|
Name |
Accession |
Description |
Interval |
E-value |
| PRK10880 |
PRK10880 |
adenine DNA glycosylase; |
2-351 |
0e+00 |
|
adenine DNA glycosylase;
Pssm-ID: 182805 [Multi-domain] Cd Length: 350 Bit Score: 790.06 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501072796 2 MQAQQFSRQVLDWYDKYGRKTLPWQQEKTPYKVWLSEVMLQQTQVTTVIPYFERFMARFPDVTALANAPLDDVLHLWTGL 81
Cdd:PRK10880 1 MQASQFSAQVLDWYDKYGRKTLPWQIDKTPYKVWLSEVMLQQTQVATVIPYFERFMARFPTVTDLANAPLDEVLHLWTGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501072796 82 GYYARARNLHKAAQQVATLHGGKFPETFEEVAALPGVGRSTAGAVLSLSLGKHFPILDGNVKRVLARCYAVEGWPGKKEV 161
Cdd:PRK10880 81 GYYARARNLHKAAQQVATLHGGEFPETFEEVAALPGVGRSTAGAILSLSLGKHFPILDGNVKRVLARCYAVSGWPGKKEV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501072796 162 ENRLWQISETVTPAEGVARFNQAMMDLGAMVCTRSKPKCEICPLNNGCEAFAHQSYAKYPGKKPKQILPEKTGYFLLLQH 241
Cdd:PRK10880 161 ENRLWQLSEQVTPAVGVERFNQAMMDLGAMVCTRSKPKCELCPLQNGCIAYANHSWALYPGKKPKQTLPERTGYFLLLQH 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501072796 242 EGALFLQQRPPVGLWGGLYCFPQFESETALREWLSARGINDDGLTQLTAFRHTFSHFHLDIVPMWLGVQQTAACMDEASG 321
Cdd:PRK10880 241 GDEVWLEQRPPSGLWGGLFCFPQFADEEELRQWLAQRGIAADNLTQLTAFRHTFSHFHLDIVPMWLPVSSFTGCMDEGNG 320
|
330 340 350
....*....|....*....|....*....|
gi 501072796 322 LWYNLAQPPAVGLAAPVERLLQQVRAEPVA 351
Cdd:PRK10880 321 LWYNLAQPPSVGLAAPVERLLQQLRTGAPV 350
|
|
| MutY |
COG1194 |
Adenine-specific DNA glycosylase, acts on AG and A-oxoG pairs [Replication, recombination and ... |
2-347 |
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: 562.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501072796 2 MQAQQFSRQVLDWYDKYGRkTLPWQQEKTPYKVWLSEVMLQQTQVTTVIPYFERFMARFPDVTALANAPLDDVLHLWTGL 81
Cdd:COG1194 1 MDMASFAKRLLAWYDRHGR-DLPWRQTRDPYRVWLSEIMLQQTQVATVIPYYERFLERFPTVEALAAAPEDEVLKLWEGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501072796 82 GYYARARNLHKAAQQVATLHGGKFPETFEEVAALPGVGRSTAGAVLSLSLGKHFPILDGNVKRVLARCYAVEGWPGKKEV 161
Cdd:COG1194 80 GYYSRARNLHKAAQQVVEEHGGVFPDTYEELLALPGIGPYTAAAIASIAFGEPAPIVDGNVKRVLSRLFAIEGPIGSPAA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501072796 162 ENRLWQISETVTPAEGVARFNQAMMDLGAMVCTRSKPKCEICPLNNGCEAFAHQSYAKYPGKKPKQILPEKTGYFLLLQH 241
Cdd:COG1194 160 KKELWALAEELLPPERPGDFNQALMDLGATVCTPKKPKCLLCPLQDDCAAFAEGRQEELPVKKPKKKKPERYGAALVIRD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501072796 242 EGALFLQQRPPVGLWGGLYCFPQFESETA-----LREWLSAR-GINDDGLTQLTAFRHTFSHFHLDIVPMWLGVQQTAAC 315
Cdd:COG1194 240 DGRVLLEKRPPKGLWGGLWEFPEFEWEEAedpeaLERWLREElGLEVEWLEPLGTVRHVFTHFRLHLTVYLARVPAGPPA 319
|
330 340 350
....*....|....*....|....*....|..
