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Conserved domains on  [gi|2544150864|ref|WP_299962208|]
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uracil-DNA glycosylase family protein [uncultured Roseobacter sp.]

Protein Classification

uracil-DNA glycosylase family protein( domain architecture ID 10178257)

uracil-DNA glycosylase family protein similar to Haemophilus influenzae uncharacterized protein HI_0220.2

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
UDG_like cd10033
uncharacterized family of the uracil-DNA glycosylase superfamily; Uracil-DNA glycosylases ...
 22-192 6.31e-93

uncharacterized family of the uracil-DNA glycosylase superfamily; Uracil-DNA glycosylases (UDGs) initiate repair of uracils in DNA. Uracil may arise from mis-incorporation 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: 381683  Cd Length: 171  Bit Score: 268.57  E-value: 6.31e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544150864  22 PLGPRPIFQLDQEARILIVGQAPGRITHAKGRPFDDPSGDRLRSWLAVDKPTFYTDPRIGIFPMGLCFPGTGSGGDLPPP 101
Cdd:cd10033     1 PLGPRPVFQGSPNAKILIIGQAPGRKVHESGIPFNDASGKRLREWLGVSDETFYDPDRFAILPMGFCYPGKGKGGDLPPR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544150864 102 KICATTWRSSVMQKLEQVELTLILGAYAIAWHLPDLRGKPVTEAVRQASEGNGNMFVLPHPSPRNNRWLKQNAWFEADVV 181
Cdd:cd10033    81 KECAPTWHPRLLELLPNPELTILIGRYAQKYYLPKRRKKLLTLTVKNWREYGPKYFPLPHPSPRNNRWLKKNPWFEEEVL 160

                         170
                  ....*....|.
gi 2544150864 182 PRIQENVRRIL 192
Cdd:cd10033   161 PELRKRVRAIL 171
 
Name Accession Description Interval E-value
UDG_like cd10033
uncharacterized family of the uracil-DNA glycosylase superfamily; Uracil-DNA glycosylases ...
 22-192 6.31e-93

uncharacterized family of the uracil-DNA glycosylase superfamily; Uracil-DNA glycosylases (UDGs) initiate repair of uracils in DNA. Uracil may arise from mis-incorporation 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: 381683  Cd Length: 171  Bit Score: 268.57  E-value: 6.31e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544150864  22 PLGPRPIFQLDQEARILIVGQAPGRITHAKGRPFDDPSGDRLRSWLAVDKPTFYTDPRIGIFPMGLCFPGTGSGGDLPPP 101
Cdd:cd10033     1 PLGPRPVFQGSPNAKILIIGQAPGRKVHESGIPFNDASGKRLREWLGVSDETFYDPDRFAILPMGFCYPGKGKGGDLPPR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544150864 102 KICATTWRSSVMQKLEQVELTLILGAYAIAWHLPDLRGKPVTEAVRQASEGNGNMFVLPHPSPRNNRWLKQNAWFEADVV 181
Cdd:cd10033    81 KECAPTWHPRLLELLPNPELTILIGRYAQKYYLPKRRKKLLTLTVKNWREYGPKYFPLPHPSPRNNRWLKKNPWFEEEVL 160

                         170
                  ....*....|.
gi 2544150864 182 PRIQENVRRIL 192
Cdd:cd10033   161 PELRKRVRAIL 171
UDG pfam03167
Uracil DNA glycosylase superfamily;
28-177 2.01e-25

Uracil DNA glycosylase superfamily;


Pssm-ID: 397331  Cd Length: 154  Bit Score: 96.26  E-value: 2.01e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544150864  28 IFQLDQEARILIVGQAPGRITHAKGRPFDDPSGDRLRSWLA---VDKPTFYTDpRIGIFPMGLCFPGtgsGGDLPPPKIC 104
Cdd:pfam03167   1 PGFGPPNAKVLIVGEAPGADEDATGLPFVGRAGNLLWKLLNaagLTRDLFSPQ-GVYITNVVKCRPG---NRRKPTSHEI 76

