A0A059WP12 · A0A059WP12_CHV1

Function

function

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.
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.

Caution

Lacks conserved residue(s) required for the propagation of feature annotation.

Catalytic activity

  • Cleaves -Ala-|-Ser- and -Ala-|-Ala- bonds in the scaffold protein.
    EC:3.4.21.97 (UniProtKB | ENZYME | Rhea)

Features

Showing features for active site, site.

TypeIDPosition(s)Description
Active site61Charge relay system
Active site129Charge relay system
Active site148Charge relay system
Site247-248Cleavage; by assemblin; Release site
Site589-590Cleavage; by assemblin; Tail 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

Names & Taxonomy

Protein names

  • Recommended name
    Capsid scaffolding protein
  • Alternative names
    • 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

    • Name
      UL26

Organism names

Accessions

  • Primary accession
    A0A059WP12

Proteomes

Subcellular Location

Capsid scaffolding protein

Host cytoplasm

Assembly protein

Host nucleus

Assemblin

Host nucleus

Keywords

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_50235575191-247Assemblin
ChainPRO_50235575181-614Capsid scaffolding protein
ChainPRO_5023557520248-614Assembly 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

Assemblin

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

Assembly protein

Homomultimer. Interacts with major capsid protein.

Capsid scaffolding protein

Homomultimer. Interacts with major capsid protein.

Family & Domains

Features

Showing features for region, compositional bias.

TypeIDPosition(s)Description
Region252-318Disordered
Compositional bias297-312Pro residues
Region392-450Disordered
Compositional bias397-422Basic and acidic residues
Region488-536Disordered
Compositional bias514-536Pro residues
Region554-576Disordered
Region594-614Interaction 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

  • Sequence status
    Complete
  • Length
    614
  • Mass (Da)
    63,200
  • Last updated
    2014-09-03 v1
  • Checksum
    D723BF95B42FE262
MGPAADPEGPPGPDADRPVPIYVAGYLALYGSGDAGELALDPETVAAALPPAGPLAINVDHRARCEVGRVLAVVDDPRGPFFAGLIACAQLERVLETAASAAIFERRGPPLSREERLLYLVTNYLPSVSLSTRRLEEGETPDNTLLVHVALCAIGRRLGTIVTYDTSLDAAVAPFRHLAPDSREILRREAAEAELGLGGRVWTPGAEALTRALLSTAVNNMMLRDRWSLVAERRRQAGIAGHTYLQASEKFGLWGAGPGDSPPDGVYKRRSSGATDPGHDASASAPRAHDPPSDVPEAEMNPAPPAAGAPTPKPPGDGSYLWIPAAHYNQLVAGHPPAPVFGAPAPAPPPAFGAPAYAPHHPAGVYPGVVFPGPSPLEAQIAALVGAIAADRQPVPTPSGKRRRYEAERDCDYDDRDDAPYYPGEARAPPRVAPDSGGRGRRVPPGGGSAAANETIAALVGAVTSLQQELAHMRARAAPYGQPYAQARPALGVPGEPPAPQYAPQWEAPGAGALAHHPPPPPPARHQPYATPTNAPFVPGPQPCAVASGAQGHASATAAPGGQCAPAATAAPPPAEAGEAEAVAALVNASAATHVDVDVGRAADLFVSQMMGGR

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias297-312Pro residues
Compositional bias397-422Basic and acidic residues
Compositional bias514-536Pro residues

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
KJ566591
EMBL· GenBank· DDBJ
AIA09519.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

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