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Conserved domains on  [gi|2462509453|ref|XP_054192705|]
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adenine DNA glycosylase isoform X9 [Homo sapiens]

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 ...
 15-345 8.20e-111

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: 328.25  E-value: 8.20e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509453  15 EVNQLWAGLGYYSRGRRLQEGARKVVEELGGHMPRTAETLQQLlPGVGRYTAGAIASIAFGQATGVVDGNVARVLCRVRA 94
Cdd:COG1194    71 EVLKLWEGLGYYSRARNLHKAAQQVVEEHGGVFPDTYEELLAL-PGIGPYTAAAIASIAFGEPAPIVDGNVKRVLSRLFA 149

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509453  95 IGADPSSTLVSQQLWGLAQQLVDPARPGDFNQAAMELGATVCTPQRPLCSQCPVESLCRARQRVEQEQLlasgslsgspd 174
Cdd:COG1194   150 IEGPIGSPAAKKELWALAEELLPPERPGDFNQALMDLGATVCTPKKPKCLLCPLQDDCAAFAEGRQEEL----------- 218

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509453 175 veecapntgqchlclppsepwdqtlgvvnfPRKASRKPPREESSATCVLEQPGalgaQILLVQRPNSGLLAGLWEFPSVT 254
Cdd:COG1194   219 ------------------------------PVKKPKKKKPERYGAALVIRDDG----RVLLEKRPPKGLWGGLWEFPEFE 264

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509453 255 WEPSEQLQrkALLQELQRWAGpLPATHLRHLGEVVHTFSHIKLTYQVYGLALEGQTPVTtvPPGARWLTQEEFHTAAVST 334
Cdd:COG1194   265 WEEAEDPE--ALERWLREELG-LEVEWLEPLGTVRHVFTHFRLHLTVYLARVPAGPPAE--PDGGRWVPLEELAALPLPA 339

                         330
                  ....*....|.
gi 2462509453 335 AMKKVFRVYQG 345
Cdd:COG1194   340 PMRKLLKALLK 350
 
Name Accession Description Interval E-value
MutY COG1194
Adenine-specific DNA glycosylase, acts on AG and A-oxoG pairs [Replication, recombination and ...
 15-345 8.20e-111

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: 328.25  E-value: 8.20e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509453  15 EVNQLWAGLGYYSRGRRLQEGARKVVEELGGHMPRTAETLQQLlPGVGRYTAGAIASIAFGQATGVVDGNVARVLCRVRA 94
Cdd:COG1194    71 EVLKLWEGLGYYSRARNLHKAAQQVVEEHGGVFPDTYEELLAL-PGIGPYTAAAIASIAFGEPAPIVDGNVKRVLSRLFA 149

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509453  95 IGADPSSTLVSQQLWGLAQQLVDPARPGDFNQAAMELGATVCTPQRPLCSQCPVESLCRARQRVEQEQLlasgslsgspd 174
Cdd:COG1194   150 IEGPIGSPAAKKELWALAEELLPPERPGDFNQALMDLGATVCTPKKPKCLLCPLQDDCAAFAEGRQEEL----------- 218

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509453 175 veecapntgqchlclppsepwdqtlgvvnfPRKASRKPPREESSATCVLEQPGalgaQILLVQRPNSGLLAGLWEFPSVT 254
Cdd:COG1194   219 ------------------------------PVKKPKKKKPERYGAALVIRDDG----RVLLEKRPPKGLWGGLWEFPEFE 264

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509453 255 WEPSEQLQrkALLQELQRWAGpLPATHLRHLGEVVHTFSHIKLTYQVYGLALEGQTPVTtvPPGARWLTQEEFHTAAVST 334
Cdd:COG1194   265 WEEAEDPE--ALERWLREELG-LEVEWLEPLGTVRHVFTHFRLHLTVYLARVPAGPPAE--PDGGRWVPLEELAALPLPA 339

                         330
                  ....*....|.
gi 2462509453 335 AMKKVFRVYQG 345
Cdd:COG1194   340 PMRKLLKALLK 350
PRK10880 PRK10880
adenine DNA glycosylase;
12-297 5.31e-44

adenine DNA glycosylase;


