|
Name |
Accession |
Description |
Interval |
E-value |
| PRK10880 |
PRK10880 |
adenine DNA glycosylase; |
1-225 |
0e+00 |
|
adenine DNA glycosylase;
Pssm-ID: 182805 [Multi-domain] Cd Length: 350 Bit Score: 547.77 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1KG3_A 1 MQASQFSAQVLDWYDKYGRKTLPWQIDKTPYKVWLSEVMLQQTQVATVIPYFERFMARFPTVTDLANAPLDEVLHLWTGL 80
Cdd:PRK10880 1 MQASQFSAQVLDWYDKYGRKTLPWQIDKTPYKVWLSEVMLQQTQVATVIPYFERFMARFPTVTDLANAPLDEVLHLWTGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1KG3_A 81 GYYARARNLHKAAQQVATLHGGKFPETFEEVAALPGVGRSTAGAILSLSLGKHFPILDGNVKRVLARCYAVSGWPGKKEV 160
Cdd:PRK10880 81 GYYARARNLHKAAQQVATLHGGEFPETFEEVAALPGVGRSTAGAILSLSLGKHFPILDGNVKRVLARCYAVSGWPGKKEV 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
1KG3_A 161 ENKLWSLSEQVTPAVGVERFNQAMMDLGAMICTRSKPKCSLCPLQNGCIAAANNSWALYPGKKPK 225
Cdd:PRK10880 161 ENRLWQLSEQVTPAVGVERFNQAMMDLGAMVCTRSKPKCELCPLQNGCIAYANHSWALYPGKKPK 225
|
|
| mutY |
TIGR01084 |
A/G-specific adenine glycosylase; This equivalog model identifies mutY members of the ... |
5-225 |
1.52e-159 |
|
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: 442.23 E-value: 1.52e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1KG3_A 5 QFSAQVLDWYDKYGRKTLPWQIDKTPYKVWLSEVMLQQTQVATVIPYFERFMARFPTVTDLANAPLDEVLHLWTGLGYYA 84
Cdd:TIGR01084 1 QFSEDLLSWYDKYGRKTLPWRQNKTPYRVWLSEVMLQQTQVATVIPYFERFLERFPTVQALANAPQDEVLKLWEGLGYYA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1KG3_A 85 RARNLHKAAQQVATLHGGKFPETFEEVAALPGVGRSTAGAILSLSLGKHFPILDGNVKRVLARCYAVSGWPGKKEVENKL 164
Cdd:TIGR01084 81 RARNLHKAAQEVVEEFGGEFPQDFEDLAALPGVGRYTAGAILSFALNKPYPILDGNVKRVLSRLFAVEGWPGKKKVENRL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
1KG3_A 165 WSLSEQVTPAVGVERFNQAMMDLGAMICTRSKPKCSLCPLQNGCIAAANNSWALYPGKKPK 225
Cdd:TIGR01084 161 WTLAESLLPKADPEAFNQALMDLGAMICTRKKPKCDLCPLQDFCLAYQQGTWEEYPVKKPK 221
|
|
| MutY |
COG1194 |
Adenine-specific DNA glycosylase, acts on AG and A-oxoG pairs [Replication, recombination and ... |
1-225 |
8.87e-158 |
|
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: 440.34 E-value: 8.87e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1KG3_A 1 MQASQFSAQVLDWYDKYGRkTLPWQIDKTPYKVWLSEVMLQQTQVATVIPYFERFMARFPTVTDLANAPLDEVLHLWTGL 80
Cdd:COG1194 1 MDMASFAKRLLAWYDRHGR-DLPWRQTRDPYRVWLSEIMLQQTQVATVIPYYERFLERFPTVEALAAAPEDEVLKLWEGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1KG3_A 81 GYYARARNLHKAAQQVATLHGGKFPETFEEVAALPGVGRSTAGAILSLSLGKHFPILDGNVKRVLARCYAVSGWPGKKEV 160
Cdd:COG1194 80 GYYSRARNLHKAAQQVVEEHGGVFPDTYEELLALPGIGPYTAAAIASIAFGEPAPIVDGNVKRVLSRLFAIEGPIGSPAA 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
1KG3_A 161 ENKLWSLSEQVTPAVGVERFNQAMMDLGAMICTRSKPKCSLCPLQNGCIAAANNSWALYPGKKPK 225
Cdd:COG1194 160 KKELWALAEELLPPERPGDFNQALMDLGATVCTPKKPKCLLCPLQDDCAAFAEGRQEELPVKKPK 224
|
|
| ENDO3c |
cd00056 |
