|
Name |
Accession |
Description |
Interval |
E-value |
| MutY |
COG1194 |
Adenine-specific DNA glycosylase, acts on AG and A-oxoG pairs [Replication, recombination and ... |
62-282 |
3.04e-127 |
|
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: 366.00 E-value: 3.04e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774523 62 ADVTAFRRNLLSWYDQEKRDLPWRKrvkeeanlDRRAYAVWVSEVMLQQTQVATVIDYYTRWMQKWPTLQDLASASLEEV 141
Cdd:COG1194 1 MDMASFAKRLLAWYDRHGRDLPWRQ--------TRDPYRVWLSEIMLQQTQVATVIPYYERFLERFPTVEALAAAPEDEV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774523 142 NQLWSGLGYYSRGRRLQEGARKVVEELGGHVPRTAETLQQLlPGVGRYTAGAIASIAFDQVTGVVDGNVIRVLCRVRAIG 221
Cdd:COG1194 73 LKLWEGLGYYSRARNLHKAAQQVVEEHGGVFPDTYEELLAL-PGIGPYTAAAIASIAFGEPAPIVDGNVKRVLSRLFAIE 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958774523 222 ADPTSSFVSHHLWDLAQQLVDPARPGDFNQAAMELGATVCTPQRPLCSHCPVQSLCRAHQR 282
Cdd:COG1194 152 GPIGSPAAKKELWALAEELLPPERPGDFNQALMDLGATVCTPKKPKCLLCPLQDDCAAFAE 212
|
|
| mutY |
TIGR01084 |
A/G-specific adenine glycosylase; This equivalog model identifies mutY members of the ... |
66-281 |
2.75e-98 |
|
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: 289.70 E-value: 2.75e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774523 66 AFRRNLLSWYDQEKR-DLPWRkrvkeeanLDRRAYAVWVSEVMLQQTQVATVIDYYTRWMQKWPTLQDLASASLEEVNQL 144
Cdd:TIGR01084 1 QFSEDLLSWYDKYGRkTLPWR--------QNKTPYRVWLSEVMLQQTQVATVIPYFERFLERFPTVQALANAPQDEVLKL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774523 145 WSGLGYYSRGRRLQEGARKVVEELGGHVPRTAETLQQlLPGVGRYTAGAIASIAFDQVTGVVDGNVIRVLCRVRAIGADP 224
Cdd:TIGR01084 73 WEGLGYYARARNLHKAAQEVVEEFGGEFPQDFEDLAA-LPGVGRYTAGAILSFALNKPYPILDGNVKRVLSRLFAVEGWP 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1958774523 225 TSSFVSHHLWDLAQQLVDPARPGDFNQAAMELGATVCTPQRPLCSHCPVQSLCRAHQ 281
Cdd:TIGR01084 152 GKKKVENRLWTLAESLLPKADPEAFNQALMDLGAMICTRKKPKCDLCPLQDFCLAYQ 208
|
|
| PRK10880 |
PRK10880 |
adenine DNA glycosylase; |
67-280 |
1.73e-70 |
|
adenine DNA glycosylase;
Pssm-ID: 182805 [Multi-domain] Cd Length: 350 Bit Score: 221.51 E-value: 1.73e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774523 67 FRRNLLSWYDQEKRD-LPWRkrvkeeanLDRRAYAVWVSEVMLQQTQVATVIDYYTRWMQKWPTLQDLASASLEEVNQLW 145
Cdd:PRK10880 6 FSAQVLDWYDKYGRKtLPWQ--------IDKTPYKVWLSEVMLQQTQVATVIPYFERFMARFPTVTDLANAPLDEVLHLW 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774523 146 SGLGYYSRGRRLQEGARKVVEELGGHVPRTAETLQQlLPGVGRYTAGAIASIAFDQVTGVVDGNVIRVLCRVRAIGADPT 225
Cdd:PRK10880 78 TGLGYYARARNLHKAAQQVATLHGGEFPETFEEVAA-LPGVGRSTAGAILSLSLGKHFPILDGNVKRVLARCYAVSGWPG 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1958774523 226 SSFVSHHLWDLAQQlVDPARP-GDFNQAAMELGATVCTPQRPLCSHCPVQSLCRAH 280
Cdd:PRK10880 157 KKEVENRLWQLSEQ-VTPAVGvERFNQAMMDLGAMVCTRSKPKCELCPLQNGCIAY 211
|
|
| ENDO3c |
cd00056 |
endonuclease III; includes endonuclease III (DNA-(apurinic or apyrimidinic site) lyase), ... |
99-257 |
3.83e-51 |
|
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: 165.49 E-value: 3.83e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774523 99 YAVWVSEVMLQQTQVATVIDYYTRWMQKW-PTLQDLASASLEEVNQLWSGLGYYSRGRRLQEGARKVVEELGGHVPRTAE 177
Cdd:cd00056 1 FEVLVSEILSQQTTDKAVNKAYERLFERYgPTPEALAAADEEELRELIRSLGYRRKAKYLKELARAIVEGFGGLVLDDPD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774523 178 TLQQL--LPGVGRYTAGAIASIAFDQVTGVVDGNVIRVLCRVRAIGADPTssfvSHHLWDLAQQLVDPARPGDFNQAAME 255
Cdd:cd00056 81 AREELlaLPGVGRKTANVVLLFALGPDAFPVDTHVRRVLKRLGLIPKKKT----PEELEELLEELLPKPYWGEANQALMD 156
|
..
