|
Name |
Accession |
Description |
Interval |
E-value |
| PRK10880 |
PRK10880 |
adenine DNA glycosylase; |
18-371 |
0e+00 |
|
adenine DNA glycosylase;
Pssm-ID: 182805 [Multi-domain] Cd Length: 350 Bit Score: 559.71 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737521563 18 PFAKGVLAWYQQYGRKHLPWQQNKTLYGVWLSEVMLQQTQVATVIPYFERFVQRFPTIVNLANAPIDEVLHLWTGLGYYA 97
Cdd:PRK10880 5 QFSAQVLDWYDKYGRKTLPWQIDKTPYKVWLSEVMLQQTQVATVIPYFERFMARFPTVTDLANAPLDEVLHLWTGLGYYA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737521563 98 RARNLHKAAQQIRDEFGGQFPTDFTDVFALSGVGRSTAGAVLSSVLDAPYPILDGNVKRVLSRYFAVEGWSGEKAVENKL 177
Cdd:PRK10880 85 RARNLHKAAQQVATLHGGEFPETFEEVAALPGVGRSTAGAILSLSLGKHFPILDGNVKRVLARCYAVSGWPGKKEVENRL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737521563 178 WDLTARVTPTSQVADFNQAMMDLGAMICTRSKPKCSLCPLEKGCQANAQQAWADFPAKKPKKVLPERQSYFLILKQGTKV 257
Cdd:PRK10880 165 WQLSEQVTPAVGVERFNQAMMDLGAMVCTRSKPKCELCPLQNGCIAYANHSWALYPGKKPKQTLPERTGYFLLLQHGDEV 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737521563 258 LLEKREAKGLWGGLYVFPQFEHLDDLKRSVSGRNVQ---FTQLIAFRHTFSHFHLDIYPILAELSLQRNAeilplgVAEN 334
Cdd:PRK10880 245 WLEQRPPSGLWGGLFCFPQFADEEELRQWLAQRGIAadnLTQLTAFRHTFSHFHLDIVPMWLPVSSFTGC------MDEG 318
|
330 340 350
....*....|....*....|....*....|....*..
gi 737521563 335 QGnyhlrvsstadYWYDLTQPSEVGLATPIKRILDEL 371
Cdd:PRK10880 319 NG-----------LWYNLAQPPSVGLAAPVERLLQQL 344
|
|
| MutY |
COG1194 |
Adenine-specific DNA glycosylase, acts on AG and A-oxoG pairs [Replication, recombination and ... |
17-371 |
0e+00 |
|
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: 523.55 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737521563 17 APFAKGVLAWYQQYGRkHLPWQQNKTLYGVWLSEVMLQQTQVATVIPYFERFVQRFPTIVNLANAPIDEVLHLWTGLGYY 96
Cdd:COG1194 4 ASFAKRLLAWYDRHGR-DLPWRQTRDPYRVWLSEIMLQQTQVATVIPYYERFLERFPTVEALAAAPEDEVLKLWEGLGYY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737521563 97 ARARNLHKAAQQIRDEFGGQFPTDFTDVFALSGVGRSTAGAVLSSVLDAPYPILDGNVKRVLSRYFAVEGWSGEKAVENK 176
Cdd:COG1194 83 SRARNLHKAAQQVVEEHGGVFPDTYEELLALPGIGPYTAAAIASIAFGEPAPIVDGNVKRVLSRLFAIEGPIGSPAAKKE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737521563 177 LWDLTARVTPTSQVADFNQAMMDLGAMICTRSKPKCSLCPLEKGCQANAQQAWADFPAKKPKKVLPERQSYFLILKQGTK 256
Cdd:COG1194 163 LWALAEELLPPERPGDFNQALMDLGATVCTPKKPKCLLCPLQDDCAAFAEGRQEELPVKKPKKKKPERYGAALVIRDDGR 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737521563 257 VLLEKREAKGLWGGLYVFPQFEHLDD---------LKRSVSGRNVQFTQLIAFRHTFSHFHLDIYPILAELSLQRNAEil 327
Cdd:COG1194 243 VLLEKRPPKGLWGGLWEFPEFEWEEAedpealerwLREELGLEVEWLEPLGTVRHVFTHFRLHLTVYLARVPAGPPAE-- 320
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 737521563 328 plgvaenqgnyhlrvsSTADYWYDLTQPSEVGLATPIKRILDEL 371
