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Conserved domains on  [gi|488475009|ref|WP_002518679|]
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MULTISPECIES: endonuclease III [Cutibacterium]

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];
28-224 8.67e-103

Endonuclease III [Replication, recombination and repair];


:

Pssm-ID: 439947 [Multi-domain]  Cd Length: 198  Bit Score: 296.24  E-value: 8.67e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488475009  28 ALLAKAYPDAHCELNYAGPYQLLVATVLSAQTTDRRVNTVTPTLFNRWPGPQALADADIGEVETVVAPLGCGPTRAARLV 107
Cdd:COG0177    2 ERLKELYPDAKTELDYRDPFELLVATILSAQTTDERVNKATPRLFARYPTPEALAAADLEELEELIRPIGLYRNKAKNII 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488475009 108 SMGAKLVDNFDGAIPDDLDSLVTLPGVGRKTANVVLGNAFGIPGITPDTHVMRVSRRLGWTDATTPAKVETDLAELFDPS 187
Cdd:COG0177   82 ALARILVEKYGGEVPETREELESLPGVGRKTANVVLNFAFGKPAIAVDTHVHRVSNRLGLVPGKDPEEVEKDLMKLIPKE 161

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 488475009 188 EWVMLCHRLIWHGRRRCHSRRPACGVCPVAEWCPSFG 224
Cdd:COG0177  162 YWGDLHHLLILHGRYICKARKPKCEECPLADLCPYYG 198
 
Name Accession Description Interval E-value
Nth COG0177
Endonuclease III [Replication, recombination and repair];
28-224 8.67e-103

Endonuclease III [Replication, recombination and repair];


Pssm-ID: 439947 [Multi-domain]  Cd Length: 198  Bit Score: 296.24  E-value: 8.67e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488475009  28 ALLAKAYPDAHCELNYAGPYQLLVATVLSAQTTDRRVNTVTPTLFNRWPGPQALADADIGEVETVVAPLGCGPTRAARLV 107
Cdd:COG0177    2 ERLKELYPDAKTELDYRDPFELLVATILSAQTTDERVNKATPRLFARYPTPEALAAADLEELEELIRPIGLYRNKAKNII 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488475009 108 SMGAKLVDNFDGAIPDDLDSLVTLPGVGRKTANVVLGNAFGIPGITPDTHVMRVSRRLGWTDATTPAKVETDLAELFDPS 187
Cdd:COG0177   82 ALARILVEKYGGEVPETREELESLPGVGRKTANVVLNFAFGKPAIAVDTHVHRVSNRLGLVPGKDPEEVEKDLMKLIPKE 161

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 488475009 188 EWVMLCHRLIWHGRRRCHSRRPACGVCPVAEWCPSFG 224
Cdd:COG0177  162 YWGDLHHLLILHGRYICKARKPKCEECPLADLCPYYG 198
nth TIGR01083
endonuclease III; This equivalog model identifes nth members of the pfam00730 superfamily ...
 20-211 2.35e-85

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: 251.92  E-value: 2.35e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488475009   20 RACANEVRALLAKAYPDAHCELNYAGPYQLLVATVLSAQTTDRRVNTVTPTLFNRWPGPQALADADIGEVETVVAPLGCG 99
Cdd:TIGR01083   1 RQKAQEILERLRKNYPHPTTELDFNNPFELLVATILSAQATDKRVNKATPKLFEVYPTPQALAQAGLEELEEYIKSIGLY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488475009  100 PTRAARLVSMGAKLVDNFDGAIPDDLDSLVTLPGVGRKTANVVLGNAFGIPGITPDTHVMRVSRRLGWTDATTPAKVETD 179
Cdd:TIGR01083  81 RNKAKNIIELCRKLVERYGGEVPEDREELVKLPGVGRKTANVVLNVAFGIPAIAVDTHVFRVSNRLGLSKGKDPIKVEED 160

                         170       180       190
                  ....*....|....*....|....*....|..
gi 488475009  180 LAELFDPSEWVMLCHRLIWHGRRRCHSRRPAC 211
Cdd:TIGR01083 161 LMKLVPREFWVKLHHWLILHGRYTCKARKPLC 192
ENDO3c smart00478
endonuclease III; includes endonuclease III (DNA-(apurinic or apyrimidinic site) lyase), ...
 55-202 2.54e-52

