|
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: 555.09 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491994011 18 PFAKGVLAWYQQYGRKHLPWQQNKTLYGVWLSEVMLQQTQVATVIPYFERFIQRFPTIIDLANAPIDEVLHLWTGLGYYA 97
Cdd:PRK10880 5 QFSAQVLDWYDKYGRKTLPWQIDKTPYKVWLSEVMLQQTQVATVIPYFERFMARFPTVTDLANAPLDEVLHLWTGLGYYA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491994011 98 RARNLHKAAQQIRDEFGGQFPTDFADVFALSGVGRSTAGAVLSSVLDAPYPILDGNVKRVLSRYFAVEGWSSEKTVENKL 177
Cdd:PRK10880 85 RARNLHKAAQQVATLHGGEFPETFEEVAALPGVGRSTAGAILSLSLGKHFPILDGNVKRVLARCYAVSGWPGKKEVENRL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491994011 178 WDLTARVTPTSQVADFNQAMMDLGAMICTRSKPKCFLCPLEKGCQANAQQAWADFPAKKPQKALPEKQSYFLILKQGTKV 257
Cdd:PRK10880 165 WQLSEQVTPAVGVERFNQAMMDLGAMVCTRSKPKCELCPLQNGCIAYANHSWALYPGKKPKQTLPERTGYFLLLQHGDEV 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491994011 258 LLEKREAKGLWGGLYVFPQFEHLDDL-----KRSVSGKNLQmtQLIAFRHTFSHFHLDIYPILAELSlqknaevlPLGVA 332
Cdd:PRK10880 245 WLEQRPPSGLWGGLFCFPQFADEEELrqwlaQRGIAADNLT--QLTAFRHTFSHFHLDIVPMWLPVS--------SFTGC 314
|
330 340 350
....*....|....*....|....*....|....*....
gi 491994011 333 ENQGnyhlrvsstADYWYDLTQPSEVGLATPIKRILDEL 371
Cdd:PRK10880 315 MDEG---------NGLWYNLAQPPSVGLAAPVERLLQQL 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: 519.69 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491994011 17 APFAKGVLAWYQQYGRkHLPWQQNKTLYGVWLSEVMLQQTQVATVIPYFERFIQRFPTIIDLANAPIDEVLHLWTGLGYY 96
Cdd:COG1194 4 ASFAKRLLAWYDRHGR-DLPWRQTRDPYRVWLSEIMLQQTQVATVIPYYERFLERFPTVEALAAAPEDEVLKLWEGLGYY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491994011 97 ARARNLHKAAQQIRDEFGGQFPTDFADVFALSGVGRSTAGAVLSSVLDAPYPILDGNVKRVLSRYFAVEGWSSEKTVENK 176
Cdd:COG1194 83 SRARNLHKAAQQVVEEHGGVFPDTYEELLALPGIGPYTAAAIASIAFGEPAPIVDGNVKRVLSRLFAIEGPIGSPAAKKE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491994011 177 LWDLTARVTPTSQVADFNQAMMDLGAMICTRSKPKCFLCPLEKGCQANAQQAWADFPAKKPQKALPEKQSYFLILKQGTK 256
Cdd:COG1194 163 LWALAEELLPPERPGDFNQALMDLGATVCTPKKPKCLLCPLQDDCAAFAEGRQEELPVKKPKKKKPERYGAALVIRDDGR 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491994011 257 VLLEKREAKGLWGGLYVFPQFEHLDD---------LKRSVSGKNLQMTQLIAFRHTFSHFHLDIYPILAELSLQKNAEvl 327
Cdd:COG1194 243 VLLEKRPPKGLWGGLWEFPEFEWEEAedpealerwLREELGLEVEWLEPLGTVRHVFTHFRLHLTVYLARVPAGPPAE-- 320
