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Conserved domains on  [gi|503756652|ref|WP_013990728|]
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MULTISPECIES: endonuclease III [Streptococcus]

Protein Classification

endonuclease III( domain architecture ID 11415064)

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

EC:  4.2.99.18
Gene Symbol:  nth
Gene Ontology:  GO:0051539|GO:0140078

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Nth COG0177
Endonuclease III [Replication, recombination and repair];
11-209 2.59e-114

Endonuclease III [Replication, recombination and repair];


:

Pssm-ID: 439947 [Multi-domain]  Cd Length: 198  Bit Score: 324.36  E-value: 2.59e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503756652  11 LALMGEMFPNAHGELEWETPFQLLVAVILSAQTTDKAVNKITPGLWARYPEIEDLASANLDDVEMCLRTIGLYKNKAKNI 90
Cdd:COG0177    1 LERLKELYPDAKTELDYRDPFELLVATILSAQTTDERVNKATPRLFARYPTPEALAAADLEELEELIRPIGLYRNKAKNI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503756652  91 IKTARAVLMNFDGQVPKTRKELESLPGVGRKTANVVLAEVYGIPSIAVDTHVSRVSKRLNIAPEDaSVEEIEAELMKKIP 170
Cdd:COG0177   81 IALARILVEKYGGEVPETREELESLPGVGRKTANVVLNFAFGKPAIAVDTHVHRVSNRLGLVPGK-DPEEVEKDLMKLIP 159

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 503756652 171 KKDWIISHHRMIFFGRYHCLAKNPKCQTCPLQSYCKYYK 209
Cdd:COG0177  160 KEYWGDLHHLLILHGRYICKARKPKCEECPLADLCPYYG 198
 
Name Accession Description Interval E-value
Nth COG0177
Endonuclease III [Replication, recombination and repair];
11-209 2.59e-114

Endonuclease III [Replication, recombination and repair];


Pssm-ID: 439947 [Multi-domain]  Cd Length: 198  Bit Score: 324.36  E-value: 2.59e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503756652  11 LALMGEMFPNAHGELEWETPFQLLVAVILSAQTTDKAVNKITPGLWARYPEIEDLASANLDDVEMCLRTIGLYKNKAKNI 90
Cdd:COG0177    1 LERLKELYPDAKTELDYRDPFELLVATILSAQTTDERVNKATPRLFARYPTPEALAAADLEELEELIRPIGLYRNKAKNI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503756652  91 IKTARAVLMNFDGQVPKTRKELESLPGVGRKTANVVLAEVYGIPSIAVDTHVSRVSKRLNIAPEDaSVEEIEAELMKKIP 170
Cdd:COG0177   81 IALARILVEKYGGEVPETREELESLPGVGRKTANVVLNFAFGKPAIAVDTHVHRVSNRLGLVPGK-DPEEVEKDLMKLIP 159

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 503756652 171 KKDWIISHHRMIFFGRYHCLAKNPKCQTCPLQSYCKYYK 209
Cdd:COG0177  160 KEYWGDLHHLLILHGRYICKARKPKCEECPLADLCPYYG 198
nth TIGR01083
endonuclease III; This equivalog model identifes nth members of the pfam00730 superfamily ...
 4-196 3.14e-94

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: 273.10  E-value: 3.14e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503756652    4 RKRVNEALALMGEMFPNAHGELEWETPFQLLVAVILSAQTTDKAVNKITPGLWARYPEIEDLASANLDDVEMCLRTIGLY 83
Cdd:TIGR01083   1 RQKAQEILERLRKNYPHPTTELDFNNPFELLVATILSAQATDKRVNKATPKLFEVYPTPQALAQAGLEELEEYIKSIGLY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503756652   84 KNKAKNIIKTARAVLMNFDGQVPKTRKELESLPGVGRKTANVVLAEVYGIPSIAVDTHVSRVSKRLNIAPEDaSVEEIEA 163
Cdd:TIGR01083  81 RNKAKNIIELCRKLVERYGGEVPEDREELVKLPGVGRKTANVVLNVAFGIPAIAVDTHVFRVSNRLGLSKGK-DPIKVEE 159

