!!

Powering down the Pfam website
On October 5th, we began redirecting traffic from Pfam (pfam.xfam.org) to InterPro (www.ebi.ac.uk/interpro). The Pfam website will remain available at pfam-legacy.xfam.org until January 2023, when it will be decommissioned. You can read more about the sunset period in our blog post.

Please note: this site relies heavily on the use of javascript. Without a javascript-enabled browser, this site will not function correctly. Please enable javascript and reload the page, or switch to a different browser.
1349  structures 3091  species 0  interactions 370166  sequences 3801  architectures

Family: RRM_1 (PF00076)

Summary: RNA recognition motif. (a.k.a. RRM, RBD, or RNP domain)

Pfam includes annotations and additional family information from a range of different sources. These sources can be accessed via the tabs below.

This is the Wikipedia entry entitled "RNA recognition motif". More...

RNA recognition motif Edit Wikipedia article

RNA recognition motif. (a.k.a. RRM, RBD, or RNP domain)
Identifiers
SymbolRRM_1
PfamPF00076
InterProIPR000504
PROSITEPDOC00030
SCOP21sxl / SCOPe / SUPFAM


RNA recognition motif, RNP-1 is a putative RNA-binding domain of about 90 amino acids are known to bind single-stranded RNAs. It was found in many eukaryotic proteins[1][2][3]. The largest group of single strand RNA-binding proteins is the eukaryotic RNA recognition motif (RRM) family that contains an eight amino acid RNP-1 consensus sequence[4][5]. RRM proteins have a variety of RNA binding preferences and functions, and include heterogeneous nuclear ribonucleoproteins (hnRNPs), proteins implicated in regulation of alternative splicing (SR, U2AF, Sxl), protein components of small nuclear ribonucleoproteins (U1 and U2 snRNPs), and proteins that regulate RNA stability and translation (PABP, La, Hu)[2][3][5]. The RRM in heterodimeric splicing factor U2 snRNP auxiliary factor (U2AF) appears to have two RRM-like domains with specialised features for protein recognition[6]. The motif also appears in a few single stranded DNA binding proteins.

The typical RRM consists of four anti-parallel beta-strands and two alpha-helices arranged in a beta-alpha-beta-beta-alpha-beta fold with side chains that stack with RNA bases. Specificity of RNA binding is determined by multiple contacts with surrounding amino acids. A third helix is present during RNA binding in some cases[7]. The RRM is reviewed in a number of publications[8][9][10].

Human proteins containing this domain

A2BP1; ACF; BOLL; BRUNOL4; BRUNOL5; BRUNOL6; CCBL2; CGI-96; CIRBP; CNOT4; CPEB2; CPEB3; CPEB4; CPSF7; CSTF2; CSTF2T; CUGBP1; CUGBP2; D10S102; DAZ1; DAZ2; DAZ3; DAZ4; DAZAP1; DAZL; DNAJC17; DND1; EIF3S4; EIF3S9; EIF4B; EIF4H; ELAVL1; ELAVL2; ELAVL3; ELAVL4; ENOX1; ENOX2; EWSR1; FUS; FUSIP1; G3BP; G3BP1; G3BP2; GRSF1; HNRNPL; HNRPA0; HNRPA1; HNRPA2B1; HNRPA3; HNRPAB; HNRPC; HNRPCL1; HNRPD; HNRPDL; HNRPF; HNRPH1; HNRPH2; HNRPH3; HNRPL; HNRPLL; HNRPM; HNRPR; HRNBP1; HSU53209; HTATSF1; IGF2BP1; IGF2BP2; IGF2BP3; LARP7; LOC144983; LOC346472; LOC390748; LOC392647; LOC392896; LOC728773; LOC92906; MKI67IP; MSI1; MSI2; MSSP-2; MTHFSD; MYEF2; NCBP2; NCL; NOL8; NONO; ORF; P14; PABPC1; PABPC1L; PABPC3; PABPC4; PABPC5; PABPN1; POLDIP3; PPARGC1; PPARGC1A; PPARGC1B; PPIE; PPIL4; PPRC1; PSPC1; PTBP1; PTBP2; PUF60; RALY; RALYL; RAVER1; RAVER2; RBM10; RBM11; RBM12; RBM12B; RBM14; RBM15; RBM15B; RBM16; RBM17; RBM18; RBM19; RBM22; RBM23; RBM24; RBM25; RBM26; RBM27; RBM28; RBM3; RBM32B; RBM33; RBM34; RBM35A; RBM35B; RBM38; RBM39; RBM4; RBM41; RBM42; RBM44; RBM45; RBM46; RBM47; RBM4B; RBM5; RBM7; RBM8A; RBM9; RBMS1; RBMS2; RBMS3; RBMX; RBMX2; RBMXL2; RBMY1A1; RBMY1B; RBMY1E; RBMY1F; RBMY2FP; RBPMS; RBPMS2; RDBP; RNPC3; RNPC4; RNPS1; ROD1; SAFB; SAFB2; SART3; SETD1A; SF3B14; SF3B4; SFPQ; SFRS1; SFRS10; SFRS11; SFRS12; SFRS15; SFRS2; SFRS2B; SFRS3; SFRS4; SFRS5; SFRS6; SFRS7; SFRS9; SLIRP; SLTM; SNRP70; SNRPA; SNRPB2; SPEN; SR140; SRRP35; SSB; SYNCRIP; TAF15; TARDBP; THOC4; TIA1; TIAL1; TNRC4; TNRC6C; TRA2A; TRSPAP1; TUT1; U1SNRNPBP; U2AF1; U2AF2; UHMK1; ZCRB1; ZNF638; ZRSR1; ZRSR2; eIF4B;

