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Conserved domains on  [gi|1720409832|ref|XP_030109635|]
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adenine DNA glycosylase isoform X4 [Mus musculus]

Protein Classification

DNA_Glycosylase_C domain-containing protein( domain architecture ID 10130797)

DNA_Glycosylase_C domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
MutY super family cl34172
Adenine-specific DNA glycosylase, acts on AG and A-oxoG pairs [Replication, recombination and ...
 1-214 5.23e-43

Adenine-specific DNA glycosylase, acts on AG and A-oxoG pairs [Replication, recombination and repair];


The actual alignment was detected with superfamily member COG1194:

Pssm-ID: 440807 [Multi-domain]  Cd Length: 350  Bit Score: 149.13  E-value: 5.23e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409832   1 MELGATVCTPQRPLCSHCPVQSLCRAYQRvqrgqlsalpGRPdieecalntrqcqlcltssspwdpsmgvANFPRKASRR 80
Cdd:COG1194   184 MDLGATVCTPKKPKCLLCPLQDDCAAFAE----------GRQ----------------------------EELPVKKPKK 225

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409832  81 PPREEYSATCVVEQPGAiggplVLLVQRPDSGLLAGLWEFPSVtlEPSEQHQHKALLQELQRWCGpLPAIRLQHLGEVIH 160
Cdd:COG1194   226 KKPERYGAALVIRDDGR-----VLLEKRPPKGLWGGLWEFPEF--EWEEAEDPEALERWLREELG-LEVEWLEPLGTVRH 297

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1720409832 161 IFSHIKLTYQVYSLALDQAPAStAPPGARWLTWEEFCNAAVSTAMKKVFRMYED 214
Cdd:COG1194   298 VFTHFRLHLTVYLARVPAGPPA-EPDGGRWVPLEELAALPLPAPMRKLLKALLK 350
 
Name Accession Description Interval E-value
MutY COG1194
Adenine-specific DNA glycosylase, acts on AG and A-oxoG pairs [Replication, recombination and ...
 1-214 5.23e-43

Adenine-specific DNA glycosylase, acts on AG and A-oxoG pairs [Replication, recombination and repair];


Pssm-ID: 440807 [Multi-domain]  Cd Length: 350  Bit Score: 149.13  E-value: 5.23e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409832   1 MELGATVCTPQRPLCSHCPVQSLCRAYQRvqrgqlsalpGRPdieecalntrqcqlcltssspwdpsmgvANFPRKASRR 80
Cdd:COG1194   184 MDLGATVCTPKKPKCLLCPLQDDCAAFAE----------GRQ----------------------------EELPVKKPKK 225

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409832  81 PPREEYSATCVVEQPGAiggplVLLVQRPDSGLLAGLWEFPSVtlEPSEQHQHKALLQELQRWCGpLPAIRLQHLGEVIH 160
Cdd:COG1194   226 KKPERYGAALVIRDDGR-----VLLEKRPPKGLWGGLWEFPEF--EWEEAEDPEALERWLREELG-LEVEWLEPLGTVRH 297

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1720409832 161 IFSHIKLTYQVYSLALDQAPAStAPPGARWLTWEEFCNAAVSTAMKKVFRMYED 214
Cdd:COG1194   298 VFTHFRLHLTVYLARVPAGPPA-EPDGGRWVPLEELAALPLPAPMRKLLKALLK 350
NUDIX_DNA_Glycosylase_C-MutY cd03431
C-terminal domain of DNA glycosylase; DNA glycosylase (MutY in bacteria and hMYH in humans) is ...
 82-209 9.72e-32

C-terminal domain of DNA glycosylase; DNA glycosylase (MutY in bacteria and hMYH in humans) is responsible for repairing misread A*oxoG residues to C*G by removing the inappropriately paired adenine base from the DNA backbone. It belongs to the NUDIX hydrolase superfamily and is important for the repair of various genotoxic lesions. Enzymes belonging to this superfamily requires a divalent cation, such as Mg2+ or Mn2+ for their activity. They are also recognized by a highly conserved 23-residue NUDIX motif (GX5EX7REUXEEXGU, where U = I, L or V). However, DNA glycosylase does not seem to contain this signature motif. DNA glycosylase consists of 2 domains: the N-terminal domain contains the catalytic properties of the enzyme and the C-terminal domain affects substrate (oxoG) binding and enzymatic turnover. The C-terminal domain is highly similar to MutT, based on secondary structure and topology, despite low sequence identity. MutT sanitizes the nucleotide precursor pool by hydrolyzing oxo-dGTP to oxo-dGMO and inorganic pyrophosphate. The similarity strongly suggests that the two proteins share a common evolutionary origin.


