|
Name |
Accession |
Description |
Interval |
E-value |
| MutY |
COG1194 |
Adenine-specific DNA glycosylase, acts on AG and A-oxoG pairs [Replication, recombination and ... |
63-471 |
3.41e-156 |
|
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: 448.82 E-value: 3.41e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115298652 63 AEVTAFRGSLLSWYDQEKRDLPWRRraedemdlDRRAYAVWVSEVMLQQTQVATVINYYTGWMQKWPTLQDLASASLEEV 142
Cdd:COG1194 1 MDMASFAKRLLAWYDRHGRDLPWRQ--------TRDPYRVWLSEIMLQQTQVATVIPYYERFLERFPTVEALAAAPEDEV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115298652 143 NQLWAGLGYYSRGRRLQEGARKVVEELGGHMPRTAETLQQLlPGVGRYTAGAIASIAFGQATGVVDGNVARVLCRVRAIG 222
Cdd:COG1194 73 LKLWEGLGYYSRARNLHKAAQQVVEEHGGVFPDTYEELLAL-PGIGPYTAAAIASIAFGEPAPIVDGNVKRVLSRLFAIE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115298652 223 ADPSSTLVSQQLWGLAQQLVDPARPGDFNQAAMELGATVCTPQRPLCSQCPVESLCRARQRVEQEQLlasgslsgspdve 302
Cdd:COG1194 152 GPIGSPAAKKELWALAEELLPPERPGDFNQALMDLGATVCTPKKPKCLLCPLQDDCAAFAEGRQEEL------------- 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115298652 303 ecapntgqchlclppsepwdqtlgvvnfPRKASRKPPREESSATCVLEQPGalgaQILLVQRPNSGLLAGLWEFPSVTWE 382
Cdd:COG1194 219 ----------------------------PVKKPKKKKPERYGAALVIRDDG----RVLLEKRPPKGLWGGLWEFPEFEWE 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115298652 383 PSEQLQrkALLQELQRWAGpLPATHLRHLGEVVHTFSHIKLTYQVYGLALEGQTPVTtvPPGARWLTQEEFHTAAVSTAM 462
Cdd:COG1194 267 EAEDPE--ALERWLREELG-LEVEWLEPLGTVRHVFTHFRLHLTVYLARVPAGPPAE--PDGGRWVPLEELAALPLPAPM 341
|
....*....
gi 115298652 463 KKVFRVYQG 471
Cdd:COG1194 342 RKLLKALLK 350
|
|
| mutY |
TIGR01084 |
A/G-specific adenine glycosylase; This equivalog model identifies mutY members of the ... |
67-397 |
3.87e-99 |
|
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: 300.48 E-value: 3.87e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115298652 67 AFRGSLLSWYDQEKR-DLPWRrraedemdLDRRAYAVWVSEVMLQQTQVATVINYYTGWMQKWPTLQDLASASLEEVNQL 145
Cdd:TIGR01084 1 QFSEDLLSWYDKYGRkTLPWR--------QNKTPYRVWLSEVMLQQTQVATVIPYFERFLERFPTVQALANAPQDEVLKL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115298652 146 WAGLGYYSRGRRLQEGARKVVEELGGHMPRTAETLQQlLPGVGRYTAGAIASIAFGQATGVVDGNVARVLCRVRAIGADP 225
Cdd:TIGR01084 73 WEGLGYYARARNLHKAAQEVVEEFGGEFPQDFEDLAA-LPGVGRYTAGAILSFALNKPYPILDGNVKRVLSRLFAVEGWP 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115298652 226 SSTLVSQQLWGLAQQLVDPARPGDFNQAAMELGATVCTPQRPLCSQCPVESLCRARQRVEQEQllasgslsgspdveeca 305
Cdd:TIGR01084 152 GKKKVENRLWTLAESLLPKADPEAFNQALMDLGAMICTRKKPKCDLCPLQDFCLAYQQGTWEE----------------- 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115298652 306 pntgqchlclppsepwdqtlgvvnFPRKASRKPPREESSATCVLEQPgalGAQILLVQRPNSGLLAGLWEFPsvtwepse 385
Cdd:TIGR01084 215 ------------------------YPVKKPKAAPPERTTYFLVLQNY---DGEVLLEQRPEKGLWGGLYCFP-------- 259
|
330
....*....|..
