--SRLGLIEEDASY------DELQRLFEENLPPDVALYnefhALivEHGKEYCKK-KPKCEECPLR 211


                  ....*....
gi 1958774515 152 SLCRAHQRV 160
Cdd:COG2231   212 DLCPYGGQE 220
PRK10702 PRK10702
endonuclease III; Provisional
 27-160 9.68e-07

endonuclease III; Provisional


Pssm-ID: 182661 [Multi-domain]  Cd Length: 211  Bit Score: 49.25  E-value: 9.68e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774515  27 YYSRGRRLQEGARKVVEELGGHVPRTAETLQQLlPGVGRYTAGAIASIAFDQVTGVVDGNVIRVLCRvraigadptSSFV 106
Cdd:PRK10702   82 YNSKAENVIKTCRILLEQHNGEVPEDRAALEAL-PGVGRKTANVVLNTAFGWPTIAVDTHIFRVCNR---------TQFA 151

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1958774515 107 SHHLWDLAQQLVDPARPGDF----NQAAMELGATVCTPQRPLCSHCPVQSLCRAHQRV 160
Cdd:PRK10702  152 PGKNVEQVEEKLLKVVPAEFkvdcHHWLILHGRYTCIARKPRCGSCIIEDLCEYKEKV 209
PRK10546 PRK10546
pyrimidine (deoxy)nucleoside triphosphate diphosphatase;
221-271 3.21e-05

pyrimidine (deoxy)nucleoside triphosphate diphosphatase;


Pssm-ID: 182536 [Multi-domain]  Cd Length: 135  Bit Score: 43.19  E-value: 3.21e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1958774515 221 VVEQPGAtggplILLVQRPNSGLLAGLWEFPSVTLEPsGQHQHKALLQELQ 271
Cdd:PRK10546   10 IIERDGK-----ILLAQRPAHSDQAGLWEFAGGKVEP-GESQPQALIRELR 54
HHH pfam00633
Helix-hairpin-helix motif; The helix-hairpin-helix DNA-binding motif is found to be duplicated ...
 44-74 5.99e-05

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: 39.71  E-value: 5.99e-05
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1958774515  44 ELGGHVPRTAETLQQLlPGVGRYTAGAIASI 74
Cdd:pfam00633   1 SLEGLIPASVEELLAL-PGVGPKTAEAILSY 30
FES smart00525
iron-sulpphur binding domain in DNA-(apurinic or apyrimidinic site) lyase (subfamily of ENDO3); ...
 137-156 1.32e-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: 1.32e-03
                           10        20
                   ....*....|....*....|
gi 1958774515  137 VCTPQRPLCSHCPVQSLCRA 156
Cdd:smart00525   1 ICTARKPRCDECPLKDLCPA 20
EndIII_4Fe-2S pfam10576
Iron-sulfur binding domain of endonuclease III; Escherichia coli endonuclease III (EC 4.2.99. ...
 138-154 2.82e-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: 2.82e-03
                          10
                  ....*....|....*..
gi 1958774515 138 CTPQRPLCSHCPVQSLC 154
Cdd:pfam10576   1 CTARKPKCEECPLADLC 17
NUDIX_MutT_NudA_like cd03425
MutT pyrophosphohydrolase; The MutT pyrophosphohydrolase is a prototypical NUDIX hydrolase ...
 233-251 5.44e-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: 5.44e-03
                          10
                  ....*....|....*....
gi 1958774515 233 ILLVQRPNSGLLAGLWEFP 251
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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