Pssm-ID: 467537 [Multi-domain]  Cd Length: 118  Bit Score: 113.17  E-value: 9.72e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409832  82 PREEYSATCVVEQPGAiggplVLLVQRPDSGLLAGLWEFPSVTLEPSEQhqhkaLLQELQRWCGPLPAIRLQHLGEVIHI 161
Cdd:cd03431     1 VPERYFTVLVLRDGGR-----VLLEKRPEKGLLAGLWEFPLVETEEEEE-----EAEALLGLLAEELLLILEPLGEVKHV 70

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1720409832 162 FSHIKLTYQVYSLALDQAPAsTAPPGARWLTWEEFCNAAVSTAMKKVF 209
Cdd:cd03431    71 FSHFRLHITVYLVELPEAPP-AAPDEGRWVDLEELDEYALPAPMRKLL 117
NUDIX_4 pfam14815
NUDIX domain;
103-211 1.17e-23

NUDIX domain;


Pssm-ID: 464330 [Multi-domain]  Cd Length: 114  Bit Score: 91.99  E-value: 1.17e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409832 103 VLLVQRPDSGLLAGLWEFPSVTLEPSEqhqhkALLQELQRWCGPLPAIRLQHLGEVIHIFSHIKLTYQVYsLALDQAPAS 182
Cdd:pfam14815  12 VLLRKRPEKGLLGGLWEFPGGKVEPGE-----TLEEALARLEELGIEVEVLEPGTVKHVFTHFRLTLHVY-LVREVEGEE 85

                          90       100
                  ....*....|....*....|....*....
gi 1720409832 183 TAPPGARWLTWEEFCNAAVSTAMKKVFRM 211
Cdd:pfam14815  86 EPQQELRWVTPEELDKYALPAAVRKILEA 114
PRK10880 PRK10880
adenine DNA glycosylase;
1-167 2.46e-07

adenine DNA glycosylase;


Pssm-ID: 182805 [Multi-domain]  Cd Length: 350  Bit Score: 50.86  E-value: 2.46e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409832   1 MELGATVCTPQRPLCSHCPVQSLCRAYqrvqrgqlsalpgrpdieecalntrqcqlcltSSSPWdpsmgvANFPRKASRR 80
Cdd:PRK10880  185 MDLGAMVCTRSKPKCELCPLQNGCIAY--------------------------------ANHSW------ALYPGKKPKQ 226

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409832  81 PPREEYSATCVVEQpgaigGPLVLLVQRPDSGLLAGLWEFPSVTLEpseqhqhkallQELQRWCGP--LPAIRLQHLGEV 158
Cdd:PRK10880  227 TLPERTGYFLLLQH-----GDEVWLEQRPPSGLWGGLFCFPQFADE-----------EELRQWLAQrgIAADNLTQLTAF 290


                  ....*....
gi 1720409832 159 IHIFSHIKL 167
Cdd:PRK10880  291 RHTFSHFHL 299
FES smart00525
iron-sulpphur binding domain in DNA-(apurinic or apyrimidinic site) lyase (subfamily of ENDO3); ...
 7-27 1.37e-03

iron-sulpphur binding domain in DNA-(apurinic or apyrimidinic site) lyase (subfamily of ENDO3);


Pssm-ID: 197771 [Multi-domain]  Cd Length: 21  Bit Score: 35.22  E-value: 1.37e-03
                           10        20
                   ....*....|....*....|.
gi 1720409832    7 VCTPQRPLCSHCPVQSLCRAY 27
Cdd:smart00525   1 ICTARKPRCDECPLKDLCPAY 21
 
Name Accession Description Interval E-value
MutY COG1194
Adenine-specific DNA glycosylase, acts on AG and A-oxoG pairs [Replication, recombination and ...
 1-214 5.23e-43

Adenine-specific DNA glycosylase, acts on AG and A-oxoG pairs [Replication, recombination and repair];


