|
Name |
Accession |
Description |
Interval |
E-value |
| PRK10880 |
PRK10880 |
adenine DNA glycosylase; |
5-352 |
0e+00 |
|
adenine DNA glycosylase;
Pssm-ID: 182805 [Multi-domain] Cd Length: 350 Bit Score: 809.71 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490226835 5 AAQFSAQVLDWYDKYGRKTLPWQIGKTPYKVWLSEVMLQQTQVATVIPYFERFMARFPTITDLANAPLDEVLHLWTGLGY 84
Cdd:PRK10880 3 ASQFSAQVLDWYDKYGRKTLPWQIDKTPYKVWLSEVMLQQTQVATVIPYFERFMARFPTVTDLANAPLDEVLHLWTGLGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490226835 85 YARARNLHKAAQQVATLHGGKFPQTFDEVAALPGVGRSTAGAILSLSLGQHYPILDGNVKRVLARCYAVSGWPGKKEVEK 164
Cdd:PRK10880 83 YARARNLHKAAQQVATLHGGEFPETFEEVAALPGVGRSTAGAILSLSLGKHFPILDGNVKRVLARCYAVSGWPGKKEVEN 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490226835 165 RLWEIAEDVTPAKGVERFNQAMMDLGAMVCTRSKPKCELCPLNNGCVAYANHSWAQYPGKKPKQTIPERTGYFLLMQHGD 244
Cdd:PRK10880 163 RLWQLSEQVTPAVGVERFNQAMMDLGAMVCTRSKPKCELCPLQNGCIAYANHSWALYPGKKPKQTLPERTGYFLLLQHGD 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490226835 245 KVFLSQRPPVGLWGGLFCFPQFEDEDTLREWLAQRQIKAENLTQLTAFRHTFSHFHLDIVPMWLTVHSSGACMDEGGALW 324
Cdd:PRK10880 243 EVWLEQRPPSGLWGGLFCFPQFADEEELRQWLAQRGIAADNLTQLTAFRHTFSHFHLDIVPMWLPVSSFTGCMDEGNGLW 322
|
330 340
....*....|....*....|....*...
gi 490226835 325 YNLAQPPSVGLAAPVERLLQQLKAGAPV 352
Cdd:PRK10880 323 YNLAQPPSVGLAAPVERLLQQLRTGAPV 350
|
|
| MutY |
COG1194 |
Adenine-specific DNA glycosylase, acts on AG and A-oxoG pairs [Replication, recombination and ... |
5-348 |
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: 568.62 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490226835 5 AAQFSAQVLDWYDKYGRkTLPWQIGKTPYKVWLSEVMLQQTQVATVIPYFERFMARFPTITDLANAPLDEVLHLWTGLGY 84
Cdd:COG1194 3 MASFAKRLLAWYDRHGR-DLPWRQTRDPYRVWLSEIMLQQTQVATVIPYYERFLERFPTVEALAAAPEDEVLKLWEGLGY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490226835 85 YARARNLHKAAQQVATLHGGKFPQTFDEVAALPGVGRSTAGAILSLSLGQHYPILDGNVKRVLARCYAVSGWPGKKEVEK 164
Cdd:COG1194 82 YSRARNLHKAAQQVVEEHGGVFPDTYEELLALPGIGPYTAAAIASIAFGEPAPIVDGNVKRVLSRLFAIEGPIGSPAAKK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490226835 165 RLWEIAEDVTPAKGVERFNQAMMDLGAMVCTRSKPKCELCPLNNGCVAYANHSWAQYPGKKPKQTIPERTGYFLLMQHGD 244
