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Conserved domains on  [gi|556289785|ref|WP_023291004|]
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MULTISPECIES: A/G-specific adenine glycosylase [Klebsiella]

Protein Classification

A/G-specific adenine glycosylase( domain architecture ID 11485057)

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK10880 PRK10880
adenine DNA glycosylase;
5-352 0e+00

adenine DNA glycosylase;


:

Pssm-ID: 182805 [Multi-domain]  Cd Length: 350  Bit Score: 809.32  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556289785   5 ATQFSAQVLDWYDKYGRKTLPWQIAKTPYKVWLSEVMLQQTQVTTVIPYFERFMARFPTVVDLANAPLDEVLHLWTGLGY 84
Cdd:PRK10880   3 ASQFSAQVLDWYDKYGRKTLPWQIDKTPYKVWLSEVMLQQTQVATVIPYFERFMARFPTVTDLANAPLDEVLHLWTGLGY 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556289785  85 YARARNLHKAAQQVAAQHGGEFPQTFDEVAALPGVGRSTAGAILSLSLGQHYPILDGNVKRVLARCYAVSGWPGKKEVEK 164
Cdd:PRK10880  83 YARARNLHKAAQQVATLHGGEFPETFEEVAALPGVGRSTAGAILSLSLGKHFPILDGNVKRVLARCYAVSGWPGKKEVEN 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556289785 165 RLWEISEAVTPAKGVERFNQAMMDLGAMVCTRSKPKCELCPLSNGCVAYANHSWAEYPGKKPKQTIPERTGYFLLMQHGD 244
Cdd:PRK10880 163 RLWQLSEQVTPAVGVERFNQAMMDLGAMVCTRSKPKCELCPLQNGCIAYANHSWALYPGKKPKQTLPERTGYFLLLQHGD 242

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556289785 245 EVFLAQRPPVGLWGGLFCFPQFADEAGLREWLAQRQIKADNLTQLTAFRHTFSHFHLDIVPMWLTVHSSGACMDEGNALW 324
Cdd:PRK10880 243 EVWLEQRPPSGLWGGLFCFPQFADEEELRQWLAQRGIAADNLTQLTAFRHTFSHFHLDIVPMWLPVSSFTGCMDEGNGLW 322

                        330       340
                 ....*....|....*....|....*...
gi 556289785 325 YNLAQPPSVGLAAPVERLLQQLKAGTPV 352
Cdd:PRK10880 323 YNLAQPPSVGLAAPVERLLQQLRTGAPV 350
 
Name Accession Description Interval E-value
PRK10880 PRK10880
adenine DNA glycosylase;
5-352 0e+00

adenine DNA glycosylase;


Pssm-ID: 182805 [Multi-domain]  Cd Length: 350  Bit Score: 809.32  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556289785   5 ATQFSAQVLDWYDKYGRKTLPWQIAKTPYKVWLSEVMLQQTQVTTVIPYFERFMARFPTVVDLANAPLDEVLHLWTGLGY 84
Cdd:PRK10880   3 ASQFSAQVLDWYDKYGRKTLPWQIDKTPYKVWLSEVMLQQTQVATVIPYFERFMARFPTVTDLANAPLDEVLHLWTGLGY 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556289785  85 YARARNLHKAAQQVAAQHGGEFPQTFDEVAALPGVGRSTAGAILSLSLGQHYPILDGNVKRVLARCYAVSGWPGKKEVEK 164
Cdd:PRK10880  83 YARARNLHKAAQQVATLHGGEFPETFEEVAALPGVGRSTAGAILSLSLGKHFPILDGNVKRVLARCYAVSGWPGKKEVEN 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556289785 165 RLWEISEAVTPAKGVERFNQAMMDLGAMVCTRSKPKCELCPLSNGCVAYANHSWAEYPGKKPKQTIPERTGYFLLMQHGD 244
Cdd:PRK10880 163 RLWQLSEQVTPAVGVERFNQAMMDLGAMVCTRSKPKCELCPLQNGCIAYANHSWALYPGKKPKQTLPERTGYFLLLQHGD 242

