|
Name |
Accession |
Description |
Interval |
E-value |
| MutY |
COG1194 |
Adenine-specific DNA glycosylase, acts on AG and A-oxoG pairs [Replication, recombination and ... |
1-365 |
8.09e-133 |
|
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: 385.26 E-value: 8.09e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774513 1 MLQQTQVATVIDYYTRWMQKWPTLQDLASASLEEVNQLWSGLGYYSRGRRLQEGARKVVEELGGHVPRTAETLQQLlPGV 80
Cdd:COG1194 38 MLQQTQVATVIPYYERFLERFPTVEALAAAPEDEVLKLWEGLGYYSRARNLHKAAQQVVEEHGGVFPDTYEELLAL-PGI 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774513 81 GRYTAGAIASIAFDQVTGVVDGNVIRVLCRVRAIGADPTSSFVSHHLWDLAQQLVDPARPGDFNQAAMELGATVCTPQRP 160
Cdd:COG1194 117 GPYTAAAIASIAFGEPAPIVDGNVKRVLSRLFAIEGPIGSPAAKKELWALAEELLPPERPGDFNQALMDLGATVCTPKKP 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774513 161 LCSHCPVQSLCRAHQRvgqgqlsalpGSPDieecalntrqcqlclpstnpwdpnmgvvNFPRKASRRPPREEYSATCVVE 240
Cdd:COG1194 197 KCLLCPLQDDCAAFAE----------GRQE----------------------------ELPVKKPKKKKPERYGAALVIR 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774513 241 QPGAtggplILLVQRPNSGLLAGLWEFPSVtlEPSGQHQHKALLQELQHWsAPLPTTPLQHLGEslpptpqVIHVFSHIK 320
Cdd:COG1194 239 DDGR-----VLLEKRPPKGLWGGLWEFPEF--EWEEAEDPEALERWLREE-LGLEVEWLEPLGT-------VRHVFTHFR 303
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 1958774513 321 LTYQVYSLALEGQTPASttPPGARWLTWEEFRNAAVSTAMKKVFR 365
Cdd:COG1194 304 LHLTVYLARVPAGPPAE--PDGGRWVPLEELAALPLPAPMRKLLK 346
|
|
| mutY |
TIGR01084 |
A/G-specific adenine glycosylase; This equivalog model identifies mutY members of the ... |
1-268 |
5.19e-86 |
|
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: 263.12 E-value: 5.19e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774513 1 MLQQTQVATVIDYYTRWMQKWPTLQDLASASLEEVNQLWSGLGYYSRGRRLQEGARKVVEELGGHVPRTAETLQQlLPGV 80
Cdd:TIGR01084 35 MLQQTQVATVIPYFERFLERFPTVQALANAPQDEVLKLWEGLGYYARARNLHKAAQEVVEEFGGEFPQDFEDLAA-LPGV 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774513 81 GRYTAGAIASIAFDQVTGVVDGNVIRVLCRVRAIGADPTSSFVSHHLWDLAQQLVDPARPGDFNQAAMELGATVCTPQRP 160
Cdd:TIGR01084 114 GRYTAGAILSFALNKPYPILDGNVKRVLSRLFAVEGWPGKKKVENRLWTLAESLLPKADPEAFNQALMDLGAMICTRKKP 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774513 161 LCSHCPVQSLCRAHQrvgQGQLSALPGspdieecalntrqcqlclpstnpwdpnmgvvnfpRKASRRPPREEYSATCVVE 240
Cdd:TIGR01084 194 KCDLCPLQDFCLAYQ---QGTWEEYPV----------------------------------KKPKAAPPERTTYFLVLQN 236
|
250 260
....*....|....*....|....*...