gi 1958774523 256 LG 257
Cdd:cd00056 157 LG 158
|
|
| ENDO3c |
smart00478 |
endonuclease III; includes endonuclease III (DNA-(apurinic or apyrimidinic site) lyase), ... |
107-259 |
8.70e-45 |
|
endonuclease III; includes endonuclease III (DNA-(apurinic or apyrimidinic site) lyase), alkylbase DNA glycosidases (Alka-family) and other DNA glycosidases
Pssm-ID: 214684 [Multi-domain] Cd Length: 149 Bit Score: 148.95 E-value: 8.70e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774523 107 MLQQTQVATVIDYYTRWMQKWPTLQDLASASLEEVNQLWSGLG-YYSRGRRLQEGARKVVEELGGHVPRTAETLQQLlPG 185
Cdd:smart00478 1 LSQQTTDERVNKATERLFEKFPTPEDLAAADEEELEELIRGLGfYRRKARYLIELARILVEEYGGEVPDDREELLKL-PG 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958774523 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 |
4.57e-44 |
|
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: 146.66 E-value: 4.57e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774523 103 VSEVMLQQTQVATVIDYYTRWMQKW-PTLQDLASASLEEVNQLWSGLGYY-SRGRRLQEGARKVVEELGGHVPRTAETLQ 180
Cdd:pfam00730 1 VSAILSQQTSDKAVNKITERLFEKFfPTPEDLADADEEELRELIRGLGFYrRKAKYLKELARILVEGYGGEVPLDEEELE 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958774523 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 ... |
62-282 |
3.04e-127 |
|
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: 366.00 E-value: 3.04e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774523 62 ADVTAFRRNLLSWYDQEKRDLPWRKrvkeeanlDRRAYAVWVSEVMLQQTQVATVIDYYTRWMQKWPTLQDLASASLEEV 141
Cdd:COG1194 1 MDMASFAKRLLAWYDRHGRDLPWRQ--------TRDPYRVWLSEIMLQQTQVATVIPYYERFLERFPTVEALAAAPEDEV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774523 142 NQLWSGLGYYSRGRRLQEGARKVVEELGGHVPRTAETLQQLlPGVGRYTAGAIASIAFDQVTGVVDGNVIRVLCRVRAIG 221
Cdd:COG1194 73 LKLWEGLGYYSRARNLHKAAQQVVEEHGGVFPDTYEELLAL-PGIGPYTAAAIASIAFGEPAPIVDGNVKRVLSRLFAIE 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958774523 222 ADPTSSFVSHHLWDLAQQLVDPARPGDFNQAAMELGATVCTPQRPLCSHCPVQSLCRAHQR 282
Cdd:COG1194 152 GPIGSPAAKKELWALAEELLPPERPGDFNQALMDLGATVCTPKKPKCLLCPLQDDCAAFAE 212
|
|
| mutY |
TIGR01084 |
A/G-specific adenine glycosylase; This equivalog model identifies mutY members of the ... |
66-281 |
2.75e-98 |
|