                         170       180       190
                  ....*....|....*....|....*....|...
gi 503756652  164 ELMKKIPKKDWIISHHRMIFFGRYHCLAKNPKC 196
Cdd:TIGR01083 160 DLMKLVPREFWVKLHHWLILHGRYTCKARKPLC 192
PRK10702 PRK10702
endonuclease III; Provisional
 1-207 9.91e-61

endonuclease III; Provisional


Pssm-ID: 182661 [Multi-domain]  Cd Length: 211  Bit Score: 189.07  E-value: 9.91e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503756652   1 MLGRKRVnEALALMGEMFPNAHGELEWETPFQLLVAVILSAQTTDKAVNKITPGLWARYPEIEDLASANLDDVEMCLRTI 80
Cdd:PRK10702   1 MNKAKRL-EILTRLRDNNPHPTTELNFSSPFELLIAVLLSAQATDVSVNKATAKLYPVANTPAAMLELGVEGVKTYIKTI 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503756652  81 GLYKNKAKNIIKTARAVLMNFDGQVPKTRKELESLPGVGRKTANVVLAEVYGIPSIAVDTHVSRVSKRLNIAPeDASVEE 160
Cdd:PRK10702  80 GLYNSKAENVIKTCRILLEQHNGEVPEDRAALEALPGVGRKTANVVLNTAFGWPTIAVDTHIFRVCNRTQFAP-GKNVEQ 158

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 503756652 161 IEAELMKKIPKKDWIISHHRMIFFGRYHCLAKNPKCQTCPLQSYCKY 207
Cdd:PRK10702 159 VEEKLLKVVPAEFKVDCHHWLILHGRYTCIARKPRCGSCIIEDLCEY 205
ENDO3c cd00056
endonuclease III; includes endonuclease III (DNA-(apurinic or apyrimidinic site) lyase), ...
 31-185 5.28e-58

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: 180.13  E-value: 5.28e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503756652  31 FQLLVAVILSAQTTDKAVNKITPGLWARY-PEIEDLASANLDDVEMCLRTIGlYKNKAKNIIKTARAVLMNFDGQV---P 106
Cdd:cd00056    1 FEVLVSEILSQQTTDKAVNKAYERLFERYgPTPEALAAADEEELRELIRSLG-YRRKAKYLKELARAIVEGFGGLVlddP 79

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 503756652 107 KTRKELESLPGVGRKTANVVLAEVYGIPSIAVDTHVSRVSKRLNIAPEDASVEEIEAELMKKIPKKDWIISHHRMIFFG 185
Cdd:cd00056   80 DAREELLALPGVGRKTANVVLLFALGPDAFPVDTHVRRVLKRLGLIPKKKTPEELEELLEELLPKPYWGEANQALMDLG 158
ENDO3c smart00478
endonuclease III; includes endonuclease III (DNA-(apurinic or apyrimidinic site) lyase), ...
 39-187 2.36e-57

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: 178.23  E-value: 2.36e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503756652    39 LSAQTTDKAVNKITPGLWARYPEIEDLASANLDDVEMCLRTIGLYKNKAKNIIKTARAVLMNFDGQVPKTRKELESLPGV 118
Cdd:smart00478   1 LSQQTTDERVNKATERLFEKFPTPEDLAAADEEELEELIRGLGFYRRKARYLIELARILVEEYGGEVPDDREELLKLPGV 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 503756652   119 GRKTANVVLAEVYGIPSIAVDTHVSRVSKRLNIAPEDASVEEIEAELMKKIPKKDWIISHHRMIFFGRY 187
Cdd:smart00478  81 GRKTANAVLSFALGKPFIPVDTHVLRIAKRLGLVDKKSTPEEVEKLLEKLLPEEDWRELNLLLIDFGRT 149
HhH-GPD pfam00730
HhH-GPD superfamily base excision DNA repair protein; This family contains a diverse range of ...
 35-171 9.02e-45