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556289785 245 EVFLAQRPPVGLWGGLFCFPQFADEAGLREWLAQRQIKADNLTQLTAFRHTFSHFHLDIVPMWLTVHSSGACMDEGNALW 324
Cdd:PRK10880 243 EVWLEQRPPSGLWGGLFCFPQFADEEELRQWLAQRGIAADNLTQLTAFRHTFSHFHLDIVPMWLPVSSFTGCMDEGNGLW 322

                        330       340
                 ....*....|....*....|....*...
gi 556289785 325 YNLAQPPSVGLAAPVERLLQQLKAGTPV 352
Cdd:PRK10880 323 YNLAQPPSVGLAAPVERLLQQLRTGAPV 350
MutY COG1194
Adenine-specific DNA glycosylase, acts on AG and A-oxoG pairs [Replication, recombination and ...
 5-348 0e+00

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: 566.30  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556289785   5 ATQFSAQVLDWYDKYGRkTLPWQIAKTPYKVWLSEVMLQQTQVTTVIPYFERFMARFPTVVDLANAPLDEVLHLWTGLGY 84
Cdd:COG1194    3 MASFAKRLLAWYDRHGR-DLPWRQTRDPYRVWLSEIMLQQTQVATVIPYYERFLERFPTVEALAAAPEDEVLKLWEGLGY 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556289785  85 YARARNLHKAAQQVAAQHGGEFPQTFDEVAALPGVGRSTAGAILSLSLGQHYPILDGNVKRVLARCYAVSGWPGKKEVEK 164
Cdd:COG1194   82 YSRARNLHKAAQQVVEEHGGVFPDTYEELLALPGIGPYTAAAIASIAFGEPAPIVDGNVKRVLSRLFAIEGPIGSPAAKK 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556289785 165 RLWEISEAVTPAKGVERFNQAMMDLGAMVCTRSKPKCELCPLSNGCVAYANHSWAEYPGKKPKQTIPERTGYFLLMQHGD 244
Cdd:COG1194  162 ELWALAEELLPPERPGDFNQALMDLGATVCTPKKPKCLLCPLQDDCAAFAEGRQEELPVKKPKKKKPERYGAALVIRDDG 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556289785 245 EVFLAQRPPVGLWGGLFCFPQFADEAG-----LREWLAQR-QIKADNLTQLTAFRHTFSHFHLDIVPMWLTVhSSGACMD 318
Cdd:COG1194  242 RVLLEKRPPKGLWGGLWEFPEFEWEEAedpeaLERWLREElGLEVEWLEPLGTVRHVFTHFRLHLTVYLARV-PAGPPAE 320

                        330       340       350
                 ....*....|....*....|....*....|
gi 556289785 319 EGNALWYNLAQPPSVGLAAPVERLLQQLKA 348
Cdd:COG1194  321 PDGGRWVPLEELAALPLPAPMRKLLKALLK 350
mutY TIGR01084
A/G-specific adenine glycosylase; This equivalog model identifies mutY members of the ...
 7-280 0e+00

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: 505.02  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556289785    7 QFSAQVLDWYDKYGRKTLPWQIAKTPYKVWLSEVMLQQTQVTTVIPYFERFMARFPTVVDLANAPLDEVLHLWTGLGYYA 86
Cdd:TIGR01084   1 QFSEDLLSWYDKYGRKTLPWRQNKTPYRVWLSEVMLQQTQVATVIPYFERFLERFPTVQALANAPQDEVLKLWEGLGYYA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556289785   87 RARNLHKAAQQVAAQHGGEFPQTFDEVAALPGVGRSTAGAILSLSLGQHYPILDGNVKRVLARCYAVSGWPGKKEVEKRL 166
Cdd:TIGR01084  81 RARNLHKAAQEVVEEFGGEFPQDFEDLAALPGVGRYTAGAILSFALNKPYPILDGNVKRVLSRLFAVEGWPGKKKVENRL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556289785  167 WEISEAVTPAKGVERFNQAMMDLGAMVCTRSKPKCELCPLSNGCVAYANHSWAEYPGKKPKQTIPERTGYFLLMQHGD-E 245
Cdd:TIGR01084 161 WTLAESLLPKADPEAFNQALMDLGAMICTRKKPKCDLCPLQDFCLAYQQGTWEEYPVKKPKAAPPERTTYFLVLQNYDgE 240