endonuclease III; includes endonuclease III (DNA-(apurinic or apyrimidinic site) lyase), ... |
31-188 |
3.77e-54 |
|
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: 170.89 E-value: 3.77e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1KG3_A 31 YKVWLSEVMLQQTQVATVIPYFERFMARF-PTVTDLANAPLDEVLHLWTGLGYYARARNLHKAAQQVATLHGGKF---PE 106
Cdd:cd00056 1 FEVLVSEILSQQTTDKAVNKAYERLFERYgPTPEALAAADEEELRELIRSLGYRRKAKYLKELARAIVEGFGGLVlddPD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1KG3_A 107 TFEEVAALPGVGRSTAGAILSLSLGKHFPILDGNVKRVLARCyavsGWPGKKEVENKLWSLSEQVTPAVGVERFNQAMMD 186
Cdd:cd00056 81 AREELLALPGVGRKTANVVLLFALGPDAFPVDTHVRRVLKRL----GLIPKKKTPEELEELLEELLPKPYWGEANQALMD 156
|
..
1KG3_A 187 LG 188
Cdd:cd00056 157 LG 158
|
|
| ENDO3c |
smart00478 |
endonuclease III; includes endonuclease III (DNA-(apurinic or apyrimidinic site) lyase), ... |
39-190 |
1.00e-51 |
|
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: 164.36 E-value: 1.00e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1KG3_A 39 MLQQTQVATVIPYFERFMARFPTVTDLANAPLDEVLHLWTGLG-YYARARNLHKAAQQVATLHGGKFPETFEEVAALPGV 117
Cdd:smart00478 1 LSQQTTDERVNKATERLFEKFPTPEDLAAADEEELEELIRGLGfYRRKARYLIELARILVEEYGGEVPDDREELLKLPGV 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
1KG3_A 118 GRSTAGAILSLSLGKHFPILDGNVKRVLARCYavsgWPGKKEVENKLWSLSEQVTPAVGVERFNQAMMDLGAM 190
Cdd:smart00478 81 GRKTANAVLSFALGKPFIPVDTHVLRIAKRLG----LVDKKSTPEEVEKLLEKLLPEEDWRELNLLLIDFGRT 149
|
|
| HhH-GPD |
pfam00730 |
HhH-GPD superfamily base excision DNA repair protein; This family contains a diverse range of ... |
35-170 |
4.81e-46 |
|
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: 149.36 E-value: 4.81e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1KG3_A 35 LSEVMLQQTQVATVIPYFERFMAR-FPTVTDLANAPLDEVLHLWTGLGYYAR-ARNLHKAAQQVATLHGGKFPETFEE-V 111
Cdd:pfam00730 1 VSAILSQQTSDKAVNKITERLFEKfFPTPEDLADADEEELRELIRGLGFYRRkAKYLKELARILVEGYGGEVPLDEEElE 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
1KG3_A 112 AALPGVGRSTAGAILSLSLG--KHFPILDGNVKRVLARCYAVSGWPGKKEVENKLWSLSEQ 170
Cdd:pfam00730 81 ALLKGVGRWTAEAVLIFALGrpDPLPVVDTHVRRVLKRLGLIKEKPTPKEVERELEELWPP 141
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK10880 |
PRK10880 |
adenine DNA glycosylase; |
1-225 |
0e+00 |
|
adenine DNA glycosylase;
Pssm-ID: 182805 [Multi-domain] Cd Length: 350 Bit Score: 547.77 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1KG3_A 1 MQASQFSAQVLDWYDKYGRKTLPWQIDKTPYKVWLSEVMLQQTQVATVIPYFERFMARFPTVTDLANAPLDEVLHLWTGL 80
Cdd:PRK10880 1 MQASQFSAQVLDWYDKYGRKTLPWQIDKTPYKVWLSEVMLQQTQVATVIPYFERFMARFPTVTDLANAPLDEVLHLWTGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1KG3_A 81 GYYARARNLHKAAQQVATLHGGKFPETFEEVAALPGVGRSTAGAILSLSLGKHFPILDGNVKRVLARCYAVSGWPGKKEV 160
Cdd:PRK10880 81 GYYARARNLHKAAQQVATLHGGEFPETFEEVAALPGVGRSTAGAILSLSLGKHFPILDGNVKRVLARCYAVSGWPGKKEV 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