Cdd:COG1194 321 ----------------PDGGRWVPLEELAALPLPAPMRKLLKAL 348
|
|
| mutY |
TIGR01084 |
A/G-specific adenine glycosylase; This equivalog model identifies mutY members of the ... |
18-285 |
5.52e-164 |
|
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: 459.95 E-value: 5.52e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737521563 18 PFAKGVLAWYQQYGRKHLPWQQNKTLYGVWLSEVMLQQTQVATVIPYFERFVQRFPTIVNLANAPIDEVLHLWTGLGYYA 97
Cdd:TIGR01084 1 QFSEDLLSWYDKYGRKTLPWRQNKTPYRVWLSEVMLQQTQVATVIPYFERFLERFPTVQALANAPQDEVLKLWEGLGYYA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737521563 98 RARNLHKAAQQIRDEFGGQFPTDFTDVFALSGVGRSTAGAVLSSVLDAPYPILDGNVKRVLSRYFAVEGWSGEKAVENKL 177
Cdd:TIGR01084 81 RARNLHKAAQEVVEEFGGEFPQDFEDLAALPGVGRYTAGAILSFALNKPYPILDGNVKRVLSRLFAVEGWPGKKKVENRL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737521563 178 WDLTARVTPTSQVADFNQAMMDLGAMICTRSKPKCSLCPLEKGCQANAQQAWADFPAKKPKKVLPERQSYFLILKQGT-K 256
Cdd:TIGR01084 161 WTLAESLLPKADPEAFNQALMDLGAMICTRKKPKCDLCPLQDFCLAYQQGTWEEYPVKKPKAAPPERTTYFLVLQNYDgE 240
|
250 260
....*....|....*....|....*....
gi 737521563 257 VLLEKREAKGLWGGLYVFPQFEHLDDLKR 285
Cdd:TIGR01084 241 VLLEQRPEKGLWGGLYCFPQFEDEDSLAF 269
|
|
| ENDO3c |
cd00056 |
endonuclease III; includes endonuclease III (DNA-(apurinic or apyrimidinic site) lyase), ... |
44-201 |
1.58e-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: 163.95 E-value: 1.58e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737521563 44 YGVWLSEVMLQQTQVATVIPYFERFVQRF-PTIVNLANAPIDEVLHLWTGLGYYARARNLHKAAQQIRDEFGG---QFPT 119
Cdd:cd00056 1 FEVLVSEILSQQTTDKAVNKAYERLFERYgPTPEALAAADEEELRELIRSLGYRRKAKYLKELARAIVEGFGGlvlDDPD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737521563 120 DFTDVFALSGVGRSTAGAVLSSVLDAPYPILDGNVKRVLSRYfaveGWSGEKAVENKLWDLTARVTPTSQVADFNQAMMD 199
Cdd:cd00056 81 AREELLALPGVGRKTANVVLLFALGPDAFPVDTHVRRVLKRL----GLIPKKKTPEELEELLEELLPKPYWGEANQALMD 156
|
..
gi 737521563 200 LG 201
Cdd:cd00056 157 LG 158
|
|
| ENDO3c |
smart00478 |
endonuclease III; includes endonuclease III (DNA-(apurinic or apyrimidinic site) lyase), ... |
52-203 |
1.29e-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: 145.87 E-value: 1.29e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737521563 52 MLQQTQVATVIPYFERFVQRFPTIVNLANAPIDEVLHLWTGLG-YYARARNLHKAAQQIRDEFGGQFPTDFTDVFALSGV 130
Cdd:smart00478 1 LSQQTTDERVNKATERLFEKFPTPEDLAAADEEELEELIRGLGfYRRKARYLIELARILVEEYGGEVPDDREELLKLPGV 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 737521563 131 GRSTAGAVLSSVLDAPYPILDGNVKRVLSRYFavegWSGEKAVENKLWDLTARVTPTSQVADFNQAMMDLGAM 203
Cdd:smart00478 81 GRKTANAVLSFALGKPFIPVDTHVLRIAKRLG----LVDKKSTPEEVEKLLEKLLPEEDWRELNLLLIDFGRT 149