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 556289785  246 VFLAQRPPVGLWGGLFCFPQFADEAGLREWLAQRQ 280
Cdd:TIGR01084 241 VLLEQRPEKGLWGGLYCFPQFEDEDSLAFLLAQRG 275
ENDO3c cd00056
endonuclease III; includes endonuclease III (DNA-(apurinic or apyrimidinic site) lyase), ...
 33-190 8.58e-52

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: 168.96  E-value: 8.58e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556289785  33 YKVWLSEVMLQQTQVTTVIPYFERFMARF-PTVVDLANAPLDEVLHLWTGLGYYARARNLHKAAQQVAAQHGGEF---PQ 108
Cdd:cd00056    1 FEVLVSEILSQQTTDKAVNKAYERLFERYgPTPEALAAADEEELRELIRSLGYRRKAKYLKELARAIVEGFGGLVlddPD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556289785 109 TFDEVAALPGVGRSTAGAILSLSLGQHYPILDGNVKRVLARCyavsGWPGKKEVEKRLWEISEAVTPAKGVERFNQAMMD 188
Cdd:cd00056   81 AREELLALPGVGRKTANVVLLFALGPDAFPVDTHVRRVLKRL----GLIPKKKTPEELEELLEELLPKPYWGEANQALMD 156


                 ..
gi 556289785 189 LG 190
Cdd:cd00056  157 LG 158
ENDO3c smart00478
endonuclease III; includes endonuclease III (DNA-(apurinic or apyrimidinic site) lyase), ...
 41-192 5.22e-47

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: 156.27  E-value: 5.22e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556289785    41 MLQQTQVTTVIPYFERFMARFPTVVDLANAPLDEVLHLWTGLG-YYARARNLHKAAQQVAAQHGGEFPQTFDEVAALPGV 119
Cdd:smart00478   1 LSQQTTDERVNKATERLFEKFPTPEDLAAADEEELEELIRGLGfYRRKARYLIELARILVEEYGGEVPDDREELLKLPGV 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 556289785   120 GRSTAGAILSLSLGQHYPILDGNVKRVLARCYavsgWPGKKEVEKRLWEISEAVTPAKGVERFNQAMMDLGAM 192
Cdd:smart00478  81 GRKTANAVLSFALGKPFIPVDTHVLRIAKRLG----LVDKKSTPEEVEKLLEKLLPEEDWRELNLLLIDFGRT 149
HhH-GPD pfam00730
HhH-GPD superfamily base excision DNA repair protein; This family contains a diverse range of ...
 37-169 1.80e-43

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: 147.05  E-value: 1.80e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556289785   37 LSEVMLQQTQVTTVIPYFERFMAR-FPTVVDLANAPLDEVLHLWTGLGYYAR-ARNLHKAAQQVAAQHGGEFPQTFDE-V 113
Cdd:pfam00730   1 VSAILSQQTSDKAVNKITERLFEKfFPTPEDLADADEEELRELIRGLGFYRRkAKYLKELARILVEGYGGEVPLDEEElE 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 556289785  114 AALPGVGRSTAGAILSLSLG--QHYPILDGNVKRVLARCYAVSGWPGKKEVEKRLWEI 169
Cdd:pfam00730  81 ALLKGVGRWTAEAVLIFALGrpDPLPVVDTHVRRVLKRLGLIKEKPTPKEVERELEEL 138
 
Name Accession Description Interval E-value
PRK10880 PRK10880
adenine DNA glycosylase;
5-352 0e+00

adenine DNA glycosylase;


