|
Name |
Accession |
Description |
Interval |
E-value |
| PRK10880 |
PRK10880 |
adenine DNA glycosylase; |
2-346 |
0e+00 |
|
adenine DNA glycosylase;
Pssm-ID: 182805 [Multi-domain] Cd Length: 350 Bit Score: 755.01 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367712 2 MEAQQFSQVVLDWYHKYGRKTLPWQQEKTPYHVWLSEVMLQQTQVATVIPYFERFIARFPNVSALAKAPLDEVLHLWTGL 81
Cdd:PRK10880 1 MQASQFSAQVLDWYDKYGRKTLPWQIDKTPYKVWLSEVMLQQTQVATVIPYFERFMARFPTVTDLANAPLDEVLHLWTGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367712 82 GYYARARNLHKAAQHIVDKHQGQFPDTFEDVCALPGVGRSTAGAILSLSLKKPYPILDGNVKRVLARCYAVEGWPGKKEV 161
Cdd:PRK10880 81 GYYARARNLHKAAQQVATLHGGEFPETFEEVAALPGVGRSTAGAILSLSLGKHFPILDGNVKRVLARCYAVSGWPGKKEV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367712 162 ENKLWEISEQVTPTKGVEYFNQAMMDLGAMVCTRTKPKCELCPLNTGCIAYAHHSWADYPGKKPKKAIPEKTTYFLILQY 241
Cdd:PRK10880 161 ENRLWQLSEQVTPAVGVERFNQAMMDLGAMVCTRSKPKCELCPLQNGCIAYANHSWALYPGKKPKQTLPERTGYFLLLQH 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367712 242 DNLVWLDKRPPAGIWGGLFAFPQFETKMLLEQWLTEHGLENNKTEQLISFRHTFSHFHLDIVPICVKLSTFTSLMEAQQG 321
Cdd:PRK10880 241 GDEVWLEQRPPSGLWGGLFCFPQFADEEELRQWLAQRGIAADNLTQLTAFRHTFSHFHLDIVPMWLPVSSFTGCMDEGNG 320
|
330 340
....*....|....*....|....*
gi 490367712 322 LWYNLQTPASVGLAAPVENLLRQLA 346
Cdd:PRK10880 321 LWYNLAQPPSVGLAAPVERLLQQLR 345
|
|
| MutY |
COG1194 |
Adenine-specific DNA glycosylase, acts on AG and A-oxoG pairs [Replication, recombination and ... |
2-346 |
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: 563.22 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367712 2 MEAQQFSQVVLDWYHKYGRkTLPWQQEKTPYHVWLSEVMLQQTQVATVIPYFERFIARFPNVSALAKAPLDEVLHLWTGL 81
Cdd:COG1194 1 MDMASFAKRLLAWYDRHGR-DLPWRQTRDPYRVWLSEIMLQQTQVATVIPYYERFLERFPTVEALAAAPEDEVLKLWEGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367712 82 GYYARARNLHKAAQHIVDKHQGQFPDTFEDVCALPGVGRSTAGAILSLSLKKPYPILDGNVKRVLARCYAVEGWPGKKEV 161
Cdd:COG1194 80 GYYSRARNLHKAAQQVVEEHGGVFPDTYEELLALPGIGPYTAAAIASIAFGEPAPIVDGNVKRVLSRLFAIEGPIGSPAA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367712 162 ENKLWEISEQVTPTKGVEYFNQAMMDLGAMVCTRTKPKCELCPLNTGCIAYAHHSWADYPGKKPKKAIPEKTTYFLILQY 241
Cdd:COG1194 160 KKELWALAEELLPPERPGDFNQALMDLGATVCTPKKPKCLLCPLQDDCAAFAEGRQEELPVKKPKKKKPERYGAALVIRD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367712 242 DNLVWLDKRPPAGIWGGLFAFPQFETK-----MLLEQWLTEH-GLENNKTEQLISFRHTFSHFHLDIVPICVKLSTFTSL 315
Cdd:COG1194 240 DGRVLLEKRPPKGLWGGLWEFPEFEWEeaedpEALERWLREElGLEVEWLEPLGTVRHVFTHFRLHLTVYLARVPAGPPA 319
|
330 340 350
....*....|....*....|....*....|.
