NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1175203548|ref|WP_081751455|]
View 

endonuclease III [Corynebacterium vitaeruminis]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
Nth COG0177
Endonuclease III [Replication, recombination and repair];
54-244 5.24e-110

Endonuclease III [Replication, recombination and repair];


:

Pssm-ID: 439947 [Multi-domain]  Cd Length: 198  Bit Score: 316.65  E-value: 5.24e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1175203548  54 YPDAHCELDFTNTLELVVATVLSAQCTDVRVNQVTPALFARYRTAEDYATADEAELQEIIRPTGFYKAKAGHLIGMGRLL 133
Cdd:COG0177     8 YPDAKTELDYRDPFELLVATILSAQTTDERVNKATPRLFARYPTPEALAAADLEELEELIRPIGLYRNKAKNIIALARIL 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1175203548 134 VTDYGGEVPSALEDLVRLPGVGRKTAHVVRGNAFGIPGLTVDTHFGRLVRRLKLTEEEDPVKVERVLAKLIEKKEWTMFS 213
Cdd:COG0177    88 VEKYGGEVPETREELESLPGVGRKTANVVLNFAFGKPAIAVDTHVHRVSNRLGLVPGKDPEEVEKDLMKLIPKEYWGDLH 167
                         170       180       190
                  ....*....|....*....|....*....|.
gi 1175203548 214 HRIIFHGRRVCHARKPACGACFLAPECPSFG 244
Cdd:COG0177   168 HLLILHGRYICKARKPKCEECPLADLCPYYG 198
 
Name Accession Description Interval E-value
Nth COG0177
Endonuclease III [Replication, recombination and repair];
54-244 5.24e-110

Endonuclease III [Replication, recombination and repair];


Pssm-ID: 439947 [Multi-domain]  Cd Length: 198  Bit Score: 316.65  E-value: 5.24e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1175203548  54 YPDAHCELDFTNTLELVVATVLSAQCTDVRVNQVTPALFARYRTAEDYATADEAELQEIIRPTGFYKAKAGHLIGMGRLL 133
Cdd:COG0177     8 YPDAKTELDYRDPFELLVATILSAQTTDERVNKATPRLFARYPTPEALAAADLEELEELIRPIGLYRNKAKNIIALARIL 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1175203548 134 VTDYGGEVPSALEDLVRLPGVGRKTAHVVRGNAFGIPGLTVDTHFGRLVRRLKLTEEEDPVKVERVLAKLIEKKEWTMFS 213
Cdd:COG0177    88 VEKYGGEVPETREELESLPGVGRKTANVVLNFAFGKPAIAVDTHVHRVSNRLGLVPGKDPEEVEKDLMKLIPKEYWGDLH 167
                         170       180       190
                  ....*....|....*....|....*....|.
gi 1175203548 214 HRIIFHGRRVCHARKPACGACFLAPECPSFG 244
Cdd:COG0177   168 HLLILHGRYICKARKPKCEECPLADLCPYYG 198
nth TIGR01083
endonuclease III; This equivalog model identifes nth members of the pfam00730 superfamily ...
54-231 8.69e-95

