|
Name |
Accession |
Description |
Interval |
E-value |
| PRK10880 |
PRK10880 |
adenine DNA glycosylase; |
1-350 |
0e+00 |
|
adenine DNA glycosylase;
Pssm-ID: 182805 [Multi-domain] Cd Length: 350 Bit Score: 809.32 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130862 1 MQASQFSAQVLDWYDKYGRKTLPWQIDKTPYKVWLSEVMLQQTQVATVIPYFERFMARFPTVTDLANAPLDEVLHLWTGL 80
Cdd:PRK10880 1 MQASQFSAQVLDWYDKYGRKTLPWQIDKTPYKVWLSEVMLQQTQVATVIPYFERFMARFPTVTDLANAPLDEVLHLWTGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130862 81 GYYARARNLHKAAQQVATLHGGKFPETFEEVAALPGVGRSTAGAILSLSLGKHFPILDGNVKRVLARCYAVSGWPGKKEV 160
Cdd:PRK10880 81 GYYARARNLHKAAQQVATLHGGEFPETFEEVAALPGVGRSTAGAILSLSLGKHFPILDGNVKRVLARCYAVSGWPGKKEV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130862 161 ENKLWSLSEQVTPAVGVERFNQAMMDLGAMICTRSKPKCSLCPLQNGCIAAANNSWALYPGKKPKQTLPERTGYFLLLQH 240
Cdd:PRK10880 161 ENRLWQLSEQVTPAVGVERFNQAMMDLGAMVCTRSKPKCELCPLQNGCIAYANHSWALYPGKKPKQTLPERTGYFLLLQH 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130862 241 EDEVLLAQRPPSGLWGGLYCFPQFADEESLRQWLAQRQIAADNLTQLTAFRHTFSHFHLDIVPMWLPVSSFTGCMDEGNA 320
Cdd:PRK10880 241 GDEVWLEQRPPSGLWGGLFCFPQFADEEELRQWLAQRGIAADNLTQLTAFRHTFSHFHLDIVPMWLPVSSFTGCMDEGNG 320
|
330 340 350
....*....|....*....|....*....|
gi 16130862 321 LWYNLAQPPSVGLAAPVERLLQQLRTGAPV 350
Cdd:PRK10880 321 LWYNLAQPPSVGLAAPVERLLQQLRTGAPV 350
|
|
| MutY |
COG1194 |
Adenine-specific DNA glycosylase, acts on AG and A-oxoG pairs [Replication, recombination and ... |
1-345 |
0e+00 |
|
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: 562.84 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130862 1 MQASQFSAQVLDWYDKYGRkTLPWQIDKTPYKVWLSEVMLQQTQVATVIPYFERFMARFPTVTDLANAPLDEVLHLWTGL 80
Cdd:COG1194 1 MDMASFAKRLLAWYDRHGR-DLPWRQTRDPYRVWLSEIMLQQTQVATVIPYYERFLERFPTVEALAAAPEDEVLKLWEGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130862 81 GYYARARNLHKAAQQVATLHGGKFPETFEEVAALPGVGRSTAGAILSLSLGKHFPILDGNVKRVLARCYAVSGWPGKKEV 160
Cdd:COG1194 80 GYYSRARNLHKAAQQVVEEHGGVFPDTYEELLALPGIGPYTAAAIASIAFGEPAPIVDGNVKRVLSRLFAIEGPIGSPAA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130862 161 ENKLWSLSEQVTPAVGVERFNQAMMDLGAMICTRSKPKCSLCPLQNGCIAAANNSWALYPGKKPKQTLPERTGYFLLLQH 240
Cdd:COG1194 160 KKELWALAEELLPPERPGDFNQALMDLGATVCTPKKPKCLLCPLQDDCAAFAEGRQEELPVKKPKKKKPERYGAALVIRD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130862 241 EDEVLLAQRPPSGLWGGLYCFPQFADEES-----LRQWLAQR-QIAADNLTQLTAFRHTFSHFHLDIVPMWLPVSSfTGC 314
Cdd:COG1194 240 DGRVLLEKRPPKGLWGGLWEFPEFEWEEAedpeaLERWLREElGLEVEWLEPLGTVRHVFTHFRLHLTVYLARVPA-GPP 318
|
330 340 350
....*....|....*....|....*....|.
