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Conserved domains on  [gi|1894885767|ref|WP_185985547|]
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A/G-specific adenine glycosylase [Aureimonas mangrovi]

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 ...
 8-358 9.80e-177

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: 494.27  E-value: 9.80e-177
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894885767   8 APDARIAGLLLPWYDRHARELPWRlgperavegERADPYRVWLSEIMLQQTTVAAVKSYFARFTERWPSVEALAAAQDGE 87
Cdd:COG1194     1 MDMASFAKRLLAWYDRHGRDLPWR---------QTRDPYRVWLSEIMLQQTQVATVIPYYERFLERFPTVEALAAAPEDE 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894885767  88 VMSAWAGLGYYARARNLLACARVVAGERGGLFPTSAEGLRALPGIGDYTSAAIAAIAFGERVAVVDGNVERVTTRLHAIE 167
Cdd:COG1194    72 VLKLWEGLGYYSRARNLHKAAQQVVEEHGGVFPDTYEELLALPGIGPYTAAAIASIAFGEPAPIVDGNVKRVLSRLFAIE 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894885767 168 TPL--PAGRPFVRHHVDAMTPADRPGDFAQAMMDLGATICTPRKPACVICPIAEPCRARAEGRQETFPVKVKKAAKPSRI 245
Cdd:COG1194   152 GPIgsPAAKKELWALAEELLPPERPGDFNQALMDLGATVCTPKKPKCLLCPLQDDCAAFAEGRQEELPVKKPKKKKPERY 231

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894885767 246 GAAFVAlrRGDGAVLLRKRPSTGMLGGMSEPPTTAWSARADGAT----GEDAAPFPADW-RLVGEVRHGFTHFDLTLEVW 320
Cdd:COG1194   232 GAALVI--RDDGRVLLEKRPPKGLWGGLWEFPEFEWEEAEDPEAlerwLREELGLEVEWlEPLGTVRHVFTHFRLHLTVY 309

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|.
gi 1894885767 321 RAVV---MEVPDTSGWWAPADALDAEALPTLMRKAIETALA 358
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 ...
 8-358 9.80e-177

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: 494.27  E-value: 9.80e-177
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894885767   8 APDARIAGLLLPWYDRHARELPWRlgperavegERADPYRVWLSEIMLQQTTVAAVKSYFARFTERWPSVEALAAAQDGE 87
Cdd:COG1194     1 MDMASFAKRLLAWYDRHGRDLPWR---------QTRDPYRVWLSEIMLQQTQVATVIPYYERFLERFPTVEALAAAPEDE 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894885767  88 VMSAWAGLGYYARARNLLACARVVAGERGGLFPTSAEGLRALPGIGDYTSAAIAAIAFGERVAVVDGNVERVTTRLHAIE 167
Cdd:COG1194    72 VLKLWEGLGYYSRARNLHKAAQQVVEEHGGVFPDTYEELLALPGIGPYTAAAIASIAFGEPAPIVDGNVKRVLSRLFAIE 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894885767 168 TPL--PAGRPFVRHHVDAMTPADRPGDFAQAMMDLGATICTPRKPACVICPIAEPCRARAEGRQETFPVKVKKAAKPSRI 245
Cdd:COG1194   152 GPIgsPAAKKELWALAEELLPPERPGDFNQALMDLGATVCTPKKPKCLLCPLQDDCAAFAEGRQEELPVKKPKKKKPERY 231

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894885767 246 GAAFVAlrRGDGAVLLRKRPSTGMLGGMSEPPTTAWSARADGAT----GEDAAPFPADW-RLVGEVRHGFTHFDLTLEVW 320
Cdd:COG1194   232 GAALVI--RDDGRVLLEKRPPKGLWGGLWEFPEFEWEEAEDPEAlerwLREELGLEVEWlEPLGTVRHVFTHFRLHLTVY 309