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: 289.70 E-value: 2.75e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774523 66 AFRRNLLSWYDQEKR-DLPWRkrvkeeanLDRRAYAVWVSEVMLQQTQVATVIDYYTRWMQKWPTLQDLASASLEEVNQL 144
Cdd:TIGR01084 1 QFSEDLLSWYDKYGRkTLPWR--------QNKTPYRVWLSEVMLQQTQVATVIPYFERFLERFPTVQALANAPQDEVLKL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774523 145 WSGLGYYSRGRRLQEGARKVVEELGGHVPRTAETLQQlLPGVGRYTAGAIASIAFDQVTGVVDGNVIRVLCRVRAIGADP 224
Cdd:TIGR01084 73 WEGLGYYARARNLHKAAQEVVEEFGGEFPQDFEDLAA-LPGVGRYTAGAILSFALNKPYPILDGNVKRVLSRLFAVEGWP 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1958774523 225 TSSFVSHHLWDLAQQLVDPARPGDFNQAAMELGATVCTPQRPLCSHCPVQSLCRAHQ 281
Cdd:TIGR01084 152 GKKKVENRLWTLAESLLPKADPEAFNQALMDLGAMICTRKKPKCDLCPLQDFCLAYQ 208
|
|
| PRK10880 |
PRK10880 |
adenine DNA glycosylase; |
67-280 |
1.73e-70 |
|
adenine DNA glycosylase;
Pssm-ID: 182805 [Multi-domain] Cd Length: 350 Bit Score: 221.51 E-value: 1.73e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774523 67 FRRNLLSWYDQEKRD-LPWRkrvkeeanLDRRAYAVWVSEVMLQQTQVATVIDYYTRWMQKWPTLQDLASASLEEVNQLW 145
Cdd:PRK10880 6 FSAQVLDWYDKYGRKtLPWQ--------IDKTPYKVWLSEVMLQQTQVATVIPYFERFMARFPTVTDLANAPLDEVLHLW 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774523 146 SGLGYYSRGRRLQEGARKVVEELGGHVPRTAETLQQlLPGVGRYTAGAIASIAFDQVTGVVDGNVIRVLCRVRAIGADPT 225
Cdd:PRK10880 78 TGLGYYARARNLHKAAQQVATLHGGEFPETFEEVAA-LPGVGRSTAGAILSLSLGKHFPILDGNVKRVLARCYAVSGWPG 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1958774523 226 SSFVSHHLWDLAQQlVDPARP-GDFNQAAMELGATVCTPQRPLCSHCPVQSLCRAH 280
Cdd:PRK10880 157 KKEVENRLWQLSEQ-VTPAVGvERFNQAMMDLGAMVCTRSKPKCELCPLQNGCIAY 211
|
|
| ENDO3c |
cd00056 |
endonuclease III; includes endonuclease III (DNA-(apurinic or apyrimidinic site) lyase), ... |
99-257 |
3.83e-51 |
|
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: 165.49 E-value: 3.83e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774523 99 YAVWVSEVMLQQTQVATVIDYYTRWMQKW-PTLQDLASASLEEVNQLWSGLGYYSRGRRLQEGARKVVEELGGHVPRTAE 177
Cdd:cd00056 1 FEVLVSEILSQQTTDKAVNKAYERLFERYgPTPEALAAADEEELRELIRSLGYRRKAKYLKELARAIVEGFGGLVLDDPD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774523 178 TLQQL--LPGVGRYTAGAIASIAFDQVTGVVDGNVIRVLCRVRAIGADPTssfvSHHLWDLAQQLVDPARPGDFNQAAME 255
Cdd:cd00056 81 AREELlaLPGVGRKTANVVLLFALGPDAFPVDTHVRRVLKRLGLIPKKKT----PEELEELLEELLPKPYWGEANQALMD 156
|
..
