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Conserved domains on  [gi|480336642|gb|ENX56849|]
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endonuclease III [Acinetobacter sp. NIPH 1867]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK10702 super family cl32560
endonuclease III; Provisional
 6-213 2.75e-127

endonuclease III; Provisional


The actual alignment was detected with superfamily member PRK10702:

Pssm-ID: 182661 [Multi-domain]  Cd Length: 211  Bit Score: 358.18  E-value: 2.75e-127
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480336642   6 MTKKQIQTFFERLREQRPHPQTELNYSSPFELLIAVLLSAQATDVSVNKATDKLYPVANTAQAILDLGIDGLKSYIKTIG 85
Cdd:PRK10702   1 MNKAKRLEILTRLRDNNPHPTTELNFSSPFELLIAVLLSAQATDVSVNKATAKLYPVANTPAAMLELGVEGVKTYIKTIG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480336642  86 LYNSKAENVIKTCRILVDQYQGQIPETRKELEALPGVGRKTANVVLNTAFGQPTMAVDTHIFRVGNRTGLAVGKNVLEVE 165
Cdd:PRK10702  81 LYNSKAENVIKTCRILLEQHNGEVPEDRAALEALPGVGRKTANVVLNTAFGWPTIAVDTHIFRVCNRTQFAPGKNVEQVE 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 480336642 166 DRLIKVIPKEFIIDAHHWLILHGRYCCIARKPKCGECIVADVCNWPDR 213
Cdd:PRK10702 161 EKLLKVVPAEFKVDCHHWLILHGRYTCIARKPRCGSCIIEDLCEYKEK 208
 
Name Accession Description Interval E-value
PRK10702 PRK10702
endonuclease III; Provisional
 6-213 2.75e-127

endonuclease III; Provisional


Pssm-ID: 182661 [Multi-domain]  Cd Length: 211  Bit Score: 358.18  E-value: 2.75e-127
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480336642   6 MTKKQIQTFFERLREQRPHPQTELNYSSPFELLIAVLLSAQATDVSVNKATDKLYPVANTAQAILDLGIDGLKSYIKTIG 85
Cdd:PRK10702   1 MNKAKRLEILTRLRDNNPHPTTELNFSSPFELLIAVLLSAQATDVSVNKATAKLYPVANTPAAMLELGVEGVKTYIKTIG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480336642  86 LYNSKAENVIKTCRILVDQYQGQIPETRKELEALPGVGRKTANVVLNTAFGQPTMAVDTHIFRVGNRTGLAVGKNVLEVE 165
Cdd:PRK10702  81 LYNSKAENVIKTCRILLEQHNGEVPEDRAALEALPGVGRKTANVVLNTAFGWPTIAVDTHIFRVCNRTQFAPGKNVEQVE 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 480336642 166 DRLIKVIPKEFIIDAHHWLILHGRYCCIARKPKCGECIVADVCNWPDR 213
Cdd:PRK10702 161 EKLLKVVPAEFKVDCHHWLILHGRYTCIARKPRCGSCIIEDLCEYKEK 208
Nth COG0177
Endonuclease III [Replication, recombination and repair];
15-212 7.19e-123

Endonuclease III [Replication, recombination and repair];


Pssm-ID: 439947 [Multi-domain]  Cd Length: 198  Bit Score: 346.31  E-value: 7.19e-123
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480336642  15 FERLREQRPHPQTELNYSSPFELLIAVLLSAQATDVSVNKATDKLYPVANTAQAILDLGIDGLKSYIKTIGLYNSKAENV 94
Cdd:COG0177    1 LERLKELYPDAKTELDYRDPFELLVATILSAQTTDERVNKATPRLFARYPTPEALAAADLEELEELIRPIGLYRNKAKNI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480336642  95 IKTCRILVDQYQGQIPETRKELEALPGVGRKTANVVLNTAFGQPTMAVDTHIFRVGNRTGLAVGKNVLEVEDRLIKVIPK 174
Cdd:COG0177   81 IALARILVEKYGGEVPETREELESLPGVGRKTANVVLNFAFGKPAIAVDTHVHRVSNRLGLVPGKDPEEVEKDLMKLIPK 160

