|
Name |
Accession |
Description |
Interval |
E-value |
| MutY |
COG1194 |
Adenine-specific DNA glycosylase, acts on AG and A-oxoG pairs [Replication, recombination and ... |
19-388 |
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: 525.09 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199733524 19 SFSEKLLHWFDQFGRkNLPWQHNKTAYRVWISEIMLQQTQVTTVIPYYERFMQRFPDIESLAQASVDEVLSYWAGLGYYA 98
Cdd:COG1194 5 SFAKRLLAWYDRHGR-DLPWRQTRDPYRVWLSEIMLQQTQVATVIPYYERFLERFPTVEALAAAPEDEVLKLWEGLGYYS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199733524 99 RGRNLHKAAVTVMENFAGEFPDKLEDIQSLPGIGQSTAGAIASIALKQRAPILDGNVKRVLARFAAIEGWTGEKSVSNQL 178
Cdd:COG1194 84 RARNLHKAAQQVVEEHGGVFPDTYEELLALPGIGPYTAAAIASIAFGEPAPIVDGNVKRVLSRLFAIEGPIGSPAAKKEL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199733524 179 WKLADELTPHQRVDEYTQAIMDLGASLCSRRNPDCGQCPMQSACKAFAQGRQNELPTPKPKSKNPVKEAWILAIRDAhGR 258
Cdd:COG1194 164 WALAEELLPPERPGDFNQALMDLGATVCTPKKPKCLLCPLQDDCAAFAEGRQEELPVKKPKKKKPERYGAALVIRDD-GR 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199733524 259 LLFQKRPPTGIWGGLWSLPQVE--RDLNIAQLPDYIASQLGLQGQYKAEATPFEHQFSHFKLVLHPILFECENPVSEAVG 336
Cdd:COG1194 243 VLLEKRPPKGLWGGLWEFPEFEweEAEDPEALERWLREELGLEVEWLEPLGTVRHVFTHFRLHLTVYLARVPAGPPAEPD 322
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1199733524 337 EYslegivshevqgsykiqeahkiqegftdsQFYSRAQWREIGLPAPIKKLL 388
Cdd:COG1194 323 GG-----------------------------RWVPLEELAALPLPAPMRKLL 345
|
|
| mutY |
TIGR01084 |
A/G-specific adenine glycosylase; This equivalog model identifies mutY members of the ... |
20-288 |
1.15e-138 |
|
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: 396.78 E-value: 1.15e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199733524 20 FSEKLLHWFDQFGRKNLPWQHNKTAYRVWISEIMLQQTQVTTVIPYYERFMQRFPDIESLAQASVDEVLSYWAGLGYYAR 99
Cdd:TIGR01084 2 FSEDLLSWYDKYGRKTLPWRQNKTPYRVWLSEVMLQQTQVATVIPYFERFLERFPTVQALANAPQDEVLKLWEGLGYYAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199733524 100 GRNLHKAAVTVMENFAGEFPDKLEDIQSLPGIGQSTAGAIASIALKQRAPILDGNVKRVLARFAAIEGWTGEKSVSNQLW 179
Cdd:TIGR01084 82 ARNLHKAAQEVVEEFGGEFPQDFEDLAALPGVGRYTAGAILSFALNKPYPILDGNVKRVLSRLFAVEGWPGKKKVENRLW 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199733524 180 KLADELTPHQRVDEYTQAIMDLGASLCSRRNPDCGQCPMQSACKAFAQGRQNELPTPKPKSKNPVKEAWILAIRDAHGRL 259
Cdd:TIGR01084 162 TLAESLLPKADPEAFNQALMDLGAMICTRKKPKCDLCPLQDFCLAYQQGTWEEYPVKKPKAAPPERTTYFLVLQNYDGEV 241
|
250 260
....*....|....*....|....*....