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2544150864 105 ATTWRsSVMQKLEQVELTLI--LGAYAIAWHLPDLRGKPVTEAVRQAseGNGNMFVLPHPSPRN----NRWLKQNAWFE 177
Cdd:pfam03167  77 DACWP-YLEAEIELLRPRVIvlLGKTAAKALLGLKKITKLRGKLIDL--KGIPVLPTPHPSPLLrnklNPFLKANAWED 152
UDG smart00986
Uracil DNA glycosylase superfamily;
29-185 1.48e-24

Uracil DNA glycosylase superfamily;


Pssm-ID: 214956  Cd Length: 156  Bit Score: 93.99  E-value: 1.48e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544150864   29 FQLDQEARILIVGQAPGRITHAKGRPFDDPSGDRLRSWLAVdkpTFYTDPRIGIFPMGLCFPGTGSGGDL--PPPKICAT 106
Cdd:smart00986   2 GTGDPNAKVLIVGQAPGASEEDRGGPFVGAAGLLLSVMLGV---AGLPRLPPYLTNIVKCRPPDAGNRRPtsWELQGCLL 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544150864  107 TWRsSVMQKLEQVELTLILGAYAIAWHLPDLRGKPVTEAVRQASEGNGNM---FVLPHPSPRNNRWlkqNAWFEADVVPR 183
Cdd:smart00986  79 PWL-TVELALARPHLILLLGKFAAQALLGLLRRPLVFGLRGRVAQLKGKGhrvLPLPHPSPLNRNF---FPAKKFAAWND 154


                   ..
gi 2544150864  184 IQ 185
Cdd:smart00986 155 LL 156
Udg4 COG1573
Uracil-DNA glycosylase [Replication, recombination and repair];
1-68 2.61e-07

Uracil-DNA glycosylase [Replication, recombination and repair];


Pssm-ID: 441181  Cd Length: 189  Bit Score: 48.65  E-value: 2.61e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2544150864   1 MPKDLQTLTSDMLACTLCqdlPLGP---RPIF-QLDQEARILIVGQAPGRITHAKGRPFDDPSGDRLRSWLA 68
Cdd:COG1573     6 AAETLEELREAVAACRRC---PLVEtrtQPVFgEGDPDARLMIVGEAPGAGEDRTGRPFVGRAGQLLDKMLA 74
UDG_fam4 TIGR00758
uracil-DNA glycosylase, family 4; This well-conserved family of proteins is about 200 residues ...
 34-69 1.52e-03

uracil-DNA glycosylase, family 4; This well-conserved family of proteins is about 200 residues in length and homologous to the N-terminus of the DNA polymerase of phage SPO1 of Bacillus subtilis. The member from Thermus thermophilus HB8 is known to act as uracil-DNA glycosylase, an enzyme of DNA base excision repair. Its appearance as a domain of phage DNA polymerases could be consistent with uracil-DNA glycosylase activity. [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 129841  Cd Length: 173  Bit Score: 37.78  E-value: 1.52e-03
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 2544150864  34 EARILIVGQAPGRITHAKGRPFDDPSGDRLRSWLAV 69
Cdd:TIGR00758  21 DANIMFVGEAPGREEDRKGRPFVGRAGKLLDEMLAA 56
 
Name Accession Description Interval E-value
UDG_like cd10033
uncharacterized family of the uracil-DNA glycosylase superfamily; Uracil-DNA glycosylases ...
 22-192 6.31e-93

uncharacterized family of the uracil-DNA glycosylase superfamily; Uracil-DNA glycosylases (UDGs) initiate repair of uracils in DNA. Uracil may arise from mis-incorporation 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: 381683  Cd Length: 171  Bit Score: 268.57  E-value: 6.31e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544150864  22 PLGPRPIFQLDQEARILIVGQAPGRITHAKGRPFDDPSGDRLRSWLAVDKPTFYTDPRIGIFPMGLCFPGTGSGGDLPPP 101
Cdd:cd10033     1 PLGPRPVFQGSPNAKILIIGQAPGRKVHESGIPFNDASGKRLREWLGVSDETFYDPDRFAILPMGFCYPGKGKGGDLPPR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544150864 102 KICATTWRSSVMQKLEQVELTLILGAYAIAWHLPDLRGKPVTEAVRQASEGNGNMFVLPHPSPRNNRWLKQNAWFEADVV 181
Cdd:cd10033    81 KECAPTWHPRLLELLPNPELTILIGRYAQKYYLPKRRKKLLTLTVKNWREYGPKYFPLPHPSPRNNRWLKKNPWFEEEVL 160

