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Conserved domains on  [gi|398398678|ref|XP_003852796|]
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uncharacterized protein MYCGRDRAFT_24066, partial [Zymoseptoria tritici IPO323]

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 ...
 27-200 6.43e-74

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: 220.43  E-value: 6.43e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398398678  27 LTDILTPNLICVFVGFNPGVRTATSGHAYAHPSNLFWKLLHSSGCTDRRLEPREDVDLPRlYRMGNTNIVARPSRDAAEL 106
Cdd:cd10028    1 LPDLLAPGLDVLFCGINPGLRSAAVGHHYAHPGNRFWPLLHESGLTPRLLTPEEDRRLPE-YGIGLTNLVKRPTASAAEL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398398678 107 SKAESAAGTPILEEKIRKFRPEAVCIVGKGIWESIWRwrygrnIRKDEFRYGWQDERekmgkteDWEGAWVFVATATSGL 186
Cdd:cd10028   80 SKAELRAGVPRLLAKIARYRPRVVAFVGKGAYRAFFG------RLKKKAAYGLQPET-------GIGGTRVFVLPSTSGL 146

                        170
                 ....*....|....
gi 398398678 187 AASLRPHEKEAIWK 200
Cdd:cd10028  147 NAHYSLEDKLEPWR 160
 
Name Accession Description Interval E-value
UDG-F2_TDG_MUG cd10028
Uracil DNA glycosylase family 2, includes thymine DNA glycosylase, mismatch-specific uracil ...
 27-200 6.43e-74

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: 220.43  E-value: 6.43e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398398678  27 LTDILTPNLICVFVGFNPGVRTATSGHAYAHPSNLFWKLLHSSGCTDRRLEPREDVDLPRlYRMGNTNIVARPSRDAAEL 106
Cdd:cd10028    1 LPDLLAPGLDVLFCGINPGLRSAAVGHHYAHPGNRFWPLLHESGLTPRLLTPEEDRRLPE-YGIGLTNLVKRPTASAAEL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398398678 107 SKAESAAGTPILEEKIRKFRPEAVCIVGKGIWESIWRwrygrnIRKDEFRYGWQDERekmgkteDWEGAWVFVATATSGL 186
Cdd:cd10028   80 SKAELRAGVPRLLAKIARYRPRVVAFVGKGAYRAFFG------RLKKKAAYGLQPET-------GIGGTRVFVLPSTSGL 146

                        170
                 ....*....|....
gi 398398678 187 AASLRPHEKEAIWK 200
Cdd:cd10028  147 NAHYSLEDKLEPWR 160
mug TIGR00584
mismatch-specific thymine-DNA glycosylate (mug); All proteins in this family for whcih ...
 27-188 2.46e-36

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: 129.79  E-value: 2.46e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398398678   27 LTDILTPNLICVFVGFNPGVRTATSGHAYAHPSNLFWKLLHSSGCTDRRLEPREDVDLPRLYRMGNTNIVARPSRDAAEL 106
Cdd:TIGR00584 123 LPDILTFNLDIVIIGINPGLMAAYKGHHYPGPGNHFWKCLFMSGLSEVQLNHMDDHTLPGKYGIGFTNMVERTTPGSKDL 202

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398398678  107 SKAESAAGTPILEEKIRKFRPEAVCIVGKGIWESIWRWRYGRNIRKDEFryGWQDerEKMGKTEdwegAWVFVATATSGL 186
Cdd:TIGR00584 203 SSKEFREGGRILVQKLQKYQPRIAVFNGKCIYEIFSKEVFGVKVKNLEF--GLQP--HKIPDTE----TLCYVMPSSSAR 274


                  ..
gi 398398678  187 AA 188
Cdd:TIGR00584 275 CA 276
PRK10201 PRK10201
G/U mismatch-specific DNA glycosylase;
27-172 3.05e-31

G/U mismatch-specific DNA glycosylase;


