Summary: 3'-5' exonuclease
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3'-5' exonuclease Provide feedback
This domain is responsible for the 3'-5' exonuclease proofreading activity of E. coli DNA polymerase I (polI) and other enzymes, it catalyses 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 [4,5]. The FFA-1 protein is required for formation of a replication foci and also has helicase activity; it is a homologue 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.
Moser MJ, Holley WR, Chatterjee A, Mian IS; , Nucleic Acids Res 1997;25:5110-5118.: The proofreading domain of Escherichia coli DNA polymerase I and other DNA and/or RNA exonuclease domains. PUBMED:9396823 EPMC:9396823
Suzuki N, Shimamoto A, Imamura O, Kuromitsu J, Kitao S, Goto M, Furuichi Y; , Nucleic Acids Res 1997;25:2973-2978.: DNA helicase activity in Werner's syndrome gene product synthesized in a baculovirus system. PUBMED:9224595 EPMC:9224595
External database links
This tab holds annotation information from the InterPro database.
InterPro entry IPR002562
This domain is responsible for the 3'-5' exonuclease proofreading activity of Escherichia coli DNA polymerase I (polI) and other enzymes, it catalyses 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) [PUBMED:9697700].
|Cellular component||intracellular (GO:0005622)|
|Molecular function||3'-5' exonuclease activity (GO:0008408)|
|nucleic acid binding (GO:0003676)|
|Biological process||nucleobase-containing compound metabolic process (GO:0006139)|
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Curation and family details
|Seed source:||Pfam-B_659 (release 4.1)|
|Previous IDs:||3_5_exonuclease; 3_5_exonuc;|
|Author:||Bashton M, Bateman A, Griffiths-Jones SR|
|Number in seed:||27|
|Number in full:||6914|
|Average length of the domain:||173.20 aa|
|Average identity of full alignment:||23 %|
|Average coverage of the sequence by the domain:||27.78 %|
|HMM build commands:||
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||15|
|Download:||download the raw HMM for this family|
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For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the DNA_pol_A_exo1 domain has been found. There are 32 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein seqence.
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