gi 501072796 316 mDEASGLWYNLAQPPAVGLAAPVERLLQQVRA 347
Cdd:COG1194 320 -EPDGGRWVPLEELAALPLPAPMRKLLKALLK 350
|
|
| mutY |
TIGR01084 |
A/G-specific adenine glycosylase; This equivalog model identifies mutY members of the ... |
6-279 |
9.04e-177 |
|
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: 491.54 E-value: 9.04e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501072796 6 QFSRQVLDWYDKYGRKTLPWQQEKTPYKVWLSEVMLQQTQVTTVIPYFERFMARFPDVTALANAPLDDVLHLWTGLGYYA 85
Cdd:TIGR01084 1 QFSEDLLSWYDKYGRKTLPWRQNKTPYRVWLSEVMLQQTQVATVIPYFERFLERFPTVQALANAPQDEVLKLWEGLGYYA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501072796 86 RARNLHKAAQQVATLHGGKFPETFEEVAALPGVGRSTAGAVLSLSLGKHFPILDGNVKRVLARCYAVEGWPGKKEVENRL 165
Cdd:TIGR01084 81 RARNLHKAAQEVVEEFGGEFPQDFEDLAALPGVGRYTAGAILSFALNKPYPILDGNVKRVLSRLFAVEGWPGKKKVENRL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501072796 166 WQISETVTPAEGVARFNQAMMDLGAMVCTRSKPKCEICPLNNGCEAFAHQSYAKYPGKKPKQILPEKTGYFLLLQHE-GA 244
Cdd:TIGR01084 161 WTLAESLLPKADPEAFNQALMDLGAMICTRKKPKCDLCPLQDFCLAYQQGTWEEYPVKKPKAAPPERTTYFLVLQNYdGE 240
|
250 260 270
....*....|....*....|....*....|....*
gi 501072796 245 LFLQQRPPVGLWGGLYCFPQFESETALREWLSARG 279
Cdd:TIGR01084 241 VLLEQRPEKGLWGGLYCFPQFEDEDSLAFLLAQRG 275
|
|
| ENDO3c |
cd00056 |
endonuclease III; includes endonuclease III (DNA-(apurinic or apyrimidinic site) lyase), ... |
32-189 |
4.45e-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: 164.72 E-value: 4.45e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501072796 32 YKVWLSEVMLQQTQVTTVIPYFERFMARF-PDVTALANAPLDDVLHLWTGLGYYARARNLHKAAQQVATLHGGKF---PE 107
Cdd:cd00056 1 FEVLVSEILSQQTTDKAVNKAYERLFERYgPTPEALAAADEEELRELIRSLGYRRKAKYLKELARAIVEGFGGLVlddPD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501072796 108 TFEEVAALPGVGRSTAGAVLSLSLGKHFPILDGNVKRVLARCyaveGWPGKKEVENRLWQISETVTPAEGVARFNQAMMD 187
Cdd:cd00056 81 AREELLALPGVGRKTANVVLLFALGPDAFPVDTHVRRVLKRL----GLIPKKKTPEELEELLEELLPKPYWGEANQALMD 156
|
..