1KG3_A 161 ENKLWSLSEQVTPAVGVERFNQAMMDLGAMICTRSKPKCSLCPLQNGCIAAANNSWALYPGKKPK 225
Cdd:PRK10880 161 ENRLWQLSEQVTPAVGVERFNQAMMDLGAMVCTRSKPKCELCPLQNGCIAYANHSWALYPGKKPK 225
|
|
| mutY |
TIGR01084 |
A/G-specific adenine glycosylase; This equivalog model identifies mutY members of the ... |
5-225 |
1.52e-159 |
|
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: 442.23 E-value: 1.52e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1KG3_A 5 QFSAQVLDWYDKYGRKTLPWQIDKTPYKVWLSEVMLQQTQVATVIPYFERFMARFPTVTDLANAPLDEVLHLWTGLGYYA 84
Cdd:TIGR01084 1 QFSEDLLSWYDKYGRKTLPWRQNKTPYRVWLSEVMLQQTQVATVIPYFERFLERFPTVQALANAPQDEVLKLWEGLGYYA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1KG3_A 85 RARNLHKAAQQVATLHGGKFPETFEEVAALPGVGRSTAGAILSLSLGKHFPILDGNVKRVLARCYAVSGWPGKKEVENKL 164
Cdd:TIGR01084 81 RARNLHKAAQEVVEEFGGEFPQDFEDLAALPGVGRYTAGAILSFALNKPYPILDGNVKRVLSRLFAVEGWPGKKKVENRL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
1KG3_A 165 WSLSEQVTPAVGVERFNQAMMDLGAMICTRSKPKCSLCPLQNGCIAAANNSWALYPGKKPK 225
Cdd:TIGR01084 161 WTLAESLLPKADPEAFNQALMDLGAMICTRKKPKCDLCPLQDFCLAYQQGTWEEYPVKKPK 221
|
|
| MutY |
COG1194 |
Adenine-specific DNA glycosylase, acts on AG and A-oxoG pairs [Replication, recombination and ... |
1-225 |
8.87e-158 |
|
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: 440.34 E-value: 8.87e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1KG3_A 1 MQASQFSAQVLDWYDKYGRkTLPWQIDKTPYKVWLSEVMLQQTQVATVIPYFERFMARFPTVTDLANAPLDEVLHLWTGL 80
Cdd:COG1194 1 MDMASFAKRLLAWYDRHGR-DLPWRQTRDPYRVWLSEIMLQQTQVATVIPYYERFLERFPTVEALAAAPEDEVLKLWEGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1KG3_A 81 GYYARARNLHKAAQQVATLHGGKFPETFEEVAALPGVGRSTAGAILSLSLGKHFPILDGNVKRVLARCYAVSGWPGKKEV 160
Cdd:COG1194 80 GYYSRARNLHKAAQQVVEEHGGVFPDTYEELLALPGIGPYTAAAIASIAFGEPAPIVDGNVKRVLSRLFAIEGPIGSPAA 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
1KG3_A 161 ENKLWSLSEQVTPAVGVERFNQAMMDLGAMICTRSKPKCSLCPLQNGCIAAANNSWALYPGKKPK 225
Cdd:COG1194 160 KKELWALAEELLPPERPGDFNQALMDLGATVCTPKKPKCLLCPLQDDCAAFAEGRQEELPVKKPK 224
|
|
| ENDO3c |
cd00056 |
endonuclease III; includes endonuclease III (DNA-(apurinic or apyrimidinic site) lyase), ... |
31-188 |
3.77e-54 |
|
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: 170.89 E-value: 3.77e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1KG3_A 31 YKVWLSEVMLQQTQVATVIPYFERFMARF-PTVTDLANAPLDEVLHLWTGLGYYARARNLHKAAQQVATLHGGKF---PE 106
Cdd:cd00056 1 FEVLVSEILSQQTTDKAVNKAYERLFERYgPTPEALAAADEEELRELIRSLGYRRKAKYLKELARAIVEGFGGLVlddPD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1KG3_A 107 TFEEVAALPGVGRSTAGAILSLSLGKHFPILDGNVKRVLARCyavsGWPGKKEVENKLWSLSEQVTPAVGVERFNQAMMD 186
Cdd:cd00056 81 AREELLALPGVGRKTANVVLLFALGPDAFPVDTHVRRVLKRL----GLIPKKKTPEELEELLEELLPKPYWGEANQALMD 156
|
..