Pssm-ID: 182805 [Multi-domain]  Cd Length: 350  Bit Score: 809.32  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556289785   5 ATQFSAQVLDWYDKYGRKTLPWQIAKTPYKVWLSEVMLQQTQVTTVIPYFERFMARFPTVVDLANAPLDEVLHLWTGLGY 84
Cdd:PRK10880   3 ASQFSAQVLDWYDKYGRKTLPWQIDKTPYKVWLSEVMLQQTQVATVIPYFERFMARFPTVTDLANAPLDEVLHLWTGLGY 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556289785  85 YARARNLHKAAQQVAAQHGGEFPQTFDEVAALPGVGRSTAGAILSLSLGQHYPILDGNVKRVLARCYAVSGWPGKKEVEK 164
Cdd:PRK10880  83 YARARNLHKAAQQVATLHGGEFPETFEEVAALPGVGRSTAGAILSLSLGKHFPILDGNVKRVLARCYAVSGWPGKKEVEN 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556289785 165 RLWEISEAVTPAKGVERFNQAMMDLGAMVCTRSKPKCELCPLSNGCVAYANHSWAEYPGKKPKQTIPERTGYFLLMQHGD 244
Cdd:PRK10880 163 RLWQLSEQVTPAVGVERFNQAMMDLGAMVCTRSKPKCELCPLQNGCIAYANHSWALYPGKKPKQTLPERTGYFLLLQHGD 242

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556289785 245 EVFLAQRPPVGLWGGLFCFPQFADEAGLREWLAQRQIKADNLTQLTAFRHTFSHFHLDIVPMWLTVHSSGACMDEGNALW 324
Cdd:PRK10880 243 EVWLEQRPPSGLWGGLFCFPQFADEEELRQWLAQRGIAADNLTQLTAFRHTFSHFHLDIVPMWLPVSSFTGCMDEGNGLW 322

                        330       340
                 ....*....|....*....|....*...
gi 556289785 325 YNLAQPPSVGLAAPVERLLQQLKAGTPV 352
Cdd:PRK10880 323 YNLAQPPSVGLAAPVERLLQQLRTGAPV 350
MutY COG1194
Adenine-specific DNA glycosylase, acts on AG and A-oxoG pairs [Replication, recombination and ...
 5-348 0e+00

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: 566.30  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556289785   5 ATQFSAQVLDWYDKYGRkTLPWQIAKTPYKVWLSEVMLQQTQVTTVIPYFERFMARFPTVVDLANAPLDEVLHLWTGLGY 84
Cdd:COG1194    3 MASFAKRLLAWYDRHGR-DLPWRQTRDPYRVWLSEIMLQQTQVATVIPYYERFLERFPTVEALAAAPEDEVLKLWEGLGY 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556289785  85 YARARNLHKAAQQVAAQHGGEFPQTFDEVAALPGVGRSTAGAILSLSLGQHYPILDGNVKRVLARCYAVSGWPGKKEVEK 164
Cdd:COG1194   82 YSRARNLHKAAQQVVEEHGGVFPDTYEELLALPGIGPYTAAAIASIAFGEPAPIVDGNVKRVLSRLFAIEGPIGSPAAKK 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556289785 165 RLWEISEAVTPAKGVERFNQAMMDLGAMVCTRSKPKCELCPLSNGCVAYANHSWAEYPGKKPKQTIPERTGYFLLMQHGD 244
Cdd:COG1194  162 ELWALAEELLPPERPGDFNQALMDLGATVCTPKKPKCLLCPLQDDCAAFAEGRQEELPVKKPKKKKPERYGAALVIRDDG 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556289785 245 EVFLAQRPPVGLWGGLFCFPQFADEAG-----LREWLAQR-QIKADNLTQLTAFRHTFSHFHLDIVPMWLTVhSSGACMD 318
Cdd:COG1194  242 RVLLEKRPPKGLWGGLWEFPEFEWEEAedpeaLERWLREElGLEVEWLEPLGTVRHVFTHFRLHLTVYLARV-PAGPPAE 320