gi 16130862 315 MDEGNALWYNLAQPPSVGLAAPVERLLQQLR 345
Cdd:COG1194 319 AEPDGGRWVPLEELAALPLPAPMRKLLKALL 349
|
|
| mutY |
TIGR01084 |
A/G-specific adenine glycosylase; This equivalog model identifies mutY members of the ... |
5-278 |
0e+00 |
|
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: 521.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130862 5 QFSAQVLDWYDKYGRKTLPWQIDKTPYKVWLSEVMLQQTQVATVIPYFERFMARFPTVTDLANAPLDEVLHLWTGLGYYA 84
Cdd:TIGR01084 1 QFSEDLLSWYDKYGRKTLPWRQNKTPYRVWLSEVMLQQTQVATVIPYFERFLERFPTVQALANAPQDEVLKLWEGLGYYA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130862 85 RARNLHKAAQQVATLHGGKFPETFEEVAALPGVGRSTAGAILSLSLGKHFPILDGNVKRVLARCYAVSGWPGKKEVENKL 164
Cdd:TIGR01084 81 RARNLHKAAQEVVEEFGGEFPQDFEDLAALPGVGRYTAGAILSFALNKPYPILDGNVKRVLSRLFAVEGWPGKKKVENRL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130862 165 WSLSEQVTPAVGVERFNQAMMDLGAMICTRSKPKCSLCPLQNGCIAAANNSWALYPGKKPKQTLPERTGYFLLLQHED-E 243
Cdd:TIGR01084 161 WTLAESLLPKADPEAFNQALMDLGAMICTRKKPKCDLCPLQDFCLAYQQGTWEEYPVKKPKAAPPERTTYFLVLQNYDgE 240
|
250 260 270
....*....|....*....|....*....|....*
gi 16130862 244 VLLAQRPPSGLWGGLYCFPQFADEESLRQWLAQRQ 278
Cdd:TIGR01084 241 VLLEQRPEKGLWGGLYCFPQFEDEDSLAFLLAQRG 275
|
|
| ENDO3c |
cd00056 |
endonuclease III; includes endonuclease III (DNA-(apurinic or apyrimidinic site) lyase), ... |
31-188 |
1.60e-52 |
|
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: 170.89 E-value: 1.60e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130862 31 YKVWLSEVMLQQTQVATVIPYFERFMARF-PTVTDLANAPLDEVLHLWTGLGYYARARNLHKAAQQVATLHGGKF---PE 106
Cdd:cd00056 1 FEVLVSEILSQQTTDKAVNKAYERLFERYgPTPEALAAADEEELRELIRSLGYRRKAKYLKELARAIVEGFGGLVlddPD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130862 107 TFEEVAALPGVGRSTAGAILSLSLGKHFPILDGNVKRVLARCyavsGWPGKKEVENKLWSLSEQVTPAVGVERFNQAMMD 186
Cdd:cd00056 81 AREELLALPGVGRKTANVVLLFALGPDAFPVDTHVRRVLKRL----GLIPKKKTPEELEELLEELLPKPYWGEANQALMD 156
|
..