gi 115298652 386 QLQRKALLQELQ 397
Cdd:TIGR01084 260 QFEDEDSLAFLL 271
|
|
| PRK10880 |
PRK10880 |
adenine DNA glycosylase; |
68-423 |
2.04e-71 |
|
adenine DNA glycosylase;
Pssm-ID: 182805 [Multi-domain] Cd Length: 350 Bit Score: 231.52 E-value: 2.04e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115298652 68 FRGSLLSWYDQEKRD-LPWRrraedemdLDRRAYAVWVSEVMLQQTQVATVINYYTGWMQKWPTLQDLASASLEEVNQLW 146
Cdd:PRK10880 6 FSAQVLDWYDKYGRKtLPWQ--------IDKTPYKVWLSEVMLQQTQVATVIPYFERFMARFPTVTDLANAPLDEVLHLW 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115298652 147 AGLGYYSRGRRLQEGARKVVEELGGHMPRTAETLQQlLPGVGRYTAGAIASIAFGQATGVVDGNVARVLCRVRAIGADPS 226
Cdd:PRK10880 78 TGLGYYARARNLHKAAQQVATLHGGEFPETFEEVAA-LPGVGRSTAGAILSLSLGKHFPILDGNVKRVLARCYAVSGWPG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115298652 227 STLVSQQLWGLAQQlVDPARP-GDFNQAAMELGATVCTPQRPLCSQCPVESLCRARqrveqeqllASGSlsgspdveeca 305
Cdd:PRK10880 157 KKEVENRLWQLSEQ-VTPAVGvERFNQAMMDLGAMVCTRSKPKCELCPLQNGCIAY---------ANHS----------- 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115298652 306 pntgqchlclppsepWDQtlgvvnFPRKASRKPPREESSATCVLEQpgalGAQILLVQRPNSGLLAGLWEFPSVTWEpse 385
Cdd:PRK10880 216 ---------------WAL------YPGKKPKQTLPERTGYFLLLQH----GDEVWLEQRPPSGLWGGLFCFPQFADE--- 267
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 115298652 386 qlqrkallQELQRW--AGPLPATHLRHLGEVVHTFSHIKL 423
Cdd:PRK10880 268 --------EELRQWlaQRGIAADNLTQLTAFRHTFSHFHL 299
|
|
| ENDO3c |
cd00056 |
endonuclease III; includes endonuclease III (DNA-(apurinic or apyrimidinic site) lyase), ... |
100-258 |
1.36e-46 |
|
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: 159.71 E-value: 1.36e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115298652 100 YAVWVSEVMLQQTQVATVINYYTGWMQKW-PTLQDLASASLEEVNQLWAGLGYYSRGRRLQEGARKVVEELGG---HMPR 175
Cdd:cd00056 1 FEVLVSEILSQQTTDKAVNKAYERLFERYgPTPEALAAADEEELRELIRSLGYRRKAKYLKELARAIVEGFGGlvlDDPD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115298652 176 TAETLQQlLPGVGRYTAGAIASIAFGQATGVVDGNVARVLCRVRAIGADPSstlvSQQLWGLAQQLVDPARPGDFNQAAM 255
Cdd:cd00056 81 AREELLA-LPGVGRKTANVVLLFALGPDAFPVDTHVRRVLKRLGLIPKKKT----PEELEELLEELLPKPYWGEANQALM 155
|
...
