|
Name |
Accession |
Description |
Interval |
E-value |
| MutY |
COG1194 |
Adenine-specific DNA glycosylase, acts on AG and A-oxoG pairs [Replication, recombination and ... |
3-345 |
6.97e-170 |
|
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: 476.55 E-value: 6.97e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446206907 3 QQSSFKENLIHWFDENQREMPWRQTTNPYYIWLSEVMLQQTQVKTVIDYYHRFVERFPTVEVLSQASEDEVLKYWEGLGY 82
Cdd:COG1194 2 DMASFAKRLLAWYDRHGRDLPWRQTRDPYRVWLSEIMLQQTQVATVIPYYERFLERFPTVEALAAAPEDEVLKLWEGLGY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446206907 83 YSRARNFHTAIKEVYDKYEGLVPKDPDQFKALKGVGPYTQAAVMSIAYNVPLATVDGNVFRVWSRLNDDYRDIKLQSTRK 162
Cdd:COG1194 82 YSRARNLHKAAQQVVEEHGGVFPDTYEELLALPGIGPYTAAAIASIAFGEPAPIVDGNVKRVLSRLFAIEGPIGSPAAKK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446206907 163 SYEQ---ELLPyvTTEAGTFNQAMMELGALICTPKNPLCLFCPVQENCEAFDKGTFEKLPVKSKNVSKKVIEQSVFLIRn 239
Cdd:COG1194 162 ELWAlaeELLP--PERPGDFNQALMDLGATVCTPKKPKCLLCPLQDDCAAFAEGRQEELPVKKPKKKKPERYGAALVIR- 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446206907 240 NQGQYLLQKRSEK-LLHGMWQFPMFESEH------ARHEMTEKIGHDIQPVEtPIFELKHQFTHLTWKIKVYAVSGAINI 312
Cdd:COG1194 239 DDGRVLLEKRPPKgLWGGLWEFPEFEWEEaedpeaLERWLREELGLEVEWLE-PLGTVRHVFTHFRLHLTVYLARVPAGP 317
|
330 340 350
....*....|....*....|....*....|...
gi 446206907 313 ETLPDDMIWFDLSDRDQYTFPVPMSKIYQFING 345
Cdd:COG1194 318 PAEPDGGRWVPLEELAALPLPAPMRKLLKALLK 350
|
|
| mutY |
TIGR01084 |
A/G-specific adenine glycosylase; This equivalog model identifies mutY members of the ... |
7-277 |
1.80e-112 |
|
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: 327.83 E-value: 1.80e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446206907 7 FKENLIHWFDENQRE-MPWRQTTNPYYIWLSEVMLQQTQVKTVIDYYHRFVERFPTVEVLSQASEDEVLKYWEGLGYYSR 85
Cdd:TIGR01084 2 FSEDLLSWYDKYGRKtLPWRQNKTPYRVWLSEVMLQQTQVATVIPYFERFLERFPTVQALANAPQDEVLKLWEGLGYYAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446206907 86 ARNFHTAIKEVYDKYEGLVPKDPDQFKALKGVGPYTQAAVMSIAYNVPLATVDGNVFRVWSRL---NDDYRDIKLQSTRK 162
Cdd:TIGR01084 82 ARNLHKAAQEVVEEFGGEFPQDFEDLAALPGVGRYTAGAILSFALNKPYPILDGNVKRVLSRLfavEGWPGKKKVENRLW 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446206907 163 SYEQELLPyvTTEAGTFNQAMMELGALICTPKNPLCLFCPVQENCEAFDKGTFEKLPVKSKNVSKKVIEQSVFLIRNNQG 242
Cdd:TIGR01084 162 TLAESLLP--KADPEAFNQALMDLGAMICTRKKPKCDLCPLQDFCLAYQQGTWEEYPVKKPKAAPPERTTYFLVLQNYDG 239
|
250 260 270
....*....|....*....|....*....|....*.