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 491994011 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 |
7.92e-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: 459.57 E-value: 7.92e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491994011 18 PFAKGVLAWYQQYGRKHLPWQQNKTLYGVWLSEVMLQQTQVATVIPYFERFIQRFPTIIDLANAPIDEVLHLWTGLGYYA 97
Cdd:TIGR01084 1 QFSEDLLSWYDKYGRKTLPWRQNKTPYRVWLSEVMLQQTQVATVIPYFERFLERFPTVQALANAPQDEVLKLWEGLGYYA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491994011 98 RARNLHKAAQQIRDEFGGQFPTDFADVFALSGVGRSTAGAVLSSVLDAPYPILDGNVKRVLSRYFAVEGWSSEKTVENKL 177
Cdd:TIGR01084 81 RARNLHKAAQEVVEEFGGEFPQDFEDLAALPGVGRYTAGAILSFALNKPYPILDGNVKRVLSRLFAVEGWPGKKKVENRL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491994011 178 WDLTARVTPTSQVADFNQAMMDLGAMICTRSKPKCFLCPLEKGCQANAQQAWADFPAKKPQKALPEKQSYFLILKQGT-K 256
Cdd:TIGR01084 161 WTLAESLLPKADPEAFNQALMDLGAMICTRKKPKCDLCPLQDFCLAYQQGTWEEYPVKKPKAAPPERTTYFLVLQNYDgE 240
|
250 260
....*....|....*....|....*....
gi 491994011 257 VLLEKREAKGLWGGLYVFPQFEHLDDLKR 285
Cdd:TIGR01084 241 VLLEQRPEKGLWGGLYCFPQFEDEDSLAF 269
|
|
| ENDO3c |
cd00056 |
endonuclease III; includes endonuclease III (DNA-(apurinic or apyrimidinic site) lyase), ... |
44-201 |
9.42e-50 |
|
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: 164.72 E-value: 9.42e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491994011 44 YGVWLSEVMLQQTQVATVIPYFERFIQRF-PTIIDLANAPIDEVLHLWTGLGYYARARNLHKAAQQIRDEFGG---QFPT 119
Cdd:cd00056 1 FEVLVSEILSQQTTDKAVNKAYERLFERYgPTPEALAAADEEELRELIRSLGYRRKAKYLKELARAIVEGFGGlvlDDPD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491994011 120 DFADVFALSGVGRSTAGAVLSSVLDAPYPILDGNVKRVLSRYfaveGWSSEKTVENKLWDLTARVTPTSQVADFNQAMMD 199
Cdd:cd00056 81 AREELLALPGVGRKTANVVLLFALGPDAFPVDTHVRRVLKRL----GLIPKKKTPEELEELLEELLPKPYWGEANQALMD 156
|
..
gi 491994011 200 LG 201
Cdd:cd00056 157 LG 158
|
|
| ENDO3c |
smart00478 |
endonuclease III; includes endonuclease III (DNA-(apurinic or apyrimidinic site) lyase), ... |
52-203 |
6.25e-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: 146.64 E-value: 6.25e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491994011 52 MLQQTQVATVIPYFERFIQRFPTIIDLANAPIDEVLHLWTGLG-YYARARNLHKAAQQIRDEFGGQFPTDFADVFALSGV 130
Cdd:smart00478 1 LSQQTTDERVNKATERLFEKFPTPEDLAAADEEELEELIRGLGfYRRKARYLIELARILVEEYGGEVPDDREELLKLPGV 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491994011 131 GRSTAGAVLSSVLDAPYPILDGNVKRVLSRYFavegWSSEKTVENKLWDLTARVTPTSQVADFNQAMMDLGAM 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 |
