The domain within your query sequence starts at position 208 and ends at position 273; the E-value for the DSRM domain shown below is 1.84e-18.

EISLVFEIALKRNMPVSFEVIKESGPPHMKSFVTRVSVGEFSAEGEGNSKKLSKKRAATT
VLQELK

DSRM

Double-stranded RNA binding motif

• SMART accession number: SM00358
• Description: -
• Interpro abstract (IPR014720):

  In contrast to other RNA-binding domains, the about 65 amino acids long dsRBD domain [ (PUBMED:1438302) (PUBMED:8036511) (PUBMED:7972084) ] has been found in a number of proteins that specifically recognise double-stranded RNAs. The dsRBD domain is also known as DSRM (Double-Stranded RNA-binding Motif). dsRBD proteins are mainly involved in posttranscriptional gene regulation, for example by preventing the expression of proteins or by mediating RNAs localization. This domain is also found in RNA editing proteins. Interaction of the dsRBD with RNA is unlikely to involve the recognition of specific sequences [ (PUBMED:1357546) (PUBMED:7527340) (PUBMED:8127710) ]. Nevertheless, multiple dsRBDs may be able to act in combination to recognise the secondary structure of specific RNAs (i.e. Staufen) [ (PUBMED:1438302) ]. NMR analysis of the third dsRBD of Drosophila Staufen have revealed an alpha-beta-beta-beta-alpha structure [ (PUBMED:7628456) ].

There are 49577 DSRM domains in 36103 proteins in SMART's nrdb database.

Cellular role (predicted cellular role)

Binding / catalysis: RNA binding

Literature (relevant references for this domain)

Primary literature is listed below; Automatically-derived, secondary literature is also avaliable.

• Mian IS
• Comparative sequence analysis of ribonucleases HII, III, II PH and D.
• Nucleic Acids Res. 1997; 25: 3187-95

Escherichia coli ribonucleases (RNases) HII, III, II, PH and D have been used to characterise new and known viral, bacterial, archaeal and eucaryotic sequences similar to these endo- (HII and III) and exoribonucleases (II, PH and D). Statistical models, hidden Markov models (HMMs), were created for the RNase HII, III, II and PH and D families as well as a double-stranded RNA binding domain present in RNase III. Results suggest that the RNase D family, which includes Werner syndrome protein and the 100 kDa antigenic component of the human polymyositis scleroderma (PMSCL) autoantigen, is a 3'-->5' exoribonuclease structurally and functionally related to the 3'-->5' exodeoxyribonuclease domain of DNA polymerases. Polynucleotide phosphorylases and the RNase PH family, which includes the 75 kDa PMSCL autoantigen, possess a common domain suggesting similar structures and mechanisms of action for these 3'-->5' phosphorolytic enzymes. Examination of HMM-generated multiple sequences alignments for each family suggest amino acids that may be important for their structure, substrate binding and/or catalysis.

• Zamore PD, Williamson JR, Lehmann R
• The Pumilio protein binds RNA through a conserved domain that defines a new class of RNA-binding proteins.
• RNA. 1997; 3: 1421-33

Translation of hunchback(mat) (hb[mat]) mRNA must be repressed in the posterior of the pre-blastoderm Drosophila embryo to permit formation of abdominal segments. This translational repression requires two copies of the Nanos Response Element (NRE), a 16-nt sequence in the hb[mat] 3' untranslated region. Translational repression also requires the action of two proteins: Pumilio (PUM), a sequence-specific RNA-binding protein; and Nanos, a protein that determines the location of repression. Binding of PUM to the NRE is thought to target hb(mat) mRNA for repression. Here, we show the RNA-binding domain of PUM to be an evolutionarily conserved, 334-amino acid region at the carboxy-terminus of the approximately 158-kDa PUM protein. This contiguous region of PUM retains the RNA-binding specificity of full-length PUM protein. Proteins with sequences homologous to the PUM RNA-binding domain are found in animals, plants, and fungi. The high degree of sequence conservation of the PUM RNA-binding domain in other far-flung species suggests that the domain is an ancient protein motif, and we show that conservation of sequence reflects conservation of function: that is, the homologous region from a human protein binds RNA with sequence specificity related to but distinct from Drosophila PUM.

• Burd CG, Dreyfuss G
• Conserved structures and diversity of functions of RNA-binding proteins.
• Science. 1994; 265: 615-21

In eukaryotic cells, a multitude of RNA-binding proteins play key roles in the posttranscriptional regulation of gene expression. Characterization of these proteins has led to the identification of several RNA-binding motifs, and recent experiments have begun to illustrate how several of them bind RNA. The significance of these interactions is reflected in the recent discoveries that several human and other vertebrate genetic disorders are caused by aberrant expression of RNA-binding proteins. The major RNA-binding motifs are described and examples of how they may function are given.