gi 446206907 243 QYLLQKRSEK-LLHGMWQFPMFESEHARHEMTEKIG 277
Cdd:TIGR01084 240 EVLLEQRPEKgLWGGLYCFPQFEDEDSLAFLLAQRG 275
|
|
| PRK10880 |
PRK10880 |
adenine DNA glycosylase; |
3-296 |
1.77e-69 |
|
adenine DNA glycosylase;
Pssm-ID: 182805 [Multi-domain] Cd Length: 350 Bit Score: 220.74 E-value: 1.77e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446206907 3 QQSSFKENLIHWFDENQRE-MPWRQTTNPYYIWLSEVMLQQTQVKTVIDYYHRFVERFPTVEVLSQASEDEVLKYWEGLG 81
Cdd:PRK10880 2 QASQFSAQVLDWYDKYGRKtLPWQIDKTPYKVWLSEVMLQQTQVATVIPYFERFMARFPTVTDLANAPLDEVLHLWTGLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446206907 82 YYSRARNFHTAIKEVYDKYEGLVPKDPDQFKALKGVGPYTQAAVMSIAYNVPLATVDGNVFRVWSRlnddYRDIKLQSTR 161
Cdd:PRK10880 82 YYARARNLHKAAQQVATLHGGEFPETFEEVAALPGVGRSTAGAILSLSLGKHFPILDGNVKRVLAR----CYAVSGWPGK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446206907 162 KSYEQELLPY---VTTEAGT--FNQAMMELGALICTPKNPLCLFCPVQENCEAFDKGTFEKLPVKSknvSKKVI-EQSVF 235
Cdd:PRK10880 158 KEVENRLWQLseqVTPAVGVerFNQAMMDLGAMVCTRSKPKCELCPLQNGCIAYANHSWALYPGKK---PKQTLpERTGY 234
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446206907 236 --LIRNNQGQYLLQKRSEKLLHGMWQFPMFESEHARHEMTEKIGHDIQPVEtPIFELKHQFTH 296
Cdd:PRK10880 235 flLLQHGDEVWLEQRPPSGLWGGLFCFPQFADEEELRQWLAQRGIAADNLT-QLTAFRHTFSH 296
|
|
| ENDO3c |
cd00056 |
endonuclease III; includes endonuclease III (DNA-(apurinic or apyrimidinic site) lyase), ... |
31-187 |
1.67e-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: 160.48 E-value: 1.67e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446206907 31 YYIWLSEVMLQQTQVKTVIDYYHRFVERF-PTVEVLSQASEDEVLKYWEGLGYYSRARNFHTAIKEVYDKYEGLVPKDPD 109
Cdd:cd00056 1 FEVLVSEILSQQTTDKAVNKAYERLFERYgPTPEALAAADEEELRELIRSLGYRRKAKYLKELARAIVEGFGGLVLDDPD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446206907 110 ---QFKALKGVGPYTQAAVMSIAYNVPLATVDGNVFRVWSRLNddyrDIKLQSTRKSYEQELLPYVTTE-AGTFNQAMME 185
Cdd:cd00056 81 areELLALPGVGRKTANVVLLFALGPDAFPVDTHVRRVLKRLG----LIPKKKTPEELEELLEELLPKPyWGEANQALMD 156
|
..
gi 446206907 186 LG 187
Cdd:cd00056 157 LG 158
|
|
| ENDO3c |
smart00478 |
endonuclease III; includes endonuclease III (DNA-(apurinic or apyrimidinic site) lyase), ... |
39-189 |
4.50e-34 |
|
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: 122.37 E-value: 4.50e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446206907 39 MLQQTQVKTVIDYYHRFVERFPTVEVLSQASEDEVLKYWEGLG-YYSRARNFHTAIKEVYDKYEGLVPKDPDQFKALKGV 117
Cdd:smart00478 1 LSQQTTDERVNKATERLFEKFPTPEDLAAADEEELEELIRGLGfYRRKARYLIELARILVEEYGGEVPDDREELLKLPGV 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446206907 118 GPYTQAAVMSIAYNVPLATVDGNVFRVWSRLNddyrDIKLQSTRKSYEQELLPYV-TTEAGTFNQAMMELGAL 189
Cdd:smart00478 81 GRKTANAVLSFALGKPFIPVDTHVLRIAKRLG----LVDKKSTPEEVEKLLEKLLpEEDWRELNLLLIDFGRT 149
|
|
| HhH-GPD |
pfam00730 |
HhH-GPD superfamily base excision DNA repair protein; This family contains a diverse range of ... |
35-148 |
1.37e-27 |
|
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: 105.06 E-value: 1.37e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446206907 35 LSEVMLQQTQVKTVIDYYHRFVER-FPTVEVLSQASEDEVLKYWEGLGYY-SRARNFHTAIKEVYDKYEGLVPKDPDQFK 112
Cdd:pfam00730 1 VSAILSQQTSDKAVNKITERLFEKfFPTPEDLADADEEELRELIRGLGFYrRKAKYLKELARILVEGYGGEVPLDEEELE 80
|
90 100 110
....*....|....*....|....*....|....*....