gi 1958774523 256 LG 257
Cdd:cd00056 157 LG 158
|
|
| ENDO3c |
smart00478 |
endonuclease III; includes endonuclease III (DNA-(apurinic or apyrimidinic site) lyase), ... |
107-259 |
8.70e-45 |
|
endonuclease III; includes endonuclease III (DNA-(apurinic or apyrimidinic site) lyase), alkylbase DNA glycosidases (Alka-family) and other DNA glycosidases
Pssm-ID: 214684 [Multi-domain] Cd Length: 149 Bit Score: 148.95 E-value: 8.70e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774523 107 MLQQTQVATVIDYYTRWMQKWPTLQDLASASLEEVNQLWSGLG-YYSRGRRLQEGARKVVEELGGHVPRTAETLQQLlPG 185
Cdd:smart00478 1 LSQQTTDERVNKATERLFEKFPTPEDLAAADEEELEELIRGLGfYRRKARYLIELARILVEEYGGEVPDDREELLKL-PG 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958774523 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 |
4.57e-44 |
|
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: 146.66 E-value: 4.57e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774523 103 VSEVMLQQTQVATVIDYYTRWMQKW-PTLQDLASASLEEVNQLWSGLGYY-SRGRRLQEGARKVVEELGGHVPRTAETLQ 180
Cdd:pfam00730 1 VSAILSQQTSDKAVNKITERLFEKFfPTPEDLADADEEELRELIRGLGFYrRKAKYLKELARILVEGYGGEVPLDEEELE 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958774523 181 QLLPGVGRYTAGAIASIAF--DQVTGVVDGNVIRVLCRVRAIGADPTSSFVSHHLWDLAQQ 239
Cdd:pfam00730 81 ALLKGVGRWTAEAVLIFALgrPDPLPVVDTHVRRVLKRLGLIKEKPTPKEVERELEELWPP 141
|
|
| PRK13910 |
PRK13910 |
DNA glycosylase MutY; Provisional |
107-277 |
3.38e-34 |
|
DNA glycosylase MutY; Provisional
Pssm-ID: 172427 [Multi-domain] Cd Length: 289 Bit Score: 125.90 E-value: 3.38e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774523 107 MLQQTQVATVID-YYTRWMQKWPTLQDLASASLEEVNQLWSGLGYYSRGRRLQEGARKVVEELGGHVPRTAETLQQlLPG 185
Cdd:PRK13910 1 MSQQTQINTVVErFYSPFLEAFPTLKDLANAPLEEVLLLWRGLGYYSRAKNLKKSAEICVKEHHSQLPNDYQSLLK-LPG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774523 186 VGRYTAGAIASIAFDQVTGVVDGNVIRVLCRVraIGADPtsSFVSHHLWDLAQQLVDPARPGDFNQAAMELGATVCTPqR 265
Cdd:PRK13910 80 IGAYTANAILCFGFREKSACVDANIKRVLLRL--FGLDP--NIHAKDLQIKANDFLNLNESFNHNQALIDLGALICSP-K 154
|
170
....*....|..
gi 1958774523 266 PLCSHCPVQSLC 277
Cdd:PRK13910 155 PKCAICPLNPYC 166
|
|
| Nth |
COG0177 |
Endonuclease III [Replication, recombination and repair]; |
125-278 |
5.49e-30 |
|
Endonuclease III [Replication, recombination and repair];
Pssm-ID: 439947 [Multi-domain] Cd Length: 198 Bit Score: 112.11 E-value: 5.49e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774523 125 QKWPTLQDLASASLEEVNQLWSGLGYY-SRGRRLQEGARKVVEELGGHVPRTAETLQQLlPGVGRYTAGAIASIAFDQVT 203
Cdd:COG0177 47 ARYPTPEALAAADLEELEELIRPIGLYrNKAKNIIALARILVEKYGGEVPETREELESL-PGVGRKTANVVLNFAFGKPA 125
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958774523 204 GVVDGNVIRVLCRVR-AIGADPTSsfVSHHLwdlaQQLVDPARPGDFNQAAMELGATVCTPQRPLCSHCPVQSLCR 278
Cdd:COG0177 126 IAVDTHVHRVSNRLGlVPGKDPEE--VEKDL----MKLIPKEYWGDLHHLLILHGRYICKARKPKCEECPLADLCP 195
|
|
| nth |
TIGR01083 |
endonuclease III; This equivalog model identifes nth members of the pfam00730 superfamily ... |
125-268 |
1.29e-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: 89.75 E-value: 1.29e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774523 125 QKWPTLQDLASASLEEVNQLWSGLGYY-SRGRRLQEGARKVVEELGGHVPRTAETLQQLlPGVGRYTAGAIASIAFDQVT 203
Cdd:TIGR01083 54 EVYPTPQALAQAGLEELEEYIKSIGLYrNKAKNIIELCRKLVERYGGEVPEDREELVKL-PGVGRKTANVVLNVAFGIPA 132
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958774523 204 GVVDGNVIRVLCRVR-AIGADPTSsfVSHHLwdlaQQLVDPARPGDFNQAAMELGATVCTPQRPLC 268
Cdd:TIGR01083 133 IAVDTHVFRVSNRLGlSKGKDPIK--VEEDL----MKLVPREFWVKLHHWLILHGRYTCKARKPLC 192
|
|
| HP0602 |
COG2231 |
3-Methyladenine DNA glycosylase, HhH-GPD/Endo3 superfamily [Replication, recombination and ... |
129-283 |
2.01e-08 |
|
3-Methyladenine DNA glycosylase, HhH-GPD/Endo3 superfamily [Replication, recombination and repair];
Pssm-ID: 441832 [Multi-domain] Cd Length: 220 Bit Score: 53.69 E-value: 2.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774523 129 TLQDLASASLEEVNQLWSGLGYYSR-GRRLQEGARKVVEELGGHVPR-----TAETLQQLL--PGVGRYTAGAIASIAFD 200
Cdd:COG2231 61 DPEALAALDPEELAELIRPSGFYNQkAKRLKNLARWLVERYGGGLEKlkalpTEELREELLslKGIGPETADSILLYAFN 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774523 201 QVTGVVDGNVIRVLcrVRAIGADPTSSFvshhlwDLAQQLVDPARPGDFNQA----AM--ELGATVCTPqRPLCSHCPVQ 274
Cdd:COG2231 141 RPVFVVDAYTRRIF--SRLGLIEEDASY------DELQRLFEENLPPDVALYnefhALivEHGKEYCKK-KPKCEECPLR 211
|
....*....