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 480336642 175 EFIIDAHHWLILHGRYCCIARKPKCGECIVADVCNWPD 212
Cdd:COG0177  161 EYWGDLHHLLILHGRYICKARKPKCEECPLADLCPYYG 198
nth TIGR01083
endonuclease III; This equivalog model identifes nth members of the pfam00730 superfamily ...
 8-199 9.26e-113

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: 320.87  E-value: 9.26e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480336642    8 KKQIQTFFERLREQRPHPQTELNYSSPFELLIAVLLSAQATDVSVNKATDKLYPVANTAQAILDLGIDGLKSYIKTIGLY 87
Cdd:TIGR01083   1 RQKAQEILERLRKNYPHPTTELDFNNPFELLVATILSAQATDKRVNKATPKLFEVYPTPQALAQAGLEELEEYIKSIGLY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480336642   88 NSKAENVIKTCRILVDQYQGQIPETRKELEALPGVGRKTANVVLNTAFGQPTMAVDTHIFRVGNRTGLAVGKNVLEVEDR 167
Cdd:TIGR01083  81 RNKAKNIIELCRKLVERYGGEVPEDREELVKLPGVGRKTANVVLNVAFGIPAIAVDTHVFRVSNRLGLSKGKDPIKVEED 160

                         170       180       190
                  ....*....|....*....|....*....|..
gi 480336642  168 LIKVIPKEFIIDAHHWLILHGRYCCIARKPKC 199
Cdd:TIGR01083 161 LMKLVPREFWVKLHHWLILHGRYTCKARKPLC 192
ENDO3c cd00056
endonuclease III; includes endonuclease III (DNA-(apurinic or apyrimidinic site) lyase), ...
 35-188 3.77e-50

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: 160.48  E-value: 3.77e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480336642  35 FELLIAVLLSAQATDVSVNKATDKLYP-VANTAQAILDLGIDGLKSYIKTIGlYNSKAENVIKTCRILVDQYQGQI---P 110
Cdd:cd00056    1 FEVLVSEILSQQTTDKAVNKAYERLFErYGPTPEALAAADEEELRELIRSLG-YRRKAKYLKELARAIVEGFGGLVlddP 79

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 480336642 111 ETRKELEALPGVGRKTANVVLNTAFGQPTMAVDTHIFRVGNRTGLAV-GKNVLEVEDRLIKVIPKEFIIDAHHWLILHG 188
Cdd:cd00056   80 DAREELLALPGVGRKTANVVLLFALGPDAFPVDTHVRRVLKRLGLIPkKKTPEELEELLEELLPKPYWGEANQALMDLG 158
ENDO3c smart00478
endonuclease III; includes endonuclease III (DNA-(apurinic or apyrimidinic site) lyase), ...
 43-190 3.90e-49

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: 157.81  E-value: 3.90e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480336642    43 LSAQATDVSVNKATDKLYPVANTAQAILDLGIDGLKSYIKTIGLYNSKAENVIKTCRILVDQYQGQIPETRKELEALPGV 122
Cdd:smart00478   1 LSQQTTDERVNKATERLFEKFPTPEDLAAADEEELEELIRGLGFYRRKARYLIELARILVEEYGGEVPDDREELLKLPGV 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 480336642   123 GRKTANVVLNTAFGQPTMAVDTHIFRVGNRTGLAVGKNV-LEVEDRLIKVIPKEFIIDAHHWLILHGRY 190
Cdd:smart00478  81 GRKTANAVLSFALGKPFIPVDTHVLRIAKRLGLVDKKSTpEEVEKLLEKLLPEEDWRELNLLLIDFGRT 149
HhH-GPD pfam00730
HhH-GPD superfamily base excision DNA repair protein; This family contains a diverse range of ...
 39-174 4.34e-37