gi 501072796 188 LG 189
Cdd:cd00056 157 LG 158
|
|
| ENDO3c |
smart00478 |
endonuclease III; includes endonuclease III (DNA-(apurinic or apyrimidinic site) lyase), ... |
40-191 |
1.76e-47 |
|
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: 1.76e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501072796 40 MLQQTQVTTVIPYFERFMARFPDVTALANAPLDDVLHLWTGLG-YYARARNLHKAAQQVATLHGGKFPETFEEVAALPGV 118
Cdd:smart00478 1 LSQQTTDERVNKATERLFEKFPTPEDLAAADEEELEELIRGLGfYRRKARYLIELARILVEEYGGEVPDDREELLKLPGV 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 501072796 119 GRSTAGAVLSLSLGKHFPILDGNVKRVLARCYavegWPGKKEVENRLWQISETVTPAEGVARFNQAMMDLGAM 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 ... |
36-168 |
4.74e-42 |
|
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: 143.58 E-value: 4.74e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501072796 36 LSEVMLQQTQVTTVIPYFERFMAR-FPDVTALANAPLDDVLHLWTGLGYYAR-ARNLHKAAQQVATLHGGKFPETFEE-V 112
Cdd:pfam00730 1 VSAILSQQTSDKAVNKITERLFEKfFPTPEDLADADEEELRELIRGLGFYRRkAKYLKELARILVEGYGGEVPLDEEElE 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 501072796 113 AALPGVGRSTAGAVLSLSLG--KHFPILDGNVKRVLARCYAVEGWPGKKEVENRLWQI 168
Cdd:pfam00730 81 ALLKGVGRWTAEAVLIFALGrpDPLPVVDTHVRRVLKRLGLIKEKPTPKEVERELEEL 138
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK10880 |
PRK10880 |
adenine DNA glycosylase; |
2-351 |
0e+00 |
|
adenine DNA glycosylase;
Pssm-ID: 182805 [Multi-domain] Cd Length: 350 Bit Score: 790.06 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501072796 2 MQAQQFSRQVLDWYDKYGRKTLPWQQEKTPYKVWLSEVMLQQTQVTTVIPYFERFMARFPDVTALANAPLDDVLHLWTGL 81
Cdd:PRK10880 1 MQASQFSAQVLDWYDKYGRKTLPWQIDKTPYKVWLSEVMLQQTQVATVIPYFERFMARFPTVTDLANAPLDEVLHLWTGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501072796 82 GYYARARNLHKAAQQVATLHGGKFPETFEEVAALPGVGRSTAGAVLSLSLGKHFPILDGNVKRVLARCYAVEGWPGKKEV 161
Cdd:PRK10880 81 GYYARARNLHKAAQQVATLHGGEFPETFEEVAALPGVGRSTAGAILSLSLGKHFPILDGNVKRVLARCYAVSGWPGKKEV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501072796 162 ENRLWQISETVTPAEGVARFNQAMMDLGAMVCTRSKPKCEICPLNNGCEAFAHQSYAKYPGKKPKQILPEKTGYFLLLQH 241
Cdd:PRK10880 161 ENRLWQLSEQVTPAVGVERFNQAMMDLGAMVCTRSKPKCELCPLQNGCIAYANHSWALYPGKKPKQTLPERTGYFLLLQH 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501072796 242 EGALFLQQRPPVGLWGGLYCFPQFESETALREWLSARGINDDGLTQLTAFRHTFSHFHLDIVPMWLGVQQTAACMDEASG 321
Cdd:PRK10880 241 GDEVWLEQRPPSGLWGGLFCFPQFADEEELRQWLAQRGIAADNLTQLTAFRHTFSHFHLDIVPMWLPVSSFTGCMDEGNG 320
|
330 340 350
....*....|....*....|....*....|
gi 501072796 322 LWYNLAQPPAVGLAAPVERLLQQVRAEPVA 351
Cdd:PRK10880 321 LWYNLAQPPSVGLAAPVERLLQQLRTGAPV 350
|
|
| MutY |
COG1194 |
Adenine-specific DNA glycosylase, acts on AG and A-oxoG pairs [Replication, recombination and ... |
2-347 |
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: 562.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501072796 2 MQAQQFSRQVLDWYDKYGRkTLPWQQEKTPYKVWLSEVMLQQTQVTTVIPYFERFMARFPDVTALANAPLDDVLHLWTGL 81
Cdd:COG1194 1 MDMASFAKRLLAWYDRHGR-DLPWRQTRDPYRVWLSEIMLQQTQVATVIPYYERFLERFPTVEALAAAPEDEVLKLWEGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501072796 82 GYYARARNLHKAAQQVATLHGGKFPETFEEVAALPGVGRSTAGAVLSLSLGKHFPILDGNVKRVLARCYAVEGWPGKKEV 161
Cdd:COG1194 80 GYYSRARNLHKAAQQVVEEHGGVFPDTYEELLALPGIGPYTAAAIASIAFGEPAPIVDGNVKRVLSRLFAIEGPIGSPAA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501072796 162 ENRLWQISETVTPAEGVARFNQAMMDLGAMVCTRSKPKCEICPLNNGCEAFAHQSYAKYPGKKPKQILPEKTGYFLLLQH 241
Cdd:COG1194 160 KKELWALAEELLPPERPGDFNQALMDLGATVCTPKKPKCLLCPLQDDCAAFAEGRQEELPVKKPKKKKPERYGAALVIRD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501072796 242 EGALFLQQRPPVGLWGGLYCFPQFESETA-----LREWLSAR-GINDDGLTQLTAFRHTFSHFHLDIVPMWLGVQQTAAC 315
Cdd:COG1194 240 DGRVLLEKRPPKGLWGGLWEFPEFEWEEAedpeaLERWLREElGLEVEWLEPLGTVRHVFTHFRLHLTVYLARVPAGPPA 319
|
330 340 350
....*....|....*....|....*....|..