gi 446206907 113 A-LKGVGPYTQAAVMSIA--YNVPLATVDGNVFRVWSRL 148
Cdd:pfam00730 81 AlLKGVGRWTAEAVLIFAlgRPDPLPVVDTHVRRVLKRL 119
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| MutY |
COG1194 |
Adenine-specific DNA glycosylase, acts on AG and A-oxoG pairs [Replication, recombination and ... |
3-345 |
6.97e-170 |
|
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: 476.55 E-value: 6.97e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446206907 3 QQSSFKENLIHWFDENQREMPWRQTTNPYYIWLSEVMLQQTQVKTVIDYYHRFVERFPTVEVLSQASEDEVLKYWEGLGY 82
Cdd:COG1194 2 DMASFAKRLLAWYDRHGRDLPWRQTRDPYRVWLSEIMLQQTQVATVIPYYERFLERFPTVEALAAAPEDEVLKLWEGLGY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446206907 83 YSRARNFHTAIKEVYDKYEGLVPKDPDQFKALKGVGPYTQAAVMSIAYNVPLATVDGNVFRVWSRLNDDYRDIKLQSTRK 162
Cdd:COG1194 82 YSRARNLHKAAQQVVEEHGGVFPDTYEELLALPGIGPYTAAAIASIAFGEPAPIVDGNVKRVLSRLFAIEGPIGSPAAKK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446206907 163 SYEQ---ELLPyvTTEAGTFNQAMMELGALICTPKNPLCLFCPVQENCEAFDKGTFEKLPVKSKNVSKKVIEQSVFLIRn 239
Cdd:COG1194 162 ELWAlaeELLP--PERPGDFNQALMDLGATVCTPKKPKCLLCPLQDDCAAFAEGRQEELPVKKPKKKKPERYGAALVIR- 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446206907 240 NQGQYLLQKRSEK-LLHGMWQFPMFESEH------ARHEMTEKIGHDIQPVEtPIFELKHQFTHLTWKIKVYAVSGAINI 312
Cdd:COG1194 239 DDGRVLLEKRPPKgLWGGLWEFPEFEWEEaedpeaLERWLREELGLEVEWLE-PLGTVRHVFTHFRLHLTVYLARVPAGP 317
|
330 340 350
....*....|....*....|....*....|...
gi 446206907 313 ETLPDDMIWFDLSDRDQYTFPVPMSKIYQFING 345
Cdd:COG1194 318 PAEPDGGRWVPLEELAALPLPAPMRKLLKALLK 350
|
|
| mutY |
TIGR01084 |
A/G-specific adenine glycosylase; This equivalog model identifies mutY members of the ... |
7-277 |
1.80e-112 |
|
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: 327.83 E-value: 1.80e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446206907 7 FKENLIHWFDENQRE-MPWRQTTNPYYIWLSEVMLQQTQVKTVIDYYHRFVERFPTVEVLSQASEDEVLKYWEGLGYYSR 85
Cdd:TIGR01084 2 FSEDLLSWYDKYGRKtLPWRQNKTPYRVWLSEVMLQQTQVATVIPYFERFLERFPTVQALANAPQDEVLKLWEGLGYYAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446206907 86 ARNFHTAIKEVYDKYEGLVPKDPDQFKALKGVGPYTQAAVMSIAYNVPLATVDGNVFRVWSRL---NDDYRDIKLQSTRK 162
Cdd:TIGR01084 82 ARNLHKAAQEVVEEFGGEFPQDFEDLAALPGVGRYTAGAILSFALNKPYPILDGNVKRVLSRLfavEGWPGKKKVENRLW 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446206907 163 SYEQELLPyvTTEAGTFNQAMMELGALICTPKNPLCLFCPVQENCEAFDKGTFEKLPVKSKNVSKKVIEQSVFLIRNNQG 242
Cdd:TIGR01084 162 TLAESLLP--KADPEAFNQALMDLGAMICTRKKPKCDLCPLQDFCLAYQQGTWEEYPVKKPKAAPPERTTYFLVLQNYDG 239
|
250 260 270
....*....|....*....|....*....|....*.