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: 277.72  E-value: 8.69e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1175203548  54 YPDAHCELDFTNTLELVVATVLSAQCTDVRVNQVTPALFARYRTAEDYATADEAELQEIIRPTGFYKAKAGHLIGMGRLL 133
Cdd:TIGR01083  15 YPHPTTELDFNNPFELLVATILSAQATDKRVNKATPKLFEVYPTPQALAQAGLEELEEYIKSIGLYRNKAKNIIELCRKL 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1175203548 134 VTDYGGEVPSALEDLVRLPGVGRKTAHVVRGNAFGIPGLTVDTHFGRLVRRLKLTEEEDPVKVERVLAKLIEKKEWTMFS 213
Cdd:TIGR01083  95 VERYGGEVPEDREELVKLPGVGRKTANVVLNVAFGIPAIAVDTHVFRVSNRLGLSKGKDPIKVEEDLMKLVPREFWVKLH 174
                         170
                  ....*....|....*...
gi 1175203548 214 HRIIFHGRRVCHARKPAC 231
Cdd:TIGR01083 175 HWLILHGRYTCKARKPLC 192
ENDO3c smart00478
endonuclease III; includes endonuclease III (DNA-(apurinic or apyrimidinic site) lyase), ...
75-222 1.61e-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: 165.90  E-value: 1.61e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1175203548   75 LSAQCTDVRVNQVTPALFARYRTAEDYATADEAELQEIIRPTGFYKAKAGHLIGMGRLLVTDYGGEVPSALEDLVRLPGV 154
Cdd:smart00478   1 LSQQTTDERVNKATERLFEKFPTPEDLAAADEEELEELIRGLGFYRRKARYLIELARILVEEYGGEVPDDREELLKLPGV 80
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1175203548  155 GRKTAHVVRGNAFGIPGLTVDTHFGRLVRRLKLTEEED-PVKVERVLAKLIEKKEWTMFSHRIIFHGRR 222
Cdd:smart00478  81 GRKTANAVLSFALGKPFIPVDTHVLRIAKRLGLVDKKStPEEVEKLLEKLLPEEDWRELNLLLIDFGRT 149
ENDO3c cd00056
endonuclease III; includes endonuclease III (DNA-(apurinic or apyrimidinic site) lyase), ...
68-220 1.46e-45

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: 151.24  E-value: 1.46e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1175203548  68 ELVVATVLSAQCTDVRVNQVTPALFARYR-TAEDYATADEAELQEIIRPTGfYKAKAGHLIGMGRLLVTDYGGEV---PS 143
Cdd:cd00056     2 EVLVSEILSQQTTDKAVNKAYERLFERYGpTPEALAAADEEELRELIRSLG-YRRKAKYLKELARAIVEGFGGLVlddPD 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1175203548 144 ALEDLVRLPGVGRKTAHVVRGNAFGIPGLTVDTHFGRLVRRLKL-TEEEDPVKVERVLAKLIEKKEWTMFSHRIIFHG 220
Cdd:cd00056    81 AREELLALPGVGRKTANVVLLFALGPDAFPVDTHVRRVLKRLGLiPKKKTPEELEELLEELLPKPYWGEANQALMDLG 158
PRK10702 PRK10702
endonuclease III; Provisional
55-240 3.33e-39

endonuclease III; Provisional


Pssm-ID: 182661 [Multi-domain]  Cd Length: 211  Bit Score: 136.69  E-value: 3.33e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1175203548  55 PDAHCELDFTNTLELVVATVLSAQCTDVRVNQVTPALFARYRTAEDYATADEAELQEIIRPTGFYKAKAGHLIGMGRLLV 134
Cdd:PRK10702   18 PHPTTELNFSSPFELLIAVLLSAQATDVSVNKATAKLYPVANTPAAMLELGVEGVKTYIKTIGLYNSKAENVIKTCRILL 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1175203548 135 TDYGGEVPSALEDLVRLPGVGRKTAHVVRGNAFGIPGLTVDTHFGRLVRRLKLTEEEDPVKVERVLAKLIEKKEWTMFSH 214
Cdd:PRK10702   98 EQHNGEVPEDRAALEALPGVGRKTANVVLNTAFGWPTIAVDTHIFRVCNRTQFAPGKNVEQVEEKLLKVVPAEFKVDCHH 177
                         170       180
                  ....*....|....*....|....*.
gi 1175203548 215 RIIFHGRRVCHARKPACGACFLAPEC 240
Cdd:PRK10702  178 WLILHGRYTCIARKPRCGSCIIEDLC 203
HhH-GPD pfam00730
HhH-GPD superfamily base excision DNA repair protein; This family contains a diverse range of ...
71-206 5.81e-39