gi 1958774513 241 QPGAtggplILLVQRPNSGLLAGLWEFP 268
Cdd:TIGR01084 237 YDGE-----VLLEQRPEKGLWGGLYCFP 259
|
|
| PRK10880 |
PRK10880 |
adenine DNA glycosylase; |
1-321 |
1.63e-57 |
|
adenine DNA glycosylase;
Pssm-ID: 182805 [Multi-domain] Cd Length: 350 Bit Score: 192.23 E-value: 1.63e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774513 1 MLQQTQVATVIDYYTRWMQKWPTLQDLASASLEEVNQLWSGLGYYSRGRRLQEGARKVVEELGGHVPRTAETLQQlLPGV 80
Cdd:PRK10880 39 MLQQTQVATVIPYFERFMARFPTVTDLANAPLDEVLHLWTGLGYYARARNLHKAAQQVATLHGGEFPETFEEVAA-LPGV 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774513 81 GRYTAGAIASIAFDQVTGVVDGNVIRVLCRVRAIGADPTSSFVSHHLWDLAQQlVDPARP-GDFNQAAMELGATVCTPQR 159
Cdd:PRK10880 118 GRSTAGAILSLSLGKHFPILDGNVKRVLARCYAVSGWPGKKEVENRLWQLSEQ-VTPAVGvERFNQAMMDLGAMVCTRSK 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774513 160 PLCSHCPVQSLCRAHqrvGQGQLSALPGSPdieecalntrqcqlclpstnpwdpnmgvvnfPRKAsrRPPREEYsatCVV 239
Cdd:PRK10880 197 PKCELCPLQNGCIAY---ANHSWALYPGKK-------------------------------PKQT--LPERTGY---FLL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774513 240 EQPGATggplILLVQRPNSGLLAGLWEFPSVTLEpsgqhqhkallQELQHWsaplpttpLQHLGESLPPTPQVI---HVF 316
Cdd:PRK10880 238 LQHGDE----VWLEQRPPSGLWGGLFCFPQFADE-----------EELRQW--------LAQRGIAADNLTQLTafrHTF 294
|
....*
gi 1958774513 317 SHIKL 321
Cdd:PRK10880 295 SHFHL 299
|
|
| ENDO3c |
cd00056 |
endonuclease III; includes endonuclease III (DNA-(apurinic or apyrimidinic site) lyase), ... |
1-151 |
8.09e-45 |
|
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: 152.78 E-value: 8.09e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774513 1 MLQQTQVATVIDYYTRWMQKW-PTLQDLASASLEEVNQLWSGLGYYSRGRRLQEGARKVVEELGGHVPRTAETLQQL--L 77
Cdd:cd00056 9 LSQQTTDKAVNKAYERLFERYgPTPEALAAADEEELRELIRSLGYRRKAKYLKELARAIVEGFGGLVLDDPDAREELlaL 88
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958774513 78 PGVGRYTAGAIASIAFDQVTGVVDGNVIRVLCRVRAIGADPTssfvSHHLWDLAQQLVDPARPGDFNQAAMELG 151
Cdd:cd00056 89 PGVGRKTANVVLLFALGPDAFPVDTHVRRVLKRLGLIPKKKT----PEELEELLEELLPKPYWGEANQALMDLG 158
|
|
| ENDO3c |
smart00478 |
endonuclease III; includes endonuclease III (DNA-(apurinic or apyrimidinic site) lyase), ... |
1-153 |
1.98e-44 |
|
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: 151.26 E-value: 1.98e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774513 1 MLQQTQVATVIDYYTRWMQKWPTLQDLASASLEEVNQLWSGLG-YYSRGRRLQEGARKVVEELGGHVPRTAETLQQLlPG 79
Cdd:smart00478 1 LSQQTTDERVNKATERLFEKFPTPEDLAAADEEELEELIRGLGfYRRKARYLIELARILVEEYGGEVPDDREELLKL-PG 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958774513 80 VGRYTAGAIASIAFDQVTGVVDGNVIRVLCRVRAIGADPTSSfvshHLWDLAQQLVDPARPGDFNQAAMELGAT 153
Cdd:smart00478 80 VGRKTANAVLSFALGKPFIPVDTHVLRIAKRLGLVDKKSTPE----EVEKLLEKLLPEEDWRELNLLLIDFGRT 149
|
|
| HhH-GPD |
pfam00730 |
HhH-GPD superfamily base excision DNA repair protein; This family contains a diverse range of ... |
1-133 |
4.67e-41 |
|