gi 16130862 187 LG 188
Cdd:cd00056 157 LG 158
|
|
| ENDO3c |
smart00478 |
endonuclease III; includes endonuclease III (DNA-(apurinic or apyrimidinic site) lyase), ... |
39-190 |
2.39e-50 |
|
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: 165.13 E-value: 2.39e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130862 39 MLQQTQVATVIPYFERFMARFPTVTDLANAPLDEVLHLWTGLG-YYARARNLHKAAQQVATLHGGKFPETFEEVAALPGV 117
Cdd:smart00478 1 LSQQTTDERVNKATERLFEKFPTPEDLAAADEEELEELIRGLGfYRRKARYLIELARILVEEYGGEVPDDREELLKLPGV 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16130862 118 GRSTAGAILSLSLGKHFPILDGNVKRVLARCYavsgWPGKKEVENKLWSLSEQVTPAVGVERFNQAMMDLGAM 190
Cdd:smart00478 81 GRKTANAVLSFALGKPFIPVDTHVLRIAKRLG----LVDKKSTPEEVEKLLEKLLPEEDWRELNLLLIDFGRT 149
|
|
| HhH-GPD |
pfam00730 |
HhH-GPD superfamily base excision DNA repair protein; This family contains a diverse range of ... |
35-170 |
1.17e-44 |
|
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: 150.13 E-value: 1.17e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130862 35 LSEVMLQQTQVATVIPYFERFMAR-FPTVTDLANAPLDEVLHLWTGLGYYAR-ARNLHKAAQQVATLHGGKFPETFEE-V 111
Cdd:pfam00730 1 VSAILSQQTSDKAVNKITERLFEKfFPTPEDLADADEEELRELIRGLGFYRRkAKYLKELARILVEGYGGEVPLDEEElE 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16130862 112 AALPGVGRSTAGAILSLSLG--KHFPILDGNVKRVLARCYAVSGWPGKKEVENKLWSLSEQ 170
Cdd:pfam00730 81 ALLKGVGRWTAEAVLIFALGrpDPLPVVDTHVRRVLKRLGLIKEKPTPKEVERELEELWPP 141
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK10880 |
PRK10880 |
adenine DNA glycosylase; |
1-350 |
0e+00 |
|
adenine DNA glycosylase;
Pssm-ID: 182805 [Multi-domain] Cd Length: 350 Bit Score: 809.32 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130862 1 MQASQFSAQVLDWYDKYGRKTLPWQIDKTPYKVWLSEVMLQQTQVATVIPYFERFMARFPTVTDLANAPLDEVLHLWTGL 80
Cdd:PRK10880 1 MQASQFSAQVLDWYDKYGRKTLPWQIDKTPYKVWLSEVMLQQTQVATVIPYFERFMARFPTVTDLANAPLDEVLHLWTGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130862 81 GYYARARNLHKAAQQVATLHGGKFPETFEEVAALPGVGRSTAGAILSLSLGKHFPILDGNVKRVLARCYAVSGWPGKKEV 160
Cdd:PRK10880 81 GYYARARNLHKAAQQVATLHGGEFPETFEEVAALPGVGRSTAGAILSLSLGKHFPILDGNVKRVLARCYAVSGWPGKKEV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130862 161 ENKLWSLSEQVTPAVGVERFNQAMMDLGAMICTRSKPKCSLCPLQNGCIAAANNSWALYPGKKPKQTLPERTGYFLLLQH 240
Cdd:PRK10880 161 ENRLWQLSEQVTPAVGVERFNQAMMDLGAMVCTRSKPKCELCPLQNGCIAYANHSWALYPGKKPKQTLPERTGYFLLLQH 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130862 241 EDEVLLAQRPPSGLWGGLYCFPQFADEESLRQWLAQRQIAADNLTQLTAFRHTFSHFHLDIVPMWLPVSSFTGCMDEGNA 320
