Summary: Reovirus sigma C capsid protein
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Reovirus sigma C capsid protein Provide feedback
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Grande A, Costas C, Benavente J; , J Gen Virol 2002;83:131-139.: Subunit composition and conformational stability of the oligomeric form of the avian reovirus cell-attachment protein sigmaC. PUBMED:11752709 EPMC:11752709
External database links
This tab holds annotation information from the InterPro database.
InterPro entry IPR007662Protein sigmaC in its native state was shown to be a homotrimer. It was demonstrated that the sigmaC subunits are not covalently bound via disulphide linkages and the formation of an intrachain disulphide bond between the two cysteine residues of the sigmaC polypeptide may have a negative effect on oligomer stability. The susceptibility of the trimer to pH, temperature, ionic strength, chemical denaturants and detergents indicates that hydrophobic interactions contribute much more to oligomer stability than do ionic interactions and hydrogen bonding [PUBMED:11752709].
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Curation and family details
|Seed source:||Pfam-B_2922 (release 7.5)|
|Number in seed:||4|
|Number in full:||160|
|Average length of the domain:||239.10 aa|
|Average identity of full alignment:||45 %|
|Average coverage of the sequence by the domain:||97.25 %|
|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:||7|
|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 Reo_sigmaC domain has been found. There are 7 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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