Pssm-ID: 182301  Cd Length: 168  Bit Score: 112.14  E-value: 3.05e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398398678  27 LTDILTPNLICVFVGFNPGVRTATSGHAYAHPSNLFWKLLHSSGCTDRRLEPREDVDLPRlYRMGNTNIVARPSRDAAEL 106
Cdd:PRK10201   2 VEDILAPGLRVVFCGINPGLSSAHTGFPFAHPANRFWKVIHQAGFTDRQLKPEEAQHLLD-TRCGVTKLVDRPTVQANEV 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 398398678 107 SKAESAAGTPILEEKIRKFRPEAVCIVGKGIWESIWRwrygrnIRKDEfrygWQDEREKMGKTEDW 172
Cdd:PRK10201  81 SKQELRSGGRKLIEKIEDYQPQALAVLGKQAYEQGFS------QRGAQ----WGKQTLTIGSTQVW 136
Mug COG3663
G:T/U-mismatch repair DNA glycosylase [Replication, recombination and repair];
27-202 2.25e-28

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


Pssm-ID: 442880  Cd Length: 157  Bit Score: 104.09  E-value: 2.25e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398398678  27 LTDILTPNLICVFVGFNPGVRTATSGHAYAHPSNLFWKLLHSSGCTDRRL-EPREDVDLPRlYRMGNTNIVARPSRDAAE 105
Cdd:COG3663    1 LPPVLAPGLRVLILGSNPGLASLAAGFYYAHPRNRFWPILGAAGGTDPRLdYPERKAFLLE-HGIGLWDVVARCTRRAGS 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398398678 106 LSKAESAAGTPILEEkIRKFRP--EAVCIVGKGIWESIwrwrygrnirkdeFRY-GWQDERekmgktedWEGAWVFVATA 182
Cdd:COG3663   80 LDSAIRNAGPNDLAA-LLRYRPriKTVAFNGKTAYRLF-------------FKLvAPQPET--------IGGIELWVLPS 137

                        170       180
                 ....*....|....*....|
gi 398398678 183 TSGLAASLRPHEKEAIWKPF 202
Cdd:COG3663  138 PSPANARFSLEEKLAAWREL 157
UDG pfam03167
Uracil DNA glycosylase superfamily;
38-200 1.08e-21

Uracil DNA glycosylase superfamily;


Pssm-ID: 397331  Cd Length: 154  Bit Score: 87.02  E-value: 1.08e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398398678   38 VFVGFNPGVRTATSGHAY-AHPSNLFWKLLHSSGCTdRRLEPREDVdlprlyrmGNTNIVARPSRDAAELSKAESAAGTP 116
Cdd:pfam03167  11 LIVGEAPGADEDATGLPFvGRAGNLLWKLLNAAGLT-RDLFSPQGV--------YITNVVKCRPGNRRKPTSHEIDACWP 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398398678  117 ILEEKIRKFRPEAVCIVGKGIWESIWRWRYGRNIRkdefrygwqderekmGKTEDWEGAWVFVATATSGL-AASLRPHEK 195
Cdd:pfam03167  82 YLEAEIELLRPRVIVLLGKTAAKALLGLKKITKLR---------------GKLIDLKGIPVLPTPHPSPLlRNKLNPFLK 146


                  ....*
gi 398398678  196 EAIWK 200
Cdd:pfam03167 147 ANAWE 151
UDG smart00986
Uracil DNA glycosylase superfamily;
38-199 1.44e-07

Uracil DNA glycosylase superfamily;


Pssm-ID: 214956  Cd Length: 156  Bit Score: 49.31  E-value: 1.44e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398398678    38 VFVGFNPGVRTA-TSGHAYAHPSNLFWKLLHSSGctDRRLEPREdvdlprlyrmgnTNIVAR--PSRDAAELSKAESAA- 113
Cdd:smart00986  11 LIVGQAPGASEEdRGGPFVGAAGLLLSVMLGVAG--LPRLPPYL------------TNIVKCrpPDAGNRRPTSWELQGc 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398398678   114 GTPILEEKIRKFRPEAVCIVGKGIWESIWRWRYGRNIrkdEFRYGWQDEREkmgktedWEGAWVFVATATSGLAASLRPH 193
Cdd:smart00986  77 LLPWLTVELALARPHLILLLGKFAAQALLGLLRRPLV---FGLRGRVAQLK-------GKGHRVLPLPHPSPLNRNFFPA 146


