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Conserved domains on  [gi|568916975|ref|XP_006499555|]
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piRNA biogenesis protein EXD1 isoform X2 [Mus musculus]

Protein Classification

3'-5' exonuclease family protein( domain architecture ID 10150270)

3'-5' exonuclease family protein belonging to the DnaQ-like (or DEDD) 3'-5' exonuclease superfamily, similar to human piRNA biogenesis protein EXD1, an RNA-binding component of the PET complex, a multiprotein complex required for the processing of piRNAs during spermatogenesis

CATH:  3.30.420.10
Gene Ontology:  GO:0003676
PubMed:  11988770|11222749
SCOP:  4000547

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Egl_like_exo cd06148
DEDDy 3'-5' exonuclease domain of Drosophila Egalitarian (Egl) and similar proteins; The ...
 53-251 9.14e-87

DEDDy 3'-5' exonuclease domain of Drosophila Egalitarian (Egl) and similar proteins; The Egalitarian (Egl) protein subfamily is composed of Drosophila Egl and similar proteins. Egl is a component of an mRNA-binding complex which is required for oocyte specification. Egl 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. 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. The conservation of this subfamily throughout eukaryotes suggests that its members may be part of ancient RNA processing complexes that are likely to participate in the regulated processing of specific mRNAs. Some members of this subfamily do not have a completely conserved YX(3)D pattern at the ExoIII motif.


:

Pssm-ID: 99851  Cd Length: 197  Bit Score: 264.15  E-value: 9.14e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568916975  53 GAAMLHIKKQSVLSVAAEGANVCRHGKLCWLQVAT-NSRVYLFDIFLLGSRAFNNGLQMILEDKRILKVIHDCRWLSDCL 131
Cdd:cd06148    1 KEAIIHLKKQKVIGLDCEGVNLGRKGKLCLVQIATrTGQIYLFDILKLGSIVFINGLKDILESKKILKVIHDCRRDSDAL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568916975 132 SHQYGIMLNNVFDTQVADVLQFSMETGGFLPNCISTLQESLIRHLKVAPRylfFLEERQKRIQENPEIWLTRPLPPSLLK 211
Cdd:cd06148   81 YHQYGIKLNNVFDTQVADALLQEQETGGFNPDRVISLVQLLDKYLYISIS---LKEDVKKLMREDPKFWALRPLTEDMIR 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 568916975 212 ILALETTYLLPLRLVLLDEVMSDLTTLVDGYLNTYREGSA 251
Cdd:cd06148  158 YAALDVLCLLPLYYAMLDALISKFLKAVFKYLNTERNLSE 197
 
Name Accession Description Interval E-value
Egl_like_exo cd06148
DEDDy 3'-5' exonuclease domain of Drosophila Egalitarian (Egl) and similar proteins; The ...
 53-251 9.14e-87

DEDDy 3'-5' exonuclease domain of Drosophila Egalitarian (Egl) and similar proteins; The Egalitarian (Egl) protein subfamily is composed of Drosophila Egl and similar proteins. Egl is a component of an mRNA-binding complex which is required for oocyte specification. Egl 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. 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. The conservation of this subfamily throughout eukaryotes suggests that its members may be part of ancient RNA processing complexes that are likely to participate in the regulated processing of specific mRNAs. Some members of this subfamily do not have a completely conserved YX(3)D pattern at the ExoIII motif.


Pssm-ID: 99851  Cd Length: 197  Bit Score: 264.15  E-value: 9.14e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568916975  53 GAAMLHIKKQSVLSVAAEGANVCRHGKLCWLQVAT-NSRVYLFDIFLLGSRAFNNGLQMILEDKRILKVIHDCRWLSDCL 131
Cdd:cd06148    1 KEAIIHLKKQKVIGLDCEGVNLGRKGKLCLVQIATrTGQIYLFDILKLGSIVFINGLKDILESKKILKVIHDCRRDSDAL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568916975 132 SHQYGIMLNNVFDTQVADVLQFSMETGGFLPNCISTLQESLIRHLKVAPRylfFLEERQKRIQENPEIWLTRPLPPSLLK 211
Cdd:cd06148   81 YHQYGIKLNNVFDTQVADALLQEQETGGFNPDRVISLVQLLDKYLYISIS---LKEDVKKLMREDPKFWALRPLTEDMIR 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 568916975 212 ILALETTYLLPLRLVLLDEVMSDLTTLVDGYLNTYREGSA 251
Cdd:cd06148  158 YAALDVLCLLPLYYAMLDALISKFLKAVFKYLNTERNLSE 197
Rnd COG0349
Ribonuclease D [Translation, ribosomal structure and biogenesis];
79-148 3.77e-12

