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Conserved domains on  [gi|1720373430|ref|XP_030102871|]
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exonuclease 3'-5' domain-containing protein 2 isoform X2 [Mus musculus]

Protein Classification

3'-5' exonuclease( domain architecture ID 10150121)

3'-5' exonuclease catalyzes the excision of nucleoside monophosphates at the DNA or RNA termini in the 3'-5' direction; similar to human exonuclease 3'-5' domain-containing protein 2 that that has both 3'-5' exoribonuclease and exodeoxyribonuclease activities

CATH:  3.30.420.10
EC:  3.1.-.-
Gene Ontology:  GO:0008408|GO:0003676
PubMed:  11988770|11222749
SCOP:  4000547

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
WRN_exo cd06141
DEDDy 3'-5' exonuclease domain of WRN and similar proteins; WRN is a unique RecQ DNA helicase ...
 1-133 1.93e-42

DEDDy 3'-5' exonuclease domain of WRN and similar proteins; WRN is a unique RecQ DNA helicase exhibiting an exonuclease activity. It contains a DEDDy-type DnaQ-like 3'-5' exonuclease domain possessing three conserved sequence motifs termed ExoI, ExoII and ExoIII, with a specific YX(3)D pattern at ExoIII. These motifs are clustered around the active site and contain four conserved acidic residues that serve as ligands for the two metal ions required for catalysis. Mutations in the WRN gene cause Werner syndrome, an autosomal recessive disorder associated with premature aging and increased susceptibility to cancer and type II diabetes. WRN interacts with key proteins involved in DNA replication, recombination, and repair. It is believed to maintain genomic stability and life span by participating in DNA processes. WRN is stimulated by Ku70/80, an important regulator of genomic stability.


:

Pssm-ID: 176653 [Multi-domain]  Cd Length: 170  Bit Score: 148.50  E-value: 1.93e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373430   1 MASPSgFCALVRLPRLIYggrtLPRTLLDILADGAILKVGVGCSEDANKLLQDYGLIVRGCLDLRYLAMKQGNNilCNGL 80
Cdd:cd06141    44 LATES-RCLLFQLAHMDK----LPPSLKQLLEDPSILKVGVGIKGDARKLARDFGIEVRGVVDLSHLAKRVGPR--RKLV 116

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1720373430  81 SLKSLAETILNFPLDKSLLLRCSNWDAENLTEDQVTYAARDAQISVALFLHLL 133
Cdd:cd06141   117 SLARLVEEVLGLPLSKPKKVRCSNWEARPLSKEQILYAATDAYASLELYRKLL 169
 
Name Accession Description Interval E-value
WRN_exo cd06141
DEDDy 3'-5' exonuclease domain of WRN and similar proteins; WRN is a unique RecQ DNA helicase ...
 1-133 1.93e-42

DEDDy 3'-5' exonuclease domain of WRN and similar proteins; WRN is a unique RecQ DNA helicase exhibiting an exonuclease activity. It contains a DEDDy-type DnaQ-like 3'-5' exonuclease domain possessing three conserved sequence motifs termed ExoI, ExoII and ExoIII, with a specific YX(3)D pattern at ExoIII. These motifs are clustered around the active site and contain four conserved acidic residues that serve as ligands for the two metal ions required for catalysis. Mutations in the WRN gene cause Werner syndrome, an autosomal recessive disorder associated with premature aging and increased susceptibility to cancer and type II diabetes. WRN interacts with key proteins involved in DNA replication, recombination, and repair. It is believed to maintain genomic stability and life span by participating in DNA processes. WRN is stimulated by Ku70/80, an important regulator of genomic stability.