1KG3_A 187 LG 188
Cdd:cd00056 157 LG 158
|
|
| ENDO3c |
smart00478 |
endonuclease III; includes endonuclease III (DNA-(apurinic or apyrimidinic site) lyase), ... |
39-190 |
1.00e-51 |
|
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: 164.36 E-value: 1.00e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1KG3_A 39 MLQQTQVATVIPYFERFMARFPTVTDLANAPLDEVLHLWTGLG-YYARARNLHKAAQQVATLHGGKFPETFEEVAALPGV 117
Cdd:smart00478 1 LSQQTTDERVNKATERLFEKFPTPEDLAAADEEELEELIRGLGfYRRKARYLIELARILVEEYGGEVPDDREELLKLPGV 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
1KG3_A 118 GRSTAGAILSLSLGKHFPILDGNVKRVLARCYavsgWPGKKEVENKLWSLSEQVTPAVGVERFNQAMMDLGAM 190
Cdd:smart00478 81 GRKTANAVLSFALGKPFIPVDTHVLRIAKRLG----LVDKKSTPEEVEKLLEKLLPEEDWRELNLLLIDFGRT 149
|
|
| HhH-GPD |
pfam00730 |
HhH-GPD superfamily base excision DNA repair protein; This family contains a diverse range of ... |
35-170 |
4.81e-46 |
|
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: 149.36 E-value: 4.81e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1KG3_A 35 LSEVMLQQTQVATVIPYFERFMAR-FPTVTDLANAPLDEVLHLWTGLGYYAR-ARNLHKAAQQVATLHGGKFPETFEE-V 111
Cdd:pfam00730 1 VSAILSQQTSDKAVNKITERLFEKfFPTPEDLADADEEELRELIRGLGFYRRkAKYLKELARILVEGYGGEVPLDEEElE 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
1KG3_A 112 AALPGVGRSTAGAILSLSLG--KHFPILDGNVKRVLARCYAVSGWPGKKEVENKLWSLSEQ 170
Cdd:pfam00730 81 ALLKGVGRWTAEAVLIFALGrpDPLPVVDTHVRRVLKRLGLIKEKPTPKEVERELEELWPP 141
|
|
| PRK13910 |
PRK13910 |
DNA glycosylase MutY; Provisional |
39-210 |
1.63e-38 |
|
DNA glycosylase MutY; Provisional
Pssm-ID: 172427 [Multi-domain] Cd Length: 289 Bit Score: 134.76 E-value: 1.63e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1KG3_A 39 MLQQTQVATVIP-YFERFMARFPTVTDLANAPLDEVLHLWTGLGYYARARNLHKAAQQVATLHGGKFPETFEEVAALPGV 117
Cdd:PRK13910 1 MSQQTQINTVVErFYSPFLEAFPTLKDLANAPLEEVLLLWRGLGYYSRAKNLKKSAEICVKEHHSQLPNDYQSLLKLPGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1KG3_A 118 GRSTAGAILSLSLGKHFPILDGNVKRVLARCYAVSGWPGKKEVE---NKLWSLSEQVTpavgverFNQAMMDLGAMICTr 194
Cdd:PRK13910 81 GAYTANAILCFGFREKSACVDANIKRVLLRLFGLDPNIHAKDLQikaNDFLNLNESFN-------HNQALIDLGALICS- 152
|
170
....*....|....*.