gi 446206907 243 QYLLQKRSEK-LLHGMWQFPMFESEHARHEMTEKIG 277
Cdd:TIGR01084 240 EVLLEQRPEKgLWGGLYCFPQFEDEDSLAFLLAQRG 275
|
|
| PRK10880 |
PRK10880 |
adenine DNA glycosylase; |
3-296 |
1.77e-69 |
|
adenine DNA glycosylase;
Pssm-ID: 182805 [Multi-domain] Cd Length: 350 Bit Score: 220.74 E-value: 1.77e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446206907 3 QQSSFKENLIHWFDENQRE-MPWRQTTNPYYIWLSEVMLQQTQVKTVIDYYHRFVERFPTVEVLSQASEDEVLKYWEGLG 81
Cdd:PRK10880 2 QASQFSAQVLDWYDKYGRKtLPWQIDKTPYKVWLSEVMLQQTQVATVIPYFERFMARFPTVTDLANAPLDEVLHLWTGLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446206907 82 YYSRARNFHTAIKEVYDKYEGLVPKDPDQFKALKGVGPYTQAAVMSIAYNVPLATVDGNVFRVWSRlnddYRDIKLQSTR 161
Cdd:PRK10880 82 YYARARNLHKAAQQVATLHGGEFPETFEEVAALPGVGRSTAGAILSLSLGKHFPILDGNVKRVLAR----CYAVSGWPGK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446206907 162 KSYEQELLPY---VTTEAGT--FNQAMMELGALICTPKNPLCLFCPVQENCEAFDKGTFEKLPVKSknvSKKVI-EQSVF 235
Cdd:PRK10880 158 KEVENRLWQLseqVTPAVGVerFNQAMMDLGAMVCTRSKPKCELCPLQNGCIAYANHSWALYPGKK---PKQTLpERTGY 234
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446206907 236 --LIRNNQGQYLLQKRSEKLLHGMWQFPMFESEHARHEMTEKIGHDIQPVEtPIFELKHQFTH 296
Cdd:PRK10880 235 flLLQHGDEVWLEQRPPSGLWGGLFCFPQFADEEELRQWLAQRGIAADNLT-QLTAFRHTFSH 296
|
|
| ENDO3c |
cd00056 |
endonuclease III; includes endonuclease III (DNA-(apurinic or apyrimidinic site) lyase), ... |
31-187 |
1.67e-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: 160.48 E-value: 1.67e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446206907 31 YYIWLSEVMLQQTQVKTVIDYYHRFVERF-PTVEVLSQASEDEVLKYWEGLGYYSRARNFHTAIKEVYDKYEGLVPKDPD 109
Cdd:cd00056 1 FEVLVSEILSQQTTDKAVNKAYERLFERYgPTPEALAAADEEELRELIRSLGYRRKAKYLKELARAIVEGFGGLVLDDPD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446206907 110 ---QFKALKGVGPYTQAAVMSIAYNVPLATVDGNVFRVWSRLNddyrDIKLQSTRKSYEQELLPYVTTE-AGTFNQAMME 185
Cdd:cd00056 81 areELLALPGVGRKTANVVLLFALGPDAFPVDTHVRRVLKRLG----LIPKKKTPEELEELLEELLPKPyWGEANQALMD 156
|
..
