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Conserved domains on  [gi|504075272|ref|WP_014309266|]
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mismatch-specific DNA-glycosylase [Corynebacterium diphtheriae]

Protein Classification

mismatch-specific DNA-glycosylase( domain architecture ID 10178234)

mismatch-specific DNA-glycosylase repairs a variety of DNA lesions, such as caused by G:T and G:U mismatches, in the base-excision repair pathway

CATH:  3.40.470.10
EC:  3.2.2.-
Gene Ontology:  GO:0003677|GO:0008263|GO:0006285
PubMed:  19909758|11178247
SCOP:  4003607

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
UDG-F2_TDG_MUG cd10028
Uracil DNA glycosylase family 2, includes thymine DNA glycosylase, mismatch-specific uracil ...
 27-198 3.19e-60

Uracil DNA glycosylase family 2, includes thymine DNA glycosylase, mismatch-specific uracil DNA glycosylase and similar proteins; Uracil DNA glycosylase family 2 consists of thymine DNA glycosylase (TDG), which removes uracil and thymine from G:U and G:T mismatches in double-stranded DNA. It includes mismatch-specific uracil DNA glycosylase (MUG), the prokaryotic homolog of TDG. Escherichia coli MUG is highly specific to G:U mismatches but also repairs G:T mismatches at high enzyme concentration. Uracil-DNA glycosylases (UDGs) initiate repair of uracils in DNA. Uracil in DNA can arise as a result of misincorporation of dUMP residues by DNA polymerase or via deamination of cytosine. Uracil in DNA mispaired with guanine is one of the major pro-mutagenic events, causing G:C->A:T mutations. Thus, UDG is an essential enzyme for maintaining the integrity of genetic information. UDGs have been classified into various families on the basis of their substrate specificity, conserved motifs, and structural similarities. Although these families demonstrate different substrate specificities, often the function of one enzyme can be complemented by the other..


:

Pssm-ID: 381679  Cd Length: 163  Bit Score: 185.76  E-value: 3.19e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504075272  27 VSDRIPNsDLRLLIVGVNPGLWTAAVNAPFAHPGNRFWPSLDRAGIVTPRFDVSHgmtdeqEKHLAHLGIGMTNLVARAT 106
Cdd:cd10028    1 LPDLLAP-GLDVLFCGINPGLRSAAVGHHYAHPGNRFWPLLHESGLTPRLLTPEE------DRRLPEYGIGLTNLVKRPT 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504075272 107 ARADELTTQELIDGAQRVIHLVNALRPRVVAVVGITAYRT--GFQHRKAVLGKQDPTLIAGwpedVALWVVPQPSGLNAH 184
Cdd:cd10028   74 ASAAELSKAELRAGVPRLLAKIARYRPRVVAFVGKGAYRAffGRLKKKAAYGLQPETGIGG----TRVFVLPSTSGLNAH 149

                        170
                 ....*....|....
gi 504075272 185 ETVETLAQRWRDVW 198
Cdd:cd10028  150 YSLEDKLEPWRELA 163
 
Name Accession Description Interval E-value
UDG-F2_TDG_MUG cd10028
Uracil DNA glycosylase family 2, includes thymine DNA glycosylase, mismatch-specific uracil ...
 27-198 3.19e-60

Uracil DNA glycosylase family 2, includes thymine DNA glycosylase, mismatch-specific uracil DNA glycosylase and similar proteins; Uracil DNA glycosylase family 2 consists of thymine DNA glycosylase (TDG), which removes uracil and thymine from G:U and G:T mismatches in double-stranded DNA. It includes mismatch-specific uracil DNA glycosylase (MUG), the prokaryotic homolog of TDG. Escherichia coli MUG is highly specific to G:U mismatches but also repairs G:T mismatches at high enzyme concentration. Uracil-DNA glycosylases (UDGs) initiate repair of uracils in DNA. Uracil in DNA can arise as a result of misincorporation of dUMP residues by DNA polymerase or via deamination of cytosine. Uracil in DNA mispaired with guanine is one of the major pro-mutagenic events, causing G:C->A:T mutations. Thus, UDG is an essential enzyme for maintaining the integrity of genetic information. UDGs have been classified into various families on the basis of their substrate specificity, conserved motifs, and structural similarities. Although these families demonstrate different substrate specificities, often the function of one enzyme can be complemented by the other..