1KG3_A 195 SKPKCSLCPLQNGCIA 210
Cdd:PRK13910 153 PKPKCAICPLNPYCLG 168
|
|
| Nth |
COG0177 |
Endonuclease III [Replication, recombination and repair]; |
28-208 |
4.07e-34 |
|
Endonuclease III [Replication, recombination and repair];
Pssm-ID: 439947 [Multi-domain] Cd Length: 198 Bit Score: 120.59 E-value: 4.07e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1KG3_A 28 KTPYKVWLSEVMLQQTQVATVIPYFERFMARFPTVTDLANAPLDEVLHLWTGLGYY-ARARNLHKAAQQVATLHGGKFPE 106
Cdd:COG0177 18 RDPFELLVATILSAQTTDERVNKATPRLFARYPTPEALAAADLEELEELIRPIGLYrNKAKNIIALARILVEKYGGEVPE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1KG3_A 107 TFEEVAALPGVGRSTAGAILSLSLGKH-FPIlDGNVKRVLARcyavSGW-PGK--KEVENKLwslsEQVTPAVGVERFNQ 182
Cdd:COG0177 98 TREELESLPGVGRKTANVVLNFAFGKPaIAV-DTHVHRVSNR----LGLvPGKdpEEVEKDL----MKLIPKEYWGDLHH 168
|
170 180
....*....|....*....|....*.
1KG3_A 183 AMMDLGAMICTRSKPKCSLCPLQNGC 208
Cdd:COG0177 169 LLILHGRYICKARKPKCEECPLADLC 194
|
|
| nth |
TIGR01083 |
endonuclease III; This equivalog model identifes nth members of the pfam00730 superfamily ... |
28-199 |
8.93e-21 |
|
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: 85.89 E-value: 8.93e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1KG3_A 28 KTPYKVWLSEVMLQQTQVATVIPYFERFMARFPTVTDLANAPLDEVLHLWTGLGYY-ARARNLHKAAQQVATLHGGKFPE 106
Cdd:TIGR01083 25 NNPFELLVATILSAQATDKRVNKATPKLFEVYPTPQALAQAGLEELEEYIKSIGLYrNKAKNIIELCRKLVERYGGEVPE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1KG3_A 107 TFEEVAALPGVGRSTAGAILSLSLGKHFPILDGNVKRVLARcyavSGW-PGK--KEVENKLwslsEQVTPAVGVERFNQA 183
Cdd:TIGR01083 105 DREELVKLPGVGRKTANVVLNVAFGIPAIAVDTHVFRVSNR----LGLsKGKdpIKVEEDL----MKLVPREFWVKLHHW 176
|
170
....*....|....*.
1KG3_A 184 MMDLGAMICTRSKPKC 199
Cdd:TIGR01083 177 LILHGRYTCKARKPLC 192
|
|
| PRK10702 |
PRK10702 |
endonuclease III; Provisional |
82-208 |
1.09e-11 |
|
endonuclease III; Provisional
Pssm-ID: 182661 [Multi-domain] Cd Length: 211 Bit Score: 61.96 E-value: 1.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1KG3_A 82 YYARARNLHKAAQQVATLHGGKFPETFEEVAALPGVGRSTAGAILSLSLGKHFPILDGNVKRVlarCYAVSGWPGK--KE 159
Cdd:PRK10702 82 YNSKAENVIKTCRILLEQHNGEVPEDRAALEALPGVGRKTANVVLNTAFGWPTIAVDTHIFRV---CNRTQFAPGKnvEQ 158
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
1KG3_A 160 VENKLWslseQVTPAVGVERFNQAMMDLGAMICTRSKPKCSLCPLQNGC 208
Cdd:PRK10702 159 VEEKLL----KVVPAEFKVDCHHWLILHGRYTCIARKPRCGSCIIEDLC 203
|
|
| AlkA |
COG0122 |
3-methyladenine DNA glycosylase/8-oxoguanine DNA glycosylase [Replication, recombination and ... |
47-161 |
3.05e-09 |
|
3-methyladenine DNA glycosylase/8-oxoguanine DNA glycosylase [Replication, recombination and repair];
Pssm-ID: 439892 [Multi-domain] Cd Length: 255 Bit Score: 55.28 E-value: 3.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1KG3_A 47 TVIPYFERFMARFPTVTDLANAPLDEVLHLwtGLGYYaRARNLHKAAQQVAT-------LHGGKFPETFEEVAALPGVGR 119
Cdd:COG0122 115 EPIEGPGGGLYAFPTPEALAAASEEELRAC--GLSRR-KARYLRALARAVADgeldleaLAGLDDEEAIARLTALPGIGP 191
|
90 100 110 120
....*....|....*....|....*....|....*....|....
