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Conserved domains on  [gi|488377073|ref|WP_002446458|]
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MULTISPECIES: endonuclease III [Staphylococcus]

Protein Classification

endonuclease III domain-containing protein( domain architecture ID 11415064)

endonuclease III domain-containing protein such as endonuclease III, a DNA repair enzyme that has both DNA N-glycosylase and AP-lyase activities

CATH:  1.10.1670.10
Gene Ontology:  GO:0016798|GO:0006284|GO:0051539
PubMed:  10908318|1411536
SCOP:  4001141

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 4.66e-110

Endonuclease III [Replication, recombination and repair];


:

Pssm-ID: 439947 [Multi-domain]  Cd Length: 198  Bit Score: 313.57  E-value: 4.66e-110
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377073  11 IDVIADMFPNAECELNHRNAFDLTIAVLLSAQCTDNLVNRVTQSLFRKYRTPEDYLNVSDEELQNDIRSIGLYRNKAKNI 90
Cdd:COG0177    1 LERLKELYPDAKTELDYRDPFELLVATILSAQTTDERVNKATPRLFARYPTPEALAAADLEELEELIRPIGLYRNKAKNI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377073  91 KKLCHSLIEQFNGQIPQTHKELESLAGVGRKTANVVMSVAFGEPSLAVDTHVERVSKRLGINRWKDnVRQVEDRLCDIIP 170
Cdd:COG0177   81 IALARILVEKYGGEVPETREELESLPGVGRKTANVVLNFAFGKPAIAVDTHVHRVSNRLGLVPGKD-PEEVEKDLMKLIP 159

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 488377073 171 RDRWNKSHHQLIFFGRYHCLARKPKCEICPLLNDCREGQ 209
Cdd:COG0177  160 KEYWGDLHHLLILHGRYICKARKPKCEECPLADLCPYYG 198
 
Name Accession Description Interval E-value
Nth COG0177
Endonuclease III [Replication, recombination and repair];
11-209 4.66e-110

Endonuclease III [Replication, recombination and repair];


Pssm-ID: 439947 [Multi-domain]  Cd Length: 198  Bit Score: 313.57  E-value: 4.66e-110
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377073  11 IDVIADMFPNAECELNHRNAFDLTIAVLLSAQCTDNLVNRVTQSLFRKYRTPEDYLNVSDEELQNDIRSIGLYRNKAKNI 90
Cdd:COG0177    1 LERLKELYPDAKTELDYRDPFELLVATILSAQTTDERVNKATPRLFARYPTPEALAAADLEELEELIRPIGLYRNKAKNI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377073  91 KKLCHSLIEQFNGQIPQTHKELESLAGVGRKTANVVMSVAFGEPSLAVDTHVERVSKRLGINRWKDnVRQVEDRLCDIIP 170
Cdd:COG0177   81 IALARILVEKYGGEVPETREELESLPGVGRKTANVVLNFAFGKPAIAVDTHVHRVSNRLGLVPGKD-PEEVEKDLMKLIP 159

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 488377073 171 RDRWNKSHHQLIFFGRYHCLARKPKCEICPLLNDCREGQ 209
Cdd:COG0177  160 KEYWGDLHHLLILHGRYICKARKPKCEECPLADLCPYYG 198
nth TIGR01083
endonuclease III; This equivalog model identifes nth members of the pfam00730 superfamily ...
 4-196 4.17e-98

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: 283.12  E-value: 4.17e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377073    4 KKKALQMIDVIADMFPNAECELNHRNAFDLTIAVLLSAQCTDNLVNRVTQSLFRKYRTPEDYLNVSDEELQNDIRSIGLY 83
Cdd:TIGR01083   1 RQKAQEILERLRKNYPHPTTELDFNNPFELLVATILSAQATDKRVNKATPKLFEVYPTPQALAQAGLEELEEYIKSIGLY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377073   84 RNKAKNIKKLCHSLIEQFNGQIPQTHKELESLAGVGRKTANVVMSVAFGEPSLAVDTHVERVSKRLGINRWKDnVRQVED 163
Cdd:TIGR01083  81 RNKAKNIIELCRKLVERYGGEVPEDREELVKLPGVGRKTANVVLNVAFGIPAIAVDTHVFRVSNRLGLSKGKD-PIKVEE 159