1.37e-36 |
|
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: 129.71 E-value: 1.37e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491994011 48 LSEVMLQQTQVATVIPYFERFIQR-FPTIIDLANAPIDEVLHLWTGLGYYAR-ARNLHKAAQQIRDEFGGQFPTDF-ADV 124
Cdd:pfam00730 1 VSAILSQQTSDKAVNKITERLFEKfFPTPEDLADADEEELRELIRGLGFYRRkAKYLKELARILVEGYGGEVPLDEeELE 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491994011 125 FALSGVGRSTAGAVLSSVLDA--PYPILDGNVKRVLSRYFAVEGWSSEKTVENKLWDLTAR 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: 555.09 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491994011 18 PFAKGVLAWYQQYGRKHLPWQQNKTLYGVWLSEVMLQQTQVATVIPYFERFIQRFPTIIDLANAPIDEVLHLWTGLGYYA 97
Cdd:PRK10880 5 QFSAQVLDWYDKYGRKTLPWQIDKTPYKVWLSEVMLQQTQVATVIPYFERFMARFPTVTDLANAPLDEVLHLWTGLGYYA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491994011 98 RARNLHKAAQQIRDEFGGQFPTDFADVFALSGVGRSTAGAVLSSVLDAPYPILDGNVKRVLSRYFAVEGWSSEKTVENKL 177
Cdd:PRK10880 85 RARNLHKAAQQVATLHGGEFPETFEEVAALPGVGRSTAGAILSLSLGKHFPILDGNVKRVLARCYAVSGWPGKKEVENRL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491994011 178 WDLTARVTPTSQVADFNQAMMDLGAMICTRSKPKCFLCPLEKGCQANAQQAWADFPAKKPQKALPEKQSYFLILKQGTKV 257
Cdd:PRK10880 165 WQLSEQVTPAVGVERFNQAMMDLGAMVCTRSKPKCELCPLQNGCIAYANHSWALYPGKKPKQTLPERTGYFLLLQHGDEV 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491994011 258 LLEKREAKGLWGGLYVFPQFEHLDDL-----KRSVSGKNLQmtQLIAFRHTFSHFHLDIYPILAELSlqknaevlPLGVA 332
Cdd:PRK10880 245 WLEQRPPSGLWGGLFCFPQFADEEELrqwlaQRGIAADNLT--QLTAFRHTFSHFHLDIVPMWLPVS--------SFTGC 314
|
330 340 350
....*....|....*....|....*....|....*....
gi 491994011 333 ENQGnyhlrvsstADYWYDLTQPSEVGLATPIKRILDEL 371
Cdd:PRK10880 315 MDEG---------NGLWYNLAQPPSVGLAAPVERLLQQL 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: 519.69 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491994011 17 APFAKGVLAWYQQYGRkHLPWQQNKTLYGVWLSEVMLQQTQVATVIPYFERFIQRFPTIIDLANAPIDEVLHLWTGLGYY 96
Cdd:COG1194 4 ASFAKRLLAWYDRHGR-DLPWRQTRDPYRVWLSEIMLQQTQVATVIPYYERFLERFPTVEALAAAPEDEVLKLWEGLGYY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491994011 97 ARARNLHKAAQQIRDEFGGQFPTDFADVFALSGVGRSTAGAVLSSVLDAPYPILDGNVKRVLSRYFAVEGWSSEKTVENK 176