• StJohnston D, Brown NH, Gall JG, Jantsch M
• A conserved double-stranded RNA-binding domain.
• Proc Natl Acad Sci U S A. 1992; 89: 10979-83

We have identified a double-stranded (ds)RNA-binding domain in each of two proteins: the product of the Drosophila gene staufen, which is required for the localization of maternal mRNAs, and a protein of unknown function, Xlrbpa, from Xenopus. The amino acid sequences of the binding domains are similar to each other and to additional domains in each protein. Database searches identified similar domains in several other proteins known or thought to bind dsRNA, including human dsRNA-activated inhibitor (DAI), human trans-activating region (TAR)-binding protein, and Escherichia coli RNase III. By analyzing in detail one domain in staufen and one in Xlrbpa, we delimited the minimal region that binds dsRNA. On the basis of the binding studies and computer analysis, we have derived a consensus sequence that defines a 65- to 68-amino acid dsRNA-binding domain.

Metabolism (metabolic pathways involving proteins which contain this domain)

% proteins involved	KEGG pathway ID	Description
70.00	map00791	Atrazine degradation
20.00	map00230	Purine metabolism
10.00	map03010	Ribosome

This information is based on mapping of SMART genomic protein database to KEGG orthologous groups. Percentage points are related to the number of proteins with DSRM domain which could be assigned to a KEGG orthologous group, and not all proteins containing DSRM domain. Please note that proteins can be included in multiple pathways, ie. the numbers above will not always add up to 100%.

Structure (3D structures containing this domain)