                         170       180       190
                  ....*....|....*....|....*....|...
gi 488377073  164 RLCDIIPRDRWNKSHHQLIFFGRYHCLARKPKC 196
Cdd:TIGR01083 160 DLMKLVPREFWVKLHHWLILHGRYTCKARKPLC 192
PRK10702 PRK10702
endonuclease III; Provisional
 2-210 8.36e-61

endonuclease III; Provisional


Pssm-ID: 182661 [Multi-domain]  Cd Length: 211  Bit Score: 189.46  E-value: 8.36e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377073   2 ISKKKALQMIDVIADMFPNAECELNHRNAFDLTIAVLLSAQCTDNLVNRVTQSLFRKYRTPEDYLNVSDEELQNDIRSIG 81
Cdd:PRK10702   1 MNKAKRLEILTRLRDNNPHPTTELNFSSPFELLIAVLLSAQATDVSVNKATAKLYPVANTPAAMLELGVEGVKTYIKTIG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377073  82 LYRNKAKNIKKLCHSLIEQFNGQIPQTHKELESLAGVGRKTANVVMSVAFGEPSLAVDTHVERVSKRLGINRWKdNVRQV 161
Cdd:PRK10702  81 LYNSKAENVIKTCRILLEQHNGEVPEDRAALEALPGVGRKTANVVLNTAFGWPTIAVDTHIFRVCNRTQFAPGK-NVEQV 159

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 488377073 162 EDRLCDIIPRDRWNKSHHQLIFFGRYHCLARKPKCEICPLLNDCREGQK 210
Cdd:PRK10702 160 EEKLLKVVPAEFKVDCHHWLILHGRYTCIARKPRCGSCIIEDLCEYKEK 208
ENDO3c smart00478
endonuclease III; includes endonuclease III (DNA-(apurinic or apyrimidinic site) lyase), ...
 39-187 3.83e-54

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: 170.14  E-value: 3.83e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377073    39 LSAQCTDNLVNRVTQSLFRKYRTPEDYLNVSDEELQNDIRSIGLYRNKAKNIKKLCHSLIEQFNGQIPQTHKELESLAGV 118
Cdd:smart00478   1 LSQQTTDERVNKATERLFEKFPTPEDLAAADEEELEELIRGLGFYRRKARYLIELARILVEEYGGEVPDDREELLKLPGV 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488377073   119 GRKTANVVMSVAFGEPSLAVDTHVERVSKRLGINRWKDNVRQVEDRLCDIIPRDRWNKSHHQLIFFGRY 187
Cdd:smart00478  81 GRKTANAVLSFALGKPFIPVDTHVLRIAKRLGLVDKKSTPEEVEKLLEKLLPEEDWRELNLLLIDFGRT 149
ENDO3c cd00056
endonuclease III; includes endonuclease III (DNA-(apurinic or apyrimidinic site) lyase), ...
 31-185 3.86e-54

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: 170.50  E-value: 3.86e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377073  31 FDLTIAVLLSAQCTDNLVNRVTQSLFRKYR-TPEDYLNVSDEELQNDIRSIGlYRNKAKNIKKLCHSLIEQFNGQI---P 106
Cdd:cd00056    1 FEVLVSEILSQQTTDKAVNKAYERLFERYGpTPEALAAADEEELRELIRSLG-YRRKAKYLKELARAIVEGFGGLVlddP 79

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488377073 107 QTHKELESLAGVGRKTANVVMSVAFGEPSLAVDTHVERVSKRLGINRWKDNVRQVEDRLCDIIPRDRWNKSHHQLIFFG 185
Cdd:cd00056   80 DAREELLALPGVGRKTANVVLLFALGPDAFPVDTHVRRVLKRLGLIPKKKTPEELEELLEELLPKPYWGEANQALMDLG 158
HhH-GPD pfam00730
HhH-GPD superfamily base excision DNA repair protein; This family contains a diverse range of ...
 35-171 6.18e-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: 138.96  E-value: 6.18e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377073   35 IAVLLSAQCTDNLVNRVTQSLFRK-YRTPEDYLNVSDEELQNDIRSIGLYRNKAKNIKKLCHSLIEQFNGQIPQTHKELE 113
Cdd:pfam00730   1 VSAILSQQTSDKAVNKITERLFEKfFPTPEDLADADEEELRELIRGLGFYRRKAKYLKELARILVEGYGGEVPLDEEELE 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488377073  114 S-LAGVGRKTANVVMSVAFG--EPSLAVDTHVERVSKRLGINRWKDNVRQVEDRLCDIIPR 171
Cdd:pfam00730  81 AlLKGVGRWTAEAVLIFALGrpDPLPVVDTHVRRVLKRLGLIKEKPTPKEVERELEELWPP 141
 