Cdd:COG1194 83 SRARNLHKAAQQVVEEHGGVFPDTYEELLALPGIGPYTAAAIASIAFGEPAPIVDGNVKRVLSRLFAIEGPIGSPAAKKE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491994011 177 LWDLTARVTPTSQVADFNQAMMDLGAMICTRSKPKCFLCPLEKGCQANAQQAWADFPAKKPQKALPEKQSYFLILKQGTK 256
Cdd:COG1194 163 LWALAEELLPPERPGDFNQALMDLGATVCTPKKPKCLLCPLQDDCAAFAEGRQEELPVKKPKKKKPERYGAALVIRDDGR 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491994011 257 VLLEKREAKGLWGGLYVFPQFEHLDD---------LKRSVSGKNLQMTQLIAFRHTFSHFHLDIYPILAELSLQKNAEvl 327
Cdd:COG1194 243 VLLEKRPPKGLWGGLWEFPEFEWEEAedpealerwLREELGLEVEWLEPLGTVRHVFTHFRLHLTVYLARVPAGPPAE-- 320
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 491994011 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 |
7.92e-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: 459.57 E-value: 7.92e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491994011 18 PFAKGVLAWYQQYGRKHLPWQQNKTLYGVWLSEVMLQQTQVATVIPYFERFIQRFPTIIDLANAPIDEVLHLWTGLGYYA 97
Cdd:TIGR01084 1 QFSEDLLSWYDKYGRKTLPWRQNKTPYRVWLSEVMLQQTQVATVIPYFERFLERFPTVQALANAPQDEVLKLWEGLGYYA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491994011 98 RARNLHKAAQQIRDEFGGQFPTDFADVFALSGVGRSTAGAVLSSVLDAPYPILDGNVKRVLSRYFAVEGWSSEKTVENKL 177
Cdd:TIGR01084 81 RARNLHKAAQEVVEEFGGEFPQDFEDLAALPGVGRYTAGAILSFALNKPYPILDGNVKRVLSRLFAVEGWPGKKKVENRL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491994011 178 WDLTARVTPTSQVADFNQAMMDLGAMICTRSKPKCFLCPLEKGCQANAQQAWADFPAKKPQKALPEKQSYFLILKQGT-K 256
Cdd:TIGR01084 161 WTLAESLLPKADPEAFNQALMDLGAMICTRKKPKCDLCPLQDFCLAYQQGTWEEYPVKKPKAAPPERTTYFLVLQNYDgE 240
|
250 260
....*....|....*....|....*....
gi 491994011 257 VLLEKREAKGLWGGLYVFPQFEHLDDLKR 285
Cdd:TIGR01084 241 VLLEQRPEKGLWGGLYCFPQFEDEDSLAF 269
|
|
| ENDO3c |
cd00056 |
endonuclease III; includes endonuclease III (DNA-(apurinic or apyrimidinic site) lyase), ... |
44-201 |
9.42e-50 |
|
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: 164.72 E-value: 9.42e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491994011 44 YGVWLSEVMLQQTQVATVIPYFERFIQRF-PTIIDLANAPIDEVLHLWTGLGYYARARNLHKAAQQIRDEFGG---QFPT 119
Cdd:cd00056 1 FEVLVSEILSQQTTDKAVNKAYERLFERYgPTPEALAAADEEELRELIRSLGYRRKAKYLKELARAIVEGFGGlvlDDPD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491994011 120 DFADVFALSGVGRSTAGAVLSSVLDAPYPILDGNVKRVLSRYfaveGWSSEKTVENKLWDLTARVTPTSQVADFNQAMMD 199
Cdd:cd00056 81 AREELLALPGVGRKTANVVLLFALGPDAFPVDTHVRRVLKRL----GLIPKKKTPEELEELLEELLPKPYWGEANQALMD 156
|
..