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: 126.63  E-value: 4.34e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480336642   39 IAVLLSAQATDVSVNKATDKLY-PVANTAQAILDLGIDGLKSYIKTIGLYNSKAENVIKTCRILVDQYQGQIPETRKELE 117
Cdd:pfam00730   1 VSAILSQQTSDKAVNKITERLFeKFFPTPEDLADADEEELRELIRGLGFYRRKAKYLKELARILVEGYGGEVPLDEEELE 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 480336642  118 A-LPGVGRKTANVVLNTAFG--QPTMAVDTHIFRVGNRTGLAVGKN-VLEVEDRLIKVIPK 174
Cdd:pfam00730  81 AlLKGVGRWTAEAVLIFALGrpDPLPVVDTHVRRVLKRLGLIKEKPtPKEVERELEELWPP 141
 
Name Accession Description Interval E-value
PRK10702 PRK10702
endonuclease III; Provisional
 6-213 2.75e-127

endonuclease III; Provisional


Pssm-ID: 182661 [Multi-domain]  Cd Length: 211  Bit Score: 358.18  E-value: 2.75e-127
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480336642   6 MTKKQIQTFFERLREQRPHPQTELNYSSPFELLIAVLLSAQATDVSVNKATDKLYPVANTAQAILDLGIDGLKSYIKTIG 85
Cdd:PRK10702   1 MNKAKRLEILTRLRDNNPHPTTELNFSSPFELLIAVLLSAQATDVSVNKATAKLYPVANTPAAMLELGVEGVKTYIKTIG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480336642  86 LYNSKAENVIKTCRILVDQYQGQIPETRKELEALPGVGRKTANVVLNTAFGQPTMAVDTHIFRVGNRTGLAVGKNVLEVE 165
Cdd:PRK10702  81 LYNSKAENVIKTCRILLEQHNGEVPEDRAALEALPGVGRKTANVVLNTAFGWPTIAVDTHIFRVCNRTQFAPGKNVEQVE 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 480336642 166 DRLIKVIPKEFIIDAHHWLILHGRYCCIARKPKCGECIVADVCNWPDR 213
Cdd:PRK10702 161 EKLLKVVPAEFKVDCHHWLILHGRYTCIARKPRCGSCIIEDLCEYKEK 208
Nth COG0177
Endonuclease III [Replication, recombination and repair];
15-212 7.19e-123

Endonuclease III [Replication, recombination and repair];


Pssm-ID: 439947 [Multi-domain]  Cd Length: 198  Bit Score: 346.31  E-value: 7.19e-123
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480336642  15 FERLREQRPHPQTELNYSSPFELLIAVLLSAQATDVSVNKATDKLYPVANTAQAILDLGIDGLKSYIKTIGLYNSKAENV 94
Cdd:COG0177    1 LERLKELYPDAKTELDYRDPFELLVATILSAQTTDERVNKATPRLFARYPTPEALAAADLEELEELIRPIGLYRNKAKNI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480336642  95 IKTCRILVDQYQGQIPETRKELEALPGVGRKTANVVLNTAFGQPTMAVDTHIFRVGNRTGLAVGKNVLEVEDRLIKVIPK 174
Cdd:COG0177   81 IALARILVEKYGGEVPETREELESLPGVGRKTANVVLNFAFGKPAIAVDTHVHRVSNRLGLVPGKDPEEVEKDLMKLIPK 160

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 480336642 175 EFIIDAHHWLILHGRYCCIARKPKCGECIVADVCNWPD 212
Cdd:COG0177  161 EYWGDLHHLLILHGRYICKARKPKCEECPLADLCPYYG 198
nth TIGR01083
endonuclease III; This equivalog model identifes nth members of the pfam00730 superfamily ...
 8-199 9.26e-113