Pssm-ID: 176653 [Multi-domain]  Cd Length: 170  Bit Score: 148.50  E-value: 1.93e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373430   1 MASPSgFCALVRLPRLIYggrtLPRTLLDILADGAILKVGVGCSEDANKLLQDYGLIVRGCLDLRYLAMKQGNNilCNGL 80
Cdd:cd06141    44 LATES-RCLLFQLAHMDK----LPPSLKQLLEDPSILKVGVGIKGDARKLARDFGIEVRGVVDLSHLAKRVGPR--RKLV 116

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1720373430  81 SLKSLAETILNFPLDKSLLLRCSNWDAENLTEDQVTYAARDAQISVALFLHLL 133
Cdd:cd06141   117 SLARLVEEVLGLPLSKPKKVRCSNWEARPLSKEQILYAATDAYASLELYRKLL 169
DNA_pol_A_exo1 pfam01612
3'-5' exonuclease; This domain is responsible for the 3'-5' exonuclease proofreading activity ...
 30-133 1.36e-13

3'-5' exonuclease; This domain is responsible for the 3'-5' exonuclease proofreading activity of E. coli DNA polymerase I (polI) and other enzymes, it catalyzes the hydrolysis of unpaired or mismatched nucleotides. This domain consists of the amino-terminal half of the Klenow fragment in E. coli polI it is also found in the Werner syndrome helicase (WRN), focus forming activity 1 protein (FFA-1) and ribonuclease D (RNase D). Werner syndrome is a human genetic disorder causing premature aging; the WRN protein has helicase activity in the 3'-5' direction. The FFA-1 protein is required for formation of a replication foci and also has helicase activity; it is a homolog of the WRN protein. RNase D is a 3'-5' exonuclease involved in tRNA processing. Also found in this family is the autoantigen PM/Scl thought to be involved in polymyositis-scleroderma overlap syndrome.


Pssm-ID: 396266 [Multi-domain]  Cd Length: 173  Bit Score: 68.87  E-value: 1.36e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373430  30 ILADGAILKVGVGCSEDANKLLQDYGLIVRGCLDLRYLAMKQGnniLCNGLSLKSLAETILNFPLDKSLLlrCSNWDAEN 109
Cdd:pfam01612  71 LLEDPNITKVGHNAKFDLEVLARDFGIKLRNLFDTMLAAYLLG---YDRSHSLADLAEKYLGVELDKEEQ--CSDWQARP 145

                          90       100
                  ....*....|....*....|....
gi 1720373430 110 LTEDQVTYAARDAQISVALFLHLL 133
Cdd:pfam01612 146 LSEEQLRYAALDADYLLRLYDKLR 169
35EXOc smart00474
3'-5' exonuclease; 3\' -5' exonuclease proofreading domain present in DNA polymerase I, Werner ...
 27-133 8.35e-11

3'-5' exonuclease; 3\' -5' exonuclease proofreading domain present in DNA polymerase I, Werner syndrome helicase, RNase D and other enzymes


Pssm-ID: 214681 [Multi-domain]  Cd Length: 172  Bit Score: 60.83  E-value: 8.35e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373430   27 LLDILADGAILKVGVGCSEDANKLLQdYGLIVRGCLDLRYLAmkqgnNILCNGLS---LKSLAETILNFPLDKSLllRCS 103
Cdd:smart00474  67 LKDLLEDETITKVGHNAKFDLHVLAR-FGIELENIFDTMLAA-----YLLLGGPSkhgLATLLLGYLGVELDKEE--QKS 138

                           90       100       110
                   ....*....|....*....|....*....|
gi 1720373430  104 NWDAENLTEDQVTYAARDAQISVALFLHLL 133
Cdd:smart00474 139 DWGARPLSEEQLEYAAEDADALLRLYEKLE 168
Rnd COG0349
Ribonuclease D [Translation, ribosomal structure and biogenesis];
27-121 1.81e-08

Ribonuclease D [Translation, ribosomal structure and biogenesis];