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: 166.29  E-value: 2.54e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488475009    55 LSAQTTDRRVNTVTPTLFNRWPGPQALADADIGEVETVVAPLGCGPTRAARLVSMGAKLVDNFDGAIPDDLDSLVTLPGV 134
Cdd:smart00478   1 LSQQTTDERVNKATERLFEKFPTPEDLAAADEEELEELIRGLGFYRRKARYLIELARILVEEYGGEVPDDREELLKLPGV 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488475009   135 GRKTANVVLGNAFGIPGITPDTHVMRVSRRLGWTDAT-TPAKVETDLAELFDPSEWVMLCHRLIWHGRR 202
Cdd:smart00478  81 GRKTANAVLSFALGKPFIPVDTHVLRIAKRLGLVDKKsTPEEVEKLLEKLLPEEDWRELNLLLIDFGRT 149
ENDO3c cd00056
endonuclease III; includes endonuclease III (DNA-(apurinic or apyrimidinic site) lyase), ...
 47-200 7.19e-49

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: 157.79  E-value: 7.19e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488475009  47 YQLLVATVLSAQTTDRRVNTVTPTLFNRW-PGPQALADADIGEVETVVAPLGcGPTRAARLVSMGAKLVDNFDGAI---P 122
Cdd:cd00056    1 FEVLVSEILSQQTTDKAVNKAYERLFERYgPTPEALAAADEEELRELIRSLG-YRRKAKYLKELARAIVEGFGGLVlddP 79

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488475009 123 DDLDSLVTLPGVGRKTANVVLGNAFGIPGITPDTHVMRVSRRLGW-TDATTPAKVETDLAELFDPSEWVMLCHRLIWHG 200
Cdd:cd00056   80 DAREELLALPGVGRKTANVVLLFALGPDAFPVDTHVRRVLKRLGLiPKKKTPEELEELLEELLPKPYWGEANQALMDLG 158
PRK10702 PRK10702
endonuclease III; Provisional
 25-225 2.63e-43

endonuclease III; Provisional


Pssm-ID: 182661 [Multi-domain]  Cd Length: 211  Bit Score: 145.54  E-value: 2.63e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488475009  25 EVRALLAKAYPDAHCELNYAGPYQLLVATVLSAQTTDRRVNTVTPTLFNRWPGPQALADADIGEVETVVAPLGCGPTRAA 104
Cdd:PRK10702   8 EILTRLRDNNPHPTTELNFSSPFELLIAVLLSAQATDVSVNKATAKLYPVANTPAAMLELGVEGVKTYIKTIGLYNSKAE 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488475009 105 RLVSMGAKLVDNFDGAIPDDLDSLVTLPGVGRKTANVVLGNAFGIPGITPDTHVMRVSRRLGWTDATTPAKVETDLAELF 184
Cdd:PRK10702  88 NVIKTCRILLEQHNGEVPEDRAALEALPGVGRKTANVVLNTAFGWPTIAVDTHIFRVCNRTQFAPGKNVEQVEEKLLKVV 167

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 488475009 185 dPSEWVMLCHR-LIWHGRRRCHSRRPACGVCPVAEWCpSFGE 225
Cdd:PRK10702 168 -PAEFKVDCHHwLILHGRYTCIARKPRCGSCIIEDLC-EYKE 207
HhH-GPD pfam00730
HhH-GPD superfamily base excision DNA repair protein; This family contains a diverse range of ...
 51-186 4.29e-38

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: 129.71  E-value: 4.29e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488475009   51 VATVLSAQTTDRRVNTVTPTLFNRW-PGPQALADADIGEVETVVAPLGCGPTRAARLVSMGAKLVDNFDGAIPDDLDSLV 129
Cdd:pfam00730   1 VSAILSQQTSDKAVNKITERLFEKFfPTPEDLADADEEELRELIRGLGFYRRKAKYLKELARILVEGYGGEVPLDEEELE 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488475009  130 T-LPGVGRKTANVVLGNAFGIPGITP--DTHVMRVSRRLGWTDAT-TPAKVETDLAELFDP 186
Cdd:pfam00730  81 AlLKGVGRWTAEAVLIFALGRPDPLPvvDTHVRRVLKRLGLIKEKpTPKEVERELEELWPP 141
 