gi 1199733524 260 LFQKRPPTGIWGGLWSLPQVERDLNIAQL 288
Cdd:TIGR01084 242 LLEQRPEKGLWGGLYCFPQFEDEDSLAFL 270
|
|
| PRK10880 |
PRK10880 |
adenine DNA glycosylase; |
20-323 |
1.33e-136 |
|
adenine DNA glycosylase;
Pssm-ID: 182805 [Multi-domain] Cd Length: 350 Bit Score: 394.46 E-value: 1.33e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199733524 20 FSEKLLHWFDQFGRKNLPWQHNKTAYRVWISEIMLQQTQVTTVIPYYERFMQRFPDIESLAQASVDEVLSYWAGLGYYAR 99
Cdd:PRK10880 6 FSAQVLDWYDKYGRKTLPWQIDKTPYKVWLSEVMLQQTQVATVIPYFERFMARFPTVTDLANAPLDEVLHLWTGLGYYAR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199733524 100 GRNLHKAAVTVMENFAGEFPDKLEDIQSLPGIGQSTAGAIASIALKQRAPILDGNVKRVLARFAAIEGWTGEKSVSNQLW 179
Cdd:PRK10880 86 ARNLHKAAQQVATLHGGEFPETFEEVAALPGVGRSTAGAILSLSLGKHFPILDGNVKRVLARCYAVSGWPGKKEVENRLW 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199733524 180 KLADELTPHQRVDEYTQAIMDLGASLCSRRNPDCGQCPMQSACKAFAQGRQNELPTPKPKSKNPVKEAWILAIRdaHGRL 259
Cdd:PRK10880 166 QLSEQVTPAVGVERFNQAMMDLGAMVCTRSKPKCELCPLQNGCIAYANHSWALYPGKKPKQTLPERTGYFLLLQ--HGDE 243
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1199733524 260 LF-QKRPPTGIWGGLWSLPQVErdlNIAQLPDYIAsQLGLQGQYKAEATPFEHQFSHFKLVLHPI 323
Cdd:PRK10880 244 VWlEQRPPSGLWGGLFCFPQFA---DEEELRQWLA-QRGIAADNLTQLTAFRHTFSHFHLDIVPM 304
|
|
| ENDO3c |
cd00056 |
endonuclease III; includes endonuclease III (DNA-(apurinic or apyrimidinic site) lyase), ... |
45-202 |
3.60e-48 |
|
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: 161.26 E-value: 3.60e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199733524 45 YRVWISEIMLQQTQVTTVIPYYERFMQRF-PDIESLAQASVDEVLSYWAGLGYYARGRNLHKAAVTVMENFAGEF---PD 120
Cdd:cd00056 1 FEVLVSEILSQQTTDKAVNKAYERLFERYgPTPEALAAADEEELRELIRSLGYRRKAKYLKELARAIVEGFGGLVlddPD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199733524 121 KLEDIQSLPGIGQSTAGAIASIALKQRAPILDGNVKRVLARFaaieGWTGEKSVSNQLWKLADELTPHQRVDEYTQAIMD 200
Cdd:cd00056 81 AREELLALPGVGRKTANVVLLFALGPDAFPVDTHVRRVLKRL----GLIPKKKTPEELEELLEELLPKPYWGEANQALMD 156
|
..
gi 1199733524 201 LG 202
Cdd:cd00056 157 LG 158
|
|
| ENDO3c |
smart00478 |
endonuclease III; includes endonuclease III (DNA-(apurinic or apyrimidinic site) lyase), ... |
53-203 |
1.02e-43 |
|
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: 149.34 E-value: 1.02e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199733524 53 MLQQTQVTTVIPYYERFMQRFPDIESLAQASVDEVLSYWAGLG-YYARGRNLHKAAVTVMENFAGEFPDKLEDIQSLPGI 131
Cdd:smart00478 1 LSQQTTDERVNKATERLFEKFPTPEDLAAADEEELEELIRGLGfYRRKARYLIELARILVEEYGGEVPDDREELLKLPGV 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1199733524 132 GQSTAGAIASIALKQRAPILDGNVKRVLARFaaieGWTGEKSVSNQLWKLADELTPHQRVDEYTQAIMDLGA 203
Cdd:smart00478 81 GRKTANAVLSFALGKPFIPVDTHVLRIAKRL----GLVDKKSTPEEVEKLLEKLLPEEDWRELNLLLIDFGR 148
|
|
| HhH-GPD |
pfam00730 |
HhH-GPD superfamily base excision DNA repair protein; This family contains a diverse range of ... |
49-181 |
5.97e-34 |
|