Cdd:PRK10880 241 GDEVWLEQRPPSGLWGGLFCFPQFADEEELRQWLAQRGIAADNLTQLTAFRHTFSHFHLDIVPMWLPVSSFTGCMDEGNG 320
|
330 340 350
....*....|....*....|....*....|
gi 16130862 321 LWYNLAQPPSVGLAAPVERLLQQLRTGAPV 350
Cdd:PRK10880 321 LWYNLAQPPSVGLAAPVERLLQQLRTGAPV 350
|
|
| MutY |
COG1194 |
Adenine-specific DNA glycosylase, acts on AG and A-oxoG pairs [Replication, recombination and ... |
1-345 |
0e+00 |
|
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: 562.84 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130862 1 MQASQFSAQVLDWYDKYGRkTLPWQIDKTPYKVWLSEVMLQQTQVATVIPYFERFMARFPTVTDLANAPLDEVLHLWTGL 80
Cdd:COG1194 1 MDMASFAKRLLAWYDRHGR-DLPWRQTRDPYRVWLSEIMLQQTQVATVIPYYERFLERFPTVEALAAAPEDEVLKLWEGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130862 81 GYYARARNLHKAAQQVATLHGGKFPETFEEVAALPGVGRSTAGAILSLSLGKHFPILDGNVKRVLARCYAVSGWPGKKEV 160
Cdd:COG1194 80 GYYSRARNLHKAAQQVVEEHGGVFPDTYEELLALPGIGPYTAAAIASIAFGEPAPIVDGNVKRVLSRLFAIEGPIGSPAA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130862 161 ENKLWSLSEQVTPAVGVERFNQAMMDLGAMICTRSKPKCSLCPLQNGCIAAANNSWALYPGKKPKQTLPERTGYFLLLQH 240
Cdd:COG1194 160 KKELWALAEELLPPERPGDFNQALMDLGATVCTPKKPKCLLCPLQDDCAAFAEGRQEELPVKKPKKKKPERYGAALVIRD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130862 241 EDEVLLAQRPPSGLWGGLYCFPQFADEES-----LRQWLAQR-QIAADNLTQLTAFRHTFSHFHLDIVPMWLPVSSfTGC 314
Cdd:COG1194 240 DGRVLLEKRPPKGLWGGLWEFPEFEWEEAedpeaLERWLREElGLEVEWLEPLGTVRHVFTHFRLHLTVYLARVPA-GPP 318
|
330 340 350
....*....|....*....|....*....|.
gi 16130862 315 MDEGNALWYNLAQPPSVGLAAPVERLLQQLR 345
Cdd:COG1194 319 AEPDGGRWVPLEELAALPLPAPMRKLLKALL 349
|
|
| mutY |
TIGR01084 |
A/G-specific adenine glycosylase; This equivalog model identifies mutY members of the ... |
5-278 |
0e+00 |
|
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: 521.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130862 5 QFSAQVLDWYDKYGRKTLPWQIDKTPYKVWLSEVMLQQTQVATVIPYFERFMARFPTVTDLANAPLDEVLHLWTGLGYYA 84
Cdd:TIGR01084 1 QFSEDLLSWYDKYGRKTLPWRQNKTPYRVWLSEVMLQQTQVATVIPYFERFLERFPTVQALANAPQDEVLKLWEGLGYYA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130862 85 RARNLHKAAQQVATLHGGKFPETFEEVAALPGVGRSTAGAILSLSLGKHFPILDGNVKRVLARCYAVSGWPGKKEVENKL 164
Cdd:TIGR01084 81 RARNLHKAAQEVVEEFGGEFPQDFEDLAALPGVGRYTAGAILSFALNKPYPILDGNVKRVLSRLFAVEGWPGKKKVENRL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130862 165 WSLSEQVTPAVGVERFNQAMMDLGAMICTRSKPKCSLCPLQNGCIAAANNSWALYPGKKPKQTLPERTGYFLLLQHED-E 243
Cdd:TIGR01084 161 WTLAESLLPKADPEAFNQALMDLGAMICTRKKPKCDLCPLQDFCLAYQQGTWEEYPVKKPKAAPPERTTYFLVLQNYDgE 240
|
250 260 270
