|
Name |
Accession |
Description |
Interval |
E-value |
| MutY |
COG1194 |
Adenine-specific DNA glycosylase, acts on AG and A-oxoG pairs [Replication, recombination and ... |
8-352 |
7.25e-176 |
|
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: 491.96 E-value: 7.25e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493854769 8 RLSSILIRWYNRNKRDLPWRDTTDPYIIWISEIILQQTRVDQGYAYFTRFVKRFPSVDLLAQAEEDEVLKLWQGLGYYSR 87
Cdd:COG1194 5 SFAKRLLAWYDRHGRDLPWRQTRDPYRVWLSEIMLQQTQVATVIPYYERFLERFPTVEALAAAPEDEVLKLWEGLGYYSR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493854769 88 ARNLHAAAKIVLEKYQGVFPQDYTDVLSMKGVGEYTAAAIVSFAYDQPHAVVDGNVFRVLSRIFAVEEPIDSTKGKKLFS 167
Cdd:COG1194 85 ARNLHKAAQQVVEEHGGVFPDTYEELLALPGIGPYTAAAIASIAFGEPAPIVDGNVKRVLSRLFAIEGPIGSPAAKKELW 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493854769 168 QLAQELLDDKRAGLHNQAIMEFGALQCVPVSPDCNSCPASVMCLAYAQDKVNVYPVKAGKQKVRARFFNYFDVRYgDGYM 247
Cdd:COG1194 165 ALAEELLPPERPGDFNQALMDLGATVCTPKKPKCLLCPLQDDCAAFAEGRQEELPVKKPKKKKPERYGAALVIRD-DGRV 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493854769 248 LLHKRTAKDIWQGLYELPLIETAEAMSIEELHRTdsFRRIFeNGDGLHIKYITQMKHILSHQAIHAVFYQVEVRKVSAV- 326
Cdd:COG1194 244 LLEKRPPKGLWGGLWEFPEFEWEEAEDPEALERW--LREEL-GLEVEWLEPLGTVRHVFTHFRLHLTVYLARVPAGPPAe 320
|
330 340
....*....|....*....|....*..
gi 493854769 327 -DGYIEVRASDVDEYPVSRLVHKYLEK 352
Cdd:COG1194 321 pDGGRWVPLEELAALPLPAPMRKLLKA 347
|
|
| mutY |
TIGR01084 |
A/G-specific adenine glycosylase; This equivalog model identifies mutY members of the ... |
9-274 |
4.34e-117 |
|
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: 340.16 E-value: 4.34e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493854769 9 LSSILIRWYNRNKR-DLPWRDTTDPYIIWISEIILQQTRVDQGYAYFTRFVKRFPSVDLLAQAEEDEVLKLWQGLGYYSR 87
Cdd:TIGR01084 2 FSEDLLSWYDKYGRkTLPWRQNKTPYRVWLSEVMLQQTQVATVIPYFERFLERFPTVQALANAPQDEVLKLWEGLGYYAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493854769 88 ARNLHAAAKIVLEKYQGVFPQDYTDVLSMKGVGEYTAAAIVSFAYDQPHAVVDGNVFRVLSRIFAVEEPIDSTKGKKLFS 167
Cdd:TIGR01084 82 ARNLHKAAQEVVEEFGGEFPQDFEDLAALPGVGRYTAGAILSFALNKPYPILDGNVKRVLSRLFAVEGWPGKKKVENRLW 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493854769 168 QLAQELLDDKRAGLHNQAIMEFGALQCVPVSPDCNSCPASVMCLAYAQDKVNVYPVKAGKQKVRARFFNYFDVRYGDGYM 247
Cdd:TIGR01084 162 TLAESLLPKADPEAFNQALMDLGAMICTRKKPKCDLCPLQDFCLAYQQGTWEEYPVKKPKAAPPERTTYFLVLQNYDGEV 241
|
250 260
....*....|....*....|....*..