Name Accession Description Interval E-value
Nth COG0177
Endonuclease III [Replication, recombination and repair];
11-209 4.66e-110

Endonuclease III [Replication, recombination and repair];


Pssm-ID: 439947 [Multi-domain]  Cd Length: 198  Bit Score: 313.57  E-value: 4.66e-110
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377073  11 IDVIADMFPNAECELNHRNAFDLTIAVLLSAQCTDNLVNRVTQSLFRKYRTPEDYLNVSDEELQNDIRSIGLYRNKAKNI 90
Cdd:COG0177    1 LERLKELYPDAKTELDYRDPFELLVATILSAQTTDERVNKATPRLFARYPTPEALAAADLEELEELIRPIGLYRNKAKNI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377073  91 KKLCHSLIEQFNGQIPQTHKELESLAGVGRKTANVVMSVAFGEPSLAVDTHVERVSKRLGINRWKDnVRQVEDRLCDIIP 170
Cdd:COG0177   81 IALARILVEKYGGEVPETREELESLPGVGRKTANVVLNFAFGKPAIAVDTHVHRVSNRLGLVPGKD-PEEVEKDLMKLIP 159

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 488377073 171 RDRWNKSHHQLIFFGRYHCLARKPKCEICPLLNDCREGQ 209
Cdd:COG0177  160 KEYWGDLHHLLILHGRYICKARKPKCEECPLADLCPYYG 198
nth TIGR01083
endonuclease III; This equivalog model identifes nth members of the pfam00730 superfamily ...
 4-196 4.17e-98

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: 283.12  E-value: 4.17e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377073    4 KKKALQMIDVIADMFPNAECELNHRNAFDLTIAVLLSAQCTDNLVNRVTQSLFRKYRTPEDYLNVSDEELQNDIRSIGLY 83
Cdd:TIGR01083   1 RQKAQEILERLRKNYPHPTTELDFNNPFELLVATILSAQATDKRVNKATPKLFEVYPTPQALAQAGLEELEEYIKSIGLY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377073   84 RNKAKNIKKLCHSLIEQFNGQIPQTHKELESLAGVGRKTANVVMSVAFGEPSLAVDTHVERVSKRLGINRWKDnVRQVED 163
Cdd:TIGR01083  81 RNKAKNIIELCRKLVERYGGEVPEDREELVKLPGVGRKTANVVLNVAFGIPAIAVDTHVFRVSNRLGLSKGKD-PIKVEE 159

                         170       180       190
                  ....*....|....*....|....*....|...
gi 488377073  164 RLCDIIPRDRWNKSHHQLIFFGRYHCLARKPKC 196
Cdd:TIGR01083 160 DLMKLVPREFWVKLHHWLILHGRYTCKARKPLC 192
PRK10702 PRK10702
endonuclease III; Provisional
 2-210 8.36e-61

endonuclease III; Provisional


Pssm-ID: 182661 [Multi-domain]  Cd Length: 211  Bit Score: 189.46  E-value: 8.36e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377073   2 ISKKKALQMIDVIADMFPNAECELNHRNAFDLTIAVLLSAQCTDNLVNRVTQSLFRKYRTPEDYLNVSDEELQNDIRSIG 81
Cdd:PRK10702   1 MNKAKRLEILTRLRDNNPHPTTELNFSSPFELLIAVLLSAQATDVSVNKATAKLYPVANTPAAMLELGVEGVKTYIKTIG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377073  82 LYRNKAKNIKKLCHSLIEQFNGQIPQTHKELESLAGVGRKTANVVMSVAFGEPSLAVDTHVERVSKRLGINRWKdNVRQV 161
Cdd:PRK10702  81 LYNSKAENVIKTCRILLEQHNGEVPEDRAALEALPGVGRKTANVVLNTAFGWPTIAVDTHIFRVCNRTQFAPGK-NVEQV 159