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|.
gi 1894885767 321 RAVV---MEVPDTSGWWAPADALDAEALPTLMRKAIETALA 358
Cdd:COG1194   310 LARVpagPPAEPDGGRWVPLEELAALPLPAPMRKLLKALLK 350
mutY TIGR01084
A/G-specific adenine glycosylase; This equivalog model identifies mutY members of the ...
 17-277 1.00e-104

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: 308.96  E-value: 1.00e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894885767  17 LLPWYDRHARE-LPWRLGPeravegeraDPYRVWLSEIMLQQTTVAAVKSYFARFTERWPSVEALAAAQDGEVMSAWAGL 95
Cdd:TIGR01084   6 LLSWYDKYGRKtLPWRQNK---------TPYRVWLSEVMLQQTQVATVIPYFERFLERFPTVQALANAPQDEVLKLWEGL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894885767  96 GYYARARNLLACARVVAGERGGLFPTSAEGLRALPGIGDYTSAAIAAIAFGERVAVVDGNVERVTTRLHAIETplPAGRP 175
Cdd:TIGR01084  77 GYYARARNLHKAAQEVVEEFGGEFPQDFEDLAALPGVGRYTAGAILSFALNKPYPILDGNVKRVLSRLFAVEG--WPGKK 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894885767 176 FVR----HHVDAMTPADRPGDFAQAMMDLGATICTPRKPACVICPIAEPCRARAEGRQETFPVKVKKAAKPSRIGaAFVA 251
Cdd:TIGR01084 155 KVEnrlwTLAESLLPKADPEAFNQALMDLGAMICTRKKPKCDLCPLQDFCLAYQQGTWEEYPVKKPKAAPPERTT-YFLV 233

                         250       260
                  ....*....|....*....|....*.
gi 1894885767 252 LRRGDGAVLLRKRPSTGMLGGMSEPP 277
Cdd:TIGR01084 234 LQNYDGEVLLEQRPEKGLWGGLYCFP 259
PRK10880 PRK10880
adenine DNA glycosylase;
14-315 5.38e-74

adenine DNA glycosylase;


Pssm-ID: 182805 [Multi-domain]  Cd Length: 350  Bit Score: 233.06  E-value: 5.38e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894885767  14 AGLLLPWYDRHARE-LPWRLgperavegeRADPYRVWLSEIMLQQTTVAAVKSYFARFTERWPSVEALAAAQDGEVMSAW 92
Cdd:PRK10880    7 SAQVLDWYDKYGRKtLPWQI---------DKTPYKVWLSEVMLQQTQVATVIPYFERFMARFPTVTDLANAPLDEVLHLW 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894885767  93 AGLGYYARARNLLACARVVAGERGGLFPTSAEGLRALPGIGDYTSAAIAAIAFGERVAVVDGNVERVTTRLHAIET-Plp 171
Cdd:PRK10880   78 TGLGYYARARNLHKAAQQVATLHGGEFPETFEEVAALPGVGRSTAGAILSLSLGKHFPILDGNVKRVLARCYAVSGwP-- 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894885767 172 aGRPFVR----HHVDAMTPADRPGDFAQAMMDLGATICTPRKPACVICPIAEPCRARAEGRQETFPVKVKKAAKPSRIGa 247
Cdd:PRK10880  156 -GKKEVEnrlwQLSEQVTPAVGVERFNQAMMDLGAMVCTRSKPKCELCPLQNGCIAYANHSWALYPGKKPKQTLPERTG- 233

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1894885767 248 AFVALRRGDgAVLLRKRPSTGMLGGM-------SEPPTTAWSARAdGATGEDAAPFPAdwrlvgeVRHGFTHFDL 315
Cdd:PRK10880  234 YFLLLQHGD-EVWLEQRPPSGLWGGLfcfpqfaDEEELRQWLAQR-GIAADNLTQLTA-------FRHTFSHFHL 299
ENDO3c cd00056
endonuclease III; includes endonuclease III (DNA-(apurinic or apyrimidinic site) lyase), ...
 46-201 7.42e-45

