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Conserved domains on  [gi|515671983|ref|WP_017104583|]
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MULTISPECIES: uracil-DNA glycosylase family protein [Vibrio]

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 ...
 21-188 1.00e-112

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: 318.26  E-value: 1.00e-112
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671983  21 HGANPVIQAHPNARLLIIGQAPGIKVHQSSIPWNDASGERLREWLGMDSDTFYDEQKVAIVPMGFCYPGKGKSGDLPPRK 100
Cdd:cd10033    2 LGPRPVFQGSPNAKILIIGQAPGRKVHESGIPFNDASGKRLREWLGVSDETFYDPDRFAILPMGFCYPGKGKGGDLPPRK 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671983 101 ECAALWHQKVLQSLPNIQMTLLIGQYAQNYYLKDKATSTLTETVRNWQAWAPEFLPLPHPSPRNNIWLKKNPWFESEVIP 180
Cdd:cd10033   82 ECAPTWHPRLLELLPNPELTILIGRYAQKYYLPKRRKKLLTLTVKNWREYGPKYFPLPHPSPRNNRWLKKNPWFEEEVLP 161


                 ....*...
gi 515671983 181 YIRKHVSE 188
Cdd:cd10033  162 ELRKRVRA 169
 
Name Accession Description Interval E-value
UDG_like cd10033
uncharacterized family of the uracil-DNA glycosylase superfamily; Uracil-DNA glycosylases ...
 21-188 1.00e-112

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: 318.26  E-value: 1.00e-112
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671983  21 HGANPVIQAHPNARLLIIGQAPGIKVHQSSIPWNDASGERLREWLGMDSDTFYDEQKVAIVPMGFCYPGKGKSGDLPPRK 100
Cdd:cd10033    2 LGPRPVFQGSPNAKILIIGQAPGRKVHESGIPFNDASGKRLREWLGVSDETFYDPDRFAILPMGFCYPGKGKGGDLPPRK 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671983 101 ECAALWHQKVLQSLPNIQMTLLIGQYAQNYYLKDKATSTLTETVRNWQAWAPEFLPLPHPSPRNNIWLKKNPWFESEVIP 180
Cdd:cd10033   82 ECAPTWHPRLLELLPNPELTILIGRYAQKYYLPKRRKKLLTLTVKNWREYGPKYFPLPHPSPRNNRWLKKNPWFEEEVLP 161


                 ....*...
gi 515671983 181 YIRKHVSE 188
Cdd:cd10033  162 ELRKRVRA 169
UDG smart00986
Uracil DNA glycosylase superfamily;
31-183 1.75e-31

Uracil DNA glycosylase superfamily;


Pssm-ID: 214956  Cd Length: 156  Bit Score: 111.71  E-value: 1.75e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671983    31 PNARLLIIGQAPGIKVHQSSIPWNDASGERLREWLGmdsDTFYDEQKVAIVPMGFCYPGK--GKSGDLPPRKECAALWHQ 108
Cdd:smart00986   6 PNAKVLIVGQAPGASEEDRGGPFVGAAGLLLSVMLG---VAGLPRLPPYLTNIVKCRPPDagNRRPTSWELQGCLLPWLT 82

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515671983   109 kVLQSLPNIQMTLLIGQYAQNYYLK---DKATSTLTETVRNWQAWAPEFLPLPHPSPRNNIWlkkNPWFESEVIPYIR 183
Cdd:smart00986  83 -VELALARPHLILLLGKFAAQALLGllrRPLVFGLRGRVAQLKGKGHRVLPLPHPSPLNRNF---FPAKKFAAWNDLL 156
UDG pfam03167
Uracil DNA glycosylase superfamily;
31-175 1.64e-28

Uracil DNA glycosylase superfamily;