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: 133.56  E-value: 5.81e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1175203548  71 VATVLSAQCTDVRVNQVTPALFAR-YRTAEDYATADEAELQEIIRPTGFYKAKAGHLIGMGRLLVTDYGGEVPSALEDLV 149
Cdd:pfam00730   1 VSAILSQQTSDKAVNKITERLFEKfFPTPEDLADADEEELRELIRGLGFYRRKAKYLKELARILVEGYGGEVPLDEEELE 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1175203548 150 -RLPGVGRKTAHVVRGNAFG--IPGLTVDTHFGRLVRRLKLTEE-EDPVKVERVLAKLIEK 206
Cdd:pfam00730  81 aLLKGVGRWTAEAVLIFALGrpDPLPVVDTHVRRVLKRLGLIKEkPTPKEVERELEELWPP 141
 
Name Accession Description Interval E-value
Nth COG0177
Endonuclease III [Replication, recombination and repair];
54-244 5.24e-110

Endonuclease III [Replication, recombination and repair];


Pssm-ID: 439947 [Multi-domain]  Cd Length: 198  Bit Score: 316.65  E-value: 5.24e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1175203548  54 YPDAHCELDFTNTLELVVATVLSAQCTDVRVNQVTPALFARYRTAEDYATADEAELQEIIRPTGFYKAKAGHLIGMGRLL 133
Cdd:COG0177     8 YPDAKTELDYRDPFELLVATILSAQTTDERVNKATPRLFARYPTPEALAAADLEELEELIRPIGLYRNKAKNIIALARIL 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1175203548 134 VTDYGGEVPSALEDLVRLPGVGRKTAHVVRGNAFGIPGLTVDTHFGRLVRRLKLTEEEDPVKVERVLAKLIEKKEWTMFS 213
Cdd:COG0177    88 VEKYGGEVPETREELESLPGVGRKTANVVLNFAFGKPAIAVDTHVHRVSNRLGLVPGKDPEEVEKDLMKLIPKEYWGDLH 167
                         170       180       190
                  ....*....|....*....|....*....|.
gi 1175203548 214 HRIIFHGRRVCHARKPACGACFLAPECPSFG 244
Cdd:COG0177   168 HLLILHGRYICKARKPKCEECPLADLCPYYG 198
nth TIGR01083
endonuclease III; This equivalog model identifes nth members of the pfam00730 superfamily ...
54-231 8.69e-95

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: 277.72  E-value: 8.69e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1175203548  54 YPDAHCELDFTNTLELVVATVLSAQCTDVRVNQVTPALFARYRTAEDYATADEAELQEIIRPTGFYKAKAGHLIGMGRLL 133
Cdd:TIGR01083  15 YPHPTTELDFNNPFELLVATILSAQATDKRVNKATPKLFEVYPTPQALAQAGLEELEEYIKSIGLYRNKAKNIIELCRKL 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1175203548 134 VTDYGGEVPSALEDLVRLPGVGRKTAHVVRGNAFGIPGLTVDTHFGRLVRRLKLTEEEDPVKVERVLAKLIEKKEWTMFS 213
Cdd:TIGR01083  95 VERYGGEVPEDREELVKLPGVGRKTANVVLNVAFGIPAIAVDTHVFRVSNRLGLSKGKDPIKVEEDLMKLVPREFWVKLH 174
                         170
                  ....*....|....*...
gi 1175203548 214 HRIIFHGRRVCHARKPAC 231
Cdd:TIGR01083 175 HWLILHGRYTCKARKPLC 192
ENDO3c smart00478
endonuclease III; includes endonuclease III (DNA-(apurinic or apyrimidinic site) lyase), ...
75-222 1.61e-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: 165.90  E-value: 1.61e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1175203548   75 LSAQCTDVRVNQVTPALFARYRTAEDYATADEAELQEIIRPTGFYKAKAGHLIGMGRLLVTDYGGEVPSALEDLVRLPGV 154
Cdd:smart00478   1 LSQQTTDERVNKATERLFEKFPTPEDLAAADEEELEELIRGLGFYRRKARYLIELARILVEEYGGEVPDDREELLKLPGV 80
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1175203548  155 GRKTAHVVRGNAFGIPGLTVDTHFGRLVRRLKLTEEED-PVKVERVLAKLIEKKEWTMFSHRIIFHGRR 222
Cdd:smart00478  81 GRKTANAVLSFALGKPFIPVDTHVLRIAKRLGLVDKKStPEEVEKLLEKLLPEEDWRELNLLLIDFGRT 149
ENDO3c cd00056
endonuclease III; includes endonuclease III (DNA-(apurinic or apyrimidinic site) lyase), ...
68-220 1.46e-45

