|
Name |
Accession |
Description |
Interval |
E-value |
| MutY |
COG1194 |
Adenine-specific DNA glycosylase, acts on AG and A-oxoG pairs [Replication, recombination and ... |
62-471 |
3.75e-154 |
|
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: 443.81 E-value: 3.75e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774509 62 ADVTAFRRNLLSWYDQEKRDLPWRKrvkeeanlDRRAYAVWVSEVMLQQTQVATVIDYYTRWMQKWPTLQDLASASLEEV 141
Cdd:COG1194 1 MDMASFAKRLLAWYDRHGRDLPWRQ--------TRDPYRVWLSEIMLQQTQVATVIPYYERFLERFPTVEALAAAPEDEV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774509 142 NQLWSGLGYYSRGRRLQEGARKVVEELGGHVPRTAETLQQLlPGVGRYTAGAIASIAFDQVTGVVDGNVIRVLCRVRAIG 221
Cdd:COG1194 73 LKLWEGLGYYSRARNLHKAAQQVVEEHGGVFPDTYEELLAL-PGIGPYTAAAIASIAFGEPAPIVDGNVKRVLSRLFAIE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774509 222 ADPTSSFVSHHLWDLAQQLVDPARPGDFNQAAMELGATVCTPQRPLCSHCPVQSLCRAHQRvgqgqlsalpGSPDieeca 301
Cdd:COG1194 152 GPIGSPAAKKELWALAEELLPPERPGDFNQALMDLGATVCTPKKPKCLLCPLQDDCAAFAE----------GRQE----- 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774509 302 lntrqcqlclpstnpwdpnmgvvNFPRKASRRPPREEYSATCVVEQPGAtggplILLVQRPNSGLLAGLWEFPSVtlEPS 381
Cdd:COG1194 217 -----------------------ELPVKKPKKKKPERYGAALVIRDDGR-----VLLEKRPPKGLWGGLWEFPEF--EWE 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774509 382 GQHQHKALLQELQHWsAPLPTTPLQHLGEslpptpqVIHVFSHIKLTYQVYSLALEGQTPASttPPGARWLTWEEFRNAA 461
Cdd:COG1194 267 EAEDPEALERWLREE-LGLEVEWLEPLGT-------VRHVFTHFRLHLTVYLARVPAGPPAE--PDGGRWVPLEELAALP 336
|
410
....*....|
gi 1958774509 462 VSTAMKKVFR 471
Cdd:COG1194 337 LPAPMRKLLK 346
|
|
| mutY |
TIGR01084 |
A/G-specific adenine glycosylase; This equivalog model identifies mutY members of the ... |
66-374 |
5.62e-102 |
|
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: 307.80 E-value: 5.62e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774509 66 AFRRNLLSWYDQEKR-DLPWRkrvkeeanLDRRAYAVWVSEVMLQQTQVATVIDYYTRWMQKWPTLQDLASASLEEVNQL 144
Cdd:TIGR01084 1 QFSEDLLSWYDKYGRkTLPWR--------QNKTPYRVWLSEVMLQQTQVATVIPYFERFLERFPTVQALANAPQDEVLKL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774509 145 WSGLGYYSRGRRLQEGARKVVEELGGHVPRTAETLQQlLPGVGRYTAGAIASIAFDQVTGVVDGNVIRVLCRVRAIGADP 224
Cdd:TIGR01084 73 WEGLGYYARARNLHKAAQEVVEEFGGEFPQDFEDLAA-LPGVGRYTAGAILSFALNKPYPILDGNVKRVLSRLFAVEGWP 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774509 225 TSSFVSHHLWDLAQQLVDPARPGDFNQAAMELGATVCTPQRPLCSHCPVQSLCRAHQrvgQGQLSALPGspdieecalnt 304