Cdd:COG1194 162 ELWALAEELLPPERPGDFNQALMDLGATVCTPKKPKCLLCPLQDDCAAFAEGRQEELPVKKPKKKKPERYGAALVIRDDG 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490226835 245 KVFLSQRPPVGLWGGLFCFPQFEDE-----DTLREWLAQR-QIKAENLTQLTAFRHTFSHFHLDIVPMWLTVhSSGACMD 318
Cdd:COG1194 242 RVLLEKRPPKGLWGGLWEFPEFEWEeaedpEALERWLREElGLEVEWLEPLGTVRHVFTHFRLHLTVYLARV-PAGPPAE 320
|
330 340 350
....*....|....*....|....*....|
gi 490226835 319 EGGALWYNLAQPPSVGLAAPVERLLQQLKA 348
Cdd:COG1194 321 PDGGRWVPLEELAALPLPAPMRKLLKALLK 350
|
|
| mutY |
TIGR01084 |
A/G-specific adenine glycosylase; This equivalog model identifies mutY members of the ... |
7-280 |
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: 510.03 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490226835 7 QFSAQVLDWYDKYGRKTLPWQIGKTPYKVWLSEVMLQQTQVATVIPYFERFMARFPTITDLANAPLDEVLHLWTGLGYYA 86
Cdd:TIGR01084 1 QFSEDLLSWYDKYGRKTLPWRQNKTPYRVWLSEVMLQQTQVATVIPYFERFLERFPTVQALANAPQDEVLKLWEGLGYYA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490226835 87 RARNLHKAAQQVATLHGGKFPQTFDEVAALPGVGRSTAGAILSLSLGQHYPILDGNVKRVLARCYAVSGWPGKKEVEKRL 166
Cdd:TIGR01084 81 RARNLHKAAQEVVEEFGGEFPQDFEDLAALPGVGRYTAGAILSFALNKPYPILDGNVKRVLSRLFAVEGWPGKKKVENRL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490226835 167 WEIAEDVTPAKGVERFNQAMMDLGAMVCTRSKPKCELCPLNNGCVAYANHSWAQYPGKKPKQTIPERTGYFLLMQHGD-K 245
Cdd:TIGR01084 161 WTLAESLLPKADPEAFNQALMDLGAMICTRKKPKCDLCPLQDFCLAYQQGTWEEYPVKKPKAAPPERTTYFLVLQNYDgE 240
|
250 260 270
....*....|....*....|....*....|....*
gi 490226835 246 VFLSQRPPVGLWGGLFCFPQFEDEDTLREWLAQRQ 280
Cdd:TIGR01084 241 VLLEQRPEKGLWGGLYCFPQFEDEDSLAFLLAQRG 275
|
|
| ENDO3c |
cd00056 |
endonuclease III; includes endonuclease III (DNA-(apurinic or apyrimidinic site) lyase), ... |
33-190 |
4.21e-53 |
|
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: 172.43 E-value: 4.21e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490226835 33 YKVWLSEVMLQQTQVATVIPYFERFMARF-PTITDLANAPLDEVLHLWTGLGYYARARNLHKAAQQVATLHGGKF---PQ 108
Cdd:cd00056 1 FEVLVSEILSQQTTDKAVNKAYERLFERYgPTPEALAAADEEELRELIRSLGYRRKAKYLKELARAIVEGFGGLVlddPD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490226835 109 TFDEVAALPGVGRSTAGAILSLSLGQHYPILDGNVKRVLARCyavsGWPGKKEVEKRLWEIAEDVTPAKGVERFNQAMMD 188
Cdd:cd00056 81 AREELLALPGVGRKTANVVLLFALGPDAFPVDTHVRRVLKRL----GLIPKKKTPEELEELLEELLPKPYWGEANQALMD 156
|
..