gi 501072796 316 mDEASGLWYNLAQPPAVGLAAPVERLLQQVRA 347
Cdd:COG1194 320 -EPDGGRWVPLEELAALPLPAPMRKLLKALLK 350
|
|
| mutY |
TIGR01084 |
A/G-specific adenine glycosylase; This equivalog model identifies mutY members of the ... |
6-279 |
9.04e-177 |
|
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: 491.54 E-value: 9.04e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501072796 6 QFSRQVLDWYDKYGRKTLPWQQEKTPYKVWLSEVMLQQTQVTTVIPYFERFMARFPDVTALANAPLDDVLHLWTGLGYYA 85
Cdd:TIGR01084 1 QFSEDLLSWYDKYGRKTLPWRQNKTPYRVWLSEVMLQQTQVATVIPYFERFLERFPTVQALANAPQDEVLKLWEGLGYYA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501072796 86 RARNLHKAAQQVATLHGGKFPETFEEVAALPGVGRSTAGAVLSLSLGKHFPILDGNVKRVLARCYAVEGWPGKKEVENRL 165
Cdd:TIGR01084 81 RARNLHKAAQEVVEEFGGEFPQDFEDLAALPGVGRYTAGAILSFALNKPYPILDGNVKRVLSRLFAVEGWPGKKKVENRL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501072796 166 WQISETVTPAEGVARFNQAMMDLGAMVCTRSKPKCEICPLNNGCEAFAHQSYAKYPGKKPKQILPEKTGYFLLLQHE-GA 244
Cdd:TIGR01084 161 WTLAESLLPKADPEAFNQALMDLGAMICTRKKPKCDLCPLQDFCLAYQQGTWEEYPVKKPKAAPPERTTYFLVLQNYdGE 240
|
250 260 270
....*....|....*....|....*....|....*
gi 501072796 245 LFLQQRPPVGLWGGLYCFPQFESETALREWLSARG 279
Cdd:TIGR01084 241 VLLEQRPEKGLWGGLYCFPQFEDEDSLAFLLAQRG 275
|
|
| ENDO3c |
cd00056 |
endonuclease III; includes endonuclease III (DNA-(apurinic or apyrimidinic site) lyase), ... |
32-189 |
4.45e-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: 164.72 E-value: 4.45e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501072796 32 YKVWLSEVMLQQTQVTTVIPYFERFMARF-PDVTALANAPLDDVLHLWTGLGYYARARNLHKAAQQVATLHGGKF---PE 107
Cdd:cd00056 1 FEVLVSEILSQQTTDKAVNKAYERLFERYgPTPEALAAADEEELRELIRSLGYRRKAKYLKELARAIVEGFGGLVlddPD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501072796 108 TFEEVAALPGVGRSTAGAVLSLSLGKHFPILDGNVKRVLARCyaveGWPGKKEVENRLWQISETVTPAEGVARFNQAMMD 187
Cdd:cd00056 81 AREELLALPGVGRKTANVVLLFALGPDAFPVDTHVRRVLKRL----GLIPKKKTPEELEELLEELLPKPYWGEANQALMD 156
|
..