Cdd:TIGR01084 152 GKKKVENRLWTLAESLLPKADPEAFNQALMDLGAMICTRKKPKCDLCPLQDFCLAYQ---QGTWEEYPV----------- 217
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774509 305 rqcqlclpstnpwdpnmgvvnfpRKASRRPPREEYSATCVVEQPGAtggplILLVQRPNSGLLAGLWEFP 374
Cdd:TIGR01084 218 -----------------------KKPKAAPPERTTYFLVLQNYDGE-----VLLEQRPEKGLWGGLYCFP 259
|
|
| PRK10880 |
PRK10880 |
adenine DNA glycosylase; |
67-427 |
1.39e-68 |
|
adenine DNA glycosylase;
Pssm-ID: 182805 [Multi-domain] Cd Length: 350 Bit Score: 224.20 E-value: 1.39e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774509 67 FRRNLLSWYDQEKRD-LPWRkrvkeeanLDRRAYAVWVSEVMLQQTQVATVIDYYTRWMQKWPTLQDLASASLEEVNQLW 145
Cdd:PRK10880 6 FSAQVLDWYDKYGRKtLPWQ--------IDKTPYKVWLSEVMLQQTQVATVIPYFERFMARFPTVTDLANAPLDEVLHLW 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774509 146 SGLGYYSRGRRLQEGARKVVEELGGHVPRTAETLQQlLPGVGRYTAGAIASIAFDQVTGVVDGNVIRVLCRVRAIGADPT 225
Cdd:PRK10880 78 TGLGYYARARNLHKAAQQVATLHGGEFPETFEEVAA-LPGVGRSTAGAILSLSLGKHFPILDGNVKRVLARCYAVSGWPG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774509 226 SSFVSHHLWDLAQQlVDPARP-GDFNQAAMELGATVCTPQRPLCSHCPVQSLCRAHqrvGQGQLSALPGSPdieecalnt 304
Cdd:PRK10880 157 KKEVENRLWQLSEQ-VTPAVGvERFNQAMMDLGAMVCTRSKPKCELCPLQNGCIAY---ANHSWALYPGKK--------- 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774509 305 rqcqlclpstnpwdpnmgvvnfPRKAsrRPPREEYsatCVVEQPGATggplILLVQRPNSGLLAGLWEFPSVTLEpsgqh 384
Cdd:PRK10880 224 ----------------------PKQT--LPERTGY---FLLLQHGDE----VWLEQRPPSGLWGGLFCFPQFADE----- 267
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1958774509 385 qhkallQELQHWsaplpttpLQHLGESLPPTPQVI---HVFSHIKL 427
Cdd:PRK10880 268 ------EELRQW--------LAQRGIAADNLTQLTafrHTFSHFHL 299
|
|
| ENDO3c |
cd00056 |
endonuclease III; includes endonuclease III (DNA-(apurinic or apyrimidinic site) lyase), ... |
99-257 |
2.32e-49 |
|
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: 167.03 E-value: 2.32e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774509 99 YAVWVSEVMLQQTQVATVIDYYTRWMQKW-PTLQDLASASLEEVNQLWSGLGYYSRGRRLQEGARKVVEELGGHVPRTAE 177
Cdd:cd00056 1 FEVLVSEILSQQTTDKAVNKAYERLFERYgPTPEALAAADEEELRELIRSLGYRRKAKYLKELARAIVEGFGGLVLDDPD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774509 178 TLQQL--LPGVGRYTAGAIASIAFDQVTGVVDGNVIRVLCRVRAIGADPTssfvSHHLWDLAQQLVDPARPGDFNQAAME 255
Cdd:cd00056 81 AREELlaLPGVGRKTANVVLLFALGPDAFPVDTHVRRVLKRLGLIPKKKT----PEELEELLEELLPKPYWGEANQALMD 156
|
..