Pssm-ID: 381679  Cd Length: 163  Bit Score: 185.76  E-value: 3.19e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504075272  27 VSDRIPNsDLRLLIVGVNPGLWTAAVNAPFAHPGNRFWPSLDRAGIVTPRFDVSHgmtdeqEKHLAHLGIGMTNLVARAT 106
Cdd:cd10028    1 LPDLLAP-GLDVLFCGINPGLRSAAVGHHYAHPGNRFWPLLHESGLTPRLLTPEE------DRRLPEYGIGLTNLVKRPT 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504075272 107 ARADELTTQELIDGAQRVIHLVNALRPRVVAVVGITAYRT--GFQHRKAVLGKQDPTLIAGwpedVALWVVPQPSGLNAH 184
Cdd:cd10028   74 ASAAELSKAELRAGVPRLLAKIARYRPRVVAFVGKGAYRAffGRLKKKAAYGLQPETGIGG----TRVFVLPSTSGLNAH 149

                        170
                 ....*....|....
gi 504075272 185 ETVETLAQRWRDVW 198
Cdd:cd10028  150 YSLEDKLEPWRELA 163
Mug COG3663
G:T/U-mismatch repair DNA glycosylase [Replication, recombination and repair];
33-197 3.18e-49

G:T/U-mismatch repair DNA glycosylase [Replication, recombination and repair];


Pssm-ID: 442880  Cd Length: 157  Bit Score: 157.63  E-value: 3.18e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504075272  33 NSDLRLLIVGVNPGLWTAAVNAPFAHPGNRFWPSLDRAGIVTPRFDVshgmtDEQEKHLAHLGIGMTNLVARATARADEL 112
Cdd:COG3663    6 APGLRVLILGSNPGLASLAAGFYYAHPRNRFWPILGAAGGTDPRLDY-----PERKAFLLEHGIGLWDVVARCTRRAGSL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504075272 113 TTQELIDGAQRVIHLVnALRPRV--VAVVGITAYRTGFQHrkavLGKQDPTLiagwpEDVALWVVPQPSGLNAHETVETL 190
Cdd:COG3663   81 DSAIRNAGPNDLAALL-RYRPRIktVAFNGKTAYRLFFKL----VAPQPETI-----GGIELWVLPSPSPANARFSLEEK 150


                 ....*..
gi 504075272 191 AQRWRDV 197
Cdd:COG3663  151 LAAWREL 157
PRK10201 PRK10201
G/U mismatch-specific DNA glycosylase;
35-206 3.17e-35

G/U mismatch-specific DNA glycosylase;


Pssm-ID: 182301  Cd Length: 168  Bit Score: 122.16  E-value: 3.17e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504075272  35 DLRLLIVGVNPGLWTAAVNAPFAHPGNRFWPSLDRAGIvTPRfdvshGMTDEQEKHLAHLGIGMTNLVARATARADELTT 114
Cdd:PRK10201   9 GLRVVFCGINPGLSSAHTGFPFAHPANRFWKVIHQAGF-TDR-----QLKPEEAQHLLDTRCGVTKLVDRPTVQANEVSK 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504075272 115 QELIDGAQRVIHLVNALRPRVVAVVGITAYRTGFQHRKAVLGKQDPTLiagwpEDVALWVVPQPSGLNaHETVETLAQRW 194
Cdd:PRK10201  83 QELRSGGRKLIEKIEDYQPQALAVLGKQAYEQGFSQRGAQWGKQTLTI-----GSTQVWVLPNPSGLN-RASLEKLVEAY 156