gi 501072796 188 LG 189
Cdd:cd00056 157 LG 158
|
|
| ENDO3c |
smart00478 |
endonuclease III; includes endonuclease III (DNA-(apurinic or apyrimidinic site) lyase), ... |
40-191 |
1.76e-47 |
|
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: 1.76e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501072796 40 MLQQTQVTTVIPYFERFMARFPDVTALANAPLDDVLHLWTGLG-YYARARNLHKAAQQVATLHGGKFPETFEEVAALPGV 118
Cdd:smart00478 1 LSQQTTDERVNKATERLFEKFPTPEDLAAADEEELEELIRGLGfYRRKARYLIELARILVEEYGGEVPDDREELLKLPGV 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 501072796 119 GRSTAGAVLSLSLGKHFPILDGNVKRVLARCYavegWPGKKEVENRLWQISETVTPAEGVARFNQAMMDLGAM 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 ... |
36-168 |
4.74e-42 |
|
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: 143.58 E-value: 4.74e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501072796 36 LSEVMLQQTQVTTVIPYFERFMAR-FPDVTALANAPLDDVLHLWTGLGYYAR-ARNLHKAAQQVATLHGGKFPETFEE-V 112
Cdd:pfam00730 1 VSAILSQQTSDKAVNKITERLFEKfFPTPEDLADADEEELRELIRGLGFYRRkAKYLKELARILVEGYGGEVPLDEEElE 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 501072796 113 AALPGVGRSTAGAVLSLSLG--KHFPILDGNVKRVLARCYAVEGWPGKKEVENRLWQI 168
Cdd:pfam00730 81 ALLKGVGRWTAEAVLIFALGrpDPLPVVDTHVRRVLKRLGLIKEKPTPKEVERELEEL 138
|
|
| PRK13910 |
PRK13910 |
DNA glycosylase MutY; Provisional |
40-302 |
1.34e-36 |
|
DNA glycosylase MutY; Provisional
Pssm-ID: 172427 [Multi-domain] Cd Length: 289 Bit Score: 133.99 E-value: 1.34e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501072796 40 MLQQTQVTTVIP-YFERFMARFPDVTALANAPLDDVLHLWTGLGYYARARNLHKAAQQVATLHGGKFPETFEEVAALPGV 118
Cdd:PRK13910 1 MSQQTQINTVVErFYSPFLEAFPTLKDLANAPLEEVLLLWRGLGYYSRAKNLKKSAEICVKEHHSQLPNDYQSLLKLPGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501072796 119 GRSTAGAVLSLSLGKHFPILDGNVKRVLARCYAVEGWPGKKEVE---NRLWQISETVTpaegvarFNQAMMDLGAMVCTr 195
Cdd:PRK13910 81 GAYTANAILCFGFREKSACVDANIKRVLLRLFGLDPNIHAKDLQikaNDFLNLNESFN-------HNQALIDLGALICS- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501072796 196 SKPKCEICPLNNGCEAFAHQSyaKYPGKKPKQILPEKTGYFLLLQHEGALF--LQQRppvgLWGGLYCFPQfesetaLRE 273
Cdd:PRK13910 153 PKPKCAICPLNPYCLGKNNPE--KHTLKKKQEIVQEERYLGVVIQNNQIALekIEQK----LYLGMHHFPN------LKE 220
|
250 260
....*....|....*....|....*....
gi 501072796 274 WLSARginddgLTQLTAFRHTFSHFHLDI 302
Cdd:PRK13910 221 NLEYK------LPFLGAIKHSHTKFKLNL 243
|
|
| Nth |
COG0177 |
Endonuclease III [Replication, recombination and repair]; |
29-213 |
2.25e-33 |
|
Endonuclease III [Replication, recombination and repair];
Pssm-ID: 439947 [Multi-domain] Cd Length: 198 Bit Score: 122.51 E-value: 2.25e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501072796 29 KTPYKVWLSEVMLQQT---QVTTVipyFERFMARFPDVTALANAPLDDVLHLWTGLGYY-ARARNLHKAAQQVATLHGGK 104
Cdd:COG0177 18 RDPFELLVATILSAQTtdeRVNKA---TPRLFARYPTPEALAAADLEELEELIRPIGLYrNKAKNIIALARILVEKYGGE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501072796 105 FPETFEEVAALPGVGRSTAGAVLSLSLGKH-FPIlDGNVKRVLARCyaveGW-PGK--KEVENRLwqisETVTPAEGVAR 180
Cdd:COG0177 95 VPETREELESLPGVGRKTANVVLNFAFGKPaIAV-DTHVHRVSNRL----GLvPGKdpEEVEKDL----MKLIPKEYWGD 165
|
170 180 190
....*....|....*....|....*....|...