gi 115298652 256 ELG 258
Cdd:cd00056 156 DLG 158
|
|
| ENDO3c |
smart00478 |
endonuclease III; includes endonuclease III (DNA-(apurinic or apyrimidinic site) lyase), ... |
108-260 |
8.80e-43 |
|
endonuclease III; includes endonuclease III (DNA-(apurinic or apyrimidinic site) lyase), alkylbase DNA glycosidases (Alka-family) and other DNA glycosidases
Pssm-ID: 214684 [Multi-domain] Cd Length: 149 Bit Score: 149.34 E-value: 8.80e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115298652 108 MLQQTQVATVINYYTGWMQKWPTLQDLASASLEEVNQLWAGLG-YYSRGRRLQEGARKVVEELGGHMPRTAETLQQLlPG 186
Cdd:smart00478 1 LSQQTTDERVNKATERLFEKFPTPEDLAAADEEELEELIRGLGfYRRKARYLIELARILVEEYGGEVPDDREELLKL-PG 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 115298652 187 VGRYTAGAIASIAFGQATGVVDGNVARVLCRVRAIGAdpssTLVSQQLWGLAQQLVDPARPGDFNQAAMELGAT 260
Cdd:smart00478 80 VGRKTANAVLSFALGKPFIPVDTHVLRIAKRLGLVDK----KSTPEEVEKLLEKLLPEEDWRELNLLLIDFGRT 149
|
|
| HhH-GPD |
pfam00730 |
HhH-GPD superfamily base excision DNA repair protein; This family contains a diverse range of ... |
104-240 |
1.00e-40 |
|
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: 143.58 E-value: 1.00e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115298652 104 VSEVMLQQTQVATVINYYTGWMQKW-PTLQDLASASLEEVNQLWAGLGYY-SRGRRLQEGARKVVEELGGHMPRTAETLQ 181
Cdd:pfam00730 1 VSAILSQQTSDKAVNKITERLFEKFfPTPEDLADADEEELRELIRGLGFYrRKAKYLKELARILVEGYGGEVPLDEEELE 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 115298652 182 QLLPGVGRYTAGAIASIAFG--QATGVVDGNVARVLCRVRAIGADPSSTLVSQQLWGLAQQ 240
Cdd:pfam00730 81 ALLKGVGRWTAEAVLIFALGrpDPLPVVDTHVRRVLKRLGLIKEKPTPKEVERELEELWPP 141
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| MutY |
COG1194 |
Adenine-specific DNA glycosylase, acts on AG and A-oxoG pairs [Replication, recombination and ... |
63-471 |
3.41e-156 |
|
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: 448.82 E-value: 3.41e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115298652 63 AEVTAFRGSLLSWYDQEKRDLPWRRraedemdlDRRAYAVWVSEVMLQQTQVATVINYYTGWMQKWPTLQDLASASLEEV 142
Cdd:COG1194 1 MDMASFAKRLLAWYDRHGRDLPWRQ--------TRDPYRVWLSEIMLQQTQVATVIPYYERFLERFPTVEALAAAPEDEV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115298652 143 NQLWAGLGYYSRGRRLQEGARKVVEELGGHMPRTAETLQQLlPGVGRYTAGAIASIAFGQATGVVDGNVARVLCRVRAIG 222
Cdd:COG1194 73 LKLWEGLGYYSRARNLHKAAQQVVEEHGGVFPDTYEELLAL-PGIGPYTAAAIASIAFGEPAPIVDGNVKRVLSRLFAIE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115298652 223 ADPSSTLVSQQLWGLAQQLVDPARPGDFNQAAMELGATVCTPQRPLCSQCPVESLCRARQRVEQEQLlasgslsgspdve 302
Cdd:COG1194 152 GPIGSPAAKKELWALAEELLPPERPGDFNQALMDLGATVCTPKKPKCLLCPLQDDCAAFAEGRQEEL------------- 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115298652 303 ecapntgqchlclppsepwdqtlgvvnfPRKASRKPPREESSATCVLEQPGalgaQILLVQRPNSGLLAGLWEFPSVTWE 382
Cdd:COG1194 219 ----------------------------PVKKPKKKKPERYGAALVIRDDG----RVLLEKRPPKGLWGGLWEFPEFEWE 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115298652 383 PSEQLQrkALLQELQRWAGpLPATHLRHLGEVVHTFSHIKLTYQVYGLALEGQTPVTtvPPGARWLTQEEFHTAAVSTAM 462
Cdd:COG1194 267 EAEDPE--ALERWLREELG-LEVEWLEPLGTVRHVFTHFRLHLTVYLARVPAGPPAE--PDGGRWVPLEELAALPLPAPM 341
|
....*....
gi 115298652 463 KKVFRVYQG 471
Cdd:COG1194 342 RKLLKALLK 350
|
|
| mutY |
TIGR01084 |
A/G-specific adenine glycosylase; This equivalog model identifies mutY members of the ... |
67-397 |
3.87e-99 |
|
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: 300.48 E-value: 3.87e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115298652 67 AFRGSLLSWYDQEKR-DLPWRrraedemdLDRRAYAVWVSEVMLQQTQVATVINYYTGWMQKWPTLQDLASASLEEVNQL 145
Cdd:TIGR01084 1 QFSEDLLSWYDKYGRkTLPWR--------QNKTPYRVWLSEVMLQQTQVATVIPYFERFLERFPTVQALANAPQDEVLKL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115298652 146 WAGLGYYSRGRRLQEGARKVVEELGGHMPRTAETLQQlLPGVGRYTAGAIASIAFGQATGVVDGNVARVLCRVRAIGADP 225
Cdd:TIGR01084 73 WEGLGYYARARNLHKAAQEVVEEFGGEFPQDFEDLAA-LPGVGRYTAGAILSFALNKPYPILDGNVKRVLSRLFAVEGWP 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115298652 226 SSTLVSQQLWGLAQQLVDPARPGDFNQAAMELGATVCTPQRPLCSQCPVESLCRARQRVEQEQllasgslsgspdveeca 305
Cdd:TIGR01084 152 GKKKVENRLWTLAESLLPKADPEAFNQALMDLGAMICTRKKPKCDLCPLQDFCLAYQQGTWEE----------------- 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115298652 306 pntgqchlclppsepwdqtlgvvnFPRKASRKPPREESSATCVLEQPgalGAQILLVQRPNSGLLAGLWEFPsvtwepse 385
Cdd:TIGR01084 215 ------------------------YPVKKPKAAPPERTTYFLVLQNY---DGEVLLEQRPEKGLWGGLYCFP-------- 259
|
330
....*....|..
gi 115298652 386 QLQRKALLQELQ 397
Cdd:TIGR01084 260 QFEDEDSLAFLL 271
|
|
| PRK10880 |
PRK10880 |
adenine DNA glycosylase; |
68-423 |
2.04e-71 |
|
adenine DNA glycosylase;
Pssm-ID: 182805 [Multi-domain] Cd Length: 350 Bit Score: 231.52 E-value: 2.04e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115298652 68 FRGSLLSWYDQEKRD-LPWRrraedemdLDRRAYAVWVSEVMLQQTQVATVINYYTGWMQKWPTLQDLASASLEEVNQLW 146
Cdd:PRK10880 6 FSAQVLDWYDKYGRKtLPWQ--------IDKTPYKVWLSEVMLQQTQVATVIPYFERFMARFPTVTDLANAPLDEVLHLW 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115298652 147 AGLGYYSRGRRLQEGARKVVEELGGHMPRTAETLQQlLPGVGRYTAGAIASIAFGQATGVVDGNVARVLCRVRAIGADPS 226
Cdd:PRK10880 78 TGLGYYARARNLHKAAQQVATLHGGEFPETFEEVAA-LPGVGRSTAGAILSLSLGKHFPILDGNVKRVLARCYAVSGWPG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115298652 227 STLVSQQLWGLAQQlVDPARP-GDFNQAAMELGATVCTPQRPLCSQCPVESLCRARqrveqeqllASGSlsgspdveeca 305
Cdd:PRK10880 157 KKEVENRLWQLSEQ-VTPAVGvERFNQAMMDLGAMVCTRSKPKCELCPLQNGCIAY---------ANHS----------- 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115298652 306 pntgqchlclppsepWDQtlgvvnFPRKASRKPPREESSATCVLEQpgalGAQILLVQRPNSGLLAGLWEFPSVTWEpse 385
Cdd:PRK10880 216 ---------------WAL------YPGKKPKQTLPERTGYFLLLQH----GDEVWLEQRPPSGLWGGLFCFPQFADE--- 267
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 115298652 386 qlqrkallQELQRW--AGPLPATHLRHLGEVVHTFSHIKL 423
Cdd:PRK10880 268 --------EELRQWlaQRGIAADNLTQLTAFRHTFSHFHL 299
|
|
| ENDO3c |
cd00056 |
endonuclease III; includes endonuclease III (DNA-(apurinic or apyrimidinic site) lyase), ... |
100-258 |
1.36e-46 |
|
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: 159.71 E-value: 1.36e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115298652 100 YAVWVSEVMLQQTQVATVINYYTGWMQKW-PTLQDLASASLEEVNQLWAGLGYYSRGRRLQEGARKVVEELGG---HMPR 175
Cdd:cd00056 1 FEVLVSEILSQQTTDKAVNKAYERLFERYgPTPEALAAADEEELRELIRSLGYRRKAKYLKELARAIVEGFGGlvlDDPD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115298652 176 TAETLQQlLPGVGRYTAGAIASIAFGQATGVVDGNVARVLCRVRAIGADPSstlvSQQLWGLAQQLVDPARPGDFNQAAM 255
Cdd:cd00056 81 AREELLA-LPGVGRKTANVVLLFALGPDAFPVDTHVRRVLKRLGLIPKKKT----PEELEELLEELLPKPYWGEANQALM 155
|
...
gi 115298652 256 ELG 258
Cdd:cd00056 156 DLG 158
|
|
| ENDO3c |
smart00478 |
endonuclease III; includes endonuclease III (DNA-(apurinic or apyrimidinic site) lyase), ... |
108-260 |
8.80e-43 |
|
endonuclease III; includes endonuclease III (DNA-(apurinic or apyrimidinic site) lyase), alkylbase DNA glycosidases (Alka-family) and other DNA glycosidases
Pssm-ID: 214684 [Multi-domain] Cd Length: 149 Bit Score: 149.34 E-value: 8.80e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115298652 108 MLQQTQVATVINYYTGWMQKWPTLQDLASASLEEVNQLWAGLG-YYSRGRRLQEGARKVVEELGGHMPRTAETLQQLlPG 186
Cdd:smart00478 1 LSQQTTDERVNKATERLFEKFPTPEDLAAADEEELEELIRGLGfYRRKARYLIELARILVEEYGGEVPDDREELLKL-PG 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 115298652 187 VGRYTAGAIASIAFGQATGVVDGNVARVLCRVRAIGAdpssTLVSQQLWGLAQQLVDPARPGDFNQAAMELGAT 260
Cdd:smart00478 80 VGRKTANAVLSFALGKPFIPVDTHVLRIAKRLGLVDK----KSTPEEVEKLLEKLLPEEDWRELNLLLIDFGRT 149
|
|
| HhH-GPD |
pfam00730 |
HhH-GPD superfamily base excision DNA repair protein; This family contains a diverse range of ... |
104-240 |
1.00e-40 |
|
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: 143.58 E-value: 1.00e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115298652 104 VSEVMLQQTQVATVINYYTGWMQKW-PTLQDLASASLEEVNQLWAGLGYY-SRGRRLQEGARKVVEELGGHMPRTAETLQ 181
Cdd:pfam00730 1 VSAILSQQTSDKAVNKITERLFEKFfPTPEDLADADEEELRELIRGLGFYrRKAKYLKELARILVEGYGGEVPLDEEELE 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 115298652 182 QLLPGVGRYTAGAIASIAFG--QATGVVDGNVARVLCRVRAIGADPSSTLVSQQLWGLAQQ 240
Cdd:pfam00730 81 ALLKGVGRWTAEAVLIFALGrpDPLPVVDTHVRRVLKRLGLIKEKPTPKEVERELEELWPP 141
|
|
| PRK13910 |
PRK13910 |
DNA glycosylase MutY; Provisional |
108-289 |
9.26e-35 |
|
DNA glycosylase MutY; Provisional
Pssm-ID: 172427 [Multi-domain] Cd Length: 289 Bit Score: 132.07 E-value: 9.26e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115298652 108 MLQQTQVATVIN-YYTGWMQKWPTLQDLASASLEEVNQLWAGLGYYSRGRRLQEGARKVVEELGGHMPRTAETLQQlLPG 186
Cdd:PRK13910 1 MSQQTQINTVVErFYSPFLEAFPTLKDLANAPLEEVLLLWRGLGYYSRAKNLKKSAEICVKEHHSQLPNDYQSLLK-LPG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115298652 187 VGRYTAGAIASIAFGQATGVVDGNVARVLCRVraIGADPSSTlvSQQLWGLAQQLVDPARPGDFNQAAMELGATVCTPqR 266
Cdd:PRK13910 80 IGAYTANAILCFGFREKSACVDANIKRVLLRL--FGLDPNIH--AKDLQIKANDFLNLNESFNHNQALIDLGALICSP-K 154
|
170 180
....*....|....*....|...
gi 115298652 267 PLCSQCPVESLCRARQRVEQEQL 289
Cdd:PRK13910 155 PKCAICPLNPYCLGKNNPEKHTL 177
|
|
| NUDIX_DNA_Glycosylase_C-MutY |
cd03431 |
C-terminal domain of DNA glycosylase; DNA glycosylase (MutY in bacteria and hMYH in humans) is ... |
339-466 |
1.52e-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: 115.09 E-value: 1.52e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115298652 339 PREESSATCVLEQPGalgaQILLVQRPNSGLLAGLWEFPSVTWEPSEQlqrkaLLQELQRWAGPLPATHLRHLGEVVHTF 418
Cdd:cd03431 1 VPERYFTVLVLRDGG----RVLLEKRPEKGLLAGLWEFPLVETEEEEE-----EAEALLGLLAEELLLILEPLGEVKHVF 71
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 115298652 419 SHIKLTYQVYGLALEGQTPVTtvPPGARWLTQEEFHTAAVSTAMKKVF 466
Cdd:cd03431 72 SHFRLHITVYLVELPEAPPAA--PDEGRWVDLEELDEYALPAPMRKLL 117
|
|
| Nth |
COG0177 |
Endonuclease III [Replication, recombination and repair]; |
126-282 |
3.18e-30 |
|
Endonuclease III [Replication, recombination and repair];
Pssm-ID: 439947 [Multi-domain] Cd Length: 198 Bit Score: 116.73 E-value: 3.18e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115298652 126 QKWPTLQDLASASLEEVNQLWAGLGYY-SRGRRLQEGARKVVEELGGHMPRTAETLQQLlPGVGRYTAGAIASIAFGQAT 204
Cdd:COG0177 47 ARYPTPEALAAADLEELEELIRPIGLYrNKAKNIIALARILVEKYGGEVPETREELESL-PGVGRKTANVVLNFAFGKPA 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115298652 205 GVVDGNVARVLCRvraIG-ADPSSTL-VSQQLwglaQQLVDPARPGDFNQAAMELGATVCTPQRPLCSQCPVESLCRARQ 282
Cdd:COG0177 126 IAVDTHVHRVSNR---LGlVPGKDPEeVEKDL----MKLIPKEYWGDLHHLLILHGRYICKARKPKCEECPLADLCPYYG 198
|
|
| NUDIX_4 |
pfam14815 |
NUDIX domain; |
358-467 |
4.22e-23 |
|
NUDIX domain;
Pssm-ID: 464330 [Multi-domain] Cd Length: 114 Bit Score: 94.30 E-value: 4.22e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115298652 358 QILLVQRPNSGLLAGLWEFPSVTWEPSEQLQRKalLQELQRWAgpLPATHLRHlGEVVHTFSHIKLTYQVYGLALEGQTP 437
Cdd:pfam14815 11 RVLLRKRPEKGLLGGLWEFPGGKVEPGETLEEA--LARLEELG--IEVEVLEP-GTVKHVFTHFRLTLHVYLVREVEGEE 85
|
90 100 110
....*....|....*....|....*....|
gi 115298652 438 vtTVPPGARWLTQEEFHTAAVSTAMKKVFR 467
Cdd:pfam14815 86 --EPQQELRWVTPEELDKYALPAAVRKILE 113
|
|
| nth |
TIGR01083 |
endonuclease III; This equivalog model identifes nth members of the pfam00730 superfamily ... |
126-269 |
4.14e-22 |
|
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: 93.98 E-value: 4.14e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115298652 126 QKWPTLQDLASASLEEVNQLWAGLGYY-SRGRRLQEGARKVVEELGGHMPRTAETLQQLlPGVGRYTAGAIASIAFGQAT 204
Cdd:TIGR01083 54 EVYPTPQALAQAGLEELEEYIKSIGLYrNKAKNIIELCRKLVERYGGEVPEDREELVKL-PGVGRKTANVVLNVAFGIPA 132
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 115298652 205 GVVDGNVARVLCRVR-AIGADPSST------LVSQQLWglaqqlvdparpGDFNQAAMELGATVCTPQRPLC 269
Cdd:TIGR01083 133 IAVDTHVFRVSNRLGlSKGKDPIKVeedlmkLVPREFW------------VKLHHWLILHGRYTCKARKPLC 192
|
|
| PRK10702 |
PRK10702 |
endonuclease III; Provisional |
151-284 |
1.74e-08 |
|
endonuclease III; Provisional
Pssm-ID: 182661 [Multi-domain] Cd Length: 211 Bit Score: 55.02 E-value: 1.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115298652 151 YYSRGRRLQEGARKVVEELGGHMPRTAETLQQLlPGVGRYTAGAIASIAFGQATGVVDGNVARVLCRVraiGADPSSTLv 230
Cdd:PRK10702 82 YNSKAENVIKTCRILLEQHNGEVPEDRAALEAL-PGVGRKTANVVLNTAFGWPTIAVDTHIFRVCNRT---QFAPGKNV- 156
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 115298652 231 sQQLWGLAQQLVDPARPGDFNQAAMELGATVCTPQRPLCSQCPVESLCRARQRV 284
Cdd:PRK10702 157 -EQVEEKLLKVVPAEFKVDCHHWLILHGRYTCIARKPRCGSCIIEDLCEYKEKV 209
|
|
| HP0602 |
COG2231 |
3-Methyladenine DNA glycosylase, HhH-GPD/Endo3 superfamily [Replication, recombination and ... |
130-284 |
1.56e-06 |
|
3-Methyladenine DNA glycosylase, HhH-GPD/Endo3 superfamily [Replication, recombination and repair];
Pssm-ID: 441832 [Multi-domain] Cd Length: 220 Bit Score: 49.07 E-value: 1.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115298652 130 TLQDLASASLEEVNQLWAGLGYYSR-GRRLQEGARKVVEELGGHMPR-----TAETLQQLL--PGVGRYTAGAIASIAFG 201
Cdd:COG2231 61 DPEALAALDPEELAELIRPSGFYNQkAKRLKNLARWLVERYGGGLEKlkalpTEELREELLslKGIGPETADSILLYAFN 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115298652 202 QATGVVDGNVARVLCRVrAIGADPSStlvsqqlWGLAQQLVDPARPGDFNQA----AM--ELGATVCTPqRPLCSQCPVE 275
Cdd:COG2231 141 RPVFVVDAYTRRIFSRL-GLIEEDAS-------YDELQRLFEENLPPDVALYnefhALivEHGKEYCKK-KPKCEECPLR 211
|
....*....
gi 115298652 276 SLCRARQRV 284
Cdd:COG2231 212 DLCPYGGQE 220
|
|
| NUDIX_MutT_NudA_like |
cd03425 |
MutT pyrophosphohydrolase; The MutT pyrophosphohydrolase is a prototypical NUDIX hydrolase ... |
348-455 |
2.70e-05 |
|
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: 43.59 E-value: 2.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115298652 348 VLEQPGalgaQILLVQRPNSGLLAGLWEFP--SVtwEPSEQLQrKALLQELQ---RWAgplpATHLRHLGEVVHTFSHIK 422
Cdd:cd03425 7 IIVDDG----RVLIAQRPEGKHLAGLWEFPggKV--EPGETPE-QALVRELReelGIE----VEVGEPLGTVEHDYPDFH 75
|
90 100 110
....*....|....*....|....*....|...
gi 115298652 423 LTYQVYGLALEGQTPVTTVPPGARWLTQEEFHT 455
Cdd:cd03425 76 VRLHVYLCTLWSGEPQLLEHQELRWVTPEELDD 108
|
|
| FES |
smart00525 |
iron-sulpphur binding domain in DNA-(apurinic or apyrimidinic site) lyase (subfamily of ENDO3); ... |
261-281 |
3.23e-05 |
|
iron-sulpphur binding domain in DNA-(apurinic or apyrimidinic site) lyase (subfamily of ENDO3);
Pssm-ID: 197771 [Multi-domain] Cd Length: 21 Bit Score: 40.61 E-value: 3.23e-05
|
| PRK10546 |
PRK10546 |
pyrimidine (deoxy)nucleoside triphosphate diphosphatase; |
348-397 |
3.29e-05 |
|
pyrimidine (deoxy)nucleoside triphosphate diphosphatase;
Pssm-ID: 182536 [Multi-domain] Cd Length: 135 Bit Score: 43.58 E-value: 3.29e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 115298652 348 VLEQPGalgaQILLVQRPNSGLLAGLWEFPSVTWEPSEQlQRKALLQELQ 397
Cdd:PRK10546 10 IIERDG----KILLAQRPAHSDQAGLWEFAGGKVEPGES-QPQALIRELR 54
|
|
| HHH |
pfam00633 |
Helix-hairpin-helix motif; The helix-hairpin-helix DNA-binding motif is found to be duplicated ... |
168-198 |
9.92e-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: 39.32 E-value: 9.92e-05
10 20 30
....*....|....*....|....*....|.
