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Conserved domains on  [gi|16129591|ref|NP_416150|]
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endonuclease III [Escherichia coli str. K-12 substr. MG1655]

Protein Classification

endonuclease III( domain architecture ID 11484879)

endonuclease III is a DNA repair enzyme that has both DNA N-glycosylase and AP-lyase activities

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK10702 PRK10702
endonuclease III; Provisional
 1-211 4.22e-165

endonuclease III; Provisional


:

Pssm-ID: 182661 [Multi-domain]  Cd Length: 211  Bit Score: 452.93  E-value: 4.22e-165
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129591    1 MNKAKRLEILTRLRENNPHPTTELNFSSPFELLIAVLLSAQATDVSVNKATAKLYPVANTPAAMLELGVEGVKTYIKTIG 80
Cdd:PRK10702   1 MNKAKRLEILTRLRDNNPHPTTELNFSSPFELLIAVLLSAQATDVSVNKATAKLYPVANTPAAMLELGVEGVKTYIKTIG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129591   81 LYNSKAENIIKTCRILLEQHNGEVPEDRAALEALPGVGRKTANVVLNTAFGWPTIAVDTHIFRVCNRTQFAPGKNVEQVE 160
Cdd:PRK10702  81 LYNSKAENVIKTCRILLEQHNGEVPEDRAALEALPGVGRKTANVVLNTAFGWPTIAVDTHIFRVCNRTQFAPGKNVEQVE 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 16129591  161 EKLLKVVPAEFKVDCHHWLILHGRYTCIARKPRCGSCIIEDLCEYKEKVDI 211
Cdd:PRK10702 161 EKLLKVVPAEFKVDCHHWLILHGRYTCIARKPRCGSCIIEDLCEYKEKVDI 211
 
Name Accession Description Interval E-value
PRK10702 PRK10702
endonuclease III; Provisional
 1-211 4.22e-165

endonuclease III; Provisional


Pssm-ID: 182661 [Multi-domain]  Cd Length: 211  Bit Score: 452.93  E-value: 4.22e-165
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129591    1 MNKAKRLEILTRLRENNPHPTTELNFSSPFELLIAVLLSAQATDVSVNKATAKLYPVANTPAAMLELGVEGVKTYIKTIG 80
Cdd:PRK10702   1 MNKAKRLEILTRLRDNNPHPTTELNFSSPFELLIAVLLSAQATDVSVNKATAKLYPVANTPAAMLELGVEGVKTYIKTIG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129591   81 LYNSKAENIIKTCRILLEQHNGEVPEDRAALEALPGVGRKTANVVLNTAFGWPTIAVDTHIFRVCNRTQFAPGKNVEQVE 160
Cdd:PRK10702  81 LYNSKAENVIKTCRILLEQHNGEVPEDRAALEALPGVGRKTANVVLNTAFGWPTIAVDTHIFRVCNRTQFAPGKNVEQVE 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 16129591  161 EKLLKVVPAEFKVDCHHWLILHGRYTCIARKPRCGSCIIEDLCEYKEKVDI 211
Cdd:PRK10702 161 EKLLKVVPAEFKVDCHHWLILHGRYTCIARKPRCGSCIIEDLCEYKEKVDI 211
nth TIGR01083
endonuclease III; This equivalog model identifes nth members of the pfam00730 superfamily ...
 3-194 1.73e-123

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: 347.06  E-value: 1.73e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129591     3 KAKRLEILTRLRENNPHPTTELNFSSPFELLIAVLLSAQATDVSVNKATAKLYPVANTPAAMLELGVEGVKTYIKTIGLY 82
Cdd:TIGR01083   1 RQKAQEILERLRKNYPHPTTELDFNNPFELLVATILSAQATDKRVNKATPKLFEVYPTPQALAQAGLEELEEYIKSIGLY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129591    83 NSKAENIIKTCRILLEQHNGEVPEDRAALEALPGVGRKTANVVLNTAFGWPTIAVDTHIFRVCNRTQFAPGKNVEQVEEK 162
Cdd:TIGR01083  81 RNKAKNIIELCRKLVERYGGEVPEDREELVKLPGVGRKTANVVLNVAFGIPAIAVDTHVFRVSNRLGLSKGKDPIKVEED 160