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: 151.24  E-value: 7.42e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894885767  46 YRVWLSEIMLQQTTVAAVKSYFARFTERW-PSVEALAAAQDGEVMSAWAGLGYYARARNLLACARVVAGERGGLF---PT 121
Cdd:cd00056     1 FEVLVSEILSQQTTDKAVNKAYERLFERYgPTPEALAAADEEELRELIRSLGYRRKAKYLKELARAIVEGFGGLVlddPD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894885767 122 SAEGLRALPGIGDYTSAAIAAIAFGERVAVVDGNVERVTTRLHAIETPLPAGRpfVRHHVDAMTPADRPGDFAQAMMDLG 201
Cdd:cd00056    81 AREELLALPGVGRKTANVVLLFALGPDAFPVDTHVRRVLKRLGLIPKKKTPEE--LEELLEELLPKPYWGEANQALMDLG 158
ENDO3c smart00478
endonuclease III; includes endonuclease III (DNA-(apurinic or apyrimidinic site) lyase), ...
 54-203 4.76e-34

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: 122.76  E-value: 4.76e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894885767   54 MLQQTTVAAVKSYFARFTERWPSVEALAAAQDGEVMSAWAGLG-YYARARNLLACARVVAGERGGLFPTSAEGLRALPGI 132
Cdd:smart00478   1 LSQQTTDERVNKATERLFEKFPTPEDLAAADEEELEELIRGLGfYRRKARYLIELARILVEEYGGEVPDDREELLKLPGV 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1894885767  133 GDYTSAAIAAIAFGERVAVVDGNVERVTTRLHAIETPLPAGRpfVRHHVDAMTPADRPGDFAQAMMDLGAT 203
Cdd:smart00478  81 GRKTANAVLSFALGKPFIPVDTHVLRIAKRLGLVDKKSTPEE--VEKLLEKLLPEEDWRELNLLLIDFGRT 149
HhH-GPD pfam00730
HhH-GPD superfamily base excision DNA repair protein; This family contains a diverse range of ...
 50-168 1.61e-27

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: 105.44  E-value: 1.61e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894885767  50 LSEIMLQQTTVAAVKSYFARFTERW-PSVEALAAAQDGEVMSAWAGLGYYAR-ARNLLACARVVAGERGGLFPTSAEGLR 127
Cdd:pfam00730   1 VSAILSQQTSDKAVNKITERLFEKFfPTPEDLADADEEELRELIRGLGFYRRkAKYLKELARILVEGYGGEVPLDEEELE 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1894885767 128 A-LPGIGDYTSAAIAAIAFG--ERVAVVDGNVERVTTRLHAIET 168
Cdd:pfam00730  81 AlLKGVGRWTAEAVLIFALGrpDPLPVVDTHVRRVLKRLGLIKE 124
 
Name Accession Description Interval E-value
MutY COG1194
Adenine-specific DNA glycosylase, acts on AG and A-oxoG pairs [Replication, recombination and ...
 8-358 9.80e-177

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: 494.27  E-value: 9.80e-177
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894885767   8 APDARIAGLLLPWYDRHARELPWRlgperavegERADPYRVWLSEIMLQQTTVAAVKSYFARFTERWPSVEALAAAQDGE 87
Cdd:COG1194     1 MDMASFAKRLLAWYDRHGRDLPWR---------QTRDPYRVWLSEIMLQQTQVATVIPYYERFLERFPTVEALAAAPEDE 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894885767  88 VMSAWAGLGYYARARNLLACARVVAGERGGLFPTSAEGLRALPGIGDYTSAAIAAIAFGERVAVVDGNVERVTTRLHAIE 167
Cdd:COG1194    72 VLKLWEGLGYYSRARNLHKAAQQVVEEHGGVFPDTYEELLALPGIGPYTAAAIASIAFGEPAPIVDGNVKRVLSRLFAIE 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894885767 168 TPL--PAGRPFVRHHVDAMTPADRPGDFAQAMMDLGATICTPRKPACVICPIAEPCRARAEGRQETFPVKVKKAAKPSRI 245
Cdd:COG1194   152 GPIgsPAAKKELWALAEELLPPERPGDFNQALMDLGATVCTPKKPKCLLCPLQDDCAAFAEGRQEELPVKKPKKKKPERY 231