|
|
| HhH-GPD |
pfam00730 |
HhH-GPD superfamily base excision DNA repair protein; This family contains a diverse range of ... |
48-183 |
3.19e-37 |
|
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: 131.25 E-value: 3.19e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737521563 48 LSEVMLQQTQVATVIPYFERFVQR-FPTIVNLANAPIDEVLHLWTGLGYYAR-ARNLHKAAQQIRDEFGGQFPTDFT-DV 124
Cdd:pfam00730 1 VSAILSQQTSDKAVNKITERLFEKfFPTPEDLADADEEELRELIRGLGFYRRkAKYLKELARILVEGYGGEVPLDEEeLE 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 737521563 125 FALSGVGRSTAGAVLSSVLDA--PYPILDGNVKRVLSRYFAVEGWSGEKAVENKLWDLTAR 183
Cdd:pfam00730 81 ALLKGVGRWTAEAVLIFALGRpdPLPVVDTHVRRVLKRLGLIKEKPTPKEVERELEELWPP 141
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK10880 |
PRK10880 |
adenine DNA glycosylase; |
18-371 |
0e+00 |
|
adenine DNA glycosylase;
Pssm-ID: 182805 [Multi-domain] Cd Length: 350 Bit Score: 559.71 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737521563 18 PFAKGVLAWYQQYGRKHLPWQQNKTLYGVWLSEVMLQQTQVATVIPYFERFVQRFPTIVNLANAPIDEVLHLWTGLGYYA 97
Cdd:PRK10880 5 QFSAQVLDWYDKYGRKTLPWQIDKTPYKVWLSEVMLQQTQVATVIPYFERFMARFPTVTDLANAPLDEVLHLWTGLGYYA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737521563 98 RARNLHKAAQQIRDEFGGQFPTDFTDVFALSGVGRSTAGAVLSSVLDAPYPILDGNVKRVLSRYFAVEGWSGEKAVENKL 177
Cdd:PRK10880 85 RARNLHKAAQQVATLHGGEFPETFEEVAALPGVGRSTAGAILSLSLGKHFPILDGNVKRVLARCYAVSGWPGKKEVENRL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737521563 178 WDLTARVTPTSQVADFNQAMMDLGAMICTRSKPKCSLCPLEKGCQANAQQAWADFPAKKPKKVLPERQSYFLILKQGTKV 257
Cdd:PRK10880 165 WQLSEQVTPAVGVERFNQAMMDLGAMVCTRSKPKCELCPLQNGCIAYANHSWALYPGKKPKQTLPERTGYFLLLQHGDEV 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737521563 258 LLEKREAKGLWGGLYVFPQFEHLDDLKRSVSGRNVQ---FTQLIAFRHTFSHFHLDIYPILAELSLQRNAeilplgVAEN 334
Cdd:PRK10880 245 WLEQRPPSGLWGGLFCFPQFADEEELRQWLAQRGIAadnLTQLTAFRHTFSHFHLDIVPMWLPVSSFTGC------MDEG 318
|
330 340 350
....*....|....*....|....*....|....*..
gi 737521563 335 QGnyhlrvsstadYWYDLTQPSEVGLATPIKRILDEL 371
Cdd:PRK10880 319 NG-----------LWYNLAQPPSVGLAAPVERLLQQL 344
|
|
| MutY |
COG1194 |
Adenine-specific DNA glycosylase, acts on AG and A-oxoG pairs [Replication, recombination and ... |
17-371 |
0e+00 |
|
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: 523.55 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737521563 17 APFAKGVLAWYQQYGRkHLPWQQNKTLYGVWLSEVMLQQTQVATVIPYFERFVQRFPTIVNLANAPIDEVLHLWTGLGYY 96
Cdd:COG1194 4 ASFAKRLLAWYDRHGR-DLPWRQTRDPYRVWLSEIMLQQTQVATVIPYYERFLERFPTVEALAAAPEDEVLKLWEGLGYY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737521563 97 ARARNLHKAAQQIRDEFGGQFPTDFTDVFALSGVGRSTAGAVLSSVLDAPYPILDGNVKRVLSRYFAVEGWSGEKAVENK 176
