|
Name |
Accession |
Description |
Interval |
E-value |
| MutY |
COG1194 |
Adenine-specific DNA glycosylase, acts on AG and A-oxoG pairs [Replication, recombination and ... |
15-384 |
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: 526.63 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446808878 15 EKIISFREKLLNWYDENKRDLPWRRSKNPYHIWVSEIMLQQTRVDTVIPYYERFLDWFPTVESLANAPEERLLKAWEGLG 94
Cdd:COG1194 1 MDMASFAKRLLAWYDRHGRDLPWRQTRDPYRVWLSEIMLQQTQVATVIPYYERFLERFPTVEALAAAPEDEVLKLWEGLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446808878 95 YYSRVRNMQAAAQQIMADFGGQFPNTYEGISSLKGIGPYTAGAISSIAFNLPEPAVDGNVMRVLARLFEVNHDIGVPSNR 174
Cdd:COG1194 81 YYSRARNLHKAAQQVVEEHGGVFPDTYEELLALPGIGPYTAAAIASIAFGEPAPIVDGNVKRVLSRLFAIEGPIGSPAAK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446808878 175 KIFQAMMEILIDPKRPGDFNQALMDLGSDIEAPVNPRPEESPVKDFSAAYQNGTMGRYPIKEPKKKPLPIYLKALVVRnD 254
Cdd:COG1194 161 KELWALAEELLPPERPGDFNQALMDLGATVCTPKKPKCLLCPLQDDCAAFAEGRQEELPVKKPKKKKPERYGAALVIR-D 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446808878 255 QGQFLLEKNESEKLLAGFWHFPLIEVDDFSSDDnqldlfsqvteesrvfgpSPQENFEQDYDLEVNWSQQvFDQVKHVFS 334
Cdd:COG1194 240 DGRVLLEKRPPKGLWGGLWEFPEFEWEEAEDPE------------------ALERWLREELGLEVEWLEP-LGTVRHVFT 300
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 446808878 335 HRKWHIQIIAGQVTETKQFSDREIRWVSPQEFSDYPLAKPQQKIWQAYKN 384
Cdd:COG1194 301 HFRLHLTVYLARVPAGPPAEPDGGRWVPLEELAALPLPAPMRKLLKALLK 350
|
|
| mutY |
TIGR01084 |
A/G-specific adenine glycosylase; This equivalog model identifies mutY members of the ... |
20-282 |
3.69e-124 |
|
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: 359.42 E-value: 3.69e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446808878 20 FREKLLNWYDENKR-DLPWRRSKNPYHIWVSEIMLQQTRVDTVIPYYERFLDWFPTVESLANAPEERLLKAWEGLGYYSR 98
Cdd:TIGR01084 2 FSEDLLSWYDKYGRkTLPWRQNKTPYRVWLSEVMLQQTQVATVIPYFERFLERFPTVQALANAPQDEVLKLWEGLGYYAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446808878 99 VRNMQAAAQQIMADFGGQFPNTYEGISSLKGIGPYTAGAISSIAFNLPEPAVDGNVMRVLARLFEVNHDIGVPSNRKIFQ 178
Cdd:TIGR01084 82 ARNLHKAAQEVVEEFGGEFPQDFEDLAALPGVGRYTAGAILSFALNKPYPILDGNVKRVLSRLFAVEGWPGKKKVENRLW 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446808878 179 AMMEILIDPKRPGDFNQALMDLGSDIEAPVNPRPEESPVKDFSAAYQNGTMGRYPIKEPKKKPLPIYLKALVVRNDQGQF 258
Cdd:TIGR01084 162 TLAESLLPKADPEAFNQALMDLGAMICTRKKPKCDLCPLQDFCLAYQQGTWEEYPVKKPKAAPPERTTYFLVLQNYDGEV 241
|
250 260
....*....|....*....|....
