|
Name |
Accession |
Description |
Interval |
E-value |
| MutY |
COG1194 |
Adenine-specific DNA glycosylase, acts on AG and A-oxoG pairs [Replication, recombination and ... |
10-356 |
4.61e-120 |
|
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: 352.52 E-value: 4.61e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183596750 10 MLKWPTLQDLASASLEEVNQLWAGLGYYSRGRRLQEGARKVVEELGGHMPRTAETLQQLlPGVGRYTAGAIASIAFGQAT 89
Cdd:COG1194 55 LERFPTVEALAAAPEDEVLKLWEGLGYYSRARNLHKAAQQVVEEHGGVFPDTYEELLAL-PGIGPYTAAAIASIAFGEPA 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183596750 90 GVVDGNVARVLCRVRAIGADPSSTLVSQQLWGLAQQLVDPARPGDFNQAAMELGATVCTPQRPLCSQCPVESLCRARQRV 169
Cdd:COG1194 134 PIVDGNVKRVLSRLFAIEGPIGSPAAKKELWALAEELLPPERPGDFNQALMDLGATVCTPKKPKCLLCPLQDDCAAFAEG 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183596750 170 EQEQLlasgslsgspdveecapntgqchlclppsepwdqtlgvvnfPRKASRKPPREESSATCVLEQPGalgaQILLVQR 249
Cdd:COG1194 214 RQEEL-----------------------------------------PVKKPKKKKPERYGAALVIRDDG----RVLLEKR 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183596750 250 PNSGLLAGLWEFPSVTWEPSEQLQrkALLQELQRWAGpLPATHLRHLGEVVHTFSHIKLTYQVYGLALEGQTPVTtvPPG 329
Cdd:COG1194 249 PPKGLWGGLWEFPEFEWEEAEDPE--ALERWLREELG-LEVEWLEPLGTVRHVFTHFRLHLTVYLARVPAGPPAE--PDG 323
|
330 340
....*....|....*....|....*..
gi 1183596750 330 ARWLTQEEFHTAAVSTAMKKVFRVYQG 356
Cdd:COG1194 324 GRWVPLEELAALPLPAPMRKLLKALLK 350
|
|
| PRK10880 |
PRK10880 |
adenine DNA glycosylase; |
10-308 |
4.49e-50 |
|
adenine DNA glycosylase;
Pssm-ID: 182805 [Multi-domain] Cd Length: 350 Bit Score: 172.20 E-value: 4.49e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183596750 10 MLKWPTLQDLASASLEEVNQLWAGLGYYSRGRRLQEGARKVVEELGGHMPRTAETLQQlLPGVGRYTAGAIASIAFGQAT 89
Cdd:PRK10880 56 MARFPTVTDLANAPLDEVLHLWTGLGYYARARNLHKAAQQVATLHGGEFPETFEEVAA-LPGVGRSTAGAILSLSLGKHF 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183596750 90 GVVDGNVARVLCRVRAIGADPSSTLVSQQLWGLAQQlVDPARP-GDFNQAAMELGATVCTPQRPLCSQCPVESLCRARqr 168
Cdd:PRK10880 135 PILDGNVKRVLARCYAVSGWPGKKEVENRLWQLSEQ-VTPAVGvERFNQAMMDLGAMVCTRSKPKCELCPLQNGCIAY-- 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183596750 169 veqeqllASGSlsgspdveecapntgqchlclppsepWDQtlgvvnFPRKASRKPPREESSATCVLEQpgalGAQILLVQ 248
Cdd:PRK10880 212 -------ANHS--------------------------WAL------YPGKKPKQTLPERTGYFLLLQH----GDEVWLEQ 248
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1183596750 249 RPNSGLLAGLWEFPSVTWEpseqlqrkallQELQRW--AGPLPATHLRHLGEVVHTFSHIKL 308
Cdd:PRK10880 249 RPPSGLWGGLFCFPQFADE-----------EELRQWlaQRGIAADNLTQLTAFRHTFSHFHL 299
|
|
| ENDO3c |
smart00478 |
endonuclease III; includes endonuclease III (DNA-(apurinic or apyrimidinic site) lyase), ... |
12-145 |
5.64e-35 |
|
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: 126.22 E-value: 5.64e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183596750 12 KWPTLQDLASASLEEVNQLWAGLG-YYSRGRRLQEGARKVVEELGGHMPRTAETLQQLlPGVGRYTAGAIASIAFGQATG 90
Cdd:smart00478 20 KFPTPEDLAAADEEELEELIRGLGfYRRKARYLIELARILVEEYGGEVPDDREELLKL-PGVGRKTANAVLSFALGKPFI 98
