|
Name |
Accession |
Description |
Interval |
E-value |
| MutY |
COG1194 |
Adenine-specific DNA glycosylase, acts on AG and A-oxoG pairs [Replication, recombination and ... |
62-467 |
3.63e-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: 448.43 E-value: 3.63e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157254 62 ADVTAFRSNLLSWYDQEKRDLPWRNlakeeansDRRAYAVWVSEVMLQQTQVATVIDYYTRWMQKWPKLQDLASASLEEV 141
Cdd:COG1194 1 MDMASFAKRLLAWYDRHGRDLPWRQ--------TRDPYRVWLSEIMLQQTQVATVIPYYERFLERFPTVEALAAAPEDEV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157254 142 NQLWSGLGYYSRGRRLQEGARKVVEELGGHMPRTAETLQQLlPGVGRYTAGAIASIAFDQVTGVVDGNVLRVLCRVRAIG 221
Cdd:COG1194 73 LKLWEGLGYYSRARNLHKAAQQVVEEHGGVFPDTYEELLAL-PGIGPYTAAAIASIAFGEPAPIVDGNVKRVLSRLFAIE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157254 222 ADPTSTLVSHHLWNLAQQLVDPARPGDFNQAAMELGATVCTPQRPLCSHCPVQSLCRAYQRvqrgqlsalpGRPdieeca 301
Cdd:COG1194 152 GPIGSPAAKKELWALAEELLPPERPGDFNQALMDLGATVCTPKKPKCLLCPLQDDCAAFAE----------GRQ------ 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157254 302 lntrqcqlcltssspwdpsmgvANFPRKASRRPPREEYSATCVVEQPGAiggplVLLVQRPDSGLLAGLWEFPSVtlEPS 381
Cdd:COG1194 216 ----------------------EELPVKKPKKKKPERYGAALVIRDDGR-----VLLEKRPPKGLWGGLWEFPEF--EWE 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157254 382 EQHQHKALLQELQRWCGpLPAIRLQHLGEVIHIFSHIKLTYQVYSLALDQAPAStAPPGARWLTWEEFCNAAVSTAMKKV 461
Cdd:COG1194 267 EAEDPEALERWLREELG-LEVEWLEPLGTVRHVFTHFRLHLTVYLARVPAGPPA-EPDGGRWVPLEELAALPLPAPMRKL 344
|
....*.
gi 1907157254 462 FRMYED 467
Cdd:COG1194 345 LKALLK 350
|
|
| mutY |
TIGR01084 |
A/G-specific adenine glycosylase; This equivalog model identifies mutY members of the ... |
66-374 |
6.75e-100 |
|
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: 302.02 E-value: 6.75e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157254 66 AFRSNLLSWYDQEKR-DLPWRNlakeeansDRRAYAVWVSEVMLQQTQVATVIDYYTRWMQKWPKLQDLASASLEEVNQL 144
Cdd:TIGR01084 1 QFSEDLLSWYDKYGRkTLPWRQ--------NKTPYRVWLSEVMLQQTQVATVIPYFERFLERFPTVQALANAPQDEVLKL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157254 145 WSGLGYYSRGRRLQEGARKVVEELGGHMPRTAETLQQlLPGVGRYTAGAIASIAFDQVTGVVDGNVLRVLCRVRAIGADP 224
Cdd:TIGR01084 73 WEGLGYYARARNLHKAAQEVVEEFGGEFPQDFEDLAA-LPGVGRYTAGAILSFALNKPYPILDGNVKRVLSRLFAVEGWP 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157254 225 TSTLVSHHLWNLAQQLVDPARPGDFNQAAMELGATVCTPQRPLCSHCPVQSLCRAYqrvQRGQLSALPGrpdieecalnt 304