Name Accession Description Interval E-value
Nth COG0177
Endonuclease III [Replication, recombination and repair];
28-224 8.67e-103

Endonuclease III [Replication, recombination and repair];


Pssm-ID: 439947 [Multi-domain]  Cd Length: 198  Bit Score: 296.24  E-value: 8.67e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488475009  28 ALLAKAYPDAHCELNYAGPYQLLVATVLSAQTTDRRVNTVTPTLFNRWPGPQALADADIGEVETVVAPLGCGPTRAARLV 107
Cdd:COG0177    2 ERLKELYPDAKTELDYRDPFELLVATILSAQTTDERVNKATPRLFARYPTPEALAAADLEELEELIRPIGLYRNKAKNII 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488475009 108 SMGAKLVDNFDGAIPDDLDSLVTLPGVGRKTANVVLGNAFGIPGITPDTHVMRVSRRLGWTDATTPAKVETDLAELFDPS 187
Cdd:COG0177   82 ALARILVEKYGGEVPETREELESLPGVGRKTANVVLNFAFGKPAIAVDTHVHRVSNRLGLVPGKDPEEVEKDLMKLIPKE 161

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 488475009 188 EWVMLCHRLIWHGRRRCHSRRPACGVCPVAEWCPSFG 224
Cdd:COG0177  162 YWGDLHHLLILHGRYICKARKPKCEECPLADLCPYYG 198
nth TIGR01083
endonuclease III; This equivalog model identifes nth members of the pfam00730 superfamily ...
 20-211 2.35e-85

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: 251.92  E-value: 2.35e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488475009   20 RACANEVRALLAKAYPDAHCELNYAGPYQLLVATVLSAQTTDRRVNTVTPTLFNRWPGPQALADADIGEVETVVAPLGCG 99
Cdd:TIGR01083   1 RQKAQEILERLRKNYPHPTTELDFNNPFELLVATILSAQATDKRVNKATPKLFEVYPTPQALAQAGLEELEEYIKSIGLY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488475009  100 PTRAARLVSMGAKLVDNFDGAIPDDLDSLVTLPGVGRKTANVVLGNAFGIPGITPDTHVMRVSRRLGWTDATTPAKVETD 179
Cdd:TIGR01083  81 RNKAKNIIELCRKLVERYGGEVPEDREELVKLPGVGRKTANVVLNVAFGIPAIAVDTHVFRVSNRLGLSKGKDPIKVEED 160

                         170       180       190
                  ....*....|....*....|....*....|..
gi 488475009  180 LAELFDPSEWVMLCHRLIWHGRRRCHSRRPAC 211
Cdd:TIGR01083 161 LMKLVPREFWVKLHHWLILHGRYTCKARKPLC 192
ENDO3c smart00478
endonuclease III; includes endonuclease III (DNA-(apurinic or apyrimidinic site) lyase), ...
 55-202 2.54e-52

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: 166.29  E-value: 2.54e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488475009    55 LSAQTTDRRVNTVTPTLFNRWPGPQALADADIGEVETVVAPLGCGPTRAARLVSMGAKLVDNFDGAIPDDLDSLVTLPGV 134
Cdd:smart00478   1 LSQQTTDERVNKATERLFEKFPTPEDLAAADEEELEELIRGLGFYRRKARYLIELARILVEEYGGEVPDDREELLKLPGV 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488475009   135 GRKTANVVLGNAFGIPGITPDTHVMRVSRRLGWTDAT-TPAKVETDLAELFDPSEWVMLCHRLIWHGRR 202
Cdd:smart00478  81 GRKTANAVLSFALGKPFIPVDTHVLRIAKRLGLVDKKsTPEEVEKLLEKLLPEEDWRELNLLLIDFGRT 149
ENDO3c cd00056
endonuclease III; includes endonuclease III (DNA-(apurinic or apyrimidinic site) lyase), ...
 47-200 7.19e-49