gi 493854769 248 LLHKRTAKDIWQGLYELPLIETAEAMS 274
Cdd:TIGR01084 242 LLEQRPEKGLWGGLYCFPQFEDEDSLA 268
|
|
| PRK10880 |
PRK10880 |
adenine DNA glycosylase; |
10-308 |
1.11e-74 |
|
adenine DNA glycosylase;
Pssm-ID: 182805 [Multi-domain] Cd Length: 350 Bit Score: 234.60 E-value: 1.11e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493854769 10 SSILIRWYNRNKRD-LPWRDTTDPYIIWISEIILQQTRVDQGYAYFTRFVKRFPSVDLLAQAEEDEVLKLWQGLGYYSRA 88
Cdd:PRK10880 7 SAQVLDWYDKYGRKtLPWQIDKTPYKVWLSEVMLQQTQVATVIPYFERFMARFPTVTDLANAPLDEVLHLWTGLGYYARA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493854769 89 RNLHAAAKIVLEKYQGVFPQDYTDVLSMKGVGEYTAAAIVSFAYDQPHAVVDGNVFRVLSRIFAVEE-PIDSTKGKKLFs 167
Cdd:PRK10880 87 RNLHKAAQQVATLHGGEFPETFEEVAALPGVGRSTAGAILSLSLGKHFPILDGNVKRVLARCYAVSGwPGKKEVENRLW- 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493854769 168 QLAQELLDDKRAGLHNQAIMEFGALQCVPVSPDCNSCPASVMCLAYAQDKVNVYPVKAGKQKVRARfFNYFDVRYGDGYM 247
Cdd:PRK10880 166 QLSEQVTPAVGVERFNQAMMDLGAMVCTRSKPKCELCPLQNGCIAYANHSWALYPGKKPKQTLPER-TGYFLLLQHGDEV 244
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 493854769 248 LLHKRTAKDIWQGLYELPLIETAEAMSiEELHRtdsfRRIfeNGDGLhiKYITQMKHILSH 308
Cdd:PRK10880 245 WLEQRPPSGLWGGLFCFPQFADEEELR-QWLAQ----RGI--AADNL--TQLTAFRHTFSH 296
|
|
| ENDO3c |
cd00056 |
endonuclease III; includes endonuclease III (DNA-(apurinic or apyrimidinic site) lyase), ... |
33-190 |
3.08e-47 |
|
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: 157.40 E-value: 3.08e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493854769 33 YIIWISEIILQQTRVDQGYAYFTRFVKRF-PSVDLLAQAEEDEVLKLWQGLGYYSRARNLHAAAKIVLEKYQGVF---PQ 108
Cdd:cd00056 1 FEVLVSEILSQQTTDKAVNKAYERLFERYgPTPEALAAADEEELRELIRSLGYRRKAKYLKELARAIVEGFGGLVlddPD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493854769 109 DYTDVLSMKGVGEYTAAAIVSFAYDQPHAVVDGNVFRVLSRIFAVEEPIDstkgKKLFSQLAQELLDDKRAGLHNQAIME 188
Cdd:cd00056 81 AREELLALPGVGRKTANVVLLFALGPDAFPVDTHVRRVLKRLGLIPKKKT----PEELEELLEELLPKPYWGEANQALMD 156
|
..