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1183596750 91 VVDGNVARVLCRVRAIGAdpssTLVSQQLWGLAQQLVDPARPGDFNQAAMELGAT 145
Cdd:smart00478 99 PVDTHVLRIAKRLGLVDK----KSTPEEVEKLLEKLLPEEDWRELNLLLIDFGRT 149
|
|
| ENDO3c |
cd00056 |
endonuclease III; includes endonuclease III (DNA-(apurinic or apyrimidinic site) lyase), ... |
14-143 |
2.35e-34 |
|
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: 125.05 E-value: 2.35e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183596750 14 PTLQDLASASLEEVNQLWAGLGYYSRGRRLQEGARKVVEELGG---HMPRTAETLQQlLPGVGRYTAGAIASIAFGQATG 90
Cdd:cd00056 31 PTPEALAAADEEELRELIRSLGYRRKAKYLKELARAIVEGFGGlvlDDPDAREELLA-LPGVGRKTANVVLLFALGPDAF 109
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1183596750 91 VVDGNVARVLCRVRAIGADPSstlvSQQLWGLAQQLVDPARPGDFNQAAMELG 143
Cdd:cd00056 110 PVDTHVRRVLKRLGLIPKKKT----PEELEELLEELLPKPYWGEANQALMDLG 158
|
|
| HhH-GPD |
pfam00730 |
HhH-GPD superfamily base excision DNA repair protein; This family contains a diverse range of ... |
13-125 |
6.73e-32 |
|
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: 117.77 E-value: 6.73e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183596750 13 WPTLQDLASASLEEVNQLWAGLGYY-SRGRRLQEGARKVVEELGGHMPRTAETLQQLLPGVGRYTAGAIASIAFG--QAT 89
Cdd:pfam00730 26 FPTPEDLADADEEELRELIRGLGFYrRKAKYLKELARILVEGYGGEVPLDEEELEALLKGVGRWTAEAVLIFALGrpDPL 105
|
90 100 110
....*....|....*....|....*....|....*.
gi 1183596750 90 GVVDGNVARVLCRVRAIGADPSSTLVSQQLWGLAQQ 125
Cdd:pfam00730 106 PVVDTHVRRVLKRLGLIKEKPTPKEVERELEELWPP 141
|
|
| nth |
TIGR01083 |
endonuclease III; This equivalog model identifes nth members of the pfam00730 superfamily ... |
12-154 |
5.44e-22 |
|
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: 92.44 E-value: 5.44e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183596750 12 KWPTLQDLASASLEEVNQLWAGLGYY-SRGRRLQEGARKVVEELGGHMPRTAETLQQLlPGVGRYTAGAIASIAFGQATG 90
Cdd:TIGR01083 55 VYPTPQALAQAGLEELEEYIKSIGLYrNKAKNIIELCRKLVERYGGEVPEDREELVKL-PGVGRKTANVVLNVAFGIPAI 133
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1183596750 91 VVDGNVARVLCRVR-AIGADPSST------LVSQQLWglaqqlvdparpGDFNQAAMELGATVCTPQRPLC 154
Cdd:TIGR01083 134 AVDTHVFRVSNRLGlSKGKDPIKVeedlmkLVPREFW------------VKLHHWLILHGRYTCKARKPLC 192
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| MutY |
COG1194 |
Adenine-specific DNA glycosylase, acts on AG and A-oxoG pairs [Replication, recombination and ... |
10-356 |
4.61e-120 |
|
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: 352.52 E-value: 4.61e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183596750 10 MLKWPTLQDLASASLEEVNQLWAGLGYYSRGRRLQEGARKVVEELGGHMPRTAETLQQLlPGVGRYTAGAIASIAFGQAT 89
Cdd:COG1194 55 LERFPTVEALAAAPEDEVLKLWEGLGYYSRARNLHKAAQQVVEEHGGVFPDTYEELLAL-PGIGPYTAAAIASIAFGEPA 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183596750 90 GVVDGNVARVLCRVRAIGADPSSTLVSQQLWGLAQQLVDPARPGDFNQAAMELGATVCTPQRPLCSQCPVESLCRARQRV 169