                         170
                  ....*....|.
gi 2544150864 182 PRIQENVRRIL 192
Cdd:cd10033   161 PELRKRVRAIL 171
UDG pfam03167
Uracil DNA glycosylase superfamily;
28-177 2.01e-25

Uracil DNA glycosylase superfamily;


Pssm-ID: 397331  Cd Length: 154  Bit Score: 96.26  E-value: 2.01e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544150864  28 IFQLDQEARILIVGQAPGRITHAKGRPFDDPSGDRLRSWLA---VDKPTFYTDpRIGIFPMGLCFPGtgsGGDLPPPKIC 104
Cdd:pfam03167   1 PGFGPPNAKVLIVGEAPGADEDATGLPFVGRAGNLLWKLLNaagLTRDLFSPQ-GVYITNVVKCRPG---NRRKPTSHEI 76

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2544150864 105 ATTWRsSVMQKLEQVELTLI--LGAYAIAWHLPDLRGKPVTEAVRQAseGNGNMFVLPHPSPRN----NRWLKQNAWFE 177
Cdd:pfam03167  77 DACWP-YLEAEIELLRPRVIvlLGKTAAKALLGLKKITKLRGKLIDL--KGIPVLPTPHPSPLLrnklNPFLKANAWED 152
UDG smart00986
Uracil DNA glycosylase superfamily;
29-185 1.48e-24

Uracil DNA glycosylase superfamily;


Pssm-ID: 214956  Cd Length: 156  Bit Score: 93.99  E-value: 1.48e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544150864   29 FQLDQEARILIVGQAPGRITHAKGRPFDDPSGDRLRSWLAVdkpTFYTDPRIGIFPMGLCFPGTGSGGDL--PPPKICAT 106
Cdd:smart00986   2 GTGDPNAKVLIVGQAPGASEEDRGGPFVGAAGLLLSVMLGV---AGLPRLPPYLTNIVKCRPPDAGNRRPtsWELQGCLL 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544150864  107 TWRsSVMQKLEQVELTLILGAYAIAWHLPDLRGKPVTEAVRQASEGNGNM---FVLPHPSPRNNRWlkqNAWFEADVVPR 183
Cdd:smart00986  79 PWL-TVELALARPHLILLLGKFAAQALLGLLRRPLVFGLRGRVAQLKGKGhrvLPLPHPSPLNRNF---FPAKKFAAWND 154


                   ..
gi 2544150864  184 IQ 185
Cdd:smart00986 155 LL 156
UDG-like cd09593
uracil-DNA glycosylases (UDG) and related enzymes; Uracil-DNA glycosylases (UDGs) initiate ...
 37-166 1.21e-17

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: 75.12  E-value: 1.21e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544150864  37 ILIVGQAPGRITHAKGRPFDDPSGDRLRSWLAVDKPTF-YTDPRIGIFPMGLCFPGTGSGGDLPPPKICATTWRSSVMQK 115
Cdd:cd09593     1 VLIVGQNPGPHGARAGGVPPGPSGNRLWRLLAAAGGTPrLFRYGVGLTNTVPRGPPGAAAGSEKKELRFCGRWLRKLLEL 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2544150864 116 LeQVELTLILGAYAiawhlpDLRGKPVTEAVRQASEGNGNMFVLPHPSPRN 166
Cdd:cd09593    81 L-NPRVVVLLGKKA------QEAYLAVLTSSKGAPGKGTEVLVLPHPSPRN 124
Udg4 COG1573
Uracil-DNA glycosylase [Replication, recombination and repair];
1-68 2.61e-07

Uracil-DNA glycosylase [Replication, recombination and repair];


Pssm-ID: 441181  Cd Length: 189  Bit Score: 48.65  E-value: 2.61e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2544150864   1 MPKDLQTLTSDMLACTLCqdlPLGP---RPIF-QLDQEARILIVGQAPGRITHAKGRPFDDPSGDRLRSWLA 68
Cdd:COG1573     6 AAETLEELREAVAACRRC---PLVEtrtQPVFgEGDPDARLMIVGEAPGAGEDRTGRPFVGRAGQLLDKMLA 74
UDG-F4_TTUDGA_SPO1dp_like cd10030
Uracil DNA glycosylase family 4, includes Thermotoga maritima TTUDGA, Bacillus phage SPO1 DNA ...
 15-68 1.40e-04