gi 1958774509 256 LG 257
Cdd:cd00056 157 LG 158
|
|
| ENDO3c |
smart00478 |
endonuclease III; includes endonuclease III (DNA-(apurinic or apyrimidinic site) lyase), ... |
107-259 |
1.38e-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: 151.26 E-value: 1.38e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774509 107 MLQQTQVATVIDYYTRWMQKWPTLQDLASASLEEVNQLWSGLG-YYSRGRRLQEGARKVVEELGGHVPRTAETLQQLlPG 185
Cdd:smart00478 1 LSQQTTDERVNKATERLFEKFPTPEDLAAADEEELEELIRGLGfYRRKARYLIELARILVEEYGGEVPDDREELLKL-PG 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958774509 186 VGRYTAGAIASIAFDQVTGVVDGNVIRVLCRVRAIGADPTSSfvshHLWDLAQQLVDPARPGDFNQAAMELGAT 259
Cdd:smart00478 80 VGRKTANAVLSFALGKPFIPVDTHVLRIAKRLGLVDKKSTPE----EVEKLLEKLLPEEDWRELNLLLIDFGRT 149
|
|
| HhH-GPD |
pfam00730 |
HhH-GPD superfamily base excision DNA repair protein; This family contains a diverse range of ... |
103-239 |
1.65e-42 |
|
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: 148.20 E-value: 1.65e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774509 103 VSEVMLQQTQVATVIDYYTRWMQKW-PTLQDLASASLEEVNQLWSGLGYY-SRGRRLQEGARKVVEELGGHVPRTAETLQ 180
Cdd:pfam00730 1 VSAILSQQTSDKAVNKITERLFEKFfPTPEDLADADEEELRELIRGLGFYrRKAKYLKELARILVEGYGGEVPLDEEELE 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958774509 181 QLLPGVGRYTAGAIASIAF--DQVTGVVDGNVIRVLCRVRAIGADPTSSFVSHHLWDLAQQ 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 ... |
62-471 |
3.75e-154 |
|
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: 443.81 E-value: 3.75e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774509 62 ADVTAFRRNLLSWYDQEKRDLPWRKrvkeeanlDRRAYAVWVSEVMLQQTQVATVIDYYTRWMQKWPTLQDLASASLEEV 141
Cdd:COG1194 1 MDMASFAKRLLAWYDRHGRDLPWRQ--------TRDPYRVWLSEIMLQQTQVATVIPYYERFLERFPTVEALAAAPEDEV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774509 142 NQLWSGLGYYSRGRRLQEGARKVVEELGGHVPRTAETLQQLlPGVGRYTAGAIASIAFDQVTGVVDGNVIRVLCRVRAIG 221
Cdd:COG1194 73 LKLWEGLGYYSRARNLHKAAQQVVEEHGGVFPDTYEELLAL-PGIGPYTAAAIASIAFGEPAPIVDGNVKRVLSRLFAIE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774509 222 ADPTSSFVSHHLWDLAQQLVDPARPGDFNQAAMELGATVCTPQRPLCSHCPVQSLCRAHQRvgqgqlsalpGSPDieeca 301
Cdd:COG1194 152 GPIGSPAAKKELWALAEELLPPERPGDFNQALMDLGATVCTPKKPKCLLCPLQDDCAAFAE----------GRQE----- 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774509 302 lntrqcqlclpstnpwdpnmgvvNFPRKASRRPPREEYSATCVVEQPGAtggplILLVQRPNSGLLAGLWEFPSVtlEPS 381
Cdd:COG1194 217 -----------------------ELPVKKPKKKKPERYGAALVIRDDGR-----VLLEKRPPKGLWGGLWEFPEF--EWE 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774509 382 GQHQHKALLQELQHWsAPLPTTPLQHLGEslpptpqVIHVFSHIKLTYQVYSLALEGQTPASttPPGARWLTWEEFRNAA 461
Cdd:COG1194 267 EAEDPEALERWLREE-LGLEVEWLEPLGT-------VRHVFTHFRLHLTVYLARVPAGPPAE--PDGGRWVPLEELAALP 336
|
410
....*....|
gi 1958774509 462 VSTAMKKVFR 471
Cdd:COG1194 337 LPAPMRKLLK 346
|
|
| mutY |
TIGR01084 |
A/G-specific adenine glycosylase; This equivalog model identifies mutY members of the ... |
66-374 |
5.62e-102 |
|