Cdd:COG1194 134 PIVDGNVKRVLSRLFAIEGPIGSPAAKKELWALAEELLPPERPGDFNQALMDLGATVCTPKKPKCLLCPLQDDCAAFAEG 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183596750 170 EQEQLlasgslsgspdveecapntgqchlclppsepwdqtlgvvnfPRKASRKPPREESSATCVLEQPGalgaQILLVQR 249
Cdd:COG1194 214 RQEEL-----------------------------------------PVKKPKKKKPERYGAALVIRDDG----RVLLEKR 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183596750 250 PNSGLLAGLWEFPSVTWEPSEQLQrkALLQELQRWAGpLPATHLRHLGEVVHTFSHIKLTYQVYGLALEGQTPVTtvPPG 329
Cdd:COG1194 249 PPKGLWGGLWEFPEFEWEEAEDPE--ALERWLREELG-LEVEWLEPLGTVRHVFTHFRLHLTVYLARVPAGPPAE--PDG 323
|
330 340
....*....|....*....|....*..
gi 1183596750 330 ARWLTQEEFHTAAVSTAMKKVFRVYQG 356
Cdd:COG1194 324 GRWVPLEELAALPLPAPMRKLLKALLK 350
|
|
| PRK10880 |
PRK10880 |
adenine DNA glycosylase; |
10-308 |
4.49e-50 |
|
adenine DNA glycosylase;
Pssm-ID: 182805 [Multi-domain] Cd Length: 350 Bit Score: 172.20 E-value: 4.49e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183596750 10 MLKWPTLQDLASASLEEVNQLWAGLGYYSRGRRLQEGARKVVEELGGHMPRTAETLQQlLPGVGRYTAGAIASIAFGQAT 89
Cdd:PRK10880 56 MARFPTVTDLANAPLDEVLHLWTGLGYYARARNLHKAAQQVATLHGGEFPETFEEVAA-LPGVGRSTAGAILSLSLGKHF 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183596750 90 GVVDGNVARVLCRVRAIGADPSSTLVSQQLWGLAQQlVDPARP-GDFNQAAMELGATVCTPQRPLCSQCPVESLCRARqr 168
Cdd:PRK10880 135 PILDGNVKRVLARCYAVSGWPGKKEVENRLWQLSEQ-VTPAVGvERFNQAMMDLGAMVCTRSKPKCELCPLQNGCIAY-- 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183596750 169 veqeqllASGSlsgspdveecapntgqchlclppsepWDQtlgvvnFPRKASRKPPREESSATCVLEQpgalGAQILLVQ 248
Cdd:PRK10880 212 -------ANHS--------------------------WAL------YPGKKPKQTLPERTGYFLLLQH----GDEVWLEQ 248
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1183596750 249 RPNSGLLAGLWEFPSVTWEpseqlqrkallQELQRW--AGPLPATHLRHLGEVVHTFSHIKL 308
Cdd:PRK10880 249 RPPSGLWGGLFCFPQFADE-----------EELRQWlaQRGIAADNLTQLTAFRHTFSHFHL 299
|
|
| ENDO3c |
smart00478 |
endonuclease III; includes endonuclease III (DNA-(apurinic or apyrimidinic site) lyase), ... |
12-145 |
5.64e-35 |
|
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: 126.22 E-value: 5.64e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183596750 12 KWPTLQDLASASLEEVNQLWAGLG-YYSRGRRLQEGARKVVEELGGHMPRTAETLQQLlPGVGRYTAGAIASIAFGQATG 90
Cdd:smart00478 20 KFPTPEDLAAADEEELEELIRGLGfYRRKARYLIELARILVEEYGGEVPDDREELLKL-PGVGRKTANAVLSFALGKPFI 98
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1183596750 91 VVDGNVARVLCRVRAIGAdpssTLVSQQLWGLAQQLVDPARPGDFNQAAMELGAT 145
Cdd:smart00478 99 PVDTHVLRIAKRLGLVDK----KSTPEEVEKLLEKLLPEEDWRELNLLLIDFGRT 149
|
|
| ENDO3c |
cd00056 |
endonuclease III; includes endonuclease III (DNA-(apurinic or apyrimidinic site) lyase), ... |
14-143 |
2.35e-34 |
|
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: 125.05 E-value: 2.35e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183596750 14 PTLQDLASASLEEVNQLWAGLGYYSRGRRLQEGARKVVEELGG---HMPRTAETLQQlLPGVGRYTAGAIASIAFGQATG 90
Cdd:cd00056 31 PTPEALAAADEEELRELIRSLGYRRKAKYLKELARAIVEGFGGlvlDDPDAREELLA-LPGVGRKTANVVLLFALGPDAF 109