gi 491994011 200 LG 201
Cdd:cd00056 157 LG 158
|
|
| ENDO3c |
smart00478 |
endonuclease III; includes endonuclease III (DNA-(apurinic or apyrimidinic site) lyase), ... |
52-203 |
6.25e-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: 146.64 E-value: 6.25e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491994011 52 MLQQTQVATVIPYFERFIQRFPTIIDLANAPIDEVLHLWTGLG-YYARARNLHKAAQQIRDEFGGQFPTDFADVFALSGV 130
Cdd:smart00478 1 LSQQTTDERVNKATERLFEKFPTPEDLAAADEEELEELIRGLGfYRRKARYLIELARILVEEYGGEVPDDREELLKLPGV 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491994011 131 GRSTAGAVLSSVLDAPYPILDGNVKRVLSRYFavegWSSEKTVENKLWDLTARVTPTSQVADFNQAMMDLGAM 203
Cdd:smart00478 81 GRKTANAVLSFALGKPFIPVDTHVLRIAKRLG----LVDKKSTPEEVEKLLEKLLPEEDWRELNLLLIDFGRT 149
|
|
| PRK13910 |
PRK13910 |
DNA glycosylase MutY; Provisional |
52-323 |
7.59e-39 |
|
DNA glycosylase MutY; Provisional
Pssm-ID: 172427 [Multi-domain] Cd Length: 289 Bit Score: 140.54 E-value: 7.59e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491994011 52 MLQQTQVATVIP-YFERFIQRFPTIIDLANAPIDEVLHLWTGLGYYARARNLHKAAQQIRDEFGGQFPTDFADVFALSGV 130
Cdd:PRK13910 1 MSQQTQINTVVErFYSPFLEAFPTLKDLANAPLEEVLLLWRGLGYYSRAKNLKKSAEICVKEHHSQLPNDYQSLLKLPGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491994011 131 GRSTAGAVLSSVLDAPYPILDGNVKRVLSRYFAVEGWSSEKTVENKLWDLTArvtpTSQVADFNQAMMDLGAMICTrSKP 210
Cdd:PRK13910 81 GAYTANAILCFGFREKSACVDANIKRVLLRLFGLDPNIHAKDLQIKANDFLN----LNESFNHNQALIDLGALICS-PKP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491994011 211 KCFLCPLEKGCQanAQQAWADFPAKKPQKALPEKQsYFLILKQGTKVLLEKREAKgLWGGLYVFPqfehldDLKRSVSGK 290
Cdd:PRK13910 156 KCAICPLNPYCL--GKNNPEKHTLKKKQEIVQEER-YLGVVIQNNQIALEKIEQK-LYLGMHHFP------NLKENLEYK 225
|
250 260 270
....*....|....*....|....*....|...
gi 491994011 291 nlqMTQLIAFRHTFSHFHLDIYPILAELSLQKN 323
Cdd:PRK13910 226 ---LPFLGAIKHSHTKFKLNLNLYLAAIKDLKN 255
|
|
| HhH-GPD |
pfam00730 |
HhH-GPD superfamily base excision DNA repair protein; This family contains a diverse range of ... |
48-183 |
1.37e-36 |
|
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: 129.71 E-value: 1.37e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491994011 48 LSEVMLQQTQVATVIPYFERFIQR-FPTIIDLANAPIDEVLHLWTGLGYYAR-ARNLHKAAQQIRDEFGGQFPTDF-ADV 124
Cdd:pfam00730 1 VSAILSQQTSDKAVNKITERLFEKfFPTPEDLADADEEELRELIRGLGFYRRkAKYLKELARILVEGYGGEVPLDEeELE 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491994011 125 FALSGVGRSTAGAVLSSVLDA--PYPILDGNVKRVLSRYFAVEGWSSEKTVENKLWDLTAR 183
Cdd:pfam00730 81 ALLKGVGRWTAEAVLIFALGRpdPLPVVDTHVRRVLKRLGLIKEKPTPKEVERELEELWPP 141
|
|
| Nth |
COG0177 |
Endonuclease III [Replication, recombination and repair]; |
51-221 |
1.21e-29 |
|
Endonuclease III [Replication, recombination and repair];
Pssm-ID: 439947 [Multi-domain] Cd Length: 198 Bit Score: 113.27 E-value: 1.21e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491994011 51 VML-QQTQVATVIPYFERFIQRFPTIIDLANAPIDEVLHLWTGLGYY-ARARNLHKAAQQIRDEFGGQFPTDFADVFALS 128
Cdd:COG0177 27 TILsAQTTDERVNKATPRLFARYPTPEALAAADLEELEELIRPIGLYrNKAKNIIALARILVEKYGGEVPETREELESLP 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491994011 129 GVGRSTAGAVLSSVLDAPYPILDGNVKRVLSRYfaveGWSSEKT---VENKLwdltARVTPTSQVADFNQAMMDLGAMIC 205
Cdd:COG0177 107 GVGRKTANVVLNFAFGKPAIAVDTHVHRVSNRL----GLVPGKDpeeVEKDL----MKLIPKEYWGDLHHLLILHGRYIC 178
|
170
....*....|....*.