                        170
                 ....*....|..
gi 504075272 195 RDVwdDSALSSR 206
Cdd:PRK10201 157 REL--DQALVVR 166
UDG pfam03167
Uracil DNA glycosylase superfamily;
32-197 6.58e-25

Uracil DNA glycosylase superfamily;


Pssm-ID: 397331  Cd Length: 154  Bit Score: 95.11  E-value: 6.58e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504075272   32 PNSDLRLLIVGVNPGLWTAAVNAPF-AHPGNRFWPSLDRAGIVTPRFDVShgmtdeqekhlahlGIGMTNLVARATARAD 110
Cdd:pfam03167   4 GPPNAKVLIVGEAPGADEDATGLPFvGRAGNLLWKLLNAAGLTRDLFSPQ--------------GVYITNVVKCRPGNRR 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504075272  111 ELTTQELIDGAQRVIHLVNALRPRVVAVVGITAYrtgfqhrKAVLGKQDPTLIAG-WPE--DVALWVVPQPSGLNAHE-T 186
Cdd:pfam03167  70 KPTSHEIDACWPYLEAEIELLRPRVIVLLGKTAA-------KALLGLKKITKLRGkLIDlkGIPVLPTPHPSPLLRNKlN 142

                         170
                  ....*....|.
gi 504075272  187 VETLAQRWRDV 197
Cdd:pfam03167 143 PFLKANAWEDL 153
mug TIGR00584
mismatch-specific thymine-DNA glycosylate (mug); All proteins in this family for whcih ...
 35-180 2.55e-17

mismatch-specific thymine-DNA glycosylate (mug); All proteins in this family for whcih functions are known are G-T or G-U mismatch glycosylases that function in base excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). Used 2pf model. [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 273154  Cd Length: 328  Bit Score: 78.56  E-value: 2.55e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504075272   35 DLRLLIVGVNPGLWTAAVNAPFAHPGNRFWPSLDRAGIVTPRFDvshgMTDEQEKHLAHlGIGMTNLVARATARADELTT 114
Cdd:TIGR00584 130 NLDIVIIGINPGLMAAYKGHHYPGPGNHFWKCLFMSGLSEVQLN----HMDDHTLPGKY-GIGFTNMVERTTPGSKDLSS 204

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504075272  115 QELIDGAQRVIHLVNALRPRVVAVVGITAYRtgfQHRKAVLGKQDPTLIAGW-PE-----DVALWVVPQPSG 180
Cdd:TIGR00584 205 KEFREGGRILVQKLQKYQPRIAVFNGKCIYE---IFSKEVFGVKVKNLEFGLqPHkipdtETLCYVMPSSSA 273
UDG smart00986
Uracil DNA glycosylase superfamily;
31-197 3.85e-10

Uracil DNA glycosylase superfamily;


Pssm-ID: 214956  Cd Length: 156  Bit Score: 56.24  E-value: 3.85e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504075272    31 IPNSDLRLLIVGVNPGLWTAAVNAPF-AHPGNRFWPSLDRAGIvtPRFDVShgmtdeqekhLAHlGIGMTNLVARATARA 109
Cdd:smart00986   3 TGDPNAKVLIVGQAPGASEEDRGGPFvGAAGLLLSVMLGVAGL--PRLPPY----------LTN-IVKCRPPDAGNRRPT 69

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504075272   110 DELTTQELIDGAQRVIHLVnalRPRVVAVVGITAYRtgfqhrkAVLGKQDPTLIAGW--------PEDVALWVVPQPSGL 181
Cdd:smart00986  70 SWELQGCLLPWLTVELALA---RPHLILLLGKFAAQ-------ALLGLLRRPLVFGLrgrvaqlkGKGHRVLPLPHPSPL 139

                          170
                   ....*....|....*.
gi 504075272   182 NAHETVETLAQRWRDV 197
Cdd:smart00986 140 NRNFFPAKKFAAWNDL 155
 
Name Accession Description Interval E-value
UDG-F2_TDG_MUG cd10028
Uracil DNA glycosylase family 2, includes thymine DNA glycosylase, mismatch-specific uracil ...
 27-198 3.19e-60