                        330       340       350
                 ....*....|....*....|....*....|
gi 556289785 319 EGNALWYNLAQPPSVGLAAPVERLLQQLKA 348
Cdd:COG1194  321 PDGGRWVPLEELAALPLPAPMRKLLKALLK 350
mutY TIGR01084
A/G-specific adenine glycosylase; This equivalog model identifies mutY members of the ...
 7-280 0e+00

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: 505.02  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556289785    7 QFSAQVLDWYDKYGRKTLPWQIAKTPYKVWLSEVMLQQTQVTTVIPYFERFMARFPTVVDLANAPLDEVLHLWTGLGYYA 86
Cdd:TIGR01084   1 QFSEDLLSWYDKYGRKTLPWRQNKTPYRVWLSEVMLQQTQVATVIPYFERFLERFPTVQALANAPQDEVLKLWEGLGYYA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556289785   87 RARNLHKAAQQVAAQHGGEFPQTFDEVAALPGVGRSTAGAILSLSLGQHYPILDGNVKRVLARCYAVSGWPGKKEVEKRL 166
Cdd:TIGR01084  81 RARNLHKAAQEVVEEFGGEFPQDFEDLAALPGVGRYTAGAILSFALNKPYPILDGNVKRVLSRLFAVEGWPGKKKVENRL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556289785  167 WEISEAVTPAKGVERFNQAMMDLGAMVCTRSKPKCELCPLSNGCVAYANHSWAEYPGKKPKQTIPERTGYFLLMQHGD-E 245
Cdd:TIGR01084 161 WTLAESLLPKADPEAFNQALMDLGAMICTRKKPKCDLCPLQDFCLAYQQGTWEEYPVKKPKAAPPERTTYFLVLQNYDgE 240

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 556289785  246 VFLAQRPPVGLWGGLFCFPQFADEAGLREWLAQRQ 280
Cdd:TIGR01084 241 VLLEQRPEKGLWGGLYCFPQFEDEDSLAFLLAQRG 275
ENDO3c cd00056
endonuclease III; includes endonuclease III (DNA-(apurinic or apyrimidinic site) lyase), ...
 33-190 8.58e-52

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: 168.96  E-value: 8.58e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556289785  33 YKVWLSEVMLQQTQVTTVIPYFERFMARF-PTVVDLANAPLDEVLHLWTGLGYYARARNLHKAAQQVAAQHGGEF---PQ 108
Cdd:cd00056    1 FEVLVSEILSQQTTDKAVNKAYERLFERYgPTPEALAAADEEELRELIRSLGYRRKAKYLKELARAIVEGFGGLVlddPD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556289785 109 TFDEVAALPGVGRSTAGAILSLSLGQHYPILDGNVKRVLARCyavsGWPGKKEVEKRLWEISEAVTPAKGVERFNQAMMD 188
Cdd:cd00056   81 AREELLALPGVGRKTANVVLLFALGPDAFPVDTHVRRVLKRL----GLIPKKKTPEELEELLEELLPKPYWGEANQALMD 156


                 ..
gi 556289785 189 LG 190
Cdd:cd00056  157 LG 158
ENDO3c smart00478
endonuclease III; includes endonuclease III (DNA-(apurinic or apyrimidinic site) lyase), ...
 41-192 5.22e-47

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: 156.27  E-value: 5.22e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556289785    41 MLQQTQVTTVIPYFERFMARFPTVVDLANAPLDEVLHLWTGLG-YYARARNLHKAAQQVAAQHGGEFPQTFDEVAALPGV 119
Cdd:smart00478   1 LSQQTTDERVNKATERLFEKFPTPEDLAAADEEELEELIRGLGfYRRKARYLIELARILVEEYGGEVPDDREELLKLPGV 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 556289785   120 GRSTAGAILSLSLGQHYPILDGNVKRVLARCYavsgWPGKKEVEKRLWEISEAVTPAKGVERFNQAMMDLGAM 192
Cdd:smart00478  81 GRKTANAVLSFALGKPFIPVDTHVLRIAKRLG----LVDKKSTPEEVEKLLEKLLPEEDWRELNLLLIDFGRT 149
HhH-GPD pfam00730
HhH-GPD superfamily base excision DNA repair protein; This family contains a diverse range of ...
 37-169 1.80e-43