Cdd:TIGR01084 152 GKKKVENRLWTLAESLLPKADPEAFNQALMDLGAMICTRKKPKCDLCPLQDFCLAY---QQGTWEEYPV----------- 217
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157254 305 rqcqlcltssspwdpsmgvanfpRKASRRPPREEYSATCVVEQPGAiggplVLLVQRPDSGLLAGLWEFP 374
Cdd:TIGR01084 218 -----------------------KKPKAAPPERTTYFLVLQNYDGE-----VLLEQRPEKGLWGGLYCFP 259
|
|
| PRK10880 |
PRK10880 |
adenine DNA glycosylase; |
67-420 |
7.36e-69 |
|
adenine DNA glycosylase;
Pssm-ID: 182805 [Multi-domain] Cd Length: 350 Bit Score: 224.59 E-value: 7.36e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157254 67 FRSNLLSWYDQEKRD-LPWRnlakeeanSDRRAYAVWVSEVMLQQTQVATVIDYYTRWMQKWPKLQDLASASLEEVNQLW 145
Cdd:PRK10880 6 FSAQVLDWYDKYGRKtLPWQ--------IDKTPYKVWLSEVMLQQTQVATVIPYFERFMARFPTVTDLANAPLDEVLHLW 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157254 146 SGLGYYSRGRRLQEGARKVVEELGGHMPRTAETLQQlLPGVGRYTAGAIASIAFDQVTGVVDGNVLRVLCRVRAIGADPT 225
Cdd:PRK10880 78 TGLGYYARARNLHKAAQQVATLHGGEFPETFEEVAA-LPGVGRSTAGAILSLSLGKHFPILDGNVKRVLARCYAVSGWPG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157254 226 STLVSHHLWNLAQQlVDPARP-GDFNQAAMELGATVCTPQRPLCSHCPVQSLCRAYqrvqrgqlsalpgrpdieecalnt 304
Cdd:PRK10880 157 KKEVENRLWQLSEQ-VTPAVGvERFNQAMMDLGAMVCTRSKPKCELCPLQNGCIAY------------------------ 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157254 305 rqcqlcltSSSPWdpsmgvANFPRKASRRPPREEYSATCVVEQpgaigGPLVLLVQRPDSGLLAGLWEFPSVTLEpseqh 384
Cdd:PRK10880 212 --------ANHSW------ALYPGKKPKQTLPERTGYFLLLQH-----GDEVWLEQRPPSGLWGGLFCFPQFADE----- 267
|
330 340 350
....*....|....*....|....*....|....*...
gi 1907157254 385 qhkallQELQRWCGP--LPAIRLQHLGEVIHIFSHIKL 420
Cdd:PRK10880 268 ------EELRQWLAQrgIAADNLTQLTAFRHTFSHFHL 299
|
|
| ENDO3c |
cd00056 |
endonuclease III; includes endonuclease III (DNA-(apurinic or apyrimidinic site) lyase), ... |
99-257 |
1.53e-47 |
|
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: 162.03 E-value: 1.53e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157254 99 YAVWVSEVMLQQTQVATVIDYYTRWMQKW-PKLQDLASASLEEVNQLWSGLGYYSRGRRLQEGARKVVEELGG---HMPR 174
Cdd:cd00056 1 FEVLVSEILSQQTTDKAVNKAYERLFERYgPTPEALAAADEEELRELIRSLGYRRKAKYLKELARAIVEGFGGlvlDDPD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157254 175 TAETLQQLlPGVGRYTAGAIASIAFDQVTGVVDGNVLRVLCRVRAIGADPTstlvSHHLWNLAQQLVDPARPGDFNQAAM 254
Cdd:cd00056 81 AREELLAL-PGVGRKTANVVLLFALGPDAFPVDTHVRRVLKRLGLIPKKKT----PEELEELLEELLPKPYWGEANQALM 155
|
...