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: 307.80 E-value: 5.62e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774509 66 AFRRNLLSWYDQEKR-DLPWRkrvkeeanLDRRAYAVWVSEVMLQQTQVATVIDYYTRWMQKWPTLQDLASASLEEVNQL 144
Cdd:TIGR01084 1 QFSEDLLSWYDKYGRkTLPWR--------QNKTPYRVWLSEVMLQQTQVATVIPYFERFLERFPTVQALANAPQDEVLKL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774509 145 WSGLGYYSRGRRLQEGARKVVEELGGHVPRTAETLQQlLPGVGRYTAGAIASIAFDQVTGVVDGNVIRVLCRVRAIGADP 224
Cdd:TIGR01084 73 WEGLGYYARARNLHKAAQEVVEEFGGEFPQDFEDLAA-LPGVGRYTAGAILSFALNKPYPILDGNVKRVLSRLFAVEGWP 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774509 225 TSSFVSHHLWDLAQQLVDPARPGDFNQAAMELGATVCTPQRPLCSHCPVQSLCRAHQrvgQGQLSALPGspdieecalnt 304
Cdd:TIGR01084 152 GKKKVENRLWTLAESLLPKADPEAFNQALMDLGAMICTRKKPKCDLCPLQDFCLAYQ---QGTWEEYPV----------- 217
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774509 305 rqcqlclpstnpwdpnmgvvnfpRKASRRPPREEYSATCVVEQPGAtggplILLVQRPNSGLLAGLWEFP 374
Cdd:TIGR01084 218 -----------------------KKPKAAPPERTTYFLVLQNYDGE-----VLLEQRPEKGLWGGLYCFP 259
|
|
| PRK10880 |
PRK10880 |
adenine DNA glycosylase; |
67-427 |
1.39e-68 |
|
adenine DNA glycosylase;
Pssm-ID: 182805 [Multi-domain] Cd Length: 350 Bit Score: 224.20 E-value: 1.39e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774509 67 FRRNLLSWYDQEKRD-LPWRkrvkeeanLDRRAYAVWVSEVMLQQTQVATVIDYYTRWMQKWPTLQDLASASLEEVNQLW 145
Cdd:PRK10880 6 FSAQVLDWYDKYGRKtLPWQ--------IDKTPYKVWLSEVMLQQTQVATVIPYFERFMARFPTVTDLANAPLDEVLHLW 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774509 146 SGLGYYSRGRRLQEGARKVVEELGGHVPRTAETLQQlLPGVGRYTAGAIASIAFDQVTGVVDGNVIRVLCRVRAIGADPT 225
Cdd:PRK10880 78 TGLGYYARARNLHKAAQQVATLHGGEFPETFEEVAA-LPGVGRSTAGAILSLSLGKHFPILDGNVKRVLARCYAVSGWPG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774509 226 SSFVSHHLWDLAQQlVDPARP-GDFNQAAMELGATVCTPQRPLCSHCPVQSLCRAHqrvGQGQLSALPGSPdieecalnt 304
Cdd:PRK10880 157 KKEVENRLWQLSEQ-VTPAVGvERFNQAMMDLGAMVCTRSKPKCELCPLQNGCIAY---ANHSWALYPGKK--------- 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774509 305 rqcqlclpstnpwdpnmgvvnfPRKAsrRPPREEYsatCVVEQPGATggplILLVQRPNSGLLAGLWEFPSVTLEpsgqh 384
Cdd:PRK10880 224 ----------------------PKQT--LPERTGY---FLLLQHGDE----VWLEQRPPSGLWGGLFCFPQFADE----- 267
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1958774509 385 qhkallQELQHWsaplpttpLQHLGESLPPTPQVI---HVFSHIKL 427
Cdd:PRK10880 268 ------EELRQW--------LAQRGIAADNLTQLTafrHTFSHFHL 299
|
|
| ENDO3c |
cd00056 |
endonuclease III; includes endonuclease III (DNA-(apurinic or apyrimidinic site) lyase), ... |
99-257 |
2.32e-49 |
|
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: 167.03 E-value: 2.32e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774509 99 YAVWVSEVMLQQTQVATVIDYYTRWMQKW-PTLQDLASASLEEVNQLWSGLGYYSRGRRLQEGARKVVEELGGHVPRTAE 177
Cdd:cd00056 1 FEVLVSEILSQQTTDKAVNKAYERLFERYgPTPEALAAADEEELRELIRSLGYRRKAKYLKELARAIVEGFGGLVLDDPD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774509 178 TLQQL--LPGVGRYTAGAIASIAFDQVTGVVDGNVIRVLCRVRAIGADPTssfvSHHLWDLAQQLVDPARPGDFNQAAME 255
Cdd:cd00056 81 AREELlaLPGVGRKTANVVLLFALGPDAFPVDTHVRRVLKRLGLIPKKKT----PEELEELLEELLPKPYWGEANQALMD 156
|
..