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: 147.05  E-value: 1.80e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556289785   37 LSEVMLQQTQVTTVIPYFERFMAR-FPTVVDLANAPLDEVLHLWTGLGYYAR-ARNLHKAAQQVAAQHGGEFPQTFDE-V 113
Cdd:pfam00730   1 VSAILSQQTSDKAVNKITERLFEKfFPTPEDLADADEEELRELIRGLGFYRRkAKYLKELARILVEGYGGEVPLDEEElE 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 556289785  114 AALPGVGRSTAGAILSLSLG--QHYPILDGNVKRVLARCYAVSGWPGKKEVEKRLWEI 169
Cdd:pfam00730  81 ALLKGVGRWTAEAVLIFALGrpDPLPVVDTHVRRVLKRLGLIKEKPTPKEVERELEEL 138
PRK13910 PRK13910
DNA glycosylase MutY; Provisional
 41-303 4.63e-38

DNA glycosylase MutY; Provisional


Pssm-ID: 172427 [Multi-domain]  Cd Length: 289  Bit Score: 137.46  E-value: 4.63e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556289785  41 MLQQTQVTTVIP-YFERFMARFPTVVDLANAPLDEVLHLWTGLGYYARARNLHKAAQQVAAQHGGEFPQTFDEVAALPGV 119
Cdd:PRK13910   1 MSQQTQINTVVErFYSPFLEAFPTLKDLANAPLEEVLLLWRGLGYYSRAKNLKKSAEICVKEHHSQLPNDYQSLLKLPGI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556289785 120 GRSTAGAILSLSLGQHYPILDGNVKRVLARCYAVSGWPGKKEVEKR---LWEISEAVTpakgverFNQAMMDLGAMVCTr 196
Cdd:PRK13910  81 GAYTANAILCFGFREKSACVDANIKRVLLRLFGLDPNIHAKDLQIKandFLNLNESFN-------HNQALIDLGALICS- 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556289785 197 SKPKCELCPLSNGCVAyANHswAEYPGKKPKQTIPERTGYFLLMQHGDEVFLaQRPPVGLWGGLFCFPQfadeagLREWL 276
Cdd:PRK13910 153 PKPKCAICPLNPYCLG-KNN--PEKHTLKKKQEIVQEERYLGVVIQNNQIAL-EKIEQKLYLGMHHFPN------LKENL 222

                        250       260
                 ....*....|....*....|....*..
gi 556289785 277 AQRqikadnLTQLTAFRHTFSHFHLDI 303
Cdd:PRK13910 223 EYK------LPFLGAIKHSHTKFKLNL 243
Nth COG0177
Endonuclease III [Replication, recombination and repair];
30-210 4.05e-35

Endonuclease III [Replication, recombination and repair];


Pssm-ID: 439947 [Multi-domain]  Cd Length: 198  Bit Score: 127.13  E-value: 4.05e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556289785  30 KTPYKVWLSEVMLQQT---QVTTVipyFERFMARFPTVVDLANAPLDEVLHLWTGLGYY-ARARNLHKAAQQVAAQHGGE 105
Cdd:COG0177   18 RDPFELLVATILSAQTtdeRVNKA---TPRLFARYPTPEALAAADLEELEELIRPIGLYrNKAKNIIALARILVEKYGGE 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556289785 106 FPQTFDEVAALPGVGRSTAGAILSLSLGQHYPILDGNVKRVLARcyavSGW-PGK--KEVEKRLweisEAVTPAKGVERF 182
Cdd:COG0177   95 VPETREELESLPGVGRKTANVVLNFAFGKPAIAVDTHVHRVSNR----LGLvPGKdpEEVEKDL----MKLIPKEYWGDL 166