gi 490367712 316 mEAQQGLWYNLQTPASVGLAAPVENLLRQLA 346
Cdd:COG1194 320 -EPDGGRWVPLEELAALPLPAPMRKLLKALL 349
|
|
| mutY |
TIGR01084 |
A/G-specific adenine glycosylase; This equivalog model identifies mutY members of the ... |
6-279 |
9.28e-173 |
|
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: 480.75 E-value: 9.28e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367712 6 QFSQVVLDWYHKYGRKTLPWQQEKTPYHVWLSEVMLQQTQVATVIPYFERFIARFPNVSALAKAPLDEVLHLWTGLGYYA 85
Cdd:TIGR01084 1 QFSEDLLSWYDKYGRKTLPWRQNKTPYRVWLSEVMLQQTQVATVIPYFERFLERFPTVQALANAPQDEVLKLWEGLGYYA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367712 86 RARNLHKAAQHIVDKHQGQFPDTFEDVCALPGVGRSTAGAILSLSLKKPYPILDGNVKRVLARCYAVEGWPGKKEVENKL 165
Cdd:TIGR01084 81 RARNLHKAAQEVVEEFGGEFPQDFEDLAALPGVGRYTAGAILSFALNKPYPILDGNVKRVLSRLFAVEGWPGKKKVENRL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367712 166 WEISEQVTPTKGVEYFNQAMMDLGAMVCTRTKPKCELCPLNTGCIAYAHHSWADYPGKKPKKAIPEKTTYFLILQ-YDNL 244
Cdd:TIGR01084 161 WTLAESLLPKADPEAFNQALMDLGAMICTRKKPKCDLCPLQDFCLAYQQGTWEEYPVKKPKAAPPERTTYFLVLQnYDGE 240
|
250 260 270
....*....|....*....|....*....|....*
gi 490367712 245 VWLDKRPPAGIWGGLFAFPQFETKMLLEQWLTEHG 279
Cdd:TIGR01084 241 VLLEQRPEKGLWGGLYCFPQFEDEDSLAFLLAQRG 275
|
|
| ENDO3c |
cd00056 |
endonuclease III; includes endonuclease III (DNA-(apurinic or apyrimidinic site) lyase), ... |
32-189 |
2.91e-55 |
|
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: 177.82 E-value: 2.91e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367712 32 YHVWLSEVMLQQTQVATVIPYFERFIARF-PNVSALAKAPLDEVLHLWTGLGYYARARNLHKAAQHIVDKHQG---QFPD 107
Cdd:cd00056 1 FEVLVSEILSQQTTDKAVNKAYERLFERYgPTPEALAAADEEELRELIRSLGYRRKAKYLKELARAIVEGFGGlvlDDPD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367712 108 TFEDVCALPGVGRSTAGAILSLSLKKPYPILDGNVKRVLARCyaveGWPGKKEVENKLWEISEQVTPTKGVEYFNQAMMD 187
Cdd:cd00056 81 AREELLALPGVGRKTANVVLLFALGPDAFPVDTHVRRVLKRL----GLIPKKKTPEELEELLEELLPKPYWGEANQALMD 156
|
..
gi 490367712 188 LG 189
Cdd:cd00056 157 LG 158
|
|
| ENDO3c |
smart00478 |
endonuclease III; includes endonuclease III (DNA-(apurinic or apyrimidinic site) lyase), ... |
40-191 |
1.53e-48 |
|
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: 160.12 E-value: 1.53e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367712 40 MLQQTQVATVIPYFERFIARFPNVSALAKAPLDEVLHLWTGLG-YYARARNLHKAAQHIVDKHQGQFPDTFEDVCALPGV 118
Cdd:smart00478 1 LSQQTTDERVNKATERLFEKFPTPEDLAAADEEELEELIRGLGfYRRKARYLIELARILVEEYGGEVPDDREELLKLPGV 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490367712 119 GRSTAGAILSLSLKKPYPILDGNVKRVLARCYavegWPGKKEVENKLWEISEQVTPTKGVEYFNQAMMDLGAM 191
Cdd:smart00478 81 GRKTANAVLSFALGKPFIPVDTHVLRIAKRLG----LVDKKSTPEEVEKLLEKLLPEEDWRELNLLLIDFGRT 149
|
|
| HhH-GPD |
pfam00730 |
HhH-GPD superfamily base excision DNA repair protein; This family contains a diverse range of ... |
36-171 |
1.88e-43 |
|
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: 146.66 E-value: 1.88e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367712 36 LSEVMLQQTQVATVIPYFERFIAR-FPNVSALAKAPLDEVLHLWTGLGYYAR-ARNLHKAAQHIVDKHQGQFPDTF-EDV 112