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: 123.16 E-value: 5.97e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199733524 49 ISEIMLQQTQVTTVIPYYERFMQR-FPDIESLAQASVDEVLSYWAGLGYYAR-GRNLHKAAVTVMENFAGEFP-DKLEDI 125
Cdd:pfam00730 1 VSAILSQQTSDKAVNKITERLFEKfFPTPEDLADADEEELRELIRGLGFYRRkAKYLKELARILVEGYGGEVPlDEEELE 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1199733524 126 QSLPGIGQSTAGAIASIAL--KQRAPILDGNVKRVLARFAAIEGWTGEKSVSNQLWKL 181
Cdd:pfam00730 81 ALLKGVGRWTAEAVLIFALgrPDPLPVVDTHVRRVLKRLGLIKEKPTPKEVERELEEL 138
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| MutY |
COG1194 |
Adenine-specific DNA glycosylase, acts on AG and A-oxoG pairs [Replication, recombination and ... |
19-388 |
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: 525.09 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199733524 19 SFSEKLLHWFDQFGRkNLPWQHNKTAYRVWISEIMLQQTQVTTVIPYYERFMQRFPDIESLAQASVDEVLSYWAGLGYYA 98
Cdd:COG1194 5 SFAKRLLAWYDRHGR-DLPWRQTRDPYRVWLSEIMLQQTQVATVIPYYERFLERFPTVEALAAAPEDEVLKLWEGLGYYS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199733524 99 RGRNLHKAAVTVMENFAGEFPDKLEDIQSLPGIGQSTAGAIASIALKQRAPILDGNVKRVLARFAAIEGWTGEKSVSNQL 178
Cdd:COG1194 84 RARNLHKAAQQVVEEHGGVFPDTYEELLALPGIGPYTAAAIASIAFGEPAPIVDGNVKRVLSRLFAIEGPIGSPAAKKEL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199733524 179 WKLADELTPHQRVDEYTQAIMDLGASLCSRRNPDCGQCPMQSACKAFAQGRQNELPTPKPKSKNPVKEAWILAIRDAhGR 258
Cdd:COG1194 164 WALAEELLPPERPGDFNQALMDLGATVCTPKKPKCLLCPLQDDCAAFAEGRQEELPVKKPKKKKPERYGAALVIRDD-GR 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199733524 259 LLFQKRPPTGIWGGLWSLPQVE--RDLNIAQLPDYIASQLGLQGQYKAEATPFEHQFSHFKLVLHPILFECENPVSEAVG 336
Cdd:COG1194 243 VLLEKRPPKGLWGGLWEFPEFEweEAEDPEALERWLREELGLEVEWLEPLGTVRHVFTHFRLHLTVYLARVPAGPPAEPD 322
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1199733524 337 EYslegivshevqgsykiqeahkiqegftdsQFYSRAQWREIGLPAPIKKLL 388
Cdd:COG1194 323 GG-----------------------------RWVPLEELAALPLPAPMRKLL 345
|
|
| mutY |
TIGR01084 |
A/G-specific adenine glycosylase; This equivalog model identifies mutY members of the ... |
20-288 |
1.15e-138 |
|
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: 396.78 E-value: 1.15e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199733524 20 FSEKLLHWFDQFGRKNLPWQHNKTAYRVWISEIMLQQTQVTTVIPYYERFMQRFPDIESLAQASVDEVLSYWAGLGYYAR 99
Cdd:TIGR01084 2 FSEDLLSWYDKYGRKTLPWRQNKTPYRVWLSEVMLQQTQVATVIPYFERFLERFPTVQALANAPQDEVLKLWEGLGYYAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199733524 100 GRNLHKAAVTVMENFAGEFPDKLEDIQSLPGIGQSTAGAIASIALKQRAPILDGNVKRVLARFAAIEGWTGEKSVSNQLW 179
Cdd:TIGR01084 82 ARNLHKAAQEVVEEFGGEFPQDFEDLAALPGVGRYTAGAILSFALNKPYPILDGNVKRVLSRLFAVEGWPGKKKVENRLW 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199733524 180 KLADELTPHQRVDEYTQAIMDLGASLCSRRNPDCGQCPMQSACKAFAQGRQNELPTPKPKSKNPVKEAWILAIRDAHGRL 259
Cdd:TIGR01084 162 TLAESLLPKADPEAFNQALMDLGAMICTRKKPKCDLCPLQDFCLAYQQGTWEEYPVKKPKAAPPERTTYFLVLQNYDGEV 241
|
250 260
....*....|....*....|....*....