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: 320.87  E-value: 9.26e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480336642    8 KKQIQTFFERLREQRPHPQTELNYSSPFELLIAVLLSAQATDVSVNKATDKLYPVANTAQAILDLGIDGLKSYIKTIGLY 87
Cdd:TIGR01083   1 RQKAQEILERLRKNYPHPTTELDFNNPFELLVATILSAQATDKRVNKATPKLFEVYPTPQALAQAGLEELEEYIKSIGLY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480336642   88 NSKAENVIKTCRILVDQYQGQIPETRKELEALPGVGRKTANVVLNTAFGQPTMAVDTHIFRVGNRTGLAVGKNVLEVEDR 167
Cdd:TIGR01083  81 RNKAKNIIELCRKLVERYGGEVPEDREELVKLPGVGRKTANVVLNVAFGIPAIAVDTHVFRVSNRLGLSKGKDPIKVEED 160

                         170       180       190
                  ....*....|....*....|....*....|..
gi 480336642  168 LIKVIPKEFIIDAHHWLILHGRYCCIARKPKC 199
Cdd:TIGR01083 161 LMKLVPREFWVKLHHWLILHGRYTCKARKPLC 192
ENDO3c cd00056
endonuclease III; includes endonuclease III (DNA-(apurinic or apyrimidinic site) lyase), ...
 35-188 3.77e-50

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: 160.48  E-value: 3.77e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480336642  35 FELLIAVLLSAQATDVSVNKATDKLYP-VANTAQAILDLGIDGLKSYIKTIGlYNSKAENVIKTCRILVDQYQGQI---P 110
Cdd:cd00056    1 FEVLVSEILSQQTTDKAVNKAYERLFErYGPTPEALAAADEEELRELIRSLG-YRRKAKYLKELARAIVEGFGGLVlddP 79

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 480336642 111 ETRKELEALPGVGRKTANVVLNTAFGQPTMAVDTHIFRVGNRTGLAV-GKNVLEVEDRLIKVIPKEFIIDAHHWLILHG 188
Cdd:cd00056   80 DAREELLALPGVGRKTANVVLLFALGPDAFPVDTHVRRVLKRLGLIPkKKTPEELEELLEELLPKPYWGEANQALMDLG 158
ENDO3c smart00478
endonuclease III; includes endonuclease III (DNA-(apurinic or apyrimidinic site) lyase), ...
 43-190 3.90e-49

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: 157.81  E-value: 3.90e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480336642    43 LSAQATDVSVNKATDKLYPVANTAQAILDLGIDGLKSYIKTIGLYNSKAENVIKTCRILVDQYQGQIPETRKELEALPGV 122
Cdd:smart00478   1 LSQQTTDERVNKATERLFEKFPTPEDLAAADEEELEELIRGLGFYRRKARYLIELARILVEEYGGEVPDDREELLKLPGV 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 480336642   123 GRKTANVVLNTAFGQPTMAVDTHIFRVGNRTGLAVGKNV-LEVEDRLIKVIPKEFIIDAHHWLILHGRY 190
Cdd:smart00478  81 GRKTANAVLSFALGKPFIPVDTHVLRIAKRLGLVDKKSTpEEVEKLLEKLLPEEDWRELNLLLIDFGRT 149
HhH-GPD pfam00730
HhH-GPD superfamily base excision DNA repair protein; This family contains a diverse range of ...
 39-174 4.34e-37

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: 126.63  E-value: 4.34e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480336642   39 IAVLLSAQATDVSVNKATDKLY-PVANTAQAILDLGIDGLKSYIKTIGLYNSKAENVIKTCRILVDQYQGQIPETRKELE 117
Cdd:pfam00730   1 VSAILSQQTSDKAVNKITERLFeKFFPTPEDLADADEEELRELIRGLGFYRRKAKYLKELARILVEGYGGEVPLDEEELE 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 480336642  118 A-LPGVGRKTANVVLNTAFG--QPTMAVDTHIFRVGNRTGLAVGKN-VLEVEDRLIKVIPK 174
Cdd:pfam00730  81 AlLKGVGRWTAEAVLIFALGrpDPLPVVDTHVRRVLKRLGLIKEKPtPKEVERELEELWPP 141
HP0602 COG2231
3-Methyladenine DNA glycosylase, HhH-GPD/Endo3 superfamily [Replication, recombination and ...
 33-210 1.31e-23