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: 145.89  E-value: 9.02e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503756652   35 VAVILSAQTTDKAVNKITPGLWAR-YPEIEDLASANLDDVEMCLRTIGLYKNKAKNIIKTARAVLMNFDGQVPKTRKELE 113
Cdd:pfam00730   1 VSAILSQQTSDKAVNKITERLFEKfFPTPEDLADADEEELRELIRGLGFYRRKAKYLKELARILVEGYGGEVPLDEEELE 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 503756652  114 S-LPGVGRKTANVVLAEVYG--IPSIAVDTHVSRVSKRLNIAPEDASVEEIEAELMKKIPK 171
Cdd:pfam00730  81 AlLKGVGRWTAEAVLIFALGrpDPLPVVDTHVRRVLKRLGLIKEKPTPKEVERELEELWPP 141
 
Name Accession Description Interval E-value
Nth COG0177
Endonuclease III [Replication, recombination and repair];
11-209 2.59e-114

Endonuclease III [Replication, recombination and repair];


Pssm-ID: 439947 [Multi-domain]  Cd Length: 198  Bit Score: 324.36  E-value: 2.59e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503756652  11 LALMGEMFPNAHGELEWETPFQLLVAVILSAQTTDKAVNKITPGLWARYPEIEDLASANLDDVEMCLRTIGLYKNKAKNI 90
Cdd:COG0177    1 LERLKELYPDAKTELDYRDPFELLVATILSAQTTDERVNKATPRLFARYPTPEALAAADLEELEELIRPIGLYRNKAKNI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503756652  91 IKTARAVLMNFDGQVPKTRKELESLPGVGRKTANVVLAEVYGIPSIAVDTHVSRVSKRLNIAPEDaSVEEIEAELMKKIP 170
Cdd:COG0177   81 IALARILVEKYGGEVPETREELESLPGVGRKTANVVLNFAFGKPAIAVDTHVHRVSNRLGLVPGK-DPEEVEKDLMKLIP 159

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 503756652 171 KKDWIISHHRMIFFGRYHCLAKNPKCQTCPLQSYCKYYK 209
Cdd:COG0177  160 KEYWGDLHHLLILHGRYICKARKPKCEECPLADLCPYYG 198
nth TIGR01083
endonuclease III; This equivalog model identifes nth members of the pfam00730 superfamily ...
 4-196 3.14e-94

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: 273.10  E-value: 3.14e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503756652    4 RKRVNEALALMGEMFPNAHGELEWETPFQLLVAVILSAQTTDKAVNKITPGLWARYPEIEDLASANLDDVEMCLRTIGLY 83
Cdd:TIGR01083   1 RQKAQEILERLRKNYPHPTTELDFNNPFELLVATILSAQATDKRVNKATPKLFEVYPTPQALAQAGLEELEEYIKSIGLY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503756652   84 KNKAKNIIKTARAVLMNFDGQVPKTRKELESLPGVGRKTANVVLAEVYGIPSIAVDTHVSRVSKRLNIAPEDaSVEEIEA 163
Cdd:TIGR01083  81 RNKAKNIIELCRKLVERYGGEVPEDREELVKLPGVGRKTANVVLNVAFGIPAIAVDTHVFRVSNRLGLSKGK-DPIKVEE 159