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: 151.24  E-value: 1.46e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1175203548  68 ELVVATVLSAQCTDVRVNQVTPALFARYR-TAEDYATADEAELQEIIRPTGfYKAKAGHLIGMGRLLVTDYGGEV---PS 143
Cdd:cd00056     2 EVLVSEILSQQTTDKAVNKAYERLFERYGpTPEALAAADEEELRELIRSLG-YRRKAKYLKELARAIVEGFGGLVlddPD 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1175203548 144 ALEDLVRLPGVGRKTAHVVRGNAFGIPGLTVDTHFGRLVRRLKL-TEEEDPVKVERVLAKLIEKKEWTMFSHRIIFHG 220
Cdd:cd00056    81 AREELLALPGVGRKTANVVLLFALGPDAFPVDTHVRRVLKRLGLiPKKKTPEELEELLEELLPKPYWGEANQALMDLG 158
PRK10702 PRK10702
endonuclease III; Provisional
55-240 3.33e-39

endonuclease III; Provisional


Pssm-ID: 182661 [Multi-domain]  Cd Length: 211  Bit Score: 136.69  E-value: 3.33e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1175203548  55 PDAHCELDFTNTLELVVATVLSAQCTDVRVNQVTPALFARYRTAEDYATADEAELQEIIRPTGFYKAKAGHLIGMGRLLV 134
Cdd:PRK10702   18 PHPTTELNFSSPFELLIAVLLSAQATDVSVNKATAKLYPVANTPAAMLELGVEGVKTYIKTIGLYNSKAENVIKTCRILL 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1175203548 135 TDYGGEVPSALEDLVRLPGVGRKTAHVVRGNAFGIPGLTVDTHFGRLVRRLKLTEEEDPVKVERVLAKLIEKKEWTMFSH 214
Cdd:PRK10702   98 EQHNGEVPEDRAALEALPGVGRKTANVVLNTAFGWPTIAVDTHIFRVCNRTQFAPGKNVEQVEEKLLKVVPAEFKVDCHH 177
                         170       180
                  ....*....|....*....|....*.
gi 1175203548 215 RIIFHGRRVCHARKPACGACFLAPEC 240
Cdd:PRK10702  178 WLILHGRYTCIARKPRCGSCIIEDLC 203
HhH-GPD pfam00730
HhH-GPD superfamily base excision DNA repair protein; This family contains a diverse range of ...
71-206 5.81e-39

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: 133.56  E-value: 5.81e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1175203548  71 VATVLSAQCTDVRVNQVTPALFAR-YRTAEDYATADEAELQEIIRPTGFYKAKAGHLIGMGRLLVTDYGGEVPSALEDLV 149
Cdd:pfam00730   1 VSAILSQQTSDKAVNKITERLFEKfFPTPEDLADADEEELRELIRGLGFYRRKAKYLKELARILVEGYGGEVPLDEEELE 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1175203548 150 -RLPGVGRKTAHVVRGNAFG--IPGLTVDTHFGRLVRRLKLTEE-EDPVKVERVLAKLIEK 206
Cdd:pfam00730  81 aLLKGVGRWTAEAVLIFALGrpDPLPVVDTHVRRVLKRLGLIKEkPTPKEVERELEELWPP 141
HP0602 COG2231
3-Methyladenine DNA glycosylase, HhH-GPD/Endo3 superfamily [Replication, recombination and ...
97-241 6.17e-17