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: 142.42 E-value: 4.67e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774513 1 MLQQTQVATVIDYYTRWMQKW-PTLQDLASASLEEVNQLWSGLGYY-SRGRRLQEGARKVVEELGGHVPRTAETLQQLLP 78
Cdd:pfam00730 5 LSQQTSDKAVNKITERLFEKFfPTPEDLADADEEELRELIRGLGFYrRKAKYLKELARILVEGYGGEVPLDEEELEALLK 84
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1958774513 79 GVGRYTAGAIASIAF--DQVTGVVDGNVIRVLCRVRAIGADPTSSFVSHHLWDLAQQ 133
Cdd:pfam00730 85 GVGRWTAEAVLIFALgrPDPLPVVDTHVRRVLKRLGLIKEKPTPKEVERELEELWPP 141
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| MutY |
COG1194 |
Adenine-specific DNA glycosylase, acts on AG and A-oxoG pairs [Replication, recombination and ... |
1-365 |
8.09e-133 |
|
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: 385.26 E-value: 8.09e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774513 1 MLQQTQVATVIDYYTRWMQKWPTLQDLASASLEEVNQLWSGLGYYSRGRRLQEGARKVVEELGGHVPRTAETLQQLlPGV 80
Cdd:COG1194 38 MLQQTQVATVIPYYERFLERFPTVEALAAAPEDEVLKLWEGLGYYSRARNLHKAAQQVVEEHGGVFPDTYEELLAL-PGI 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774513 81 GRYTAGAIASIAFDQVTGVVDGNVIRVLCRVRAIGADPTSSFVSHHLWDLAQQLVDPARPGDFNQAAMELGATVCTPQRP 160
Cdd:COG1194 117 GPYTAAAIASIAFGEPAPIVDGNVKRVLSRLFAIEGPIGSPAAKKELWALAEELLPPERPGDFNQALMDLGATVCTPKKP 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774513 161 LCSHCPVQSLCRAHQRvgqgqlsalpGSPDieecalntrqcqlclpstnpwdpnmgvvNFPRKASRRPPREEYSATCVVE 240
Cdd:COG1194 197 KCLLCPLQDDCAAFAE----------GRQE----------------------------ELPVKKPKKKKPERYGAALVIR 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774513 241 QPGAtggplILLVQRPNSGLLAGLWEFPSVtlEPSGQHQHKALLQELQHWsAPLPTTPLQHLGEslpptpqVIHVFSHIK 320
Cdd:COG1194 239 DDGR-----VLLEKRPPKGLWGGLWEFPEF--EWEEAEDPEALERWLREE-LGLEVEWLEPLGT-------VRHVFTHFR 303
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 1958774513 321 LTYQVYSLALEGQTPASttPPGARWLTWEEFRNAAVSTAMKKVFR 365
Cdd:COG1194 304 LHLTVYLARVPAGPPAE--PDGGRWVPLEELAALPLPAPMRKLLK 346
|
|
| mutY |
TIGR01084 |
A/G-specific adenine glycosylase; This equivalog model identifies mutY members of the ... |
1-268 |
5.19e-86 |
|
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: 263.12 E-value: 5.19e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774513 1 MLQQTQVATVIDYYTRWMQKWPTLQDLASASLEEVNQLWSGLGYYSRGRRLQEGARKVVEELGGHVPRTAETLQQlLPGV 80
Cdd:TIGR01084 35 MLQQTQVATVIPYFERFLERFPTVQALANAPQDEVLKLWEGLGYYARARNLHKAAQEVVEEFGGEFPQDFEDLAA-LPGV 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774513 81 GRYTAGAIASIAFDQVTGVVDGNVIRVLCRVRAIGADPTSSFVSHHLWDLAQQLVDPARPGDFNQAAMELGATVCTPQRP 160
Cdd:TIGR01084 114 GRYTAGAILSFALNKPYPILDGNVKRVLSRLFAVEGWPGKKKVENRLWTLAESLLPKADPEAFNQALMDLGAMICTRKKP 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774513 161 LCSHCPVQSLCRAHQrvgQGQLSALPGspdieecalntrqcqlclpstnpwdpnmgvvnfpRKASRRPPREEYSATCVVE 240
Cdd:TIGR01084 194 KCDLCPLQDFCLAYQ---QGTWEEYPV----------------------------------KKPKAAPPERTTYFLVLQN 236
|
250 260
....*....|....*....|....*...