                         170       180       190
                  ....*....|....*....|....*....|..
gi 16129591   163 LLKVVPAEFKVDCHHWLILHGRYTCIARKPRC 194
Cdd:TIGR01083 161 LMKLVPREFWVKLHHWLILHGRYTCKARKPLC 192
Nth COG0177
Endonuclease III [Replication, recombination and repair];
10-207 5.55e-123

Endonuclease III [Replication, recombination and repair];


Pssm-ID: 439947 [Multi-domain]  Cd Length: 198  Bit Score: 345.93  E-value: 5.55e-123
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129591  10 LTRLRENNPHPTTELNFSSPFELLIAVLLSAQATDVSVNKATAKLYPVANTPAAMLELGVEGVKTYIKTIGLYNSKAENI 89
Cdd:COG0177   1 LERLKELYPDAKTELDYRDPFELLVATILSAQTTDERVNKATPRLFARYPTPEALAAADLEELEELIRPIGLYRNKAKNI 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129591  90 IKTCRILLEQHNGEVPEDRAALEALPGVGRKTANVVLNTAFGWPTIAVDTHIFRVCNRTQFAPGKNVEQVEEKLLKVVPA 169
Cdd:COG0177  81 IALARILVEKYGGEVPETREELESLPGVGRKTANVVLNFAFGKPAIAVDTHVHRVSNRLGLVPGKDPEEVEKDLMKLIPK 160

                       170       180       190
                ....*....|....*....|....*....|....*...
gi 16129591 170 EFKVDCHHWLILHGRYTCIARKPRCGSCIIEDLCEYKE 207
Cdd:COG0177 161 EYWGDLHHLLILHGRYICKARKPKCEECPLADLCPYYG 198
ENDO3c cd00056
endonuclease III; includes endonuclease III (DNA-(apurinic or apyrimidinic site) lyase), ...
 30-183 3.91e-53

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: 167.80  E-value: 3.91e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129591  30 FELLIAVLLSAQATDVSVNKATAKLYP-VANTPAAMLELGVEGVKTYIKTIGlYNSKAENIIKTCRILLEQHNGEV---P 105
Cdd:cd00056   1 FEVLVSEILSQQTTDKAVNKAYERLFErYGPTPEALAAADEEELRELIRSLG-YRRKAKYLKELARAIVEGFGGLVlddP 79

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16129591 106 EDRAALEALPGVGRKTANVVLNTAFGWPTIAVDTHIFRVCNRTQFAP-GKNVEQVEEKLLKVVPAEFKVDCHHWLILHG 183
Cdd:cd00056  80 DAREELLALPGVGRKTANVVLLFALGPDAFPVDTHVRRVLKRLGLIPkKKTPEELEELLEELLPKPYWGEANQALMDLG 158
ENDO3c smart00478
endonuclease III; includes endonuclease III (DNA-(apurinic or apyrimidinic site) lyase), ...
 38-185 7.93e-51

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: 161.28  E-value: 7.93e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129591     38 LSAQATDVSVNKATAKLYPVANTPAAMLELGVEGVKTYIKTIGLYNSKAENIIKTCRILLEQHNGEVPEDRAALEALPGV 117
Cdd:smart00478   1 LSQQTTDERVNKATERLFEKFPTPEDLAAADEEELEELIRGLGFYRRKARYLIELARILVEEYGGEVPDDREELLKLPGV 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16129591    118 GRKTANVVLNTAFGWPTIAVDTHIFRVCNRTQFAPGKNV-EQVEEKLLKVVPAEFKVDCHHWLILHGRY 185
Cdd:smart00478  81 GRKTANAVLSFALGKPFIPVDTHVLRIAKRLGLVDKKSTpEEVEKLLEKLLPEEDWRELNLLLIDFGRT 149
HhH-GPD pfam00730
HhH-GPD superfamily base excision DNA repair protein; This family contains a diverse range of ...
 34-168 6.39e-42