gi 1958774509 256 LG 257
Cdd:cd00056 157 LG 158
|
|
| ENDO3c |
smart00478 |
endonuclease III; includes endonuclease III (DNA-(apurinic or apyrimidinic site) lyase), ... |
107-259 |
1.38e-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: 151.26 E-value: 1.38e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774509 107 MLQQTQVATVIDYYTRWMQKWPTLQDLASASLEEVNQLWSGLG-YYSRGRRLQEGARKVVEELGGHVPRTAETLQQLlPG 185
Cdd:smart00478 1 LSQQTTDERVNKATERLFEKFPTPEDLAAADEEELEELIRGLGfYRRKARYLIELARILVEEYGGEVPDDREELLKL-PG 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958774509 186 VGRYTAGAIASIAFDQVTGVVDGNVIRVLCRVRAIGADPTSSfvshHLWDLAQQLVDPARPGDFNQAAMELGAT 259
Cdd:smart00478 80 VGRKTANAVLSFALGKPFIPVDTHVLRIAKRLGLVDKKSTPE----EVEKLLEKLLPEEDWRELNLLLIDFGRT 149
|
|
| HhH-GPD |
pfam00730 |
HhH-GPD superfamily base excision DNA repair protein; This family contains a diverse range of ... |
103-239 |
1.65e-42 |
|
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: 148.20 E-value: 1.65e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774509 103 VSEVMLQQTQVATVIDYYTRWMQKW-PTLQDLASASLEEVNQLWSGLGYY-SRGRRLQEGARKVVEELGGHVPRTAETLQ 180
Cdd:pfam00730 1 VSAILSQQTSDKAVNKITERLFEKFfPTPEDLADADEEELRELIRGLGFYrRKAKYLKELARILVEGYGGEVPLDEEELE 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958774509 181 QLLPGVGRYTAGAIASIAF--DQVTGVVDGNVIRVLCRVRAIGADPTSSFVSHHLWDLAQQ 239
Cdd:pfam00730 81 ALLKGVGRWTAEAVLIFALgrPDPLPVVDTHVRRVLKRLGLIKEKPTPKEVERELEELWPP 141
|
|
| PRK13910 |
PRK13910 |
DNA glycosylase MutY; Provisional |
107-277 |
9.18e-32 |
|
DNA glycosylase MutY; Provisional
Pssm-ID: 172427 [Multi-domain] Cd Length: 289 Bit Score: 123.98 E-value: 9.18e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774509 107 MLQQTQVATVID-YYTRWMQKWPTLQDLASASLEEVNQLWSGLGYYSRGRRLQEGARKVVEELGGHVPRTAETLQQlLPG 185
Cdd:PRK13910 1 MSQQTQINTVVErFYSPFLEAFPTLKDLANAPLEEVLLLWRGLGYYSRAKNLKKSAEICVKEHHSQLPNDYQSLLK-LPG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774509 186 VGRYTAGAIASIAFDQVTGVVDGNVIRVLCRVraIGADPtsSFVSHHLWDLAQQLVDPARPGDFNQAAMELGATVCTPqR 265
Cdd:PRK13910 80 IGAYTANAILCFGFREKSACVDANIKRVLLRL--FGLDP--NIHAKDLQIKANDFLNLNESFNHNQALIDLGALICSP-K 154
|
170
....*....|..