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


Pssm-ID: 441832 [Multi-domain]  Cd Length: 220  Bit Score: 94.14  E-value: 1.31e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480336642  33 SPFELLI-AVLlsAQATD-VSVNKATDKLYP-VANTAQAILDLGIDGLKSYIKTIGLYNSKAENVIKTCRILVDQYQGQI 109
Cdd:COG2231   28 TPFEVIVgAIL--TQNTSwKNVEKAIANLKEaGLLDPEALAALDPEELAELIRPSGFYNQKAKRLKNLARWLVERYGGGL 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480336642 110 --------PETRKELEALPGVGRKTANVVLNTAFGQPTMAVDTHIFRVGNRTGLAVG-KNVLEVEDRLIKVIP------K 174
Cdd:COG2231  106 eklkalptEELREELLSLKGIGPETADSILLYAFNRPVFVVDAYTRRIFSRLGLIEEdASYDELQRLFEENLPpdvalyN 185

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 480336642 175 EFiidaHHWLILHGRYCCiARKPKCGECIVADVCNW 210
Cdd:COG2231  186 EF----HALIVEHGKEYC-KKKPKCEECPLRDLCPY 216
MutY COG1194
Adenine-specific DNA glycosylase, acts on AG and A-oxoG pairs [Replication, recombination and ...
 85-208 6.14e-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: 78.26  E-value: 6.14e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480336642  85 GL-YNSKAENVIKTCRILVDQYQGQIPETRKELEALPGVGRKTANVVLNTAFGQPTMAVDTHIFRV-----GNRTGLAVG 158
Cdd:COG1194   78 GLgYYSRARNLHKAAQQVVEEHGGVFPDTYEELLALPGIGPYTAAAIASIAFGEPAPIVDGNVKRVlsrlfAIEGPIGSP 157

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 480336642 159 KNVLEVEDRLIKVIPKEfiiDAHHW---------LIlhgrycCIARKPKCGECIVADVC 208
Cdd:COG1194  158 AAKKELWALAEELLPPE---RPGDFnqalmdlgaTV------CTPKKPKCLLCPLQDDC 207
PRK10880 PRK10880
adenine DNA glycosylase;
85-208 3.42e-12

adenine DNA glycosylase;


Pssm-ID: 182805 [Multi-domain]  Cd Length: 350  Bit Score: 64.73  E-value: 3.42e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480336642  85 GL-YNSKAENVIKTCRILVDQYQGQIPETRKELEALPGVGRKTANVVLNTAFGQPTMAVDTHIFRVGNRTgLAV----GK 159
Cdd:PRK10880  79 GLgYYARARNLHKAAQQVATLHGGEFPETFEEVAALPGVGRSTAGAILSLSLGKHFPILDGNVKRVLARC-YAVsgwpGK 157

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 480336642 160 NvlEVEDRLI----KVIPKEFIIDAHHWLILHGRYCCIARKPKCGECIVADVC 208
Cdd:PRK10880 158 K--EVENRLWqlseQVTPAVGVERFNQAMMDLGAMVCTRSKPKCELCPLQNGC 208
AlkA COG0122
3-methyladenine DNA glycosylase/8-oxoguanine DNA glycosylase [Replication, recombination and ...
 33-146 4.78e-09

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


Pssm-ID: 439892 [Multi-domain]  Cd Length: 255  Bit Score: 54.89  E-value: 4.78e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480336642  33 SPFELLIAVLLSAQatdVSVNKAT-----------------DKLYPVANTAQAILDLGIDGLKSyiktIGLYNSKAENVI 95
Cdd:COG0122   83 DPFEALVRAILGQQ---VSVAAARtiwrrlvalfgepiegpGGGLYAFPTPEALAAASEEELRA----CGLSRRKARYLR 155