Pssm-ID: 182805 [Multi-domain]  Cd Length: 350  Bit Score: 156.02  E-value: 5.31e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509453  12 PVMEVNQLWAGLGYYSRGRRLQEGARKVVEELGGHMPRTAETLQQLlPGVGRYTAGAIASIAFGQATGVVDGNVARVLCR 91
Cdd:PRK10880   69 PLDEVLHLWTGLGYYARARNLHKAAQQVATLHGGEFPETFEEVAAL-PGVGRSTAGAILSLSLGKHFPILDGNVKRVLAR 147

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509453  92 VRAIGADPSSTLVSQQLWGLAQQlVDPARP-GDFNQAAMELGATVCTPQRPLCSQCPVESLCRARqrveqeqllASGSls 170
Cdd:PRK10880  148 CYAVSGWPGKKEVENRLWQLSEQ-VTPAVGvERFNQAMMDLGAMVCTRSKPKCELCPLQNGCIAY---------ANHS-- 215

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509453 171 gspdveecapntgqchlclppsepWDQtlgvvnFPRKASRKPPREESSATCVLEQpgalGAQILLVQRPNSGLLAGLWEF 250
Cdd:PRK10880  216 ------------------------WAL------YPGKKPKQTLPERTGYFLLLQH----GDEVWLEQRPPSGLWGGLFCF 261

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 2462509453 251 PSVTWEpseqlqrkallQELQRW--AGPLPATHLRHLGEVVHTFSHIKL 297
Cdd:PRK10880  262 PQFADE-----------EELRQWlaQRGIAADNLTQLTAFRHTFSHFHL 299
NUDIX_DNA_Glycosylase_C-MutY cd03431
C-terminal domain of DNA glycosylase; DNA glycosylase (MutY in bacteria and hMYH in humans) is ...
 213-340 2.50e-31

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: 115.48  E-value: 2.50e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509453 213 PREESSATCVLEQPGalgaQILLVQRPNSGLLAGLWEFPSVTWEPSEQlqrkaLLQELQRWAGPLPATHLRHLGEVVHTF 292
Cdd:cd03431     1 VPERYFTVLVLRDGG----RVLLEKRPEKGLLAGLWEFPLVETEEEEE-----EAEALLGLLAEELLLILEPLGEVKHVF 71

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 2462509453 293 SHIKLTYQVYGLALEGQTPVTtvPPGARWLTQEEFHTAAVSTAMKKVF 340
Cdd:cd03431    72 SHFRLHITVYLVELPEAPPAA--PDEGRWVDLEELDEYALPAPMRKLL 117
ENDO3c smart00478
endonuclease III; includes endonuclease III (DNA-(apurinic or apyrimidinic site) lyase), ...
 11-134 1.34e-28

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: 109.28  E-value: 1.34e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509453   11 LPVMEVNQLWAGLG-YYSRGRRLQEGARKVVEELGGHMPRTAETLQQLlPGVGRYTAGAIASIAFGQATGVVDGNVARVL 89
Cdd:smart00478  30 ADEEELEELIRGLGfYRRKARYLIELARILVEEYGGEVPDDREELLKL-PGVGRKTANAVLSFALGKPFIPVDTHVLRIA 108

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 2462509453   90 CRVRAIGAdpssTLVSQQLWGLAQQLVDPARPGDFNQAAMELGAT 134
Cdd:smart00478 109 KRLGLVDK----KSTPEEVEKLLEKLLPEEDWRELNLLLIDFGRT 149
HhH-GPD pfam00730
HhH-GPD superfamily base excision DNA repair protein; This family contains a diverse range of ...
 15-114 2.20e-25

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: 100.05  E-value: 2.20e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509453  15 EVNQLWAGLGYY-SRGRRLQEGARKVVEELGGHMPRTAETLQQLLPGVGRYTAGAIASIAFG--QATGVVDGNVARVLCR 91
Cdd:pfam00730  39 ELRELIRGLGFYrRKAKYLKELARILVEGYGGEVPLDEEELEALLKGVGRWTAEAVLIFALGrpDPLPVVDTHVRRVLKR 118

                          90       100
                  ....*....|....*....|...
gi 2462509453  92 VRAIGADPSSTLVSQQLWGLAQQ 114
Cdd:pfam00730 119 LGLIKEKPTPKEVERELEELWPP 141
nth TIGR01083
endonuclease III; This equivalog model identifes nth members of the pfam00730 superfamily ...
 9-143 2.88e-16

