P52369 · SCAF_EHV2

Function

function

Capsid scaffolding protein

Acts as a scaffold protein by binding major capsid protein in the cytoplasm, inducing the nuclear localization of both proteins. Multimerizes in the nucleus such as major capsid protein forms the icosahedral T=16 capsid. Autocatalytic cleavage releases the assembly protein, and subsequently abolishes interaction with major capsid protein. Cleavages products are evicted from the capsid before or during DNA packaging.

Assemblin

Protease that plays an essential role in virion assembly within the nucleus. Catalyzes the cleavage of the assembly protein after formation of the spherical procapsid. By that cleavage, the capsid matures and gains its icosahedral shape. The cleavage sites seem to include -Ala-Ser-, -Ala-Ala-, as well as Ala-Thr bonds. Assemblin and cleavages products are evicted from the capsid before or during DNA packaging.

Assembly protein

Plays a major role in capsid assembly. Acts as a scaffold protein by binding major capsid protein. Multimerizes in the nucleus such as major capsid protein forms the icosahedral T=16 capsid. Cleaved by assemblin after capsid completion. The cleavages products are evicted from the capsid before or during DNA packaging.

Catalytic activity

Features

Showing features for active site, site.

TypeIDPosition(s)Description
Active site82Charge relay system
Active site151Charge relay system
Active site173Charge relay system
Site269-270Cleavage; by assemblin; Release site
Site621-622Cleavage; by assemblin; Maturation site

GO annotations

AspectTerm
Cellular Componenthost cell cytoplasm
Cellular Componenthost cell nucleus
Molecular Functionidentical protein binding
Molecular Functionserine-type endopeptidase activity
Biological Processnuclear capsid assembly
Biological Processproteolysis
Biological Processviral release from host cell

Keywords

Protein family/group databases

Names & Taxonomy

Protein names

  • Recommended name
    Capsid scaffolding protein
  • Alternative names
    • Capsid protein P40
    • Protease precursor
      (pPR
      )
  • Cleaved into 2 chains
    • Assemblin
      (EC:3.4.21.97 (UniProtKB | ENZYME | Rhea)
      ) Alternative names: Protease
      (Pr
      )
    • Assembly protein
      (AP
      ) Alternative names: Capsid assembly protein

Gene names

    • ORF names
      17

Organism names

Accessions

  • Primary accession
    P52369

Proteomes

Subcellular Location

Capsid scaffolding protein

Host cytoplasm

Assemblin

Host nucleus

Assembly protein

Host nucleus

Keywords

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00000272631-269Assemblin
ChainPRO_00003768001-643Capsid scaffolding protein
ChainPRO_0000027264270-643Assembly protein

Post-translational modification

Capsid scaffolding protein

Capsid scaffolding protein is cleaved by assemblin after formation of the spherical procapsid. As a result, the capsid obtains its mature, icosahedral shape. Cleavages occur at two or more sites: release (R-site) and maturation (M-site).

Keywords

Interaction

Subunit

Capsid scaffolding protein

Homomultimer. Interacts with major capsid protein.

Assemblin

Exists in a monomer-dimer equilibrium with the dimer being the active species.

Assembly protein

Homomultimer. Interacts with major capsid protein.

Structure

3D structure databases

Family & Domains

Features

Showing features for compositional bias, region, motif.

TypeIDPosition(s)Description
Compositional bias1-15Polar residues
Region1-31Disordered
Region283-306Disordered
Region324-343Interaction with pAP
Motif439-445Nuclear localization signal
Region485-519Disordered
Compositional bias491-515Pro residues
Region544-625Disordered
Compositional bias593-625Polar residues
Region623-643Interaction with major capsid protein

Domain

Region of interaction between pPR and pAP is called Amino conserved domain (ACD). The region of interaction with major capsid protein is called carboxyl conserved domain (CCD).

Sequence similarities

Belongs to the herpesviridae capsid scaffolding protein family.

Family and domain databases

Sequence & Isoform

Align isoforms (2)
  • Sequence status
    Complete

This entry describes 2 isoforms produced by Alternative promoter usage.

P52369-1

This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

  • Name
    Capsid scaffolding protein
  • Synonyms
    pPR
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Length
    643
  • Mass (Da)
    68,394
  • Last updated
    1996-10-01 v1
  • Checksum
    1108A7A40E9FCA38
MSSPSPSSSSSDHPSSPAPVPAPPGPVPEAAAASRASRAPVYLGGFVDVFSYPKDSRALYLNPADVGAHLPLPGPIPLNVEHLQEAHVGWTLGLHLTRYGLFCVAVITAEEFFTLLDRLCAASSVARTRADHHLPPNPTLEMLHTWLPELSLSSIHPDALPGAKGGDTPIFQHVALCAMGQRRGTVAVYGESLDWILSKFTSLSPEERGAIAEGYASPAPESLPEPHFTCSNEILMAKAIDAGFIKNRLEILKTDKGVAEVKAPTYLKASVQGLPANLDEVDSARGGEDPPTAAIATTPHPATDATTMNQQQPFAAQAPAGGCEDLISVPRSTFMTMLQTNLDTMRQTSLGQRFGQPIDAPAAPPAQLRVPPPAAPFPVHPGYYPAPYHPQVDAQAQYLPYVPLPPPGAMPFAPPPLPDFYKYGGIPAPGYSPVAHPARPGKRKRDCDEEFEGPLFPGEIHKDVQSLSKSIAALQSELKDIKNSQQFPQPLPQPQLQPQAQPQPQPAPQLYPAPPQAFYHPAAGDQGYYVRYLNPFQASGGVPCAPGPQGVGEPQAPQVTVTHNGHQAAPQAGGGATGATAANVEQRQPEGGEACGAQQQQPPQPQPQQQQQPQQQAFVEASTKPSQISQLQKIFCEELLNKT

P52369-2

  • Name
    pAP
  • Synonyms
    Assembly protein
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical

Features

Showing features for compositional bias, alternative sequence.

TypeIDPosition(s)Description
Compositional bias1-15Polar residues
Alternative sequenceVSP_0374171-307in isoform pAP
Compositional bias491-515Pro residues
Compositional bias593-625Polar residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
U20824
EMBL· GenBank· DDBJ
AAC13804.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
FeedbackHelp