Summary: Hepatitis C virus non-structural 5a protein membrane anchor
Hepatitis C virus non-structural 5a protein membrane anchor Provide feedback
The molecular function of the non-structural 5a protein is uncertain. The NS5a protein is phosphorylated when expressed in mammalian cells. It is thought to interact with the ds RNA dependent (interferon inducible) kinase PKR, P19525 [1,2]. The N-terminal region of the NS5a protein has been used in the construction of the alignment for this family. The C-terminal region has not been included because it is too heterogeneous.
Gale M Jr, Blakely CM, Kwieciszewski B, Tan SL, Dossett M, Tang NM, Korth MJ, Polyak SJ, Gretch DR, Katze MG; , Mol Cell Biol 1998;18:5208-5218.: Control of PKR protein kinase by hepatitis C virus nonstructural 5A protein: molecular mechanisms of kinase regulation. PUBMED:9710605 EPMC:9710605
Gale MJ Jr, Korth MJ, Tang NM, Tan SL, Hopkins DA, Dever TE, Polyak SJ, Gretch DR, Katze MG; , Virology 1997;230:217-227.: Evidence that hepatitis C virus resistance to interferon is mediated through repression of the PKR protein kinase by the nonstructural 5A protein. PUBMED:9143277 EPMC:9143277
External database links
This tab holds annotation information from the InterPro database.
InterPro entry IPR002868The molecular function of the non-structural 5a viral protein is uncertain. The NS5a protein is phosphorylated when expressed in mammalian cells. It is thought to interact with the dsRNA-dependent (interferon inducible) kinase PKR, SWISSPROT [PUBMED:9710605, PUBMED:9143277].
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|Molecular function||serine-type endopeptidase activity (GO:0004252)|
|cysteine-type endopeptidase activity (GO:0004197)|
|nucleoside-triphosphatase activity (GO:0017111)|
|RNA-directed RNA polymerase activity (GO:0003968)|
- the number of sequences which exhibit this architecture
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This example describes an architecture with one
Gladomain, followed by two consecutive
EGFdomains, and finally a single
- the UniProt description of the protein sequence
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We make a range of alignments for each Pfam-A family:
- the curated alignment from which the HMM for the family is built
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Curation and family details
|Seed source:||Bateman A|
|Author:||Paterson M, Bateman A|
|Number in seed:||19|
|Number in full:||5540|
|Average length of the domain:||22.40 aa|
|Average identity of full alignment:||82 %|
|Average coverage of the sequence by the domain:||2.09 %|
|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:||14|
|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 HCV_NS5a domain has been found. There are 5 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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