gi 493854769 189 FG 190
Cdd:cd00056 157 LG 158
|
|
| ENDO3c |
smart00478 |
endonuclease III; includes endonuclease III (DNA-(apurinic or apyrimidinic site) lyase), ... |
41-192 |
1.53e-36 |
|
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: 129.31 E-value: 1.53e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493854769 41 ILQQTRVDQGYAYFTRFVKRFPSVDLLAQAEEDEVLKLWQGLG-YYSRARNLHAAAKIVLEKYQGVFPQDYTDVLSMKGV 119
Cdd:smart00478 1 LSQQTTDERVNKATERLFEKFPTPEDLAAADEEELEELIRGLGfYRRKARYLIELARILVEEYGGEVPDDREELLKLPGV 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 493854769 120 GEYTAAAIVSFAYDQPHAVVDGNVFRVLSRIFAVEEpidsTKGKKLFSQLAQELLDDKRAGLHNQAIMEFGAL 192
Cdd:smart00478 81 GRKTANAVLSFALGKPFIPVDTHVLRIAKRLGLVDK----KSTPEEVEKLLEKLLPEEDWRELNLLLIDFGRT 149
|
|
| HhH-GPD |
pfam00730 |
HhH-GPD superfamily base excision DNA repair protein; This family contains a diverse range of ... |
37-174 |
2.88e-32 |
|
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: 117.77 E-value: 2.88e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493854769 37 ISEIILQQTRVDQGYAYFTRFVKR-FPSVDLLAQAEEDEVLKLWQGLGYY-SRARNLHAAAKIVLEKYQGVFPQDYTDVL 114
Cdd:pfam00730 1 VSAILSQQTSDKAVNKITERLFEKfFPTPEDLADADEEELRELIRGLGFYrRKAKYLKELARILVEGYGGEVPLDEEELE 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 493854769 115 SM-KGVGEYTAAAIVSFA--YDQPHAVVDGNVFRVLSRIFAveepIDSTKGKKLFSQLAQELL 174
Cdd:pfam00730 81 ALlKGVGRWTAEAVLIFAlgRPDPLPVVDTHVRRVLKRLGL----IKEKPTPKEVERELEELW 139
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| MutY |
COG1194 |
Adenine-specific DNA glycosylase, acts on AG and A-oxoG pairs [Replication, recombination and ... |
8-352 |
7.25e-176 |
|
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: 491.96 E-value: 7.25e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493854769 8 RLSSILIRWYNRNKRDLPWRDTTDPYIIWISEIILQQTRVDQGYAYFTRFVKRFPSVDLLAQAEEDEVLKLWQGLGYYSR 87
Cdd:COG1194 5 SFAKRLLAWYDRHGRDLPWRQTRDPYRVWLSEIMLQQTQVATVIPYYERFLERFPTVEALAAAPEDEVLKLWEGLGYYSR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493854769 88 ARNLHAAAKIVLEKYQGVFPQDYTDVLSMKGVGEYTAAAIVSFAYDQPHAVVDGNVFRVLSRIFAVEEPIDSTKGKKLFS 167
Cdd:COG1194 85 ARNLHKAAQQVVEEHGGVFPDTYEELLALPGIGPYTAAAIASIAFGEPAPIVDGNVKRVLSRLFAIEGPIGSPAAKKELW 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493854769 168 QLAQELLDDKRAGLHNQAIMEFGALQCVPVSPDCNSCPASVMCLAYAQDKVNVYPVKAGKQKVRARFFNYFDVRYgDGYM 247
Cdd:COG1194 165 ALAEELLPPERPGDFNQALMDLGATVCTPKKPKCLLCPLQDDCAAFAEGRQEELPVKKPKKKKPERYGAALVIRD-DGRV 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493854769 248 LLHKRTAKDIWQGLYELPLIETAEAMSIEELHRTdsFRRIFeNGDGLHIKYITQMKHILSHQAIHAVFYQVEVRKVSAV- 326
Cdd:COG1194 244 LLEKRPPKGLWGGLWEFPEFEWEEAEDPEALERW--LREEL-GLEVEWLEPLGTVRHVFTHFRLHLTVYLARVPAGPPAe 320
|
330 340
....*....|....*....|....*..