                         170       180       190
                  ....*....|....*....|....*....|...
gi 503756652  164 ELMKKIPKKDWIISHHRMIFFGRYHCLAKNPKC 196
Cdd:TIGR01083 160 DLMKLVPREFWVKLHHWLILHGRYTCKARKPLC 192
PRK10702 PRK10702
endonuclease III; Provisional
 1-207 9.91e-61

endonuclease III; Provisional


Pssm-ID: 182661 [Multi-domain]  Cd Length: 211  Bit Score: 189.07  E-value: 9.91e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503756652   1 MLGRKRVnEALALMGEMFPNAHGELEWETPFQLLVAVILSAQTTDKAVNKITPGLWARYPEIEDLASANLDDVEMCLRTI 80
Cdd:PRK10702   1 MNKAKRL-EILTRLRDNNPHPTTELNFSSPFELLIAVLLSAQATDVSVNKATAKLYPVANTPAAMLELGVEGVKTYIKTI 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503756652  81 GLYKNKAKNIIKTARAVLMNFDGQVPKTRKELESLPGVGRKTANVVLAEVYGIPSIAVDTHVSRVSKRLNIAPeDASVEE 160
Cdd:PRK10702  80 GLYNSKAENVIKTCRILLEQHNGEVPEDRAALEALPGVGRKTANVVLNTAFGWPTIAVDTHIFRVCNRTQFAP-GKNVEQ 158

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 503756652 161 IEAELMKKIPKKDWIISHHRMIFFGRYHCLAKNPKCQTCPLQSYCKY 207
Cdd:PRK10702 159 VEEKLLKVVPAEFKVDCHHWLILHGRYTCIARKPRCGSCIIEDLCEY 205
ENDO3c cd00056
endonuclease III; includes endonuclease III (DNA-(apurinic or apyrimidinic site) lyase), ...
 31-185 5.28e-58

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: 180.13  E-value: 5.28e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503756652  31 FQLLVAVILSAQTTDKAVNKITPGLWARY-PEIEDLASANLDDVEMCLRTIGlYKNKAKNIIKTARAVLMNFDGQV---P 106
Cdd:cd00056    1 FEVLVSEILSQQTTDKAVNKAYERLFERYgPTPEALAAADEEELRELIRSLG-YRRKAKYLKELARAIVEGFGGLVlddP 79

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 503756652 107 KTRKELESLPGVGRKTANVVLAEVYGIPSIAVDTHVSRVSKRLNIAPEDASVEEIEAELMKKIPKKDWIISHHRMIFFG 185
Cdd:cd00056   80 DAREELLALPGVGRKTANVVLLFALGPDAFPVDTHVRRVLKRLGLIPKKKTPEELEELLEELLPKPYWGEANQALMDLG 158
ENDO3c smart00478
endonuclease III; includes endonuclease III (DNA-(apurinic or apyrimidinic site) lyase), ...
 39-187 2.36e-57

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: 178.23  E-value: 2.36e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503756652    39 LSAQTTDKAVNKITPGLWARYPEIEDLASANLDDVEMCLRTIGLYKNKAKNIIKTARAVLMNFDGQVPKTRKELESLPGV 118
Cdd:smart00478   1 LSQQTTDERVNKATERLFEKFPTPEDLAAADEEELEELIRGLGFYRRKARYLIELARILVEEYGGEVPDDREELLKLPGV 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 503756652   119 GRKTANVVLAEVYGIPSIAVDTHVSRVSKRLNIAPEDASVEEIEAELMKKIPKKDWIISHHRMIFFGRY 187
Cdd:smart00478  81 GRKTANAVLSFALGKPFIPVDTHVLRIAKRLGLVDKKSTPEEVEKLLEKLLPEEDWRELNLLLIDFGRT 149
HhH-GPD pfam00730
HhH-GPD superfamily base excision DNA repair protein; This family contains a diverse range of ...
 35-171 9.02e-45

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: 145.89  E-value: 9.02e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503756652   35 VAVILSAQTTDKAVNKITPGLWAR-YPEIEDLASANLDDVEMCLRTIGLYKNKAKNIIKTARAVLMNFDGQVPKTRKELE 113
Cdd:pfam00730   1 VSAILSQQTSDKAVNKITERLFEKfFPTPEDLADADEEELRELIRGLGFYRRKAKYLKELARILVEGYGGEVPLDEEELE 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 503756652  114 S-LPGVGRKTANVVLAEVYG--IPSIAVDTHVSRVSKRLNIAPEDASVEEIEAELMKKIPK 171
Cdd:pfam00730  81 AlLKGVGRWTAEAVLIFALGrpDPLPVVDTHVRRVLKRLGLIKEKPTPKEVERELEELWPP 141
mutY TIGR01084
A/G-specific adenine glycosylase; This equivalog model identifies mutY members of the ...
 25-212 8.79e-30