References

  1. ^ Swanson MS, Dreyfuss G, Pinol-Roma S (1988). "Heterogeneous nuclear ribonucleoprotein particles and the pathway of mRNA formation". Trends Biochem. Sci. 13 (3): 86–91. PMID 3072706.{{cite journal}}: CS1 maint: multiple names: authors list (link)
  2. ^ a b Keene JD, Chambers JC, Kenan D, Martin BJ (1988). "Genomic structure and amino acid sequence domains of the human La autoantigen". J. Biol. Chem. 263 (34): -. PMID 3192525.{{cite journal}}: CS1 maint: multiple names: authors list (link)
  3. ^ a b Davis RW, Sachs AB, Kornberg RD (1987). "A single domain of yeast poly(A)-binding protein is necessary and sufficient for RNA binding and cell viability". Mol. Cell. Biol. 7 (9): -. PMID 3313012.{{cite journal}}: CS1 maint: multiple names: authors list (link)
  4. ^ Bandziulis RJ, Swanson MS, Dreyfuss G (1989). "RNA-binding proteins as developmental regulators". Genes Dev. 3 (4): 431–437. PMID 2470643.{{cite journal}}: CS1 maint: multiple names: authors list (link)
  5. ^ a b Keene JD, Query CC, Bentley RC (1989). "A common RNA recognition motif identified within a defined U1 RNA binding domain of the 70K U1 snRNP protein". Cell. 57 (1): -. PMID 2467746.{{cite journal}}: CS1 maint: multiple names: authors list (link)
  6. ^ Green MR, Kielkopf CL, Lucke S (2004). "U2AF homology motifs: protein recognition in the RRM world". Genes Dev. 18 (13): 1513–1526. PMID 15231733.{{cite journal}}: CS1 maint: multiple names: authors list (link)
  7. ^ Kumar S, Birney E, Krainer AR (1993). "Analysis of the RNA-recognition motif and RS and RGG domains: conservation in metazoan pre-mRNA splicing factors". Nucleic Acids Res. 21 (25): 5803–5816. PMID 8290338.{{cite journal}}: CS1 maint: multiple names: authors list (link)
  8. ^ Keene JD, Kenan DJ, Query CC (1991). "RNA recognition: towards identifying determinants of specificity". Trends Biochem. Sci. 16 (6): -. PMID 1716386.{{cite journal}}: CS1 maint: multiple names: authors list (link)
  9. ^ Allain FH, Dominguez C, Maris C (2005). "The RNA recognition motif, a plastic RNA-binding platform to regulate post-transcriptional gene expression". FEBS J. 272 (9): -. PMID 15853797.{{cite journal}}: CS1 maint: multiple names: authors list (link)
  10. ^ Teplova M, Yuan YR, Patel DJ, Malinina L, Teplov A, Phan AT, Ilin S (2006). "Structural basis for recognition and sequestration of UUU(OH) 3' temini of nascent RNA polymerase III transcripts by La, a rheumatic disease autoantigen". Mol. Cell. 21 (1): -. PMID 16387655.{{cite journal}}: CS1 maint: multiple names: authors list (link)
This article incorporates text from the public domain Pfam and InterPro: IPR000504

This page is based on a Wikipedia article. The text is available under the Creative Commons Attribution/Share-Alike License.

This tab holds the annotation information that is stored in the Pfam database. As we move to using Wikipedia as our main source of annotation, the contents of this tab will be gradually replaced by the Wikipedia tab.