gi 501072796 181 FNQAMMDLGAMVCTRSKPKCEICPLNNGCEAFA 213
Cdd:COG0177 166 LHHLLILHGRYICKARKPKCEECPLADLCPYYG 198
|
|
| NUDIX_DNA_Glycosylase_C-MutY |
cd03431 |
C-terminal domain of DNA glycosylase; DNA glycosylase (MutY in bacteria and hMYH in humans) is ... |
230-343 |
3.20e-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: 119.72 E-value: 3.20e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501072796 230 PEKTGYFLLLQHEGALFLQQRPPVGLWGGLYCFPQFESETALREWLSARGINDDG----LTQLTAFRHTFSHFHLDIVPm 305
Cdd:cd03431 2 PERYFTVLVLRDGGRVLLEKRPEKGLLAGLWEFPLVETEEEEEEAEALLGLLAEEllliLEPLGEVKHVFSHFRLHITV- 80
|
90 100 110
....*....|....*....|....*....|....*...
gi 501072796 306 WLGVQQTAACMDEASGLWYNLAQPPAVGLAAPVERLLQ 343
Cdd:cd03431 81 YLVELPEAPPAAPDEGRWVDLEELDEYALPAPMRKLLE 118
|
|
| NUDIX_4 |
pfam14815 |
NUDIX domain; |
235-344 |
4.99e-23 |
|
NUDIX domain;
Pssm-ID: 464330 [Multi-domain] Cd Length: 114 Bit Score: 92.38 E-value: 4.99e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501072796 235 YFLLLQHEGALFLQQRPPVGLWGGLYCFPQFESET--ALREWLSAR---GINDDGLTQLTAfRHTFSHFHLDIVpMWLGV 309
Cdd:pfam14815 2 VLVIRNGDGRVLLRKRPEKGLLGGLWEFPGGKVEPgeTLEEALARLeelGIEVEVLEPGTV-KHVFTHFRLTLH-VYLVR 79
|
90 100 110
....*....|....*....|....*....|....*
gi 501072796 310 QQTAACMDEASGLWYNLAQPPAVGLAAPVERLLQQ 344
Cdd:pfam14815 80 EVEGEEEPQQELRWVTPEELDKYALPAAVRKILEA 114
|
|
| nth |
TIGR01083 |
endonuclease III; This equivalog model identifes nth members of the pfam00730 superfamily ... |
29-200 |
3.30e-19 |
|
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: 84.35 E-value: 3.30e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501072796 29 KTPYKVWLSEVMLQQTQVTTVIPYFERFMARFPDVTALANAPLDDVLHLWTGLGYY-ARARNLHKAAQQVATLHGGKFPE 107
Cdd:TIGR01083 25 NNPFELLVATILSAQATDKRVNKATPKLFEVYPTPQALAQAGLEELEEYIKSIGLYrNKAKNIIELCRKLVERYGGEVPE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501072796 108 TFEEVAALPGVGRSTAGAVLSLSLGKHFPILDGNVKRVLARCyaveGW-PGK--KEVENRLWQisetVTPAEGVARFNQA 184
Cdd:TIGR01083 105 DREELVKLPGVGRKTANVVLNVAFGIPAIAVDTHVFRVSNRL----GLsKGKdpIKVEEDLMK----LVPREFWVKLHHW 176
|
170
....*....|....*.