gi 490226835 189 LG 190
Cdd:cd00056 157 LG 158
|
|
| ENDO3c |
smart00478 |
endonuclease III; includes endonuclease III (DNA-(apurinic or apyrimidinic site) lyase), ... |
41-192 |
1.08e-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: 160.89 E-value: 1.08e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490226835 41 MLQQTQVATVIPYFERFMARFPTITDLANAPLDEVLHLWTGLG-YYARARNLHKAAQQVATLHGGKFPQTFDEVAALPGV 119
Cdd:smart00478 1 LSQQTTDERVNKATERLFEKFPTPEDLAAADEEELEELIRGLGfYRRKARYLIELARILVEEYGGEVPDDREELLKLPGV 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490226835 120 GRSTAGAILSLSLGQHYPILDGNVKRVLARCYavsgWPGKKEVEKRLWEIAEDVTPAKGVERFNQAMMDLGAM 192
Cdd:smart00478 81 GRKTANAVLSFALGKPFIPVDTHVLRIAKRLG----LVDKKSTPEEVEKLLEKLLPEEDWRELNLLLIDFGRT 149
|
|
| HhH-GPD |
pfam00730 |
HhH-GPD superfamily base excision DNA repair protein; This family contains a diverse range of ... |
37-171 |
8.42e-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: 147.82 E-value: 8.42e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490226835 37 LSEVMLQQTQVATVIPYFERFMAR-FPTITDLANAPLDEVLHLWTGLGYYAR-ARNLHKAAQQVATLHGGKFPQTFDE-V 113
Cdd:pfam00730 1 VSAILSQQTSDKAVNKITERLFEKfFPTPEDLADADEEELRELIRGLGFYRRkAKYLKELARILVEGYGGEVPLDEEElE 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 490226835 114 AALPGVGRSTAGAILSLSLG--QHYPILDGNVKRVLARCYAVSGWPGKKEVEKRLWEIAE 171
Cdd:pfam00730 81 ALLKGVGRWTAEAVLIFALGrpDPLPVVDTHVRRVLKRLGLIKEKPTPKEVERELEELWP 140
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK10880 |
PRK10880 |
adenine DNA glycosylase; |
5-352 |
0e+00 |
|
adenine DNA glycosylase;
Pssm-ID: 182805 [Multi-domain] Cd Length: 350 Bit Score: 809.71 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490226835 5 AAQFSAQVLDWYDKYGRKTLPWQIGKTPYKVWLSEVMLQQTQVATVIPYFERFMARFPTITDLANAPLDEVLHLWTGLGY 84
Cdd:PRK10880 3 ASQFSAQVLDWYDKYGRKTLPWQIDKTPYKVWLSEVMLQQTQVATVIPYFERFMARFPTVTDLANAPLDEVLHLWTGLGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490226835 85 YARARNLHKAAQQVATLHGGKFPQTFDEVAALPGVGRSTAGAILSLSLGQHYPILDGNVKRVLARCYAVSGWPGKKEVEK 164
Cdd:PRK10880 83 YARARNLHKAAQQVATLHGGEFPETFEEVAALPGVGRSTAGAILSLSLGKHFPILDGNVKRVLARCYAVSGWPGKKEVEN 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490226835 165 RLWEIAEDVTPAKGVERFNQAMMDLGAMVCTRSKPKCELCPLNNGCVAYANHSWAQYPGKKPKQTIPERTGYFLLMQHGD 244
Cdd:PRK10880 163 RLWQLSEQVTPAVGVERFNQAMMDLGAMVCTRSKPKCELCPLQNGCIAYANHSWALYPGKKPKQTLPERTGYFLLLQHGD 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490226835 245 KVFLSQRPPVGLWGGLFCFPQFEDEDTLREWLAQRQIKAENLTQLTAFRHTFSHFHLDIVPMWLTVHSSGACMDEGGALW 324
Cdd:PRK10880 243 EVWLEQRPPSGLWGGLFCFPQFADEEELRQWLAQRGIAADNLTQLTAFRHTFSHFHLDIVPMWLPVSSFTGCMDEGNGLW 322
|
330 340
....*....|....*....|....*...