gi 446206907 186 LG 187
Cdd:cd00056 157 LG 158
|
|
| ENDO3c |
smart00478 |
endonuclease III; includes endonuclease III (DNA-(apurinic or apyrimidinic site) lyase), ... |
39-189 |
4.50e-34 |
|
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: 122.37 E-value: 4.50e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446206907 39 MLQQTQVKTVIDYYHRFVERFPTVEVLSQASEDEVLKYWEGLG-YYSRARNFHTAIKEVYDKYEGLVPKDPDQFKALKGV 117
Cdd:smart00478 1 LSQQTTDERVNKATERLFEKFPTPEDLAAADEEELEELIRGLGfYRRKARYLIELARILVEEYGGEVPDDREELLKLPGV 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446206907 118 GPYTQAAVMSIAYNVPLATVDGNVFRVWSRLNddyrDIKLQSTRKSYEQELLPYV-TTEAGTFNQAMMELGAL 189
Cdd:smart00478 81 GRKTANAVLSFALGKPFIPVDTHVLRIAKRLG----LVDKKSTPEEVEKLLEKLLpEEDWRELNLLLIDFGRT 149
|
|
| PRK13910 |
PRK13910 |
DNA glycosylase MutY; Provisional |
39-261 |
2.95e-31 |
|
DNA glycosylase MutY; Provisional
Pssm-ID: 172427 [Multi-domain] Cd Length: 289 Bit Score: 119.36 E-value: 2.95e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446206907 39 MLQQTQVKTVID-YYHRFVERFPTVEVLSQASEDEVLKYWEGLGYYSRARNFHTAIKEVYDKYEGLVPKDPDQFKALKGV 117
Cdd:PRK13910 1 MSQQTQINTVVErFYSPFLEAFPTLKDLANAPLEEVLLLWRGLGYYSRAKNLKKSAEICVKEHHSQLPNDYQSLLKLPGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446206907 118 GPYTQAAVMSIAYNVPLATVDGNVFRVWSRLNDDYRDIKLQSTRKSYEQELlpyVTTEAGTFNQAMMELGALICTPKnPL 197
Cdd:PRK13910 81 GAYTANAILCFGFREKSACVDANIKRVLLRLFGLDPNIHAKDLQIKANDFL---NLNESFNHNQALIDLGALICSPK-PK 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446206907 198 CLFCPVQENCeaFDKGTFEKLPVKSKnvsKKVIEQSVFL---IRNNqgQYLLQKRSEKLLHGMWQFP 261
Cdd:PRK13910 157 CAICPLNPYC--LGKNNPEKHTLKKK---QEIVQEERYLgvvIQNN--QIALEKIEQKLYLGMHHFP 216
|
|
| NUDIX_DNA_Glycosylase_C-MutY |
cd03431 |
C-terminal domain of DNA glycosylase; DNA glycosylase (MutY in bacteria and hMYH in humans) is ... |
227-341 |
3.86e-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: 111.24 E-value: 3.86e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446206907 227 KKVIEQSVFLIRNnQGQYLLQKRSEK-LLHGMWQFPMFESEHARHEMTEKIGHDIQPVE---TPIFELKHQFTHLTWKIK 302
Cdd:cd03431 1 VPERYFTVLVLRD-GGRVLLEKRPEKgLLAGLWEFPLVETEEEEEEAEALLGLLAEELLlilEPLGEVKHVFSHFRLHIT 79
|
90 100 110
....*....|....*....|....*....|....*....
gi 446206907 303 VYAVSGAINIETLPDDMIWFDLSDRDQYTFPVPMSKIYQ 341
Cdd:cd03431 80 VYLVELPEAPPAAPDEGRWVDLEELDEYALPAPMRKLLE 118
|
|
| HhH-GPD |
pfam00730 |
HhH-GPD superfamily base excision DNA repair protein; This family contains a diverse range of ... |
35-148 |
1.37e-27 |
|
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: 105.06 E-value: 1.37e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446206907 35 LSEVMLQQTQVKTVIDYYHRFVER-FPTVEVLSQASEDEVLKYWEGLGYY-SRARNFHTAIKEVYDKYEGLVPKDPDQFK 112
Cdd:pfam00730 1 VSAILSQQTSDKAVNKITERLFEKfFPTPEDLADADEEELRELIRGLGFYrRKAKYLKELARILVEGYGGEVPLDEEELE 80
|
90 100 110
....*....|....*....|....*....|....*....