gi 1907157254 255 ELG 257
Cdd:cd00056 156 DLG 158
|
|
| ENDO3c |
smart00478 |
endonuclease III; includes endonuclease III (DNA-(apurinic or apyrimidinic site) lyase), ... |
107-259 |
1.17e-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: 148.95 E-value: 1.17e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157254 107 MLQQTQVATVIDYYTRWMQKWPKLQDLASASLEEVNQLWSGLG-YYSRGRRLQEGARKVVEELGGHMPRTAETLQQLlPG 185
Cdd:smart00478 1 LSQQTTDERVNKATERLFEKFPTPEDLAAADEEELEELIRGLGfYRRKARYLIELARILVEEYGGEVPDDREELLKL-PG 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907157254 186 VGRYTAGAIASIAFDQVTGVVDGNVLRVLCRVRAIGADPTstlvSHHLWNLAQQLVDPARPGDFNQAAMELGAT 259
Cdd:smart00478 80 VGRKTANAVLSFALGKPFIPVDTHVLRIAKRLGLVDKKST----PEEVEKLLEKLLPEEDWRELNLLLIDFGRT 149
|
|
| HhH-GPD |
pfam00730 |
HhH-GPD superfamily base excision DNA repair protein; This family contains a diverse range of ... |
103-239 |
4.93e-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: 144.35 E-value: 4.93e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157254 103 VSEVMLQQTQVATVIDYYTRWMQKW-PKLQDLASASLEEVNQLWSGLGYY-SRGRRLQEGARKVVEELGGHMPRTAETLQ 180
Cdd:pfam00730 1 VSAILSQQTSDKAVNKITERLFEKFfPTPEDLADADEEELRELIRGLGFYrRKAKYLKELARILVEGYGGEVPLDEEELE 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907157254 181 QLLPGVGRYTAGAIASIAF--DQVTGVVDGNVLRVLCRVRAIGADPTSTLVSHHLWNLAQQ 239
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 ... |
62-467 |
3.63e-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: 448.43 E-value: 3.63e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157254 62 ADVTAFRSNLLSWYDQEKRDLPWRNlakeeansDRRAYAVWVSEVMLQQTQVATVIDYYTRWMQKWPKLQDLASASLEEV 141
Cdd:COG1194 1 MDMASFAKRLLAWYDRHGRDLPWRQ--------TRDPYRVWLSEIMLQQTQVATVIPYYERFLERFPTVEALAAAPEDEV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157254 142 NQLWSGLGYYSRGRRLQEGARKVVEELGGHMPRTAETLQQLlPGVGRYTAGAIASIAFDQVTGVVDGNVLRVLCRVRAIG 221
Cdd:COG1194 73 LKLWEGLGYYSRARNLHKAAQQVVEEHGGVFPDTYEELLAL-PGIGPYTAAAIASIAFGEPAPIVDGNVKRVLSRLFAIE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157254 222 ADPTSTLVSHHLWNLAQQLVDPARPGDFNQAAMELGATVCTPQRPLCSHCPVQSLCRAYQRvqrgqlsalpGRPdieeca 301
Cdd:COG1194 152 GPIGSPAAKKELWALAEELLPPERPGDFNQALMDLGATVCTPKKPKCLLCPLQDDCAAFAE----------GRQ------ 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157254 302 lntrqcqlcltssspwdpsmgvANFPRKASRRPPREEYSATCVVEQPGAiggplVLLVQRPDSGLLAGLWEFPSVtlEPS 381
Cdd:COG1194 216 ----------------------EELPVKKPKKKKPERYGAALVIRDDGR-----VLLEKRPPKGLWGGLWEFPEF--EWE 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157254 382 EQHQHKALLQELQRWCGpLPAIRLQHLGEVIHIFSHIKLTYQVYSLALDQAPAStAPPGARWLTWEEFCNAAVSTAMKKV 461
Cdd:COG1194 267 EAEDPEALERWLREELG-LEVEWLEPLGTVRHVFTHFRLHLTVYLARVPAGPPA-EPDGGRWVPLEELAALPLPAPMRKL 344
|
....*.