gi 446808878 259 LLEKNESEKLLAGFWHFPLIEVDD 282
Cdd:TIGR01084 242 LLEQRPEKGLWGGLYCFPQFEDED 265
|
|
| PRK10880 |
PRK10880 |
adenine DNA glycosylase; |
20-273 |
1.70e-70 |
|
adenine DNA glycosylase;
Pssm-ID: 182805 [Multi-domain] Cd Length: 350 Bit Score: 224.97 E-value: 1.70e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446808878 20 FREKLLNWYDENKRD-LPWRRSKNPYHIWVSEIMLQQTRVDTVIPYYERFLDWFPTVESLANAPEERLLKAWEGLGYYSR 98
Cdd:PRK10880 6 FSAQVLDWYDKYGRKtLPWQIDKTPYKVWLSEVMLQQTQVATVIPYFERFMARFPTVTDLANAPLDEVLHLWTGLGYYAR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446808878 99 VRNMQAAAQQIMADFGGQFPNTYEGISSLKGIGPYTAGAISSIAFNLPEPAVDGNVMRVLARLFEVNhdiGVPSNRKIFQ 178
Cdd:PRK10880 86 ARNLHKAAQQVATLHGGEFPETFEEVAALPGVGRSTAGAILSLSLGKHFPILDGNVKRVLARCYAVS---GWPGKKEVEN 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446808878 179 AMMEIL--IDPKRP-GDFNQALMDLGSDIEAPVNPRPEESPVKDFSAAYQNGTMGRYPIKEPKKKpLPiylkalvvrNDQ 255
Cdd:PRK10880 163 RLWQLSeqVTPAVGvERFNQAMMDLGAMVCTRSKPKCELCPLQNGCIAYANHSWALYPGKKPKQT-LP---------ERT 232
|
250 260
....*....|....*....|...
gi 446808878 256 GQFLLEKNESEKLLA-----GFW 273
Cdd:PRK10880 233 GYFLLLQHGDEVWLEqrppsGLW 255
|
|
| ENDO3c |
cd00056 |
endonuclease III; includes endonuclease III (DNA-(apurinic or apyrimidinic site) lyase), ... |
44-201 |
8.98e-55 |
|
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: 177.82 E-value: 8.98e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446808878 44 YHIWVSEIMLQQTRVDTVIPYYERFLD-WFPTVESLANAPEERLLKAWEGLGYYSRVRNMQAAAQQIMADFGG---QFPN 119
Cdd:cd00056 1 FEVLVSEILSQQTTDKAVNKAYERLFErYGPTPEALAAADEEELRELIRSLGYRRKAKYLKELARAIVEGFGGlvlDDPD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446808878 120 TYEGISSLKGIGPYTAGAISSIAFNLPEPAVDGNVMRVLARLFevnhDIGVPSNRKIFQAMMEILIDPKRPGDFNQALMD 199
Cdd:cd00056 81 AREELLALPGVGRKTANVVLLFALGPDAFPVDTHVRRVLKRLG----LIPKKKTPEELEELLEELLPKPYWGEANQALMD 156
|
..