gi 1958774513 241 QPGAtggplILLVQRPNSGLLAGLWEFP 268
Cdd:TIGR01084 237 YDGE-----VLLEQRPEKGLWGGLYCFP 259
|
|
| PRK10880 |
PRK10880 |
adenine DNA glycosylase; |
1-321 |
1.63e-57 |
|
adenine DNA glycosylase;
Pssm-ID: 182805 [Multi-domain] Cd Length: 350 Bit Score: 192.23 E-value: 1.63e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774513 1 MLQQTQVATVIDYYTRWMQKWPTLQDLASASLEEVNQLWSGLGYYSRGRRLQEGARKVVEELGGHVPRTAETLQQlLPGV 80
Cdd:PRK10880 39 MLQQTQVATVIPYFERFMARFPTVTDLANAPLDEVLHLWTGLGYYARARNLHKAAQQVATLHGGEFPETFEEVAA-LPGV 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774513 81 GRYTAGAIASIAFDQVTGVVDGNVIRVLCRVRAIGADPTSSFVSHHLWDLAQQlVDPARP-GDFNQAAMELGATVCTPQR 159
Cdd:PRK10880 118 GRSTAGAILSLSLGKHFPILDGNVKRVLARCYAVSGWPGKKEVENRLWQLSEQ-VTPAVGvERFNQAMMDLGAMVCTRSK 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774513 160 PLCSHCPVQSLCRAHqrvGQGQLSALPGSPdieecalntrqcqlclpstnpwdpnmgvvnfPRKAsrRPPREEYsatCVV 239
Cdd:PRK10880 197 PKCELCPLQNGCIAY---ANHSWALYPGKK-------------------------------PKQT--LPERTGY---FLL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774513 240 EQPGATggplILLVQRPNSGLLAGLWEFPSVTLEpsgqhqhkallQELQHWsaplpttpLQHLGESLPPTPQVI---HVF 316
Cdd:PRK10880 238 LQHGDE----VWLEQRPPSGLWGGLFCFPQFADE-----------EELRQW--------LAQRGIAADNLTQLTafrHTF 294
|
....*
gi 1958774513 317 SHIKL 321
Cdd:PRK10880 295 SHFHL 299
|
|
| ENDO3c |
cd00056 |
endonuclease III; includes endonuclease III (DNA-(apurinic or apyrimidinic site) lyase), ... |
1-151 |
8.09e-45 |
|
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: 152.78 E-value: 8.09e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774513 1 MLQQTQVATVIDYYTRWMQKW-PTLQDLASASLEEVNQLWSGLGYYSRGRRLQEGARKVVEELGGHVPRTAETLQQL--L 77
Cdd:cd00056 9 LSQQTTDKAVNKAYERLFERYgPTPEALAAADEEELRELIRSLGYRRKAKYLKELARAIVEGFGGLVLDDPDAREELlaL 88
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958774513 78 PGVGRYTAGAIASIAFDQVTGVVDGNVIRVLCRVRAIGADPTssfvSHHLWDLAQQLVDPARPGDFNQAAMELG 151
Cdd:cd00056 89 PGVGRKTANVVLLFALGPDAFPVDTHVRRVLKRLGLIPKKKT----PEELEELLEELLPKPYWGEANQALMDLG 158
|
|
| ENDO3c |
smart00478 |
endonuclease III; includes endonuclease III (DNA-(apurinic or apyrimidinic site) lyase), ... |
1-153 |
1.98e-44 |
|
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: 151.26 E-value: 1.98e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774513 1 MLQQTQVATVIDYYTRWMQKWPTLQDLASASLEEVNQLWSGLG-YYSRGRRLQEGARKVVEELGGHVPRTAETLQQLlPG 79
Cdd:smart00478 1 LSQQTTDERVNKATERLFEKFPTPEDLAAADEEELEELIRGLGfYRRKARYLIELARILVEEYGGEVPDDREELLKL-PG 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958774513 80 VGRYTAGAIASIAFDQVTGVVDGNVIRVLCRVRAIGADPTSSfvshHLWDLAQQLVDPARPGDFNQAAMELGAT 153