gi 490226835 325 YNLAQPPSVGLAAPVERLLQQLKAGAPV 352
Cdd:PRK10880 323 YNLAQPPSVGLAAPVERLLQQLRTGAPV 350
|
|
| MutY |
COG1194 |
Adenine-specific DNA glycosylase, acts on AG and A-oxoG pairs [Replication, recombination and ... |
5-348 |
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: 568.62 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490226835 5 AAQFSAQVLDWYDKYGRkTLPWQIGKTPYKVWLSEVMLQQTQVATVIPYFERFMARFPTITDLANAPLDEVLHLWTGLGY 84
Cdd:COG1194 3 MASFAKRLLAWYDRHGR-DLPWRQTRDPYRVWLSEIMLQQTQVATVIPYYERFLERFPTVEALAAAPEDEVLKLWEGLGY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490226835 85 YARARNLHKAAQQVATLHGGKFPQTFDEVAALPGVGRSTAGAILSLSLGQHYPILDGNVKRVLARCYAVSGWPGKKEVEK 164
Cdd:COG1194 82 YSRARNLHKAAQQVVEEHGGVFPDTYEELLALPGIGPYTAAAIASIAFGEPAPIVDGNVKRVLSRLFAIEGPIGSPAAKK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490226835 165 RLWEIAEDVTPAKGVERFNQAMMDLGAMVCTRSKPKCELCPLNNGCVAYANHSWAQYPGKKPKQTIPERTGYFLLMQHGD 244
Cdd:COG1194 162 ELWALAEELLPPERPGDFNQALMDLGATVCTPKKPKCLLCPLQDDCAAFAEGRQEELPVKKPKKKKPERYGAALVIRDDG 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490226835 245 KVFLSQRPPVGLWGGLFCFPQFEDE-----DTLREWLAQR-QIKAENLTQLTAFRHTFSHFHLDIVPMWLTVhSSGACMD 318
Cdd:COG1194 242 RVLLEKRPPKGLWGGLWEFPEFEWEeaedpEALERWLREElGLEVEWLEPLGTVRHVFTHFRLHLTVYLARV-PAGPPAE 320
|
330 340 350
....*....|....*....|....*....|
gi 490226835 319 EGGALWYNLAQPPSVGLAAPVERLLQQLKA 348
Cdd:COG1194 321 PDGGRWVPLEELAALPLPAPMRKLLKALLK 350
|
|
| mutY |
TIGR01084 |
A/G-specific adenine glycosylase; This equivalog model identifies mutY members of the ... |
7-280 |
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: 510.03 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490226835 7 QFSAQVLDWYDKYGRKTLPWQIGKTPYKVWLSEVMLQQTQVATVIPYFERFMARFPTITDLANAPLDEVLHLWTGLGYYA 86
Cdd:TIGR01084 1 QFSEDLLSWYDKYGRKTLPWRQNKTPYRVWLSEVMLQQTQVATVIPYFERFLERFPTVQALANAPQDEVLKLWEGLGYYA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490226835 87 RARNLHKAAQQVATLHGGKFPQTFDEVAALPGVGRSTAGAILSLSLGQHYPILDGNVKRVLARCYAVSGWPGKKEVEKRL 166
Cdd:TIGR01084 81 RARNLHKAAQEVVEEFGGEFPQDFEDLAALPGVGRYTAGAILSFALNKPYPILDGNVKRVLSRLFAVEGWPGKKKVENRL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490226835 167 WEIAEDVTPAKGVERFNQAMMDLGAMVCTRSKPKCELCPLNNGCVAYANHSWAQYPGKKPKQTIPERTGYFLLMQHGD-K 245
Cdd:TIGR01084 161 WTLAESLLPKADPEAFNQALMDLGAMICTRKKPKCDLCPLQDFCLAYQQGTWEEYPVKKPKAAPPERTTYFLVLQNYDgE 240
|
250 260 270
....*....|....*....|....*....|....*
gi 490226835 246 VFLSQRPPVGLWGGLFCFPQFEDEDTLREWLAQRQ 280
Cdd:TIGR01084 241 VLLEQRPEKGLWGGLYCFPQFEDEDSLAFLLAQRG 275
|
|
| ENDO3c |
cd00056 |
endonuclease III; includes endonuclease III (DNA-(apurinic or apyrimidinic site) lyase), ... |
33-190 |
4.21e-53 |
|
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: 172.43 E-value: 4.21e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490226835 33 YKVWLSEVMLQQTQVATVIPYFERFMARF-PTITDLANAPLDEVLHLWTGLGYYARARNLHKAAQQVATLHGGKF---PQ 108
Cdd:cd00056 1 FEVLVSEILSQQTTDKAVNKAYERLFERYgPTPEALAAADEEELRELIRSLGYRRKAKYLKELARAIVEGFGGLVlddPD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490226835 109 TFDEVAALPGVGRSTAGAILSLSLGQHYPILDGNVKRVLARCyavsGWPGKKEVEKRLWEIAEDVTPAKGVERFNQAMMD 188
Cdd:cd00056 81 AREELLALPGVGRKTANVVLLFALGPDAFPVDTHVRRVLKRL----GLIPKKKTPEELEELLEELLPKPYWGEANQALMD 156
|
..