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: 76.65  E-value: 2.88e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509453   9 SLLPVMEVNQLWAGLGYY-SRGRRLQEGARKVVEELGGHMPRTAETLQQLlPGVGRYTAGAIASIAFGQATGVVDGNVAR 87
Cdd:TIGR01083  63 AQAGLEELEEYIKSIGLYrNKAKNIIELCRKLVERYGGEVPEDREELVKL-PGVGRKTANVVLNVAFGIPAIAVDTHVFR 141

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462509453  88 VLCRVR-AIGADPSST------LVSQQLWglaqqlvdparpGDFNQAAMELGATVCTPQRPLC 143
Cdd:TIGR01083 142 VSNRLGlSKGKDPIKVeedlmkLVPREFW------------VKLHHWLILHGRYTCKARKPLC 192
 
Name Accession Description Interval E-value
MutY COG1194
Adenine-specific DNA glycosylase, acts on AG and A-oxoG pairs [Replication, recombination and ...
 15-345 8.20e-111

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: 328.25  E-value: 8.20e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509453  15 EVNQLWAGLGYYSRGRRLQEGARKVVEELGGHMPRTAETLQQLlPGVGRYTAGAIASIAFGQATGVVDGNVARVLCRVRA 94
Cdd:COG1194    71 EVLKLWEGLGYYSRARNLHKAAQQVVEEHGGVFPDTYEELLAL-PGIGPYTAAAIASIAFGEPAPIVDGNVKRVLSRLFA 149

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509453  95 IGADPSSTLVSQQLWGLAQQLVDPARPGDFNQAAMELGATVCTPQRPLCSQCPVESLCRARQRVEQEQLlasgslsgspd 174
Cdd:COG1194   150 IEGPIGSPAAKKELWALAEELLPPERPGDFNQALMDLGATVCTPKKPKCLLCPLQDDCAAFAEGRQEEL----------- 218

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509453 175 veecapntgqchlclppsepwdqtlgvvnfPRKASRKPPREESSATCVLEQPGalgaQILLVQRPNSGLLAGLWEFPSVT 254
Cdd:COG1194   219 ------------------------------PVKKPKKKKPERYGAALVIRDDG----RVLLEKRPPKGLWGGLWEFPEFE 264

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509453 255 WEPSEQLQrkALLQELQRWAGpLPATHLRHLGEVVHTFSHIKLTYQVYGLALEGQTPVTtvPPGARWLTQEEFHTAAVST 334
Cdd:COG1194   265 WEEAEDPE--ALERWLREELG-LEVEWLEPLGTVRHVFTHFRLHLTVYLARVPAGPPAE--PDGGRWVPLEELAALPLPA 339

                         330
                  ....*....|.
gi 2462509453 335 AMKKVFRVYQG 345
Cdd:COG1194   340 PMRKLLKALLK 350
PRK10880 PRK10880
adenine DNA glycosylase;
12-297 5.31e-44

adenine DNA glycosylase;


Pssm-ID: 182805 [Multi-domain]  Cd Length: 350  Bit Score: 156.02  E-value: 5.31e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509453  12 PVMEVNQLWAGLGYYSRGRRLQEGARKVVEELGGHMPRTAETLQQLlPGVGRYTAGAIASIAFGQATGVVDGNVARVLCR 91
Cdd:PRK10880   69 PLDEVLHLWTGLGYYARARNLHKAAQQVATLHGGEFPETFEEVAAL-PGVGRSTAGAILSLSLGKHFPILDGNVKRVLAR 147

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509453  92 VRAIGADPSSTLVSQQLWGLAQQlVDPARP-GDFNQAAMELGATVCTPQRPLCSQCPVESLCRARqrveqeqllASGSls 170
Cdd:PRK10880  148 CYAVSGWPGKKEVENRLWQLSEQ-VTPAVGvERFNQAMMDLGAMVCTRSKPKCELCPLQNGCIAY---------ANHS-- 215

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509453 171 gspdveecapntgqchlclppsepWDQtlgvvnFPRKASRKPPREESSATCVLEQpgalGAQILLVQRPNSGLLAGLWEF 250
Cdd:PRK10880  216 ------------------------WAL------YPGKKPKQTLPERTGYFLLLQH----GDEVWLEQRPPSGLWGGLFCF 261