gi 1958774523 275 SLCRAHQRV 283
Cdd:COG2231 212 DLCPYGGQE 220
|
|
| PRK10702 |
PRK10702 |
endonuclease III; Provisional |
150-283 |
5.82e-07 |
|
endonuclease III; Provisional
Pssm-ID: 182661 [Multi-domain] Cd Length: 211 Bit Score: 49.25 E-value: 5.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774523 150 YYSRGRRLQEGARKVVEELGGHVPRTAETLQQLlPGVGRYTAGAIASIAFDQVTGVVDGNVIRVLCRvraigadptSSFV 229
Cdd:PRK10702 82 YNSKAENVIKTCRILLEQHNGEVPEDRAALEAL-PGVGRKTANVVLNTAFGWPTIAVDTHIFRVCNR---------TQFA 151
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1958774523 230 SHHLWDLAQQLVDPARPGDF----NQAAMELGATVCTPQRPLCSHCPVQSLCRAHQRV 283
Cdd:PRK10702 152 PGKNVEQVEEKLLKVVPAEFkvdcHHWLILHGRYTCIARKPRCGSCIIEDLCEYKEKV 209
|
|
| HHH |
pfam00633 |
Helix-hairpin-helix motif; The helix-hairpin-helix DNA-binding motif is found to be duplicated ... |
167-197 |
4.40e-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: 4.40e-05
10 20 30
....*....|....*....|....*....|.
gi 1958774523 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 |
2.51e-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: 37.53 E-value: 2.51e-04
|
| EndIII_4Fe-2S |
pfam10576 |
Iron-sulfur binding domain of endonuclease III; Escherichia coli endonuclease III (EC 4.2.99. ... |
261-277 |
4.88e-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: 36.60 E-value: 4.88e-04
|
| Bbox2_TRIM65-like |
cd19793 |
B-box-type 2 zinc finger found in tripartite motif-containing protein 65 (TRIM65), B box and ... |
261-289 |
1.64e-03 |
|
B-box-type 2 zinc finger found in tripartite motif-containing protein 65 (TRIM65), B box and SPRY domain-containing protein (BSPRY) and similar proteins; The family includes TRIM65 and BSPRY. TRIM65 is an E3 ubiquitin-protein ligase that interacts with the innate immune receptor MDA5 enhancing its ability to stimulate interferon-beta signaling. It functions as a potential oncogenic protein that negatively regulates p53 through ubiquitination, providing insight into development of novel approaches targeting TRIM65 for non-small cell lung carcinoma (NSCLC) treatment, and also overcoming chemotherapy resistance. Moreover, TRIM65 negatively regulates microRNA-driven suppression of mRNA translation by targeting TNRC6 proteins for ubiquitination and degradation. BSPRY is a regulatory protein for maintaining calcium homeostasis. It may regulate epithelial calcium transport by inhibiting TRPV5 activity. The type 2 B-box (Bbox2) zinc finger is characterized by a CHC3H2 zinc-binding consensus motif.
Pssm-ID: 380851 Cd Length: 43 Bit Score: 35.75 E-value: 1.64e-03
10 20
....*....|....*....|....*....
gi 1958774523 261 CTPQRPLCSHCPVQSLCRAHQRVSLQRKS 289
Cdd:cd19793 15 RTEKRCVCAQCASKGECRGHRVTLLEERA 43
|
|
| |