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894885767 246 GAAFVAlrRGDGAVLLRKRPSTGMLGGMSEPPTTAWSARADGAT----GEDAAPFPADW-RLVGEVRHGFTHFDLTLEVW 320
Cdd:COG1194   232 GAALVI--RDDGRVLLEKRPPKGLWGGLWEFPEFEWEEAEDPEAlerwLREELGLEVEWlEPLGTVRHVFTHFRLHLTVY 309

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|.
gi 1894885767 321 RAVV---MEVPDTSGWWAPADALDAEALPTLMRKAIETALA 358
Cdd:COG1194   310 LARVpagPPAEPDGGRWVPLEELAALPLPAPMRKLLKALLK 350
mutY TIGR01084
A/G-specific adenine glycosylase; This equivalog model identifies mutY members of the ...
 17-277 1.00e-104

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: 308.96  E-value: 1.00e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894885767  17 LLPWYDRHARE-LPWRLGPeravegeraDPYRVWLSEIMLQQTTVAAVKSYFARFTERWPSVEALAAAQDGEVMSAWAGL 95
Cdd:TIGR01084   6 LLSWYDKYGRKtLPWRQNK---------TPYRVWLSEVMLQQTQVATVIPYFERFLERFPTVQALANAPQDEVLKLWEGL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894885767  96 GYYARARNLLACARVVAGERGGLFPTSAEGLRALPGIGDYTSAAIAAIAFGERVAVVDGNVERVTTRLHAIETplPAGRP 175
Cdd:TIGR01084  77 GYYARARNLHKAAQEVVEEFGGEFPQDFEDLAALPGVGRYTAGAILSFALNKPYPILDGNVKRVLSRLFAVEG--WPGKK 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894885767 176 FVR----HHVDAMTPADRPGDFAQAMMDLGATICTPRKPACVICPIAEPCRARAEGRQETFPVKVKKAAKPSRIGaAFVA 251
Cdd:TIGR01084 155 KVEnrlwTLAESLLPKADPEAFNQALMDLGAMICTRKKPKCDLCPLQDFCLAYQQGTWEEYPVKKPKAAPPERTT-YFLV 233

                         250       260
                  ....*....|....*....|....*.
gi 1894885767 252 LRRGDGAVLLRKRPSTGMLGGMSEPP 277
Cdd:TIGR01084 234 LQNYDGEVLLEQRPEKGLWGGLYCFP 259
PRK10880 PRK10880
adenine DNA glycosylase;
14-315 5.38e-74

adenine DNA glycosylase;


Pssm-ID: 182805 [Multi-domain]  Cd Length: 350  Bit Score: 233.06  E-value: 5.38e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894885767  14 AGLLLPWYDRHARE-LPWRLgperavegeRADPYRVWLSEIMLQQTTVAAVKSYFARFTERWPSVEALAAAQDGEVMSAW 92
Cdd:PRK10880    7 SAQVLDWYDKYGRKtLPWQI---------DKTPYKVWLSEVMLQQTQVATVIPYFERFMARFPTVTDLANAPLDEVLHLW 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894885767  93 AGLGYYARARNLLACARVVAGERGGLFPTSAEGLRALPGIGDYTSAAIAAIAFGERVAVVDGNVERVTTRLHAIET-Plp 171
Cdd:PRK10880   78 TGLGYYARARNLHKAAQQVATLHGGEFPETFEEVAALPGVGRSTAGAILSLSLGKHFPILDGNVKRVLARCYAVSGwP-- 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894885767 172 aGRPFVR----HHVDAMTPADRPGDFAQAMMDLGATICTPRKPACVICPIAEPCRARAEGRQETFPVKVKKAAKPSRIGa 247
Cdd:PRK10880  156 -GKKEVEnrlwQLSEQVTPAVGVERFNQAMMDLGAMVCTRSKPKCELCPLQNGCIAYANHSWALYPGKKPKQTLPERTG- 233