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 2462509453 251 PSVTWEpseqlqrkallQELQRW--AGPLPATHLRHLGEVVHTFSHIKL 297
Cdd:PRK10880  262 PQFADE-----------EELRQWlaQRGIAADNLTQLTAFRHTFSHFHL 299
NUDIX_DNA_Glycosylase_C-MutY cd03431
C-terminal domain of DNA glycosylase; DNA glycosylase (MutY in bacteria and hMYH in humans) is ...
 213-340 2.50e-31

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: 115.48  E-value: 2.50e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509453 213 PREESSATCVLEQPGalgaQILLVQRPNSGLLAGLWEFPSVTWEPSEQlqrkaLLQELQRWAGPLPATHLRHLGEVVHTF 292
Cdd:cd03431     1 VPERYFTVLVLRDGG----RVLLEKRPEKGLLAGLWEFPLVETEEEEE-----EAEALLGLLAEELLLILEPLGEVKHVF 71

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 2462509453 293 SHIKLTYQVYGLALEGQTPVTtvPPGARWLTQEEFHTAAVSTAMKKVF 340
Cdd:cd03431    72 SHFRLHITVYLVELPEAPPAA--PDEGRWVDLEELDEYALPAPMRKLL 117
ENDO3c smart00478
endonuclease III; includes endonuclease III (DNA-(apurinic or apyrimidinic site) lyase), ...
 11-134 1.34e-28

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: 109.28  E-value: 1.34e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509453   11 LPVMEVNQLWAGLG-YYSRGRRLQEGARKVVEELGGHMPRTAETLQQLlPGVGRYTAGAIASIAFGQATGVVDGNVARVL 89
Cdd:smart00478  30 ADEEELEELIRGLGfYRRKARYLIELARILVEEYGGEVPDDREELLKL-PGVGRKTANAVLSFALGKPFIPVDTHVLRIA 108

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 2462509453   90 CRVRAIGAdpssTLVSQQLWGLAQQLVDPARPGDFNQAAMELGAT 134
Cdd:smart00478 109 KRLGLVDK----KSTPEEVEKLLEKLLPEEDWRELNLLLIDFGRT 149
ENDO3c cd00056
endonuclease III; includes endonuclease III (DNA-(apurinic or apyrimidinic site) lyase), ...
 15-132 5.12e-28

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: 107.71  E-value: 5.12e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509453  15 EVNQLWAGLGYYSRGRRLQEGARKVVEELGG---HMPRTAETLQQLlPGVGRYTAGAIASIAFGQATGVVDGNVARVLCR 91
Cdd:cd00056    43 ELRELIRSLGYRRKAKYLKELARAIVEGFGGlvlDDPDAREELLAL-PGVGRKTANVVLLFALGPDAFPVDTHVRRVLKR 121

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 2462509453  92 VRAIGADPSstlvSQQLWGLAQQLVDPARPGDFNQAAMELG 132
Cdd:cd00056   122 LGLIPKKKT----PEELEELLEELLPKPYWGEANQALMDLG 158
HhH-GPD pfam00730
HhH-GPD superfamily base excision DNA repair protein; This family contains a diverse range of ...
 15-114 2.20e-25

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: 100.05  E-value: 2.20e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509453  15 EVNQLWAGLGYY-SRGRRLQEGARKVVEELGGHMPRTAETLQQLLPGVGRYTAGAIASIAFG--QATGVVDGNVARVLCR 91
Cdd:pfam00730  39 ELRELIRGLGFYrRKAKYLKELARILVEGYGGEVPLDEEELEALLKGVGRWTAEAVLIFALGrpDPLPVVDTHVRRVLKR 118

                          90       100
                  ....*....|....*....|...
gi 2462509453  92 VRAIGADPSSTLVSQQLWGLAQQ 114
Cdd:pfam00730 119 LGLIKEKPTPKEVERELEELWPP 141
Nth COG0177
Endonuclease III [Replication, recombination and repair];
11-156 1.91e-24

Endonuclease III [Replication, recombination and repair];