                        170       180
                 ....*....|....*....|....*...
gi 556289785 183 NQAMMDLGAMVCTRSKPKCELCPLSNGC 210
Cdd:COG0177  167 HHLLILHGRYICKARKPKCEECPLADLC 194
NUDIX_DNA_Glycosylase_C-MutY cd03431
C-terminal domain of DNA glycosylase; DNA glycosylase (MutY in bacteria and hMYH in humans) is ...
 230-344 3.07e-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: 114.32  E-value: 3.07e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556289785 230 IPERTGYFLLMQHGDEVFLAQRPPVGLWGGLFCFPQFADEAGLREWLAQRQIKAD----NLTQLTAFRHTFSHFHLDIVP 305
Cdd:cd03431    1 VPERYFTVLVLRDGGRVLLEKRPEKGLLAGLWEFPLVETEEEEEEAEALLGLLAEelllILEPLGEVKHVFSHFRLHITV 80

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 556289785 306 MWLTVhSSGACMDEGNALWYNLAQPPSVGLAAPVERLLQ 344
Cdd:cd03431   81 YLVEL-PEAPPAAPDEGRWVDLEELDEYALPAPMRKLLE 118
NUDIX_4 pfam14815
NUDIX domain;
236-345 1.56e-23

NUDIX domain;


Pssm-ID: 464330 [Multi-domain]  Cd Length: 114  Bit Score: 93.53  E-value: 1.56e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556289785  236 YFLLMQHGDEVFLAQRPPVGLWGGLFCFPQFADEAG--LREWLAQRQIKADNLTQLTAFR--HTFSHFHLDIVpMWLTVH 311
Cdd:pfam14815   2 VLVIRNGDGRVLLRKRPEKGLLGGLWEFPGGKVEPGetLEEALARLEELGIEVEVLEPGTvkHVFTHFRLTLH-VYLVRE 80

                          90       100       110
                  ....*....|....*....|....*....|....
gi 556289785  312 SSGACMDEGNALWYNLAQPPSVGLAAPVERLLQQ 345
Cdd:pfam14815  81 VEGEEEPQQELRWVTPEELDKYALPAAVRKILEA 114
nth TIGR01083
endonuclease III; This equivalog model identifes nth members of the pfam00730 superfamily ...
 30-201 1.34e-20

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: 88.21  E-value: 1.34e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556289785   30 KTPYKVWLSEVMLQQTQVTTVIPYFERFMARFPTVVDLANAPLDEVLHLWTGLGYY-ARARNLHKAAQQVAAQHGGEFPQ 108
Cdd:TIGR01083  25 NNPFELLVATILSAQATDKRVNKATPKLFEVYPTPQALAQAGLEELEEYIKSIGLYrNKAKNIIELCRKLVERYGGEVPE 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556289785  109 TFDEVAALPGVGRSTAGAILSLSLGQHYPILDGNVKRVLARcyavSGWPGKKEVEKRLWEISEaVTPAKGVERFNQAMMD 188
Cdd:TIGR01083 105 DREELVKLPGVGRKTANVVLNVAFGIPAIAVDTHVFRVSNR----LGLSKGKDPIKVEEDLMK-LVPREFWVKLHHWLIL 179

                         170
                  ....*....|...
gi 556289785  189 LGAMVCTRSKPKC 201
Cdd:TIGR01083 180 HGRYTCKARKPLC 192
PRK10702 PRK10702
endonuclease III; Provisional
 84-210 1.10e-10

endonuclease III; Provisional


Pssm-ID: 182661 [Multi-domain]  Cd Length: 211  Bit Score: 60.42  E-value: 1.10e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556289785  84 YYARARNLHKAAQQVAAQHGGEFPQTFDEVAALPGVGRSTAGAILSLSLGQHYPILDGNVKRVlarCYAVSGWPGK--KE 161
Cdd:PRK10702  82 YNSKAENVIKTCRILLEQHNGEVPEDRAALEALPGVGRKTANVVLNTAFGWPTIAVDTHIFRV---CNRTQFAPGKnvEQ 158