gi 446808878 200 LG 201
Cdd:cd00056 157 LG 158
|
|
| ENDO3c |
smart00478 |
endonuclease III; includes endonuclease III (DNA-(apurinic or apyrimidinic site) lyase), ... |
52-201 |
7.25e-42 |
|
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: 143.94 E-value: 7.25e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446808878 52 MLQQTRVDTVIPYYERFLDWFPTVESLANAPEERLLKAWEGLG-YYSRVRNMQAAAQQIMADFGGQFPNTYEGISSLKGI 130
Cdd:smart00478 1 LSQQTTDERVNKATERLFEKFPTPEDLAAADEEELEELIRGLGfYRRKARYLIELARILVEEYGGEVPDDREELLKLPGV 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446808878 131 GPYTAGAISSIAFNLPEPAVDGNVMRVLARLFEVNHdigvPSNRKIFQAMMEILIDPKRPGDFNQALMDLG 201
Cdd:smart00478 81 GRKTANAVLSFALGKPFIPVDTHVLRIAKRLGLVDK----KSTPEEVEKLLEKLLPEEDWRELNLLLIDFG 147
|
|
| HhH-GPD |
pfam00730 |
HhH-GPD superfamily base excision DNA repair protein; This family contains a diverse range of ... |
48-184 |
2.06e-35 |
|
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: 126.63 E-value: 2.06e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446808878 48 VSEIMLQQTRVDTVIPYYERFLD-WFPTVESLANAPEERLLKAWEGLGYY-SRVRNMQAAAQQIMADFGGQFPNTY-EGI 124
Cdd:pfam00730 1 VSAILSQQTSDKAVNKITERLFEkFFPTPEDLADADEEELRELIRGLGFYrRKAKYLKELARILVEGYGGEVPLDEeELE 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446808878 125 SSLKGIGPYTAGAISSIAFNLPE--PAVDGNVMRVLARLFEVNhdiGVPSNRKIFQAMMEIL 184
Cdd:pfam00730 81 ALLKGVGRWTAEAVLIFALGRPDplPVVDTHVRRVLKRLGLIK---EKPTPKEVERELEELW 139
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| MutY |
COG1194 |
Adenine-specific DNA glycosylase, acts on AG and A-oxoG pairs [Replication, recombination and ... |
15-384 |
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: 526.63 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446808878 15 EKIISFREKLLNWYDENKRDLPWRRSKNPYHIWVSEIMLQQTRVDTVIPYYERFLDWFPTVESLANAPEERLLKAWEGLG 94
Cdd:COG1194 1 MDMASFAKRLLAWYDRHGRDLPWRQTRDPYRVWLSEIMLQQTQVATVIPYYERFLERFPTVEALAAAPEDEVLKLWEGLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446808878 95 YYSRVRNMQAAAQQIMADFGGQFPNTYEGISSLKGIGPYTAGAISSIAFNLPEPAVDGNVMRVLARLFEVNHDIGVPSNR 174
Cdd:COG1194 81 YYSRARNLHKAAQQVVEEHGGVFPDTYEELLALPGIGPYTAAAIASIAFGEPAPIVDGNVKRVLSRLFAIEGPIGSPAAK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446808878 175 KIFQAMMEILIDPKRPGDFNQALMDLGSDIEAPVNPRPEESPVKDFSAAYQNGTMGRYPIKEPKKKPLPIYLKALVVRnD 254
Cdd:COG1194 161 KELWALAEELLPPERPGDFNQALMDLGATVCTPKKPKCLLCPLQDDCAAFAEGRQEELPVKKPKKKKPERYGAALVIR-D 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446808878 255 QGQFLLEKNESEKLLAGFWHFPLIEVDDFSSDDnqldlfsqvteesrvfgpSPQENFEQDYDLEVNWSQQvFDQVKHVFS 334
Cdd:COG1194 240 DGRVLLEKRPPKGLWGGLWEFPEFEWEEAEDPE------------------ALERWLREELGLEVEWLEP-LGTVRHVFT 300
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 446808878 335 HRKWHIQIIAGQVTETKQFSDREIRWVSPQEFSDYPLAKPQQKIWQAYKN 384
Cdd:COG1194 301 HFRLHLTVYLARVPAGPPAEPDGGRWVPLEELAALPLPAPMRKLLKALLK 350
|
|
| mutY |
TIGR01084 |
A/G-specific adenine glycosylase; This equivalog model identifies mutY members of the ... |
20-282 |
3.69e-124 |
|
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: 359.42 E-value: 3.69e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446808878 20 FREKLLNWYDENKR-DLPWRRSKNPYHIWVSEIMLQQTRVDTVIPYYERFLDWFPTVESLANAPEERLLKAWEGLGYYSR 98
Cdd:TIGR01084 2 FSEDLLSWYDKYGRkTLPWRQNKTPYRVWLSEVMLQQTQVATVIPYFERFLERFPTVQALANAPQDEVLKLWEGLGYYAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446808878 99 VRNMQAAAQQIMADFGGQFPNTYEGISSLKGIGPYTAGAISSIAFNLPEPAVDGNVMRVLARLFEVNHDIGVPSNRKIFQ 178
Cdd:TIGR01084 82 ARNLHKAAQEVVEEFGGEFPQDFEDLAALPGVGRYTAGAILSFALNKPYPILDGNVKRVLSRLFAVEGWPGKKKVENRLW 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446808878 179 AMMEILIDPKRPGDFNQALMDLGSDIEAPVNPRPEESPVKDFSAAYQNGTMGRYPIKEPKKKPLPIYLKALVVRNDQGQF 258
Cdd:TIGR01084 162 TLAESLLPKADPEAFNQALMDLGAMICTRKKPKCDLCPLQDFCLAYQQGTWEEYPVKKPKAAPPERTTYFLVLQNYDGEV 241
|
250 260
....*....|....*....|....