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1894885767 248 AFVALRRGDgAVLLRKRPSTGMLGGM-------SEPPTTAWSARAdGATGEDAAPFPAdwrlvgeVRHGFTHFDL 315
Cdd:PRK10880  234 YFLLLQHGD-EVWLEQRPPSGLWGGLfcfpqfaDEEELRQWLAQR-GIAADNLTQLTA-------FRHTFSHFHL 299
ENDO3c cd00056
endonuclease III; includes endonuclease III (DNA-(apurinic or apyrimidinic site) lyase), ...
 46-201 7.42e-45

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: 151.24  E-value: 7.42e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894885767  46 YRVWLSEIMLQQTTVAAVKSYFARFTERW-PSVEALAAAQDGEVMSAWAGLGYYARARNLLACARVVAGERGGLF---PT 121
Cdd:cd00056     1 FEVLVSEILSQQTTDKAVNKAYERLFERYgPTPEALAAADEEELRELIRSLGYRRKAKYLKELARAIVEGFGGLVlddPD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894885767 122 SAEGLRALPGIGDYTSAAIAAIAFGERVAVVDGNVERVTTRLHAIETPLPAGRpfVRHHVDAMTPADRPGDFAQAMMDLG 201
Cdd:cd00056    81 AREELLALPGVGRKTANVVLLFALGPDAFPVDTHVRRVLKRLGLIPKKKTPEE--LEELLEELLPKPYWGEANQALMDLG 158
ENDO3c smart00478
endonuclease III; includes endonuclease III (DNA-(apurinic or apyrimidinic site) lyase), ...
 54-203 4.76e-34

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: 122.76  E-value: 4.76e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894885767   54 MLQQTTVAAVKSYFARFTERWPSVEALAAAQDGEVMSAWAGLG-YYARARNLLACARVVAGERGGLFPTSAEGLRALPGI 132
Cdd:smart00478   1 LSQQTTDERVNKATERLFEKFPTPEDLAAADEEELEELIRGLGfYRRKARYLIELARILVEEYGGEVPDDREELLKLPGV 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1894885767  133 GDYTSAAIAAIAFGERVAVVDGNVERVTTRLHAIETPLPAGRpfVRHHVDAMTPADRPGDFAQAMMDLGAT 203
Cdd:smart00478  81 GRKTANAVLSFALGKPFIPVDTHVLRIAKRLGLVDKKSTPEE--VEKLLEKLLPEEDWRELNLLLIDFGRT 149
PRK13910 PRK13910
DNA glycosylase MutY; Provisional
 54-346 5.60e-31

DNA glycosylase MutY; Provisional


Pssm-ID: 172427 [Multi-domain]  Cd Length: 289  Bit Score: 118.97  E-value: 5.60e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894885767  54 MLQQTTVAAV-KSYFARFTERWPSVEALAAAQDGEVMSAWAGLGYYARARNLLACARVVAGERGGLFPTSAEGLRALPGI 132
Cdd:PRK13910    1 MSQQTQINTVvERFYSPFLEAFPTLKDLANAPLEEVLLLWRGLGYYSRAKNLKKSAEICVKEHHSQLPNDYQSLLKLPGI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894885767 133 GDYTSAAIAAIAFGERVAVVDGNVERVTTRLHAIETPLPAGRpfVRHHVDAMTPADRPGDFAQAMMDLGATICTPrKPAC 212
Cdd:PRK13910   81 GAYTANAILCFGFREKSACVDANIKRVLLRLFGLDPNIHAKD--LQIKANDFLNLNESFNHNQALIDLGALICSP-KPKC 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894885767 213 VICPIAEPCRARAEGRQETFPVKVKKAAKPSRIGaafVALRRGDGAVllrKRPSTGMLGGMSEPPTTAWSAradgatgED 292
Cdd:PRK13910  158 AICPLNPYCLGKNNPEKHTLKKKQEIVQEERYLG---VVIQNNQIAL---EKIEQKLYLGMHHFPNLKENL-------EY 224