Cdd:COG1194 83 SRARNLHKAAQQVVEEHGGVFPDTYEELLALPGIGPYTAAAIASIAFGEPAPIVDGNVKRVLSRLFAIEGPIGSPAAKKE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737521563 177 LWDLTARVTPTSQVADFNQAMMDLGAMICTRSKPKCSLCPLEKGCQANAQQAWADFPAKKPKKVLPERQSYFLILKQGTK 256
Cdd:COG1194 163 LWALAEELLPPERPGDFNQALMDLGATVCTPKKPKCLLCPLQDDCAAFAEGRQEELPVKKPKKKKPERYGAALVIRDDGR 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737521563 257 VLLEKREAKGLWGGLYVFPQFEHLDD---------LKRSVSGRNVQFTQLIAFRHTFSHFHLDIYPILAELSLQRNAEil 327
Cdd:COG1194 243 VLLEKRPPKGLWGGLWEFPEFEWEEAedpealerwLREELGLEVEWLEPLGTVRHVFTHFRLHLTVYLARVPAGPPAE-- 320
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 737521563 328 plgvaenqgnyhlrvsSTADYWYDLTQPSEVGLATPIKRILDEL 371
Cdd:COG1194 321 ----------------PDGGRWVPLEELAALPLPAPMRKLLKAL 348
|
|
| mutY |
TIGR01084 |
A/G-specific adenine glycosylase; This equivalog model identifies mutY members of the ... |
18-285 |
5.52e-164 |
|
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: 459.95 E-value: 5.52e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737521563 18 PFAKGVLAWYQQYGRKHLPWQQNKTLYGVWLSEVMLQQTQVATVIPYFERFVQRFPTIVNLANAPIDEVLHLWTGLGYYA 97
Cdd:TIGR01084 1 QFSEDLLSWYDKYGRKTLPWRQNKTPYRVWLSEVMLQQTQVATVIPYFERFLERFPTVQALANAPQDEVLKLWEGLGYYA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737521563 98 RARNLHKAAQQIRDEFGGQFPTDFTDVFALSGVGRSTAGAVLSSVLDAPYPILDGNVKRVLSRYFAVEGWSGEKAVENKL 177
Cdd:TIGR01084 81 RARNLHKAAQEVVEEFGGEFPQDFEDLAALPGVGRYTAGAILSFALNKPYPILDGNVKRVLSRLFAVEGWPGKKKVENRL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737521563 178 WDLTARVTPTSQVADFNQAMMDLGAMICTRSKPKCSLCPLEKGCQANAQQAWADFPAKKPKKVLPERQSYFLILKQGT-K 256
Cdd:TIGR01084 161 WTLAESLLPKADPEAFNQALMDLGAMICTRKKPKCDLCPLQDFCLAYQQGTWEEYPVKKPKAAPPERTTYFLVLQNYDgE 240
|
250 260
....*....|....*....|....*....
gi 737521563 257 VLLEKREAKGLWGGLYVFPQFEHLDDLKR 285
Cdd:TIGR01084 241 VLLEQRPEKGLWGGLYCFPQFEDEDSLAF 269
|
|
| ENDO3c |
cd00056 |
endonuclease III; includes endonuclease III (DNA-(apurinic or apyrimidinic site) lyase), ... |
44-201 |
1.58e-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: 163.95 E-value: 1.58e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737521563 44 YGVWLSEVMLQQTQVATVIPYFERFVQRF-PTIVNLANAPIDEVLHLWTGLGYYARARNLHKAAQQIRDEFGG---QFPT 119
Cdd:cd00056 1 FEVLVSEILSQQTTDKAVNKAYERLFERYgPTPEALAAADEEELRELIRSLGYRRKAKYLKELARAIVEGFGGlvlDDPD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737521563 120 DFTDVFALSGVGRSTAGAVLSSVLDAPYPILDGNVKRVLSRYfaveGWSGEKAVENKLWDLTARVTPTSQVADFNQAMMD 199
Cdd:cd00056 81 AREELLALPGVGRKTANVVLLFALGPDAFPVDTHVRRVLKRL----GLIPKKKTPEELEELLEELLPKPYWGEANQALMD 156
|
..
