A0A7T7DH33 · A0A7T7DH33_9BETA

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.

Type
IDPosition(s)Description
Active site47Charge relay system
Active site118Charge relay system
Active site142Charge relay system
Site263-264Cleavage; by assemblin; Release 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

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • 24655
  • Taxonomic lineage
    Viruses > Duplodnaviria > Heunggongvirae > Peploviricota > Herviviricetes > Herpesvirales > Orthoherpesviridae > Betaherpesvirinae > Cytomegalovirus

Accessions

  • Primary accession
    A0A7T7DH33

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_50316520621-263Assemblin
ChainPRO_50316520631-624Capsid scaffolding protein
ChainPRO_5031652061264-624Assembly 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.

Type
IDPosition(s)Description
Region194-224Disordered
Compositional bias199-213Basic and acidic residues
Compositional bias272-287Basic and acidic residues
Region272-307Disordered
Compositional bias288-307Polar residues
Region426-509Disordered
Compositional bias428-453Polar residues
Compositional bias454-483Basic and acidic residues
Compositional bias492-509Basic and acidic residues
Region538-606Disordered
Compositional bias540-578Polar residues
Region604-624Interaction 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
    624
  • Mass (Da)
    67,423
  • Last updated
    2021-06-02 v1
  • Checksum
    B71F0B3250004561
MAAPVYVGGFLVRYDEAPEEAELVLPSDVVDRWLRESRGPLPLNVNHDESATVGHVAGLKNVRAGLFCLGRVTSPKFLDIVQKASEKSELVSRGPPSQSSLQPDGVLEFLSGSYSGLSLSSRRDINAADSASGDAKTACFKHVALCSVGRRRGTLAVYGREPDWVMERFPDLTEADREALRAQLAATTTIAAVAGGEEEGDDDVVRKKNNNKSQGPDADPFQSDSYGLLGNSVDALYIQERLPKLRYDKRLVGVTARESYVKASVSPAEQEACDIKVEKERPNESQHSRAPSESMSHPMSSVATPAASSVAPSQASLALAHDGVYLPKDAFFSLIGASRHATDSAGARAVYPAAPPPHHAYPVMNYEDPSRGFDYTAWLRRAGYDAGHHPQYPPVPFHHLPPYRRRDFSMMDDGDRMAWERGYAHPSNYDSSYGNNGGSSWSRGRNGGNGSHNNGNKRRRDRDLSSSDEEDMSFPGEAEHGKARKRLKAHHTRGGGGGDHSSDAKGDHRYDEIREALQELRREMMAVRQIAPPALLGPAQLTVPTSSPTTTSHPSDVVVTSEPPQTSSSPSSAHSSKSAADRGGVVNASCGVSVQPQDGGPTPPVKDIVDLNRRLFVAALNKME

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias199-213Basic and acidic residues
Compositional bias272-287Basic and acidic residues
Compositional bias288-307Polar residues
Compositional bias428-453Polar residues
Compositional bias454-483Basic and acidic residues
Compositional bias492-509Basic and acidic residues
Compositional bias540-578Polar residues

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
MT157324
EMBL· GenBank· DDBJ
QQL10227.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

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