gi 490226835 189 LG 190
Cdd:cd00056 157 LG 158
|
|
| ENDO3c |
smart00478 |
endonuclease III; includes endonuclease III (DNA-(apurinic or apyrimidinic site) lyase), ... |
41-192 |
1.08e-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: 160.89 E-value: 1.08e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490226835 41 MLQQTQVATVIPYFERFMARFPTITDLANAPLDEVLHLWTGLG-YYARARNLHKAAQQVATLHGGKFPQTFDEVAALPGV 119
Cdd:smart00478 1 LSQQTTDERVNKATERLFEKFPTPEDLAAADEEELEELIRGLGfYRRKARYLIELARILVEEYGGEVPDDREELLKLPGV 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490226835 120 GRSTAGAILSLSLGQHYPILDGNVKRVLARCYavsgWPGKKEVEKRLWEIAEDVTPAKGVERFNQAMMDLGAM 192
Cdd:smart00478 81 GRKTANAVLSFALGKPFIPVDTHVLRIAKRLG----LVDKKSTPEEVEKLLEKLLPEEDWRELNLLLIDFGRT 149
|
|
| HhH-GPD |
pfam00730 |
HhH-GPD superfamily base excision DNA repair protein; This family contains a diverse range of ... |
37-171 |
8.42e-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: 147.82 E-value: 8.42e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490226835 37 LSEVMLQQTQVATVIPYFERFMAR-FPTITDLANAPLDEVLHLWTGLGYYAR-ARNLHKAAQQVATLHGGKFPQTFDE-V 113
Cdd:pfam00730 1 VSAILSQQTSDKAVNKITERLFEKfFPTPEDLADADEEELRELIRGLGFYRRkAKYLKELARILVEGYGGEVPLDEEElE 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 490226835 114 AALPGVGRSTAGAILSLSLG--QHYPILDGNVKRVLARCYAVSGWPGKKEVEKRLWEIAE 171
Cdd:pfam00730 81 ALLKGVGRWTAEAVLIFALGrpDPLPVVDTHVRRVLKRLGLIKEKPTPKEVERELEELWP 140
|
|
| PRK13910 |
PRK13910 |
DNA glycosylase MutY; Provisional |
41-268 |
7.53e-39 |
|
DNA glycosylase MutY; Provisional
Pssm-ID: 172427 [Multi-domain] Cd Length: 289 Bit Score: 139.77 E-value: 7.53e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490226835 41 MLQQTQVATVIP-YFERFMARFPTITDLANAPLDEVLHLWTGLGYYARARNLHKAAQQVATLHGGKFPQTFDEVAALPGV 119
Cdd:PRK13910 1 MSQQTQINTVVErFYSPFLEAFPTLKDLANAPLEEVLLLWRGLGYYSRAKNLKKSAEICVKEHHSQLPNDYQSLLKLPGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490226835 120 GRSTAGAILSLSLGQHYPILDGNVKRVLARCYAVSGWPGKKEVEKRlweiAEDVTPAKGVERFNQAMMDLGAMVCTrSKP 199
Cdd:PRK13910 81 GAYTANAILCFGFREKSACVDANIKRVLLRLFGLDPNIHAKDLQIK----ANDFLNLNESFNHNQALIDLGALICS-PKP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490226835 200 KCELCPLNNGCVAyANHswAQYPGKKPKQTIPERTGYFLLMQHGDKVFLsQRPPVGLWGGLFCFPQFED 268
Cdd:PRK13910 156 KCAICPLNPYCLG-KNN--PEKHTLKKKQEIVQEERYLGVVIQNNQIAL-EKIEQKLYLGMHHFPNLKE 220
|
|
| Nth |
COG0177 |
Endonuclease III [Replication, recombination and repair]; |
30-210 |
2.40e-34 |
|
Endonuclease III [Replication, recombination and repair];
Pssm-ID: 439947 [Multi-domain] Cd Length: 198 Bit Score: 124.82 E-value: 2.40e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490226835 30 KTPYKVWLSEVMLQQTQVATVIPYFERFMARFPTITDLANAPLDEVLHLWTGLGYY-ARARNLHKAAQQVATLHGGKFPQ 108
Cdd:COG0177 18 RDPFELLVATILSAQTTDERVNKATPRLFARYPTPEALAAADLEELEELIRPIGLYrNKAKNIIALARILVEKYGGEVPE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490226835 109 TFDEVAALPGVGRSTAGAILSLSLGQHYPILDGNVKRVLARcyavSGW-PGK--KEVEKRLWEIaedvTPAKGVERFNQA 185
Cdd:COG0177 98 TREELESLPGVGRKTANVVLNFAFGKPAIAVDTHVHRVSNR----LGLvPGKdpEEVEKDLMKL----IPKEYWGDLHHL 169
|
170 180
....*....|....*....|....*
gi 490226835 186 MMDLGAMVCTRSKPKCELCPLNNGC 210
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 ... |
230-344 |
4.58e-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: 118.95 E-value: 4.58e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490226835 230 IPERTGYFLLMQHGDKVFLSQRPPVGLWGGLFCFPQFEDEDTLREWLAQRQIKAE----NLTQLTAFRHTFSHFHLDIVP 305
Cdd:cd03431 1 VPERYFTVLVLRDGGRVLLEKRPEKGLLAGLWEFPLVETEEEEEEAEALLGLLAEelllILEPLGEVKHVFSHFRLHITV 80
|
90 100 110
....*....|....*....|....*....|....*....