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: 111.35  E-value: 8.79e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503756652   25 LEW---ETPFQLLVAVILSAQTTDKAVNKITPGLWARYPEIEDLASANLDDVEMCLRTIGLYkNKAKNIIKTARAVLMNF 101
Cdd:TIGR01084  18 LPWrqnKTPYRVWLSEVMLQQTQVATVIPYFERFLERFPTVQALANAPQDEVLKLWEGLGYY-ARARNLHKAAQEVVEEF 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503756652  102 DGQVPKTRKELESLPGVGRKTANVVLAEVYGIPSIAVDTHVSRVSKRL---NIAPEDASVEEIEAELMKK-IPKKDWIIS 177
Cdd:TIGR01084  97 GGEFPQDFEDLAALPGVGRYTAGAILSFALNKPYPILDGNVKRVLSRLfavEGWPGKKKVENRLWTLAESlLPKADPEAF 176

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 503756652  178 HHRMIFFGRYHCLAKNPKCQTCPLQSYCKYYKETT 212
Cdd:TIGR01084 177 NQALMDLGAMICTRKKPKCDLCPLQDFCLAYQQGT 211
HP0602 COG2231
3-Methyladenine DNA glycosylase, HhH-GPD/Endo3 superfamily [Replication, recombination and ...
 21-210 8.32e-28

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


Pssm-ID: 441832 [Multi-domain]  Cd Length: 220  Bit Score: 104.54  E-value: 8.32e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503756652  21 AHGELEW---ETPFQLLVAVILSAQTT----DKAVNKITPglwARYPEIEDLASANLDDVEMCLRTIGLYKNKAKNIIKT 93
Cdd:COG2231   17 HYGPQHWwpaETPFEVIVGAILTQNTSwknvEKAIANLKE---AGLLDPEALAALDPEELAELIRPSGFYNQKAKRLKNL 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503756652  94 ARAVLMNFDGQVPKT--------RKELESLPGVGRKTANVVLAEVYGIPSIAVDTHVSRVSKRLNIAPEDASVEEIEAEL 165
Cdd:COG2231   94 ARWLVERYGGGLEKLkalpteelREELLSLKGIGPETADSILLYAFNRPVFVVDAYTRRIFSRLGLIEEDASYDELQRLF 173

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 503756652 166 MKKIPK-----KDWiishHRMIF-FGRYHCLaKNPKCQTCPLQSYCKYYKE 210
Cdd:COG2231  174 EENLPPdvalyNEF----HALIVeHGKEYCK-KKPKCEECPLRDLCPYGGQ 219
MutY COG1194
Adenine-specific DNA glycosylase, acts on AG and A-oxoG pairs [Replication, recombination and ...
 57-210 2.72e-25

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: 100.60  E-value: 2.72e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503756652  57 ARYPEIEDLASANLDDV----EmclrtiGL-YKNKAKNIIKTARAVLMNFDGQVPKTRKELESLPGVGRKTANVVLAEVY 131
Cdd:COG1194   56 ERFPTVEALAAAPEDEVlklwE------GLgYYSRARNLHKAAQQVVEEHGGVFPDTYEELLALPGIGPYTAAAIASIAF 129

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503756652 132 GIPSIAVDTHVSRVSKRL-NIaPEDASVEEIEAELMKKIpkkDWIISHHRM-IF------FGRYHCLAKNPKCQTCPLQS 203
Cdd:COG1194  130 GEPAPIVDGNVKRVLSRLfAI-EGPIGSPAAKKELWALA---EELLPPERPgDFnqalmdLGATVCTPKKPKCLLCPLQD 205