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: 138.57  E-value: 6.39e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129591    34 IAVLLSAQATDVSVNKATAKLY-PVANTPAAMLELGVEGVKTYIKTIGLYNSKAENIIKTCRILLEQHNGEVPEDRAALE 112
Cdd:pfam00730   1 VSAILSQQTSDKAVNKITERLFeKFFPTPEDLADADEEELRELIRGLGFYRRKAKYLKELARILVEGYGGEVPLDEEELE 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129591   113 A-LPGVGRKTANVVLNTAFG--WPTIAVDTHIFRVCNRTQFAPGKN-VEQVEEKLLKVVP 168
Cdd:pfam00730  81 AlLKGVGRWTAEAVLIFALGrpDPLPVVDTHVRRVLKRLGLIKEKPtPKEVERELEELWP 140
 
Name Accession Description Interval E-value
PRK10702 PRK10702
endonuclease III; Provisional
 1-211 4.22e-165

endonuclease III; Provisional


Pssm-ID: 182661 [Multi-domain]  Cd Length: 211  Bit Score: 452.93  E-value: 4.22e-165
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129591    1 MNKAKRLEILTRLRENNPHPTTELNFSSPFELLIAVLLSAQATDVSVNKATAKLYPVANTPAAMLELGVEGVKTYIKTIG 80
Cdd:PRK10702   1 MNKAKRLEILTRLRDNNPHPTTELNFSSPFELLIAVLLSAQATDVSVNKATAKLYPVANTPAAMLELGVEGVKTYIKTIG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129591   81 LYNSKAENIIKTCRILLEQHNGEVPEDRAALEALPGVGRKTANVVLNTAFGWPTIAVDTHIFRVCNRTQFAPGKNVEQVE 160
Cdd:PRK10702  81 LYNSKAENVIKTCRILLEQHNGEVPEDRAALEALPGVGRKTANVVLNTAFGWPTIAVDTHIFRVCNRTQFAPGKNVEQVE 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 16129591  161 EKLLKVVPAEFKVDCHHWLILHGRYTCIARKPRCGSCIIEDLCEYKEKVDI 211
Cdd:PRK10702 161 EKLLKVVPAEFKVDCHHWLILHGRYTCIARKPRCGSCIIEDLCEYKEKVDI 211
nth TIGR01083
endonuclease III; This equivalog model identifes nth members of the pfam00730 superfamily ...
 3-194 1.73e-123

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: 347.06  E-value: 1.73e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129591     3 KAKRLEILTRLRENNPHPTTELNFSSPFELLIAVLLSAQATDVSVNKATAKLYPVANTPAAMLELGVEGVKTYIKTIGLY 82
Cdd:TIGR01083   1 RQKAQEILERLRKNYPHPTTELDFNNPFELLVATILSAQATDKRVNKATPKLFEVYPTPQALAQAGLEELEEYIKSIGLY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129591    83 NSKAENIIKTCRILLEQHNGEVPEDRAALEALPGVGRKTANVVLNTAFGWPTIAVDTHIFRVCNRTQFAPGKNVEQVEEK 162
Cdd:TIGR01083  81 RNKAKNIIELCRKLVERYGGEVPEDREELVKLPGVGRKTANVVLNVAFGIPAIAVDTHVFRVSNRLGLSKGKDPIKVEED 160

                         170       180       190
                  ....*....|....*....|....*....|..
gi 16129591   163 LLKVVPAEFKVDCHHWLILHGRYTCIARKPRC 194
Cdd:TIGR01083 161 LMKLVPREFWVKLHHWLILHGRYTCKARKPLC 192
Nth COG0177
Endonuclease III [Replication, recombination and repair];
10-207 5.55e-123

Endonuclease III [Replication, recombination and repair];


Pssm-ID: 439947 [Multi-domain]  Cd Length: 198  Bit Score: 345.93  E-value: 5.55e-123
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129591  10 LTRLRENNPHPTTELNFSSPFELLIAVLLSAQATDVSVNKATAKLYPVANTPAAMLELGVEGVKTYIKTIGLYNSKAENI 89
Cdd:COG0177   1 LERLKELYPDAKTELDYRDPFELLVATILSAQTTDERVNKATPRLFARYPTPEALAAADLEELEELIRPIGLYRNKAKNI 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129591  90 IKTCRILLEQHNGEVPEDRAALEALPGVGRKTANVVLNTAFGWPTIAVDTHIFRVCNRTQFAPGKNVEQVEEKLLKVVPA 169
Cdd:COG0177  81 IALARILVEKYGGEVPETREELESLPGVGRKTANVVLNFAFGKPAIAVDTHVHRVSNRLGLVPGKDPEEVEKDLMKLIPK 160