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 480336642  96 KTCRILVDqyqGQIP----------ETRKELEALPGVGRKTANVVLNTAFGQPT--MAVDTHI 146
Cdd:COG0122  156 ALARAVAD---GELDlealaglddeEAIARLTALPGIGPWTAEMVLLFALGRPDafPAGDLGL 215
HHH pfam00633
Helix-hairpin-helix motif; The helix-hairpin-helix DNA-binding motif is found to be duplicated ...
 105-131 7.14e-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: 47.03  E-value: 7.14e-08
                          10        20
                  ....*....|....*....|....*..
gi 480336642  105 YQGQIPETRKELEALPGVGRKTANVVL 131
Cdd:pfam00633   2 LEGLIPASVEELLALPGVGPKTAEAIL 28
PRK13910 PRK13910
DNA glycosylase MutY; Provisional
 87-208 9.75e-07

DNA glycosylase MutY; Provisional


Pssm-ID: 172427 [Multi-domain]  Cd Length: 289  Bit Score: 48.48  E-value: 9.75e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480336642  87 YNSKAENVIKTCRILVDQYQGQIPETRKELEALPGVGRKTANVVLNTAFGQPTMAVDTHIFRVGNRT-GLAVGKNVLEVE 165
Cdd:PRK13910  45 YYSRAKNLKKSAEICVKEHHSQLPNDYQSLLKLPGIGAYTANAILCFGFREKSACVDANIKRVLLRLfGLDPNIHAKDLQ 124

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 480336642 166 DRLIKVIPKEFIIDAHHWLILHGRYCCiARKPKCGECIVADVC 208
Cdd:PRK13910 125 IKANDFLNLNESFNHNQALIDLGALIC-SPKPKCAICPLNPYC 166
EndIII_4Fe-2S pfam10576
Iron-sulfur binding domain of endonuclease III; Escherichia coli endonuclease III (EC 4.2.99. ...
 192-208 3.17e-05

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: 39.68  E-value: 3.17e-05
                          10
                  ....*....|....*..
gi 480336642  192 CIARKPKCGECIVADVC 208
Cdd:pfam10576   1 CTARKPKCEECPLADLC 17
PRK13913 PRK13913
3-methyladenine DNA glycosylase; Provisional
 35-148 1.32e-04

3-methyladenine DNA glycosylase; Provisional


Pssm-ID: 184390  Cd Length: 218  Bit Score: 41.76  E-value: 1.32e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480336642  35 FELLIAVLLSAQATDVSVNKATD---KLYPVANTAQAILD----LGIDGLKSYIKTIGLYNSKAENVIKTCR-ILVD--- 103
Cdd:PRK13913  31 FEALLGAVLTQNTKFEAVEKSLEnlkNAFILENDDEINLKkiayIEFSKLAECVRPSGFYNQKAKRLIDLSEnILKDfgs 110

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 480336642 104 --QYQGQIpeTRKELEALPGVGRKTANVVLNTAFGQPTMAVDTHIFR 148
Cdd:PRK13913 111 feNFKQEV--TREWLLDQKGIGKESADAILCYVCAKEVMVVDKYSYL 155
FES smart00525
iron-sulpphur binding domain in DNA-(apurinic or apyrimidinic site) lyase (subfamily of ENDO3); ...
 192-210 2.82e-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: 2.82e-04
                           10
                   ....*....|....*....
gi 480336642   192 CIARKPKCGECIVADVCNW 210
Cdd:smart00525   2 CTARKPRCDECPLKDLCPA 20
ogg TIGR00588
8-oxoguanine DNA-glycosylase (ogg); All proteins in this family for which functions are known ...
 90-152 4.88e-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: 40.28  E-value: 4.88e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 480336642   90 KAENVIKTCRILVDQYQG----------QIPETRKELEALPGVGRKTANVVLNTAFGQP-TMAVDTHIFRVGNR 152
Cdd:TIGR00588 186 RARYIRETARALLEEQGGrawlqqirgaSYEDAREALCELPGVGPKVADCICLMGLDKPqAVPVDVHVWRIANR 259
 
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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