Cdd:pfam00730 1 VSAILSQQTSDKAVNKITERLFEKfFPTPEDLADADEEELRELIRGLGFYRRkAKYLKELARILVEGYGGEVPLDEeELE 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490367712 113 CALPGVGRSTAGAILSLSL--KKPYPILDGNVKRVLARCYAVEGWPGKKEVENKLWEISEQ 171
Cdd:pfam00730 81 ALLKGVGRWTAEAVLIFALgrPDPLPVVDTHVRRVLKRLGLIKEKPTPKEVERELEELWPP 141
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK10880 |
PRK10880 |
adenine DNA glycosylase; |
2-346 |
0e+00 |
|
adenine DNA glycosylase;
Pssm-ID: 182805 [Multi-domain] Cd Length: 350 Bit Score: 755.01 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367712 2 MEAQQFSQVVLDWYHKYGRKTLPWQQEKTPYHVWLSEVMLQQTQVATVIPYFERFIARFPNVSALAKAPLDEVLHLWTGL 81
Cdd:PRK10880 1 MQASQFSAQVLDWYDKYGRKTLPWQIDKTPYKVWLSEVMLQQTQVATVIPYFERFMARFPTVTDLANAPLDEVLHLWTGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367712 82 GYYARARNLHKAAQHIVDKHQGQFPDTFEDVCALPGVGRSTAGAILSLSLKKPYPILDGNVKRVLARCYAVEGWPGKKEV 161
Cdd:PRK10880 81 GYYARARNLHKAAQQVATLHGGEFPETFEEVAALPGVGRSTAGAILSLSLGKHFPILDGNVKRVLARCYAVSGWPGKKEV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367712 162 ENKLWEISEQVTPTKGVEYFNQAMMDLGAMVCTRTKPKCELCPLNTGCIAYAHHSWADYPGKKPKKAIPEKTTYFLILQY 241
Cdd:PRK10880 161 ENRLWQLSEQVTPAVGVERFNQAMMDLGAMVCTRSKPKCELCPLQNGCIAYANHSWALYPGKKPKQTLPERTGYFLLLQH 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367712 242 DNLVWLDKRPPAGIWGGLFAFPQFETKMLLEQWLTEHGLENNKTEQLISFRHTFSHFHLDIVPICVKLSTFTSLMEAQQG 321
Cdd:PRK10880 241 GDEVWLEQRPPSGLWGGLFCFPQFADEEELRQWLAQRGIAADNLTQLTAFRHTFSHFHLDIVPMWLPVSSFTGCMDEGNG 320
|
330 340
....*....|....*....|....*
gi 490367712 322 LWYNLQTPASVGLAAPVENLLRQLA 346
Cdd:PRK10880 321 LWYNLAQPPSVGLAAPVERLLQQLR 345
|
|
| MutY |
COG1194 |
Adenine-specific DNA glycosylase, acts on AG and A-oxoG pairs [Replication, recombination and ... |
2-346 |
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: 563.22 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367712 2 MEAQQFSQVVLDWYHKYGRkTLPWQQEKTPYHVWLSEVMLQQTQVATVIPYFERFIARFPNVSALAKAPLDEVLHLWTGL 81
Cdd:COG1194 1 MDMASFAKRLLAWYDRHGR-DLPWRQTRDPYRVWLSEIMLQQTQVATVIPYYERFLERFPTVEALAAAPEDEVLKLWEGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367712 82 GYYARARNLHKAAQHIVDKHQGQFPDTFEDVCALPGVGRSTAGAILSLSLKKPYPILDGNVKRVLARCYAVEGWPGKKEV 161
Cdd:COG1194 80 GYYSRARNLHKAAQQVVEEHGGVFPDTYEELLALPGIGPYTAAAIASIAFGEPAPIVDGNVKRVLSRLFAIEGPIGSPAA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367712 162 ENKLWEISEQVTPTKGVEYFNQAMMDLGAMVCTRTKPKCELCPLNTGCIAYAHHSWADYPGKKPKKAIPEKTTYFLILQY 241
Cdd:COG1194 160 KKELWALAEELLPPERPGDFNQALMDLGATVCTPKKPKCLLCPLQDDCAAFAEGRQEELPVKKPKKKKPERYGAALVIRD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367712 242 DNLVWLDKRPPAGIWGGLFAFPQFETK-----MLLEQWLTEH-GLENNKTEQLISFRHTFSHFHLDIVPICVKLSTFTSL 315
Cdd:COG1194 240 DGRVLLEKRPPKGLWGGLWEFPEFEWEeaedpEALERWLREElGLEVEWLEPLGTVRHVFTHFRLHLTVYLARVPAGPPA 319
|
330 340 350
....*....|....*....|....*....|.
