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Conserved domains on  [gi|1391723917|ref|NP_001350541|]
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G/T mismatch-specific thymine DNA glycosylase isoform 2 [Homo sapiens]

Protein Classification

uracil-DNA glycosylase family protein( domain architecture ID 1526)

uracil-DNA glycosylase family protein may be a DNA repair enzyme that catalyzes the removal of mismatched uracil from DNA to initiate DNA base excision repair pathway

EC:  3.2.2.-
PubMed:  11178247|19909758
SCOP:  4003607

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
UDG-like super family cl00483
uracil-DNA glycosylases (UDG) and related enzymes; Uracil-DNA glycosylases (UDGs) initiate ...
 1-186 2.23e-136

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.


The actual alignment was detected with superfamily member TIGR00584:

Pssm-ID: 444933  Cd Length: 328  Bit Score: 387.49  E-value: 2.23e-136
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723917   1 MAAYKGHHYPGPGNHFWKCLFMSGLSEVQLNHMDDHTLPGKYGIGFTNMVERTTPGSKDLSSKEFREGGRILVQKLQKYQ 80
Cdd:TIGR00584 143 MAAYKGHHYPGPGNHFWKCLFMSGLSEVQLNHMDDHTLPGKYGIGFTNMVERTTPGSKDLSSKEFREGGRILVQKLQKYQ 222

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723917  81 PRIAVFNGKCIYEIFSKEVFGVKVKNLEFGLQPHKIPDTETLCYVMPSSSARCAQFPRAQDKVHYYIKLKDLRDQLKGIE 160
Cdd:TIGR00584 223 PRIAVFNGKCIYEIFSKEVFGVKVKNLEFGLQPHKIPDTETLCYVMPSSSARCAQFPRAQDKVHYYIKLKDLRDQLKGIE 302

                         170       180
                  ....*....|....*....|....*.
gi 1391723917 161 RNMDVQEVQYTFDLQLAQEDAKKMAV 186
Cdd:TIGR00584 303 RNLDVQEVQYTFDLQLAQEDAKKMAV 328
 
Name Accession Description Interval E-value
mug TIGR00584
mismatch-specific thymine-DNA glycosylate (mug); All proteins in this family for whcih ...
 1-186 2.23e-136

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: 387.49  E-value: 2.23e-136
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723917   1 MAAYKGHHYPGPGNHFWKCLFMSGLSEVQLNHMDDHTLPGKYGIGFTNMVERTTPGSKDLSSKEFREGGRILVQKLQKYQ 80
Cdd:TIGR00584 143 MAAYKGHHYPGPGNHFWKCLFMSGLSEVQLNHMDDHTLPGKYGIGFTNMVERTTPGSKDLSSKEFREGGRILVQKLQKYQ 222

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723917  81 PRIAVFNGKCIYEIFSKEVFGVKVKNLEFGLQPHKIPDTETLCYVMPSSSARCAQFPRAQDKVHYYIKLKDLRDQLKGIE 160
Cdd:TIGR00584 223 PRIAVFNGKCIYEIFSKEVFGVKVKNLEFGLQPHKIPDTETLCYVMPSSSARCAQFPRAQDKVHYYIKLKDLRDQLKGIE 302

                         170       180
                  ....*....|....*....|....*.
gi 1391723917 161 RNMDVQEVQYTFDLQLAQEDAKKMAV 186
Cdd:TIGR00584 303 RNLDVQEVQYTFDLQLAQEDAKKMAV 328
UDG-F2_TDG_MUG cd10028
Uracil DNA glycosylase family 2, includes thymine DNA glycosylase, mismatch-specific uracil ...
 1-150 3.31e-63

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: 195.39  E-value: 3.31e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723917   1 MAAYKGHHYPGPGNHFWKCLFMSGLSEVQLNHMDDHTLPgKYGIGFTNMVERTTPGSKDLSSKEFREGGRILVQKLQKYQ 80
Cdd:cd10028    21 RSAAVGHHYAHPGNRFWPLLHESGLTPRLLTPEEDRRLP-EYGIGLTNLVKRPTASAAELSKAELRAGVPRLLAKIARYR 99