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1183596750 91 VVDGNVARVLCRVRAIGADPSstlvSQQLWGLAQQLVDPARPGDFNQAAMELG 143
Cdd:cd00056 110 PVDTHVRRVLKRLGLIPKKKT----PEELEELLEELLPKPYWGEANQALMDLG 158
|
|
| HhH-GPD |
pfam00730 |
HhH-GPD superfamily base excision DNA repair protein; This family contains a diverse range of ... |
13-125 |
6.73e-32 |
|
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: 117.77 E-value: 6.73e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183596750 13 WPTLQDLASASLEEVNQLWAGLGYY-SRGRRLQEGARKVVEELGGHMPRTAETLQQLLPGVGRYTAGAIASIAFG--QAT 89
Cdd:pfam00730 26 FPTPEDLADADEEELRELIRGLGFYrRKAKYLKELARILVEGYGGEVPLDEEELEALLKGVGRWTAEAVLIFALGrpDPL 105
|
90 100 110
....*....|....*....|....*....|....*.
gi 1183596750 90 GVVDGNVARVLCRVRAIGADPSSTLVSQQLWGLAQQ 125
Cdd:pfam00730 106 PVVDTHVRRVLKRLGLIKEKPTPKEVERELEELWPP 141
|
|
| NUDIX_DNA_Glycosylase_C-MutY |
cd03431 |
C-terminal domain of DNA glycosylase; DNA glycosylase (MutY in bacteria and hMYH in humans) is ... |
224-351 |
7.49e-31 |
|
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: 114.32 E-value: 7.49e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183596750 224 PREESSATCVLEQPGalgaQILLVQRPNSGLLAGLWEFPSVTWEPSEQlqrkaLLQELQRWAGPLPATHLRHLGEVVHTF 303
Cdd:cd03431 1 VPERYFTVLVLRDGG----RVLLEKRPEKGLLAGLWEFPLVETEEEEE-----EAEALLGLLAEELLLILEPLGEVKHVF 71
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1183596750 304 SHIKLTYQVYGLALEGQTPVTtvPPGARWLTQEEFHTAAVSTAMKKVF 351
Cdd:cd03431 72 SHFRLHITVYLVELPEAPPAA--PDEGRWVDLEELDEYALPAPMRKLL 117
|
|
| Nth |
COG0177 |
Endonuclease III [Replication, recombination and repair]; |
12-167 |
8.38e-31 |
|
Endonuclease III [Replication, recombination and repair];
Pssm-ID: 439947 [Multi-domain] Cd Length: 198 Bit Score: 116.73 E-value: 8.38e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183596750 12 KWPTLQDLASASLEEVNQLWAGLGYY-SRGRRLQEGARKVVEELGGHMPRTAETLQQLlPGVGRYTAGAIASIAFGQATG 90
Cdd:COG0177 48 RYPTPEALAAADLEELEELIRPIGLYrNKAKNIIALARILVEKYGGEVPETREELESL-PGVGRKTANVVLNFAFGKPAI 126
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1183596750 91 VVDGNVARVLCRvraIG-ADPSSTL-VSQQLwglaQQLVDPARPGDFNQAAMELGATVCTPQRPLCSQCPVESLCRARQ 167
Cdd:COG0177 127 AVDTHVHRVSNR---LGlVPGKDPEeVEKDL----MKLIPKEYWGDLHHLLILHGRYICKARKPKCEECPLADLCPYYG 198
|
|
| PRK13910 |
PRK13910 |
DNA glycosylase MutY; Provisional |
13-174 |
7.92e-30 |
|
DNA glycosylase MutY; Provisional
Pssm-ID: 172427 [Multi-domain] Cd Length: 289 Bit Score: 116.66 E-value: 7.92e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183596750 13 WPTLQDLASASLEEVNQLWAGLGYYSRGRRLQEGARKVVEELGGHMPRTAETLQQlLPGVGRYTAGAIASIAFGQATGVV 92
Cdd:PRK13910 22 FPTLKDLANAPLEEVLLLWRGLGYYSRAKNLKKSAEICVKEHHSQLPNDYQSLLK-LPGIGAYTANAILCFGFREKSACV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183596750 93 DGNVARVLCRVraIGADPSSTlvSQQLWGLAQQLVDPARPGDFNQAAMELGATVCTPqRPLCSQCPVESLCRARQRVEQE 172
Cdd:PRK13910 101 DANIKRVLLRL--FGLDPNIH--AKDLQIKANDFLNLNESFNHNQALIDLGALICSP-KPKCAICPLNPYCLGKNNPEKH 175
|
..