gi 446808878 259 LLEKNESEKLLAGFWHFPLIEVDD 282
Cdd:TIGR01084 242 LLEQRPEKGLWGGLYCFPQFEDED 265
|
|
| PRK10880 |
PRK10880 |
adenine DNA glycosylase; |
20-273 |
1.70e-70 |
|
adenine DNA glycosylase;
Pssm-ID: 182805 [Multi-domain] Cd Length: 350 Bit Score: 224.97 E-value: 1.70e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446808878 20 FREKLLNWYDENKRD-LPWRRSKNPYHIWVSEIMLQQTRVDTVIPYYERFLDWFPTVESLANAPEERLLKAWEGLGYYSR 98
Cdd:PRK10880 6 FSAQVLDWYDKYGRKtLPWQIDKTPYKVWLSEVMLQQTQVATVIPYFERFMARFPTVTDLANAPLDEVLHLWTGLGYYAR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446808878 99 VRNMQAAAQQIMADFGGQFPNTYEGISSLKGIGPYTAGAISSIAFNLPEPAVDGNVMRVLARLFEVNhdiGVPSNRKIFQ 178
Cdd:PRK10880 86 ARNLHKAAQQVATLHGGEFPETFEEVAALPGVGRSTAGAILSLSLGKHFPILDGNVKRVLARCYAVS---GWPGKKEVEN 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446808878 179 AMMEIL--IDPKRP-GDFNQALMDLGSDIEAPVNPRPEESPVKDFSAAYQNGTMGRYPIKEPKKKpLPiylkalvvrNDQ 255
Cdd:PRK10880 163 RLWQLSeqVTPAVGvERFNQAMMDLGAMVCTRSKPKCELCPLQNGCIAYANHSWALYPGKKPKQT-LP---------ERT 232
|
250 260
....*....|....*....|...
gi 446808878 256 GQFLLEKNESEKLLA-----GFW 273
Cdd:PRK10880 233 GYFLLLQHGDEVWLEqrppsGLW 255
|
|
| ENDO3c |
cd00056 |
endonuclease III; includes endonuclease III (DNA-(apurinic or apyrimidinic site) lyase), ... |
44-201 |
8.98e-55 |
|
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: 177.82 E-value: 8.98e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446808878 44 YHIWVSEIMLQQTRVDTVIPYYERFLD-WFPTVESLANAPEERLLKAWEGLGYYSRVRNMQAAAQQIMADFGG---QFPN 119
Cdd:cd00056 1 FEVLVSEILSQQTTDKAVNKAYERLFErYGPTPEALAAADEEELRELIRSLGYRRKAKYLKELARAIVEGFGGlvlDDPD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446808878 120 TYEGISSLKGIGPYTAGAISSIAFNLPEPAVDGNVMRVLARLFevnhDIGVPSNRKIFQAMMEILIDPKRPGDFNQALMD 199
Cdd:cd00056 81 AREELLALPGVGRKTANVVLLFALGPDAFPVDTHVRRVLKRLG----LIPKKKTPEELEELLEELLPKPYWGEANQALMD 156
|
..