....*....|....*....|....*....|....*
gi 16130862 244 VLLAQRPPSGLWGGLYCFPQFADEESLRQWLAQRQ 278
Cdd:TIGR01084 241 VLLEQRPEKGLWGGLYCFPQFEDEDSLAFLLAQRG 275
|
|
| ENDO3c |
cd00056 |
endonuclease III; includes endonuclease III (DNA-(apurinic or apyrimidinic site) lyase), ... |
31-188 |
1.60e-52 |
|
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: 170.89 E-value: 1.60e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130862 31 YKVWLSEVMLQQTQVATVIPYFERFMARF-PTVTDLANAPLDEVLHLWTGLGYYARARNLHKAAQQVATLHGGKF---PE 106
Cdd:cd00056 1 FEVLVSEILSQQTTDKAVNKAYERLFERYgPTPEALAAADEEELRELIRSLGYRRKAKYLKELARAIVEGFGGLVlddPD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130862 107 TFEEVAALPGVGRSTAGAILSLSLGKHFPILDGNVKRVLARCyavsGWPGKKEVENKLWSLSEQVTPAVGVERFNQAMMD 186
Cdd:cd00056 81 AREELLALPGVGRKTANVVLLFALGPDAFPVDTHVRRVLKRL----GLIPKKKTPEELEELLEELLPKPYWGEANQALMD 156
|
..
gi 16130862 187 LG 188
Cdd:cd00056 157 LG 158
|
|
| ENDO3c |
smart00478 |
endonuclease III; includes endonuclease III (DNA-(apurinic or apyrimidinic site) lyase), ... |
39-190 |
2.39e-50 |
|
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: 165.13 E-value: 2.39e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130862 39 MLQQTQVATVIPYFERFMARFPTVTDLANAPLDEVLHLWTGLG-YYARARNLHKAAQQVATLHGGKFPETFEEVAALPGV 117
Cdd:smart00478 1 LSQQTTDERVNKATERLFEKFPTPEDLAAADEEELEELIRGLGfYRRKARYLIELARILVEEYGGEVPDDREELLKLPGV 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16130862 118 GRSTAGAILSLSLGKHFPILDGNVKRVLARCYavsgWPGKKEVENKLWSLSEQVTPAVGVERFNQAMMDLGAM 190
Cdd:smart00478 81 GRKTANAVLSFALGKPFIPVDTHVLRIAKRLG----LVDKKSTPEEVEKLLEKLLPEEDWRELNLLLIDFGRT 149
|
|
| HhH-GPD |
pfam00730 |
HhH-GPD superfamily base excision DNA repair protein; This family contains a diverse range of ... |
35-170 |
1.17e-44 |
|
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: 150.13 E-value: 1.17e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130862 35 LSEVMLQQTQVATVIPYFERFMAR-FPTVTDLANAPLDEVLHLWTGLGYYAR-ARNLHKAAQQVATLHGGKFPETFEE-V 111
Cdd:pfam00730 1 VSAILSQQTSDKAVNKITERLFEKfFPTPEDLADADEEELRELIRGLGFYRRkAKYLKELARILVEGYGGEVPLDEEElE 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16130862 112 AALPGVGRSTAGAILSLSLG--KHFPILDGNVKRVLARCYAVSGWPGKKEVENKLWSLSEQ 170
Cdd:pfam00730 81 ALLKGVGRWTAEAVLIFALGrpDPLPVVDTHVRRVLKRLGLIKEKPTPKEVERELEELWPP 141
|
|
| PRK13910 |
PRK13910 |
DNA glycosylase MutY; Provisional |
39-301 |
4.66e-38 |
|
DNA glycosylase MutY; Provisional
Pssm-ID: 172427 [Multi-domain] Cd Length: 289 Bit Score: 137.46 E-value: 4.66e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130862 39 MLQQTQVATVIP-YFERFMARFPTVTDLANAPLDEVLHLWTGLGYYARARNLHKAAQQVATLHGGKFPETFEEVAALPGV 117
