PWIPWI, domain in splicing factors |
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| SMART accession number: | SM00311
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| Description: |
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| Interpro abstract (IPR002483): |
The PWI domain, named after a highly conserved PWI tri-peptide located within its N-terminal region, is a ~80 amino acid module, which is found either at the N terminus or at the C terminus of eukaryotic proteins involved in pre-mRNA processing [(PUBMED:10322432)]. It is generally found in association with other domains such as RRM and RS. The PWI domain is a RNA/DNA-binding domain that has an equal preference for single- and double-stranded nucleic acids and is likely to have multiple important functions in pre-mRNA processing [(PUBMED:12600940)]. Proteins containing this domain include the SR-related nuclear matrix protein of 160kDa (SRm160) splicing and 3'-end cleavage-stimulatory factor, and the mammalian splicing factor PRP3. The PWI domain is a soluble, globular and independently folded domain which consists of a four-helix bundle, with structured N- and C-terminal elements [(PUBMED:12600940)].
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| GO process: | mRNA processing (GO:0006397) |
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There are 170
PWI domains in 170 proteins in SMART's nrdb database.
Click on the following links for more information.
- Evolution (species in which this domain is found)
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- Literature (relevant references for this domain)
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Primary literature is listed below; Automatically-derived, secondary literature is also avaliable.
- Szymczyna BR et al.
- Structure and function of the PWI motif: a novel nucleic acid-binding domain that facilitates pre-mRNA processing.
- Genes Dev. 2003; 17: 461-75
- Display abstract
The PWI motif is a highly conserved domain of unknown function in the SRm160 splicing and 3'-end cleavage-stimulatory factor, as well as in several other known or putative pre-mRNA processing components. We show here that the PWI motif is a new type of RNA/DNA-binding domain that has an equal preference for single- and double-stranded nucleic acids. Deletion of the motif prevents SRm160 from binding RNA and stimulating 3'-end cleavage, and its substitution with a heterologous RNA-binding domain restores these functions. The NMR solution structure of the SRm160-PWI motif reveals a novel, four-helix bundle and represents the first example of an alpha-helical fold that can bind single-stranded (ss)RNA. Structure-guided mutagenesis indicates that the same surface is involved in RNA and DNA binding and requires the cooperative action of a highly conserved, adjacent basic region. Thus, the PWI motif is a novel type of nucleic acid-binding domain that likely has multiple important functions in pre-mRNA processing, including SRm160-dependent stimulation of 3'-end formation.
- Structure (3D structures containing this domain)
3D Structures of PWI domains in PDB
| PDB code | Main view | Title | | 1mp1 |  | Solution structure of the pwi motif from srm160 |
| 1x4q |  | Solution structure of pwi domain in u4/u6 small nuclear ribonucleoprotein prp3(hprp3) |
- Links (links to other resources describing this domain)
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