gi 446808878 200 LG 201
Cdd:cd00056 157 LG 158
|
|
| ENDO3c |
smart00478 |
endonuclease III; includes endonuclease III (DNA-(apurinic or apyrimidinic site) lyase), ... |
52-201 |
7.25e-42 |
|
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: 143.94 E-value: 7.25e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446808878 52 MLQQTRVDTVIPYYERFLDWFPTVESLANAPEERLLKAWEGLG-YYSRVRNMQAAAQQIMADFGGQFPNTYEGISSLKGI 130
Cdd:smart00478 1 LSQQTTDERVNKATERLFEKFPTPEDLAAADEEELEELIRGLGfYRRKARYLIELARILVEEYGGEVPDDREELLKLPGV 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446808878 131 GPYTAGAISSIAFNLPEPAVDGNVMRVLARLFEVNHdigvPSNRKIFQAMMEILIDPKRPGDFNQALMDLG 201
Cdd:smart00478 81 GRKTANAVLSFALGKPFIPVDTHVLRIAKRLGLVDK----KSTPEEVEKLLEKLLPEEDWRELNLLLIDFG 147
|
|
| HhH-GPD |
pfam00730 |
HhH-GPD superfamily base excision DNA repair protein; This family contains a diverse range of ... |
48-184 |
2.06e-35 |
|
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: 126.63 E-value: 2.06e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446808878 48 VSEIMLQQTRVDTVIPYYERFLD-WFPTVESLANAPEERLLKAWEGLGYY-SRVRNMQAAAQQIMADFGGQFPNTY-EGI 124
Cdd:pfam00730 1 VSAILSQQTSDKAVNKITERLFEkFFPTPEDLADADEEELRELIRGLGFYrRKAKYLKELARILVEGYGGEVPLDEeELE 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446808878 125 SSLKGIGPYTAGAISSIAFNLPE--PAVDGNVMRVLARLFEVNhdiGVPSNRKIFQAMMEIL 184
Cdd:pfam00730 81 ALLKGVGRWTAEAVLIFALGRPDplPVVDTHVRRVLKRLGLIK---EKPTPKEVERELEELW 139
|
|
| PRK13910 |
PRK13910 |
DNA glycosylase MutY; Provisional |
52-276 |
3.10e-29 |
|
DNA glycosylase MutY; Provisional
Pssm-ID: 172427 [Multi-domain] Cd Length: 289 Bit Score: 114.73 E-value: 3.10e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446808878 52 MLQQTRVDTVIP-YYERFLDWFPTVESLANAPEERLLKAWEGLGYYSRVRNMQAAAQQIMADFGGQFPNTYEGISSLKGI 130
Cdd:PRK13910 1 MSQQTQINTVVErFYSPFLEAFPTLKDLANAPLEEVLLLWRGLGYYSRAKNLKKSAEICVKEHHSQLPNDYQSLLKLPGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446808878 131 GPYTAGAISSIAFNLPEPAVDGNVMRVLARLFEVNHDIgvpsNRKIFQAMMEILIDPKRPGDFNQALMDLGSDIEAPvNP 210
Cdd:PRK13910 81 GAYTANAILCFGFREKSACVDANIKRVLLRLFGLDPNI----HAKDLQIKANDFLNLNESFNHNQALIDLGALICSP-KP 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446808878 211 RPEESPVKDFsaayqngTMGR-YPIKEPKKKPLPI-----YLkALVVRNDqgQFLLEKNEsEKLLAGFWHFP 276
Cdd:PRK13910 156 KCAICPLNPY-------CLGKnNPEKHTLKKKQEIvqeerYL-GVVIQNN--QIALEKIE-QKLYLGMHHFP 216
|
|
| Nth |
COG0177 |
Endonuclease III [Replication, recombination and repair]; |
22-220 |
4.28e-29 |
|