Pssm-ID: 397331  Cd Length: 154  Bit Score: 103.97  E-value: 1.64e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671983   31 PNARLLIIGQAPGIKVHQSSIPWNDASGERLREWL---GMDSDTFYDeQKVAIVPMGFCYPGKGKsgdLPPRKECAALW- 106
Cdd:pfam03167   6 PNAKVLIVGEAPGADEDATGLPFVGRAGNLLWKLLnaaGLTRDLFSP-QGVYITNVVKCRPGNRR---KPTSHEIDACWp 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515671983  107 -HQKVLQSLPNiQMTLLIGQYAQNYYLKDKATSTLTETVRNWQawAPEFLPLPHPSPRN----NIWLKKNPWFE 175
Cdd:pfam03167  82 yLEAEIELLRP-RVIVLLGKTAAKALLGLKKITKLRGKLIDLK--GIPVLPTPHPSPLLrnklNPFLKANAWED 152
Udg4 COG1573
Uracil-DNA glycosylase [Replication, recombination and repair];
4-161 9.87e-07

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


Pssm-ID: 441181  Cd Length: 189  Bit Score: 47.11  E-value: 9.87e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671983   4 SLLTEIRQCTACEphLSHGA-NPVI-QAHPNARLLIIGQAPGIKVHQSSIPWNDASGERLREWL---GMDSDTFYdeqKV 78
Cdd:COG1573   12 ELREAVAACRRCP--LVETRtQPVFgEGDPDARLMIVGEAPGAGEDRTGRPFVGRAGQLLDKMLaaaGLAREDVY---IT 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671983  79 AIVPmgfCYPGKGKSgdlPPRKECAA----LWHQ------KVLqslpniqmtLLIGQYAQNYYLKDKAtsTLTETVRNWQ 148
Cdd:COG1573   87 NAVK---CRPPGNRK---PTPEEIAAcrpfLEREialirpKVI---------VALGATAAQALLGAGE--RITRLRGKWH 149

                        170
                 ....*....|....*
gi 515671983 149 AWAPEF--LPLPHPS 161
Cdd:COG1573  150 ELPGGIplLPTYHPS 164
 
Name Accession Description Interval E-value
UDG_like cd10033
uncharacterized family of the uracil-DNA glycosylase superfamily; Uracil-DNA glycosylases ...
 21-188 1.00e-112

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: 318.26  E-value: 1.00e-112
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671983  21 HGANPVIQAHPNARLLIIGQAPGIKVHQSSIPWNDASGERLREWLGMDSDTFYDEQKVAIVPMGFCYPGKGKSGDLPPRK 100
Cdd:cd10033    2 LGPRPVFQGSPNAKILIIGQAPGRKVHESGIPFNDASGKRLREWLGVSDETFYDPDRFAILPMGFCYPGKGKGGDLPPRK 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671983 101 ECAALWHQKVLQSLPNIQMTLLIGQYAQNYYLKDKATSTLTETVRNWQAWAPEFLPLPHPSPRNNIWLKKNPWFESEVIP 180
Cdd:cd10033   82 ECAPTWHPRLLELLPNPELTILIGRYAQKYYLPKRRKKLLTLTVKNWREYGPKYFPLPHPSPRNNRWLKKNPWFEEEVLP 161


                 ....*...
gi 515671983 181 YIRKHVSE 188
Cdd:cd10033  162 ELRKRVRA 169
UDG smart00986
Uracil DNA glycosylase superfamily;
31-183 1.75e-31

Uracil DNA glycosylase superfamily;


Pssm-ID: 214956  Cd Length: 156  Bit Score: 111.71  E-value: 1.75e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671983    31 PNARLLIIGQAPGIKVHQSSIPWNDASGERLREWLGmdsDTFYDEQKVAIVPMGFCYPGK--GKSGDLPPRKECAALWHQ 108
Cdd:smart00986   6 PNAKVLIVGQAPGASEEDRGGPFVGAAGLLLSVMLG---VAGLPRLPPYLTNIVKCRPPDagNRRPTSWELQGCLLPWLT 82

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515671983   109 kVLQSLPNIQMTLLIGQYAQNYYLK---DKATSTLTETVRNWQAWAPEFLPLPHPSPRNNIWlkkNPWFESEVIPYIR 183
Cdd:smart00986  83 -VELALARPHLILLLGKFAAQALLGllrRPLVFGLRGRVAQLKGKGHRVLPLPHPSPLNRNF---FPAKKFAAWNDLL 156
UDG pfam03167
Uracil DNA glycosylase superfamily;
31-175 1.64e-28

Uracil DNA glycosylase superfamily;