Ribonuclease D [Translation, ribosomal structure and biogenesis];


Pssm-ID: 440118 [Multi-domain]  Cd Length: 365  Bit Score: 67.59  E-value: 3.77e-12
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568916975  79 KLCWLQVATNSRVYLFDIFLLGSRAfnnGLQMILEDKRILKVIHDCRwlSD--CLSHQYGIMLNNVFDTQVA 148
Cdd:COG0349   36 RLCLIQLADGEEVALIDPLAIGDLS---PLWELLADPAIVKVFHAAR--EDleILYHLFGILPKPLFDTQIA 102
35EXOc smart00474
3'-5' exonuclease; 3\' -5' exonuclease proofreading domain present in DNA polymerase I, Werner ...
 64-219 2.01e-09

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: 56.60  E-value: 2.01e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568916975    64 VLSVAAEGANV-CRHGKLCWLQVATNS-RVYLFDIFLLGSRAfnNGLQMILEDKRILKVIHDCRWLSDCLsHQYGIMLNN 141
Cdd:smart00474  23 EVALDTETTGLdSYSGKLVLIQISVTGeGAFIIDPLALGDDL--EILKDLLEDETITKVGHNAKFDLHVL-ARFGIELEN 99

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568916975   142 VFDTQVAdvLQFSMETGGFLpncisTLQESLIRHLKVaprylfFLEerqKRIQENpeIWLTRPLPPSLLKILALETTY 219
Cdd:smart00474 100 IFDTMLA--AYLLLGGPSKH-----GLATLLLGYLGV------ELD---KEEQKS--DWGARPLSEEQLEYAAEDADA 159
DNA_pol_A_exo1 pfam01612
3'-5' exonuclease; This domain is responsible for the 3'-5' exonuclease proofreading activity ...
 78-206 4.88e-08

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: 52.69  E-value: 4.88e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568916975   78 GKLCWLQVATNSRVYLFDIFLLGSrAFNNGLQMILEDKRILKVIHDCRWLSDCLSHQYGIMLNNVFDTQVAD-VLQFSME 156
Cdd:pfam01612  39 LRGALIQIGTGEGAYIIDPLALGD-DVLSALKRLLEDPNITKVGHNAKFDLEVLARDFGIKLRNLFDTMLAAyLLGYDRS 117

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 568916975  157 TGgflpncistlqeslirhLKV-APRYLFFLEERQKRIQEnpeiWLTRPLP 206
Cdd:pfam01612 118 HS-----------------LADlAEKYLGVELDKEEQCSD----WQARPLS 147
 
Name Accession Description Interval E-value
Egl_like_exo cd06148
DEDDy 3'-5' exonuclease domain of Drosophila Egalitarian (Egl) and similar proteins; The ...
 53-251 9.14e-87

DEDDy 3'-5' exonuclease domain of Drosophila Egalitarian (Egl) and similar proteins; The Egalitarian (Egl) protein subfamily is composed of Drosophila Egl and similar proteins. Egl is a component of an mRNA-binding complex which is required for oocyte specification. Egl 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. 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. The conservation of this subfamily throughout eukaryotes suggests that its members may be part of ancient RNA processing complexes that are likely to participate in the regulated processing of specific mRNAs. Some members of this subfamily do not have a completely conserved YX(3)D pattern at the ExoIII motif.