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723917  81 PRIAVFNGKCIYEIFskevFGVKVKNLEFGLQPHKIPDtETLCYVMPSSSARCAQFPRAqDKVHYYIKLK 150
Cdd:cd10028   100 PRVVAFVGKGAYRAF----FGRLKKKAAYGLQPETGIG-GTRVFVLPSTSGLNAHYSLE-DKLEPWRELA 163
Mug COG3663
G:T/U-mismatch repair DNA glycosylase [Replication, recombination and repair];
5-149 3.26e-23

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


Pssm-ID: 442880  Cd Length: 157  Bit Score: 92.53  E-value: 3.26e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723917   5 KGHHYPGPGNHFWKCLFMSGLSEVQLN-HMDDHTLPgKYGIGFTNMVERTTPGSKDLSSKEFREGGRILVQkLQKYQPRI 83
Cdd:COG3663    25 AGFYYAHPRNRFWPILGAAGGTDPRLDyPERKAFLL-EHGIGLWDVVARCTRRAGSLDSAIRNAGPNDLAA-LLRYRPRI 102

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1391723917  84 A--VFNGKCIYEIFSKevfgvkvknlEFGLQPHKIPDTETlcYVMPSSSARCAQFPRAqDKVHYYIKL 149
Cdd:COG3663   103 KtvAFNGKTAYRLFFK----------LVAPQPETIGGIEL--WVLPSPSPANARFSLE-EKLAAWREL 157
PRK10201 PRK10201
G/U mismatch-specific DNA glycosylase;
2-130 6.04e-21

G/U mismatch-specific DNA glycosylase;


Pssm-ID: 182301  Cd Length: 168  Bit Score: 86.72  E-value: 6.04e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723917   2 AAYKGHHYPGPGNHFWKCLFMSGLSEVQLNHMDDHTLPgKYGIGFTNMVERTTPGSKDLSSKEFREGGRILVQKLQKYQP 81
Cdd:PRK10201   23 SAHTGFPFAHPANRFWKVIHQAGFTDRQLKPEEAQHLL-DTRCGVTKLVDRPTVQANEVSKQELRSGGRKLIEKIEDYQP 101

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1391723917  82 RIAVFNGKCIYEifskEVFGvkVKNLEFGLQPHKIPDTETlcYVMPSSS 130
Cdd:PRK10201  102 QALAVLGKQAYE----QGFS--QRGAQWGKQTLTIGSTQV--WVLPNPS 142
UDG pfam03167
Uracil DNA glycosylase superfamily;
5-150 1.82e-14

Uracil DNA glycosylase superfamily;


Pssm-ID: 397331  Cd Length: 154  Bit Score: 68.91  E-value: 1.82e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723917   5 KGHHYPGP-GNHFWKCLFMSGLSEVQLNHmddhtlpgkYGIGFTNMVERTTPGSKDLSSKEFREGGRILVQKLQKYQPRI 83
Cdd:pfam03167  24 TGLPFVGRaGNLLWKLLNAAGLTRDLFSP---------QGVYITNVVKCRPGNRRKPTSHEIDACWPYLEAEIELLRPRV 94

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1391723917  84 AVFNGKCIYEIFSKEVFGVKVKNLEFGLQPHKIpdtetlcYVMPSSSARCAQFPRAQDKVHYYIKLK 150
Cdd:pfam03167  95 IVLLGKTAAKALLGLKKITKLRGKLIDLKGIPV-------LPTPHPSPLLRNKLNPFLKANAWEDLK 154
UDG smart00986
Uracil DNA glycosylase superfamily;
6-142 2.88e-03

Uracil DNA glycosylase superfamily;


Pssm-ID: 214956  Cd Length: 156  Bit Score: 37.37  E-value: 2.88e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723917    6 GHHYPGPGNHFWKCLFMSGLSEVQlnhmddhtLPGKYGIGFTNMVER-TTPGSKDLSSKEFreggRILVQKLQKYQPRIA 84
Cdd:smart00986  26 GPFVGAAGLLLSVMLGVAGLPRLP--------PYLTNIVKCRPPDAGnRRPTSWELQGCLL----PWLTVELALARPHLI 93