                       170       180       190
                ....*....|....*....|....*....|....*...
gi 16129591 170 EFKVDCHHWLILHGRYTCIARKPRCGSCIIEDLCEYKE 207
Cdd:COG0177 161 EYWGDLHHLLILHGRYICKARKPKCEECPLADLCPYYG 198
ENDO3c cd00056
endonuclease III; includes endonuclease III (DNA-(apurinic or apyrimidinic site) lyase), ...
 30-183 3.91e-53

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: 167.80  E-value: 3.91e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129591  30 FELLIAVLLSAQATDVSVNKATAKLYP-VANTPAAMLELGVEGVKTYIKTIGlYNSKAENIIKTCRILLEQHNGEV---P 105
Cdd:cd00056   1 FEVLVSEILSQQTTDKAVNKAYERLFErYGPTPEALAAADEEELRELIRSLG-YRRKAKYLKELARAIVEGFGGLVlddP 79

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16129591 106 EDRAALEALPGVGRKTANVVLNTAFGWPTIAVDTHIFRVCNRTQFAP-GKNVEQVEEKLLKVVPAEFKVDCHHWLILHG 183
Cdd:cd00056  80 DAREELLALPGVGRKTANVVLLFALGPDAFPVDTHVRRVLKRLGLIPkKKTPEELEELLEELLPKPYWGEANQALMDLG 158
ENDO3c smart00478
endonuclease III; includes endonuclease III (DNA-(apurinic or apyrimidinic site) lyase), ...
 38-185 7.93e-51

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: 161.28  E-value: 7.93e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129591     38 LSAQATDVSVNKATAKLYPVANTPAAMLELGVEGVKTYIKTIGLYNSKAENIIKTCRILLEQHNGEVPEDRAALEALPGV 117
Cdd:smart00478   1 LSQQTTDERVNKATERLFEKFPTPEDLAAADEEELEELIRGLGFYRRKARYLIELARILVEEYGGEVPDDREELLKLPGV 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16129591    118 GRKTANVVLNTAFGWPTIAVDTHIFRVCNRTQFAPGKNV-EQVEEKLLKVVPAEFKVDCHHWLILHGRY 185
Cdd:smart00478  81 GRKTANAVLSFALGKPFIPVDTHVLRIAKRLGLVDKKSTpEEVEKLLEKLLPEEDWRELNLLLIDFGRT 149
HhH-GPD pfam00730
HhH-GPD superfamily base excision DNA repair protein; This family contains a diverse range of ...
 34-168 6.39e-42

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: 138.57  E-value: 6.39e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129591    34 IAVLLSAQATDVSVNKATAKLY-PVANTPAAMLELGVEGVKTYIKTIGLYNSKAENIIKTCRILLEQHNGEVPEDRAALE 112
Cdd:pfam00730   1 VSAILSQQTSDKAVNKITERLFeKFFPTPEDLADADEEELRELIRGLGFYRRKAKYLKELARILVEGYGGEVPLDEEELE 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129591   113 A-LPGVGRKTANVVLNTAFG--WPTIAVDTHIFRVCNRTQFAPGKN-VEQVEEKLLKVVP 168
Cdd:pfam00730  81 AlLKGVGRWTAEAVLIFALGrpDPLPVVDTHVRRVLKRLGLIKEKPtPKEVERELEELWP 140
HP0602 COG2231
3-Methyladenine DNA glycosylase, HhH-GPD/Endo3 superfamily [Replication, recombination and ...
 28-205 2.86e-23