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: 157.79  E-value: 7.19e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488475009  47 YQLLVATVLSAQTTDRRVNTVTPTLFNRW-PGPQALADADIGEVETVVAPLGcGPTRAARLVSMGAKLVDNFDGAI---P 122
Cdd:cd00056    1 FEVLVSEILSQQTTDKAVNKAYERLFERYgPTPEALAAADEEELRELIRSLG-YRRKAKYLKELARAIVEGFGGLVlddP 79

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488475009 123 DDLDSLVTLPGVGRKTANVVLGNAFGIPGITPDTHVMRVSRRLGW-TDATTPAKVETDLAELFDPSEWVMLCHRLIWHG 200
Cdd:cd00056   80 DAREELLALPGVGRKTANVVLLFALGPDAFPVDTHVRRVLKRLGLiPKKKTPEELEELLEELLPKPYWGEANQALMDLG 158
PRK10702 PRK10702
endonuclease III; Provisional
 25-225 2.63e-43

endonuclease III; Provisional


Pssm-ID: 182661 [Multi-domain]  Cd Length: 211  Bit Score: 145.54  E-value: 2.63e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488475009  25 EVRALLAKAYPDAHCELNYAGPYQLLVATVLSAQTTDRRVNTVTPTLFNRWPGPQALADADIGEVETVVAPLGCGPTRAA 104
Cdd:PRK10702   8 EILTRLRDNNPHPTTELNFSSPFELLIAVLLSAQATDVSVNKATAKLYPVANTPAAMLELGVEGVKTYIKTIGLYNSKAE 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488475009 105 RLVSMGAKLVDNFDGAIPDDLDSLVTLPGVGRKTANVVLGNAFGIPGITPDTHVMRVSRRLGWTDATTPAKVETDLAELF 184
Cdd:PRK10702  88 NVIKTCRILLEQHNGEVPEDRAALEALPGVGRKTANVVLNTAFGWPTIAVDTHIFRVCNRTQFAPGKNVEQVEEKLLKVV 167

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 488475009 185 dPSEWVMLCHR-LIWHGRRRCHSRRPACGVCPVAEWCpSFGE 225
Cdd:PRK10702 168 -PAEFKVDCHHwLILHGRYTCIARKPRCGSCIIEDLC-EYKE 207
HhH-GPD pfam00730
HhH-GPD superfamily base excision DNA repair protein; This family contains a diverse range of ...
 51-186 4.29e-38

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: 129.71  E-value: 4.29e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488475009   51 VATVLSAQTTDRRVNTVTPTLFNRW-PGPQALADADIGEVETVVAPLGCGPTRAARLVSMGAKLVDNFDGAIPDDLDSLV 129
Cdd:pfam00730   1 VSAILSQQTSDKAVNKITERLFEKFfPTPEDLADADEEELRELIRGLGFYRRKAKYLKELARILVEGYGGEVPLDEEELE 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488475009  130 T-LPGVGRKTANVVLGNAFGIPGITP--DTHVMRVSRRLGWTDAT-TPAKVETDLAELFDP 186
Cdd:pfam00730  81 AlLKGVGRWTAEAVLIFALGRPDPLPvvDTHVRRVLKRLGLIKEKpTPKEVERELEELWPP 141
MutY COG1194
Adenine-specific DNA glycosylase, acts on AG and A-oxoG pairs [Replication, recombination and ...
 58-226 2.92e-17

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: 79.41  E-value: 2.92e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488475009  58 QTtdrRVNTVTPtLFNR----WPGPQALADADIGEVETVVAPLGcg-----ptRAARLVsmgaklVDNFDGAIPDDLDSL 128
Cdd:COG1194   41 QT---QVATVIP-YYERflerFPTVEALAAAPEDEVLKLWEGLGyysrarnlhKAAQQV------VEEHGGVFPDTYEEL 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488475009 129 VTLPGVGRKTANVVLGNAFGIPGITPDTHVMRV-SRRLGWTDATTPAKVE---TDLAELF----DPSEW---VM-Lchrl 196
Cdd:COG1194  111 LALPGIGPYTAAAIASIAFGEPAPIVDGNVKRVlSRLFAIEGPIGSPAAKkelWALAEELlppeRPGDFnqaLMdL---- 186