Pssm-ID: 440118 [Multi-domain]  Cd Length: 365  Bit Score: 56.42  E-value: 1.81e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373430  27 LLDILADGAILKVGVGCSEDANKLLQDYGLIVRGCLDLRYLAMkqgnniLCN---GLSLKSLAETILNFPLDKSLllRCS 103
Cdd:COG0349    62 LWELLADPAIVKVFHAAREDLEILYHLFGILPKPLFDTQIAAA------LLGygdSVGYAALVEELLGVELDKSE--QRS 133

                          90
                  ....*....|....*...
gi 1720373430 104 NWDAENLTEDQVTYAARD 121
Cdd:COG0349   134 DWLRRPLSEEQLEYAAAD 151
 
Name Accession Description Interval E-value
WRN_exo cd06141
DEDDy 3'-5' exonuclease domain of WRN and similar proteins; WRN is a unique RecQ DNA helicase ...
 1-133 1.93e-42

DEDDy 3'-5' exonuclease domain of WRN and similar proteins; WRN is a unique RecQ DNA helicase exhibiting an exonuclease activity. It contains a DEDDy-type DnaQ-like 3'-5' exonuclease domain possessing three conserved sequence motifs termed ExoI, ExoII and ExoIII, with a specific YX(3)D pattern at ExoIII. These motifs are clustered around the active site and contain four conserved acidic residues that serve as ligands for the two metal ions required for catalysis. Mutations in the WRN gene cause Werner syndrome, an autosomal recessive disorder associated with premature aging and increased susceptibility to cancer and type II diabetes. WRN interacts with key proteins involved in DNA replication, recombination, and repair. It is believed to maintain genomic stability and life span by participating in DNA processes. WRN is stimulated by Ku70/80, an important regulator of genomic stability.


Pssm-ID: 176653 [Multi-domain]  Cd Length: 170  Bit Score: 148.50  E-value: 1.93e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373430   1 MASPSgFCALVRLPRLIYggrtLPRTLLDILADGAILKVGVGCSEDANKLLQDYGLIVRGCLDLRYLAMKQGNNilCNGL 80
Cdd:cd06141    44 LATES-RCLLFQLAHMDK----LPPSLKQLLEDPSILKVGVGIKGDARKLARDFGIEVRGVVDLSHLAKRVGPR--RKLV 116

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1720373430  81 SLKSLAETILNFPLDKSLLLRCSNWDAENLTEDQVTYAARDAQISVALFLHLL 133
Cdd:cd06141   117 SLARLVEEVLGLPLSKPKKVRCSNWEARPLSKEQILYAATDAYASLELYRKLL 169
RNaseD_like cd06129
DEDDy 3'-5' exonuclease domain of RNase D, WRN, and similar proteins; The RNase D-like group ...
 24-122 1.52e-14

DEDDy 3'-5' exonuclease domain of RNase D, WRN, and similar proteins; The RNase D-like group is composed of RNase D, WRN, and similar proteins. They contain a DEDDy-type, DnaQ-like, 3'-5' exonuclease domain that contains three conserved sequence motifs termed ExoI, ExoII and ExoIII, with a specific YX(3)D pattern at ExoIII. These motifs are clustered around the active site and contain four conserved acidic residues that serve as ligands for the two metal ions required for catalysis. RNase D is involved in the 3'-end processing of tRNA precursors. RNase D-like proteins in eukaryotes include yeast Rrp6p, human PM/Scl-100 and Drosophila melanogaster egalitarian (Egl) protein. WRN is a unique DNA helicase possessing exonuclease activity. Mutation in the WRN gene is implicated in Werner syndrome, a disease associated with premature aging and increased predisposition to cancer. Yeast Rrp6p and the human Polymyositis/scleroderma autoantigen 100kDa (PM/Scl-100) are exosome-associated proteins involved in the degradation and processing of precursors to stable RNAs. Egl is a component of an mRNA-binding complex which is required for oocyte specification. The Egl subfamily does not possess a completely conserved YX(3)D pattern at the ExoIII motif.