Pssm-ID: 397331  Cd Length: 154  Bit Score: 103.97  E-value: 1.64e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671983   31 PNARLLIIGQAPGIKVHQSSIPWNDASGERLREWL---GMDSDTFYDeQKVAIVPMGFCYPGKGKsgdLPPRKECAALW- 106
Cdd:pfam03167   6 PNAKVLIVGEAPGADEDATGLPFVGRAGNLLWKLLnaaGLTRDLFSP-QGVYITNVVKCRPGNRR---KPTSHEIDACWp 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515671983  107 -HQKVLQSLPNiQMTLLIGQYAQNYYLKDKATSTLTETVRNWQawAPEFLPLPHPSPRN----NIWLKKNPWFE 175
Cdd:pfam03167  82 yLEAEIELLRP-RVIVLLGKTAAKALLGLKKITKLRGKLIDLK--GIPVLPTPHPSPLLrnklNPFLKANAWED 152
UDG-like cd09593
uracil-DNA glycosylases (UDG) and related enzymes; Uracil-DNA glycosylases (UDGs) initiate ...
 35-164 3.53e-23

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: 89.37  E-value: 3.53e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671983  35 LLIIGQAPGIKVHQSSIPWNDASGERLREWLGMDSDTF-YDEQKVAIVPMGFCYPGKGKSGDLPPRKECAALWHQKVLQS 113
Cdd:cd09593    1 VLIVGQNPGPHGARAGGVPPGPSGNRLWRLLAAAGGTPrLFRYGVGLTNTVPRGPPGAAAGSEKKELRFCGRWLRKLLEL 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 515671983 114 LpNIQMTLLIGQYAQNYYLKDKATSTLTETVRnwqawaPEFLPLPHPSPRN 164
Cdd:cd09593   81 L-NPRVVVLLGKKAQEAYLAVLTSSKGAPGKG------TEVLVLPHPSPRN 124
Udg4 COG1573
Uracil-DNA glycosylase [Replication, recombination and repair];
4-161 9.87e-07

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


Pssm-ID: 441181  Cd Length: 189  Bit Score: 47.11  E-value: 9.87e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671983   4 SLLTEIRQCTACEphLSHGA-NPVI-QAHPNARLLIIGQAPGIKVHQSSIPWNDASGERLREWL---GMDSDTFYdeqKV 78
Cdd:COG1573   12 ELREAVAACRRCP--LVETRtQPVFgEGDPDARLMIVGEAPGAGEDRTGRPFVGRAGQLLDKMLaaaGLAREDVY---IT 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671983  79 AIVPmgfCYPGKGKSgdlPPRKECAA----LWHQ------KVLqslpniqmtLLIGQYAQNYYLKDKAtsTLTETVRNWQ 148
Cdd:COG1573   87 NAVK---CRPPGNRK---PTPEEIAAcrpfLEREialirpKVI---------VALGATAAQALLGAGE--RITRLRGKWH 149

                        170
                 ....*....|....*
gi 515671983 149 AWAPEF--LPLPHPS 161
Cdd:COG1573  150 ELPGGIplLPTYHPS 164
UDG-F4_TTUDGA_SPO1dp_like cd10030
Uracil DNA glycosylase family 4, includes Thermotoga maritima TTUDGA, Bacillus phage SPO1 DNA ...
 12-161 1.45e-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: 1.45e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671983  12 CTACEphLSHGA-NPVI-QAHPNARLLIIGQAPGIKVHQSSIPWNDASGERLREWL---GMDSDTFYdeqkVA-IVPmgf 85
Cdd:cd10030    1 CTRCP--LSKTRtNVVFgEGNPDAKLMFIGEAPGAEEDRQGRPFVGRAGKLLDKMLaaiGLSREDVY----ITnVVK--- 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515671983  86 CYPGKGKSgdlPPRKECAA----LWHQ------KVLqslpniqmtLLIGQYAQNYYLKDKAtsTLTETVRNWQAWAPEF- 154
Cdd:cd10030   72 CRPPGNRT---PTPEEIAAcrpfLDRQielikpKVI---------VTLGRTAAQALLGKDA--PISKLRGKWHEYEKGIp 137


                 ....*...
gi 515671983 155 -LPLPHPS 161
Cdd:cd10030  138 vLPTYHPA 145
 
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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