Pssm-ID: 440807 [Multi-domain]  Cd Length: 350  Bit Score: 149.13  E-value: 5.23e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409832   1 MELGATVCTPQRPLCSHCPVQSLCRAYQRvqrgqlsalpGRPdieecalntrqcqlcltssspwdpsmgvANFPRKASRR 80
Cdd:COG1194   184 MDLGATVCTPKKPKCLLCPLQDDCAAFAE----------GRQ----------------------------EELPVKKPKK 225

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409832  81 PPREEYSATCVVEQPGAiggplVLLVQRPDSGLLAGLWEFPSVtlEPSEQHQHKALLQELQRWCGpLPAIRLQHLGEVIH 160
Cdd:COG1194   226 KKPERYGAALVIRDDGR-----VLLEKRPPKGLWGGLWEFPEF--EWEEAEDPEALERWLREELG-LEVEWLEPLGTVRH 297

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1720409832 161 IFSHIKLTYQVYSLALDQAPAStAPPGARWLTWEEFCNAAVSTAMKKVFRMYED 214
Cdd:COG1194   298 VFTHFRLHLTVYLARVPAGPPA-EPDGGRWVPLEELAALPLPAPMRKLLKALLK 350
NUDIX_DNA_Glycosylase_C-MutY cd03431
C-terminal domain of DNA glycosylase; DNA glycosylase (MutY in bacteria and hMYH in humans) is ...
 82-209 9.72e-32

C-terminal domain of DNA glycosylase; DNA glycosylase (MutY in bacteria and hMYH in humans) is responsible for repairing misread A*oxoG residues to C*G by removing the inappropriately paired adenine base from the DNA backbone. It belongs to the NUDIX hydrolase superfamily and is important for the repair of various genotoxic lesions. Enzymes belonging to this superfamily requires a divalent cation, such as Mg2+ or Mn2+ for their activity. They are also recognized by a highly conserved 23-residue NUDIX motif (GX5EX7REUXEEXGU, where U = I, L or V). However, DNA glycosylase does not seem to contain this signature motif. DNA glycosylase consists of 2 domains: the N-terminal domain contains the catalytic properties of the enzyme and the C-terminal domain affects substrate (oxoG) binding and enzymatic turnover. The C-terminal domain is highly similar to MutT, based on secondary structure and topology, despite low sequence identity. MutT sanitizes the nucleotide precursor pool by hydrolyzing oxo-dGTP to oxo-dGMO and inorganic pyrophosphate. The similarity strongly suggests that the two proteins share a common evolutionary origin.


Pssm-ID: 467537 [Multi-domain]  Cd Length: 118  Bit Score: 113.17  E-value: 9.72e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409832  82 PREEYSATCVVEQPGAiggplVLLVQRPDSGLLAGLWEFPSVTLEPSEQhqhkaLLQELQRWCGPLPAIRLQHLGEVIHI 161
Cdd:cd03431     1 VPERYFTVLVLRDGGR-----VLLEKRPEKGLLAGLWEFPLVETEEEEE-----EAEALLGLLAEELLLILEPLGEVKHV 70

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1720409832 162 FSHIKLTYQVYSLALDQAPAsTAPPGARWLTWEEFCNAAVSTAMKKVF 209
Cdd:cd03431    71 FSHFRLHITVYLVELPEAPP-AAPDEGRWVDLEELDEYALPAPMRKLL 117
NUDIX_4 pfam14815
NUDIX domain;
103-211 1.17e-23

NUDIX domain;


Pssm-ID: 464330 [Multi-domain]  Cd Length: 114  Bit Score: 91.99  E-value: 1.17e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409832 103 VLLVQRPDSGLLAGLWEFPSVTLEPSEqhqhkALLQELQRWCGPLPAIRLQHLGEVIHIFSHIKLTYQVYsLALDQAPAS 182
Cdd:pfam14815  12 VLLRKRPEKGLLGGLWEFPGGKVEPGE-----TLEEALARLEELGIEVEVLEPGTVKHVFTHFRLTLHVY-LVREVEGEE 85

                          90       100
                  ....*....|....*....|....*....
gi 1720409832 183 TAPPGARWLTWEEFCNAAVSTAMKKVFRM 211
Cdd:pfam14815  86 EPQQELRWVTPEELDKYALPAAVRKILEA 114
PRK10880 PRK10880
adenine DNA glycosylase;
1-167 2.46e-07

adenine DNA glycosylase;