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


Pssm-ID: 441832 [Multi-domain]  Cd Length: 220  Bit Score: 77.58  E-value: 6.17e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1175203548  97 TAEDYATADEAELQEIIRPTGFYKAKAGHLIGMGRLLVTDYGGEVPSAL--------EDLVRLPGVGRKTAHVVRGNAFG 168
Cdd:COG2231    61 DPEALAALDPEELAELIRPSGFYNQKAKRLKNLARWLVERYGGGLEKLKalpteelrEELLSLKGIGPETADSILLYAFN 140
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1175203548 169 IPGLTVDTHFGRLVRRLKLTEEE---DPVK--VERVLAK-LIEKKEWtmfsHR-IIFHGRRVCHArKPACGACFLAPECP 241
Cdd:COG2231   141 RPVFVVDAYTRRIFSRLGLIEEDasyDELQrlFEENLPPdVALYNEF----HAlIVEHGKEYCKK-KPKCEECPLRDLCP 215
MutY COG1194
Adenine-specific DNA glycosylase, acts on AG and A-oxoG pairs [Replication, recombination and ...
83-240 2.37e-09

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: 57.46  E-value: 2.37e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1175203548  83 RVNQVTP--ALF-ARYRTAEDYATADEAE-------LqeiirptGFYkAKAGHLIGMGRLLVTDYGGEVPSALEDLVRLP 152
Cdd:COG1194    43 QVATVIPyyERFlERFPTVEALAAAPEDEvlklwegL-------GYY-SRARNLHKAAQQVVEEHGGVFPDTYEELLALP 114
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1175203548 153 GVGRKTAHVVRGNAFGIPGLTVDthfG---RLVRRLkLTEEEDP--VKVERVLAKLIEkkewTMFSHR--------IIFH 219
Cdd:COG1194   115 GIGPYTAAAIASIAFGEPAPIVD---GnvkRVLSRL-FAIEGPIgsPAAKKELWALAE----ELLPPErpgdfnqaLMDL 186
                         170       180
                  ....*....|....*....|.
gi 1175203548 220 GRRVCHARKPACGACFLAPEC 240
Cdd:COG1194   187 GATVCTPKKPKCLLCPLQDDC 207
PRK10880 PRK10880
adenine DNA glycosylase;
93-244 1.51e-07

adenine DNA glycosylase;


Pssm-ID: 182805 [Multi-domain]  Cd Length: 350  Bit Score: 52.02  E-value: 1.51e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1175203548  93 ARYRTAEDYATAdeaELQEIIRP-TGF-YKAKAGHLIGMGRLLVTDYGGEVPSALEDLVRLPGVGRKTAHvvrgnafGIP 170
Cdd:PRK10880   57 ARFPTVTDLANA---PLDEVLHLwTGLgYYARARNLHKAAQQVATLHGGEFPETFEEVAALPGVGRSTAG-------AIL 126
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1175203548 171 GLTVDTHFgrlvrrlklteeedPV---KVERVLA-----------KLIEKKEWTM------------FSHRIIFHGRRVC 224
Cdd:PRK10880  127 SLSLGKHF--------------PIldgNVKRVLArcyavsgwpgkKEVENRLWQLseqvtpavgverFNQAMMDLGAMVC 192
                         170       180
                  ....*....|....*....|
gi 1175203548 225 HARKPACGACFLAPECPSFG 244
Cdd:PRK10880  193 TRSKPKCELCPLQNGCIAYA 212
PRK13910 PRK13910
DNA glycosylase MutY; Provisional
95-240 5.10e-06