Pssm-ID: 176650 [Multi-domain]  Cd Length: 161  Bit Score: 71.39  E-value: 1.52e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373430  24 PRTLLDILADGAILKVGVGCSEDANKLLQDYGLIVRGCLDLRYLAMKQGnniLCNGLSLKSLAETILNFPLDKSLllRCS 103
Cdd:cd06129    56 WQGLKMLLENPSIVKALHGIEGDLWKLLRDFGEKLQRLFDTTIAANLKG---LPERWSLASLVEHFLGKTLDKSI--SCA 130

                          90
                  ....*....|....*....
gi 1720373430 104 NWDAENLTEDQVTYAARDA 122
Cdd:cd06129   131 DWSYRPLTEDQKLYAAADV 149
DNA_pol_A_exo1 pfam01612
3'-5' exonuclease; This domain is responsible for the 3'-5' exonuclease proofreading activity ...
 30-133 1.36e-13

3'-5' exonuclease; This domain is responsible for the 3'-5' exonuclease proofreading activity of E. coli DNA polymerase I (polI) and other enzymes, it catalyzes the hydrolysis of unpaired or mismatched nucleotides. This domain consists of the amino-terminal half of the Klenow fragment in E. coli polI it is also found in the Werner syndrome helicase (WRN), focus forming activity 1 protein (FFA-1) and ribonuclease D (RNase D). Werner syndrome is a human genetic disorder causing premature aging; the WRN protein has helicase activity in the 3'-5' direction. The FFA-1 protein is required for formation of a replication foci and also has helicase activity; it is a homolog of the WRN protein. RNase D is a 3'-5' exonuclease involved in tRNA processing. Also found in this family is the autoantigen PM/Scl thought to be involved in polymyositis-scleroderma overlap syndrome.


Pssm-ID: 396266 [Multi-domain]  Cd Length: 173  Bit Score: 68.87  E-value: 1.36e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373430  30 ILADGAILKVGVGCSEDANKLLQDYGLIVRGCLDLRYLAMKQGnniLCNGLSLKSLAETILNFPLDKSLLlrCSNWDAEN 109
Cdd:pfam01612  71 LLEDPNITKVGHNAKFDLEVLARDFGIKLRNLFDTMLAAYLLG---YDRSHSLADLAEKYLGVELDKEEQ--CSDWQARP 145

                          90       100
                  ....*....|....*....|....
gi 1720373430 110 LTEDQVTYAARDAQISVALFLHLL 133
Cdd:pfam01612 146 LSEEQLRYAALDADYLLRLYDKLR 169
DEDDy_polA_RNaseD_like_exo cd09018
DEDDy 3'-5' exonuclease domain of family-A DNA polymerases, RNase D, WRN, and similar proteins; ...
 24-132 4.05e-12

DEDDy 3'-5' exonuclease domain of family-A DNA polymerases, RNase D, WRN, and similar proteins; DEDDy exonucleases, part of the DnaQ-like (or DEDD) exonuclease superfamily, catalyze the excision of nucleoside monophosphates at the DNA or RNA termini in the 3'-5' direction. They contain four invariant acidic residues in three conserved sequence motifs termed ExoI, ExoII and ExoIII. DEDDy exonucleases are classified as such because of the presence of a specific YX(3)D pattern at ExoIII. The four conserved acidic residues serve as ligands for the two metal ions required for catalysis. This family of DEDDy exonucleases includes the proofreading domains of family A DNA polymerases, as well as RNases such as RNase D and yeast Rrp6p. The Egalitarian (Egl) and Bacillus-like DNA Polymerase I subfamilies do not possess a completely conserved YX(3)D pattern at the ExoIII motif. In addition, the Bacillus-like DNA polymerase I subfamily has inactive 3'-5' exonuclease domains which do not possess the metal-binding residues necessary for activity.