gi 1183596750 173 QL 174
Cdd:PRK13910 176 TL 177
|
|
| NUDIX_4 |
pfam14815 |
NUDIX domain; |
243-352 |
3.33e-23 |
|
NUDIX domain;
Pssm-ID: 464330 [Multi-domain] Cd Length: 114 Bit Score: 93.53 E-value: 3.33e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183596750 243 QILLVQRPNSGLLAGLWEFPSVTWEPSEQLQRKalLQELQRWAgpLPATHLRHlGEVVHTFSHIKLTYQVYGLALEGQTP 322
Cdd:pfam14815 11 RVLLRKRPEKGLLGGLWEFPGGKVEPGETLEEA--LARLEELG--IEVEVLEP-GTVKHVFTHFRLTLHVYLVREVEGEE 85
|
90 100 110
....*....|....*....|....*....|
gi 1183596750 323 vtTVPPGARWLTQEEFHTAAVSTAMKKVFR 352
Cdd:pfam14815 86 --EPQQELRWVTPEELDKYALPAAVRKILE 113
|
|
| nth |
TIGR01083 |
endonuclease III; This equivalog model identifes nth members of the pfam00730 superfamily ... |
12-154 |
5.44e-22 |
|
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: 92.44 E-value: 5.44e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183596750 12 KWPTLQDLASASLEEVNQLWAGLGYY-SRGRRLQEGARKVVEELGGHMPRTAETLQQLlPGVGRYTAGAIASIAFGQATG 90
Cdd:TIGR01083 55 VYPTPQALAQAGLEELEEYIKSIGLYrNKAKNIIELCRKLVERYGGEVPEDREELVKL-PGVGRKTANVVLNVAFGIPAI 133
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1183596750 91 VVDGNVARVLCRVR-AIGADPSST------LVSQQLWglaqqlvdparpGDFNQAAMELGATVCTPQRPLC 154
Cdd:TIGR01083 134 AVDTHVFRVSNRLGlSKGKDPIKVeedlmkLVPREFW------------VKLHHWLILHGRYTCKARKPLC 192
|
|
| PRK10702 |
PRK10702 |
endonuclease III; Provisional |
36-169 |
1.23e-08 |
|
endonuclease III; Provisional
Pssm-ID: 182661 [Multi-domain] Cd Length: 211 Bit Score: 55.02 E-value: 1.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183596750 36 YYSRGRRLQEGARKVVEELGGHMPRTAETLQQLlPGVGRYTAGAIASIAFGQATGVVDGNVARVLCRVraiGADPSSTLv 115
Cdd:PRK10702 82 YNSKAENVIKTCRILLEQHNGEVPEDRAALEAL-PGVGRKTANVVLNTAFGWPTIAVDTHIFRVCNRT---QFAPGKNV- 156
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1183596750 116 sQQLWGLAQQLVDPARPGDFNQAAMELGATVCTPQRPLCSQCPVESLCRARQRV 169
Cdd:PRK10702 157 -EQVEEKLLKVVPAEFKVDCHHWLILHGRYTCIARKPRCGSCIIEDLCEYKEKV 209
|
|
| HP0602 |
COG2231 |
3-Methyladenine DNA glycosylase, HhH-GPD/Endo3 superfamily [Replication, recombination and ... |
15-169 |
1.10e-06 |
|
3-Methyladenine DNA glycosylase, HhH-GPD/Endo3 superfamily [Replication, recombination and repair];
Pssm-ID: 441832 [Multi-domain] Cd Length: 220 Bit Score: 49.07 E-value: 1.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183596750 15 TLQDLASASLEEVNQLWAGLGYYSR-GRRLQEGARKVVEELGGHMPR-----TAETLQQLL--PGVGRYTAGAIASIAFG 86
Cdd:COG2231 61 DPEALAALDPEELAELIRPSGFYNQkAKRLKNLARWLVERYGGGLEKlkalpTEELREELLslKGIGPETADSILLYAFN 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183596750 87 QATGVVDGNVARVLCRVrAIGADPSStlvsqqlWGLAQQLVDPARPGDFNQA----AM--ELGATVCTPqRPLCSQCPVE 160