Uracil DNA glycosylase family 2, includes thymine DNA glycosylase, mismatch-specific uracil DNA glycosylase and similar proteins; Uracil DNA glycosylase family 2 consists of thymine DNA glycosylase (TDG), which removes uracil and thymine from G:U and G:T mismatches in double-stranded DNA. It includes mismatch-specific uracil DNA glycosylase (MUG), the prokaryotic homolog of TDG. Escherichia coli MUG is highly specific to G:U mismatches but also repairs G:T mismatches at high enzyme concentration. Uracil-DNA glycosylases (UDGs) initiate repair of uracils in DNA. Uracil in DNA can arise as a result of misincorporation of dUMP residues by DNA polymerase or via deamination of cytosine. Uracil in DNA mispaired with guanine is one of the major pro-mutagenic events, causing G:C->A:T mutations. Thus, UDG is an essential enzyme for maintaining the integrity of genetic information. UDGs have been classified into various families on the basis of their substrate specificity, conserved motifs, and structural similarities. Although these families demonstrate different substrate specificities, often the function of one enzyme can be complemented by the other..


Pssm-ID: 381679  Cd Length: 163  Bit Score: 185.76  E-value: 3.19e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504075272  27 VSDRIPNsDLRLLIVGVNPGLWTAAVNAPFAHPGNRFWPSLDRAGIVTPRFDVSHgmtdeqEKHLAHLGIGMTNLVARAT 106
Cdd:cd10028    1 LPDLLAP-GLDVLFCGINPGLRSAAVGHHYAHPGNRFWPLLHESGLTPRLLTPEE------DRRLPEYGIGLTNLVKRPT 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504075272 107 ARADELTTQELIDGAQRVIHLVNALRPRVVAVVGITAYRT--GFQHRKAVLGKQDPTLIAGwpedVALWVVPQPSGLNAH 184
Cdd:cd10028   74 ASAAELSKAELRAGVPRLLAKIARYRPRVVAFVGKGAYRAffGRLKKKAAYGLQPETGIGG----TRVFVLPSTSGLNAH 149

                        170
                 ....*....|....
gi 504075272 185 ETVETLAQRWRDVW 198
Cdd:cd10028  150 YSLEDKLEPWRELA 163
Mug COG3663
G:T/U-mismatch repair DNA glycosylase [Replication, recombination and repair];
33-197 3.18e-49

G:T/U-mismatch repair DNA glycosylase [Replication, recombination and repair];


Pssm-ID: 442880  Cd Length: 157  Bit Score: 157.63  E-value: 3.18e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504075272  33 NSDLRLLIVGVNPGLWTAAVNAPFAHPGNRFWPSLDRAGIVTPRFDVshgmtDEQEKHLAHLGIGMTNLVARATARADEL 112
Cdd:COG3663    6 APGLRVLILGSNPGLASLAAGFYYAHPRNRFWPILGAAGGTDPRLDY-----PERKAFLLEHGIGLWDVVARCTRRAGSL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504075272 113 TTQELIDGAQRVIHLVnALRPRV--VAVVGITAYRTGFQHrkavLGKQDPTLiagwpEDVALWVVPQPSGLNAHETVETL 190
Cdd:COG3663   81 DSAIRNAGPNDLAALL-RYRPRIktVAFNGKTAYRLFFKL----VAPQPETI-----GGIELWVLPSPSPANARFSLEEK 150


                 ....*..
gi 504075272 191 AQRWRDV 197
Cdd:COG3663  151 LAAWREL 157
PRK10201 PRK10201
G/U mismatch-specific DNA glycosylase;
35-206 3.17e-35

G/U mismatch-specific DNA glycosylase;