gi 446206907 113 A-LKGVGPYTQAAVMSIA--YNVPLATVDGNVFRVWSRL 148
Cdd:pfam00730 81 AlLKGVGRWTAEAVLIFAlgRPDPLPVVDTHVRRVLKRL 119
|
|
| Nth |
COG0177 |
Endonuclease III [Replication, recombination and repair]; |
23-211 |
5.47e-26 |
|
Endonuclease III [Replication, recombination and repair];
Pssm-ID: 439947 [Multi-domain] Cd Length: 198 Bit Score: 102.48 E-value: 5.47e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446206907 23 PWRQTTNPYYIWLSEVMLQQTQVKTVIDYYHRFVERFPTVEVLSQASEDEVLKYWEGLGYY-SRARNFHTAIKEVYDKYE 101
Cdd:COG0177 13 TELDYRDPFELLVATILSAQTTDERVNKATPRLFARYPTPEALAAADLEELEELIRPIGLYrNKAKNIIALARILVEKYG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446206907 102 GLVPKDPDQFKALKGVGPYTQAAVMSIAYNVPLATVDGNVFRVWSRL----NDDYRDIklqstrksyEQELLPYVTTEAG 177
Cdd:COG0177 93 GEVPETREELESLPGVGRKTANVVLNFAFGKPAIAVDTHVHRVSNRLglvpGKDPEEV---------EKDLMKLIPKEYW 163
|
170 180 190
....*....|....*....|....*....|....*
gi 446206907 178 T-FNQAMMELGALICTPKNPLCLFCPVQENCEAFD 211
Cdd:COG0177 164 GdLHHLLILHGRYICKARKPKCEECPLADLCPYYG 198
|
|
| NUDIX_4 |
pfam14815 |
NUDIX domain; |
234-339 |
4.72e-25 |
|
NUDIX domain;
Pssm-ID: 464330 [Multi-domain] Cd Length: 114 Bit Score: 97.77 E-value: 4.72e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446206907 234 VFLIRNNQGQYLLQKRSEK-LLHGMWQFP---MFESEHARHEMTEKIGHDIQPVETPIFELKHQFTHLTWKIKVYAVSGA 309
Cdd:pfam14815 2 VLVIRNGDGRVLLRKRPEKgLLGGLWEFPggkVEPGETLEEALARLEELGIEVEVLEPGTVKHVFTHFRLTLHVYLVREV 81
|
90 100 110
....*....|....*....|....*....|
gi 446206907 310 INIETLPDDMIWFDLSDRDQYTFPVPMSKI 339
Cdd:pfam14815 82 EGEEEPQQELRWVTPEELDKYALPAAVRKI 111
|
|
| PRK10702 |
PRK10702 |
endonuclease III; Provisional |
61-212 |
9.69e-09 |
|
endonuclease III; Provisional
Pssm-ID: 182661 [Multi-domain] Cd Length: 211 Bit Score: 55.02 E-value: 9.69e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446206907 61 TVEVLSQASEDEVLKYWEGLGYY-SRARNFHTAIKEVYDKYEGLVPKDPDQFKALKGVGPYTQAAVMSIAYNVPLATVDG 139
Cdd:PRK10702 60 TPAAMLELGVEGVKTYIKTIGLYnSKAENVIKTCRILLEQHNGEVPEDRAALEALPGVGRKTANVVLNTAFGWPTIAVDT 139
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446206907 140 NVFRVWSRLNddyrdIKLQSTRKSYEQELLPYVTTEAGTFNQAMMEL-GALICTPKNPLCLFCPVQENCEAFDK 212
Cdd:PRK10702 140 HIFRVCNRTQ-----FAPGKNVEQVEEKLLKVVPAEFKVDCHHWLILhGRYTCIARKPRCGSCIIEDLCEYKEK 208
|
|
| YjhB |
COG1051 |
ADP-ribose pyrophosphatase YjhB, NUDIX family [Nucleotide transport and metabolism]; |
236-333 |
3.44e-06 |
|
ADP-ribose pyrophosphatase YjhB, NUDIX family [Nucleotide transport and metabolism];
Pssm-ID: 440671 [Multi-domain] Cd Length: 125 Bit Score: 45.74 E-value: 3.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446206907 236 LIRNNQGQYLLQKRSEKLLHGMWQFP-----MFESEH--ARHEMTEKIGHDIQPVE-TPIFELKHQFTHLTWKIKVYAVS 307
Cdd:COG1051 12 VIFRKDGRVLLVRRADEPGKGLWALPggkvePGETPEeaALRELREETGLEVEVLElLGVFDHPDRGHVVSVAFLAEVLS 91
|
90 100
....*....|....*....|....*.