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 556289785 162 VEKRLWEiseaVTPAKGVERFNQAMMDLGAMVCTRSKPKCELCPLSNGC 210
Cdd:PRK10702 159 VEEKLLK----VVPAEFKVDCHHWLILHGRYTCIARKPRCGSCIIEDLC 203
HP0602 COG2231
3-Methyladenine DNA glycosylase, HhH-GPD/Endo3 superfamily [Replication, recombination and ...
 16-217 2.35e-09

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


Pssm-ID: 441832 [Multi-domain]  Cd Length: 220  Bit Score: 56.78  E-value: 2.35e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556289785  16 YDKYGRktLPWQIAKTPYKVWLSEVMLQQTQVTTVipyfERFMARFP-----TVVDLANAPLDEVLHLWTGLGYYAR-AR 89
Cdd:COG2231   15 LEHYGP--QHWWPAETPFEVIVGAILTQNTSWKNV----EKAIANLKeagllDPEALAALDPEELAELIRPSGFYNQkAK 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556289785  90 NLHKAAQQVAAQHGGEFPQTF--------DEVAALPGVGRSTAGAILSLSLgqHYPIL--DGNVKRVLARcyaVSGWPGK 159
Cdd:COG2231   89 RLKNLARWLVERYGGGLEKLKalpteelrEELLSLKGIGPETADSILLYAF--NRPVFvvDAYTRRIFSR---LGLIEED 163

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 556289785 160 KEVEkrlwEISEAVTPA--KGVERFNQ--AMMD-LGAMVCtRSKPKCELCPLSNGCvAYANHS 217
Cdd:COG2231  164 ASYD----ELQRLFEENlpPDVALYNEfhALIVeHGKEYC-KKKPKCEECPLRDLC-PYGGQE 220
HHH pfam00633
Helix-hairpin-helix motif; The helix-hairpin-helix DNA-binding motif is found to be duplicated ...
 102-129 1.54e-06

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: 43.94  E-value: 1.54e-06
                          10        20
                  ....*....|....*....|....*...
gi 556289785  102 HGGEFPQTFDEVAALPGVGRSTAGAILS 129
Cdd:pfam00633   2 LEGLIPASVEELLALPGVGPKTAEAILS 29
AlkA COG0122
3-methyladenine DNA glycosylase/8-oxoguanine DNA glycosylase [Replication, recombination and ...
 49-166 7.46e-06

3-methyladenine DNA glycosylase/8-oxoguanine DNA glycosylase [Replication, recombination and repair];


Pssm-ID: 439892 [Multi-domain]  Cd Length: 255  Bit Score: 46.80  E-value: 7.46e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556289785  49 TVIPYFERFMARFPTVVDLANAPLDEVLHLwtGLGYYaRARNLHKAAQQVAAQ-------HGGEFPQTFDEVAALPGVGR 121
Cdd:COG0122  115 EPIEGPGGGLYAFPTPEALAAASEEELRAC--GLSRR-KARYLRALARAVADGeldlealAGLDDEEAIARLTALPGIGP 191

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 556289785 122 STAGAILSLSLGQH--YPILDGNVKRVLARCYAVSGWPGKKEVEKRL 166
Cdd:COG0122  192 WTAEMVLLFALGRPdaFPAGDLGLRRALGRLYGLGERPTPKELRELA 238
FES smart00525
iron-sulpphur binding domain in DNA-(apurinic or apyrimidinic site) lyase (subfamily of ENDO3); ...
 193-213 8.90e-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: 39.07  E-value: 8.90e-05
                           10        20
                   ....*....|....*....|.
gi 556289785   193 VCTRSKPKCELCPLSNGCVAY 213
Cdd:smart00525   1 ICTARKPRCDECPLKDLCPAY 21
EndIII_4Fe-2S pfam10576
Iron-sulfur binding domain of endonuclease III; Escherichia coli endonuclease III (EC 4.2.99. ...
 194-210 3.24e-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: 37.37  E-value: 3.24e-04
                          10
                  ....*....|....*..
gi 556289785  194 CTRSKPKCELCPLSNGC 210
Cdd:pfam10576   1 CTARKPKCEECPLADLC 17
 
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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