gi 1958774509 266 PLCSHCPVQSLC 277
Cdd:PRK13910 155 PKCAICPLNPYC 166
|
|
| Nth |
COG0177 |
Endonuclease III [Replication, recombination and repair]; |
125-278 |
1.19e-28 |
|
Endonuclease III [Replication, recombination and repair];
Pssm-ID: 439947 [Multi-domain] Cd Length: 198 Bit Score: 112.50 E-value: 1.19e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774509 125 QKWPTLQDLASASLEEVNQLWSGLGYY-SRGRRLQEGARKVVEELGGHVPRTAETLQQLlPGVGRYTAGAIASIAFDQVT 203
Cdd:COG0177 47 ARYPTPEALAAADLEELEELIRPIGLYrNKAKNIIALARILVEKYGGEVPETREELESL-PGVGRKTANVVLNFAFGKPA 125
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958774509 204 GVVDGNVIRVLCRVR-AIGADPTSsfVSHHLwdlaQQLVDPARPGDFNQAAMELGATVCTPQRPLCSHCPVQSLCR 278
Cdd:COG0177 126 IAVDTHVHRVSNRLGlVPGKDPEE--VEKDL----MKLIPKEYWGDLHHLLILHGRYICKARKPKCEECPLADLCP 195
|
|
| NUDIX_DNA_Glycosylase_C-MutY |
cd03431 |
C-terminal domain of DNA glycosylase; DNA glycosylase (MutY in bacteria and hMYH in humans) is ... |
335-470 |
7.08e-26 |
|
C-terminal domain of DNA glycosylase; DNA glycosylase (MutY in bacteria and hMYH in humans) is responsible for repairing misread A*oxoG residues to C*G by removing the inappropriately paired adenine base from the DNA backbone. It belongs to the NUDIX hydrolase superfamily and is important for the repair of various genotoxic lesions. Enzymes belonging to this superfamily requires a divalent cation, such as Mg2+ or Mn2+ for their activity. They are also recognized by a highly conserved 23-residue NUDIX motif (GX5EX7REUXEEXGU, where U = I, L or V). However, DNA glycosylase does not seem to contain this signature motif. DNA glycosylase consists of 2 domains: the N-terminal domain contains the catalytic properties of the enzyme and the C-terminal domain affects substrate (oxoG) binding and enzymatic turnover. The C-terminal domain is highly similar to MutT, based on secondary structure and topology, despite low sequence identity. MutT sanitizes the nucleotide precursor pool by hydrolyzing oxo-dGTP to oxo-dGMO and inorganic pyrophosphate. The similarity strongly suggests that the two proteins share a common evolutionary origin.