gi 490367712 316 mEAQQGLWYNLQTPASVGLAAPVENLLRQLA 346
Cdd:COG1194 320 -EPDGGRWVPLEELAALPLPAPMRKLLKALL 349
|
|
| mutY |
TIGR01084 |
A/G-specific adenine glycosylase; This equivalog model identifies mutY members of the ... |
6-279 |
9.28e-173 |
|
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: 480.75 E-value: 9.28e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367712 6 QFSQVVLDWYHKYGRKTLPWQQEKTPYHVWLSEVMLQQTQVATVIPYFERFIARFPNVSALAKAPLDEVLHLWTGLGYYA 85
Cdd:TIGR01084 1 QFSEDLLSWYDKYGRKTLPWRQNKTPYRVWLSEVMLQQTQVATVIPYFERFLERFPTVQALANAPQDEVLKLWEGLGYYA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367712 86 RARNLHKAAQHIVDKHQGQFPDTFEDVCALPGVGRSTAGAILSLSLKKPYPILDGNVKRVLARCYAVEGWPGKKEVENKL 165
Cdd:TIGR01084 81 RARNLHKAAQEVVEEFGGEFPQDFEDLAALPGVGRYTAGAILSFALNKPYPILDGNVKRVLSRLFAVEGWPGKKKVENRL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367712 166 WEISEQVTPTKGVEYFNQAMMDLGAMVCTRTKPKCELCPLNTGCIAYAHHSWADYPGKKPKKAIPEKTTYFLILQ-YDNL 244
Cdd:TIGR01084 161 WTLAESLLPKADPEAFNQALMDLGAMICTRKKPKCDLCPLQDFCLAYQQGTWEEYPVKKPKAAPPERTTYFLVLQnYDGE 240
|
250 260 270
....*....|....*....|....*....|....*
gi 490367712 245 VWLDKRPPAGIWGGLFAFPQFETKMLLEQWLTEHG 279
Cdd:TIGR01084 241 VLLEQRPEKGLWGGLYCFPQFEDEDSLAFLLAQRG 275
|
|
| ENDO3c |
cd00056 |
endonuclease III; includes endonuclease III (DNA-(apurinic or apyrimidinic site) lyase), ... |
32-189 |
2.91e-55 |
|
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: 177.82 E-value: 2.91e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367712 32 YHVWLSEVMLQQTQVATVIPYFERFIARF-PNVSALAKAPLDEVLHLWTGLGYYARARNLHKAAQHIVDKHQG---QFPD 107
Cdd:cd00056 1 FEVLVSEILSQQTTDKAVNKAYERLFERYgPTPEALAAADEEELRELIRSLGYRRKAKYLKELARAIVEGFGGlvlDDPD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367712 108 TFEDVCALPGVGRSTAGAILSLSLKKPYPILDGNVKRVLARCyaveGWPGKKEVENKLWEISEQVTPTKGVEYFNQAMMD 187
Cdd:cd00056 81 AREELLALPGVGRKTANVVLLFALGPDAFPVDTHVRRVLKRL----GLIPKKKTPEELEELLEELLPKPYWGEANQALMD 156
|
..