Cdd:smart00478 80 VGRKTANAVLSFALGKPFIPVDTHVLRIAKRLGLVDKKSTPE----EVEKLLEKLLPEEDWRELNLLLIDFGRT 149
|
|
| HhH-GPD |
pfam00730 |
HhH-GPD superfamily base excision DNA repair protein; This family contains a diverse range of ... |
1-133 |
4.67e-41 |
|
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: 142.42 E-value: 4.67e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774513 1 MLQQTQVATVIDYYTRWMQKW-PTLQDLASASLEEVNQLWSGLGYY-SRGRRLQEGARKVVEELGGHVPRTAETLQQLLP 78
Cdd:pfam00730 5 LSQQTSDKAVNKITERLFEKFfPTPEDLADADEEELRELIRGLGFYrRKAKYLKELARILVEGYGGEVPLDEEELEALLK 84
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1958774513 79 GVGRYTAGAIASIAF--DQVTGVVDGNVIRVLCRVRAIGADPTSSFVSHHLWDLAQQ 133
Cdd:pfam00730 85 GVGRWTAEAVLIFALgrPDPLPVVDTHVRRVLKRLGLIKEKPTPKEVERELEELWPP 141
|
|
| PRK13910 |
PRK13910 |
DNA glycosylase MutY; Provisional |
1-171 |
1.04e-32 |
|
DNA glycosylase MutY; Provisional
Pssm-ID: 172427 [Multi-domain] Cd Length: 289 Bit Score: 124.75 E-value: 1.04e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774513 1 MLQQTQVATVID-YYTRWMQKWPTLQDLASASLEEVNQLWSGLGYYSRGRRLQEGARKVVEELGGHVPRTAETLQQlLPG 79
Cdd:PRK13910 1 MSQQTQINTVVErFYSPFLEAFPTLKDLANAPLEEVLLLWRGLGYYSRAKNLKKSAEICVKEHHSQLPNDYQSLLK-LPG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774513 80 VGRYTAGAIASIAFDQVTGVVDGNVIRVLCRVraIGADPtsSFVSHHLWDLAQQLVDPARPGDFNQAAMELGATVCTPqR 159
Cdd:PRK13910 80 IGAYTANAILCFGFREKSACVDANIKRVLLRL--FGLDP--NIHAKDLQIKANDFLNLNESFNHNQALIDLGALICSP-K 154
|
170
....*....|..
gi 1958774513 160 PLCSHCPVQSLC 171
Cdd:PRK13910 155 PKCAICPLNPYC 166
|
|
| Nth |
COG0177 |
Endonuclease III [Replication, recombination and repair]; |
19-172 |
1.91e-29 |
|
Endonuclease III [Replication, recombination and repair];
Pssm-ID: 439947 [Multi-domain] Cd Length: 198 Bit Score: 113.27 E-value: 1.91e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774513 19 QKWPTLQDLASASLEEVNQLWSGLGYY-SRGRRLQEGARKVVEELGGHVPRTAETLQQLlPGVGRYTAGAIASIAFDQVT 97
Cdd:COG0177 47 ARYPTPEALAAADLEELEELIRPIGLYrNKAKNIIALARILVEKYGGEVPETREELESL-PGVGRKTANVVLNFAFGKPA 125
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958774513 98 GVVDGNVIRVLCRVR-AIGADPTSsfVSHHLwdlaQQLVDPARPGDFNQAAMELGATVCTPQRPLCSHCPVQSLCR 172
Cdd:COG0177 126 IAVDTHVHRVSNRLGlVPGKDPEE--VEKDL----MKLIPKEYWGDLHHLLILHGRYICKARKPKCEECPLADLCP 195
|
|
| NUDIX_DNA_Glycosylase_C-MutY |
cd03431 |
C-terminal domain of DNA glycosylase; DNA glycosylase (MutY in bacteria and hMYH in humans) is ... |
229-364 |
2.40e-26 |
|
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: 102.38 E-value: 2.40e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774513 229 PREEYSATCVVEQPGAtggplILLVQRPNSGLLAGLWEFPSVTLEPSGQhqhkaLLQELQHWSAPLPTTPLQHLGEslpp 308