Endonuclease III [Replication, recombination and repair];
Pssm-ID: 439947 [Multi-domain] Cd Length: 198 Bit Score: 111.73 E-value: 4.28e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446808878 22 EKLLNWYDENKRDLPWRrskNPYHIWVSEIMLQQTRVDTVIPYYERFLDWFPTVESLANAPEERLLKAWEGLGYY-SRVR 100
Cdd:COG0177 2 ERLKELYPDAKTELDYR---DPFELLVATILSAQTTDERVNKATPRLFARYPTPEALAAADLEELEELIRPIGLYrNKAK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446808878 101 NMQAAAQQIMADFGGQFPNTYEGISSLKGIGPYTAGAISSIAFNLPEPAVDGNVMRVLARLfevnhdiG-VPSN--RKIF 177
Cdd:COG0177 79 NIIALARILVEKYGGEVPETREELESLPGVGRKTANVVLNFAFGKPAIAVDTHVHRVSNRL-------GlVPGKdpEEVE 151
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 446808878 178 QAMMEIlIDPKRPGDFNQALMDLGSDIEAPVNPRPEESPVKDF 220
Cdd:COG0177 152 KDLMKL-IPKEYWGDLHHLLILHGRYICKARKPKCEECPLADL 193
|
|
| NUDIX_DNA_Glycosylase_C-MutY |
cd03431 |
C-terminal domain of DNA glycosylase; DNA glycosylase (MutY in bacteria and hMYH in humans) is ... |
243-380 |
2.56e-27 |
|
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: 104.31 E-value: 2.56e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446808878 243 PIYLKALVVRnDQGQFLLEKNESEKLLAGFWHFPLIEVDDfssddnqldlfsqvteesrvfGPSPQENFEQDYDLEVNWS 322
Cdd:cd03431 3 ERYFTVLVLR-DGGRVLLEKRPEKGLLAGLWEFPLVETEE---------------------EEEEAEALLGLLAEELLLI 60
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 446808878 323 QQVFDQVKHVFSHRKWHIQIIAGQVTETKQFSDREIRWVSPQEFSDYPLAKPQQKIWQ 380
Cdd:cd03431 61 LEPLGEVKHVFSHFRLHITVYLVELPEAPPAAPDEGRWVDLEELDEYALPAPMRKLLE 118
|
|
| NUDIX_4 |
pfam14815 |
NUDIX domain; |
248-381 |
4.80e-19 |
|
NUDIX domain;
Pssm-ID: 464330 [Multi-domain] Cd Length: 114 Bit Score: 81.98 E-value: 4.80e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446808878 248 ALVVRNDQGQFLLEKNESEKLLAGFWHFPLIEVDDfssddnqldlfsqvteesrvfGPSPQENFEQDYDLEVNWSQQVFD 327
Cdd:pfam14815 2 VLVIRNGDGRVLLRKRPEKGLLGGLWEFPGGKVEP---------------------GETLEEALARLEELGIEVEVLEPG 60
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 446808878 328 QVKHVFSHRKWHIQIIAGQVTETKQFSDREIRWVSPQEFSDYPLAKPQQKIWQA 381
Cdd:pfam14815 61 TVKHVFTHFRLTLHVYLVREVEGEEEPQQELRWVTPEELDKYALPAAVRKILEA 114
|
|
| HP0602 |
COG2231 |
3-Methyladenine DNA glycosylase, HhH-GPD/Endo3 superfamily [Replication, recombination and ... |
19-226 |
2.98e-06 |
|
3-Methyladenine DNA glycosylase, HhH-GPD/Endo3 superfamily [Replication, recombination and repair];
Pssm-ID: 441832 [Multi-domain] Cd Length: 220 Bit Score: 47.92 E-value: 2.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446808878 19 SFREKLLNWYDENKR---DLPWRRSKNPYHIWVSEIMLQQTR---VDTVIpyyERF-----LDwfptVESLANAPEERLL 87