gi 493854769 327 -DGYIEVRASDVDEYPVSRLVHKYLEK 352
Cdd:COG1194 321 pDGGRWVPLEELAALPLPAPMRKLLKA 347
|
|
| mutY |
TIGR01084 |
A/G-specific adenine glycosylase; This equivalog model identifies mutY members of the ... |
9-274 |
4.34e-117 |
|
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: 340.16 E-value: 4.34e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493854769 9 LSSILIRWYNRNKR-DLPWRDTTDPYIIWISEIILQQTRVDQGYAYFTRFVKRFPSVDLLAQAEEDEVLKLWQGLGYYSR 87
Cdd:TIGR01084 2 FSEDLLSWYDKYGRkTLPWRQNKTPYRVWLSEVMLQQTQVATVIPYFERFLERFPTVQALANAPQDEVLKLWEGLGYYAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493854769 88 ARNLHAAAKIVLEKYQGVFPQDYTDVLSMKGVGEYTAAAIVSFAYDQPHAVVDGNVFRVLSRIFAVEEPIDSTKGKKLFS 167
Cdd:TIGR01084 82 ARNLHKAAQEVVEEFGGEFPQDFEDLAALPGVGRYTAGAILSFALNKPYPILDGNVKRVLSRLFAVEGWPGKKKVENRLW 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493854769 168 QLAQELLDDKRAGLHNQAIMEFGALQCVPVSPDCNSCPASVMCLAYAQDKVNVYPVKAGKQKVRARFFNYFDVRYGDGYM 247
Cdd:TIGR01084 162 TLAESLLPKADPEAFNQALMDLGAMICTRKKPKCDLCPLQDFCLAYQQGTWEEYPVKKPKAAPPERTTYFLVLQNYDGEV 241
|
250 260
....*....|....*....|....*..
gi 493854769 248 LLHKRTAKDIWQGLYELPLIETAEAMS 274
Cdd:TIGR01084 242 LLEQRPEKGLWGGLYCFPQFEDEDSLA 268
|
|
| PRK10880 |
PRK10880 |
adenine DNA glycosylase; |
10-308 |
1.11e-74 |
|
adenine DNA glycosylase;
Pssm-ID: 182805 [Multi-domain] Cd Length: 350 Bit Score: 234.60 E-value: 1.11e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493854769 10 SSILIRWYNRNKRD-LPWRDTTDPYIIWISEIILQQTRVDQGYAYFTRFVKRFPSVDLLAQAEEDEVLKLWQGLGYYSRA 88
Cdd:PRK10880 7 SAQVLDWYDKYGRKtLPWQIDKTPYKVWLSEVMLQQTQVATVIPYFERFMARFPTVTDLANAPLDEVLHLWTGLGYYARA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493854769 89 RNLHAAAKIVLEKYQGVFPQDYTDVLSMKGVGEYTAAAIVSFAYDQPHAVVDGNVFRVLSRIFAVEE-PIDSTKGKKLFs 167
Cdd:PRK10880 87 RNLHKAAQQVATLHGGEFPETFEEVAALPGVGRSTAGAILSLSLGKHFPILDGNVKRVLARCYAVSGwPGKKEVENRLW- 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493854769 168 QLAQELLDDKRAGLHNQAIMEFGALQCVPVSPDCNSCPASVMCLAYAQDKVNVYPVKAGKQKVRARfFNYFDVRYGDGYM 247
Cdd:PRK10880 166 QLSEQVTPAVGVERFNQAMMDLGAMVCTRSKPKCELCPLQNGCIAYANHSWALYPGKKPKQTLPER-TGYFLLLQHGDEV 244
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 493854769 248 LLHKRTAKDIWQGLYELPLIETAEAMSiEELHRtdsfRRIfeNGDGLhiKYITQMKHILSH 308
Cdd:PRK10880 245 WLEQRPPSGLWGGLFCFPQFADEEELR-QWLAQ----RGI--AADNL--TQLTAFRHTFSH 296
|
|
| ENDO3c |
cd00056 |
endonuclease III; includes endonuclease III (DNA-(apurinic or apyrimidinic site) lyase), ... |
33-190 |
3.08e-47 |
|
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: 157.40 E-value: 3.08e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493854769 33 YIIWISEIILQQTRVDQGYAYFTRFVKRF-PSVDLLAQAEEDEVLKLWQGLGYYSRARNLHAAAKIVLEKYQGVF---PQ 108
Cdd:cd00056 1 FEVLVSEILSQQTTDKAVNKAYERLFERYgPTPEALAAADEEELRELIRSLGYRRKAKYLKELARAIVEGFGGLVlddPD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493854769 109 DYTDVLSMKGVGEYTAAAIVSFAYDQPHAVVDGNVFRVLSRIFAVEEPIDstkgKKLFSQLAQELLDDKRAGLHNQAIME 188
Cdd:cd00056 81 AREELLALPGVGRKTANVVLLFALGPDAFPVDTHVRRVLKRLGLIPKKKT----PEELEELLEELLPKPYWGEANQALMD 156
|
..