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 488377073 162 EDRLCDIIPRDRWNKSHHQLIFFGRYHCLARKPKCEICPLLNDCREGQK 210
Cdd:PRK10702 160 EEKLLKVVPAEFKVDCHHWLILHGRYTCIARKPRCGSCIIEDLCEYKEK 208
ENDO3c smart00478
endonuclease III; includes endonuclease III (DNA-(apurinic or apyrimidinic site) lyase), ...
 39-187 3.83e-54

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: 170.14  E-value: 3.83e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377073    39 LSAQCTDNLVNRVTQSLFRKYRTPEDYLNVSDEELQNDIRSIGLYRNKAKNIKKLCHSLIEQFNGQIPQTHKELESLAGV 118
Cdd:smart00478   1 LSQQTTDERVNKATERLFEKFPTPEDLAAADEEELEELIRGLGFYRRKARYLIELARILVEEYGGEVPDDREELLKLPGV 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488377073   119 GRKTANVVMSVAFGEPSLAVDTHVERVSKRLGINRWKDNVRQVEDRLCDIIPRDRWNKSHHQLIFFGRY 187
Cdd:smart00478  81 GRKTANAVLSFALGKPFIPVDTHVLRIAKRLGLVDKKSTPEEVEKLLEKLLPEEDWRELNLLLIDFGRT 149
ENDO3c cd00056
endonuclease III; includes endonuclease III (DNA-(apurinic or apyrimidinic site) lyase), ...
 31-185 3.86e-54

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: 170.50  E-value: 3.86e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377073  31 FDLTIAVLLSAQCTDNLVNRVTQSLFRKYR-TPEDYLNVSDEELQNDIRSIGlYRNKAKNIKKLCHSLIEQFNGQI---P 106
Cdd:cd00056    1 FEVLVSEILSQQTTDKAVNKAYERLFERYGpTPEALAAADEEELRELIRSLG-YRRKAKYLKELARAIVEGFGGLVlddP 79

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488377073 107 QTHKELESLAGVGRKTANVVMSVAFGEPSLAVDTHVERVSKRLGINRWKDNVRQVEDRLCDIIPRDRWNKSHHQLIFFG 185
Cdd:cd00056   80 DAREELLALPGVGRKTANVVLLFALGPDAFPVDTHVRRVLKRLGLIPKKKTPEELEELLEELLPKPYWGEANQALMDLG 158
HhH-GPD pfam00730
HhH-GPD superfamily base excision DNA repair protein; This family contains a diverse range of ...
 35-171 6.18e-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: 138.96  E-value: 6.18e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377073   35 IAVLLSAQCTDNLVNRVTQSLFRK-YRTPEDYLNVSDEELQNDIRSIGLYRNKAKNIKKLCHSLIEQFNGQIPQTHKELE 113
Cdd:pfam00730   1 VSAILSQQTSDKAVNKITERLFEKfFPTPEDLADADEEELRELIRGLGFYRRKAKYLKELARILVEGYGGEVPLDEEELE 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488377073  114 S-LAGVGRKTANVVMSVAFG--EPSLAVDTHVERVSKRLGINRWKDNVRQVEDRLCDIIPR 171
Cdd:pfam00730  81 AlLKGVGRWTAEAVLIFALGrpDPLPVVDTHVRRVLKRLGLIKEKPTPKEVERELEELWPP 141
HP0602 COG2231
3-Methyladenine DNA glycosylase, HhH-GPD/Endo3 superfamily [Replication, recombination and ...
 61-209 7.06e-25

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


Pssm-ID: 441832 [Multi-domain]  Cd Length: 220  Bit Score: 97.22  E-value: 7.06e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377073  61 TPEDYLNVSDEELQNDIRSIGLYRNKAKNIKKLCHSLIEQFNGQI--------PQTHKELESLAGVGRKTANVVMSVAFG 132
Cdd:COG2231   61 DPEALAALDPEELAELIRPSGFYNQKAKRLKNLARWLVERYGGGLeklkalptEELREELLSLKGIGPETADSILLYAFN 140