Cdd:PRK13910 1 MSQQTQINTVVErFYSPFLEAFPTLKDLANAPLEEVLLLWRGLGYYSRAKNLKKSAEICVKEHHSQLPNDYQSLLKLPGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130862 118 GRSTAGAILSLSLGKHFPILDGNVKRVLARCYAVSGWPGKKEVE---NKLWSLSEQVTpavgverFNQAMMDLGAMICTr 194
Cdd:PRK13910 81 GAYTANAILCFGFREKSACVDANIKRVLLRLFGLDPNIHAKDLQikaNDFLNLNESFN-------HNQALIDLGALICS- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130862 195 SKPKCSLCPLQNGCIAAAnnswalYPGK---KPKQTLPERTGYFLLLQHEDEVLLaQRPPSGLWGGLYCFPQFADEESLR 271
Cdd:PRK13910 153 PKPKCAICPLNPYCLGKN------NPEKhtlKKKQEIVQEERYLGVVIQNNQIAL-EKIEQKLYLGMHHFPNLKENLEYK 225
|
250 260 270
....*....|....*....|....*....|
gi 16130862 272 qwlaqrqiaadnLTQLTAFRHTFSHFHLDI 301
Cdd:PRK13910 226 ------------LPFLGAIKHSHTKFKLNL 243
|
|
| NUDIX_DNA_Glycosylase_C-MutY |
cd03431 |
C-terminal domain of DNA glycosylase; DNA glycosylase (MutY in bacteria and hMYH in humans) is ... |
229-342 |
1.79e-33 |
|
C-terminal domain of DNA glycosylase; DNA glycosylase (MutY in bacteria and hMYH in humans) is responsible for repairing misread A*oxoG residues to C*G by removing the inappropriately paired adenine base from the DNA backbone. It belongs to the NUDIX hydrolase superfamily and is important for the repair of various genotoxic lesions. Enzymes belonging to this superfamily requires a divalent cation, such as Mg2+ or Mn2+ for their activity. They are also recognized by a highly conserved 23-residue NUDIX motif (GX5EX7REUXEEXGU, where U = I, L or V). However, DNA glycosylase does not seem to contain this signature motif. DNA glycosylase consists of 2 domains: the N-terminal domain contains the catalytic properties of the enzyme and the C-terminal domain affects substrate (oxoG) binding and enzymatic turnover. The C-terminal domain is highly similar to MutT, based on secondary structure and topology, despite low sequence identity. MutT sanitizes the nucleotide precursor pool by hydrolyzing oxo-dGTP to oxo-dGMO and inorganic pyrophosphate. The similarity strongly suggests that the two proteins share a common evolutionary origin.
Pssm-ID: 467537 [Multi-domain] Cd Length: 118 Bit Score: 120.10 E-value: 1.79e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130862 229 PERTGYFLLLQHEDEVLLAQRPPSGLWGGLYCFPQFADEESLRQWLAQRQIAAD----NLTQLTAFRHTFSHFHLDIVPM 304
Cdd:cd03431 2 PERYFTVLVLRDGGRVLLEKRPEKGLLAGLWEFPLVETEEEEEEAEALLGLLAEelllILEPLGEVKHVFSHFRLHITVY 81
|
90 100 110
....*....|....*....|....*....|....*...