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723917   85 VFNGKCIYEIFskevFGVKVKNLEFGLQ--PHKIPDTETLCYVMPSSSARCAQFPRAQDK 142
Cdd:smart00986  94 LLLGKFAAQAL----LGLLRRPLVFGLRgrVAQLKGKGHRVLPLPHPSPLNRNFFPAKKF 149
 
Name Accession Description Interval E-value
mug TIGR00584
mismatch-specific thymine-DNA glycosylate (mug); All proteins in this family for whcih ...
 1-186 2.23e-136

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: 387.49  E-value: 2.23e-136
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723917   1 MAAYKGHHYPGPGNHFWKCLFMSGLSEVQLNHMDDHTLPGKYGIGFTNMVERTTPGSKDLSSKEFREGGRILVQKLQKYQ 80
Cdd:TIGR00584 143 MAAYKGHHYPGPGNHFWKCLFMSGLSEVQLNHMDDHTLPGKYGIGFTNMVERTTPGSKDLSSKEFREGGRILVQKLQKYQ 222

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723917  81 PRIAVFNGKCIYEIFSKEVFGVKVKNLEFGLQPHKIPDTETLCYVMPSSSARCAQFPRAQDKVHYYIKLKDLRDQLKGIE 160
Cdd:TIGR00584 223 PRIAVFNGKCIYEIFSKEVFGVKVKNLEFGLQPHKIPDTETLCYVMPSSSARCAQFPRAQDKVHYYIKLKDLRDQLKGIE 302

                         170       180
                  ....*....|....*....|....*.
gi 1391723917 161 RNMDVQEVQYTFDLQLAQEDAKKMAV 186
Cdd:TIGR00584 303 RNLDVQEVQYTFDLQLAQEDAKKMAV 328
UDG-F2_TDG_MUG cd10028
Uracil DNA glycosylase family 2, includes thymine DNA glycosylase, mismatch-specific uracil ...
 1-150 3.31e-63

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: 195.39  E-value: 3.31e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723917   1 MAAYKGHHYPGPGNHFWKCLFMSGLSEVQLNHMDDHTLPgKYGIGFTNMVERTTPGSKDLSSKEFREGGRILVQKLQKYQ 80
Cdd:cd10028    21 RSAAVGHHYAHPGNRFWPLLHESGLTPRLLTPEEDRRLP-EYGIGLTNLVKRPTASAAELSKAELRAGVPRLLAKIARYR 99

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723917  81 PRIAVFNGKCIYEIFskevFGVKVKNLEFGLQPHKIPDtETLCYVMPSSSARCAQFPRAqDKVHYYIKLK 150
Cdd:cd10028   100 PRVVAFVGKGAYRAF----FGRLKKKAAYGLQPETGIG-GTRVFVLPSTSGLNAHYSLE-DKLEPWRELA 163
UDG-like cd09593
uracil-DNA glycosylases (UDG) and related enzymes; Uracil-DNA glycosylases (UDGs) initiate ...
 6-134 4.72e-28

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: 104.01  E-value: 4.72e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723917   6 GHHYPGPGNHFWKCLFMSGLSEVqlnhmddhtlPGKYGIGFTNMVERTTPGSKDLS-SKEFREGGRILVQKLQKYQPRIA 84
Cdd:cd09593    17 GVPPGPSGNRLWRLLAAAGGTPR----------LFRYGVGLTNTVPRGPPGAAAGSeKKELRFCGRWLRKLLELLNPRVV 86

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1391723917  85 VFNGKCIYEIFSKEVFGVKvknlefglqphKIPDTETLCYVMPSSSARCA 134
Cdd:cd09593    87 VLLGKKAQEAYLAVLTSSK-----------GAPGKGTEVLVLPHPSPRNR 125
Mug COG3663
G:T/U-mismatch repair DNA glycosylase [Replication, recombination and repair];
5-149 3.26e-23