gi 501072796 185 MMDLGAMVCTRSKPKC 200
Cdd:TIGR01083 177 LILHGRYTCKARKPLC 192
|
|
| PRK10702 |
PRK10702 |
endonuclease III; Provisional |
83-210 |
9.31e-13 |
|
endonuclease III; Provisional
Pssm-ID: 182661 [Multi-domain] Cd Length: 211 Bit Score: 66.58 E-value: 9.31e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501072796 83 YYARARNLHKAAQQVATLHGGKFPETFEEVAALPGVGRSTAGAVLSLSLGKHFPILDGNVKRVlarCYAVEGWPGK--KE 160
Cdd:PRK10702 82 YNSKAENVIKTCRILLEQHNGEVPEDRAALEALPGVGRKTANVVLNTAFGWPTIAVDTHIFRV---CNRTQFAPGKnvEQ 158
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 501072796 161 VENRLWQisetVTPAEGVARFNQAMMDLGAMVCTRSKPKCEICPLNNGCE 210
Cdd:PRK10702 159 VEEKLLK----VVPAEFKVDCHHWLILHGRYTCIARKPRCGSCIIEDLCE 204
|
|
| AlkA |
COG0122 |
3-methyladenine DNA glycosylase/8-oxoguanine DNA glycosylase [Replication, recombination and ... |
48-165 |
2.06e-08 |
|
3-methyladenine DNA glycosylase/8-oxoguanine DNA glycosylase [Replication, recombination and repair];
Pssm-ID: 439892 [Multi-domain] Cd Length: 255 Bit Score: 54.51 E-value: 2.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501072796 48 TVIPYFERFMARFPDVTALANAPLDDVLHLwtGLGYYaRARNLHKAAQQVAT-------LHGGKFPETFEEVAALPGVGR 120
Cdd:COG0122 115 EPIEGPGGGLYAFPTPEALAAASEEELRAC--GLSRR-KARYLRALARAVADgeldleaLAGLDDEEAIARLTALPGIGP 191
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 501072796 121 STAGAVLSLSLGKH--FPILDGNVKRVLARCYAVEGWPGKKEVENRL 165
Cdd:COG0122 192 WTAEMVLLFALGRPdaFPAGDLGLRRALGRLYGLGERPTPKELRELA 238
|
|
| HP0602 |
COG2231 |
3-Methyladenine DNA glycosylase, HhH-GPD/Endo3 superfamily [Replication, recombination and ... |
15-210 |
4.94e-08 |
|
3-Methyladenine DNA glycosylase, HhH-GPD/Endo3 superfamily [Replication, recombination and repair];
Pssm-ID: 441832 [Multi-domain] Cd Length: 220 Bit Score: 52.92 E-value: 4.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501072796 15 YDKYGRktLPWQQEKTPYKVWLSEVMLQQTQVTTVipyfERFMARF-------PDvtALANAPLDDVLHLWTGLGYYAR- 86
Cdd:COG2231 15 LEHYGP--QHWWPAETPFEVIVGAILTQNTSWKNV----EKAIANLkeaglldPE--ALAALDPEELAELIRPSGFYNQk 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501072796 87 ARNLHKAAQQVATLHGGKFPETF--------EEVAALPGVGRSTAGAVLSLSLGKH-FPIlDGNVKRVLARCYAVEGWPG 157
Cdd:COG2231 87 AKRLKNLARWLVERYGGGLEKLKalpteelrEELLSLKGIGPETADSILLYAFNRPvFVV-DAYTRRIFSRLGLIEEDAS 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 501072796 158 KKEVENRLwqisETVTPAEgVARFNQ--AMMD-LGAMVCtRSKPKCEICPLNNGCE 210
Cdd:COG2231 166 YDELQRLF----EENLPPD-VALYNEfhALIVeHGKEYC-KKKPKCEECPLRDLCP 215
|
|
| HHH |
pfam00633 |
Helix-hairpin-helix motif; The helix-hairpin-helix DNA-binding motif is found to be duplicated ... |
101-128 |
6.52e-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: 42.40 E-value: 6.52e-06
10 20
....*....|....*....|....*...
gi 501072796 101 HGGKFPETFEEVAALPGVGRSTAGAVLS 128
Cdd:pfam00633 2 LEGLIPASVEELLALPGVGPKTAEAILS 29
|
|
| FES |
smart00525 |
iron-sulpphur binding domain in DNA-(apurinic or apyrimidinic site) lyase (subfamily of ENDO3); ... |
192-212 |
5.65e-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: 39.46 E-value: 5.65e-05
|
| EndIII_4Fe-2S |
pfam10576 |
Iron-sulfur binding domain of endonuclease III; Escherichia coli endonuclease III (EC 4.2.99. ... |
193-209 |
9.77e-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: 38.91 E-value: 9.77e-05
|
| |