Cdd:COG2231 2 NTKEDLLEIYERLLEhygPQHWWPAETPFEVIVGAILTQNTSwknVEKAI---ANLkeaglLD----PEALAALDPEELA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446808878 88 KAWEGLGYY----SRVRNMqaaAQQIMADFGGQFPNTYEG--------ISSLKGIGPYTAGAISSIAFNLPEPAVDGNVM 155
Cdd:COG2231 75 ELIRPSGFYnqkaKRLKNL---ARWLVERYGGGLEKLKALpteelreeLLSLKGIGPETADSILLYAFNRPVFVVDAYTR 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446808878 156 RVLARLFEVNHDIGVPSNRKIFqamMEILidPKRPGDFNQ--ALMD-LGSDIEAPvNPRPEESPVKDFSAAYQN 226
Cdd:COG2231 152 RIFSRLGLIEEDASYDELQRLF---EENL--PPDVALYNEfhALIVeHGKEYCKK-KPKCEECPLRDLCPYGGQ 219
|
|
| AlkA |
COG0122 |
3-methyladenine DNA glycosylase/8-oxoguanine DNA glycosylase [Replication, recombination and ... |
33-182 |
3.57e-06 |
|
3-methyladenine DNA glycosylase/8-oxoguanine DNA glycosylase [Replication, recombination and repair];
Pssm-ID: 439892 [Multi-domain] Cd Length: 255 Bit Score: 47.96 E-value: 3.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446808878 33 RDLPWRRSKNPYHIWVSEIMLQQ--------------TRVDTVIPYYERFLDWFPTVESLANAPEERLLKAweGLGYYsR 98
Cdd:COG0122 74 PGLRLPRRPDPFEALVRAILGQQvsvaaartiwrrlvALFGEPIEGPGGGLYAFPTPEALAAASEEELRAC--GLSRR-K 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446808878 99 VRNMQAAAQQIMA---DFGGQFPNTYEGI----SSLKGIGPYTAG--AIssiaFNL--PE--PAVDGNVMRVLARLFevn 165
Cdd:COG0122 151 ARYLRALARAVADgelDLEALAGLDDEEAiarlTALPGIGPWTAEmvLL----FALgrPDafPAGDLGLRRALGRLY--- 223
|
170
....*....|....*..
gi 446808878 166 hDIGVPSNRKIFQAMME 182
Cdd:COG0122 224 -GLGERPTPKELRELAE 239
|
|
| PRK10702 |
PRK10702 |
endonuclease III; Provisional |
78-160 |
3.08e-05 |
|
endonuclease III; Provisional
Pssm-ID: 182661 [Multi-domain] Cd Length: 211 Bit Score: 44.62 E-value: 3.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446808878 78 LANAPEERLLKAWEGLGYY--------SRVRNMQAAAQQIMADFGGQFPNTYEGISSLKGIGPYTAGAISSIAFNLPEPA 149
Cdd:PRK10702 57 VANTPAAMLELGVEGVKTYiktiglynSKAENVIKTCRILLEQHNGEVPEDRAALEALPGVGRKTANVVLNTAFGWPTIA 136
|
90
....*....|.
gi 446808878 150 VDGNVMRVLAR 160
Cdd:PRK10702 137 VDTHIFRVCNR 147
|
|
| HHH |
pfam00633 |
Helix-hairpin-helix motif; The helix-hairpin-helix DNA-binding motif is found to be duplicated ... |
112-141 |
3.09e-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: 40.48 E-value: 3.09e-05
10 20 30
....*....|....*....|....*....|
gi 446808878 112 DFGGQFPNTYEGISSLKGIGPYTAGAISSI 141
Cdd:pfam00633 1 SLEGLIPASVEELLALPGVGPKTAEAILSY 30
|
|
|