gi 490226835 306 MWLTVhSSGACMDEGGALWYNLAQPPSVGLAAPVERLLQ 344
Cdd:cd03431 81 YLVEL-PEAPPAAPDEGRWVDLEELDEYALPAPMRKLLE 118
|
|
| NUDIX_4 |
pfam14815 |
NUDIX domain; |
236-345 |
3.88e-24 |
|
NUDIX domain;
Pssm-ID: 464330 [Multi-domain] Cd Length: 114 Bit Score: 95.07 E-value: 3.88e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490226835 236 YFLLMQHGDKVFLSQRPPVGLWGGLFCFPQF--EDEDTLREWLAQRQ---IKAENLTQLTAfRHTFSHFHLDIVpMWLTV 310
Cdd:pfam14815 2 VLVIRNGDGRVLLRKRPEKGLLGGLWEFPGGkvEPGETLEEALARLEelgIEVEVLEPGTV-KHVFTHFRLTLH-VYLVR 79
|
90 100 110
....*....|....*....|....*....|....*
gi 490226835 311 HSSGACMDEGGALWYNLAQPPSVGLAAPVERLLQQ 345
Cdd:pfam14815 80 EVEGEEEPQQELRWVTPEELDKYALPAAVRKILEA 114
|
|
| nth |
TIGR01083 |
endonuclease III; This equivalog model identifes nth members of the pfam00730 superfamily ... |
30-201 |
1.14e-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: 85.51 E-value: 1.14e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490226835 30 KTPYKVWLSEVMLQQTQVATVIPYFERFMARFPTITDLANAPLDEVLHLWTGLGYY-ARARNLHKAAQQVATLHGGKFPQ 108
Cdd:TIGR01083 25 NNPFELLVATILSAQATDKRVNKATPKLFEVYPTPQALAQAGLEELEEYIKSIGLYrNKAKNIIELCRKLVERYGGEVPE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490226835 109 TFDEVAALPGVGRSTAGAILSLSLGQHYPILDGNVKRVLARcyavSGW-PGK--KEVEKRLweiaEDVTPAKGVERFNQA 185
Cdd:TIGR01083 105 DREELVKLPGVGRKTANVVLNVAFGIPAIAVDTHVFRVSNR----LGLsKGKdpIKVEEDL----MKLVPREFWVKLHHW 176
|
170
....*....|....*.