Pssm-ID: 467537 [Multi-domain] Cd Length: 118 Bit Score: 102.00 E-value: 7.08e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774509 335 PREEYSATCVVEQPGAtggplILLVQRPNSGLLAGLWEFPSVTLEPSGQhqhkaLLQELQHWSAPLPTTPLQHLGEslpp 414
Cdd:cd03431 1 VPERYFTVLVLRDGGR-----VLLEKRPEKGLLAGLWEFPLVETEEEEE-----EAEALLGLLAEELLLILEPLGE---- 66
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1958774509 415 tpqVIHVFSHIKLTYQVYSLALEGQTPASttPPGARWLTWEEFRNAAVSTAMKKVF 470
Cdd:cd03431 67 ---VKHVFSHFRLHITVYLVELPEAPPAA--PDEGRWVDLEELDEYALPAPMRKLL 117
|
|
| nth |
TIGR01083 |
endonuclease III; This equivalog model identifes nth members of the pfam00730 superfamily ... |
125-268 |
1.19e-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: 89.75 E-value: 1.19e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774509 125 QKWPTLQDLASASLEEVNQLWSGLGYY-SRGRRLQEGARKVVEELGGHVPRTAETLQQLlPGVGRYTAGAIASIAFDQVT 203
Cdd:TIGR01083 54 EVYPTPQALAQAGLEELEEYIKSIGLYrNKAKNIIELCRKLVERYGGEVPEDREELVKL-PGVGRKTANVVLNVAFGIPA 132
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958774509 204 GVVDGNVIRVLCRVR-AIGADPTSsfVSHHLwdlaQQLVDPARPGDFNQAAMELGATVCTPQRPLC 268
Cdd:TIGR01083 133 IAVDTHVFRVSNRLGlSKGKDPIK--VEEDL----MKLVPREFWVKLHHWLILHGRYTCKARKPLC 192
|
|
| NUDIX_4 |
pfam14815 |
NUDIX domain; |
356-471 |
6.06e-19 |
|
NUDIX domain;
Pssm-ID: 464330 [Multi-domain] Cd Length: 114 Bit Score: 82.36 E-value: 6.06e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774509 356 ILLVQRPNSGLLAGLWEFPSVTLEPSGQHQHKALLQELQHwsapLPTTPLQHLgeslpptpQVIHVFSHIKLTYQVYSLA 435
Cdd:pfam14815 12 VLLRKRPEKGLLGGLWEFPGGKVEPGETLEEALARLEELG----IEVEVLEPG--------TVKHVFTHFRLTLHVYLVR 79
|
90 100 110
....*....|....*....|....*....|....*.
gi 1958774509 436 LEGQTPASttPPGARWLTWEEFRNAAVSTAMKKVFR 471
Cdd:pfam14815 80 EVEGEEEP--QQELRWVTPEELDKYALPAAVRKILE 113
|
|
| HP0602 |
COG2231 |
3-Methyladenine DNA glycosylase, HhH-GPD/Endo3 superfamily [Replication, recombination and ... |
129-283 |
3.18e-08 |
|
3-Methyladenine DNA glycosylase, HhH-GPD/Endo3 superfamily [Replication, recombination and repair];
Pssm-ID: 441832 [Multi-domain] Cd Length: 220 Bit Score: 54.08 E-value: 3.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774509 129 TLQDLASASLEEVNQLWSGLGYYSR-GRRLQEGARKVVEELGGHVPR-----TAETLQQLL--PGVGRYTAGAIASIAFD 200
Cdd:COG2231 61 DPEALAALDPEELAELIRPSGFYNQkAKRLKNLARWLVERYGGGLEKlkalpTEELREELLslKGIGPETADSILLYAFN 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774509 201 QVTGVVDGNVIRVLcrVRAIGADPTSSFvshhlwDLAQQLVDPARPGDFNQA----AM--ELGATVCTPqRPLCSHCPVQ 274
Cdd:COG2231 141 RPVFVVDAYTRRIF--SRLGLIEEDASY------DELQRLFEENLPPDVALYnefhALivEHGKEYCKK-KPKCEECPLR 211
|
....*....