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1894885767 293 AAPFpadwrlVGEVRHGFTHFDLTLEVWRAVVMEVPDTSGWWAPAdalDAEALP 346
Cdd:PRK13910  225 KLPF------LGAIKHSHTKFKLNLNLYLAAIKDLKNPIRFYSLK---DLETLP 269
Nth COG0177
Endonuclease III [Replication, recombination and repair];
34-222 6.48e-31

Endonuclease III [Replication, recombination and repair];


Pssm-ID: 439947 [Multi-domain]  Cd Length: 198  Bit Score: 115.96  E-value: 6.48e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894885767  34 PERAVEGERADPYRVWLSEIMLQQTTVAAVKSYFARFTERWPSVEALAAAQDGEVMSAWAGLGYY-ARARNLLACARVVA 112
Cdd:COG0177     9 PDAKTELDYRDPFELLVATILSAQTTDERVNKATPRLFARYPTPEALAAADLEELEELIRPIGLYrNKAKNIIALARILV 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894885767 113 GERGGLFPTSAEGLRALPGIGDYTSAAIAAIAFGERVAVVDGNVERVTTRLHAIE--TPLPagrpfVRHHVDAMTPADRP 190
Cdd:COG0177    89 EKYGGEVPETREELESLPGVGRKTANVVLNFAFGKPAIAVDTHVHRVSNRLGLVPgkDPEE-----VEKDLMKLIPKEYW 163

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1894885767 191 GDFAQAMMDLGATICTPRKPACVICPIAEPCR 222
Cdd:COG0177   164 GDLHHLLILHGRYICKARKPKCEECPLADLCP 195
HhH-GPD pfam00730
HhH-GPD superfamily base excision DNA repair protein; This family contains a diverse range of ...
 50-168 1.61e-27

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: 105.44  E-value: 1.61e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894885767  50 LSEIMLQQTTVAAVKSYFARFTERW-PSVEALAAAQDGEVMSAWAGLGYYAR-ARNLLACARVVAGERGGLFPTSAEGLR 127
Cdd:pfam00730   1 VSAILSQQTSDKAVNKITERLFEKFfPTPEDLADADEEELRELIRGLGFYRRkAKYLKELARILVEGYGGEVPLDEEELE 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1894885767 128 A-LPGIGDYTSAAIAAIAFG--ERVAVVDGNVERVTTRLHAIET 168
Cdd:pfam00730  81 AlLKGVGRWTAEAVLIFALGrpDPLPVVDTHVRRVLKRLGLIKE 124
NUDIX_DNA_Glycosylase_C-MutY cd03431
C-terminal domain of DNA glycosylase; DNA glycosylase (MutY in bacteria and hMYH in humans) is ...
 241-354 3.87e-27

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: 103.54  E-value: 3.87e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894885767 241 KPSRIGAAFVALRrgDGAVLLRKRPSTGMLGGMSEPPTTAWSARADGAT---GEDAAPFPADWRLVGEVRHGFTHFDLTL 317
Cdd:cd03431     1 VPERYFTVLVLRD--GGRVLLEKRPEKGLLAGLWEFPLVETEEEEEEAEallGLLAEELLLILEPLGEVKHVFSHFRLHI 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1894885767 318 EVWRAVVMEVPDT---SGWWAPADALDAEALPTLMRKAIE 354
Cdd:cd03431    79 TVYLVELPEAPPAapdEGRWVDLEELDEYALPAPMRKLLE 118
NUDIX_4 pfam14815
NUDIX domain;
248-354 2.94e-21

NUDIX domain;


