Summary
C protein of Paramyovirinae families
C proteins of the Paramyxovirinae families are one of several genes transcribed from overlapping frames of the phosphoprotein (P) gene. The C proteins cluster in three groups, which are made up of measles, Nipah, and Sendai viruses. All C proteins have a similar organisation which consists of a variable, disordered N-terminus and a conserved, alpha-helical C-terminus [1].
This clan contains 3 families and the total number of domains in the clan is 28. The clan was built by P Coggill.
Literature references
- Lo MK, Sogaard TM, Karlin DG;, PLoS One. 2014;9:e90003.: Evolution and structural organization of the C proteins of paramyxovirinae. PUBMED:24587180 EPMC:24587180
Members
This clan contains the following 3 member families:
C_Hendra Paramyxo_C Paramyxo_NS_CDomain organisation
Below is a listing of the unique domain organisations or architectures from this clan. More...
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Alignments
The table below shows the number of occurrences of each domain throughout the sequence database. More...
Pfam family | Num. domains | Alignment |
---|---|---|
C_Hendra (PF16821) | 14 (50.0%) | View |
Paramyxo_NS_C (PF02725) | 10 (35.7%) | View |
Paramyxo_C (PF01692) | 4 (14.3%) | View |
Total: 3 | Total: 28 | Clan alignment |
Please note: Clan alignments can be very large and can cause problems for some browsers. Read the note above before viewing.
Family relationships
This diagram shows the relationships between members of this clan. More...
Species distribution
Tree controls
HideThis tree shows the occurrence of the domains in this clan across different species. More...
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Structures
For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the MSD group, to allow us to map Pfam domains onto UniProt three-dimensional structures. The table below shows the mapping between the Pfam families in this clan, the corresponding UniProt entries, and the region of the three-dimensional structures that are available for that sequence.
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