RNA recognition motif. (a.k.a. RRM, RBD, or RNP domain) Provide feedback

The RRM motif is probably diagnostic of an RNA binding protein. RRMs are found in a variety of RNA binding proteins, including various hnRNP proteins, proteins implicated in regulation of alternative splicing, and protein components of 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 The C-terminal beta strand (4th strand) and final helix are hard to align and have been omitted in the SEED alignment The LA proteins (P05455) have an N terminal rrm which is included in the seed. There is a second region towards the C terminus that has some features characteristic of a rrm but does not appear to have the important structural core of a rrm. The LA proteins (P05455) are one of the main autoantigens in Systemic lupus erythematosus (SLE), an autoimmune disease.

Literature references

  1. Birney E., Kumar S., Krainer A.R. , Nucleic Acid Res 1993;21:5803-5816.: Analysis of the RNA-recognition motif and RS and RGG domains: conservation in metazoan pre-mRNA splicing factors. PUBMED:8290338 EPMC:8290338


Internal database links

External database links

This tab holds annotation information from the InterPro database.

InterPro entry IPR000504

Many eukaryotic proteins containing one or more copies of a putative RNA-binding domain of about 90 amino acids are known to bind single-stranded RNAs [ PUBMED:3072706 , PUBMED:3192525 , PUBMED:3313012 ]. The largest group of single strand RNA-binding proteins is the eukaryotic RNA recognition motif (RRM) family that contains an eight amino acid RNP-1 consensus sequence [ PUBMED:2470643 , PUBMED:2467746 ]. RRM proteins have a variety of RNA binding preferences and functions, and include heterogeneous nuclear ribonucleoproteins (hnRNPs), proteins implicated in regulation of alternative splicing (SR, U2AF, Sxl), protein components of small nuclear ribonucleoproteins (U1 and U2 snRNPs), and proteins that regulate RNA stability and translation (PABP, La, Hu) [ PUBMED:3192525 , PUBMED:3313012 , PUBMED:2467746 ]. The RRM in heterodimeric splicing factor U2 snRNP auxiliary factor (U2AF) appears to have two RRM-like domains with specialised features for protein recognition [ PUBMED:15231733 ]. The motif also appears in a few single stranded DNA binding proteins.

The typical RRM consists of four anti-parallel beta-strands and two alpha-helices arranged in a beta-alpha-beta-beta-alpha-beta fold with side chains that stack with RNA bases. Specificity of RNA binding is determined by multiple contacts with surrounding amino acids. A third helix is present during RNA binding in some cases [ PUBMED:8290338 ]. The RRM is reviewed in a number of publications [ PUBMED:1716386 , PUBMED:15853797 , PUBMED:16387655 ].

Gene Ontology

The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.

Domain organisation

Below is a listing of the unique domain organisations or architectures in which this domain is found. More...

Loading domain graphics...

Pfam Clan

This family is a member of clan RRM (CL0221), which has the following description:

This clan contains families that are related to the RNA recognition motif domains. However, not all these families are RNA binding.

The clan contains the following 33 members:

BRAP2 Calcipressin DbpA DUF1743 DUF1866 DUF4523 GlcNAc-1_reg GUCT MARF1_RRM1 Nup35_RRM Nup35_RRM_2 PHM7_cyt Ret2_MD RL RNA_bind RRM_1 RRM_2 RRM_3 RRM_5 RRM_7 RRM_8 RRM_9 RRM_occluded RRM_Rrp7 SET_assoc Smg4_UPF3 Spo7_2_N Tap-RNA_bind Transposase_22 U1snRNP70_N xRRM XS YlmH_RBD

Alignments

We store a range of different sequence alignments for families. As well as the seed alignment from which the family is built, we provide the full alignment, generated by searching the sequence database (reference proteomes) using the family HMM. We also generate alignments using four representative proteomes (RP) sets and the UniProtKB sequence database. More...

View options

We make a range of alignments for each Pfam-A family. You can see a description of each above. You can view these alignments in various ways but please note that some types of alignment are never generated while others may not be available for all families, most commonly because the alignments are too large to handle.

  Seed
(68)
Full
(370166)
Representative proteomes UniProt
(607422)
RP15
(60121)
RP35
(151111)
RP55
(282223)
RP75
(384008)
Jalview View  View  View  View  View  View  View 
HTML View             
PP/heatmap 1            

1Cannot generate PP/Heatmap alignments for seeds; no PP data available

Key: ✓ available, x not generated, not available.

Format an alignment

  Seed
(68)
Full
(370166)
Representative proteomes UniProt
(607422)
RP15
(60121)
RP35
(151111)
RP55
(282223)
RP75
(384008)
Alignment:
Format:
Order:
Sequence:
Gaps:
Download/view:

Download options

We make all of our alignments available in Stockholm format. You can download them here as raw, plain text files or as gzip-compressed files.