3D Structures of DSRM domains in PDB

PDB code	Title
1di2	CRYSTAL STRUCTURE OF A DSRNA-BINDING DOMAIN COMPLEXED WITH DSRNA: MOLECULAR BASIS OF DOUBLE-STRANDED RNA-PROTEIN INTERACTIONS
1ekz	NMR STRUCTURE OF THE COMPLEX BETWEEN THE THIRD DSRBD FROM DROSOPHILA STAUFEN AND A RNA HAIRPIN
1o0w	Crystal structure of Ribonuclease III (TM1102) from Thermotoga maritima at 2.0 A resolution
1qu6	STRUCTURE OF THE DOUBLE-STRANDED RNA-BINDING DOMAIN OF THE PROTEIN KINASE PKR REVEALS THE MOLECULAR BASIS OF ITS DSRNA-MEDIATED ACTIVATION
1rc7	Crystal structure of RNase III Mutant E110K from Aquifex Aeolicus complexed with ds-RNA at 2.15 Angstrom Resolution
1stu	DOUBLE STRANDED RNA BINDING DOMAIN
1t4l	Solution structure of double-stranded RNA binding domain of S. cerevisiae RNase III (Rnt1p) in complex with the 5' terminal RNA hairpin of snR47 precursor
1t4n	Solution structure of Rnt1p dsRBD
1t4o	Crystal structure of rnt1p dsRBD
1uhz	Solution structure of dsRNA binding domain in Staufen homolog 2
1uil	Double-stranded RNA-binding motif of Hypothetical protein BAB28848
1whn	Solution structure of the dsRBD from hypothetical protein BAB26260
1whq	Solution structure of the N-terminal dsRBD from hypothetical protein BAB28848
1x47	Solution structure of DSRM domain in DGCR8 protein
1x48	Solution structure of the second DSRM domain in Interferon-induced, double-stranded RNA-activated protein kinase
1x49	Solution structure of the first DSRM domain in Interferon-induced, double-stranded RNA-activated protein kinase
1yyk	Crystal structure of RNase III from Aquifex Aeolicus complexed with double-stranded RNA at 2.5-angstrom resolution
1yyo	Crystal structure of RNase III mutant E110K from Aquifex aeolicus complexed with double-stranded RNA at 2.9-Angstrom Resolution
1yyw	Crystal structure of RNase III from Aquifex aeolicus complexed with double stranded RNA at 2.8-Angstrom Resolution
1yz9	Crystal structure of RNase III mutant E110Q from Aquifex aeolicus complexed with double stranded RNA at 2.1-Angstrom Resolution
2a11	Crystal Structure of Nuclease Domain of Ribonuclase III from Mycobacterium Tuberculosis
2b7t	Structure of ADAR2 dsRBM1
2b7v	Structure of ADAR2 dsRBM2
2cpn	Solution structure of the second dsRBD of TAR RNA-binding protein 2
2dix	Solution structure of the DSRM domain of Protein activator of the interferon-induced protein kinase
2dmy	Solution structure of DSRM domain in Spermatid perinuclear RNA-bind protein
2ez6	Crystal structure of Aquifex aeolicus RNase III (D44N) complexed with product of double-stranded RNA processing
2khx	Drosha double-stranded RNA binding motif
2l2k	Solution NMR structure of the R/G STEM LOOP RNA-ADAR2 DSRBM2 Complex
2l2m	Solution structure of the second dsRBD of HYL1
2l2n	Backbone 1H, 13C, and 15N Chemical Shift Assignments for the first dsRBD of protein HYL1
2l33	Solution NMR Structure of DRBM 2 domain of Interleukin enhancer-binding factor 3 from Homo sapiens, Northeast Structural Genomics Consortium Target HR4527E
2l3c	Solution structure of ADAR2 dsRBM1 bound to LSL RNA
2l3j	The solution structure of the ADAR2 dsRBM-RNA complex reveals a sequence-specific read out of the minor groove
2lbs	Solution structure of double-stranded RNA binding domain of S. cerevisiae RNase III (Rnt1p) in complex with AAGU tetraloop hairpin
2ljh	NMR structure of Double-stranded RNA-specific editase Adar
2lrs	The second dsRBD domain from A. thaliana DICER-LIKE 1
2ltr	Solution structure of RDE-4(32-136)
2lts	Solution structure of RDE-4(150-235)
2lup	RDC refined solution structure of double-stranded RNA binding domain of S. cerevisiae RNase III (rnt1p) in complex with the terminal RNA hairpin of snr47 precursor
2luq	Solution structure of double-stranded RNA binding domain of S.cerevisiae RNase III (rnt1p)
2mdr	Solution structure of the third double-stranded RNA-binding domain (dsRBD3) of human adenosine-deaminase ADAR1
2n3f	2N3F
2n3g	2N3G
2n3h	2N3H
2nue	Crystal structure of RNase III from Aquifex aeolicus complexed with ds-RNA at 2.9-Angstrom Resolution
2nuf	Crystal structure of RNase III from Aquifex aeolicus complexed with ds-RNA at 2.5-Angstrom Resolution
2nug	Crystal structure of RNase III from Aquifex aeolicus complexed with ds-RNA at 1.7-Angstrom Resolution
2rs6	Solution structure of the N-terminal dsRBD from RNA helicase A
2rs7	Solution structure of the second dsRBD from RNA helicase A
2yt4	Crystal structure of human DGCR8 core
3adg	Structure of Arabidopsis HYL1 and its molecular implications for miRNA processing
3adi	Structure of Arabidopsis HYL1 and its molecular implications for miRNA processing
3adj	Structure of Arabidopsis HYL1 and its molecular implications for miRNA processing
3adl	Structure of TRBP2 and its molecule implications for miRNA processing
3c4b	Structure of RNaseIIIb and dsRNA binding domains of mouse Dicer
3c4t	Structure of RNaseIIIb and dsRNA binding domains of mouse Dicer
3htx	Crystal structure of small RNA methyltransferase HEN1
3j6b	3J6B
3llh	Crystal structure of the first dsRBD of TAR RNA-binding protein 2
3n3w	2.2 Angstrom Resolution Crystal Structure of Nuclease Domain of Ribonuclase III (rnc) from Campylobacter jejuni
3p1x	Crystal structure of DRBM 2 domain of Interleukin enhancer-binding factor 3 from Homo sapiens, Northeast Structural Genomics Consortium Target HR4527E
3rv0	Crystal structure of K. polysporus Dcr1 without the C-terminal dsRBD
3vyx	Structural insights into RISC assembly facilitated by dsRNA binding domains of human RNA helicase (DHX9)
3vyy	Structural insights into RISC assembly facilitated by dsRNA binding domains of human RNA helicase A (DHX9)
4m2z	Crystal structure of RNASE III complexed with double-stranded RNA and CMP (TYPE II CLEAVAGE)
4m30	Crystal structure of RNASE III complexed with double-stranded RNA AND AMP (TYPE II CLEAVAGE)
4oog	Crystal structure of yeast RNase III (Rnt1p) complexed with the product of dsRNA processing
4wft	4WFT
4x8w	4X8W
5aor	5AOR
5b16	5B16
5dv7	5DV7

Links (links to other resources describing this domain)

• INTERPRO: IPR014720
• PFAM: dsrm