gi 1199733524 260 LFQKRPPTGIWGGLWSLPQVERDLNIAQL 288
Cdd:TIGR01084 242 LLEQRPEKGLWGGLYCFPQFEDEDSLAFL 270
|
|
| PRK10880 |
PRK10880 |
adenine DNA glycosylase; |
20-323 |
1.33e-136 |
|
adenine DNA glycosylase;
Pssm-ID: 182805 [Multi-domain] Cd Length: 350 Bit Score: 394.46 E-value: 1.33e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199733524 20 FSEKLLHWFDQFGRKNLPWQHNKTAYRVWISEIMLQQTQVTTVIPYYERFMQRFPDIESLAQASVDEVLSYWAGLGYYAR 99
Cdd:PRK10880 6 FSAQVLDWYDKYGRKTLPWQIDKTPYKVWLSEVMLQQTQVATVIPYFERFMARFPTVTDLANAPLDEVLHLWTGLGYYAR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199733524 100 GRNLHKAAVTVMENFAGEFPDKLEDIQSLPGIGQSTAGAIASIALKQRAPILDGNVKRVLARFAAIEGWTGEKSVSNQLW 179
Cdd:PRK10880 86 ARNLHKAAQQVATLHGGEFPETFEEVAALPGVGRSTAGAILSLSLGKHFPILDGNVKRVLARCYAVSGWPGKKEVENRLW 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199733524 180 KLADELTPHQRVDEYTQAIMDLGASLCSRRNPDCGQCPMQSACKAFAQGRQNELPTPKPKSKNPVKEAWILAIRdaHGRL 259
Cdd:PRK10880 166 QLSEQVTPAVGVERFNQAMMDLGAMVCTRSKPKCELCPLQNGCIAYANHSWALYPGKKPKQTLPERTGYFLLLQ--HGDE 243
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1199733524 260 LF-QKRPPTGIWGGLWSLPQVErdlNIAQLPDYIAsQLGLQGQYKAEATPFEHQFSHFKLVLHPI 323
Cdd:PRK10880 244 VWlEQRPPSGLWGGLFCFPQFA---DEEELRQWLA-QRGIAADNLTQLTAFRHTFSHFHLDIVPM 304
|
|
| ENDO3c |
cd00056 |
endonuclease III; includes endonuclease III (DNA-(apurinic or apyrimidinic site) lyase), ... |
45-202 |
3.60e-48 |
|
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: 161.26 E-value: 3.60e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199733524 45 YRVWISEIMLQQTQVTTVIPYYERFMQRF-PDIESLAQASVDEVLSYWAGLGYYARGRNLHKAAVTVMENFAGEF---PD 120
Cdd:cd00056 1 FEVLVSEILSQQTTDKAVNKAYERLFERYgPTPEALAAADEEELRELIRSLGYRRKAKYLKELARAIVEGFGGLVlddPD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199733524 121 KLEDIQSLPGIGQSTAGAIASIALKQRAPILDGNVKRVLARFaaieGWTGEKSVSNQLWKLADELTPHQRVDEYTQAIMD 200
Cdd:cd00056 81 AREELLALPGVGRKTANVVLLFALGPDAFPVDTHVRRVLKRL----GLIPKKKTPEELEELLEELLPKPYWGEANQALMD 156
|
..
gi 1199733524 201 LG 202
Cdd:cd00056 157 LG 158
|
|
| ENDO3c |
smart00478 |
endonuclease III; includes endonuclease III (DNA-(apurinic or apyrimidinic site) lyase), ... |
53-203 |
1.02e-43 |
|
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: 149.34 E-value: 1.02e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199733524 53 MLQQTQVTTVIPYYERFMQRFPDIESLAQASVDEVLSYWAGLG-YYARGRNLHKAAVTVMENFAGEFPDKLEDIQSLPGI 131
Cdd:smart00478 1 LSQQTTDERVNKATERLFEKFPTPEDLAAADEEELEELIRGLGfYRRKARYLIELARILVEEYGGEVPDDREELLKLPGV 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1199733524 132 GQSTAGAIASIALKQRAPILDGNVKRVLARFaaieGWTGEKSVSNQLWKLADELTPHQRVDEYTQAIMDLGA 203
Cdd:smart00478 81 GRKTANAVLSFALGKPFIPVDTHVLRIAKRL----GLVDKKSTPEEVEKLLEKLLPEEDWRELNLLLIDFGR 148
|
|
| HhH-GPD |
pfam00730 |
HhH-GPD superfamily base excision DNA repair protein; This family contains a diverse range of ... |
49-181 |
5.97e-34 |
|