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


Pssm-ID: 441832 [Multi-domain]  Cd Length: 220  Bit Score: 92.60  E-value: 2.86e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129591  28 SPFELLI-AVLlsAQATD-VSVNKATAKLYP-VANTPAAMLELGVEGVKTYIKTIGLYNSKAENIIKTCRILLEQHNGEV 104
Cdd:COG2231  28 TPFEVIVgAIL--TQNTSwKNVEKAIANLKEaGLLDPEALAALDPEELAELIRPSGFYNQKAKRLKNLARWLVERYGGGL 105

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129591 105 --------PEDRAALEALPGVGRKTANVVLNTAFGWPTIAVDTHIFRVCNRTQFAPG-KNVEQVEEKLLKVVPA------ 169
Cdd:COG2231 106 eklkalptEELREELLSLKGIGPETADSILLYAFNRPVFVVDAYTRRIFSRLGLIEEdASYDELQRLFEENLPPdvalyn 185

                       170       180       190
                ....*....|....*....|....*....|....*.
gi 16129591 170 EFkvdcHHWLILHGRYTCiARKPRCGSCIIEDLCEY 205
Cdd:COG2231 186 EF----HALIVEHGKEYC-KKKPKCEECPLRDLCPY 216
MutY COG1194
Adenine-specific DNA glycosylase, acts on AG and A-oxoG pairs [Replication, recombination and ...
 80-204 3.56e-15

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: 72.86  E-value: 3.56e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129591  80 GL-YNSKAENIIKTCRILLEQHNGEVPEDRAALEALPGVGRKTANVVLNTAFGWPTIAVDTHIFRVCNRtQFA----PG- 153
Cdd:COG1194  78 GLgYYSRARNLHKAAQQVVEEHGGVFPDTYEELLALPGIGPYTAAAIASIAFGEPAPIVDGNVKRVLSR-LFAiegpIGs 156

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16129591 154 -KNVEQVEEKLLKVVPAEfkvDChhwlilhGRYT----------CIARKPRCGSCIIEDLCE 204
Cdd:COG1194 157 pAAKKELWALAEELLPPE---RP-------GDFNqalmdlgatvCTPKKPKCLLCPLQDDCA 208
PRK10880 PRK10880
adenine DNA glycosylase;
80-203 5.12e-11

adenine DNA glycosylase;


Pssm-ID: 182805 [Multi-domain]  Cd Length: 350  Bit Score: 60.88  E-value: 5.12e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129591   80 GL-YNSKAENIIKTCRILLEQHNGEVPEDRAALEALPGVGRKTANVVLNTAFGWPTIAVDTHIFRVCNRTqFA----PGK 154
Cdd:PRK10880  79 GLgYYARARNLHKAAQQVATLHGGEFPETFEEVAALPGVGRSTAGAILSLSLGKHFPILDGNVKRVLARC-YAvsgwPGK 157

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 16129591  155 nvEQVEEKLL----KVVPAEFKVDCHHWLILHGRYTCIARKPRCGSCIIEDLC 203
Cdd:PRK10880 158 --KEVENRLWqlseQVTPAVGVERFNQAMMDLGAMVCTRSKPKCELCPLQNGC 208
AlkA COG0122
3-methyladenine DNA glycosylase/8-oxoguanine DNA glycosylase [Replication, recombination and ...
 28-141 2.30e-10

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


Pssm-ID: 439892 [Multi-domain]  Cd Length: 255  Bit Score: 58.36  E-value: 2.30e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129591  28 SPFELLIAVLLSAQatdVSVNKATA-----------------KLYPVANTPAAMLELGVEGvktyIKTIGLYNSKAENII 90
Cdd:COG0122  83 DPFEALVRAILGQQ---VSVAAARTiwrrlvalfgepiegpgGGLYAFPTPEALAAASEEE----LRACGLSRRKARYLR 155

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129591  91 KTCRILLEQ-------HNGEVPEDRAALEALPGVGRKTANVVLNTAFGWPTI--AVDTHI 141
Cdd:COG0122 156 ALARAVADGeldlealAGLDDEEAIARLTALPGIGPWTAEMVLLFALGRPDAfpAGDLGL 215
PRK13910 PRK13910
DNA glycosylase MutY; Provisional
 82-203 1.54e-08