DNA glycosylase MutY; Provisional


Pssm-ID: 172427 [Multi-domain]  Cd Length: 289  Bit Score: 46.94  E-value: 5.10e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1175203548  95 YRTAEDYATADEAELQEIIRPTGFYkAKAGHLIGMGRLLVTDYGGEVPSALEDLVRLPGVGRKTAHVVRGNAFGIPGLTV 174
Cdd:PRK13910   22 FPTLKDLANAPLEEVLLLWRGLGYY-SRAKNLKKSAEICVKEHHSQLPNDYQSLLKLPGIGAYTANAILCFGFREKSACV 100
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1175203548 175 DTHFGR-LVRRLKLTEEEDPVKVERVLAKLIEKKEWTMFSHRIIFHGRRVChARKPACGACFLAPEC 240
Cdd:PRK13910  101 DANIKRvLLRLFGLDPNIHAKDLQIKANDFLNLNESFNHNQALIDLGALIC-SPKPKCAICPLNPYC 166
FES smart00525
iron-sulpphur binding domain in DNA-(apurinic or apyrimidinic site) lyase (subfamily of ENDO3); ...
223-243 3.58e-05

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


Pssm-ID: 197771 [Multi-domain]  Cd Length: 21  Bit Score: 39.84  E-value: 3.58e-05
                           10        20
                   ....*....|....*....|.
gi 1175203548  223 VCHARKPACGACFLAPECPSF 243
Cdd:smart00525   1 ICTARKPRCDECPLKDLCPAY 21
PRK13913 PRK13913
3-methyladenine DNA glycosylase; Provisional
99-223 4.21e-05

3-methyladenine DNA glycosylase; Provisional


Pssm-ID: 184390  Cd Length: 218  Bit Score: 43.68  E-value: 4.21e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1175203548  99 EDYATADEAELQEIIRPTGFYKAKAGHLIGMGRLLVTDYGG------EVpsALEDLVRLPGVGRKTAHVVRGNAFGIPGL 172
Cdd:PRK13913   70 KKIAYIEFSKLAECVRPSGFYNQKAKRLIDLSENILKDFGSfenfkqEV--TREWLLDQKGIGKESADAILCYVCAKEVM 147
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1175203548 173 TVDTHFGRLVRRLKLT-EEEDPVK------VERVLAKLIEKKEWTMFSHRII--FHGRRV 223
Cdd:PRK13913  148 VVDKYSYLFLKKLGIEiEDYDELQhffekgVQENLNSALALYENTISLAQLYarFHGKIV 207
AlkA COG0122
3-methyladenine DNA glycosylase/8-oxoguanine DNA glycosylase [Replication, recombination and ...
97-202 3.01e-04

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


Pssm-ID: 439892 [Multi-domain]  Cd Length: 255  Bit Score: 41.41  E-value: 3.01e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1175203548  97 TAEDYATADEAELQEIirptGFYKAKAGHLIGMGRLLVTD-------YGGEVPSALEDLVRLPGVGRKTAHVV------R 163
Cdd:COG0122   129 TPEALAAASEEELRAC----GLSRRKARYLRALARAVADGeldlealAGLDDEEAIARLTALPGIGPWTAEMVllfalgR 204
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1175203548 164 GNAFgipgLTVDTHFGRLVRRLKLTEEE-DPVKVERVLAK 202
Cdd:COG0122   205 PDAF----PAGDLGLRRALGRLYGLGERpTPKELRELAEP 240
HHH pfam00633
Helix-hairpin-helix motif; The helix-hairpin-helix DNA-binding motif is found to be duplicated ...
136-163 3.31e-04

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: 37.40  E-value: 3.31e-04
                          10        20
                  ....*....|....*....|....*...
gi 1175203548 136 DYGGEVPSALEDLVRLPGVGRKTAHVVR 163
Cdd:pfam00633   1 SLEGLIPASVEELLALPGVGPKTAEAIL 28
EndIII_4Fe-2S pfam10576
Iron-sulfur binding domain of endonuclease III; Escherichia coli endonuclease III (EC 4.2.99. ...
224-240 2.06e-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: 2.06e-03
                          10
                  ....*....|....*..
gi 1175203548 224 CHARKPACGACFLAPEC 240
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH