|
Name |
Accession |
Description |
Interval |
E-value |
| MutY |
COG1194 |
Adenine-specific DNA glycosylase, acts on AG and A-oxoG pairs [Replication, recombination and ... |
91-499 |
2.25e-155 |
|
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: 447.66 E-value: 2.25e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358497 91 AEVTAFRGSLLSWYDQEKRDLPWRRraedemdlDRRAYAVWVSEVMLQQTQVATVINYYTGWMQKWPTLQDLASASLEEV 170
Cdd:COG1194 1 MDMASFAKRLLAWYDRHGRDLPWRQ--------TRDPYRVWLSEIMLQQTQVATVIPYYERFLERFPTVEALAAAPEDEV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358497 171 NQLWAGLGYYSRGRRLQEGARKVVEELGGHMPRTAETLQQLlPGVGRYTAGAIASIAFGQATGVVDGNVARVLCRVRAIG 250
Cdd:COG1194 73 LKLWEGLGYYSRARNLHKAAQQVVEEHGGVFPDTYEELLAL-PGIGPYTAAAIASIAFGEPAPIVDGNVKRVLSRLFAIE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358497 251 ADPSSTLVSQQLWGLAQQLVDPARPGDFNQAAMELGATVCTPQRPLCSQCPVESLCRARQRVEQEQLlasgslsgspdve 330
Cdd:COG1194 152 GPIGSPAAKKELWALAEELLPPERPGDFNQALMDLGATVCTPKKPKCLLCPLQDDCAAFAEGRQEEL------------- 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358497 331 ecapntgqchlclppsepwdqtlgvvnfPRKASRKPPREESSATCVLEQPGalgaQILLVQRPNSGLLAGLWEFPSVTWE 410
Cdd:COG1194 219 ----------------------------PVKKPKKKKPERYGAALVIRDDG----RVLLEKRPPKGLWGGLWEFPEFEWE 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358497 411 PSEQLQrkALLQELQRWAGpLPATHLRHLGEVVHTFSHIKLTYQVYGLALEGQTPVTtvPPGARWLTQEEFHTAAVSTAM 490
Cdd:COG1194 267 EAEDPE--ALERWLREELG-LEVEWLEPLGTVRHVFTHFRLHLTVYLARVPAGPPAE--PDGGRWVPLEELAALPLPAPM 341
|
....*....
gi 190358497 491 KKVFRVYQG 499
Cdd:COG1194 342 RKLLKALLK 350
|
|
| mutY |
TIGR01084 |
A/G-specific adenine glycosylase; This equivalog model identifies mutY members of the ... |
95-425 |
9.18e-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: 9.18e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358497 95 AFRGSLLSWYDQEKR-DLPWRrraedemdLDRRAYAVWVSEVMLQQTQVATVINYYTGWMQKWPTLQDLASASLEEVNQL 173
Cdd:TIGR01084 1 QFSEDLLSWYDKYGRkTLPWR--------QNKTPYRVWLSEVMLQQTQVATVIPYFERFLERFPTVQALANAPQDEVLKL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358497 174 WAGLGYYSRGRRLQEGARKVVEELGGHMPRTAETLQQlLPGVGRYTAGAIASIAFGQATGVVDGNVARVLCRVRAIGADP 253
Cdd:TIGR01084 73 WEGLGYYARARNLHKAAQEVVEEFGGEFPQDFEDLAA-LPGVGRYTAGAILSFALNKPYPILDGNVKRVLSRLFAVEGWP 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358497 254 SSTLVSQQLWGLAQQLVDPARPGDFNQAAMELGATVCTPQRPLCSQCPVESLCRARQRVEQEQllasgslsgspdveeca 333
Cdd:TIGR01084 152 GKKKVENRLWTLAESLLPKADPEAFNQALMDLGAMICTRKKPKCDLCPLQDFCLAYQQGTWEE----------------- 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358497 334 pntgqchlclppsepwdqtlgvvnFPRKASRKPPREESSATCVLEQPgalGAQILLVQRPNSGLLAGLWEFPsvtwepse 413
Cdd:TIGR01084 215 ------------------------YPVKKPKAAPPERTTYFLVLQNY---DGEVLLEQRPEKGLWGGLYCFP-------- 259
|
330
....*....|..
gi 190358497 414 QLQRKALLQELQ 425
Cdd:TIGR01084 260 QFEDEDSLAFLL 271
|
|
| PRK10880 |
PRK10880 |
adenine DNA glycosylase; |
96-451 |
4.59e-71 |
|
adenine DNA glycosylase;
Pssm-ID: 182805 [Multi-domain] Cd Length: 350 Bit Score: 231.52 E-value: 4.59e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358497 96 FRGSLLSWYDQEKRD-LPWRrraedemdLDRRAYAVWVSEVMLQQTQVATVINYYTGWMQKWPTLQDLASASLEEVNQLW 174
Cdd:PRK10880 6 FSAQVLDWYDKYGRKtLPWQ--------IDKTPYKVWLSEVMLQQTQVATVIPYFERFMARFPTVTDLANAPLDEVLHLW 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358497 175 AGLGYYSRGRRLQEGARKVVEELGGHMPRTAETLQQlLPGVGRYTAGAIASIAFGQATGVVDGNVARVLCRVRAIGADPS 254
Cdd:PRK10880 78 TGLGYYARARNLHKAAQQVATLHGGEFPETFEEVAA-LPGVGRSTAGAILSLSLGKHFPILDGNVKRVLARCYAVSGWPG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358497 255 STLVSQQLWGLAQQlVDPARP-GDFNQAAMELGATVCTPQRPLCSQCPVESLCRARqrveqeqllASGSlsgspdveeca 333
Cdd:PRK10880 157 KKEVENRLWQLSEQ-VTPAVGvERFNQAMMDLGAMVCTRSKPKCELCPLQNGCIAY---------ANHS----------- 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358497 334 pntgqchlclppsepWDQtlgvvnFPRKASRKPPREESSATCVLEQpgalGAQILLVQRPNSGLLAGLWEFPSVTWEpse 413
Cdd:PRK10880 216 ---------------WAL------YPGKKPKQTLPERTGYFLLLQH----GDEVWLEQRPPSGLWGGLFCFPQFADE--- 267
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 190358497 414 qlqrkallQELQRW--AGPLPATHLRHLGEVVHTFSHIKL 451
Cdd:PRK10880 268 --------EELRQWlaQRGIAADNLTQLTAFRHTFSHFHL 299
|
|
| ENDO3c |
cd00056 |
endonuclease III; includes endonuclease III (DNA-(apurinic or apyrimidinic site) lyase), ... |
128-286 |
2.14e-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: 2.14e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358497 128 YAVWVSEVMLQQTQVATVINYYTGWMQKW-PTLQDLASASLEEVNQLWAGLGYYSRGRRLQEGARKVVEELGG---HMPR 203
Cdd:cd00056 1 FEVLVSEILSQQTTDKAVNKAYERLFERYgPTPEALAAADEEELRELIRSLGYRRKAKYLKELARAIVEGFGGlvlDDPD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358497 204 TAETLQQlLPGVGRYTAGAIASIAFGQATGVVDGNVARVLCRVRAIGADPSstlvSQQLWGLAQQLVDPARPGDFNQAAM 283
Cdd:cd00056 81 AREELLA-LPGVGRKTANVVLLFALGPDAFPVDTHVRRVLKRLGLIPKKKT----PEELEELLEELLPKPYWGEANQALM 155
|
...
gi 190358497 284 ELG 286
Cdd:cd00056 156 DLG 158
|
|
| ENDO3c |
smart00478 |
endonuclease III; includes endonuclease III (DNA-(apurinic or apyrimidinic site) lyase), ... |
136-288 |
1.32e-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: 149.34 E-value: 1.32e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358497 136 MLQQTQVATVINYYTGWMQKWPTLQDLASASLEEVNQLWAGLG-YYSRGRRLQEGARKVVEELGGHMPRTAETLQQLlPG 214
Cdd:smart00478 1 LSQQTTDERVNKATERLFEKFPTPEDLAAADEEELEELIRGLGfYRRKARYLIELARILVEEYGGEVPDDREELLKL-PG 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 190358497 215 VGRYTAGAIASIAFGQATGVVDGNVARVLCRVRAIGAdpssTLVSQQLWGLAQQLVDPARPGDFNQAAMELGAT 288
Cdd:smart00478 80 VGRKTANAVLSFALGKPFIPVDTHVLRIAKRLGLVDK----KSTPEEVEKLLEKLLPEEDWRELNLLLIDFGRT 149
|
|
| HhH-GPD |
pfam00730 |
HhH-GPD superfamily base excision DNA repair protein; This family contains a diverse range of ... |
132-268 |
1.45e-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: 1.45e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358497 132 VSEVMLQQTQVATVINYYTGWMQKW-PTLQDLASASLEEVNQLWAGLGYY-SRGRRLQEGARKVVEELGGHMPRTAETLQ 209
Cdd:pfam00730 1 VSAILSQQTSDKAVNKITERLFEKFfPTPEDLADADEEELRELIRGLGFYrRKAKYLKELARILVEGYGGEVPLDEEELE 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 190358497 210 QLLPGVGRYTAGAIASIAFG--QATGVVDGNVARVLCRVRAIGADPSSTLVSQQLWGLAQQ 268
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 ... |
91-499 |
2.25e-155 |
|
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: 447.66 E-value: 2.25e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358497 91 AEVTAFRGSLLSWYDQEKRDLPWRRraedemdlDRRAYAVWVSEVMLQQTQVATVINYYTGWMQKWPTLQDLASASLEEV 170
Cdd:COG1194 1 MDMASFAKRLLAWYDRHGRDLPWRQ--------TRDPYRVWLSEIMLQQTQVATVIPYYERFLERFPTVEALAAAPEDEV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358497 171 NQLWAGLGYYSRGRRLQEGARKVVEELGGHMPRTAETLQQLlPGVGRYTAGAIASIAFGQATGVVDGNVARVLCRVRAIG 250
Cdd:COG1194 73 LKLWEGLGYYSRARNLHKAAQQVVEEHGGVFPDTYEELLAL-PGIGPYTAAAIASIAFGEPAPIVDGNVKRVLSRLFAIE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358497 251 ADPSSTLVSQQLWGLAQQLVDPARPGDFNQAAMELGATVCTPQRPLCSQCPVESLCRARQRVEQEQLlasgslsgspdve 330
Cdd:COG1194 152 GPIGSPAAKKELWALAEELLPPERPGDFNQALMDLGATVCTPKKPKCLLCPLQDDCAAFAEGRQEEL------------- 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358497 331 ecapntgqchlclppsepwdqtlgvvnfPRKASRKPPREESSATCVLEQPGalgaQILLVQRPNSGLLAGLWEFPSVTWE 410
Cdd:COG1194 219 ----------------------------PVKKPKKKKPERYGAALVIRDDG----RVLLEKRPPKGLWGGLWEFPEFEWE 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358497 411 PSEQLQrkALLQELQRWAGpLPATHLRHLGEVVHTFSHIKLTYQVYGLALEGQTPVTtvPPGARWLTQEEFHTAAVSTAM 490
Cdd:COG1194 267 EAEDPE--ALERWLREELG-LEVEWLEPLGTVRHVFTHFRLHLTVYLARVPAGPPAE--PDGGRWVPLEELAALPLPAPM 341
|
....*....
gi 190358497 491 KKVFRVYQG 499
Cdd:COG1194 342 RKLLKALLK 350
|
|
| mutY |
TIGR01084 |
A/G-specific adenine glycosylase; This equivalog model identifies mutY members of the ... |
95-425 |
9.18e-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: 9.18e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358497 95 AFRGSLLSWYDQEKR-DLPWRrraedemdLDRRAYAVWVSEVMLQQTQVATVINYYTGWMQKWPTLQDLASASLEEVNQL 173
Cdd:TIGR01084 1 QFSEDLLSWYDKYGRkTLPWR--------QNKTPYRVWLSEVMLQQTQVATVIPYFERFLERFPTVQALANAPQDEVLKL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358497 174 WAGLGYYSRGRRLQEGARKVVEELGGHMPRTAETLQQlLPGVGRYTAGAIASIAFGQATGVVDGNVARVLCRVRAIGADP 253
Cdd:TIGR01084 73 WEGLGYYARARNLHKAAQEVVEEFGGEFPQDFEDLAA-LPGVGRYTAGAILSFALNKPYPILDGNVKRVLSRLFAVEGWP 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358497 254 SSTLVSQQLWGLAQQLVDPARPGDFNQAAMELGATVCTPQRPLCSQCPVESLCRARQRVEQEQllasgslsgspdveeca 333
Cdd:TIGR01084 152 GKKKVENRLWTLAESLLPKADPEAFNQALMDLGAMICTRKKPKCDLCPLQDFCLAYQQGTWEE----------------- 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358497 334 pntgqchlclppsepwdqtlgvvnFPRKASRKPPREESSATCVLEQPgalGAQILLVQRPNSGLLAGLWEFPsvtwepse 413
Cdd:TIGR01084 215 ------------------------YPVKKPKAAPPERTTYFLVLQNY---DGEVLLEQRPEKGLWGGLYCFP-------- 259
|
330
....*....|..
gi 190358497 414 QLQRKALLQELQ 425
Cdd:TIGR01084 260 QFEDEDSLAFLL 271
|
|
| PRK10880 |
PRK10880 |
adenine DNA glycosylase; |
96-451 |
4.59e-71 |
|
adenine DNA glycosylase;
Pssm-ID: 182805 [Multi-domain] Cd Length: 350 Bit Score: 231.52 E-value: 4.59e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358497 96 FRGSLLSWYDQEKRD-LPWRrraedemdLDRRAYAVWVSEVMLQQTQVATVINYYTGWMQKWPTLQDLASASLEEVNQLW 174
Cdd:PRK10880 6 FSAQVLDWYDKYGRKtLPWQ--------IDKTPYKVWLSEVMLQQTQVATVIPYFERFMARFPTVTDLANAPLDEVLHLW 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358497 175 AGLGYYSRGRRLQEGARKVVEELGGHMPRTAETLQQlLPGVGRYTAGAIASIAFGQATGVVDGNVARVLCRVRAIGADPS 254
Cdd:PRK10880 78 TGLGYYARARNLHKAAQQVATLHGGEFPETFEEVAA-LPGVGRSTAGAILSLSLGKHFPILDGNVKRVLARCYAVSGWPG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358497 255 STLVSQQLWGLAQQlVDPARP-GDFNQAAMELGATVCTPQRPLCSQCPVESLCRARqrveqeqllASGSlsgspdveeca 333
Cdd:PRK10880 157 KKEVENRLWQLSEQ-VTPAVGvERFNQAMMDLGAMVCTRSKPKCELCPLQNGCIAY---------ANHS----------- 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358497 334 pntgqchlclppsepWDQtlgvvnFPRKASRKPPREESSATCVLEQpgalGAQILLVQRPNSGLLAGLWEFPSVTWEpse 413
Cdd:PRK10880 216 ---------------WAL------YPGKKPKQTLPERTGYFLLLQH----GDEVWLEQRPPSGLWGGLFCFPQFADE--- 267
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 190358497 414 qlqrkallQELQRW--AGPLPATHLRHLGEVVHTFSHIKL 451
Cdd:PRK10880 268 --------EELRQWlaQRGIAADNLTQLTAFRHTFSHFHL 299
|
|
| ENDO3c |
cd00056 |
endonuclease III; includes endonuclease III (DNA-(apurinic or apyrimidinic site) lyase), ... |
128-286 |
2.14e-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: 2.14e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358497 128 YAVWVSEVMLQQTQVATVINYYTGWMQKW-PTLQDLASASLEEVNQLWAGLGYYSRGRRLQEGARKVVEELGG---HMPR 203
Cdd:cd00056 1 FEVLVSEILSQQTTDKAVNKAYERLFERYgPTPEALAAADEEELRELIRSLGYRRKAKYLKELARAIVEGFGGlvlDDPD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358497 204 TAETLQQlLPGVGRYTAGAIASIAFGQATGVVDGNVARVLCRVRAIGADPSstlvSQQLWGLAQQLVDPARPGDFNQAAM 283
Cdd:cd00056 81 AREELLA-LPGVGRKTANVVLLFALGPDAFPVDTHVRRVLKRLGLIPKKKT----PEELEELLEELLPKPYWGEANQALM 155
|
...
gi 190358497 284 ELG 286
Cdd:cd00056 156 DLG 158
|
|
| ENDO3c |
smart00478 |
endonuclease III; includes endonuclease III (DNA-(apurinic or apyrimidinic site) lyase), ... |
136-288 |
1.32e-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: 149.34 E-value: 1.32e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358497 136 MLQQTQVATVINYYTGWMQKWPTLQDLASASLEEVNQLWAGLG-YYSRGRRLQEGARKVVEELGGHMPRTAETLQQLlPG 214
Cdd:smart00478 1 LSQQTTDERVNKATERLFEKFPTPEDLAAADEEELEELIRGLGfYRRKARYLIELARILVEEYGGEVPDDREELLKL-PG 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 190358497 215 VGRYTAGAIASIAFGQATGVVDGNVARVLCRVRAIGAdpssTLVSQQLWGLAQQLVDPARPGDFNQAAMELGAT 288
Cdd:smart00478 80 VGRKTANAVLSFALGKPFIPVDTHVLRIAKRLGLVDK----KSTPEEVEKLLEKLLPEEDWRELNLLLIDFGRT 149
|
|
| HhH-GPD |
pfam00730 |
HhH-GPD superfamily base excision DNA repair protein; This family contains a diverse range of ... |
132-268 |
1.45e-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: 1.45e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358497 132 VSEVMLQQTQVATVINYYTGWMQKW-PTLQDLASASLEEVNQLWAGLGYY-SRGRRLQEGARKVVEELGGHMPRTAETLQ 209
Cdd:pfam00730 1 VSAILSQQTSDKAVNKITERLFEKFfPTPEDLADADEEELRELIRGLGFYrRKAKYLKELARILVEGYGGEVPLDEEELE 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 190358497 210 QLLPGVGRYTAGAIASIAFG--QATGVVDGNVARVLCRVRAIGADPSSTLVSQQLWGLAQQ 268
Cdd:pfam00730 81 ALLKGVGRWTAEAVLIFALGrpDPLPVVDTHVRRVLKRLGLIKEKPTPKEVERELEELWPP 141
|
|
| PRK13910 |
PRK13910 |
DNA glycosylase MutY; Provisional |
136-317 |
1.26e-34 |
|
DNA glycosylase MutY; Provisional
Pssm-ID: 172427 [Multi-domain] Cd Length: 289 Bit Score: 132.07 E-value: 1.26e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358497 136 MLQQTQVATVIN-YYTGWMQKWPTLQDLASASLEEVNQLWAGLGYYSRGRRLQEGARKVVEELGGHMPRTAETLQQlLPG 214
Cdd:PRK13910 1 MSQQTQINTVVErFYSPFLEAFPTLKDLANAPLEEVLLLWRGLGYYSRAKNLKKSAEICVKEHHSQLPNDYQSLLK-LPG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358497 215 VGRYTAGAIASIAFGQATGVVDGNVARVLCRVraIGADPSSTlvSQQLWGLAQQLVDPARPGDFNQAAMELGATVCTPqR 294
Cdd:PRK13910 80 IGAYTANAILCFGFREKSACVDANIKRVLLRL--FGLDPNIH--AKDLQIKANDFLNLNESFNHNQALIDLGALICSP-K 154
|
170 180
....*....|....*....|...
gi 190358497 295 PLCSQCPVESLCRARQRVEQEQL 317
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 ... |
367-494 |
1.58e-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: 1.58e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358497 367 PREESSATCVLEQPGalgaQILLVQRPNSGLLAGLWEFPSVTWEPSEQlqrkaLLQELQRWAGPLPATHLRHLGEVVHTF 446
Cdd:cd03431 1 VPERYFTVLVLRDGG----RVLLEKRPEKGLLAGLWEFPLVETEEEEE-----EAEALLGLLAEELLLILEPLGEVKHVF 71
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 190358497 447 SHIKLTYQVYGLALEGQTPVTtvPPGARWLTQEEFHTAAVSTAMKKVF 494
Cdd:cd03431 72 SHFRLHITVYLVELPEAPPAA--PDEGRWVDLEELDEYALPAPMRKLL 117
|
|
| Nth |
COG0177 |
Endonuclease III [Replication, recombination and repair]; |
154-310 |
5.69e-30 |
|
Endonuclease III [Replication, recombination and repair];
Pssm-ID: 439947 [Multi-domain] Cd Length: 198 Bit Score: 116.35 E-value: 5.69e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358497 154 QKWPTLQDLASASLEEVNQLWAGLGYY-SRGRRLQEGARKVVEELGGHMPRTAETLQQLlPGVGRYTAGAIASIAFGQAT 232
Cdd:COG0177 47 ARYPTPEALAAADLEELEELIRPIGLYrNKAKNIIALARILVEKYGGEVPETREELESL-PGVGRKTANVVLNFAFGKPA 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358497 233 GVVDGNVARVLCRvraIG-ADPSSTL-VSQQLwglaQQLVDPARPGDFNQAAMELGATVCTPQRPLCSQCPVESLCRARQ 310
Cdd:COG0177 126 IAVDTHVHRVSNR---LGlVPGKDPEeVEKDL----MKLIPKEYWGDLHHLLILHGRYICKARKPKCEECPLADLCPYYG 198
|
|
| NUDIX_4 |
pfam14815 |
NUDIX domain; |
386-495 |
4.81e-23 |
|
NUDIX domain;
Pssm-ID: 464330 [Multi-domain] Cd Length: 114 Bit Score: 93.92 E-value: 4.81e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358497 386 QILLVQRPNSGLLAGLWEFPSVTWEPSEQLQRKalLQELQRWAgpLPATHLRHlGEVVHTFSHIKLTYQVYGLALEGQTP 465
Cdd:pfam14815 11 RVLLRKRPEKGLLGGLWEFPGGKVEPGETLEEA--LARLEELG--IEVEVLEP-GTVKHVFTHFRLTLHVYLVREVEGEE 85
|
90 100 110
....*....|....*....|....*....|
gi 190358497 466 vtTVPPGARWLTQEEFHTAAVSTAMKKVFR 495
Cdd:pfam14815 86 --EPQQELRWVTPEELDKYALPAAVRKILE 113
|
|
| nth |
TIGR01083 |
endonuclease III; This equivalog model identifes nth members of the pfam00730 superfamily ... |
154-297 |
4.61e-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: 4.61e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358497 154 QKWPTLQDLASASLEEVNQLWAGLGYY-SRGRRLQEGARKVVEELGGHMPRTAETLQQLlPGVGRYTAGAIASIAFGQAT 232
Cdd:TIGR01083 54 EVYPTPQALAQAGLEELEEYIKSIGLYrNKAKNIIELCRKLVERYGGEVPEDREELVKL-PGVGRKTANVVLNVAFGIPA 132
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 190358497 233 GVVDGNVARVLCRVR-AIGADPSST------LVSQQLWglaqqlvdparpGDFNQAAMELGATVCTPQRPLC 297
Cdd:TIGR01083 133 IAVDTHVFRVSNRLGlSKGKDPIKVeedlmkLVPREFW------------VKLHHWLILHGRYTCKARKPLC 192
|
|
| PRK10702 |
PRK10702 |
endonuclease III; Provisional |
179-312 |
1.87e-08 |
|
endonuclease III; Provisional
Pssm-ID: 182661 [Multi-domain] Cd Length: 211 Bit Score: 55.02 E-value: 1.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358497 179 YYSRGRRLQEGARKVVEELGGHMPRTAETLQQLlPGVGRYTAGAIASIAFGQATGVVDGNVARVLCRVraiGADPSSTLv 258
Cdd:PRK10702 82 YNSKAENVIKTCRILLEQHNGEVPEDRAALEAL-PGVGRKTANVVLNTAFGWPTIAVDTHIFRVCNRT---QFAPGKNV- 156
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 190358497 259 sQQLWGLAQQLVDPARPGDFNQAAMELGATVCTPQRPLCSQCPVESLCRARQRV 312
Cdd:PRK10702 157 -EQVEEKLLKVVPAEFKVDCHHWLILHGRYTCIARKPRCGSCIIEDLCEYKEKV 209
|
|
| HP0602 |
COG2231 |
3-Methyladenine DNA glycosylase, HhH-GPD/Endo3 superfamily [Replication, recombination and ... |
158-312 |
1.67e-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: 1.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358497 158 TLQDLASASLEEVNQLWAGLGYYSR-GRRLQEGARKVVEELGGHMPR-----TAETLQQLL--PGVGRYTAGAIASIAFG 229
Cdd:COG2231 61 DPEALAALDPEELAELIRPSGFYNQkAKRLKNLARWLVERYGGGLEKlkalpTEELREELLslKGIGPETADSILLYAFN 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358497 230 QATGVVDGNVARVLCRVrAIGADPSStlvsqqlWGLAQQLVDPARPGDFNQA----AM--ELGATVCTPqRPLCSQCPVE 303
Cdd:COG2231 141 RPVFVVDAYTRRIFSRL-GLIEEDAS-------YDELQRLFEENLPPDVALYnefhALivEHGKEYCKK-KPKCEECPLR 211
|
....*....
gi 190358497 304 SLCRARQRV 312
Cdd:COG2231 212 DLCPYGGQE 220
|
|
| NUDIX_MutT_NudA_like |
cd03425 |
MutT pyrophosphohydrolase; The MutT pyrophosphohydrolase is a prototypical NUDIX hydrolase ... |
376-483 |
3.07e-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: 3.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358497 376 VLEQPGalgaQILLVQRPNSGLLAGLWEFP--SVtwEPSEQLQrKALLQELQ---RWAgplpATHLRHLGEVVHTFSHIK 450
Cdd:cd03425 7 IIVDDG----RVLIAQRPEGKHLAGLWEFPggKV--EPGETPE-QALVRELReelGIE----VEVGEPLGTVEHDYPDFH 75
|
90 100 110
....*....|....*....|....*....|...
gi 190358497 451 LTYQVYGLALEGQTPVTTVPPGARWLTQEEFHT 483
Cdd:cd03425 76 VRLHVYLCTLWSGEPQLLEHQELRWVTPEELDD 108
|
|
| PRK10546 |
PRK10546 |
pyrimidine (deoxy)nucleoside triphosphate diphosphatase; |
376-425 |
3.89e-05 |
|
pyrimidine (deoxy)nucleoside triphosphate diphosphatase;
Pssm-ID: 182536 [Multi-domain] Cd Length: 135 Bit Score: 43.58 E-value: 3.89e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 190358497 376 VLEQPGalgaQILLVQRPNSGLLAGLWEFPSVTWEPSEQlQRKALLQELQ 425
Cdd:PRK10546 10 IIERDG----KILLAQRPAHSDQAGLWEFAGGKVEPGES-QPQALIRELR 54
|
|
| FES |
smart00525 |
iron-sulpphur binding domain in DNA-(apurinic or apyrimidinic site) lyase (subfamily of ENDO3); ... |
289-309 |
5.60e-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: 40.23 E-value: 5.60e-05
|
| HHH |
pfam00633 |
Helix-hairpin-helix motif; The helix-hairpin-helix DNA-binding motif is found to be duplicated ... |
196-226 |
1.04e-04 |
|
Helix-hairpin-helix motif; The helix-hairpin-helix DNA-binding motif is found to be duplicated in the central domain of RuvA. The HhH domain of DisA, a bacterial checkpoint control protein, is a DNA-binding domain.
Pssm-ID: 425789 [Multi-domain] Cd Length: 30 Bit Score: 39.32 E-value: 1.04e-04
10 20 30
....*....|....*....|....*....|.
gi 190358497 196 ELGGHMPRTAETLQQLlPGVGRYTAGAIASI 226
Cdd:pfam00633 1 SLEGLIPASVEELLAL-PGVGPKTAEAILSY 30
|
|
| PRK10776 |
PRK10776 |
8-oxo-dGTP diphosphatase MutT; |
386-480 |
1.69e-04 |
|
8-oxo-dGTP diphosphatase MutT;
Pssm-ID: 182721 [Multi-domain] Cd Length: 129 Bit Score: 41.51 E-value: 1.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358497 386 QILLVQRPNSGLLAGLWEFPSVTWEPSEQLQrKALLQELQRWAGpLPATHLRHLGEVVHTFS--HIKLTY--------QV 455
Cdd:PRK10776 17 EIFITRRAADAHMAGKWEFPGGKIEAGETPE-QALIRELQEEVG-ITVQHATLFEKLEYEFPdrHITLWFwlveswegEP 94
|
90 100
....*....|....*....|....*
gi 190358497 456 YGlaLEGQtpvttvpPGaRWLTQEE 480
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. ... |
290-306 |
3.90e-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: 34.67 E-value: 3.90e-03
|
| PRK08999 |
PRK08999 |
Nudix family hydrolase; |
386-481 |
4.50e-03 |
|
Nudix family hydrolase;
Pssm-ID: 236361 [Multi-domain] Cd Length: 312 Bit Score: 39.47 E-value: 4.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358497 386 QILLVQRPNSGLLAGLWEFPSVTWEPSEQLqRKALLQELQRWAGpLPATHLRHLGEVVHTFSHIKLT---YQVYG----- 457
Cdd:PRK08999 18 RILLARRPEGKHQGGLWEFPGGKVEPGETV-EQALARELQEELG-IEVTAARPLITVRHDYPDKRVRldvRRVTAwqgep 95
|
90 100
....*....|....*....|....
gi 190358497 458 LALEGQtPVTTVPPgaRWLTQEEF 481
Cdd:PRK08999 96 HGREGQ-PLAWVAP--DELAVYPF 116
|
|
| |
