Summary: Rotavirus non-structural protein NSP3
Rotavirus non-structural protein NSP3 Provide feedback
This family consist of rotaviral non-structural RNA binding protein 34 (NS34 or NSP3). The NSP3 protein has been shown to bind viral RNA. The NSP3 protein consists of 3 conserved functional domains; a basic region which binds ssRNA, a region containing heptapeptide repeats mediating oligomerisation and a leucine zipper motif . NSP3 may play a central role in replication and assembly of genomic RNA structures . Rotaviruses have a dsRNA genome and are a major cause cause of acute gastroenteritis in the young of many species . The rotavirus non-structural protein NSP3 is a sequence-specific RNA binding protein that binds the nonpolyadenylated 3' end of the rotavirus mRNAs. NSP3 also interacts with the translation initiation factor eIF4GI and competes with the poly(A) binding protein .
Rao CD, Das M, Ilango P, Lalwani R, Rao BS, Gowda K; , Virology 1995;207:327-333.: Comparative nucleotide and amino acid sequence analysis of the sequence- specific RNA-binding rotavirus nonstructural protein NSP3. PUBMED:7871749 EPMC:7871749
Mattion NM, Cohen J, Aponte C, Estes MK; , Virology 1992;190:68-83.: Characterization of an oligomerization domain and RNA-binding properties on rotavirus nonstructural protein NS34. PUBMED:1326821 EPMC:1326821
Piron M, Vende P, Cohen J, Poncet D; , EMBO J 1998;17:5811-5821.: Rotavirus RNA-binding protein NSP3 interacts with eIF4GI and evicts the poly(A) binding protein from eIF4F. PUBMED:9755181 EPMC:9755181
External database links
This tab holds annotation information from the InterPro database.
InterPro entry IPR002873
This family consists of rotaviral non-structural RNA binding protein 34 (NS34 or NSP3). The NSP3 protein has been shown to bind viral RNA. The NSP3 protein consists of 3 conserved functional domains; a basic region which binds ssRNA, a region containing heptapeptide repeats mediating oligomerisation and a leucine zipper motif [PUBMED:1326821]. NSP3 may play a central role in replication and assembly of genomic RNA structures [PUBMED:1326821]. Rotaviruses have a dsRNA genome and are a major cause cause of acute gastroenteritis in the young of many species [PUBMED:7871749].
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|Molecular function||RNA binding (GO:0003723)|
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We make a range of alignments for each Pfam-A family:
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Curation and family details
|Seed source:||Pfam-B_1010 (release 4.1)|
|Author:||Bashton M, Bateman A|
|Number in seed:||6|
|Number in full:||508|
|Average length of the domain:||266.80 aa|
|Average identity of full alignment:||87 %|
|Average coverage of the sequence by the domain:||89.08 %|
|HMM build commands:||
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||11|
|Download:||download the raw HMM for this family|
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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 Rota_NSP3 domain has been found. There are 10 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 seqence.
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