Pssm-ID: 176656 [Multi-domain]  Cd Length: 150  Bit Score: 63.80  E-value: 4.05e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373430  24 PRTLLDILADGAILKVGVGCSEDANKLLQDYGLIVRGCLDLRYLAMKQGNnilCNGL-SLKSLAETILNFPLDKSLLLRC 102
Cdd:cd09018    42 LELLKPLLEDEKALKVGQNLKYDRGILLNYFIELRGIAFDTMLEAYILNS---VAGRwDMDSLVERWLGHKLIKFESIAG 118

                          90       100       110
                  ....*....|....*....|....*....|
gi 1720373430 103 SNWDAENLTEDQVTYAARDAQISVALFLHL 132
Cdd:cd09018   119 KLWFNQPLTEEQGRYAAEDADVTLQIHLKL 148
35EXOc smart00474
3'-5' exonuclease; 3\' -5' exonuclease proofreading domain present in DNA polymerase I, Werner ...
 27-133 8.35e-11

3'-5' exonuclease; 3\' -5' exonuclease proofreading domain present in DNA polymerase I, Werner syndrome helicase, RNase D and other enzymes


Pssm-ID: 214681 [Multi-domain]  Cd Length: 172  Bit Score: 60.83  E-value: 8.35e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373430   27 LLDILADGAILKVGVGCSEDANKLLQdYGLIVRGCLDLRYLAmkqgnNILCNGLS---LKSLAETILNFPLDKSLllRCS 103
Cdd:smart00474  67 LKDLLEDETITKVGHNAKFDLHVLAR-FGIELENIFDTMLAA-----YLLLGGPSkhgLATLLLGYLGVELDKEE--QKS 138

                           90       100       110
                   ....*....|....*....|....*....|
gi 1720373430  104 NWDAENLTEDQVTYAARDAQISVALFLHLL 133
Cdd:smart00474 139 DWGARPLSEEQLEYAAEDADALLRLYEKLE 168
mut-7_like_exo cd06146
DEDDy 3'-5' exonuclease domain of Caenorhabditis elegans mut-7 and similar proteins; The mut-7 ...
 22-133 5.90e-10

DEDDy 3'-5' exonuclease domain of Caenorhabditis elegans mut-7 and similar proteins; The mut-7 subfamily is composed of Caenorhabditis elegans mut-7 and similar proteins found in plants and metazoans. Mut-7 is implicated in posttranscriptional gene silencing. It contains a DEDDy-type DnaQ-like 3'-5' exonuclease domain possessing three conserved sequence motifs, termed ExoI, ExoII and ExoIII, with a specific YX(3)D pattern at ExoIII. These motifs are clustered around the active site and contain four conserved acidic residues that serve as ligands for the two metal ions required for catalysis.


Pssm-ID: 176655  Cd Length: 193  Bit Score: 58.84  E-value: 5.90e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373430  22 TLPRTLLDILADGAILKVGVGCSEDANKL------LQDYGLIVRGCLDLRYLA---MKQGNNILCNGL-----SLKSLAE 87
Cdd:cd06146    69 DWDRLLKRLFEDPDVLKLGFGFKQDLKALsasypaLKCMFERVQNVLDLQNLAkelQKSDMGRLKGNLpsktkGLADLVQ 148

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1720373430  88 TILNFPLDKSLllRCSNWDAENLTEDQVTYAARDAQISVALFLHLL 133
Cdd:cd06146   149 EVLGKPLDKSE--QCSNWERRPLREEQILYAALDAYCLLEVFDKLL 192
Rnd COG0349
Ribonuclease D [Translation, ribosomal structure and biogenesis];
27-121 1.81e-08

Ribonuclease D [Translation, ribosomal structure and biogenesis];


Pssm-ID: 440118 [Multi-domain]  Cd Length: 365  Bit Score: 56.42  E-value: 1.81e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373430  27 LLDILADGAILKVGVGCSEDANKLLQDYGLIVRGCLDLRYLAMkqgnniLCN---GLSLKSLAETILNFPLDKSLllRCS 103
Cdd:COG0349    62 LWELLADPAIVKVFHAAREDLEILYHLFGILPKPLFDTQIAAA------LLGygdSVGYAALVEELLGVELDKSE--QRS 133