gi 115298652 168 ELGGHMPRTAETLQQLlPGVGRYTAGAIASI 198
Cdd:pfam00633 1 SLEGLIPASVEELLAL-PGVGPKTAEAILSY 30
|
|
| PRK10776 |
PRK10776 |
8-oxo-dGTP diphosphatase MutT; |
358-452 |
1.71e-04 |
|
8-oxo-dGTP diphosphatase MutT;
Pssm-ID: 182721 [Multi-domain] Cd Length: 129 Bit Score: 41.51 E-value: 1.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115298652 358 QILLVQRPNSGLLAGLWEFPSVTWEPSEQLQrKALLQELQRWAGpLPATHLRHLGEVVHTFS--HIKLTY--------QV 427
Cdd:PRK10776 17 EIFITRRAADAHMAGKWEFPGGKIEAGETPE-QALIRELQEEVG-ITVQHATLFEKLEYEFPdrHITLWFwlveswegEP 94
|
90 100
....*....|....*....|....*
gi 115298652 428 YGlaLEGQtpvttvpPGaRWLTQEE 452
Cdd:PRK10776 95 WG--KEGQ-------PG-RWVSQVA 109
|
|
| EndIII_4Fe-2S |
pfam10576 |
Iron-sulfur binding domain of endonuclease III; Escherichia coli endonuclease III (EC 4.2.99. ... |
262-278 |
2.30e-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: 35.44 E-value: 2.30e-03
|
| PRK08999 |
PRK08999 |
Nudix family hydrolase; |
358-453 |
3.46e-03 |
|
Nudix family hydrolase;
Pssm-ID: 236361 [Multi-domain] Cd Length: 312 Bit Score: 39.47 E-value: 3.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115298652 358 QILLVQRPNSGLLAGLWEFPSVTWEPSEQLqRKALLQELQRWAGpLPATHLRHLGEVVHTFSHIKLT---YQVYG----- 429
Cdd:PRK08999 18 RILLARRPEGKHQGGLWEFPGGKVEPGETV-EQALARELQEELG-IEVTAARPLITVRHDYPDKRVRldvRRVTAwqgep 95
|
90 100
....*....|....*....|....
gi 115298652 430 LALEGQtPVTTVPPgaRWLTQEEF 453
Cdd:PRK08999 96 HGREGQ-PLAWVAP--DELAVYPF 116
|
|
| YjhB |
COG1051 |
ADP-ribose pyrophosphatase YjhB, NUDIX family [Nucleotide transport and metabolism]; |
344-467 |
9.64e-03 |
|
ADP-ribose pyrophosphatase YjhB, NUDIX family [Nucleotide transport and metabolism];
Pssm-ID: 440671 [Multi-domain] Cd Length: 125 Bit Score: 36.49 E-value: 9.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115298652 344 SATCVLEQPGAlgaQILLVQRPNsGLLAGLWEFPSVTWEPSEQLqRKALLQELqrW--AGpLPATHLRHLGEVVHTFSHI 421
Cdd:COG1051 8 AVDAVIFRKDG---RVLLVRRAD-EPGKGLWALPGGKVEPGETP-EEAALREL--ReeTG-LEVEVLELLGVFDHPDRGH 79
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 115298652 422 KLTYQVYGLALEGQTPVTTVPPGARWLTQEEFHTAAVSTAMKKVFR 467
Cdd:COG1051 80 VVSVAFLAEVLSGEPRADDEIDEARWFPLDELPELAFTPADHEILE 125
|
|
| |