gi 490367712 188 LG 189
Cdd:cd00056 157 LG 158
|
|
| ENDO3c |
smart00478 |
endonuclease III; includes endonuclease III (DNA-(apurinic or apyrimidinic site) lyase), ... |
40-191 |
1.53e-48 |
|
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: 160.12 E-value: 1.53e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367712 40 MLQQTQVATVIPYFERFIARFPNVSALAKAPLDEVLHLWTGLG-YYARARNLHKAAQHIVDKHQGQFPDTFEDVCALPGV 118
Cdd:smart00478 1 LSQQTTDERVNKATERLFEKFPTPEDLAAADEEELEELIRGLGfYRRKARYLIELARILVEEYGGEVPDDREELLKLPGV 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490367712 119 GRSTAGAILSLSLKKPYPILDGNVKRVLARCYavegWPGKKEVENKLWEISEQVTPTKGVEYFNQAMMDLGAM 191
Cdd:smart00478 81 GRKTANAVLSFALGKPFIPVDTHVLRIAKRLG----LVDKKSTPEEVEKLLEKLLPEEDWRELNLLLIDFGRT 149
|
|
| HhH-GPD |
pfam00730 |
HhH-GPD superfamily base excision DNA repair protein; This family contains a diverse range of ... |
36-171 |
1.88e-43 |
|
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: 146.66 E-value: 1.88e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367712 36 LSEVMLQQTQVATVIPYFERFIAR-FPNVSALAKAPLDEVLHLWTGLGYYAR-ARNLHKAAQHIVDKHQGQFPDTF-EDV 112
Cdd:pfam00730 1 VSAILSQQTSDKAVNKITERLFEKfFPTPEDLADADEEELRELIRGLGFYRRkAKYLKELARILVEGYGGEVPLDEeELE 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490367712 113 CALPGVGRSTAGAILSLSL--KKPYPILDGNVKRVLARCYAVEGWPGKKEVENKLWEISEQ 171
Cdd:pfam00730 81 ALLKGVGRWTAEAVLIFALgrPDPLPVVDTHVRRVLKRLGLIKEKPTPKEVERELEELWPP 141
|
|
| PRK13910 |
PRK13910 |
DNA glycosylase MutY; Provisional |
40-269 |
1.26e-37 |
|
DNA glycosylase MutY; Provisional
Pssm-ID: 172427 [Multi-domain] Cd Length: 289 Bit Score: 136.31 E-value: 1.26e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367712 40 MLQQTQVATVIP-YFERFIARFPNVSALAKAPLDEVLHLWTGLGYYARARNLHKAAQHIVDKHQGQFPDTFEDVCALPGV 118
Cdd:PRK13910 1 MSQQTQINTVVErFYSPFLEAFPTLKDLANAPLEEVLLLWRGLGYYSRAKNLKKSAEICVKEHHSQLPNDYQSLLKLPGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367712 119 GRSTAGAILSLSLKKPYPILDGNVKRVLARCYAVEGWPGKKEVE---NKLWEISEQVTptkgveyFNQAMMDLGAMVCTr 195
Cdd:PRK13910 81 GAYTANAILCFGFREKSACVDANIKRVLLRLFGLDPNIHAKDLQikaNDFLNLNESFN-------HNQALIDLGALICS- 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490367712 196 TKPKCELCPLNTGCIAYAHhswADYPGKKPKKAIPEKTTYFLILQYDNLVWLDKRPPAgIWGGLFAFPQFETKM 269
Cdd:PRK13910 153 PKPKCAICPLNPYCLGKNN---PEKHTLKKKQEIVQEERYLGVVIQNNQIALEKIEQK-LYLGMHHFPNLKENL 222
|
|
| Nth |
COG0177 |
Endonuclease III [Replication, recombination and repair]; |
29-209 |
1.18e-34 |
|
Endonuclease III [Replication, recombination and repair];
Pssm-ID: 439947 [Multi-domain] Cd Length: 198 Bit Score: 125.59 E-value: 1.18e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367712 29 KTPYHVWLSEVMLQQTQVATVIPYFERFIARFPNVSALAKAPLDEVLHLWTGLGYY-ARARNLHKAAQHIVDKHQGQFPD 107
Cdd:COG0177 18 RDPFELLVATILSAQTTDERVNKATPRLFARYPTPEALAAADLEELEELIRPIGLYrNKAKNIIALARILVEKYGGEVPE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367712 108 TFEDVCALPGVGRSTAGAILSLSLKKPYPILDGNVKRVLARCyaveGW-PGK--KEVENKLweisEQVTPTKGVEYFNQA 184
Cdd:COG0177 98 TREELESLPGVGRKTANVVLNFAFGKPAIAVDTHVHRVSNRL----GLvPGKdpEEVEKDL----MKLIPKEYWGDLHHL 169
|
170 180
....*....|....*....|....*
gi 490367712 185 MMDLGAMVCTRTKPKCELCPLNTGC 209
Cdd:COG0177 170 LILHGRYICKARKPKCEECPLADLC 194
|
|
| NUDIX_DNA_Glycosylase_C-MutY |
cd03431 |
C-terminal domain of DNA glycosylase; DNA glycosylase (MutY in bacteria and hMYH in humans) is ... |
229-342 |
7.38e-30 |
|
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: 110.47 E-value: 7.38e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367712 229 IPEKTTYFLILQYDNLVWLDKRPPAGIWGGLFAFPQFETKMLLEQWLTEHGLE----NNKTEQLISFRHTFSHFHLDIVP 304
Cdd:cd03431 1 VPERYFTVLVLRDGGRVLLEKRPEKGLLAGLWEFPLVETEEEEEEAEALLGLLaeelLLILEPLGEVKHVFSHFRLHITV 80
|
90 100 110
....*....|....*....|....*....|....*...