gi 737521563 200 LG 201
Cdd:cd00056 157 LG 158
|
|
| ENDO3c |
smart00478 |
endonuclease III; includes endonuclease III (DNA-(apurinic or apyrimidinic site) lyase), ... |
52-203 |
1.29e-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: 145.87 E-value: 1.29e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737521563 52 MLQQTQVATVIPYFERFVQRFPTIVNLANAPIDEVLHLWTGLG-YYARARNLHKAAQQIRDEFGGQFPTDFTDVFALSGV 130
Cdd:smart00478 1 LSQQTTDERVNKATERLFEKFPTPEDLAAADEEELEELIRGLGfYRRKARYLIELARILVEEYGGEVPDDREELLKLPGV 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 737521563 131 GRSTAGAVLSSVLDAPYPILDGNVKRVLSRYFavegWSGEKAVENKLWDLTARVTPTSQVADFNQAMMDLGAM 203
Cdd:smart00478 81 GRKTANAVLSFALGKPFIPVDTHVLRIAKRLG----LVDKKSTPEEVEKLLEKLLPEEDWRELNLLLIDFGRT 149
|
|
| PRK13910 |
PRK13910 |
DNA glycosylase MutY; Provisional |
52-312 |
3.28e-38 |
|
DNA glycosylase MutY; Provisional
Pssm-ID: 172427 [Multi-domain] Cd Length: 289 Bit Score: 138.62 E-value: 3.28e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737521563 52 MLQQTQVATVIP-YFERFVQRFPTIVNLANAPIDEVLHLWTGLGYYARARNLHKAAQQIRDEFGGQFPTDFTDVFALSGV 130
Cdd:PRK13910 1 MSQQTQINTVVErFYSPFLEAFPTLKDLANAPLEEVLLLWRGLGYYSRAKNLKKSAEICVKEHHSQLPNDYQSLLKLPGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737521563 131 GRSTAGAVLSSVLDAPYPILDGNVKRVLSRYFAVEGWSGEKAVENKLWDLTArvtpTSQVADFNQAMMDLGAMICTrSKP 210
Cdd:PRK13910 81 GAYTANAILCFGFREKSACVDANIKRVLLRLFGLDPNIHAKDLQIKANDFLN----LNESFNHNQALIDLGALICS-PKP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737521563 211 KCSLCPLEKGCQANaqqawaDFPAK---KPKKVLPERQSYFLILKQGTKVLLEKREAKgLWGGLYVFPQFEHLDDLKrsv 287
Cdd:PRK13910 156 KCAICPLNPYCLGK------NNPEKhtlKKKQEIVQEERYLGVVIQNNQIALEKIEQK-LYLGMHHFPNLKENLEYK--- 225
|
250 260
....*....|....*....|....*
gi 737521563 288 sgrnVQFTQLIAFRHTFSHFHLDIY 312
Cdd:PRK13910 226 ----LPFLGAIKHSHTKFKLNLNLY 246
|
|
| HhH-GPD |
pfam00730 |
HhH-GPD superfamily base excision DNA repair protein; This family contains a diverse range of ... |
48-183 |
3.19e-37 |
|
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: 131.25 E-value: 3.19e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737521563 48 LSEVMLQQTQVATVIPYFERFVQR-FPTIVNLANAPIDEVLHLWTGLGYYAR-ARNLHKAAQQIRDEFGGQFPTDFT-DV 124
Cdd:pfam00730 1 VSAILSQQTSDKAVNKITERLFEKfFPTPEDLADADEEELRELIRGLGFYRRkAKYLKELARILVEGYGGEVPLDEEeLE 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 737521563 125 FALSGVGRSTAGAVLSSVLDA--PYPILDGNVKRVLSRYFAVEGWSGEKAVENKLWDLTAR 183
Cdd:pfam00730 81 ALLKGVGRWTAEAVLIFALGRpdPLPVVDTHVRRVLKRLGLIKEKPTPKEVERELEELWPP 141
|
|
| Nth |
COG0177 |
Endonuclease III [Replication, recombination and repair]; |
51-221 |
6.62e-29 |
|
Endonuclease III [Replication, recombination and repair];
Pssm-ID: 439947 [Multi-domain] Cd Length: 198 Bit Score: 111.34 E-value: 6.62e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737521563 51 VML-QQTQVATVIPYFERFVQRFPTIVNLANAPIDEVLHLWTGLGYY-ARARNLHKAAQQIRDEFGGQFPTDFTDVFALS 128
Cdd:COG0177 27 TILsAQTTDERVNKATPRLFARYPTPEALAAADLEELEELIRPIGLYrNKAKNIIALARILVEKYGGEVPETREELESLP 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737521563 129 GVGRSTAGAVLSSVLDAPYPILDGNVKRVLSRYfaveGWSGEK---AVENKLwdltARVTPTSQVADFNQAMMDLGAMIC 205
Cdd:COG0177 107 GVGRKTANVVLNFAFGKPAIAVDTHVHRVSNRL----GLVPGKdpeEVEKDL----MKLIPKEYWGDLHHLLILHGRYIC 178
|
170
....*....|....*.
