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InterPro: IPR001159 Double-stranded RNA binding

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UniProtKB

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3214 proteins

Overview:	sorted by AC,	sorted by name,	of known structure,	proteins with splice variants
Detailed:	sorted by AC,	sorted by name,	of known structure	proteins with splice variants
Table:	For all matching proteins,	of known structure
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Accession List
Matches in BioMart

Accession

IPR001159 Ds-RNA_bd

Type

Domain

Signatures Help

Database	ID	Name	Proteins
Pfam	PF00035	dsrm	3074
PROSITE profile	PS50137	DS_RBD	3021
SMART	SM00358	DSRM	3005
Signatures in BioMart

InterPro Relationships Help

Parent

IPR014720 Double-stranded RNA-binding-like

Found in

IPR009179 Interferon resistance/PKR inhibitor, vaccinia E3L type
IPR011907 Ribonuclease III, bacterial

GO Term annotation Help

Function

GO:0003725 double-stranded RNA binding

Component

GO:0005622 intracellular

InterPro annotation

Entry Details in BioMart

Abstract

The DsRBD domain is found in a variety of RNA-binding proteins with different structures and exhibiting a diversity of functions [1]. It is involved in localisation of at least five different mRNAs in the early Drosophila embryo and by interferon-induced protein kinase in humans, which is part of the cellular response to dsRNA.

Structural links Help

PDB - click here

SCOP: d.50.1.1

CATH: 3.30.160.20

Database links Help

Enzyme: EC:3.1.26

PROSITE doc: PDOC50137

PANDIT: PF00035

Blocks: IPB001159

Pfam Clan: CL0196.8

Interactions Help

This domain has been experimentally proven to be involved in Protein:Protein interactions.
Representative data is shown with the following example proteins:

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR001159

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

O01326 Ribonuclease 3

O70133 ATP-dependent RNA helicase A

O75569 Interferon-inducible double stranded RNA-dependent protein kinase activator A

P25159 Maternal effect protein staufen

Q02555 Ribonuclease 3

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR001159	Double-stranded RNA binding
IPR014021	Helicase, superfamily 1/2, ATP-binding domain
IPR011709	Domain of unknown function DUF1605
IPR000999	Ribonuclease III
IPR002464	DNA/RNA helicase, ATP-dependent, DEAH-box type, conserved site
IPR001650	DNA/RNA helicase, C-terminal
IPR007502	Helicase-associated domain
IPR011545	DNA/RNA helicase, DEAD/DEAH box type, N-terminal
IPR014001	DEAD-like helicase, N-terminal
IPR014720	Double-stranded RNA-binding-like
	PDB Chain
	ModBase
	CATH Domain
	SWISS-MODEL
	SCOP Domain

Publications Open in usermanual
1.	Burd CG, Dreyfuss G. Conserved structures and diversity of functions of RNA-binding proteins. Science 265 615-21 1994 [PubMed: 8036511] http://www.sciencemag.org/cgi/content/abstract/265/5172/615

Additional Reading Open in usermanual
	Gan J, Tropea JE, Austin BP, Court DL, Waugh DS, Ji X. Intermediate states of ribonuclease III in complex with double-stranded RNA. Structure 13 2005 1435-42 [PubMed: 16216575] http://dx.doi.org/10.1016/j.str.2005.06.014
	Blaszczyk J, Gan J, Tropea JE, Court DL, Waugh DS, Ji X. Noncatalytic assembly of ribonuclease III with double-stranded RNA. Structure 12 2004 457-66 [PubMed: 15016361] http://dx.doi.org/10.1016/j.str.2004.02.004
	Manche L, Green SR, Schmedt C, Mathews MB. Interactions between double-stranded RNA regulators and the protein kinase DAI. Mol. Cell. Biol. 12 1992 5238-48 [PubMed: 1357546] http://ukpmc.ac.uk/picrender.cgi?tool=EBI&pubmedid=1357546&action=stream&blobtype=pdf
	Kim U, Wang Y, Sanford T, Zeng Y, Nishikura K. Molecular cloning of cDNA for double-stranded RNA adenosine deaminase, a candidate enzyme for nuclear RNA editing. Proc. Natl. Acad. Sci. U.S.A. 91 1994 11457-61 [PubMed: 7972084] http://ukpmc.ac.uk/articlerender.cgi?tool=EBI&pubmedid=7972084
	Stefl R, Xu M, Skrisovska L, Emeson RB, Allain FH. Structure and specific RNA binding of ADAR2 double-stranded RNA binding motifs. Structure 14 2006 345-55 [PubMed: 16472753] http://dx.doi.org/10.1016/j.str.2005.11.013
	Bycroft M, Grunert S, Murzin AG, Proctor M, St Johnston D. NMR solution structure of a dsRNA binding domain from Drosophila staufen protein reveals homology to the N-terminal domain of ribosomal protein S5. EMBO J. 14 1995 3563-71 [PubMed: 7628456] http://ukpmc.ac.uk/articlerender.cgi?tool=EBI&pubmedid=7628456
	Gan J, Shaw G, Tropea JE, Waugh DS, Court DL, Ji X. A stepwise model for double-stranded RNA processing by ribonuclease III. Mol. Microbiol. 67 2008 143-54 [PubMed: 18047582]
	Gan J, Tropea JE, Austin BP, Court DL, Waugh DS, Ji X. Structural insight into the mechanism of double-stranded RNA processing by ribonuclease III. Cell 124 2006 355-66 [PubMed: 16439209] http://dx.doi.org/10.1016/j.cell.2005.11.034
	Tahbaz N, Kolb FA, Zhang H, Jaronczyk K, Filipowicz W, Hobman TC. Characterization of the interactions between mammalian PAZ PIWI domain proteins and Dicer. EMBO Rep. 5 2004 189-94 [PubMed: 14749716] http://dx.doi.org/10.1038/sj.embor.7400070
	Schweisguth DC, Chelladurai BS, Nicholson AW, Moore PB. Structural characterization of a ribonuclease III processing signal. Nucleic Acids Res. 22 1994 604-12 [PubMed: 8127710] http://dx.doi.org/10.1093/nar/22.4.604
	Polson AG, Bass BL. Preferential selection of adenosines for modification by double-stranded RNA adenosine deaminase. EMBO J. 13 1994 5701-11 [PubMed: 7527340] http://ukpmc.ac.uk/picrender.cgi?tool=EBI&pubmedid=7527340&action=stream&blobtype=pdf

InterPro 23.1