gi 446206907 308 GAINIETLPDDMIWFDLSDRDQYTFP 333
Cdd:COG1051 92 GEPRADDEIDEARWFPLDELPELAFT 117
|
|
| HHH |
pfam00633 |
Helix-hairpin-helix motif; The helix-hairpin-helix DNA-binding motif is found to be duplicated ... |
99-128 |
3.72e-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: 40.09 E-value: 3.72e-05
10 20 30
....*....|....*....|....*....|
gi 446206907 99 KYEGLVPKDPDQFKALKGVGPYTQAAVMSI 128
Cdd:pfam00633 1 SLEGLIPASVEELLALPGVGPKTAEAILSY 30
|
|
| NUDIX_Hydrolase |
cd02883 |
NUDIX hydrolase superfamily; NUDIX hydrolase is a superfamily of enzymes found in all three ... |
236-323 |
2.03e-04 |
|
NUDIX hydrolase superfamily; NUDIX hydrolase is a superfamily of enzymes found in all three kingdoms of life, and it catalyzes the hydrolysis of NUcleoside DIphosphates linked to other moieties, X. Enzymes belonging to this superfamily require a divalent cation, such as Mg2+ or Mn2+ for their activity. Members of this family are recognized by a highly conserved 23-residue NUDIX motif (GX5EX7REUXEEXGU, where U = I, L or V), which forms a structural motif that functions as a metal binding and catalytic site. Substrates of NUDIX hydrolase include intact and oxidatively damaged nucleoside triphosphates, dinucleoside polyphosphates, nucleotide-sugars and dinucleotide enzymes. These substrates are metabolites or cell signaling molecules that require regulation during different stages of the cell cycle or during periods of stress. In general, the role of the NUDIX hydrolase is to sanitize the nucleotide pools and to maintain cell viability, thereby serving as surveillance and "house-cleaning" enzymes. Substrate specificity is used to define child families within the superfamily. Differences in substrate specificity are determined by the N-terminal extension or by residues in variable loop regions. Mechanistically, substrate hydrolysis occurs by a nucleophilic substitution reaction, with variation in the numbers and roles of divalent cations required. This superfamily consists of at least nine families: IPP (isopentenyl diphosphate) isomerase, ADP ribose pyrophosphatase, mutT pyrophosphohydrolase, coenzyme-A pyrophosphatase, MTH1-7,8-dihydro-8-oxoguanine-triphosphatase, diadenosine tetraphosphate hydrolase, NADH pyrophosphatase, GDP-mannose hydrolase and the c-terminal portion of the mutY adenine glycosylase.
Pssm-ID: 467528 [Multi-domain] Cd Length: 106 Bit Score: 40.08 E-value: 2.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446206907 236 LIRNNQGQYLLQKRSEKLLHGMWQFP---MFESEH----ARHEMTEKIGHDIQPVE-TPIFELKHQFTHLTWKIKVYAVS 307
Cdd:cd02883 6 VVFDDEGRVLLVRRSDGPGPGGWELPgggVEPGETpeeaAVREVREETGLDVEVLRlLGVYEFPDPDEGRHVVVLVFLAR 85
|
90 100
....*....|....*....|.
gi 446206907 308 GAINIETLPD-----DMIWFD 323
Cdd:cd02883 86 VVGGEPPPLDdeeisEVRWVP 106
|
|
| HP0602 |
COG2231 |
3-Methyladenine DNA glycosylase, HhH-GPD/Endo3 superfamily [Replication, recombination and ... |
61-208 |
1.12e-03 |
|
3-Methyladenine DNA glycosylase, HhH-GPD/Endo3 superfamily [Replication, recombination and repair];
Pssm-ID: 441832 [Multi-domain] Cd Length: 220 Bit Score: 39.83 E-value: 1.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446206907 61 TVEVLSQASEDEVLKYWEGLGYY----SRARNFHTAIKEVYDK-YEGLVPKDPDQFK----ALKGVGPYTQAAVMSIAYN 131
Cdd:COG2231 61 DPEALAALDPEELAELIRPSGFYnqkaKRLKNLARWLVERYGGgLEKLKALPTEELReellSLKGIGPETADSILLYAFN 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446206907 132 VPLATVDGNVFRVWSRLNddyrdikLQSTRKSYEQ------ELLPYvttEAGTFNQ--AMM-ELGALICTPKnPLCLFCP 202
Cdd:COG2231 141 RPVFVVDAYTRRIFSRLG-------LIEEDASYDElqrlfeENLPP---DVALYNEfhALIvEHGKEYCKKK-PKCEECP 209
|
....*.