gi 493854769 189 FG 190
Cdd:cd00056 157 LG 158
|
|
| ENDO3c |
smart00478 |
endonuclease III; includes endonuclease III (DNA-(apurinic or apyrimidinic site) lyase), ... |
41-192 |
1.53e-36 |
|
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: 129.31 E-value: 1.53e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493854769 41 ILQQTRVDQGYAYFTRFVKRFPSVDLLAQAEEDEVLKLWQGLG-YYSRARNLHAAAKIVLEKYQGVFPQDYTDVLSMKGV 119
Cdd:smart00478 1 LSQQTTDERVNKATERLFEKFPTPEDLAAADEEELEELIRGLGfYRRKARYLIELARILVEEYGGEVPDDREELLKLPGV 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 493854769 120 GEYTAAAIVSFAYDQPHAVVDGNVFRVLSRIFAVEEpidsTKGKKLFSQLAQELLDDKRAGLHNQAIMEFGAL 192
Cdd:smart00478 81 GRKTANAVLSFALGKPFIPVDTHVLRIAKRLGLVDK----KSTPEEVEKLLEKLLPEEDWRELNLLLIDFGRT 149
|
|
| PRK13910 |
PRK13910 |
DNA glycosylase MutY; Provisional |
43-212 |
4.77e-33 |
|
DNA glycosylase MutY; Provisional
Pssm-ID: 172427 [Multi-domain] Cd Length: 289 Bit Score: 124.36 E-value: 4.77e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493854769 43 QQTRVDQGYA-YFTRFVKRFPSVDLLAQAEEDEVLKLWQGLGYYSRARNLHAAAKIVLEKYQGVFPQDYTDVLSMKGVGE 121
Cdd:PRK13910 3 QQTQINTVVErFYSPFLEAFPTLKDLANAPLEEVLLLWRGLGYYSRAKNLKKSAEICVKEHHSQLPNDYQSLLKLPGIGA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493854769 122 YTAAAIVSFAYDQPHAVVDGNVFRVLSRIFAVEEPIDStkgkKLFSQLAQELLDDKRAGLHNQAIMEFGALQCVPvSPDC 201
Cdd:PRK13910 83 YTANAILCFGFREKSACVDANIKRVLLRLFGLDPNIHA----KDLQIKANDFLNLNESFNHNQALIDLGALICSP-KPKC 157
|
170
....*....|.
gi 493854769 202 NSCPASVMCLA 212
Cdd:PRK13910 158 AICPLNPYCLG 168
|
|
| HhH-GPD |
pfam00730 |
HhH-GPD superfamily base excision DNA repair protein; This family contains a diverse range of ... |
37-174 |
2.88e-32 |
|
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: 117.77 E-value: 2.88e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493854769 37 ISEIILQQTRVDQGYAYFTRFVKR-FPSVDLLAQAEEDEVLKLWQGLGYY-SRARNLHAAAKIVLEKYQGVFPQDYTDVL 114
Cdd:pfam00730 1 VSAILSQQTSDKAVNKITERLFEKfFPTPEDLADADEEELRELIRGLGFYrRKAKYLKELARILVEGYGGEVPLDEEELE 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 493854769 115 SM-KGVGEYTAAAIVSFA--YDQPHAVVDGNVFRVLSRIFAveepIDSTKGKKLFSQLAQELL 174
Cdd:pfam00730 81 ALlKGVGRWTAEAVLIFAlgRPDPLPVVDTHVRRVLKRLGL----IKEKPTPKEVERELEELW 139
|
|
| NUDIX_DNA_Glycosylase_C-MutY |
cd03431 |
C-terminal domain of DNA glycosylase; DNA glycosylase (MutY in bacteria and hMYH in humans) is ... |
230-351 |