1KG3_A 120 STAGAILSLSLGKH--FPILDGNVKRVLARCYAVSGWPGKKEVE 161
Cdd:COG0122 192 WTAEMVLLFALGRPdaFPAGDLGLRRALGRLYGLGERPTPKELR 235
|
|
| HP0602 |
COG2231 |
3-Methyladenine DNA glycosylase, HhH-GPD/Endo3 superfamily [Replication, recombination and ... |
14-214 |
1.12e-07 |
|
3-Methyladenine DNA glycosylase, HhH-GPD/Endo3 superfamily [Replication, recombination and repair];
Pssm-ID: 441832 [Multi-domain] Cd Length: 220 Bit Score: 50.61 E-value: 1.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1KG3_A 14 YDKYGRktLPWQIDKTPYKVWLSEVMLQQTQVATVipyfERFMARFP-----TVTDLANAPLDEVLHLWTGLGYYAR-AR 87
Cdd:COG2231 15 LEHYGP--QHWWPAETPFEVIVGAILTQNTSWKNV----EKAIANLKeagllDPEALAALDPEELAELIRPSGFYNQkAK 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1KG3_A 88 NLHKAAQQVATLHGGKFPETF--------EEVAALPGVGRSTAGAILSLSLGKH-FPIlDGNVKRVLARcyaVSGWPGKK 158
Cdd:COG2231 89 RLKNLARWLVERYGGGLEKLKalpteelrEELLSLKGIGPETADSILLYAFNRPvFVV-DAYTRRIFSR---LGLIEEDA 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
1KG3_A 159 EVEnklwSLSEQVTPAVG--VERFNQ--AMMD-LGAMICtRSKPKCSLCPLQNGCIAAANN 214
Cdd:COG2231 165 SYD----ELQRLFEENLPpdVALYNEfhALIVeHGKEYC-KKKPKCEECPLRDLCPYGGQE 220
|
|
| HHH |
pfam00633 |
Helix-hairpin-helix motif; The helix-hairpin-helix DNA-binding motif is found to be duplicated ... |
100-127 |
1.51e-06 |
|
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: 43.56 E-value: 1.51e-06
10 20
....*....|....*....|....*...
1KG3_A 100 HGGKFPETFEEVAALPGVGRSTAGAILS 127
Cdd:pfam00633 2 LEGLIPASVEELLALPGVGPKTAEAILS 29
|
|
| FES |
smart00525 |
iron-sulpphur binding domain in DNA-(apurinic or apyrimidinic site) lyase (subfamily of ENDO3); ... |
191-211 |
2.72e-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: 37.14 E-value: 2.72e-04
10 20
....*....|....*....|.
1KG3_A 191 ICTRSKPKCSLCPLQNGCIAA 211
Cdd:smart00525 1 ICTARKPRCDECPLKDLCPAY 21
|
|
| EndIII_4Fe-2S |
pfam10576 |
Iron-sulfur binding domain of endonuclease III; Escherichia coli endonuclease III (EC 4.2.99. ... |
192-208 |
6.95e-04 |
|
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: 6.95e-04
|
| |