Cdd:COG2231 141 RPVFVVDAYTRRIFSRL-GLIEEDAS-------YDELQRLFEENLPPDVALYnefhALivEHGKEYCKK-KPKCEECPLR 211
|
....*....
gi 1183596750 161 SLCRARQRV 169
Cdd:COG2231 212 DLCPYGGQE 220
|
|
| NUDIX_MutT_NudA_like |
cd03425 |
MutT pyrophosphohydrolase; The MutT pyrophosphohydrolase is a prototypical NUDIX hydrolase ... |
233-340 |
2.14e-05 |
|
MutT pyrophosphohydrolase; The MutT pyrophosphohydrolase is a prototypical NUDIX hydrolase that catalyzes the hydrolysis of nucleoside and deoxynucleoside triphosphates (NTPs and dNTPs) by substitution at a beta-phosphorus to yield a nucleotide monophosphate (NMP) and inorganic pyrophosphate (PPi). This enzyme requires two divalent cations for activity; one coordinates the phosphoryl groups of the NTP/dNTP substrate, and the other coordinates to the enzyme. It also contains the NUDIX motif, a highly conserved 23-residue block (GX5EX7REUXEEXGU, where U = I, L or V), that functions as metal binding and catalytic site. MutT pyrophosphohydrolase is important in preventing errors in DNA replication by hydrolyzing mutagenic nucleotides such as 8-oxo-dGTP (a product of oxidative damage), which can mispair with template adenine during DNA replication, to guanine nucleotides.
Pssm-ID: 467531 [Multi-domain] Cd Length: 123 Bit Score: 43.59 E-value: 2.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183596750 233 VLEQPGalgaQILLVQRPNSGLLAGLWEFP--SVtwEPSEQLQrKALLQELQ---RWAgplpATHLRHLGEVVHTFSHIK 307
Cdd:cd03425 7 IIVDDG----RVLIAQRPEGKHLAGLWEFPggKV--EPGETPE-QALVRELReelGIE----VEVGEPLGTVEHDYPDFH 75
|
90 100 110
....*....|....*....|....*....|...
gi 1183596750 308 LTYQVYGLALEGQTPVTTVPPGARWLTQEEFHT 340
Cdd:cd03425 76 VRLHVYLCTLWSGEPQLLEHQELRWVTPEELDD 108
|
|
| PRK10546 |
PRK10546 |
pyrimidine (deoxy)nucleoside triphosphate diphosphatase; |
233-282 |
2.16e-05 |
|
pyrimidine (deoxy)nucleoside triphosphate diphosphatase;
Pssm-ID: 182536 [Multi-domain] Cd Length: 135 Bit Score: 43.96 E-value: 2.16e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1183596750 233 VLEQPGalgaQILLVQRPNSGLLAGLWEFPSVTWEPSEQlQRKALLQELQ 282
Cdd:PRK10546 10 IIERDG----KILLAQRPAHSDQAGLWEFAGGKVEPGES-QPQALIRELR 54
|
|
| FES |
smart00525 |
iron-sulpphur binding domain in DNA-(apurinic or apyrimidinic site) lyase (subfamily of ENDO3); ... |
146-166 |
5.00e-05 |
|
iron-sulpphur binding domain in DNA-(apurinic or apyrimidinic site) lyase (subfamily of ENDO3);
Pssm-ID: 197771 [Multi-domain] Cd Length: 21 Bit Score: 39.84 E-value: 5.00e-05
|
| HHH |
pfam00633 |
Helix-hairpin-helix motif; The helix-hairpin-helix DNA-binding motif is found to be duplicated ... |
53-83 |
7.77e-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: 39.32 E-value: 7.77e-05
10 20 30
....*....|....*....|....*....|.