7.97e-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: 7.97e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493854769 230 VRARFFNYFDVRYGDGYmLLHKRTAKDIWQGLYELPLIETAEAMSIEELHrtdsfRRIFENGDGLHIKYITQMKHILSHQ 309
Cdd:cd03431 1 VPERYFTVLVLRDGGRV-LLEKRPEKGLLAGLWEFPLVETEEEEEEAEAL-----LGLLAEELLLILEPLGEVKHVFSHF 74
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 493854769 310 AIHAVFYQVEVRKVSAV--DGYIEVRASDVDEYPVSRLVHKYLE 351
Cdd:cd03431 75 RLHITVYLVELPEAPPAapDEGRWVDLEELDEYALPAPMRKLLE 118
|
|
| Nth |
COG0177 |
Endonuclease III [Replication, recombination and repair]; |
12-214 |
2.82e-28 |
|
Endonuclease III [Replication, recombination and repair];
Pssm-ID: 439947 [Multi-domain] Cd Length: 198 Bit Score: 109.03 E-value: 2.82e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493854769 12 ILIRWYNRNKRDLPWRDttdPYIIWISEIILQQT---RVDQGYAyftRFVKRFPSVDLLAQAEEDEVLKLWQGLGYY-SR 87
Cdd:COG0177 3 RLKELYPDAKTELDYRD---PFELLVATILSAQTtdeRVNKATP---RLFARYPTPEALAAADLEELEELIRPIGLYrNK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493854769 88 ARNLHAAAKIVLEKYQGVFPQDYTDVLSMKGVGEYTAAAIVSFAYDQPHAVVDGNVFRVLSRI--------FAVEepids 159
Cdd:COG0177 77 AKNIIALARILVEKYGGEVPETREELESLPGVGRKTANVVLNFAFGKPAIAVDTHVHRVSNRLglvpgkdpEEVE----- 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 493854769 160 tkgKKLfsqlaQELLDDKRAGLHNQAIMEFGALQCVPVSPDCNSCPASVMCLAYA 214
Cdd:COG0177 152 ---KDL-----MKLIPKEYWGDLHHLLILHGRYICKARKPKCEECPLADLCPYYG 198
|
|
| NUDIX_4 |
pfam14815 |
NUDIX domain; |
240-352 |
2.24e-17 |
|
NUDIX domain;
Pssm-ID: 464330 [Multi-domain] Cd Length: 114 Bit Score: 76.97 E-value: 2.24e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493854769 240 VRYGDGYMLLHKRTAKDIWQGLYELPLIETAEAMSIEELHrtdsFRRIFENGDGLHIKYITqMKHILSHQAIHAVFYQVE 319
Cdd:pfam14815 5 IRNGDGRVLLRKRPEKGLLGGLWEFPGGKVEPGETLEEAL----ARLEELGIEVEVLEPGT-VKHVFTHFRLTLHVYLVR 79
|
90 100 110
....*....|....*....|....*....|....*
gi 493854769 320 --VRKVSAVDGYIEVRASDVDEYPVSRLVHKYLEK 352
Cdd:pfam14815 80 evEGEEEPQQELRWVTPEELDKYALPAAVRKILEA 114
|
|
| PRK10702 |
PRK10702 |
endonuclease III; Provisional |
1-222 |
4.13e-11 |
|
endonuclease III; Provisional
Pssm-ID: 182661 [Multi-domain] Cd Length: 211 Bit Score: 61.96 E-value: 4.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493854769 1 MSKEKDLrlsSILIRWYNRNKRDLPWRDTTDPYIIWISEII-LQQTRVDQGYAYftrfVKRFPSVDLLAQAEE---DEVL 76
Cdd:PRK10702 1 MNKAKRL---EILTRLRDNNPHPTTELNFSSPFELLIAVLLsAQATDVSVNKAT----AKLYPVANTPAAMLElgvEGVK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493854769 77 KLWQGLGYY-SRARNLHAAAKIVLEKYQGVFPQDYTDVLSMKGVGEYTAAAIVSFAYDQPHAVVDGNVFRVLSRI-FAVE 154