Pssm-ID: 182301  Cd Length: 168  Bit Score: 122.16  E-value: 3.17e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504075272  35 DLRLLIVGVNPGLWTAAVNAPFAHPGNRFWPSLDRAGIvTPRfdvshGMTDEQEKHLAHLGIGMTNLVARATARADELTT 114
Cdd:PRK10201   9 GLRVVFCGINPGLSSAHTGFPFAHPANRFWKVIHQAGF-TDR-----QLKPEEAQHLLDTRCGVTKLVDRPTVQANEVSK 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504075272 115 QELIDGAQRVIHLVNALRPRVVAVVGITAYRTGFQHRKAVLGKQDPTLiagwpEDVALWVVPQPSGLNaHETVETLAQRW 194
Cdd:PRK10201  83 QELRSGGRKLIEKIEDYQPQALAVLGKQAYEQGFSQRGAQWGKQTLTI-----GSTQVWVLPNPSGLN-RASLEKLVEAY 156

                        170
                 ....*....|..
gi 504075272 195 RDVwdDSALSSR 206
Cdd:PRK10201 157 REL--DQALVVR 166
UDG pfam03167
Uracil DNA glycosylase superfamily;
32-197 6.58e-25

Uracil DNA glycosylase superfamily;


Pssm-ID: 397331  Cd Length: 154  Bit Score: 95.11  E-value: 6.58e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504075272   32 PNSDLRLLIVGVNPGLWTAAVNAPF-AHPGNRFWPSLDRAGIVTPRFDVShgmtdeqekhlahlGIGMTNLVARATARAD 110
Cdd:pfam03167   4 GPPNAKVLIVGEAPGADEDATGLPFvGRAGNLLWKLLNAAGLTRDLFSPQ--------------GVYITNVVKCRPGNRR 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504075272  111 ELTTQELIDGAQRVIHLVNALRPRVVAVVGITAYrtgfqhrKAVLGKQDPTLIAG-WPE--DVALWVVPQPSGLNAHE-T 186
Cdd:pfam03167  70 KPTSHEIDACWPYLEAEIELLRPRVIVLLGKTAA-------KALLGLKKITKLRGkLIDlkGIPVLPTPHPSPLLRNKlN 142

                         170
                  ....*....|.
gi 504075272  187 VETLAQRWRDV 197
Cdd:pfam03167 143 PFLKANAWEDL 153
mug TIGR00584
mismatch-specific thymine-DNA glycosylate (mug); All proteins in this family for whcih ...
 35-180 2.55e-17

mismatch-specific thymine-DNA glycosylate (mug); All proteins in this family for whcih functions are known are G-T or G-U mismatch glycosylases that function in base excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). Used 2pf model. [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 273154  Cd Length: 328  Bit Score: 78.56  E-value: 2.55e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504075272   35 DLRLLIVGVNPGLWTAAVNAPFAHPGNRFWPSLDRAGIVTPRFDvshgMTDEQEKHLAHlGIGMTNLVARATARADELTT 114
Cdd:TIGR00584 130 NLDIVIIGINPGLMAAYKGHHYPGPGNHFWKCLFMSGLSEVQLN----HMDDHTLPGKY-GIGFTNMVERTTPGSKDLSS 204

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504075272  115 QELIDGAQRVIHLVNALRPRVVAVVGITAYRtgfQHRKAVLGKQDPTLIAGW-PE-----DVALWVVPQPSG 180
Cdd:TIGR00584 205 KEFREGGRILVQKLQKYQPRIAVFNGKCIYE---IFSKEVFGVKVKNLEFGLqPHkipdtETLCYVMPSSSA 273
UDG-like cd09593
uracil-DNA glycosylases (UDG) and related enzymes; Uracil-DNA glycosylases (UDGs) initiate ...
 38-183 2.02e-13