gi 490226835 186 MMDLGAMVCTRSKPKC 201
Cdd:TIGR01083 177 LILHGRYTCKARKPLC 192
|
|
| PRK10702 |
PRK10702 |
endonuclease III; Provisional |
84-210 |
1.22e-09 |
|
endonuclease III; Provisional
Pssm-ID: 182661 [Multi-domain] Cd Length: 211 Bit Score: 57.33 E-value: 1.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490226835 84 YYARARNLHKAAQQVATLHGGKFPQTFDEVAALPGVGRSTAGAILSLSLGQHYPILDGNVKRVlarCYAVSGWPGK--KE 161
Cdd:PRK10702 82 YNSKAENVIKTCRILLEQHNGEVPEDRAALEALPGVGRKTANVVLNTAFGWPTIAVDTHIFRV---CNRTQFAPGKnvEQ 158
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 490226835 162 VEKRLWEiaedVTPAKGVERFNQAMMDLGAMVCTRSKPKCELCPLNNGC 210
Cdd:PRK10702 159 VEEKLLK----VVPAEFKVDCHHWLILHGRYTCIARKPRCGSCIIEDLC 203
|
|
| HP0602 |
COG2231 |
3-Methyladenine DNA glycosylase, HhH-GPD/Endo3 superfamily [Replication, recombination and ... |
16-217 |
3.86e-08 |
|
3-Methyladenine DNA glycosylase, HhH-GPD/Endo3 superfamily [Replication, recombination and repair];
Pssm-ID: 441832 [Multi-domain] Cd Length: 220 Bit Score: 53.31 E-value: 3.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490226835 16 YDKYGRktLPWQIGKTPYKVWLSEVMLQQTQVATVipyfERFMARFP-----TITDLANAPLDEVLHLWTGLGYYAR-AR 89
Cdd:COG2231 15 LEHYGP--QHWWPAETPFEVIVGAILTQNTSWKNV----EKAIANLKeagllDPEALAALDPEELAELIRPSGFYNQkAK 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490226835 90 NLHKAAQQVATLHGGKFPQTF--------DEVAALPGVGRSTAGAILSLSLgqHYPIL--DGNVKRVLARcyaVSGWPGK 159
Cdd:COG2231 89 RLKNLARWLVERYGGGLEKLKalpteelrEELLSLKGIGPETADSILLYAF--NRPVFvvDAYTRRIFSR---LGLIEED 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490226835 160 KEVEKrLWEIAEDVTPaKGVERFNQ--AMMD-LGAMVCtRSKPKCELCPLNNGCvAYANHS 217
Cdd:COG2231 164 ASYDE-LQRLFEENLP-PDVALYNEfhALIVeHGKEYC-KKKPKCEECPLRDLC-PYGGQE 220
|
|
| HHH |
pfam00633 |
Helix-hairpin-helix motif; The helix-hairpin-helix DNA-binding motif is found to be duplicated ... |
102-129 |
2.61e-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: 2.61e-06
10 20
....*....|....*....|....*...
gi 490226835 102 HGGKFPQTFDEVAALPGVGRSTAGAILS 129
Cdd:pfam00633 2 LEGLIPASVEELLALPGVGPKTAEAILS 29
|
|
| AlkA |
COG0122 |
3-methyladenine DNA glycosylase/8-oxoguanine DNA glycosylase [Replication, recombination and ... |
49-166 |
5.18e-06 |
|
3-methyladenine DNA glycosylase/8-oxoguanine DNA glycosylase [Replication, recombination and repair];
Pssm-ID: 439892 [Multi-domain] Cd Length: 255 Bit Score: 47.19 E-value: 5.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490226835 49 TVIPYFERFMARFPTITDLANAPLDEVLHLwtGLGYYaRARNLHKAAQQVA--TLHGGKFPQTFDEVA-----ALPGVGR 121
Cdd:COG0122 115 EPIEGPGGGLYAFPTPEALAAASEEELRAC--GLSRR-KARYLRALARAVAdgELDLEALAGLDDEEAiarltALPGIGP 191
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 490226835 122 STAGAILSLSLGQH--YPILDGNVKRVLARCYAVSGWPGKKEVEKRL 166
Cdd:COG0122 192 WTAEMVLLFALGRPdaFPAGDLGLRRALGRLYGLGERPTPKELRELA 238
|
|
| FES |
smart00525 |
iron-sulpphur binding domain in DNA-(apurinic or apyrimidinic site) lyase (subfamily of ENDO3); ... |
193-213 |
3.80e-05 |
|
iron-sulpphur binding domain in DNA-(apurinic or apyrimidinic site) lyase (subfamily of ENDO3);
Pssm-ID: 197771 [Multi-domain] Cd Length: 21 Bit Score: 39.84 E-value: 3.80e-05
|
| EndIII_4Fe-2S |
pfam10576 |
Iron-sulfur binding domain of endonuclease III; Escherichia coli endonuclease III (EC 4.2.99. ... |
194-210 |
2.32e-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: 37.75 E-value: 2.32e-04
|
| |