Pssm-ID: 182805 [Multi-domain]  Cd Length: 350  Bit Score: 50.86  E-value: 2.46e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409832   1 MELGATVCTPQRPLCSHCPVQSLCRAYqrvqrgqlsalpgrpdieecalntrqcqlcltSSSPWdpsmgvANFPRKASRR 80
Cdd:PRK10880  185 MDLGAMVCTRSKPKCELCPLQNGCIAY--------------------------------ANHSW------ALYPGKKPKQ 226

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409832  81 PPREEYSATCVVEQpgaigGPLVLLVQRPDSGLLAGLWEFPSVTLEpseqhqhkallQELQRWCGP--LPAIRLQHLGEV 158
Cdd:PRK10880  227 TLPERTGYFLLLQH-----GDEVWLEQRPPSGLWGGLFCFPQFADE-----------EELRQWLAQrgIAADNLTQLTAF 290


                  ....*....
gi 1720409832 159 IHIFSHIKL 167
Cdd:PRK10880  291 RHTFSHFHL 299
PRK10546 PRK10546
pyrimidine (deoxy)nucleoside triphosphate diphosphatase;
91-141 1.54e-05

pyrimidine (deoxy)nucleoside triphosphate diphosphatase;


Pssm-ID: 182536 [Multi-domain]  Cd Length: 135  Bit Score: 43.58  E-value: 1.54e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1720409832  91 VVEQPGAIggplvLLVQRPDSGLLAGLWEFPSVTLEPSEQhQHKALLQELQ 141
Cdd:PRK10546   10 IIERDGKI-----LLAQRPAHSDQAGLWEFAGGKVEPGES-QPQALIRELR 54
NUDIX_MutT_NudA_like cd03425
MutT pyrophosphohydrolase; The MutT pyrophosphohydrolase is a prototypical NUDIX hydrolase ...
 103-195 1.31e-04

MutT pyrophosphohydrolase; The MutT pyrophosphohydrolase is a prototypical NUDIX hydrolase that catalyzes the hydrolysis of nucleoside and deoxynucleoside triphosphates (NTPs and dNTPs) by substitution at a beta-phosphorus to yield a nucleotide monophosphate (NMP) and inorganic pyrophosphate (PPi). This enzyme requires two divalent cations for activity; one coordinates the phosphoryl groups of the NTP/dNTP substrate, and the other coordinates to the enzyme. It also contains the NUDIX motif, a highly conserved 23-residue block (GX5EX7REUXEEXGU, where U = I, L or V), that functions as metal binding and catalytic site. MutT pyrophosphohydrolase is important in preventing errors in DNA replication by hydrolyzing mutagenic nucleotides such as 8-oxo-dGTP (a product of oxidative damage), which can mispair with template adenine during DNA replication, to guanine nucleotides.


Pssm-ID: 467531 [Multi-domain]  Cd Length: 123  Bit Score: 40.51  E-value: 1.31e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409832 103 VLLVQRPDSGLLAGLWEFPSVTLEPSEQHQHkALLQELQRWCGpLPAIRLQHLGEVIHIFSHIKLTYQVYS-LALDQAPA 181
Cdd:cd03425    14 VLIAQRPEGKHLAGLWEFPGGKVEPGETPEQ-ALVRELREELG-IEVEVGEPLGTVEHDYPDFHVRLHVYLcTLWSGEPQ 91

                          90
                  ....*....|....
gi 1720409832 182 STAPPGARWLTWEE 195
Cdd:cd03425    92 LLEHQELRWVTPEE 105
Nth COG0177
Endonuclease III [Replication, recombination and repair];
3-28 3.13e-04

Endonuclease III [Replication, recombination and repair];


Pssm-ID: 439947 [Multi-domain]  Cd Length: 198  Bit Score: 40.85  E-value: 3.13e-04
                          10        20
                  ....*....|....*....|....*.
gi 1720409832   3 LGATVCTPQRPLCSHCPVQSLCRAYQ 28
Cdd:COG0177   173 HGRYICKARKPKCEECPLADLCPYYG 198
MutT COG0494
8-oxo-dGTP pyrophosphatase MutT and related house-cleaning NTP pyrophosphohydrolases, NUDIX ...
 103-208 9.17e-04

8-oxo-dGTP pyrophosphatase MutT and related house-cleaning NTP pyrophosphohydrolases, NUDIX family [Defense mechanisms];