                 ....*..
gi 503756652 204 YCKYYKE 210
Cdd:COG1194  206 DCAAFAE 212
PRK10880 PRK10880
adenine DNA glycosylase;
25-208 3.93e-17

adenine DNA glycosylase;


Pssm-ID: 182805 [Multi-domain]  Cd Length: 350  Bit Score: 78.21  E-value: 3.93e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503756652  25 LEWE---TPFQLLVAVILSAQTTDKAVNKITPGLWARYPEIEDLASANLDDVeMCLRTiGL-YKNKAKNIIKTARAVLMN 100
Cdd:PRK10880  22 LPWQidkTPYKVWLSEVMLQQTQVATVIPYFERFMARFPTVTDLANAPLDEV-LHLWT-GLgYYARARNLHKAAQQVATL 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503756652 101 FDGQVPKTRKELESLPGVGRKTANVVLAEVYGIPSIAVDTHVSRVSKRLNIAPEDASVEEIEAELmkkipkkdWIISHHR 180
Cdd:PRK10880 100 HGGEFPETFEEVAALPGVGRSTAGAILSLSLGKHFPILDGNVKRVLARCYAVSGWPGKKEVENRL--------WQLSEQV 171

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 503756652 181 ------------MIFFGRYHCLAKNPKCQTCPLQSYCKYY 208
Cdd:PRK10880 172 tpavgverfnqaMMDLGAMVCTRSKPKCELCPLQNGCIAY 211
PRK13910 PRK13910
DNA glycosylase MutY; Provisional
 59-205 4.31e-14

DNA glycosylase MutY; Provisional


Pssm-ID: 172427 [Multi-domain]  Cd Length: 289  Bit Score: 69.28  E-value: 4.31e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503756652  59 YPEIEDLASANLDDVEMCLRTIGLYkNKAKNIIKTARAVLMNFDGQVPKTRKELESLPGVGRKTANVVLAEVYGIPSIAV 138
Cdd:PRK13910  22 FPTLKDLANAPLEEVLLLWRGLGYY-SRAKNLKKSAEICVKEHHSQLPNDYQSLLKLPGIGAYTANAILCFGFREKSACV 100

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 503756652 139 DTHVSRVSKRLNIAPEDASVEEIEAELMKKIPKKDWIISHHRMIFFGRYHCLAKnPKCQTCPLQSYC 205
Cdd:PRK13910 101 DANIKRVLLRLFGLDPNIHAKDLQIKANDFLNLNESFNHNQALIDLGALICSPK-PKCAICPLNPYC 166
AlkA COG0122
3-methyladenine DNA glycosylase/8-oxoguanine DNA glycosylase [Replication, recombination and ...
 28-163 1.64e-13

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


Pssm-ID: 439892 [Multi-domain]  Cd Length: 255  Bit Score: 67.22  E-value: 1.64e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503756652  28 ETPFQLLVAVILSAQTTDKAVNKIT--------------PGLWARYPEIEDLASANLDDvemcLRTIGLYKNKAKNIIKT 93
Cdd:COG0122   82 PDPFEALVRAILGQQVSVAAARTIWrrlvalfgepiegpGGGLYAFPTPEALAAASEEE----LRACGLSRRKARYLRAL 157

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503756652  94 ARAVLmnfDGQVPK----------TRKELESLPGVGRKTANVVLAEVYGIPSI--AVDTHVSRVSKRLNIAPEDASVEEI 161
Cdd:COG0122  158 ARAVA---DGELDLealaglddeeAIARLTALPGIGPWTAEMVLLFALGRPDAfpAGDLGLRRALGRLYGLGERPTPKEL 234


                 ..
gi 503756652 162 EA 163
Cdd:COG0122  235 RE 236
HHH pfam00633
Helix-hairpin-helix motif; The helix-hairpin-helix DNA-binding motif is found to be duplicated ...
 101-128 7.94e-08