gi 1907157254 462 FRMYED 467
Cdd:COG1194 345 LKALLK 350
|
|
| mutY |
TIGR01084 |
A/G-specific adenine glycosylase; This equivalog model identifies mutY members of the ... |
66-374 |
6.75e-100 |
|
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: 302.02 E-value: 6.75e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157254 66 AFRSNLLSWYDQEKR-DLPWRNlakeeansDRRAYAVWVSEVMLQQTQVATVIDYYTRWMQKWPKLQDLASASLEEVNQL 144
Cdd:TIGR01084 1 QFSEDLLSWYDKYGRkTLPWRQ--------NKTPYRVWLSEVMLQQTQVATVIPYFERFLERFPTVQALANAPQDEVLKL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157254 145 WSGLGYYSRGRRLQEGARKVVEELGGHMPRTAETLQQlLPGVGRYTAGAIASIAFDQVTGVVDGNVLRVLCRVRAIGADP 224
Cdd:TIGR01084 73 WEGLGYYARARNLHKAAQEVVEEFGGEFPQDFEDLAA-LPGVGRYTAGAILSFALNKPYPILDGNVKRVLSRLFAVEGWP 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157254 225 TSTLVSHHLWNLAQQLVDPARPGDFNQAAMELGATVCTPQRPLCSHCPVQSLCRAYqrvQRGQLSALPGrpdieecalnt 304
Cdd:TIGR01084 152 GKKKVENRLWTLAESLLPKADPEAFNQALMDLGAMICTRKKPKCDLCPLQDFCLAY---QQGTWEEYPV----------- 217
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157254 305 rqcqlcltssspwdpsmgvanfpRKASRRPPREEYSATCVVEQPGAiggplVLLVQRPDSGLLAGLWEFP 374
Cdd:TIGR01084 218 -----------------------KKPKAAPPERTTYFLVLQNYDGE-----VLLEQRPEKGLWGGLYCFP 259
|
|
| PRK10880 |
PRK10880 |
adenine DNA glycosylase; |
67-420 |
7.36e-69 |
|
adenine DNA glycosylase;
Pssm-ID: 182805 [Multi-domain] Cd Length: 350 Bit Score: 224.59 E-value: 7.36e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157254 67 FRSNLLSWYDQEKRD-LPWRnlakeeanSDRRAYAVWVSEVMLQQTQVATVIDYYTRWMQKWPKLQDLASASLEEVNQLW 145
Cdd:PRK10880 6 FSAQVLDWYDKYGRKtLPWQ--------IDKTPYKVWLSEVMLQQTQVATVIPYFERFMARFPTVTDLANAPLDEVLHLW 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157254 146 SGLGYYSRGRRLQEGARKVVEELGGHMPRTAETLQQlLPGVGRYTAGAIASIAFDQVTGVVDGNVLRVLCRVRAIGADPT 225
Cdd:PRK10880 78 TGLGYYARARNLHKAAQQVATLHGGEFPETFEEVAA-LPGVGRSTAGAILSLSLGKHFPILDGNVKRVLARCYAVSGWPG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157254 226 STLVSHHLWNLAQQlVDPARP-GDFNQAAMELGATVCTPQRPLCSHCPVQSLCRAYqrvqrgqlsalpgrpdieecalnt 304
Cdd:PRK10880 157 KKEVENRLWQLSEQ-VTPAVGvERFNQAMMDLGAMVCTRSKPKCELCPLQNGCIAY------------------------ 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157254 305 rqcqlcltSSSPWdpsmgvANFPRKASRRPPREEYSATCVVEQpgaigGPLVLLVQRPDSGLLAGLWEFPSVTLEpseqh 384
Cdd:PRK10880 212 --------ANHSW------ALYPGKKPKQTLPERTGYFLLLQH-----GDEVWLEQRPPSGLWGGLFCFPQFADE----- 267
|
330 340 350
....*....|....*....|....*....|....*...