gi 490367712 305 ICVKLSTfTSLMEAQQGLWYNLQTPASVGLAAPVENLL 342
Cdd:cd03431 81 YLVELPE-APPAAPDEGRWVDLEELDEYALPAPMRKLL 117
|
|
| nth |
TIGR01083 |
endonuclease III; This equivalog model identifes nth members of the pfam00730 superfamily ... |
29-200 |
4.06e-21 |
|
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: 89.36 E-value: 4.06e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367712 29 KTPYHVWLSEVMLQQTQVATVIPYFERFIARFPNVSALAKAPLDEVLHLWTGLGYY-ARARNLHKAAQHIVDKHQGQFPD 107
Cdd:TIGR01083 25 NNPFELLVATILSAQATDKRVNKATPKLFEVYPTPQALAQAGLEELEEYIKSIGLYrNKAKNIIELCRKLVERYGGEVPE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367712 108 TFEDVCALPGVGRSTAGAILSLSLKKPYPILDGNVKRVLARCyaveGW-PGK--KEVENKLWEiseqVTPTKGVEYFNQA 184
Cdd:TIGR01083 105 DREELVKLPGVGRKTANVVLNVAFGIPAIAVDTHVFRVSNRL----GLsKGKdpIKVEEDLMK----LVPREFWVKLHHW 176
|
170
....*....|....*.
gi 490367712 185 MMDLGAMVCTRTKPKC 200
Cdd:TIGR01083 177 LILHGRYTCKARKPLC 192
|
|
| NUDIX_4 |
pfam14815 |
NUDIX domain; |
234-344 |
3.55e-20 |
|
NUDIX domain;
Pssm-ID: 464330 [Multi-domain] Cd Length: 114 Bit Score: 84.67 E-value: 3.55e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367712 234 TYFLILQYDNLVWLDKRPPAGIWGGLFAFPQF--ETKMLLEQWL---TEHGLENNKTEQlISFRHTFSHFHLDI-VPICV 307
Cdd:pfam14815 1 AVLVIRNGDGRVLLRKRPEKGLLGGLWEFPGGkvEPGETLEEALarlEELGIEVEVLEP-GTVKHVFTHFRLTLhVYLVR 79
|
90 100 110
....*....|....*....|....*....|....*..
gi 490367712 308 KLSTFTSlmEAQQGLWYNLQTPASVGLAAPVENLLRQ 344
Cdd:pfam14815 80 EVEGEEE--PQQELRWVTPEELDKYALPAAVRKILEA 114
|
|
| PRK10702 |
PRK10702 |
endonuclease III; Provisional |
83-209 |
1.31e-10 |
|
endonuclease III; Provisional
Pssm-ID: 182661 [Multi-domain] Cd Length: 211 Bit Score: 60.42 E-value: 1.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367712 83 YYARARNLHKAAQHIVDKHQGQFPDTFEDVCALPGVGRSTAGAILSLSLKKPYPILDGNVKRVlarCYAVEGWPGK--KE 160
Cdd:PRK10702 82 YNSKAENVIKTCRILLEQHNGEVPEDRAALEALPGVGRKTANVVLNTAFGWPTIAVDTHIFRV---CNRTQFAPGKnvEQ 158
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 490367712 161 VENKLWeiseQVTPTKGVEYFNQAMMDLGAMVCTRTKPKCELCPLNTGC 209
Cdd:PRK10702 159 VEEKLL----KVVPAEFKVDCHHWLILHGRYTCIARKPRCGSCIIEDLC 203
|
|
| HP0602 |
COG2231 |
3-Methyladenine DNA glycosylase, HhH-GPD/Endo3 superfamily [Replication, recombination and ... |
1-216 |
1.75e-08 |
|
3-Methyladenine DNA glycosylase, HhH-GPD/Endo3 superfamily [Replication, recombination and repair];
Pssm-ID: 441832 [Multi-domain] Cd Length: 220 Bit Score: 54.08 E-value: 1.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367712 1 MMEAQQFSQVVLDWYHKYGRktLPWQQEKTPYHVWLSEVMLQQTQVATVipyfERFIARFPN-----VSALAKAPLDEVL 75