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: 46.64  E-value: 7.94e-08
                          10        20
                  ....*....|....*....|....*...
gi 503756652  101 FDGQVPKTRKELESLPGVGRKTANVVLA 128
Cdd:pfam00633   2 LEGLIPASVEELLALPGVGPKTAEAILS 29
PRK13913 PRK13913
3-methyladenine DNA glycosylase; Provisional
 27-155 2.82e-06

3-methyladenine DNA glycosylase; Provisional


Pssm-ID: 184390  Cd Length: 218  Bit Score: 46.38  E-value: 2.82e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503756652  27 WET--PFQLLVAVILSAQTTDKAVNKITPGLWARY-------PEIEDLASANLDDVEMCLRTIGLYKNKAKNIIKTARAV 97
Cdd:PRK13913  25 WPNalKFEALLGAVLTQNTKFEAVEKSLENLKNAFilenddeINLKKIAYIEFSKLAECVRPSGFYNQKAKRLIDLSENI 104

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 503756652  98 LMNF-DGQVPK---TRKELESLPGVGRKTANVVLAEVYGIPSIAVDTHVSRVSKRLNIAPED 155
Cdd:PRK13913 105 LKDFgSFENFKqevTREWLLDQKGIGKESADAILCYVCAKEVMVVDKYSYLFLKKLGIEIED 166
PRK10308 PRK10308
3-methyl-adenine DNA glycosylase II; Provisional
 34-124 6.76e-06

3-methyl-adenine DNA glycosylase II; Provisional


Pssm-ID: 236671 [Multi-domain]  Cd Length: 283  Bit Score: 45.52  E-value: 6.76e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503756652  34 LVAVILSAQTTDKAVNKI------TPGlWARYPEIEDLASANlddvEMCLRTIGLYKNKAKNIIKTARAVLmnfDGQVPK 107
Cdd:PRK10308 125 LVSVAMAAKLTAKVAQLYgerlddFPE-YVCFPTPERLAAAD----PQALKALGMPLKRAEALIHLANAAL---EGTLPL 196

                         90       100
                 ....*....|....*....|....*
gi 503756652 108 TR--------KELESLPGVGRKTAN 124
Cdd:PRK10308 197 TIpgdveqamKTLQTFPGIGRWTAN 221
ogg TIGR00588
8-oxoguanine DNA-glycosylase (ogg); All proteins in this family for which functions are known ...
 59-148 6.77e-06

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: 45.67  E-value: 6.77e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503756652   59 YPEIEDLASAnldDVEMCLRTIGL-YKnkAKNIIKTARAVLMNFDG----------QVPKTRKELESLPGVGRKTANVVL 127
Cdd:TIGR00588 163 FPSLHALTGP---EAEAHLRKLGLgYR--ARYIRETARALLEEQGGrawlqqirgaSYEDAREALCELPGVGPKVADCIC 237

                          90       100
                  ....*....|....*....|..
gi 503756652  128 AEVYGIPSIA-VDTHVSRVSKR 148
Cdd:TIGR00588 238 LMGLDKPQAVpVDVHVWRIANR 259
EndIII_4Fe-2S pfam10576
Iron-sulfur binding domain of endonuclease III; Escherichia coli endonuclease III (EC 4.2.99. ...
 189-205 1.03e-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: 38.14  E-value: 1.03e-04
                          10
                  ....*....|....*..
gi 503756652  189 CLAKNPKCQTCPLQSYC 205
Cdd:pfam10576   1 CTARKPKCEECPLADLC 17
FES smart00525
iron-sulpphur binding domain in DNA-(apurinic or apyrimidinic site) lyase (subfamily of ENDO3); ...
 188-208 1.03e-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: 38.30  E-value: 1.03e-04
                           10        20
                   ....*....|....*....|.
gi 503756652   188 HCLAKNPKCQTCPLQSYCKYY 208
Cdd:smart00525   1 ICTARKPRCDECPLKDLCPAY 21
 
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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