                   ....*.
gi 398398678   194 EKEAIW 199
Cdd:smart00986 147 KKFAAW 152
 
Name Accession Description Interval E-value
UDG-F2_TDG_MUG cd10028
Uracil DNA glycosylase family 2, includes thymine DNA glycosylase, mismatch-specific uracil ...
 27-200 6.43e-74

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: 220.43  E-value: 6.43e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398398678  27 LTDILTPNLICVFVGFNPGVRTATSGHAYAHPSNLFWKLLHSSGCTDRRLEPREDVDLPRlYRMGNTNIVARPSRDAAEL 106
Cdd:cd10028    1 LPDLLAPGLDVLFCGINPGLRSAAVGHHYAHPGNRFWPLLHESGLTPRLLTPEEDRRLPE-YGIGLTNLVKRPTASAAEL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398398678 107 SKAESAAGTPILEEKIRKFRPEAVCIVGKGIWESIWRwrygrnIRKDEFRYGWQDERekmgkteDWEGAWVFVATATSGL 186
Cdd:cd10028   80 SKAELRAGVPRLLAKIARYRPRVVAFVGKGAYRAFFG------RLKKKAAYGLQPET-------GIGGTRVFVLPSTSGL 146

                        170
                 ....*....|....
gi 398398678 187 AASLRPHEKEAIWK 200
Cdd:cd10028  147 NAHYSLEDKLEPWR 160
mug TIGR00584
mismatch-specific thymine-DNA glycosylate (mug); All proteins in this family for whcih ...
 27-188 2.46e-36

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: 129.79  E-value: 2.46e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398398678   27 LTDILTPNLICVFVGFNPGVRTATSGHAYAHPSNLFWKLLHSSGCTDRRLEPREDVDLPRLYRMGNTNIVARPSRDAAEL 106
Cdd:TIGR00584 123 LPDILTFNLDIVIIGINPGLMAAYKGHHYPGPGNHFWKCLFMSGLSEVQLNHMDDHTLPGKYGIGFTNMVERTTPGSKDL 202

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398398678  107 SKAESAAGTPILEEKIRKFRPEAVCIVGKGIWESIWRWRYGRNIRKDEFryGWQDerEKMGKTEdwegAWVFVATATSGL 186
Cdd:TIGR00584 203 SSKEFREGGRILVQKLQKYQPRIAVFNGKCIYEIFSKEVFGVKVKNLEF--GLQP--HKIPDTE----TLCYVMPSSSAR 274


                  ..
gi 398398678  187 AA 188
Cdd:TIGR00584 275 CA 276
PRK10201 PRK10201
G/U mismatch-specific DNA glycosylase;
27-172 3.05e-31

G/U mismatch-specific DNA glycosylase;


Pssm-ID: 182301  Cd Length: 168  Bit Score: 112.14  E-value: 3.05e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398398678  27 LTDILTPNLICVFVGFNPGVRTATSGHAYAHPSNLFWKLLHSSGCTDRRLEPREDVDLPRlYRMGNTNIVARPSRDAAEL 106
Cdd:PRK10201   2 VEDILAPGLRVVFCGINPGLSSAHTGFPFAHPANRFWKVIHQAGFTDRQLKPEEAQHLLD-TRCGVTKLVDRPTVQANEV 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 398398678 107 SKAESAAGTPILEEKIRKFRPEAVCIVGKGIWESIWRwrygrnIRKDEfrygWQDEREKMGKTEDW 172
Cdd:PRK10201  81 SKQELRSGGRKLIEKIEDYQPQALAVLGKQAYEQGFS------QRGAQ----WGKQTLTIGSTQVW 136
Mug COG3663
G:T/U-mismatch repair DNA glycosylase [Replication, recombination and repair];
27-202 2.25e-28