Pssm-ID: 440260 [Multi-domain]  Cd Length: 143  Bit Score: 38.48  E-value: 9.17e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409832 103 VLLVQRPDSGLLAGLWEFPSVTLEPSEQHQHkALLQELQ----------RWCGPLPAIRlqHLGEVIHIFsHIKLTYQVY 172
Cdd:COG0494    27 VLLVRRYRYGVGPGLWEFPGGKIEPGESPEE-AALRELReetgltaedlELLGELPSPG--YTDEKVHVF-LARGLGPGE 102

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1720409832 173 SLALDQAPASTAppgARWLTWEEFCNAAVSTAMKKV 208
Cdd:COG0494   103 EVGLDDEDEFIE---VRWVPLDEALALVTAGEIAKT 135
FES smart00525
iron-sulpphur binding domain in DNA-(apurinic or apyrimidinic site) lyase (subfamily of ENDO3); ...
 7-27 1.37e-03

iron-sulpphur binding domain in DNA-(apurinic or apyrimidinic site) lyase (subfamily of ENDO3);


Pssm-ID: 197771 [Multi-domain]  Cd Length: 21  Bit Score: 35.22  E-value: 1.37e-03
                           10        20
                   ....*....|....*....|.
gi 1720409832    7 VCTPQRPLCSHCPVQSLCRAY 27
Cdd:smart00525   1 ICTARKPRCDECPLKDLCPAY 21
PRK10776 PRK10776
8-oxo-dGTP diphosphatase MutT;
107-167 1.92e-03

8-oxo-dGTP diphosphatase MutT;


Pssm-ID: 182721 [Multi-domain]  Cd Length: 129  Bit Score: 37.27  E-value: 1.92e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720409832 107 QRPDSGLLAGLWEFPSVTLEPSEQHQhKALLQELQRWCGpLPAIRLQHLGEVIHIFS--HIKL 167
Cdd:PRK10776   22 RRAADAHMAGKWEFPGGKIEAGETPE-QALIRELQEEVG-ITVQHATLFEKLEYEFPdrHITL 82
NUDIX_Ap6A_hydrolase cd03673
diadenosine hexaphosphate (Ap6A) hydrolase; Diadenosine hexaphosphate (Ap6A) hydrolase is a ...
 85-214 4.92e-03

diadenosine hexaphosphate (Ap6A) hydrolase; Diadenosine hexaphosphate (Ap6A) hydrolase is a member of the NUDIX hydrolase superfamily. Ap6A hydrolase specifically hydrolyzes diadenosine polyphosphates, but not ATP or diadenosine triphosphate, and it generates ATP as the product. Ap6A, the most preferred substrate, hydrolyzes to produce two ATP molecules, which is a novel hydrolysis mode for Ap6A. These results indicate that Ap6A hydrolase is a diadenosine polyphosphate hydrolase. It requires the presence of a divalent cation, such as Mn2+, Mg2+, Zn2+, and Co2+, for activity. Members of the NUDIX hydrolase superfamily are recognized by a highly conserved 23-residue NUDIX motif (GX5EX7REUXEEXGU, where U = I, L or V), which forms a structural motif that functions as a metal binding and catalytic site.


Pssm-ID: 467541 [Multi-domain]  Cd Length: 131  Bit Score: 36.38  E-value: 4.92e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409832  85 EYSATCVVEQPGAiGGPLVLLVQRPDSgllaGLWEFPSVTLEPSEQHQHKAL---LQElqrwCGpLPAIRLQHLGEVIHI 161
Cdd:cd03673     1 VEAAGGVVWRGRG-GGGEVLLIHRPRY----DDWSLPKGKLEPGETPEEAAVrevEEE----TG-LRVRLGRPLGTTRYT 70

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720409832 162 FSH-----IKLTYqvYSLAldQAPASTAPP-------GARWLTWEEFCNAAVSTAMKKVFRMYED 214
Cdd:cd03673    71 YTRkgkgiLKKVH--YWLM--RALGGEFLPqpeeeidEVRWLPPDEARRLLTYPSDREVLDAALE 131
PRK08999 PRK08999
Nudix family hydrolase;
103-141 7.33e-03

Nudix family hydrolase;


Pssm-ID: 236361 [Multi-domain]  Cd Length: 312  Bit Score: 37.16  E-value: 7.33e-03
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1720409832 103 VLLVQRPDSGLLAGLWEFPSVTLEPSEQHQHkALLQELQ 141
Cdd:PRK08999   19 ILLARRPEGKHQGGLWEFPGGKVEPGETVEQ-ALARELQ 56
 
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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