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: 123.16 E-value: 5.97e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199733524 49 ISEIMLQQTQVTTVIPYYERFMQR-FPDIESLAQASVDEVLSYWAGLGYYAR-GRNLHKAAVTVMENFAGEFP-DKLEDI 125
Cdd:pfam00730 1 VSAILSQQTSDKAVNKITERLFEKfFPTPEDLADADEEELRELIRGLGFYRRkAKYLKELARILVEGYGGEVPlDEEELE 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1199733524 126 QSLPGIGQSTAGAIASIAL--KQRAPILDGNVKRVLARFAAIEGWTGEKSVSNQLWKL 181
Cdd:pfam00730 81 ALLKGVGRWTAEAVLIFALgrPDPLPVVDTHVRRVLKRLGLIKEKPTPKEVERELEEL 138
|
|
| Nth |
COG0177 |
Endonuclease III [Replication, recombination and repair]; |
40-226 |
1.11e-29 |
|
Endonuclease III [Replication, recombination and repair];
Pssm-ID: 439947 [Multi-domain] Cd Length: 198 Bit Score: 113.65 E-value: 1.11e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199733524 40 HNKTAYRVWISEIMLQQT---QVTTVipyYERFMQRFPDIESLAQASVDEVLSYWAGLGYY-ARGRNLHKAAVTVMENFA 115
Cdd:COG0177 16 DYRDPFELLVATILSAQTtdeRVNKA---TPRLFARYPTPEALAAADLEELEELIRPIGLYrNKAKNIIALARILVEKYG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199733524 116 GEFPDKLEDIQSLPGIGQSTAGAIASIALKQRAPILDGNVKRVLARFaaieGWTGEKS---VSNQLWKladeLTPHQRVD 192
Cdd:COG0177 93 GEVPETREELESLPGVGRKTANVVLNFAFGKPAIAVDTHVHRVSNRL----GLVPGKDpeeVEKDLMK----LIPKEYWG 164
|
170 180 190
....*....|....*....|....*....|....
gi 1199733524 193 EYTQAIMDLGASLCSRRNPDCGQCPMQSACKAFA 226
Cdd:COG0177 165 DLHHLLILHGRYICKARKPKCEECPLADLCPYYG 198
|
|
| PRK13910 |
PRK13910 |
DNA glycosylase MutY; Provisional |
53-222 |
3.28e-28 |
|
DNA glycosylase MutY; Provisional
Pssm-ID: 172427 [Multi-domain] Cd Length: 289 Bit Score: 112.42 E-value: 3.28e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199733524 53 MLQQTQVTTVIP-YYERFMQRFPDIESLAQASVDEVLSYWAGLGYYARGRNLHKAAVTVMENFAGEFPDKLEDIQSLPGI 131
Cdd:PRK13910 1 MSQQTQINTVVErFYSPFLEAFPTLKDLANAPLEEVLLLWRGLGYYSRAKNLKKSAEICVKEHHSQLPNDYQSLLKLPGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199733524 132 GQSTAGAIASIALKQRAPILDGNVKRVLARFAAIEgwtgEKSVSNQLWKLADELTPHQRVDEYTQAIMDLGASLCSRRnP 211
Cdd:PRK13910 81 GAYTANAILCFGFREKSACVDANIKRVLLRLFGLD----PNIHAKDLQIKANDFLNLNESFNHNQALIDLGALICSPK-P 155
|
170
....*....|.
gi 1199733524 212 DCGQCPMQSAC 222
Cdd:PRK13910 156 KCAICPLNPYC 166
|
|
| NUDIX_DNA_Glycosylase_C-MutY |
cd03431 |
C-terminal domain of DNA glycosylase; DNA glycosylase (MutY in bacteria and hMYH in humans) is ... |
243-388 |
1.22e-24 |
|
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: 97.37 E-value: 1.22e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199733524 243 PVKEAWILAIRDaHGRLLFQKRPPTGIWGGLWSLPQVERDLNIAQLPDYIASQLGLQGQYKAEATPFEHQFSHFKLVLHP 322
Cdd:cd03431 2 PERYFTVLVLRD-GGRVLLEKRPEKGLLAGLWEFPLVETEEEEEEAEALLGLLAEELLLILEPLGEVKHVFSHFRLHITV 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1199733524 323 ILFECENPVSEAVGEYslegivshevqgsykiqeahkiqegftdsQFYSRAQWREIGLPAPIKKLL 388
Cdd:cd03431 81 YLVELPEAPPAAPDEG-----------------------------RWVDLEELDEYALPAPMRKLL 117
|
|
| NUDIX_4 |
pfam14815 |
NUDIX domain; |
249-388 |
1.04e-16 |
|
NUDIX domain;
