| SMART accession number: | SM00360
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| Description: |
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| Interpro abstract (IPR000504): |
Many eukaryotic proteins that are known or supposed to bind single-stranded RNA contain one or more copies of a putative RNA-binding domain of about 90 amino acids. This is known as the eukaryotic putative RNA-binding region RNP-1 signature or RNA recognition motif (RRM). RRMs are found in a variety of RNA binding proteins, including heterogeneous nuclear ribonucleoproteins (hnRNPs), proteins implicated in regulation of alternative splicing, and protein components of small nuclear ribonucleoproteins (snRNPs). The motif also appears in a few single stranded DNA binding proteins. The RRM structure consists of four strands and two helices arranged in an alpha/beta sandwich, with a third helix present during RNA binding in some cases. Two individual models were built which identify subtypes of this domain, but there is no functional difference between the subtypes.
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| GO function: | RNA binding (GO:0003723) |
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| Family alignment: |
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Click on the following links for more information.
- Evolution (species in which this domain is found)
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- Cellular role (predicted cellular role)
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Binding / catalysis: RNA-binding
- Literature (relevant references for this domain)
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Primary literature is listed below; Automatically-derived, secondary literature is also avaliable.
- Birney E, Kumar S, Krainer AR
- Analysis of the RNA-recognition motif and RS and RGG domains: conservation in metazoan pre-mRNA splicing factors.
- Nucleic Acids Res. 1993; 21: 5803-16
- Display abstract
We present a systematic analysis of sequence motifs found in metazoan protein factors involved in constitutive pre-mRNA splicing and in alternative splicing regulation. Using profile analysis we constructed a database enriched in protein sequences containing one or more presumptive copies of the RNA-recognition motif (RRM). We provide an accurate alignment of RRMs and structure-based criteria for identifying new RRMs, including many that lack the prototype RNP-1 submotif. We present a comprehensive table of 125 sequences containing 252 RRMs, including 22 previously unreported RRMs in 17 proteins. The presence of a putative RRM in these proteins, which are implicated in a variety of cellular processes, strongly suggests that their function involves binding to RNA. Unreported homologies in the RRM-enriched database to the metazoan SR family of splicing factors are described for an Arg-rich human nuclear protein and two yeast proteins (S. pombe mei2 and S. cerevisiae Npl3). We have rigorously tested the phylogenetic relationships of a large sample of RRMs. This analysis indicates that the RRM is an ancient conserved region (ACR) that has diversified by duplication of genes and intragenic domains. Statistical analyses and classification of repeated Arg-Ser (RS) and RGG domains in various protein splicing factors are presented.
- Structure (3D structures containing this domain)
3D Structures of RRM domains in PDB
1a9n, 1aud, 1b7f, 1cvj, 1cx0, 1d8z, 1d9a, 1drz, 1dz5, 1fht, 1fj7, 1fjc, 1fje, 1fnx, 1fxl, 1g2e, 1h2t, 1h2u, 1h2v, 1h6k, 1ha1, 1hd0, 1hd1, 1hl6, 1iqt, 1jmt, 1l3k, 1m5k, 1m5o, 1m5p, 1m5v, 1n52, 1n54, 1no8, 1nu4, 1o0p, 1oia, 1oo0, 1opi, 1p1t, 1p27, 1pgz, 1po6, 1qm9, 1rk8, 1rkj, 1s79, 1sj3, 1sj4, 1sjf, 1sjq, 1sjr, 1sxl, 1u1k, 1u1l, 1u1m, 1u1n, 1u1o, 1u1p, 1u1q, 1u1r, 1u2f, 1u6b, 1u6f, 1uaw, 1up1, 1urn, 1vbx, 1vby, 1vbz, 1vc0, 1vc5, 1vc6, 1vc7, 1wel, 1wex, 1wez, 1wf0, 1wf1, 1wf2, 1wg1, 1wg4, 1wg5, 1whw, 1whx, 1why, 1wi6, 1wi8, 1wtb, 1x0f, 1zzn, 2ad9, 2adb, 2adc, 2mss, 2mst, 2sxl, 2u1a, 2u2f, 2up1, 3sxl
- Links (links to other resources describing this domain)
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to expand nodes. To display all proteins with a RRM domain in a specific node, click on it.