  Seed
(68)
Full
(370166)
Representative proteomes UniProt
(607422)
RP15
(60121)
RP35
(151111)
RP55
(282223)
RP75
(384008)
Raw Stockholm Download   Download   Download   Download   Download      
Gzipped Download   Download   Download   Download   Download      

You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.

HMM logo

HMM logos is one way of visualising profile HMMs. Logos provide a quick overview of the properties of an HMM in a graphical form. You can see a more detailed description of HMM logos and find out how you can interpret them here. More...

Trees

This page displays the phylogenetic tree for this family's seed alignment. We use FastTree to calculate neighbour join trees with a local bootstrap based on 100 resamples (shown next to the tree nodes). FastTree calculates approximately-maximum-likelihood phylogenetic trees from our seed alignment.

Note: You can also download the data file for the tree.

Curation and family details

This section shows the detailed information about the Pfam family. You can see the definitions of many of the terms in this section in the glossary and a fuller explanation of the scoring system that we use in the scores section of the help pages.

Curation View help on the curation process

Seed source: Published_alignment
Previous IDs: rrm;
Type: Domain
Sequence Ontology: SO:0000417
Author: Eddy SR , Birney E
Number in seed: 68
Number in full: 370166
Average length of the domain: 67.4 aa
Average identity of full alignment: 23 %
Average coverage of the sequence by the domain: 22.58 %

HMM information View help on HMM parameters

HMM build commands:
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 61295632 -E 1000 --cpu 4 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 20.7 20.7
Trusted cut-off 20.7 20.7
Noise cut-off 20.6 20.6
Model length: 70
Family (HMM) version: 25
Download: download the raw HMM for this family

Species distribution

Sunburst controls

Hide

Weight segments by...


Change the size of the sunburst

Small
Large

Colour assignments

Archea Archea Eukaryota Eukaryota
Bacteria Bacteria Other sequences Other sequences
Viruses Viruses Unclassified Unclassified
Viroids Viroids Unclassified sequence Unclassified sequence

Selections

Generate a FASTA-format file

Clear selection

This visualisation provides a simple graphical representation of the distribution of this family across species. You can find the original interactive tree in the adjacent tab. More...

Loading sunburst data...

Tree controls

Hide

The tree shows the occurrence of this domain across different species. More...

Loading...

Please note: for large trees this can take some time. While the tree is loading, you can safely switch away from this tab but if you browse away from the family page entirely, the tree will not be loaded.

Structures

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 RRM_1 domain has been found. There are 1349 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 sequence.

Loading structure mapping...

AlphaFold Structure Predictions

The list of proteins below match this family and have AlphaFold predicted structures. Click on the protein accession to view the predicted structure.

Protein Predicted structure External Information
A0A023GRW3 View 3D Structure Click here
A0A044QJK5 View 3D Structure Click here
A0A044QMU1 View 3D Structure Click here
A0A044QWW4 View 3D Structure Click here
A0A044QYF6 View 3D Structure Click here
A0A044QZN3 View 3D Structure Click here
A0A044R0Y4 View 3D Structure Click here
A0A044R230 View 3D Structure Click here
A0A044R537 View 3D Structure Click here
A0A044R8G9 View 3D Structure Click here
A0A044RF39 View 3D Structure Click here
A0A044RFK9 View 3D Structure Click here
A0A044RG24 View 3D Structure Click here
A0A044RL20 View 3D Structure Click here
A0A044RLJ6 View 3D Structure Click here
A0A044RLK2 View 3D Structure Click here
A0A044RR67 View 3D Structure Click here
A0A044S1M2 View 3D Structure Click here
A0A044S2I1 View 3D Structure Click here
A0A044S4S4 View 3D Structure Click here
A0A044S6J5 View 3D Structure Click here
A0A044SDX3 View 3D Structure Click here
A0A044SFM9 View 3D Structure Click here
A0A044SIV5 View 3D Structure Click here
A0A044SIW0 View 3D Structure Click here
A0A044SKP8 View 3D Structure Click here
A0A044SMT2 View 3D Structure Click here
A0A044SPU6 View 3D Structure Click here
A0A044STG1 View 3D Structure Click here
A0A044SUD3 View 3D Structure Click here
A0A044SZY4 View 3D Structure Click here
A0A044T1W6 View 3D Structure Click here
A0A044T1Y1 View 3D Structure Click here
A0A044T2B5 View 3D Structure Click here
A0A044TA51 View 3D Structure Click here
A0A044TBY8 View 3D Structure Click here
A0A044TD44 View 3D Structure Click here
A0A044TDF5 View 3D Structure Click here
A0A044TFN6 View 3D Structure Click here
A0A044TFW6 View 3D Structure Click here