Pssm-ID: 464330 [Multi-domain]  Cd Length: 114  Bit Score: 87.75  E-value: 2.94e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894885767 248 AFVALRRGDGAVLLRKRPSTGMLGGMSEPPTTAWsarADGATGEDAAPFPADWRLV------GEVRHGFTHFDLTLEVWR 321
Cdd:pfam14815   1 AVLVIRNGDGRVLLRKRPEKGLLGGLWEFPGGKV---EPGETLEEALARLEELGIEvevlepGTVKHVFTHFRLTLHVYL 77

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1894885767 322 AVVME---VPDTSGWWAPADALDAEALPTLMRKAIE 354
Cdd:pfam14815  78 VREVEgeeEPQQELRWVTPEELDKYALPAAVRKILE 113
PRK10702 PRK10702
endonuclease III; Provisional
 34-221 8.92e-09

endonuclease III; Provisional


Pssm-ID: 182661 [Multi-domain]  Cd Length: 211  Bit Score: 55.02  E-value: 8.92e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894885767  34 PERAVEGERADPYRVWLSEIMLQQTTVAAVKSYFARFTERWPSVEALAAAQDGEVMSAWAGLGYY-ARARNLLACARVVA 112
Cdd:PRK10702   18 PHPTTELNFSSPFELLIAVLLSAQATDVSVNKATAKLYPVANTPAAMLELGVEGVKTYIKTIGLYnSKAENVIKTCRILL 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894885767 113 GERGGLFPTSAEGLRALPGIGDYTSAAIAAIAFGERVAVVDGNVERVTTRlhaieTPLPAGRPF--VRHHVDAMTPADRP 190
Cdd:PRK10702   98 EQHNGEVPEDRAALEALPGVGRKTANVVLNTAFGWPTIAVDTHIFRVCNR-----TQFAPGKNVeqVEEKLLKVVPAEFK 172

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1894885767 191 GDFAQAMMDLGATICTPRKPACVICPIAEPC 221
Cdd:PRK10702  173 VDCHHWLILHGRYTCIARKPRCGSCIIEDLC 203
FES smart00525
iron-sulpphur binding domain in DNA-(apurinic or apyrimidinic site) lyase (subfamily of ENDO3); ...
 204-224 7.03e-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: 7.03e-05
                           10        20
                   ....*....|....*....|.
gi 1894885767  204 ICTPRKPACVICPIAEPCRAR 224
Cdd:smart00525   1 ICTARKPRCDECPLKDLCPAY 21
EndIII_4Fe-2S pfam10576
Iron-sulfur binding domain of endonuclease III; Escherichia coli endonuclease III (EC 4.2.99. ...
 205-221 1.07e-04

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: 38.91  E-value: 1.07e-04
                          10
                  ....*....|....*..
gi 1894885767 205 CTPRKPACVICPIAEPC 221
Cdd:pfam10576   1 CTARKPKCEECPLADLC 17
HP0602 COG2231
3-Methyladenine DNA glycosylase, HhH-GPD/Endo3 superfamily [Replication, recombination and ...
 76-226 9.58e-04

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


Pssm-ID: 441832 [Multi-domain]  Cd Length: 220  Bit Score: 40.21  E-value: 9.58e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894885767  76 SVEALAAAQDGEVMSAWAGLGYYAR-ARNLLACARVVAGERGG----LFPTSAEGLR----ALPGIGDYTSAAIAAIAFG 146
Cdd:COG2231    61 DPEALAALDPEELAELIRPSGFYNQkAKRLKNLARWLVERYGGglekLKALPTEELReellSLKGIGPETADSILLYAFN 140

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894885767 147 ERVAVVDGNVERVTTRLHAIetPLPAGRPFVRHHVDAMTPADrPGDFAQ--AMMD-LGATICTPrKPACVICPIAEPCRA 223
Cdd:COG2231   141 RPVFVVDAYTRRIFSRLGLI--EEDASYDELQRLFEENLPPD-VALYNEfhALIVeHGKEYCKK-KPKCEECPLRDLCPY 216


                  ...
gi 1894885767 224 RAE 226
Cdd:COG2231   217 GGQ 219
 
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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