gi 1907157254 385 qhkallQELQRWCGP--LPAIRLQHLGEVIHIFSHIKL 420
Cdd:PRK10880 268 ------EELRQWLAQrgIAADNLTQLTAFRHTFSHFHL 299
|
|
| ENDO3c |
cd00056 |
endonuclease III; includes endonuclease III (DNA-(apurinic or apyrimidinic site) lyase), ... |
99-257 |
1.53e-47 |
|
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: 162.03 E-value: 1.53e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157254 99 YAVWVSEVMLQQTQVATVIDYYTRWMQKW-PKLQDLASASLEEVNQLWSGLGYYSRGRRLQEGARKVVEELGG---HMPR 174
Cdd:cd00056 1 FEVLVSEILSQQTTDKAVNKAYERLFERYgPTPEALAAADEEELRELIRSLGYRRKAKYLKELARAIVEGFGGlvlDDPD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157254 175 TAETLQQLlPGVGRYTAGAIASIAFDQVTGVVDGNVLRVLCRVRAIGADPTstlvSHHLWNLAQQLVDPARPGDFNQAAM 254
Cdd:cd00056 81 AREELLAL-PGVGRKTANVVLLFALGPDAFPVDTHVRRVLKRLGLIPKKKT----PEELEELLEELLPKPYWGEANQALM 155
|
...
gi 1907157254 255 ELG 257
Cdd:cd00056 156 DLG 158
|
|
| ENDO3c |
smart00478 |
endonuclease III; includes endonuclease III (DNA-(apurinic or apyrimidinic site) lyase), ... |
107-259 |
1.17e-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: 148.95 E-value: 1.17e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157254 107 MLQQTQVATVIDYYTRWMQKWPKLQDLASASLEEVNQLWSGLG-YYSRGRRLQEGARKVVEELGGHMPRTAETLQQLlPG 185
Cdd:smart00478 1 LSQQTTDERVNKATERLFEKFPTPEDLAAADEEELEELIRGLGfYRRKARYLIELARILVEEYGGEVPDDREELLKL-PG 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907157254 186 VGRYTAGAIASIAFDQVTGVVDGNVLRVLCRVRAIGADPTstlvSHHLWNLAQQLVDPARPGDFNQAAMELGAT 259
Cdd:smart00478 80 VGRKTANAVLSFALGKPFIPVDTHVLRIAKRLGLVDKKST----PEEVEKLLEKLLPEEDWRELNLLLIDFGRT 149
|
|
| HhH-GPD |
pfam00730 |
HhH-GPD superfamily base excision DNA repair protein; This family contains a diverse range of ... |
103-239 |
4.93e-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: 144.35 E-value: 4.93e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157254 103 VSEVMLQQTQVATVIDYYTRWMQKW-PKLQDLASASLEEVNQLWSGLGYY-SRGRRLQEGARKVVEELGGHMPRTAETLQ 180
Cdd:pfam00730 1 VSAILSQQTSDKAVNKITERLFEKFfPTPEDLADADEEELRELIRGLGFYrRKAKYLKELARILVEGYGGEVPLDEEELE 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907157254 181 QLLPGVGRYTAGAIASIAF--DQVTGVVDGNVLRVLCRVRAIGADPTSTLVSHHLWNLAQQ 239
Cdd:pfam00730 81 ALLKGVGRWTAEAVLIFALgrPDPLPVVDTHVRRVLKRLGLIKEKPTPKEVERELEELWPP 141
|
|
| PRK13910 |
PRK13910 |
DNA glycosylase MutY; Provisional |
107-288 |
1.22e-31 |
|
DNA glycosylase MutY; Provisional
Pssm-ID: 172427 [Multi-domain] Cd Length: 289 Bit Score: 123.59 E-value: 1.22e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157254 107 MLQQTQVATVID-YYTRWMQKWPKLQDLASASLEEVNQLWSGLGYYSRGRRLQEGARKVVEELGGHMPRTAETLQQlLPG 185
Cdd:PRK13910 1 MSQQTQINTVVErFYSPFLEAFPTLKDLANAPLEEVLLLWRGLGYYSRAKNLKKSAEICVKEHHSQLPNDYQSLLK-LPG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157254 186 VGRYTAGAIASIAFDQVTGVVDGNVLRVLCRVraIGADPTSTlvSHHLWNLAQQLVDPARPGDFNQAAMELGATVCTPqR 265
Cdd:PRK13910 80 IGAYTANAILCFGFREKSACVDANIKRVLLRL--FGLDPNIH--AKDLQIKANDFLNLNESFNHNQALIDLGALICSP-K 154
|
170 180
....*....|....*....|...