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


Pssm-ID: 442880  Cd Length: 157  Bit Score: 104.09  E-value: 2.25e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398398678  27 LTDILTPNLICVFVGFNPGVRTATSGHAYAHPSNLFWKLLHSSGCTDRRL-EPREDVDLPRlYRMGNTNIVARPSRDAAE 105
Cdd:COG3663    1 LPPVLAPGLRVLILGSNPGLASLAAGFYYAHPRNRFWPILGAAGGTDPRLdYPERKAFLLE-HGIGLWDVVARCTRRAGS 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398398678 106 LSKAESAAGTPILEEkIRKFRP--EAVCIVGKGIWESIwrwrygrnirkdeFRY-GWQDERekmgktedWEGAWVFVATA 182
Cdd:COG3663   80 LDSAIRNAGPNDLAA-LLRYRPriKTVAFNGKTAYRLF-------------FKLvAPQPET--------IGGIELWVLPS 137

                        170       180
                 ....*....|....*....|
gi 398398678 183 TSGLAASLRPHEKEAIWKPF 202
Cdd:COG3663  138 PSPANARFSLEEKLAAWREL 157
UDG pfam03167
Uracil DNA glycosylase superfamily;
38-200 1.08e-21

Uracil DNA glycosylase superfamily;


Pssm-ID: 397331  Cd Length: 154  Bit Score: 87.02  E-value: 1.08e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398398678   38 VFVGFNPGVRTATSGHAY-AHPSNLFWKLLHSSGCTdRRLEPREDVdlprlyrmGNTNIVARPSRDAAELSKAESAAGTP 116
Cdd:pfam03167  11 LIVGEAPGADEDATGLPFvGRAGNLLWKLLNAAGLT-RDLFSPQGV--------YITNVVKCRPGNRRKPTSHEIDACWP 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398398678  117 ILEEKIRKFRPEAVCIVGKGIWESIWRWRYGRNIRkdefrygwqderekmGKTEDWEGAWVFVATATSGL-AASLRPHEK 195
Cdd:pfam03167  82 YLEAEIELLRPRVIVLLGKTAAKALLGLKKITKLR---------------GKLIDLKGIPVLPTPHPSPLlRNKLNPFLK 146


                  ....*
gi 398398678  196 EAIWK 200
Cdd:pfam03167 147 ANAWE 151
UDG-like cd09593
uracil-DNA glycosylases (UDG) and related enzymes; Uracil-DNA glycosylases (UDGs) initiate ...
 37-135 6.80e-11

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: 57.40  E-value: 6.80e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398398678  37 CVFVGFNPGVRTA-TSGHAYAHPSNLFWKLLHSSGCTDRrlepredvdlPRLYRMGNTNIVARPSRDAAELS-KAESAAG 114
Cdd:cd09593    1 VLIVGQNPGPHGArAGGVPPGPSGNRLWRLLAAAGGTPR----------LFRYGVGLTNTVPRGPPGAAAGSeKKELRFC 70

                         90       100
                 ....*....|....*....|.
gi 398398678 115 TPILEEKIRKFRPEAVCIVGK 135
Cdd:cd09593   71 GRWLRKLLELLNPRVVVLLGK 91
UDG smart00986
Uracil DNA glycosylase superfamily;
38-199 1.44e-07

Uracil DNA glycosylase superfamily;


Pssm-ID: 214956  Cd Length: 156  Bit Score: 49.31  E-value: 1.44e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398398678    38 VFVGFNPGVRTA-TSGHAYAHPSNLFWKLLHSSGctDRRLEPREdvdlprlyrmgnTNIVAR--PSRDAAELSKAESAA- 113
Cdd:smart00986  11 LIVGQAPGASEEdRGGPFVGAAGLLLSVMLGVAG--LPRLPPYL------------TNIVKCrpPDAGNRRPTSWELQGc 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398398678   114 GTPILEEKIRKFRPEAVCIVGKGIWESIWRWRYGRNIrkdEFRYGWQDEREkmgktedWEGAWVFVATATSGLAASLRPH 193
Cdd:smart00986  77 LLPWLTVELALARPHLILLLGKFAAQALLGLLRRPLV---FGLRGRVAQLK-------GKGHRVLPLPHPSPLNRNFFPA 146


                   ....*.
gi 398398678   194 EKEAIW 199
Cdd:smart00986 147 KKFAAW 152
 
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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