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488377073 133 EPSLAVDTHVERVSKRLGINRWKDNVRQVEDRLCDIIPRD--RWNKSHHQLIFFGRYHCLArKPKCEICPLLNDCREGQ 209
Cdd:COG2231  141 RPVFVVDAYTRRIFSRLGLIEEDASYDELQRLFEENLPPDvaLYNEFHALIVEHGKEYCKK-KPKCEECPLRDLCPYGG 218
MutY COG1194
Adenine-specific DNA glycosylase, acts on AG and A-oxoG pairs [Replication, recombination and ...
 87-218 1.05e-22

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: 94.05  E-value: 1.05e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377073  87 AKNIKKLCHSLIEQFNGQIPQTHKELESLAGVGRKTANVVMSVAFGEPSLAVDTHVERVSKRL-GINRW---KDNVRQVE 162
Cdd:COG1194   85 ARNLHKAAQQVVEEHGGVFPDTYEELLALPGIGPYTAAAIASIAFGEPAPIVDGNVKRVLSRLfAIEGPigsPAAKKELW 164

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488377073 163 DRLCDIIPRDR---WNkshhQLIF-FGRYHCLARKPKCEICPLLNDC---REGQ------KRHKAKIKE 218
Cdd:COG1194  165 ALAEELLPPERpgdFN----QALMdLGATVCTPKKPKCLLCPLQDDCaafAEGRqeelpvKKPKKKKPE 229
mutY TIGR01084
A/G-specific adenine glycosylase; This equivalog model identifies mutY members of the ...
 81-205 6.85e-22

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: 90.55  E-value: 6.85e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377073   81 GL-YRNKAKNIKKLCHSLIEQFNGQIPQTHKELESLAGVGRKTANVVMSVAFGEPSLAVDTHVERVSKRL-GINRWKDNv 158
Cdd:TIGR01084  75 GLgYYARARNLHKAAQEVVEEFGGEFPQDFEDLAALPGVGRYTAGAILSFALNKPYPILDGNVKRVLSRLfAVEGWPGK- 153

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 488377073  159 RQVEDRLCDIIPR-------DRWNKShhqLIFFGRYHCLARKPKCEICPLLNDC 205
Cdd:TIGR01084 154 KKVENRLWTLAESllpkadpEAFNQA---LMDLGAMICTRKKPKCDLCPLQDFC 204
PRK10880 PRK10880
adenine DNA glycosylase;
81-205 1.40e-16

adenine DNA glycosylase;


Pssm-ID: 182805 [Multi-domain]  Cd Length: 350  Bit Score: 77.06  E-value: 1.40e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377073  81 GL-YRNKAKNIKKLCHSLIEQFNGQIPQTHKELESLAGVGRKTANVVMSVAFGEPSLAVDTHVERVSKR-LGINRWKdNV 158
Cdd:PRK10880  79 GLgYYARARNLHKAAQQVATLHGGEFPETFEEVAALPGVGRSTAGAILSLSLGKHFPILDGNVKRVLARcYAVSGWP-GK 157

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 488377073 159 RQVEDRLCDIIPR-------DRWNKSHHQLiffGRYHCLARKPKCEICPLLNDC 205
Cdd:PRK10880 158 KEVENRLWQLSEQvtpavgvERFNQAMMDL---GAMVCTRSKPKCELCPLQNGC 208
PRK13910 PRK13910
DNA glycosylase MutY; Provisional
 45-218 5.80e-12

DNA glycosylase MutY; Provisional


Pssm-ID: 172427 [Multi-domain]  Cd Length: 289  Bit Score: 63.50  E-value: 5.80e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377073  45 DNLVNRVTQSLFRKYRTPEDYLNVSDEELQNDIRSIGLYrNKAKNIKKLCHSLIEQFNGQIPQTHKELESLAGVGRKTAN 124
Cdd:PRK13910   8 NTVVERFYSPFLEAFPTLKDLANAPLEEVLLLWRGLGYY-SRAKNLKKSAEICVKEHHSQLPNDYQSLLKLPGIGAYTAN 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377073 125 VVMSVAFGEPSLAVDTHVERVSKRLGINRWKDNVRQVEDRLCDIIPRDRWNKSHHQLIFFGRYHClARKPKCEICPLLND 204
Cdd:PRK13910  87 AILCFGFREKSACVDANIKRVLLRLFGLDPNIHAKDLQIKANDFLNLNESFNHNQALIDLGALIC-SPKPKCAICPLNPY 165