Pssm-ID: 439947 [Multi-domain]  Cd Length: 198  Bit Score: 99.40  E-value: 1.91e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509453  11 LPVMEVNQLWAGLGYY-SRGRRLQEGARKVVEELGGHMPRTAETLQQLlPGVGRYTAGAIASIAFGQATGVVDGNVARVL 89
Cdd:COG0177    58 ADLEELEELIRPIGLYrNKAKNIIALARILVEKYGGEVPETREELESL-PGVGRKTANVVLNFAFGKPAIAVDTHVHRVS 136

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462509453  90 CRvraIG-ADPSSTL-VSQQLwglaQQLVDPARPGDFNQAAMELGATVCTPQRPLCSQCPVESLCRARQ 156
Cdd:COG0177   137 NR---LGlVPGKDPEeVEKDL----MKLIPKEYWGDLHHLLILHGRYICKARKPKCEECPLADLCPYYG 198
NUDIX_4 pfam14815
NUDIX domain;
232-341 1.34e-23

NUDIX domain;


Pssm-ID: 464330 [Multi-domain]  Cd Length: 114  Bit Score: 94.30  E-value: 1.34e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509453 232 QILLVQRPNSGLLAGLWEFPSVTWEPSEQLQRKalLQELQRWAgpLPATHLRHlGEVVHTFSHIKLTYQVYGLALEGQTP 311
Cdd:pfam14815  11 RVLLRKRPEKGLLGGLWEFPGGKVEPGETLEEA--LARLEELG--IEVEVLEP-GTVKHVFTHFRLTLHVYLVREVEGEE 85

                          90       100       110
                  ....*....|....*....|....*....|
gi 2462509453 312 vtTVPPGARWLTQEEFHTAAVSTAMKKVFR 341
Cdd:pfam14815  86 --EPQQELRWVTPEELDKYALPAAVRKILE 113
PRK13910 PRK13910
DNA glycosylase MutY; Provisional
 15-163 1.17e-22

DNA glycosylase MutY; Provisional


Pssm-ID: 172427 [Multi-domain]  Cd Length: 289  Bit Score: 96.63  E-value: 1.17e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509453  15 EVNQLWAGLGYYSRGRRLQEGARKVVEELGGHMPRTAETLQQLlPGVGRYTAGAIASIAFGQATGVVDGNVARVLCRVra 94
Cdd:PRK13910   35 EVLLLWRGLGYYSRAKNLKKSAEICVKEHHSQLPNDYQSLLKL-PGIGAYTANAILCFGFREKSACVDANIKRVLLRL-- 111

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462509453  95 IGADPSSTlvSQQLWGLAQQLVDPARPGDFNQAAMELGATVCTPqRPLCSQCPVESLCRARQRVEQEQL 163
Cdd:PRK13910  112 FGLDPNIH--AKDLQIKANDFLNLNESFNHNQALIDLGALICSP-KPKCAICPLNPYCLGKNNPEKHTL 177
nth TIGR01083
endonuclease III; This equivalog model identifes nth members of the pfam00730 superfamily ...
 9-143 2.88e-16

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: 76.65  E-value: 2.88e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509453   9 SLLPVMEVNQLWAGLGYY-SRGRRLQEGARKVVEELGGHMPRTAETLQQLlPGVGRYTAGAIASIAFGQATGVVDGNVAR 87
Cdd:TIGR01083  63 AQAGLEELEEYIKSIGLYrNKAKNIIELCRKLVERYGGEVPEDREELVKL-PGVGRKTANVVLNVAFGIPAIAVDTHVFR 141

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462509453  88 VLCRVR-AIGADPSST------LVSQQLWglaqqlvdparpGDFNQAAMELGATVCTPQRPLC 143
Cdd:TIGR01083 142 VSNRLGlSKGKDPIKVeedlmkLVPREFW------------VKLHHWLILHGRYTCKARKPLC 192
PRK10702 PRK10702
endonuclease III; Provisional
 25-158 1.18e-08

endonuclease III; Provisional


Pssm-ID: 182661 [Multi-domain]  Cd Length: 211  Bit Score: 55.02  E-value: 1.18e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509453  25 YYSRGRRLQEGARKVVEELGGHMPRTAETLQQLlPGVGRYTAGAIASIAFGQATGVVDGNVARVLCRVraiGADPSSTLv 104
Cdd:PRK10702   82 YNSKAENVIKTCRILLEQHNGEVPEDRAALEAL-PGVGRKTANVVLNTAFGWPTIAVDTHIFRVCNRT---QFAPGKNV- 156