                          90
                  ....*....|....*...
gi 1720373430 104 NWDAENLTEDQVTYAARD 121
Cdd:COG0349   134 DWLRRPLSEEQLEYAAAD 151
RNaseD_exo cd06142
DEDDy 3'-5' exonuclease domain of Ribonuclease D and similar proteins; Ribonuclease (RNase) D ...
 27-164 2.74e-08

DEDDy 3'-5' exonuclease domain of Ribonuclease D and similar proteins; Ribonuclease (RNase) D is a bacterial enzyme involved in the maturation of small stable RNAs and the 3' maturation of tRNA. It contains a DEDDy-type DnaQ-like 3'-5' exonuclease domain possessing three conserved sequence motifs termed ExoI, ExoII and ExoIII, with a specific YX(3)D pattern at ExoIII. These motifs are clustered around the active site and contain four conserved acidic residues that serve as ligands for the two metal ions required for catalysis. In vivo, RNase D only becomes essential upon removal of other ribonucleases. Eukaryotic RNase D homologs include yeast Rrp6p, human PM/Scl-100, and the Drosophila melanogaster egalitarian protein.


Pssm-ID: 176654 [Multi-domain]  Cd Length: 178  Bit Score: 53.69  E-value: 2.74e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373430  27 LLDILADGAILKVGVGCSEDANKLLQDYGLIVRGCLDLrYLAMKqgnniLCN---GLSLKSLAETILNFPLDKSLllRCS 103
Cdd:cd06142    56 LKELLADPNIVKVFHAAREDLELLKRDFGILPQNLFDT-QIAAR-----LLGlgdSVGLAALVEELLGVELDKGE--QRS 127

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720373430 104 NWDAENLTEDQVTYAARDaqisVALFLHLlgypfsRDSYEEESTDQINWQKALERCRNMVD 164
Cdd:cd06142   128 DWSKRPLTDEQLEYAALD----VRYLLPL------YEKLKEELEEEGRLEWAEEECELLLD 178
Rrp6p_like_exo cd06147
DEDDy 3'-5' exonuclease domain of yeast Rrp6p, human polymyositis/scleroderma autoantigen ...
 27-122 4.77e-04

DEDDy 3'-5' exonuclease domain of yeast Rrp6p, human polymyositis/scleroderma autoantigen 100kDa, and similar proteins; Yeast Rrp6p and its human homolog, the polymyositis/scleroderma autoantigen 100kDa (PM/Scl-100), are exosome-associated proteins involved in the degradation and processing of precursors to stable RNAs. Both proteins contain a DEDDy-type DnaQ-like 3'-5' exonuclease domain possessing three conserved sequence motifs termed ExoI, ExoII and ExoIII, with a specific YX(3)D pattern at ExoIII. The motifs are clustered around the active site and contain four conserved acidic residues that serve as ligands for the two metal ions required for catalysis. PM/Scl-100, an autoantigen present in the nucleolar compartment of the cell, reacts with autoantibodies produced by about 50% of patients with polymyositis-scleroderma overlap syndrome.


Pssm-ID: 99850 [Multi-domain]  Cd Length: 192  Bit Score: 41.43  E-value: 4.77e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720373430  27 LLDILADGAILKVGVGCSEDANKLLQDYGLIVRGCLDlRYLAMKqgnnILC-NGLSLKSLAETILNFPLDKSLLLrcSNW 105
Cdd:cd06147    69 LNEVFTDPNILKVFHGADSDIIWLQRDFGLYVVNLFD-TGQAAR----VLNlPRHSLAYLLQKYCNVDADKKYQL--ADW 141

                          90
                  ....*....|....*..
gi 1720373430 106 DAENLTEDQVTYAARDA 122
Cdd:cd06147   142 RIRPLPEEMIKYAREDT 158
 
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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