Cdd:COG2231 1 MNTKEDLLEIYERLLEHYGP--QHWWPAETPFEVIVGAILTQNTSWKNV----EKAIANLKEaglldPEALAALDPEELA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367712 76 HLWTGLGYYAR-ARNLHKAAQHIVDKHQGQFPDTF--------EDVCALPGVGRSTAGAILSLSLKKPYPILDGNVKRVL 146
Cdd:COG2231 75 ELIRPSGFYNQkAKRLKNLARWLVERYGGGLEKLKalpteelrEELLSLKGIGPETADSILLYAFNRPVFVVDAYTRRIF 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490367712 147 ARCYAVEGWPGKKEVENKLweisEQVTPtKGVEYFNQ--AMMD-LGAMVCtRTKPKCELCPLNTGCiAYAHHS 216
Cdd:COG2231 155 SRLGLIEEDASYDELQRLF----EENLP-PDVALYNEfhALIVeHGKEYC-KKKPKCEECPLRDLC-PYGGQE 220
|
|
| AlkA |
COG0122 |
3-methyladenine DNA glycosylase/8-oxoguanine DNA glycosylase [Replication, recombination and ... |
48-162 |
2.53e-07 |
|
3-methyladenine DNA glycosylase/8-oxoguanine DNA glycosylase [Replication, recombination and repair];
Pssm-ID: 439892 [Multi-domain] Cd Length: 255 Bit Score: 51.04 E-value: 2.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367712 48 TVIPYFERFIARFPNVSALAKAPLDEVLHLwtGLGYYaRARNLHKAAQHIVDK--HQGQFPD-TFEDV----CALPGVGR 120
Cdd:COG0122 115 EPIEGPGGGLYAFPTPEALAAASEEELRAC--GLSRR-KARYLRALARAVADGelDLEALAGlDDEEAiarlTALPGIGP 191
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 490367712 121 STAGAILSLSLKKP--YPILDGNVKRVLARCYAVEGWPGKKEVE 162
Cdd:COG0122 192 WTAEMVLLFALGRPdaFPAGDLGLRRALGRLYGLGERPTPKELR 235
|
|
| HHH |
pfam00633 |
Helix-hairpin-helix motif; The helix-hairpin-helix DNA-binding motif is found to be duplicated ... |
100-128 |
3.54e-07 |
|
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: 45.87 E-value: 3.54e-07
10 20
....*....|....*....|....*....
gi 490367712 100 KHQGQFPDTFEDVCALPGVGRSTAGAILS 128
Cdd:pfam00633 1 SLEGLIPASVEELLALPGVGPKTAEAILS 29
|
|
| FES |
smart00525 |
iron-sulpphur binding domain in DNA-(apurinic or apyrimidinic site) lyase (subfamily of ENDO3); ... |
192-212 |
8.51e-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: 39.07 E-value: 8.51e-05
|
| EndIII_4Fe-2S |
pfam10576 |
Iron-sulfur binding domain of endonuclease III; Escherichia coli endonuclease III (EC 4.2.99. ... |
193-209 |
1.45e-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: 35.44 E-value: 1.45e-03
|
| ogg |
TIGR00588 |
8-oxoguanine DNA-glycosylase (ogg); All proteins in this family for which functions are known ... |
60-150 |
8.71e-03 |
|
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: 37.58 E-value: 8.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490367712 60 FPNVSALAKAPLDEVLHLwTGLGYyaRARNLHKAAQHIVDKHQG----------QFPDTFEDVCALPGVGRSTAGAILSL 129
Cdd:TIGR00588 163 FPSLHALTGPEAEAHLRK-LGLGY--RARYIRETARALLEEQGGrawlqqirgaSYEDAREALCELPGVGPKVADCICLM 239
|
90 100
....*....|....*....|...
gi 490367712 130 SLKKP--YPIlDGNVKRVLARCY 150
Cdd:TIGR00588 240 GLDKPqaVPV-DVHVWRIANRDY 261
|
|
|