gi 446206907 203 VQENCE 208
Cdd:COG2231 210 LRDLCP 215
|
|
| NUDIX_Hydrolase |
cd18882 |
uncharacterized NUDIX hydrolase subfamily; NUDIX hydrolase is a superfamily of enzymes found ... |
236-326 |
1.98e-03 |
|
uncharacterized NUDIX hydrolase subfamily; NUDIX hydrolase is a superfamily of enzymes found in all three kingdoms of life, and it catalyzes the hydrolysis of NUcleoside DIphosphates linked to other moieties, X. Enzymes belonging to this superfamily require a divalent cation, such as Mg2+ or Mn2+ for their activity. Members of this family are recognized by a highly conserved 23-residue NUDIX motif (GX5EX7REUXEEXGU, where U = I, L or V), which forms a structural motif that functions as a metal binding and catalytic site. Substrates of NUDIX hydrolase include intact and oxidatively damaged nucleoside triphosphates, dinucleoside polyphosphates, nucleotide-sugars and dinucleotide enzymes. These substrates are metabolites or cell signaling molecules that require regulation during different stages of the cell cycle or during periods of stress. In general, the role of the NUDIX hydrolase is to sanitize the nucleotide pools and to maintain cell viability, thereby serving as surveillance and "house-cleaning" enzymes. Substrate specificity is used to define child families within the superfamily. Differences in substrate specificity are determined by the N-terminal extension or by residues in variable loop regions. Mechanistically, substrate hydrolysis occurs by a nucleophilic substitution reaction, with variation in the numbers and roles of divalent cations required. This superfamily consists of at least nine families: IPP (isopentenyl diphosphate) isomerase, ADP ribose pyrophosphatase, mutT pyrophosphohydrolase, coenzyme-A pyrophosphatase, MTH1-7,8-dihydro-8-oxoguanine-triphosphatase, diadenosine tetraphosphate hydrolase, NADH pyrophosphatase, GDP-mannose hydrolase and the c-terminal portion of the mutY adenine glycosylase.
Pssm-ID: 467593 [Multi-domain] Cd Length: 130 Bit Score: 38.01 E-value: 1.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446206907 236 LIRNNQGQYLLQKRSEK---LLHGMWQFP---MFESEH----ARHEMTEKIGHDIQPVEtpiFELKHQFTHLTWKIK-VY 304
Cdd:cd18882 7 ILYDDRGKVLLQLRDDKpgiPYPGYWGLFgghLEPGETpeeaIRRELEEEIGYEPGEFR---FFLLYTEDDGEDRIRhVF 83
|
90 100
....*....|....*....|....*.
gi 446206907 305 AVSGAINIETLP----DDMIWFDLSD 326
Cdd:cd18882 84 HAPLDVDLSDLVlnegQALRLFSPEE 109
|
|
| FES |
smart00525 |
iron-sulpphur binding domain in DNA-(apurinic or apyrimidinic site) lyase (subfamily of ENDO3); ... |
190-210 |
3.00e-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: 34.45 E-value: 3.00e-03
|
| EndIII_4Fe-2S |
pfam10576 |
Iron-sulfur binding domain of endonuclease III; Escherichia coli endonuclease III (EC 4.2.99. ... |
191-207 |
4.08e-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: 34.28 E-value: 4.08e-03
|
| NUDIX |
pfam00293 |
NUDIX domain; |
236-341 |
9.31e-03 |
|
NUDIX domain;
Pssm-ID: 395229 [Multi-domain] Cd Length: 132 Bit Score: 35.92 E-value: 9.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446206907 236 LIRNNQGQYLLQKRSEKLLHGMWQFP---MFESEH----ARHEMTEKIGhdIQPVETPIFELKH-------QFTHLTWKI 301
Cdd:pfam00293 9 VLLNEKGRVLLVRRSKKPFPGWWSLPggkVEPGETpeeaARRELEEETG--LEPELLELLGSLHylapfdgRFPDEHEIL 86
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 446206907 302 KVYAVSGAINIETLPDDMI----WFDLSDRDQYTFPVPMSKIYQ 341
Cdd:pfam00293 87 YVFLAEVEGELEPDPDGEVeevrWVPLEELLLLKLAPGDRKLLP 130
|
|
| |