DNA glycosylase MutY; Provisional


Pssm-ID: 172427 [Multi-domain]  Cd Length: 289  Bit Score: 53.49  E-value: 1.54e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129591   82 YNSKAENIIKTCRILLEQHNGEVPEDRAALEALPGVGRKTANVVLNTAFGWPTIAVDTHIFRVCNRT-QFAPGKNVEQVE 160
Cdd:PRK13910  45 YYSRAKNLKKSAEICVKEHHSQLPNDYQSLLKLPGIGAYTANAILCFGFREKSACVDANIKRVLLRLfGLDPNIHAKDLQ 124

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 16129591  161 EKLLKVVPAEFKVDCHHWLILHGRYTCiARKPRCGSCIIEDLC 203
Cdd:PRK13910 125 IKANDFLNLNESFNHNQALIDLGALIC-SPKPKCAICPLNPYC 166
HHH pfam00633
Helix-hairpin-helix motif; The helix-hairpin-helix DNA-binding motif is found to be duplicated ...
 100-126 2.51e-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: 40.09  E-value: 2.51e-05
                          10        20
                  ....*....|....*....|....*..
gi 16129591   100 HNGEVPEDRAALEALPGVGRKTANVVL 126
Cdd:pfam00633   2 LEGLIPASVEELLALPGVGPKTAEAIL 28
FES smart00525
iron-sulpphur binding domain in DNA-(apurinic or apyrimidinic site) lyase (subfamily of ENDO3); ...
 186-206 1.11e-04

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


Pssm-ID: 197771 [Multi-domain]  Cd Length: 21  Bit Score: 37.92  E-value: 1.11e-04
                           10        20
                   ....*....|....*....|.
gi 16129591    186 TCIARKPRCGSCIIEDLCEYK 206
Cdd:smart00525   1 ICTARKPRCDECPLKDLCPAY 21
ogg TIGR00588
8-oxoguanine DNA-glycosylase (ogg); All proteins in this family for which functions are known ...
 29-147 2.20e-04

8-oxoguanine DNA-glycosylase (ogg); All proteins in this family for which functions are known are 8-oxo-guanaine DNA glycosylases that function in base excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). This family is distantly realted to the Nth-MutY superfamily. [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 211589 [Multi-domain]  Cd Length: 310  Bit Score: 41.05  E-value: 2.20e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129591    29 PFELLIAVLLSAQATDV----SVNKATAKLYPVANT---------PAAMlELGVEGVKTYIKTIGLyNSKAENIIKTCRI 95
Cdd:TIGR00588 119 PFECLISFICSSNNNIAritrMVERLCQAFGPRLITldgvtyhgfPSLH-ALTGPEAEAHLRKLGL-GYRARYIRETARA 196

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16129591    96 LLEQHNG----------EVPEDRAALEALPGVGRKTANVVLNTAFGWPTIA-VDTHIFRVCNR 147
Cdd:TIGR00588 197 LLEEQGGrawlqqirgaSYEDAREALCELPGVGPKVADCICLMGLDKPQAVpVDVHVWRIANR 259
EndIII_4Fe-2S pfam10576
Iron-sulfur binding domain of endonuclease III; Escherichia coli endonuclease III (EC 4.2.99. ...
 187-203 1.37e-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: 35.05  E-value: 1.37e-03
                          10
                  ....*....|....*..
gi 16129591   187 CIARKPRCGSCIIEDLC 203
Cdd:pfam10576   1 CTARKPKCEECPLADLC 17
PRK13913 PRK13913
3-methyladenine DNA glycosylase; Provisional
 76-143 5.37e-03

3-methyladenine DNA glycosylase; Provisional


Pssm-ID: 184390  Cd Length: 218  Bit Score: 36.75  E-value: 5.37e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16129591   76 IKTIGLYNSKAENIIKTCRILL------EQHNGEVpeDRAALEALPGVGRKTANVVLNTAFGWPTIAVDTHIFR 143
Cdd:PRK13913  84 VRPSGFYNQKAKRLIDLSENILkdfgsfENFKQEV--TREWLLDQKGIGKESADAILCYVCAKEVMVVDKYSYL 155
 
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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