gi 1183596750 53 ELGGHMPRTAETLQQLlPGVGRYTAGAIASI 83
Cdd:pfam00633 1 SLEGLIPASVEELLAL-PGVGPKTAEAILSY 30
|
|
| PRK10776 |
PRK10776 |
8-oxo-dGTP diphosphatase MutT; |
243-337 |
1.60e-04 |
|
8-oxo-dGTP diphosphatase MutT;
Pssm-ID: 182721 [Multi-domain] Cd Length: 129 Bit Score: 41.12 E-value: 1.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183596750 243 QILLVQRPNSGLLAGLWEFPSVTWEPSEQLQrKALLQELQRWAGpLPATHLRHLGEVVHTFS--HIKLTY--------QV 312
Cdd:PRK10776 17 EIFITRRAADAHMAGKWEFPGGKIEAGETPE-QALIRELQEEVG-ITVQHATLFEKLEYEFPdrHITLWFwlveswegEP 94
|
90 100
....*....|....*....|....*
gi 1183596750 313 YGlaLEGQtpvttvpPGaRWLTQEE 337
Cdd:PRK10776 95 WG--KEGQ-------PG-RWVSQVA 109
|
|
| PRK08999 |
PRK08999 |
Nudix family hydrolase; |
243-338 |
2.81e-03 |
|
Nudix family hydrolase;
Pssm-ID: 236361 [Multi-domain] Cd Length: 312 Bit Score: 39.47 E-value: 2.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183596750 243 QILLVQRPNSGLLAGLWEFPSVTWEPSEQLqRKALLQELQRWAGpLPATHLRHLGEVVHTFSHIKLT---YQVYG----- 314
Cdd:PRK08999 18 RILLARRPEGKHQGGLWEFPGGKVEPGETV-EQALARELQEELG-IEVTAARPLITVRHDYPDKRVRldvRRVTAwqgep 95
|
90 100
....*....|....*....|....
gi 1183596750 315 LALEGQtPVTTVPPgaRWLTQEEF 338
Cdd:PRK08999 96 HGREGQ-PLAWVAP--DELAVYPF 116
|
|
| EndIII_4Fe-2S |
pfam10576 |
Iron-sulfur binding domain of endonuclease III; Escherichia coli endonuclease III (EC 4.2.99. ... |
147-163 |
3.35e-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: 34.67 E-value: 3.35e-03
|
| YjhB |
COG1051 |
ADP-ribose pyrophosphatase YjhB, NUDIX family [Nucleotide transport and metabolism]; |
229-352 |
7.22e-03 |
|
ADP-ribose pyrophosphatase YjhB, NUDIX family [Nucleotide transport and metabolism];
Pssm-ID: 440671 [Multi-domain] Cd Length: 125 Bit Score: 36.49 E-value: 7.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183596750 229 SATCVLEQPGAlgaQILLVQRPNsGLLAGLWEFPSVTWEPSEQLqRKALLQELqrW--AGpLPATHLRHLGEVVHTFSHI 306
Cdd:COG1051 8 AVDAVIFRKDG---RVLLVRRAD-EPGKGLWALPGGKVEPGETP-EEAALREL--ReeTG-LEVEVLELLGVFDHPDRGH 79
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1183596750 307 KLTYQVYGLALEGQTPVTTVPPGARWLTQEEFHTAAVSTAMKKVFR 352
Cdd:COG1051 80 VVSVAFLAEVLSGEPRADDEIDEARWFPLDELPELAFTPADHEILE 125
|
|
|