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2  structures 20  species 0  interactions 39  sequences 1  architecture

Family: Paramyxo_P (PF01806)

Summary: Paramyxovirinae P phosphoprotein C-terminal region

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Paramyxovirinae P phosphoprotein C-terminal region Provide feedback

The subfamily Paramyxovirinae of the family Paramyxoviridae now contains as main genera the Rubulaviruses, avulaviruses, respiroviruses, Henipavirus-es and morbilliviruses. Protein P is the best characterised, structurally of the replicative complex of N, P and L proteins and consists of two functionally distinct moieties, an N-terminal PNT, and a C-terminal PCT [1]. The P protein is an essential part of the viral RNA polymerase complex formed from the P and L proteins [1]. P protein plays a crucial role in the enzyme by positioning L onto the N/RNA template through an interaction with the C-terminal domain of N. Without P, L is not functional.The C-terminal part of P (PCT) is only functional as an oligomer and forms with L the polymerase complex. PNT is poorly conserved and unstructured in solution while PCT contains the oligomerisation domain (PMD) that folds as a homotetrameric coiled coil (40) containing the L binding region and a C-terminal partially folded domain, PX (residues 474 to 568), identified as the nucleocapsid binding site. Interestingly, PX is also expressed as an independent polypeptide in infected cells. PX has a C-subdomain (residues 516 to 568) that consists of three {alpha}-helices arranged in an antiparallel triple-helical bundle linked to an unfolded flexible N-subdomain (residues 474 to 515).

Literature references

  1. Bowman MC, Smallwood S, Moyer SA; , J Virol 1999;73:6474-6483.: Dissection of Individual Functions of the Sendai Virus Phosphoprotein in Transcription. PUBMED:10400742 EPMC:10400742

  2. Matsuoka Y, Curran J, Pelet T, Kolakofsky D, Ray R, Compans RW; , J Virol 1991;65:3406-3410.: The P gene of human parainfluenza virus type 1 encodes P and C proteins but not a cysteine-rich V protein. PUBMED:1851888 EPMC:1851888

  3. Karlin D, Ferron F, Canard B, Longhi S; , J Gen Virol. 2003;84:3239-3252.: Structural disorder and modular organization in Paramyxovirinae N and P. PUBMED:14645906 EPMC:14645906


External database links

This tab holds annotation information from the InterPro database.

InterPro entry IPR002693

Sendai virus is a member of the Paramyxovirinae family. Its negative-sense ssRNA genome is packaged by the viral nucleoprotein (N) within a helical nucleocapsid. Paramyxovirinae use this N-RNA (nucleoprotein-RNA) complex as a template for both transcription and replication. During viral genome replication, the synthesis of viral RNA and its encapsidation by N are concomitant. Viral transcription and replication are carried out by viral RNA-dependent RNA polymerase, which consists of two proteins: L polymerase and phosphoprotein P. The L polymerase carries the enzyme activity. Phosphoprotein P binds the viral nucleocapsid, and positions the L polymerase on the template for transcription and replication formed by nucleoprotein-RNA (N-RNA) [PUBMED:10400742].

This entry represents phosphoprotein P from Sendai virus as well as from close family members. Phosphoprotein P, an indispensable subunit of the viral polymerase complex, is a modular protein organised into two moieties that are both functionally and structurally distinct: a well-conserved C-terminal moiety that contains all the regions required for transcription, and a poorly conserved, intrinsically unstructured N-terminal moiety that provides several additional functions required for replication. The N-terminal moiety is responsible for binding to newly synthesized free N(0) (nucleoprotein that has not yet bound RNA), in order to prevent the binding of N(0) to cellular RNA. The C-terminal moiety consists of an oligomerisation domain, an N-RNA (nucleoprotein-RNA)-binding domain and an L polymerase-binding domain [PUBMED:14980481, PUBMED:17459940].

Gene Ontology

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Domain organisation

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Alignments

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Representative proteomes NCBI
(49)
Meta
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RP15
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RP35
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RP55
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RP75
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  Seed
(3)
Full
(39)
Representative proteomes NCBI
(49)
Meta
(0)
RP15
(0)
RP35
(0)
RP55
(0)
RP75
(0)
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You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.

External links

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Pfam alignments:

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Curation and family details

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Curation View help on the curation process

Seed source: Pfam-B_1628 (release 4.1), Karlin D
Previous IDs: none
Type: Domain
Author: Bashton M, Bateman A, Coggill P
Number in seed: 3
Number in full: 39
Average length of the domain: 240.10 aa
Average identity of full alignment: 59 %
Average coverage of the sequence by the domain: 42.99 %

HMM information View help on HMM parameters

HMM build commands:
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 25.0 25.0
Trusted cut-off 164.0 163.8
Noise cut-off 19.9 19.0
Model length: 248
Family (HMM) version: 12
Download: download the raw HMM for this family

Species distribution

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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 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 Paramyxo_P domain has been found. There are 2 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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