Cdd:cd03431 1 VPERYFTVLVLRDGGR-----VLLEKRPEKGLLAGLWEFPLVETEEEEE-----EAEALLGLLAEELLLILEPLGE---- 66
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1958774513 309 tpqVIHVFSHIKLTYQVYSLALEGQTPASttPPGARWLTWEEFRNAAVSTAMKKVF 364
Cdd:cd03431 67 ---VKHVFSHFRLHITVYLVELPEAPPAA--PDEGRWVDLEELDEYALPAPMRKLL 117
|
|
| nth |
TIGR01083 |
endonuclease III; This equivalog model identifes nth members of the pfam00730 superfamily ... |
19-162 |
2.91e-21 |
|
endonuclease III; This equivalog model identifes nth members of the pfam00730 superfamily (HhH-GPD: Helix-hairpin-helix and Gly/Pro rich loop followed by a conserved aspartate). The major members of the superfamily are nth and mutY. [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273434 [Multi-domain] Cd Length: 192 Bit Score: 90.52 E-value: 2.91e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774513 19 QKWPTLQDLASASLEEVNQLWSGLGYY-SRGRRLQEGARKVVEELGGHVPRTAETLQQLlPGVGRYTAGAIASIAFDQVT 97
Cdd:TIGR01083 54 EVYPTPQALAQAGLEELEEYIKSIGLYrNKAKNIIELCRKLVERYGGEVPEDREELVKL-PGVGRKTANVVLNVAFGIPA 132
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958774513 98 GVVDGNVIRVLCRVR-AIGADPTSsfVSHHLwdlaQQLVDPARPGDFNQAAMELGATVCTPQRPLC 162
Cdd:TIGR01083 133 IAVDTHVFRVSNRLGlSKGKDPIK--VEEDL----MKLVPREFWVKLHHWLILHGRYTCKARKPLC 192
|
|
| NUDIX_4 |
pfam14815 |
NUDIX domain; |
250-365 |
4.06e-19 |
|
NUDIX domain;
Pssm-ID: 464330 [Multi-domain] Cd Length: 114 Bit Score: 82.36 E-value: 4.06e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774513 250 ILLVQRPNSGLLAGLWEFPSVTLEPSGQHQHKALLQELQHwsapLPTTPLQHLgeslpptpQVIHVFSHIKLTYQVYSLA 329
Cdd:pfam14815 12 VLLRKRPEKGLLGGLWEFPGGKVEPGETLEEALARLEELG----IEVEVLEPG--------TVKHVFTHFRLTLHVYLVR 79
|
90 100 110
....*....|....*....|....*....|....*.
gi 1958774513 330 LEGQTPASttPPGARWLTWEEFRNAAVSTAMKKVFR 365
Cdd:pfam14815 80 EVEGEEEP--QQELRWVTPEELDKYALPAAVRKILE 113
|
|
| HP0602 |
COG2231 |
3-Methyladenine DNA glycosylase, HhH-GPD/Endo3 superfamily [Replication, recombination and ... |
23-177 |
2.32e-08 |
|
3-Methyladenine DNA glycosylase, HhH-GPD/Endo3 superfamily [Replication, recombination and repair];
Pssm-ID: 441832 [Multi-domain] Cd Length: 220 Bit Score: 54.08 E-value: 2.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774513 23 TLQDLASASLEEVNQLWSGLGYYSR-GRRLQEGARKVVEELGGHVPR-----TAETLQQLL--PGVGRYTAGAIASIAFD 94
Cdd:COG2231 61 DPEALAALDPEELAELIRPSGFYNQkAKRLKNLARWLVERYGGGLEKlkalpTEELREELLslKGIGPETADSILLYAFN 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774513 95 QVTGVVDGNVIRVLcrVRAIGADPTSSFvshhlwDLAQQLVDPARPGDFNQA----AM--ELGATVCTPqRPLCSHCPVQ 168
Cdd:COG2231 141 RPVFVVDAYTRRIF--SRLGLIEEDASY------DELQRLFEENLPPDVALYnefhALivEHGKEYCKK-KPKCEECPLR 211
|
....*....