gi 1907157254 266 PLCSHCPVQSLCRAYQRVQRGQL 288
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 ... |
335-462 |
7.12e-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: 113.17 E-value: 7.12e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157254 335 PREEYSATCVVEQPGAiggplVLLVQRPDSGLLAGLWEFPSVTLEPSEQhqhkaLLQELQRWCGPLPAIRLQHLGEVIHI 414
Cdd:cd03431 1 VPERYFTVLVLRDGGR-----VLLEKRPEKGLLAGLWEFPLVETEEEEE-----EAEALLGLLAEELLLILEPLGEVKHV 70
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1907157254 415 FSHIKLTYQVYSLALDQAPAsTAPPGARWLTWEEFCNAAVSTAMKKVF 462
Cdd:cd03431 71 FSHFRLHITVYLVELPEAPP-AAPDEGRWVDLEELDEYALPAPMRKLL 117
|
|
| Nth |
COG0177 |
Endonuclease III [Replication, recombination and repair]; |
125-281 |
1.64e-27 |
|
Endonuclease III [Replication, recombination and repair];
Pssm-ID: 439947 [Multi-domain] Cd Length: 198 Bit Score: 109.03 E-value: 1.64e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157254 125 QKWPKLQDLASASLEEVNQLWSGLGYY-SRGRRLQEGARKVVEELGGHMPRTAETLQQLlPGVGRYTAGAIASIAFDQVT 203
Cdd:COG0177 47 ARYPTPEALAAADLEELEELIRPIGLYrNKAKNIIALARILVEKYGGEVPETREELESL-PGVGRKTANVVLNFAFGKPA 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157254 204 GVVDGNVLRVLCRvraIG-ADPTSTL-VSHHLwnlaQQLVDPARPGDFNQAAMELGATVCTPQRPLCSHCPVQSLCRAYQ 281
Cdd:COG0177 126 IAVDTHVHRVSNR---LGlVPGKDPEeVEKDL----MKLIPKEYWGDLHHLLILHGRYICKARKPKCEECPLADLCPYYG 198
|
|
| NUDIX_4 |
pfam14815 |
NUDIX domain; |
356-464 |
2.49e-22 |
|
NUDIX domain;
Pssm-ID: 464330 [Multi-domain] Cd Length: 114 Bit Score: 91.99 E-value: 2.49e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157254 356 VLLVQRPDSGLLAGLWEFPSVTLEPSEqhqhkALLQELQRWCGPLPAIRLQHLGEVIHIFSHIKLTYQVYsLALDQAPAS 435
Cdd:pfam14815 12 VLLRKRPEKGLLGGLWEFPGGKVEPGE-----TLEEALARLEELGIEVEVLEPGTVKHVFTHFRLTLHVY-LVREVEGEE 85
|
90 100
....*....|....*....|....*....