                        170       180       190
                 ....*....|....*....|....*....|
gi 488475009 197 iwhGRRRCHSRRPACGVCPVAEWCPSFGEG 226
Cdd:COG1194  187 ---GATVCTPKKPKCLLCPLQDDCAAFAEG 213
PRK10880 PRK10880
adenine DNA glycosylase;
46-224 3.51e-10

adenine DNA glycosylase;


Pssm-ID: 182805 [Multi-domain]  Cd Length: 350  Bit Score: 58.95  E-value: 3.51e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488475009  46 PYQLLVATVLSAQTtdrRVNTVTP---TLFNRWPGPQALADADIGEVETVVAPLGCgPTRAARLVSMGAKLVDNFDGAIP 122
Cdd:PRK10880  30 PYKVWLSEVMLQQT---QVATVIPyfeRFMARFPTVTDLANAPLDEVLHLWTGLGY-YARARNLHKAAQQVATLHGGEFP 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488475009 123 DDLDSLVTLPGVGRKTANVVLGNAFGIPGITPDTHVMRVSRRL----GWtdattPAK--VET---DLAELFDPSEWV--- 190
Cdd:PRK10880 106 ETFEEVAALPGVGRSTAGAILSLSLGKHFPILDGNVKRVLARCyavsGW-----PGKkeVENrlwQLSEQVTPAVGVerf 180

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 488475009 191 ---------MLCHRliwhgrrrchsRRPACGVCPVAEWCPSFG 224
Cdd:PRK10880 181 nqammdlgaMVCTR-----------SKPKCELCPLQNGCIAYA 212
HP0602 COG2231
3-Methyladenine DNA glycosylase, HhH-GPD/Endo3 superfamily [Replication, recombination and ...
 78-221 9.73e-09

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


Pssm-ID: 441832 [Multi-domain]  Cd Length: 220  Bit Score: 53.69  E-value: 9.73e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488475009  78 PQALADADIGEVETVVAPLGCGPTRAARLVSMGAKLVDNFDGAIP-------DDL-DSLVTLPGVGRKTANVVLGNAFGI 149
Cdd:COG2231   62 PEALAALDPEELAELIRPSGFYNQKAKRLKNLARWLVERYGGGLEklkalptEELrEELLSLKGIGPETADSILLYAFNR 141

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488475009 150 PGITPDTHVMRVSRRLGWTDATTP-----AKVETDL---AELFDpsEWvmlcHRLI-WHGRRRCHsRRPACGVCPVAEWC 220
Cdd:COG2231  142 PVFVVDAYTRRIFSRLGLIEEDASydelqRLFEENLppdVALYN--EF----HALIvEHGKEYCK-KKPKCEECPLRDLC 214


                 .
gi 488475009 221 P 221
Cdd:COG2231  215 P 215
PRK13910 PRK13910
DNA glycosylase MutY; Provisional
 55-220 9.29e-08

DNA glycosylase MutY; Provisional


Pssm-ID: 172427 [Multi-domain]  Cd Length: 289  Bit Score: 51.56  E-value: 9.29e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488475009  55 LSAQTtdrRVNTVTPTLF----NRWPGPQALADADIGEVETVVAPLGCgPTRAARLVSMGAKLVDNFDGAIPDDLDSLVT 130
Cdd:PRK13910   1 MSQQT---QINTVVERFYspflEAFPTLKDLANAPLEEVLLLWRGLGY-YSRAKNLKKSAEICVKEHHSQLPNDYQSLLK 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488475009 131 LPGVGRKTANVVLGNAFGIPGITPDTHVMRVSRRLGWTDATTPAK-VETDLAELFDPSEWVMLCHRLIWHGRRRChSRRP 209
Cdd:PRK13910  77 LPGIGAYTANAILCFGFREKSACVDANIKRVLLRLFGLDPNIHAKdLQIKANDFLNLNESFNHNQALIDLGALIC-SPKP 155