gi 1958774513 169 SLCRAHQRV 177
Cdd:COG2231 212 DLCPYGGQE 220
|
|
| PRK10702 |
PRK10702 |
endonuclease III; Provisional |
44-177 |
1.03e-06 |
|
endonuclease III; Provisional
Pssm-ID: 182661 [Multi-domain] Cd Length: 211 Bit Score: 49.25 E-value: 1.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774513 44 YYSRGRRLQEGARKVVEELGGHVPRTAETLQQLlPGVGRYTAGAIASIAFDQVTGVVDGNVIRVLCRvraigadptSSFV 123
Cdd:PRK10702 82 YNSKAENVIKTCRILLEQHNGEVPEDRAALEAL-PGVGRKTANVVLNTAFGWPTIAVDTHIFRVCNR---------TQFA 151
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1958774513 124 SHHLWDLAQQLVDPARPGDF----NQAAMELGATVCTPQRPLCSHCPVQSLCRAHQRV 177
Cdd:PRK10702 152 PGKNVEQVEEKLLKVVPAEFkvdcHHWLILHGRYTCIARKPRCGSCIIEDLCEYKEKV 209
|
|
| PRK10546 |
PRK10546 |
pyrimidine (deoxy)nucleoside triphosphate diphosphatase; |
238-288 |
3.18e-05 |
|
pyrimidine (deoxy)nucleoside triphosphate diphosphatase;
Pssm-ID: 182536 [Multi-domain] Cd Length: 135 Bit Score: 43.58 E-value: 3.18e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1958774513 238 VVEQPGAtggplILLVQRPNSGLLAGLWEFPSVTLEPsGQHQHKALLQELQ 288
Cdd:PRK10546 10 IIERDGK-----ILLAQRPAHSDQAGLWEFAGGKVEP-GESQPQALIRELR 54
|
|
| HHH |
pfam00633 |
Helix-hairpin-helix motif; The helix-hairpin-helix DNA-binding motif is found to be duplicated ... |
61-91 |
6.24e-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: 39.71 E-value: 6.24e-05
10 20 30
....*....|....*....|....*....|.
gi 1958774513 61 ELGGHVPRTAETLQQLlPGVGRYTAGAIASI 91
Cdd:pfam00633 1 SLEGLIPASVEELLAL-PGVGPKTAEAILSY 30
|
|
| FES |
smart00525 |
iron-sulpphur binding domain in DNA-(apurinic or apyrimidinic site) lyase (subfamily of ENDO3); ... |
154-173 |
9.96e-04 |
|
iron-sulpphur binding domain in DNA-(apurinic or apyrimidinic site) lyase (subfamily of ENDO3);
Pssm-ID: 197771 [Multi-domain] Cd Length: 21 Bit Score: 36.37 E-value: 9.96e-04
|
| EndIII_4Fe-2S |
pfam10576 |
Iron-sulfur binding domain of endonuclease III; Escherichia coli endonuclease III (EC 4.2.99. ... |
155-171 |
2.35e-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: 35.05 E-value: 2.35e-03
|
| NUDIX_MutT_NudA_like |
cd03425 |
MutT pyrophosphohydrolase; The MutT pyrophosphohydrolase is a prototypical NUDIX hydrolase ... |
250-268 |
5.55e-03 |
|
MutT pyrophosphohydrolase; The MutT pyrophosphohydrolase is a prototypical NUDIX hydrolase that catalyzes the hydrolysis of nucleoside and deoxynucleoside triphosphates (NTPs and dNTPs) by substitution at a beta-phosphorus to yield a nucleotide monophosphate (NMP) and inorganic pyrophosphate (PPi). This enzyme requires two divalent cations for activity; one coordinates the phosphoryl groups of the NTP/dNTP substrate, and the other coordinates to the enzyme. It also contains the NUDIX motif, a highly conserved 23-residue block (GX5EX7REUXEEXGU, where U = I, L or V), that functions as metal binding and catalytic site. MutT pyrophosphohydrolase is important in preventing errors in DNA replication by hydrolyzing mutagenic nucleotides such as 8-oxo-dGTP (a product of oxidative damage), which can mispair with template adenine during DNA replication, to guanine nucleotides.
Pssm-ID: 467531 [Multi-domain] Cd Length: 123 Bit Score: 36.66 E-value: 5.55e-03
|
| |