Pssm-ID: 464330 [Multi-domain] Cd Length: 114 Bit Score: 75.43 E-value: 1.04e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199733524 249 ILAIRDAHGRLLFQKRPPTGIWGGLWSLPQVERDLNIAQLPDYIASQ-LGLQGQyKAEATPFEHQFSHFKLVLHpiLFEC 327
Cdd:pfam14815 2 VLVIRNGDGRVLLRKRPEKGLLGGLWEFPGGKVEPGETLEEALARLEeLGIEVE-VLEPGTVKHVFTHFRLTLH--VYLV 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1199733524 328 enpvseavgeyslegivsHEVQGSykiqeahkiQEGFTDSQFYSRAQWREIGLPAPIKKLL 388
Cdd:pfam14815 79 ------------------REVEGE---------EEPQQELRWVTPEELDKYALPAAVRKIL 112
|
|
| PRK10702 |
PRK10702 |
endonuclease III; Provisional |
77-223 |
1.10e-08 |
|
endonuclease III; Provisional
Pssm-ID: 182661 [Multi-domain] Cd Length: 211 Bit Score: 55.02 E-value: 1.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199733524 77 ESLAQASVDEVLSYWAGLGYY-ARGRNLHKAAVTVMENFAGEFPDKLEDIQSLPGIGQSTAGAIASIALKQRAPILDGNV 155
Cdd:PRK10702 62 AAMLELGVEGVKTYIKTIGLYnSKAENVIKTCRILLEQHNGEVPEDRAALEALPGVGRKTANVVLNTAFGWPTIAVDTHI 141
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1199733524 156 KRVLARFAAIEGWTGEKsVSNQLWKLadelTPHQ-RVDEYTQAIMDlGASLCSRRNPDCGQCPMQSACK 223
Cdd:PRK10702 142 FRVCNRTQFAPGKNVEQ-VEEKLLKV----VPAEfKVDCHHWLILH-GRYTCIARKPRCGSCIIEDLCE 204
|
|
| HHH |
pfam00633 |
Helix-hairpin-helix motif; The helix-hairpin-helix DNA-binding motif is found to be duplicated ... |
114-142 |
1.74e-05 |
|
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: 41.25 E-value: 1.74e-05
10 20
....*....|....*....|....*....
gi 1199733524 114 FAGEFPDKLEDIQSLPGIGQSTAGAIASI 142
Cdd:pfam00633 2 LEGLIPASVEELLALPGVGPKTAEAILSY 30
|
|
| HP0602 |
COG2231 |
3-Methyladenine DNA glycosylase, HhH-GPD/Endo3 superfamily [Replication, recombination and ... |
75-223 |
2.07e-03 |
|
3-Methyladenine DNA glycosylase, HhH-GPD/Endo3 superfamily [Replication, recombination and repair];
Pssm-ID: 441832 [Multi-domain] Cd Length: 220 Bit Score: 39.44 E-value: 2.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199733524 75 DIESLAQASVDEVLSYWAGLGYYAR-GRNLHKAAVTVMENFAGEFPD--KLEDIQ------SLPGIGQSTAGAIASIALK 145
Cdd:COG2231 61 DPEALAALDPEELAELIRPSGFYNQkAKRLKNLARWLVERYGGGLEKlkALPTEElreellSLKGIGPETADSILLYAFN 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199733524 146 QRAPILDGNVKRVLARFaaieGWTGEKSVSNQLWKLADELTPHQrVDEYTQ--A-IMDLGASLCsRRNPDCGQCPMQSAC 222
Cdd:COG2231 141 RPVFVVDAYTRRIFSRL----GLIEEDASYDELQRLFEENLPPD-VALYNEfhAlIVEHGKEYC-KKKPKCEECPLRDLC 214
|
.
gi 1199733524 223 K 223
Cdd:COG2231 215 P 215
|
|
| EndIII_4Fe-2S |
pfam10576 |
Iron-sulfur binding domain of endonuclease III; Escherichia coli endonuclease III (EC 4.2.99. ... |
206-222 |
5.59e-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: 33.90 E-value: 5.59e-03
|
| FES |
smart00525 |
iron-sulpphur binding domain in DNA-(apurinic or apyrimidinic site) lyase (subfamily of ENDO3); ... |
206-225 |
9.94e-03 |
|
iron-sulpphur binding domain in DNA-(apurinic or apyrimidinic site) lyase (subfamily of ENDO3);
Pssm-ID: 197771 [Multi-domain] Cd Length: 21 Bit Score: 33.29 E-value: 9.94e-03
|
| |