gi 737521563 206 TRSKPKCSLCPLEKGC 221
Cdd:COG0177 179 KARKPKCEECPLADLC 194
|
|
| NUDIX_DNA_Glycosylase_C-MutY |
cd03431 |
C-terminal domain of DNA glycosylase; DNA glycosylase (MutY in bacteria and hMYH in humans) is ... |
242-369 |
2.66e-24 |
|
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: 96.22 E-value: 2.66e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737521563 242 PERQSYFLILKQGTKVLLEKREAKGLWGGLYVFPQFEHLDDL-------KRSVSGRNVQFTQLIAFRHTFSHFHLDIYPI 314
Cdd:cd03431 2 PERYFTVLVLRDGGRVLLEKRPEKGLLAGLWEFPLVETEEEEeeaeallGLLAEELLLILEPLGEVKHVFSHFRLHITVY 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 737521563 315 LAELSLQRNAEILPLgvaenqgnyhlrvsstadYWYDLTQPSEVGLATPIKRILD 369
Cdd:cd03431 82 LVELPEAPPAAPDEG------------------RWVDLEELDEYALPAPMRKLLE 118
|
|
| NUDIX_4 |
pfam14815 |
NUDIX domain; |
247-370 |
5.85e-17 |
|
NUDIX domain;
Pssm-ID: 464330 [Multi-domain] Cd Length: 114 Bit Score: 76.20 E-value: 5.85e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737521563 247 YFLILKQGTKVLLEKREAKGLWGGLYVFPQFEHLDD------LKRSVS-GRNVQFTQLIAFRHTFSHFHLDIYPILaels 319
Cdd:pfam14815 2 VLVIRNGDGRVLLRKRPEKGLLGGLWEFPGGKVEPGetleeaLARLEElGIEVEVLEPGTVKHVFTHFRLTLHVYL---- 77
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 737521563 320 lqrnAEILPLGVAENQGnyhLRvsstadyWYDLTQPSEVGLATPIKRILDE 370
Cdd:pfam14815 78 ----VREVEGEEEPQQE---LR-------WVTPEELDKYALPAAVRKILEA 114
|
|
| HP0602 |
COG2231 |
3-Methyladenine DNA glycosylase, HhH-GPD/Endo3 superfamily [Replication, recombination and ... |
78-226 |
7.73e-06 |
|
3-Methyladenine DNA glycosylase, HhH-GPD/Endo3 superfamily [Replication, recombination and repair];
Pssm-ID: 441832 [Multi-domain] Cd Length: 220 Bit Score: 46.38 E-value: 7.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737521563 78 LANAPIDEVLHLWTGLGYYAR-ARNLHKAAQQIRDEFGGqfptDFTDVFALS------------GVGRSTAGAVLSSVLD 144
Cdd:COG2231 65 LAALDPEELAELIRPSGFYNQkAKRLKNLARWLVERYGG----GLEKLKALPteelreellslkGIGPETADSILLYAFN 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737521563 145 APYPILDGNVKRVLSR-YFAVEGWSGEKA---VENKLwdltarvtpTSQVADFNQ--AMMD-LGAMICtRSKPKCSLCPL 217
Cdd:COG2231 141 RPVFVVDAYTRRIFSRlGLIEEDASYDELqrlFEENL---------PPDVALYNEfhALIVeHGKEYC-KKKPKCEECPL 210
|
....*....
gi 737521563 218 EKGCQANAQ 226
Cdd:COG2231 211 RDLCPYGGQ 219
|
|
| FES |
smart00525 |
iron-sulpphur binding domain in DNA-(apurinic or apyrimidinic site) lyase (subfamily of ENDO3); ... |
204-223 |
1.68e-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: 38.30 E-value: 1.68e-04
|
| EndIII_4Fe-2S |
pfam10576 |
Iron-sulfur binding domain of endonuclease III; Escherichia coli endonuclease III (EC 4.2.99. ... |
205-221 |
5.35e-03 |
|
Iron-sulfur binding domain of endonuclease III; Escherichia coli endonuclease III (EC 4.2.99.18) is a DNA repair enzyme that acts both as a DNA N-glycosylase, removing oxidized pyrimidines from DNA, and as an apurinic/apyrimidinic (AP) endonuclease, introducing a single-strand nick at the site from which the damaged base was removed. Endonuclease III is an iron-sulfur protein that binds a single 4Fe-4S cluster. The 4Fe-4S cluster does not seem to be important for catalytic activity, but is probably involved in the proper positioning of the enzyme along the DNA strand. The 4Fe-4S cluster is bound by four cysteines which are all located in a 17 amino acid region at the C-terminal end of endonuclease III. A similar region is also present in the central section of mutY and in the C-terminus of ORF-10 and of the Micro-coccus UV endonuclease.
Pssm-ID: 463153 [Multi-domain] Cd Length: 17 Bit Score: 33.90 E-value: 5.35e-03
|
| |