Pssm-ID: 99851  Cd Length: 197  Bit Score: 264.15  E-value: 9.14e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568916975  53 GAAMLHIKKQSVLSVAAEGANVCRHGKLCWLQVAT-NSRVYLFDIFLLGSRAFNNGLQMILEDKRILKVIHDCRWLSDCL 131
Cdd:cd06148    1 KEAIIHLKKQKVIGLDCEGVNLGRKGKLCLVQIATrTGQIYLFDILKLGSIVFINGLKDILESKKILKVIHDCRRDSDAL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568916975 132 SHQYGIMLNNVFDTQVADVLQFSMETGGFLPNCISTLQESLIRHLKVAPRylfFLEERQKRIQENPEIWLTRPLPPSLLK 211
Cdd:cd06148   81 YHQYGIKLNNVFDTQVADALLQEQETGGFNPDRVISLVQLLDKYLYISIS---LKEDVKKLMREDPKFWALRPLTEDMIR 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 568916975 212 ILALETTYLLPLRLVLLDEVMSDLTTLVDGYLNTYREGSA 251
Cdd:cd06148  158 YAALDVLCLLPLYYAMLDALISKFLKAVFKYLNTERNLSE 197
RNaseD_exo cd06142
DEDDy 3'-5' exonuclease domain of Ribonuclease D and similar proteins; Ribonuclease (RNase) D ...
 58-219 6.34e-13

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: 66.79  E-value: 6.34e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568916975  58 HIKKQSVLSVAAEGANV-CRHGKLCWLQVATNSRVYLFDIFLLGSrafNNGLQMILEDKRILKVIHDCRWLSDCLSHQYG 136
Cdd:cd06142    8 RLASAGVIAVDTEFMRLnTYYPRLCLIQISTGGEVYLIDPLAIGD---LSPLKELLADPNIVKVFHAAREDLELLKRDFG 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568916975 137 IMLNNVFDTQVAdvlqfSMETGgfLPNCIStLQESLIRHLKVAprylffLEERQKRiqENpeiWLTRPLPPSLLKILALE 216
Cdd:cd06142   85 ILPQNLFDTQIA-----ARLLG--LGDSVG-LAALVEELLGVE------LDKGEQR--SD---WSKRPLTDEQLEYAALD 145


                 ...
gi 568916975 217 TTY 219
Cdd:cd06142  146 VRY 148
Rnd COG0349
Ribonuclease D [Translation, ribosomal structure and biogenesis];
79-148 3.77e-12

Ribonuclease D [Translation, ribosomal structure and biogenesis];


Pssm-ID: 440118 [Multi-domain]  Cd Length: 365  Bit Score: 67.59  E-value: 3.77e-12
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568916975  79 KLCWLQVATNSRVYLFDIFLLGSRAfnnGLQMILEDKRILKVIHDCRwlSD--CLSHQYGIMLNNVFDTQVA 148
Cdd:COG0349   36 RLCLIQLADGEEVALIDPLAIGDLS---PLWELLADPAIVKVFHAAR--EDleILYHLFGILPKPLFDTQIA 102
35EXOc smart00474
3'-5' exonuclease; 3\' -5' exonuclease proofreading domain present in DNA polymerase I, Werner ...
 64-219 2.01e-09

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: 56.60  E-value: 2.01e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568916975    64 VLSVAAEGANV-CRHGKLCWLQVATNS-RVYLFDIFLLGSRAfnNGLQMILEDKRILKVIHDCRWLSDCLsHQYGIMLNN 141
Cdd:smart00474  23 EVALDTETTGLdSYSGKLVLIQISVTGeGAFIIDPLALGDDL--EILKDLLEDETITKVGHNAKFDLHVL-ARFGIELEN 99

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568916975   142 VFDTQVAdvLQFSMETGGFLpncisTLQESLIRHLKVaprylfFLEerqKRIQENpeIWLTRPLPPSLLKILALETTY 219
Cdd:smart00474 100 IFDTMLA--AYLLLGGPSKH-----GLATLLLGYLGV------ELD---KEEQKS--DWGARPLSEEQLEYAAEDADA 159
DNA_pol_A_exo1 pfam01612
3'-5' exonuclease; This domain is responsible for the 3'-5' exonuclease proofreading activity ...
 78-206 4.88e-08