gi 1958774509 275 SLCRAHQRV 283
Cdd:COG2231 212 DLCPYGGQE 220
|
|
| PRK10702 |
PRK10702 |
endonuclease III; Provisional |
150-283 |
1.40e-06 |
|
endonuclease III; Provisional
Pssm-ID: 182661 [Multi-domain] Cd Length: 211 Bit Score: 49.25 E-value: 1.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774509 150 YYSRGRRLQEGARKVVEELGGHVPRTAETLQQLlPGVGRYTAGAIASIAFDQVTGVVDGNVIRVLCRvraigadptSSFV 229
Cdd:PRK10702 82 YNSKAENVIKTCRILLEQHNGEVPEDRAALEAL-PGVGRKTANVVLNTAFGWPTIAVDTHIFRVCNR---------TQFA 151
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1958774509 230 SHHLWDLAQQLVDPARPGDF----NQAAMELGATVCTPQRPLCSHCPVQSLCRAHQRV 283
Cdd:PRK10702 152 PGKNVEQVEEKLLKVVPAEFkvdcHHWLILHGRYTCIARKPRCGSCIIEDLCEYKEKV 209
|
|
| PRK10546 |
PRK10546 |
pyrimidine (deoxy)nucleoside triphosphate diphosphatase; |
344-394 |
3.40e-05 |
|
pyrimidine (deoxy)nucleoside triphosphate diphosphatase;
Pssm-ID: 182536 [Multi-domain] Cd Length: 135 Bit Score: 43.58 E-value: 3.40e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1958774509 344 VVEQPGAtggplILLVQRPNSGLLAGLWEFPSVTLEPsGQHQHKALLQELQ 394
Cdd:PRK10546 10 IIERDGK-----ILLAQRPAHSDQAGLWEFAGGKVEP-GESQPQALIRELR 54
|
|
| HHH |
pfam00633 |
Helix-hairpin-helix motif; The helix-hairpin-helix DNA-binding motif is found to be duplicated ... |
167-197 |
7.79e-05 |
|
Helix-hairpin-helix motif; The helix-hairpin-helix DNA-binding motif is found to be duplicated in the central domain of RuvA. The HhH domain of DisA, a bacterial checkpoint control protein, is a DNA-binding domain.
Pssm-ID: 425789 [Multi-domain] Cd Length: 30 Bit Score: 39.71 E-value: 7.79e-05
10 20 30
....*....|....*....|....*....|.
gi 1958774509 167 ELGGHVPRTAETLQQLlPGVGRYTAGAIASI 197
Cdd:pfam00633 1 SLEGLIPASVEELLAL-PGVGPKTAEAILSY 30
|
|
| FES |
smart00525 |
iron-sulpphur binding domain in DNA-(apurinic or apyrimidinic site) lyase (subfamily of ENDO3); ... |
260-279 |
9.90e-04 |
|
iron-sulpphur binding domain in DNA-(apurinic or apyrimidinic site) lyase (subfamily of ENDO3);
Pssm-ID: 197771 [Multi-domain] Cd Length: 21 Bit Score: 36.37 E-value: 9.90e-04
|
| EndIII_4Fe-2S |
pfam10576 |
Iron-sulfur binding domain of endonuclease III; Escherichia coli endonuclease III (EC 4.2.99. ... |
261-277 |
1.97e-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: 1.97e-03
|
| NUDIX_MutT_NudA_like |
cd03425 |
MutT pyrophosphohydrolase; The MutT pyrophosphohydrolase is a prototypical NUDIX hydrolase ... |
356-374 |
7.35e-03 |
|
MutT pyrophosphohydrolase; The MutT pyrophosphohydrolase is a prototypical NUDIX hydrolase that catalyzes the hydrolysis of nucleoside and deoxynucleoside triphosphates (NTPs and dNTPs) by substitution at a beta-phosphorus to yield a nucleotide monophosphate (NMP) and inorganic pyrophosphate (PPi). This enzyme requires two divalent cations for activity; one coordinates the phosphoryl groups of the NTP/dNTP substrate, and the other coordinates to the enzyme. It also contains the NUDIX motif, a highly conserved 23-residue block (GX5EX7REUXEEXGU, where U = I, L or V), that functions as metal binding and catalytic site. MutT pyrophosphohydrolase is important in preventing errors in DNA replication by hydrolyzing mutagenic nucleotides such as 8-oxo-dGTP (a product of oxidative damage), which can mispair with template adenine during DNA replication, to guanine nucleotides.
Pssm-ID: 467531 [Multi-domain] Cd Length: 123 Bit Score: 36.66 E-value: 7.35e-03
|
| |