gi 1907157254 436 TAPPGARWLTWEEFCNAAVSTAMKKVFRM 464
Cdd:pfam14815 86 EPQQELRWVTPEELDKYALPAAVRKILEA 114
|
|
| nth |
TIGR01083 |
endonuclease III; This equivalog model identifes nth members of the pfam00730 superfamily ... |
125-268 |
7.64e-20 |
|
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: 87.44 E-value: 7.64e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157254 125 QKWPKLQDLASASLEEVNQLWSGLGYY-SRGRRLQEGARKVVEELGGHMPRTAETLQQLlPGVGRYTAGAIASIAFDQVT 203
Cdd:TIGR01083 54 EVYPTPQALAQAGLEELEEYIKSIGLYrNKAKNIIELCRKLVERYGGEVPEDREELVKL-PGVGRKTANVVLNVAFGIPA 132
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907157254 204 GVVDGNVLRVLCRVR-AIGADPTST------LVSHHLWnlaqqlvdparpGDFNQAAMELGATVCTPQRPLC 268
Cdd:TIGR01083 133 IAVDTHVFRVSNRLGlSKGKDPIKVeedlmkLVPREFW------------VKLHHWLILHGRYTCKARKPLC 192
|
|
| HP0602 |
COG2231 |
3-Methyladenine DNA glycosylase, HhH-GPD/Endo3 superfamily [Replication, recombination and ... |
130-283 |
3.93e-07 |
|
3-Methyladenine DNA glycosylase, HhH-GPD/Endo3 superfamily [Replication, recombination and repair];
Pssm-ID: 441832 [Multi-domain] Cd Length: 220 Bit Score: 51.00 E-value: 3.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157254 130 LQDLASASLEEVNQLWSGLGYYSR-GRRLQEGARKVVEELGGHMPR-----TAETLQQLL--PGVGRYTAGAIASIAFDQ 201
Cdd:COG2231 62 PEALAALDPEELAELIRPSGFYNQkAKRLKNLARWLVERYGGGLEKlkalpTEELREELLslKGIGPETADSILLYAFNR 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157254 202 VTGVVDGNVLRVLCRVrAIGADPTStlvshhlWNLAQQLVDPARPGDFNQA----AM--ELGATVCTPqRPLCSHCPVQS 275
Cdd:COG2231 142 PVFVVDAYTRRIFSRL-GLIEEDAS-------YDELQRLFEENLPPDVALYnefhALivEHGKEYCKK-KPKCEECPLRD 212
|
....*...
gi 1907157254 276 LCRAYQRV 283
Cdd:COG2231 213 LCPYGGQE 220
|
|
| PRK10702 |
PRK10702 |
endonuclease III; Provisional |
150-283 |
6.83e-06 |
|
endonuclease III; Provisional
Pssm-ID: 182661 [Multi-domain] Cd Length: 211 Bit Score: 47.32 E-value: 6.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157254 150 YYSRGRRLQEGARKVVEELGGHMPRTAETLQQLlPGVGRYTAGAIASIAFDQVTGVVDGNVLRVLCRVR-AIGAD----- 223
Cdd:PRK10702 82 YNSKAENVIKTCRILLEQHNGEVPEDRAALEAL-PGVGRKTANVVLNTAFGWPTIAVDTHIFRVCNRTQfAPGKNveqve 160
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907157254 224 -------PTSTLVSHHLWNLAQqlvdparpgdfnqaamelGATVCTPQRPLCSHCPVQSLCRAYQRV 283
Cdd:PRK10702 161 ekllkvvPAEFKVDCHHWLILH------------------GRYTCIARKPRCGSCIIEDLCEYKEKV 209
|
|
| PRK10546 |
PRK10546 |
pyrimidine (deoxy)nucleoside triphosphate diphosphatase; |
344-394 |
3.54e-05 |
|
pyrimidine (deoxy)nucleoside triphosphate diphosphatase;
Pssm-ID: 182536 [Multi-domain] Cd Length: 135 Bit Score: 43.58 E-value: 3.54e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1907157254 344 VVEQPGAIggplvLLVQRPDSGLLAGLWEFPSVTLEPSEQhQHKALLQELQ 394
Cdd:PRK10546 10 IIERDGKI-----LLAQRPAHSDQAGLWEFAGGKVEPGES-QPQALIRELR 54
|
|
| HHH |
pfam00633 |
Helix-hairpin-helix motif; The helix-hairpin-helix DNA-binding motif is found to be duplicated ... |
167-197 |
9.81e-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: 9.81e-05
10 20 30
....*....|....*....|....*....|.