                        170
                 ....*....|.
gi 488475009 210 ACGVCPVAEWC 220
Cdd:PRK13910 156 KCAICPLNPYC 166
HHH pfam00633
Helix-hairpin-helix motif; The helix-hairpin-helix DNA-binding motif is found to be duplicated ...
 117-143 1.45e-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: 43.56  E-value: 1.45e-06
                          10        20
                  ....*....|....*....|....*..
gi 488475009  117 FDGAIPDDLDSLVTLPGVGRKTANVVL 143
Cdd:pfam00633   2 LEGLIPASVEELLALPGVGPKTAEAIL 28
ogg TIGR00588
8-oxoguanine DNA-glycosylase (ogg); All proteins in this family for which functions are known ...
 63-189 1.12e-05

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: 1.12e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488475009   63 RVNTVTPTLFNRWPGPQALADAdigEVETVVAPLGCGpTRAARLVSMGAKLVDNFDGAIP----------DDLDSLVTLP 132
Cdd:TIGR00588 151 RLITLDGVTYHGFPSLHALTGP---EAEAHLRKLGLG-YRARYIRETARALLEEQGGRAWlqqirgasyeDAREALCELP 226

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488475009  133 GVGRKTANVVLGNAFGIPGITP-DTHVMRVSRRL-GWTDATTPAKVETDLA--EL--FDPSEW 189
Cdd:TIGR00588 227 GVGPKVADCICLMGLDKPQAVPvDVHVWRIANRDyPWHPKTSRAKGPSPFArkELgnFFRSLW 289
AlkA COG0122
3-methyladenine DNA glycosylase/8-oxoguanine DNA glycosylase [Replication, recombination and ...
 46-186 4.67e-05

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


Pssm-ID: 439892 [Multi-domain]  Cd Length: 255  Bit Score: 43.33  E-value: 4.67e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488475009  46 PYQLLVATVLSAQTTDRRVNTVT--------------PTLFNRWPGPQALADADIGEVETvvapLGCGPTRAARLVSMGA 111
Cdd:COG0122   84 PFEALVRAILGQQVSVAAARTIWrrlvalfgepiegpGGGLYAFPTPEALAAASEEELRA----CGLSRRKARYLRALAR 159

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488475009 112 KLVD---NFDGAIPDDLD----SLVTLPGVGRKTANVVLGNAFGIPGITP--DTHVMR-VSRRLGWTDATTPAKVEtDLA 181
Cdd:COG0122  160 AVADgelDLEALAGLDDEeaiaRLTALPGIGPWTAEMVLLFALGRPDAFPagDLGLRRaLGRLYGLGERPTPKELR-ELA 238


                 ....*
gi 488475009 182 ELFDP 186
Cdd:COG0122  239 EPWRP 243
FES smart00525
iron-sulpphur binding domain in DNA-(apurinic or apyrimidinic site) lyase (subfamily of ENDO3); ...
 204-223 3.10e-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: 37.14  E-value: 3.10e-04
                           10        20
                   ....*....|....*....|
gi 488475009   204 CHSRRPACGVCPVAEWCPSF 223
Cdd:smart00525   2 CTARKPRCDECPLKDLCPAY 21
PRK10308 PRK10308
3-methyl-adenine DNA glycosylase II; Provisional
 50-140 8.38e-04

3-methyl-adenine DNA glycosylase II; Provisional


Pssm-ID: 236671 [Multi-domain]  Cd Length: 283  Bit Score: 39.74  E-value: 8.38e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488475009  50 LVATVLSAQTTDRRVNTVTPTL-----FNRWPGPQALADADIGEVETVVAPLgcgpTRAARLVSMG-AKLVDNFDGAIPD 123
Cdd:PRK10308 125 LVSVAMAAKLTAKVAQLYGERLddfpeYVCFPTPERLAAADPQALKALGMPL----KRAEALIHLAnAALEGTLPLTIPG 200

                         90       100
                 ....*....|....*....|.
gi 488475009 124 DLDS----LVTLPGVGRKTAN 140
Cdd:PRK10308 201 DVEQamktLQTFPGIGRWTAN 221
EndIII_4Fe-2S pfam10576
Iron-sulfur binding domain of endonuclease III; Escherichia coli endonuclease III (EC 4.2.99. ...
 204-220 4.14e-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: 33.90  E-value: 4.14e-03
                          10
                  ....*....|....*..
gi 488475009  204 CHSRRPACGVCPVAEWC 220
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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