Cdd:PRK10702 74 TYIKTIGLYnSKAENVIKTCRILLEQHNGEVPEDRAALEALPGVGRKTANVVLNTAFGWPTIAVDTHIFRVCNRTqFAPG 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 493854769 155 EPIDSTKGKKLFSQLAQELLDdkragLHNQAIMEfGALQCVPVSPDCNSCPASVMClayaQDKVNVYP 222
Cdd:PRK10702 154 KNVEQVEEKLLKVVPAEFKVD-----CHHWLILH-GRYTCIARKPRCGSCIIEDLC----EYKEKVDI 211
|
|
| HP0602 |
COG2231 |
3-Methyladenine DNA glycosylase, HhH-GPD/Endo3 superfamily [Replication, recombination and ... |
63-215 |
9.91e-11 |
|
3-Methyladenine DNA glycosylase, HhH-GPD/Endo3 superfamily [Replication, recombination and repair];
Pssm-ID: 441832 [Multi-domain] Cd Length: 220 Bit Score: 60.63 E-value: 9.91e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493854769 63 SVDLLAQAEEDEVLKLWQGLGYYSR-ARNLHAAAKIVLEKYQG---VFPQDYTDV-----LSMKGVGEYTAAAIVSFAYD 133
Cdd:COG2231 61 DPEALAALDPEELAELIRPSGFYNQkAKRLKNLARWLVERYGGgleKLKALPTEElreelLSLKGIGPETADSILLYAFN 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493854769 134 QPHAVVDGNVFRVLSRIFAVEEPIDSTKGKKLF-SQLAQELLDDKRagLHNQaIMEFGALQCVPvSPDCNSCPASVMCLA 212
Cdd:COG2231 141 RPVFVVDAYTRRIFSRLGLIEEDASYDELQRLFeENLPPDVALYNE--FHAL-IVEHGKEYCKK-KPKCEECPLRDLCPY 216
|
...
gi 493854769 213 YAQ 215
Cdd:COG2231 217 GGQ 219
|
|
| AlkA |
COG0122 |
3-methyladenine DNA glycosylase/8-oxoguanine DNA glycosylase [Replication, recombination and ... |
22-158 |
7.78e-06 |
|
3-methyladenine DNA glycosylase/8-oxoguanine DNA glycosylase [Replication, recombination and repair];
Pssm-ID: 439892 [Multi-domain] Cd Length: 255 Bit Score: 46.80 E-value: 7.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493854769 22 RDLPWRDTTDPYIIWISEIILQQTRVDQGYAYFTRFVKR--------------FPSVDLLAQAEEDEVLKLwqGLGYYsR 87
Cdd:COG0122 74 PGLRLPRRPDPFEALVRAILGQQVSVAAARTIWRRLVALfgepiegpggglyaFPTPEALAAASEEELRAC--GLSRR-K 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493854769 88 ARNLHAAAKIVLEK---YQGVFPQDYTDV----LSMKGVGEYTAAAIVSFAYDQPHA--VVDGNVFRVLSRIFAVEEPID 158
Cdd:COG0122 151 ARYLRALARAVADGeldLEALAGLDDEEAiarlTALPGIGPWTAEMVLLFALGRPDAfpAGDLGLRRALGRLYGLGERPT 230
|
|
| HHH |
pfam00633 |
Helix-hairpin-helix motif; The helix-hairpin-helix DNA-binding motif is found to be duplicated ... |
101-130 |
8.05e-04 |
|
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: 36.24 E-value: 8.05e-04
10 20 30
....*....|....*....|....*....|
gi 493854769 101 KYQGVFPQDYTDVLSMKGVGEYTAAAIVSF 130
Cdd:pfam00633 1 SLEGLIPASVEELLALPGVGPKTAEAILSY 30
|
|
| |