gi 16130862 305 WLPVSSFTGcMDEGNALWYNLAQPPSVGLAAPVERLLQ 342
Cdd:cd03431 82 LVELPEAPP-AAPDEGRWVDLEELDEYALPAPMRKLLE 118
|
|
| Nth |
COG0177 |
Endonuclease III [Replication, recombination and repair]; |
28-208 |
9.43e-33 |
|
Endonuclease III [Replication, recombination and repair];
Pssm-ID: 439947 [Multi-domain] Cd Length: 198 Bit Score: 120.59 E-value: 9.43e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130862 28 KTPYKVWLSEVMLQQTQVATVIPYFERFMARFPTVTDLANAPLDEVLHLWTGLGYY-ARARNLHKAAQQVATLHGGKFPE 106
Cdd:COG0177 18 RDPFELLVATILSAQTTDERVNKATPRLFARYPTPEALAAADLEELEELIRPIGLYrNKAKNIIALARILVEKYGGEVPE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130862 107 TFEEVAALPGVGRSTAGAILSLSLGKH-FPIlDGNVKRVLARcyavSGW-PGK--KEVENKLwslsEQVTPAVGVERFNQ 182
Cdd:COG0177 98 TREELESLPGVGRKTANVVLNFAFGKPaIAV-DTHVHRVSNR----LGLvPGKdpEEVEKDL----MKLIPKEYWGDLHH 168
|
170 180
....*....|....*....|....*.
gi 16130862 183 AMMDLGAMICTRSKPKCSLCPLQNGC 208
Cdd:COG0177 169 LLILHGRYICKARKPKCEECPLADLC 194
|
|
| NUDIX_4 |
pfam14815 |
NUDIX domain; |
234-343 |
7.10e-25 |
|
NUDIX domain;
Pssm-ID: 464330 [Multi-domain] Cd Length: 114 Bit Score: 97.38 E-value: 7.10e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130862 234 YFLLLQHEDEVLLAQRPPSGLWGGLYCFPQF--ADEESLRQWLAQRQIAADNLTQLTAFR--HTFSHFHLDIVpmWLPVS 309
Cdd:pfam14815 2 VLVIRNGDGRVLLRKRPEKGLLGGLWEFPGGkvEPGETLEEALARLEELGIEVEVLEPGTvkHVFTHFRLTLH--VYLVR 79
|
90 100 110
....*....|....*....|....*....|....*
gi 16130862 310 SFTGCMDEGNAL-WYNLAQPPSVGLAAPVERLLQQ 343
Cdd:pfam14815 80 EVEGEEEPQQELrWVTPEELDKYALPAAVRKILEA 114
|
|
| nth |
TIGR01083 |
endonuclease III; This equivalog model identifes nth members of the pfam00730 superfamily ... |
28-199 |
8.13e-20 |
|
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: 85.89 E-value: 8.13e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130862 28 KTPYKVWLSEVMLQQTQVATVIPYFERFMARFPTVTDLANAPLDEVLHLWTGLGYY-ARARNLHKAAQQVATLHGGKFPE 106
Cdd:TIGR01083 25 NNPFELLVATILSAQATDKRVNKATPKLFEVYPTPQALAQAGLEELEEYIKSIGLYrNKAKNIIELCRKLVERYGGEVPE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130862 107 TFEEVAALPGVGRSTAGAILSLSLGKHFPILDGNVKRVLARcyavSGW-PGK--KEVENKLwslsEQVTPAVGVERFNQA 183
Cdd:TIGR01083 105 DREELVKLPGVGRKTANVVLNVAFGIPAIAVDTHVFRVSNR----LGLsKGKdpIKVEEDL----MKLVPREFWVKLHHW 176
|
170
....*....|....*.