Uracil DNA glycosylase family 4, includes Thermotoga maritima TTUDGA, Bacillus phage SPO1 DNA polymerase, and similar proteins; Uracil DNA glycosylase family 4 includes Thermotoga maritima TTUDGA, a robust uracil DNA glycosylase that shares narrow substrate specificity and high catalytic efficiency with family 1, acting on double-stranded and single-stranded uracil-containing DNA. Members of this family possess four conserved cysteine residues required to coordinate the [4Fe-4S] iron-sulfur cluster. This family also includes the N-terminal domain of Bacillus phage SPO1 DNA polymerase. Bacteriophage SPO1 is one of a group of large, lytic, tailed bacteriophages of Bacillus subtilis, and contains hydroxymethyluracil (hmUra) in place of thymine in their DNA. It has been speculated that this UDG domain may help discriminate between hmUra containing SPO1 DNA and thymine-containing host DNA. Uracil-DNA glycosylases (UDGs) initiate repair of uracils in DNA. Uracil in DNA can arise as a result of mis-incorporation 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: 381680  Cd Length: 165  Bit Score: 40.51  E-value: 1.40e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2544150864  15 CTLCQDLPLGPRPIF-QLDQEARILIVGQAPGRITHAKGRPFDDPSGDRLRSWLA 68
Cdd:cd10030     1 CTRCPLSKTRTNVVFgEGNPDAKLMFIGEAPGAEEDRQGRPFVGRAGKLLDKMLA 55
UDG_fam4 TIGR00758
uracil-DNA glycosylase, family 4; This well-conserved family of proteins is about 200 residues ...
 34-69 1.52e-03

uracil-DNA glycosylase, family 4; This well-conserved family of proteins is about 200 residues in length and homologous to the N-terminus of the DNA polymerase of phage SPO1 of Bacillus subtilis. The member from Thermus thermophilus HB8 is known to act as uracil-DNA glycosylase, an enzyme of DNA base excision repair. Its appearance as a domain of phage DNA polymerases could be consistent with uracil-DNA glycosylase activity. [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 129841  Cd Length: 173  Bit Score: 37.78  E-value: 1.52e-03
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 2544150864  34 EARILIVGQAPGRITHAKGRPFDDPSGDRLRSWLAV 69
Cdd:TIGR00758  21 DANIMFVGEAPGREEDRKGRPFVGRAGKLLDEMLAA 56
UDG-F5_TTUDGB_like cd10031
Uracil DNA glycosylase family 5, includes Thermotoga maritima TTUDGB and similar proteins; ...
 32-67 7.84e-03

Uracil DNA glycosylase family 5, includes Thermotoga maritima TTUDGB and similar proteins; Uracil DNA glycosylase family 5 includes Thermus thermophilus HB8 TTUDGB (also called UDGb) which is not only a UDG acting on double-stranded uracil-containing DNA, but also 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 acting on both, double-stranded and single-stranded xanthine-containing DNA. TTUDGB also excises thymine from G:T mismatched DNA, and removes analogs of uracil from DNA, including 5-hydroxymethyluracil (hmU) and 5-fluorouracil (fU). This subfamily also contains Bradyrhizobium diazoefficiens family 5 homolog Blr5068 (UdgB) which has been found to efficiently excise uracil from ssDNA and dsDNA. Uracil-DNA glycosylases (UDGs) initiate repair of uracils in DNA. Similar to family 4 UDGs, members of this family possess four conserved cysteine residues required to coordinate the [4Fe-4S] iron-sulfur cluster. Uracil in DNA can arise as a result of mis-incorporation 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: 381681  Cd Length: 204  Bit Score: 35.91  E-value: 7.84e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 2544150864  32 DQEARILIVGQAPGRitH---AKGRPFD-DPSGDrlrsWL 67
Cdd:cd10031    36 DPNARLLIVGLAPAA--HggnRTGRPFTgDRSGD----FL 69
 
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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