gi 491994011 206 TRSKPKCFLCPLEKGC 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 |
4.40e-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: 95.83 E-value: 4.40e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491994011 242 PEKQSYFLILKQGTKVLLEKREAKGLWGGLYVFPQFEHLDDL-------KRSVSGKNLQMTQLIAFRHTFSHFHLDIYPI 314
Cdd:cd03431 2 PERYFTVLVLRDGGRVLLEKRPEKGLLAGLWEFPLVETEEEEeeaeallGLLAEELLLILEPLGEVKHVFSHFRLHITVY 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 491994011 315 LAELSLQKNAEVLPLgvaenqgnyhlrvsstadYWYDLTQPSEVGLATPIKRILD 369
Cdd:cd03431 82 LVELPEAPPAAPDEG------------------RWVDLEELDEYALPAPMRKLLE 118
|
|
| NUDIX_4 |
pfam14815 |
NUDIX domain; |
247-370 |
6.27e-17 |
|
NUDIX domain;
Pssm-ID: 464330 [Multi-domain] Cd Length: 114 Bit Score: 75.81 E-value: 6.27e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491994011 247 YFLILKQGTKVLLEKREAKGLWGGLYVFPQFEHLDD------LKRSVS-GKNLQMTQLIAFRHTFSHFHLDIYPILAELs 319
Cdd:pfam14815 2 VLVIRNGDGRVLLRKRPEKGLLGGLWEFPGGKVEPGetleeaLARLEElGIEVEVLEPGTVKHVFTHFRLTLHVYLVRE- 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 491994011 320 lqknaevlplgVAENQGNYHLRVsstadyWYDLTQPSEVGLATPIKRILDE 370
Cdd:pfam14815 81 -----------VEGEEEPQQELR------WVTPEELDKYALPAAVRKILEA 114
|
|
| HP0602 |
COG2231 |
3-Methyladenine DNA glycosylase, HhH-GPD/Endo3 superfamily [Replication, recombination and ... |
78-226 |
1.16e-04 |
|
3-Methyladenine DNA glycosylase, HhH-GPD/Endo3 superfamily [Replication, recombination and repair];
Pssm-ID: 441832 [Multi-domain] Cd Length: 220 Bit Score: 42.91 E-value: 1.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491994011 78 LANAPIDEVLHLWTGLGYYAR-ARNLHKAAQQIRDEFGGqfptDFADVFALS------------GVGRSTAGAVLSSVLD 144
Cdd:COG2231 65 LAALDPEELAELIRPSGFYNQkAKRLKNLARWLVERYGG----GLEKLKALPteelreellslkGIGPETADSILLYAFN 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491994011 145 APYPILDGNVKRVLSRYfaveGWSSEKTVENKLWDLTARVTPTSqVADFNQ--AMMD-LGAMICtRSKPKCFLCPLEKGC 221
Cdd:COG2231 141 RPVFVVDAYTRRIFSRL----GLIEEDASYDELQRLFEENLPPD-VALYNEfhALIVeHGKEYC-KKKPKCEECPLRDLC 214
|
....*
gi 491994011 222 QANAQ 226
Cdd:COG2231 215 PYGGQ 219
|
|
| FES |
smart00525 |
iron-sulpphur binding domain in DNA-(apurinic or apyrimidinic site) lyase (subfamily of ENDO3); ... |
204-223 |
1.05e-03 |
|
iron-sulpphur binding domain in DNA-(apurinic or apyrimidinic site) lyase (subfamily of ENDO3);
Pssm-ID: 197771 [Multi-domain] Cd Length: 21 Bit Score: 35.99 E-value: 1.05e-03
|
| |