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: 52.69  E-value: 4.88e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568916975   78 GKLCWLQVATNSRVYLFDIFLLGSrAFNNGLQMILEDKRILKVIHDCRWLSDCLSHQYGIMLNNVFDTQVAD-VLQFSME 156
Cdd:pfam01612  39 LRGALIQIGTGEGAYIIDPLALGD-DVLSALKRLLEDPNITKVGHNAKFDLEVLARDFGIKLRNLFDTMLAAyLLGYDRS 117

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 568916975  157 TGgflpncistlqeslirhLKV-APRYLFFLEERQKRIQEnpeiWLTRPLP 206
Cdd:pfam01612 118 HS-----------------LADlAEKYLGVELDKEEQCSD----WQARPLS 147
WRN_exo cd06141
DEDDy 3'-5' exonuclease domain of WRN and similar proteins; WRN is a unique RecQ DNA helicase ...
 77-147 7.82e-08

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: 51.81  E-value: 7.82e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568916975  77 HGKLCWLQVATNSRVYLFDIFLLGsrAFNNGLQMILEDKRILKVIHDCRwlSDC--LSHQYGIMLNNVFDTQV 147
Cdd:cd06141   36 RNKVALLQLATESRCLLFQLAHMD--KLPPSLKQLLEDPSILKVGVGIK--GDArkLARDFGIEVRGVVDLSH 104
RNaseD_like cd06129
DEDDy 3'-5' exonuclease domain of RNase D, WRN, and similar proteins; The RNase D-like group ...
 78-206 1.56e-05

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: 45.20  E-value: 1.56e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568916975  78 GKLCWLQVATN-SRVYLFDIflLGSRAFNNGLQMILEDKRILKVIHDCRWLSDCLSHQYGIMLNNVFDTQVADVLQFSME 156
Cdd:cd06129   30 GEVALIQLCVSeEKCYLFDP--LSLSVDWQGLKMLLENPSIVKALHGIEGDLWKLLRDFGEKLQRLFDTTIAANLKGLPE 107

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 568916975 157 TGGFlpncistlqESLIRHlkvaprYLFFLEERQKRIQEnpeiWLTRPLP 206
Cdd:cd06129  108 RWSL---------ASLVEH------FLGKTLDKSISCAD----WSYRPLT 138
Rrp6p_like_exo cd06147
DEDDy 3'-5' exonuclease domain of yeast Rrp6p, human polymyositis/scleroderma autoantigen ...
 38-211 1.89e-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: 42.20  E-value: 1.89e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568916975  38 EEVTYTVIDQfQQKFGAAMLHIKKQSVLSVAAEganvcrH-------GKLCWLQVATNSRVYLFDIFLLgsraFNNG--L 108
Cdd:cd06147    1 DETPLTFVDT-EEKLEELVEKLKNCKEIAVDLE------HhsyrsylGFTCLMQISTREEDYIVDTLKL----RDDMhiL 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568916975 109 QMILEDKRILKVIH----DCRWLSdclsHQYGIMLNNVFDT-QVADVLQFSMETGGFLpncistlqesLIRHLKVAPryl 183
Cdd:cd06147   70 NEVFTDPNILKVFHgadsDIIWLQ----RDFGLYVVNLFDTgQAARVLNLPRHSLAYL----------LQKYCNVDA--- 132

                        170       180
                 ....*....|....*....|....*...
gi 568916975 184 ffleerQKRIQEnpEIWLTRPLPPSLLK 211
Cdd:cd06147  133 ------DKKYQL--ADWRIRPLPEEMIK 152
DEDDy_polA_RNaseD_like_exo cd09018
DEDDy 3'-5' exonuclease domain of family-A DNA polymerases, RNase D, WRN, and similar proteins; ...
 78-147 9.69e-03

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: 36.83  E-value: 9.69e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568916975  78 GKLCWLQVA-TNSRVYLFDIflLGSRAFNNGLQMILEDKRILKVIHDCRWLSDCLSHQYGIMLNNVFDTQV 147
Cdd:cd09018   16 ANLVLIQLAiEPGVAALIPV--AHDYLALELLKPLLEDEKALKVGQNLKYDRGILLNYFIELRGIAFDTML 84
 
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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