gi 1907157254 167 ELGGHMPRTAETLQQLlPGVGRYTAGAIASI 197
Cdd:pfam00633 1 SLEGLIPASVEELLAL-PGVGPKTAEAILSY 30
|
|
| FES |
smart00525 |
iron-sulpphur binding domain in DNA-(apurinic or apyrimidinic site) lyase (subfamily of ENDO3); ... |
260-280 |
1.19e-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: 39.07 E-value: 1.19e-04
|
| NUDIX_MutT_NudA_like |
cd03425 |
MutT pyrophosphohydrolase; The MutT pyrophosphohydrolase is a prototypical NUDIX hydrolase ... |
356-448 |
3.86e-04 |
|
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: 40.13 E-value: 3.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157254 356 VLLVQRPDSGLLAGLWEFPSVTLEPSEQHQHkALLQELQRWCGpLPAIRLQHLGEVIHIFSHIKLTYQVYS-LALDQAPA 434
Cdd:cd03425 14 VLIAQRPEGKHLAGLWEFPGGKVEPGETPEQ-ALVRELREELG-IEVEVGEPLGTVEHDYPDFHVRLHVYLcTLWSGEPQ 91
|
90
....*....|....
gi 1907157254 435 STAPPGARWLTWEE 448
Cdd:cd03425 92 LLEHQELRWVTPEE 105
|
|
| EndIII_4Fe-2S |
pfam10576 |
Iron-sulfur binding domain of endonuclease III; Escherichia coli endonuclease III (EC 4.2.99. ... |
261-277 |
1.76e-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: 35.83 E-value: 1.76e-03
|
| MutT |
COG0494 |
8-oxo-dGTP pyrophosphatase MutT and related house-cleaning NTP pyrophosphohydrolases, NUDIX ... |
356-461 |
3.51e-03 |
|
8-oxo-dGTP pyrophosphatase MutT and related house-cleaning NTP pyrophosphohydrolases, NUDIX family [Defense mechanisms];
Pssm-ID: 440260 [Multi-domain] Cd Length: 143 Bit Score: 38.09 E-value: 3.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157254 356 VLLVQRPDSGLLAGLWEFPSVTLEPSEQHQHkALLQELQ----------RWCGPLPAIRlqHLGEVIHIFsHIKLTYQVY 425
Cdd:COG0494 27 VLLVRRYRYGVGPGLWEFPGGKIEPGESPEE-AALRELReetgltaedlELLGELPSPG--YTDEKVHVF-LARGLGPGE 102
|
90 100 110
....*....|....*....|....*....|....*.
gi 1907157254 426 SLALDQAPASTAppgARWLTWEEFCNAAVSTAMKKV 461
Cdd:COG0494 103 EVGLDDEDEFIE---VRWVPLDEALALVTAGEIAKT 135
|
|
| PRK10776 |
PRK10776 |
8-oxo-dGTP diphosphatase MutT; |
360-420 |
3.52e-03 |
|
8-oxo-dGTP diphosphatase MutT;
Pssm-ID: 182721 [Multi-domain] Cd Length: 129 Bit Score: 37.66 E-value: 3.52e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907157254 360 QRPDSGLLAGLWEFPSVTLEPSEQHQhKALLQELQRWCGpLPAIRLQHLGEVIHIFS--HIKL 420
Cdd:PRK10776 22 RRAADAHMAGKWEFPGGKIEAGETPE-QALIRELQEEVG-ITVQHATLFEKLEYEFPdrHITL 82
|
|
| |