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


Pssm-ID: 442880  Cd Length: 157  Bit Score: 92.53  E-value: 3.26e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723917   5 KGHHYPGPGNHFWKCLFMSGLSEVQLN-HMDDHTLPgKYGIGFTNMVERTTPGSKDLSSKEFREGGRILVQkLQKYQPRI 83
Cdd:COG3663    25 AGFYYAHPRNRFWPILGAAGGTDPRLDyPERKAFLL-EHGIGLWDVVARCTRRAGSLDSAIRNAGPNDLAA-LLRYRPRI 102

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1391723917  84 A--VFNGKCIYEIFSKevfgvkvknlEFGLQPHKIPDTETlcYVMPSSSARCAQFPRAqDKVHYYIKL 149
Cdd:COG3663   103 KtvAFNGKTAYRLFFK----------LVAPQPETIGGIEL--WVLPSPSPANARFSLE-EKLAAWREL 157
PRK10201 PRK10201
G/U mismatch-specific DNA glycosylase;
2-130 6.04e-21

G/U mismatch-specific DNA glycosylase;


Pssm-ID: 182301  Cd Length: 168  Bit Score: 86.72  E-value: 6.04e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723917   2 AAYKGHHYPGPGNHFWKCLFMSGLSEVQLNHMDDHTLPgKYGIGFTNMVERTTPGSKDLSSKEFREGGRILVQKLQKYQP 81
Cdd:PRK10201   23 SAHTGFPFAHPANRFWKVIHQAGFTDRQLKPEEAQHLL-DTRCGVTKLVDRPTVQANEVSKQELRSGGRKLIEKIEDYQP 101

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1391723917  82 RIAVFNGKCIYEifskEVFGvkVKNLEFGLQPHKIPDTETlcYVMPSSS 130
Cdd:PRK10201  102 QALAVLGKQAYE----QGFS--QRGAQWGKQTLTIGSTQV--WVLPNPS 142
UDG pfam03167
Uracil DNA glycosylase superfamily;
5-150 1.82e-14

Uracil DNA glycosylase superfamily;


Pssm-ID: 397331  Cd Length: 154  Bit Score: 68.91  E-value: 1.82e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723917   5 KGHHYPGP-GNHFWKCLFMSGLSEVQLNHmddhtlpgkYGIGFTNMVERTTPGSKDLSSKEFREGGRILVQKLQKYQPRI 83
Cdd:pfam03167  24 TGLPFVGRaGNLLWKLLNAAGLTRDLFSP---------QGVYITNVVKCRPGNRRKPTSHEIDACWPYLEAEIELLRPRV 94

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1391723917  84 AVFNGKCIYEIFSKEVFGVKVKNLEFGLQPHKIpdtetlcYVMPSSSARCAQFPRAQDKVHYYIKLK 150
Cdd:pfam03167  95 IVLLGKTAAKALLGLKKITKLRGKLIDLKGIPV-------LPTPHPSPLLRNKLNPFLKANAWEDLK 154
UDG smart00986
Uracil DNA glycosylase superfamily;
6-142 2.88e-03

Uracil DNA glycosylase superfamily;


Pssm-ID: 214956  Cd Length: 156  Bit Score: 37.37  E-value: 2.88e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723917    6 GHHYPGPGNHFWKCLFMSGLSEVQlnhmddhtLPGKYGIGFTNMVER-TTPGSKDLSSKEFreggRILVQKLQKYQPRIA 84
Cdd:smart00986  26 GPFVGAAGLLLSVMLGVAGLPRLP--------PYLTNIVKCRPPDAGnRRPTSWELQGCLL----PWLTVELALARPHLI 93

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723917   85 VFNGKCIYEIFskevFGVKVKNLEFGLQ--PHKIPDTETLCYVMPSSSARCAQFPRAQDK 142
Cdd:smart00986  94 LLLGKFAAQAL----LGLLRRPLVFGLRgrVAQLKGKGHRVLPLPHPSPLNRNFFPAKKF 149
 
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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