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2462509453 105 sQQLWGLAQQLVDPARPGDFNQAAMELGATVCTPQRPLCSQCPVESLCRARQRV 158
Cdd:PRK10702  157 -EQVEEKLLKVVPAEFKVDCHHWLILHGRYTCIARKPRCGSCIIEDLCEYKEKV 209
NUDIX_MutT_NudA_like cd03425
MutT pyrophosphohydrolase; The MutT pyrophosphohydrolase is a prototypical NUDIX hydrolase ...
 222-329 1.55e-05

MutT pyrophosphohydrolase; The MutT pyrophosphohydrolase is a prototypical NUDIX hydrolase that catalyzes the hydrolysis of nucleoside and deoxynucleoside triphosphates (NTPs and dNTPs) by substitution at a beta-phosphorus to yield a nucleotide monophosphate (NMP) and inorganic pyrophosphate (PPi). This enzyme requires two divalent cations for activity; one coordinates the phosphoryl groups of the NTP/dNTP substrate, and the other coordinates to the enzyme. It also contains the NUDIX motif, a highly conserved 23-residue block (GX5EX7REUXEEXGU, where U = I, L or V), that functions as metal binding and catalytic site. MutT pyrophosphohydrolase is important in preventing errors in DNA replication by hydrolyzing mutagenic nucleotides such as 8-oxo-dGTP (a product of oxidative damage), which can mispair with template adenine during DNA replication, to guanine nucleotides.


Pssm-ID: 467531 [Multi-domain]  Cd Length: 123  Bit Score: 43.98  E-value: 1.55e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509453 222 VLEQPGalgaQILLVQRPNSGLLAGLWEFP--SVtwEPSEQLQrKALLQELQ---RWAgplpATHLRHLGEVVHTFSHIK 296
Cdd:cd03425     7 IIVDDG----RVLIAQRPEGKHLAGLWEFPggKV--EPGETPE-QALVRELReelGIE----VEVGEPLGTVEHDYPDFH 75

                          90       100       110
                  ....*....|....*....|....*....|...
gi 2462509453 297 LTYQVYGLALEGQTPVTTVPPGARWLTQEEFHT 329
Cdd:cd03425    76 VRLHVYLCTLWSGEPQLLEHQELRWVTPEELDD 108
PRK10546 PRK10546
pyrimidine (deoxy)nucleoside triphosphate diphosphatase;
222-271 1.79e-05

pyrimidine (deoxy)nucleoside triphosphate diphosphatase;


Pssm-ID: 182536 [Multi-domain]  Cd Length: 135  Bit Score: 43.96  E-value: 1.79e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 2462509453 222 VLEQPGalgaQILLVQRPNSGLLAGLWEFPSVTWEPSEQlQRKALLQELQ 271
Cdd:PRK10546   10 IIERDG----KILLAQRPAHSDQAGLWEFAGGKVEPGES-QPQALIRELR 54
HP0602 COG2231
3-Methyladenine DNA glycosylase, HhH-GPD/Endo3 superfamily [Replication, recombination and ...
 2-158 4.21e-05

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


Pssm-ID: 441832 [Multi-domain]  Cd Length: 220  Bit Score: 44.45  E-value: 4.21e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509453   2 LRTTVRPSllpvmevnqlwaglGYYSR-GRRLQEGARKVVEELGGHMPR-----TAETLQQLL--PGVGRYTAGAIASIA 73
Cdd:COG2231    73 LAELIRPS--------------GFYNQkAKRLKNLARWLVERYGGGLEKlkalpTEELREELLslKGIGPETADSILLYA 138

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509453  74 FGQATGVVDGNVARVLCRVrAIGADPSStlvsqqlWGLAQQLVDPARPGDFNQA----AM--ELGATVCTPqRPLCSQCP 147
Cdd:COG2231   139 FNRPVFVVDAYTRRIFSRL-GLIEEDAS-------YDELQRLFEENLPPDVALYnefhALivEHGKEYCKK-KPKCEECP 209

                         170
                  ....*....|.
gi 2462509453 148 VESLCRARQRV 158
Cdd:COG2231   210 LRDLCPYGGQE 220
FES smart00525
iron-sulpphur binding domain in DNA-(apurinic or apyrimidinic site) lyase (subfamily of ENDO3); ...
 135-155 6.34e-05