                        170
                 ....*....|....*.
gi 488377073 205 C--REGQKRHKAKIKE 218
Cdd:PRK13910 166 ClgKNNPEKHTLKKKQ 181
AlkA COG0122
3-methyladenine DNA glycosylase/8-oxoguanine DNA glycosylase [Replication, recombination and ...
 61-149 2.29e-07

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


Pssm-ID: 439892 [Multi-domain]  Cd Length: 255  Bit Score: 49.88  E-value: 2.29e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377073  61 TPEDYLNVSDEELqndiRSIGLYRNKAKNIKKLCHSLIEqfnGQIP----------QTHKELESLAGVGRKTANVVMSVA 130
Cdd:COG0122  129 TPEALAAASEEEL----RACGLSRRKARYLRALARAVAD---GELDlealaglddeEAIARLTALPGIGPWTAEMVLLFA 201

                         90       100
                 ....*....|....*....|.
gi 488377073 131 FGEPS--LAVDTHVERVSKRL 149
Cdd:COG0122  202 LGRPDafPAGDLGLRRALGRL 222
HHH pfam00633
Helix-hairpin-helix motif; The helix-hairpin-helix DNA-binding motif is found to be duplicated ...
 101-129 2.17e-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: 42.79  E-value: 2.17e-06
                          10        20
                  ....*....|....*....|....*....
gi 488377073  101 FNGQIPQTHKELESLAGVGRKTANVVMSV 129
Cdd:pfam00633   2 LEGLIPASVEELLALPGVGPKTAEAILSY 30
PRK13913 PRK13913
3-methyladenine DNA glycosylase; Provisional
 73-151 6.42e-05

3-methyladenine DNA glycosylase; Provisional


Pssm-ID: 184390  Cd Length: 218  Bit Score: 42.53  E-value: 6.42e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377073  73 LQNDIRSIGLYRNKAKNIKKLCHSLIEQFngQIPQTHKE------LESLAGVGRKTANVVMSVAFGEPSLAVDTHVERVS 146
Cdd:PRK13913  80 LAECVRPSGFYNQKAKRLIDLSENILKDF--GSFENFKQevtrewLLDQKGIGKESADAILCYVCAKEVMVVDKYSYLFL 157


                 ....*
gi 488377073 147 KRLGI 151
Cdd:PRK13913 158 KKLGI 162
EndIII_4Fe-2S pfam10576
Iron-sulfur binding domain of endonuclease III; Escherichia coli endonuclease III (EC 4.2.99. ...
 189-205 3.37e-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: 36.60  E-value: 3.37e-04
                          10
                  ....*....|....*..
gi 488377073  189 CLARKPKCEICPLLNDC 205
Cdd:pfam10576   1 CTARKPKCEECPLADLC 17
ogg TIGR00588
8-oxoguanine DNA-glycosylase (ogg); All proteins in this family for which functions are known ...
 46-148 7.99e-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: 39.51  E-value: 7.99e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377073   46 NLVNRVTQSLFRKYRTPEDylnVSDEELQNDIRSIGL-YRnkAKNIKKLCHSLIEQFNG----------QIPQTHKELES 114
Cdd:TIGR00588 150 PRLITLDGVTYHGFPSLHA---LTGPEAEAHLRKLGLgYR--ARYIRETARALLEEQGGrawlqqirgaSYEDAREALCE 224

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 488377073  115 LAGVGRKTANVVMSVAFGEP-SLAVDTHVERVSKR 148
Cdd:TIGR00588 225 LPGVGPKVADCICLMGLDKPqAVPVDVHVWRIANR 259
FES smart00525
iron-sulpphur binding domain in DNA-(apurinic or apyrimidinic site) lyase (subfamily of ENDO3); ...
 188-206 2.00e-03

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


Pssm-ID: 197771 [Multi-domain]  Cd Length: 21  Bit Score: 34.45  E-value: 2.00e-03
                           10
                   ....*....|....*....
gi 488377073   188 HCLARKPKCEICPLLNDCR 206
Cdd:smart00525   1 ICTARKPRCDECPLKDLCP 19
 
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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