gi 16130862 184 MMDLGAMICTRSKPKC 199
Cdd:TIGR01083 177 LILHGRYTCKARKPLC 192
|
|
| PRK10702 |
PRK10702 |
endonuclease III; Provisional |
82-208 |
3.98e-11 |
|
endonuclease III; Provisional
Pssm-ID: 182661 [Multi-domain] Cd Length: 211 Bit Score: 61.96 E-value: 3.98e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130862 82 YYARARNLHKAAQQVATLHGGKFPETFEEVAALPGVGRSTAGAILSLSLGKHFPILDGNVKRVlarCYAVSGWPGK--KE 159
Cdd:PRK10702 82 YNSKAENVIKTCRILLEQHNGEVPEDRAALEALPGVGRKTANVVLNTAFGWPTIAVDTHIFRV---CNRTQFAPGKnvEQ 158
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 16130862 160 VENKLWslseQVTPAVGVERFNQAMMDLGAMICTRSKPKCSLCPLQNGC 208
Cdd:PRK10702 159 VEEKLL----KVVPAEFKVDCHHWLILHGRYTCIARKPRCGSCIIEDLC 203
|
|
| AlkA |
COG0122 |
3-methyladenine DNA glycosylase/8-oxoguanine DNA glycosylase [Replication, recombination and ... |
47-161 |
2.54e-08 |
|
3-methyladenine DNA glycosylase/8-oxoguanine DNA glycosylase [Replication, recombination and repair];
Pssm-ID: 439892 [Multi-domain] Cd Length: 255 Bit Score: 54.12 E-value: 2.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130862 47 TVIPYFERFMARFPTVTDLANAPLDEVLHLwtGLGYYaRARNLHKAAQQVAT-------LHGGKFPETFEEVAALPGVGR 119
Cdd:COG0122 115 EPIEGPGGGLYAFPTPEALAAASEEELRAC--GLSRR-KARYLRALARAVADgeldleaLAGLDDEEAIARLTALPGIGP 191
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 16130862 120 STAGAILSLSLGKH--FPILDGNVKRVLARCYAVSGWPGKKEVE 161
Cdd:COG0122 192 WTAEMVLLFALGRPdaFPAGDLGLRRALGRLYGLGERPTPKELR 235
|
|
| HP0602 |
COG2231 |
3-Methyladenine DNA glycosylase, HhH-GPD/Endo3 superfamily [Replication, recombination and ... |
14-214 |
4.10e-07 |
|
3-Methyladenine DNA glycosylase, HhH-GPD/Endo3 superfamily [Replication, recombination and repair];
Pssm-ID: 441832 [Multi-domain] Cd Length: 220 Bit Score: 50.23 E-value: 4.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130862 14 YDKYGRktLPWQIDKTPYKVWLSEVMLQQTQVATVipyfERFMARFP-----TVTDLANAPLDEVLHLWTGLGYYAR-AR 87
Cdd:COG2231 15 LEHYGP--QHWWPAETPFEVIVGAILTQNTSWKNV----EKAIANLKeagllDPEALAALDPEELAELIRPSGFYNQkAK 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130862 88 NLHKAAQQVATLHGGKFPETF--------EEVAALPGVGRSTAGAILSLSLGKH-FPIlDGNVKRVLARcyaVSGWPGKK 158
Cdd:COG2231 89 RLKNLARWLVERYGGGLEKLKalpteelrEELLSLKGIGPETADSILLYAFNRPvFVV-DAYTRRIFSR---LGLIEEDA 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16130862 159 EVEnklwSLSEQVTPAVG--VERFNQ--AMMD-LGAMICtRSKPKCSLCPLQNGCIAAANN 214
Cdd:COG2231 165 SYD----ELQRLFEENLPpdVALYNEfhALIVeHGKEYC-KKKPKCEECPLRDLCPYGGQE 220
|
|
| HHH |
pfam00633 |
Helix-hairpin-helix motif; The helix-hairpin-helix DNA-binding motif is found to be duplicated ... |
100-127 |
2.59e-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: 2.59e-06
10 20
....*....|....*....|....*...
gi 16130862 100 HGGKFPETFEEVAALPGVGRSTAGAILS 127
Cdd:pfam00633 2 LEGLIPASVEELLALPGVGPKTAEAILS 29
|
|
| FES |
smart00525 |
iron-sulpphur binding domain in DNA-(apurinic or apyrimidinic site) lyase (subfamily of ENDO3); ... |
191-211 |
2.36e-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: 37.92 E-value: 2.36e-04
|
| EndIII_4Fe-2S |
pfam10576 |
Iron-sulfur binding domain of endonuclease III; Escherichia coli endonuclease III (EC 4.2.99. ... |
192-208 |
7.92e-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: 36.21 E-value: 7.92e-04
|
| |