uracil-DNA glycosylases (UDG) and related enzymes; Uracil-DNA glycosylases (UDGs) initiate repair of uracils in DNA. Uracil may arise from misincorporation of dUMP residues by DNA polymerase or via deamination of cytosine. Uracil in DNA mispaired with guanine is one of the major pro-mutagenic events, causing G:C->A:T mutations; thus, UDG is an essential enzyme for maintaining the integrity of genetic information. UDGs have been classified into various families on the basis of their substrate specificity, conserved motifs, and structural similarities. Although these families demonstrate different substrate specificities, often the function of one enzyme can be complemented by the other. UDG family 1 is the most efficient uracil-DNA glycosylase (UDG, also known as UNG) and shows a specificity for uracil in DNA. UDG family 2 includes thymine DNA glycosylase which removes uracil and thymine from G:U and G:T mismatches, and mismatch-specific uracil DNA glycosylase (MUG) which in Escherichia coli is highly specific to G:U mismatches, but also repairs G:T mismatches at high enzyme concentration. UDG family 3 includes Human SMUG1 which can remove uracil and its oxidized pyrimidine derivatives from, single-stranded DNA and double-stranded DNA with a preference for single-stranded DNA. Pedobacter heparinus SMUG2, which is UDG family 3 SMUG1-like, displays catalytic activities towards DNA containing uracil or hypoxanthine/xanthine. UDG family 4 includes Thermotoga maritima TTUDGA, a robust UDG which like family 1, acts on double-stranded and single-stranded uracil-containing DNA. UDG family 5 (UDGb) includes Thermus thermophilus HB8 TTUDGB which acts on double-stranded uracil-containing DNA; it is a hypoxanthine DNA glycosylase acting on double-stranded hypoxanthine-containing DNA except for the C/I base pair, as well as a xanthine DNA glycosylase which acts on both double-stranded and single-stranded xanthine-containing DNA. UDG family 6 hypoxanthine-DNA glycosylase lacks any detectable UDG activity; it excises hypoxanthine. Other UDG families include one represented by Bradyrhizobium diazoefficiens Blr0248 which prefers single-stranded DNA and removes uracil, 5-hydroxymethyl-uracil or xanthine from it.


Pssm-ID: 381677  Cd Length: 125  Bit Score: 64.33  E-value: 2.02e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504075272  38 LLIVGVNPGLWTAAV-NAPFAHPGNRFWPSLDRAGIvTPRfdvshgmtdeqekhLAHLGIGMTNLVARATARADELTTQE 116
Cdd:cd09593    1 VLIVGQNPGPHGARAgGVPPGPSGNRLWRLLAAAGG-TPR--------------LFRYGVGLTNTVPRGPPGAAAGSEKK 65

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 504075272 117 LIDGAQRVI-HLVNALRPRVVAVVGITAYRTGFQHRKAVLGKqdptliagWPEDVALWVVPQPSGLNA 183
Cdd:cd09593   66 ELRFCGRWLrKLLELLNPRVVVLLGKKAQEAYLAVLTSSKGA--------PGKGTEVLVLPHPSPRNR 125
UDG smart00986
Uracil DNA glycosylase superfamily;
31-197 3.85e-10

Uracil DNA glycosylase superfamily;


Pssm-ID: 214956  Cd Length: 156  Bit Score: 56.24  E-value: 3.85e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504075272    31 IPNSDLRLLIVGVNPGLWTAAVNAPF-AHPGNRFWPSLDRAGIvtPRFDVShgmtdeqekhLAHlGIGMTNLVARATARA 109
Cdd:smart00986   3 TGDPNAKVLIVGQAPGASEEDRGGPFvGAAGLLLSVMLGVAGL--PRLPPY----------LTN-IVKCRPPDAGNRRPT 69

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504075272   110 DELTTQELIDGAQRVIHLVnalRPRVVAVVGITAYRtgfqhrkAVLGKQDPTLIAGW--------PEDVALWVVPQPSGL 181
Cdd:smart00986  70 SWELQGCLLPWLTVELALA---RPHLILLLGKFAAQ-------ALLGLLRRPLVFGLrgrvaqlkGKGHRVLPLPHPSPL 139

                          170
                   ....*....|....*.
gi 504075272   182 NAHETVETLAQRWRDV 197
Cdd:smart00986 140 NRNFFPAKKFAAWNDL 155
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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