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


Pssm-ID: 197771 [Multi-domain]  Cd Length: 21  Bit Score: 39.46  E-value: 6.34e-05
                           10        20
                   ....*....|....*....|.
gi 2462509453  135 VCTPQRPLCSQCPVESLCRAR 155
Cdd:smart00525   1 ICTARKPRCDECPLKDLCPAY 21
HHH pfam00633
Helix-hairpin-helix motif; The helix-hairpin-helix DNA-binding motif is found to be duplicated ...
 42-72 7.57e-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: 39.32  E-value: 7.57e-05
                          10        20        30
                  ....*....|....*....|....*....|.
gi 2462509453  42 ELGGHMPRTAETLQQLlPGVGRYTAGAIASI 72
Cdd:pfam00633   1 SLEGLIPASVEELLAL-PGVGPKTAEAILSY 30
PRK10776 PRK10776
8-oxo-dGTP diphosphatase MutT;
232-326 1.04e-04

8-oxo-dGTP diphosphatase MutT;


Pssm-ID: 182721 [Multi-domain]  Cd Length: 129  Bit Score: 41.89  E-value: 1.04e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509453 232 QILLVQRPNSGLLAGLWEFPSVTWEPSEQLQrKALLQELQRWAGpLPATHLRHLGEVVHTFS--HIKLTY--------QV 301
Cdd:PRK10776   17 EIFITRRAADAHMAGKWEFPGGKIEAGETPE-QALIRELQEEVG-ITVQHATLFEKLEYEFPdrHITLWFwlveswegEP 94

                          90       100
                  ....*....|....*....|....*
gi 2462509453 302 YGlaLEGQtpvttvpPGaRWLTQEE 326
Cdd:PRK10776   95 WG--KEGQ-------PG-RWVSQVA 109
PRK08999 PRK08999
Nudix family hydrolase;
232-327 2.18e-03

Nudix family hydrolase;


Pssm-ID: 236361 [Multi-domain]  Cd Length: 312  Bit Score: 39.86  E-value: 2.18e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509453 232 QILLVQRPNSGLLAGLWEFPSVTWEPSEQLqRKALLQELQRWAGpLPATHLRHLGEVVHTFSHIKLT---YQVYG----- 303
Cdd:PRK08999   18 RILLARRPEGKHQGGLWEFPGGKVEPGETV-EQALARELQEELG-IEVTAARPLITVRHDYPDKRVRldvRRVTAwqgep 95

                          90       100
                  ....*....|....*....|....
gi 2462509453 304 LALEGQtPVTTVPPgaRWLTQEEF 327
Cdd:PRK08999   96 HGREGQ-PLAWVAP--DELAVYPF 116
EndIII_4Fe-2S pfam10576
Iron-sulfur binding domain of endonuclease III; Escherichia coli endonuclease III (EC 4.2.99. ...
 136-152 4.09e-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: 34.28  E-value: 4.09e-03
                          10
                  ....*....|....*..
gi 2462509453 136 CTPQRPLCSQCPVESLC 152
Cdd:pfam10576   1 CTARKPKCEECPLADLC 17
YjhB COG1051
ADP-ribose pyrophosphatase YjhB, NUDIX family [Nucleotide transport and metabolism];
218-341 6.29e-03

ADP-ribose pyrophosphatase YjhB, NUDIX family [Nucleotide transport and metabolism];


Pssm-ID: 440671 [Multi-domain]  Cd Length: 125  Bit Score: 36.49  E-value: 6.29e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509453 218 SATCVLEQPGAlgaQILLVQRPNsGLLAGLWEFPSVTWEPSEQLqRKALLQELqrW--AGpLPATHLRHLGEVVHTFSHI 295
Cdd:COG1051     8 AVDAVIFRKDG---RVLLVRRAD-EPGKGLWALPGGKVEPGETP-EEAALREL--ReeTG-LEVEVLELLGVFDHPDRGH 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2462509453 296 KLTYQVYGLALEGQTPVTTVPPGARWLTQEEFHTAAVSTAMKKVFR 341
Cdd:COG1051    80 VVSVAFLAEVLSGEPRADDEIDEARWFPLDELPELAFTPADHEILE 125
 
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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