| IED ID | IndEnz0002010141 |
| Enzyme Type ID | protease010141 |
| Protein Name |
Capsid scaffolding protein Protease precursor pPR Cleaved into: Assemblin EC 3.4.21.97 Protease ; Assembly protein Capsid assembly protein |
| Gene Name | 33 |
| Organism | Varicella-zoster virus (strain Dumas) (HHV-3) (Human herpesvirus 3) |
| Taxonomic Lineage | Viruses Duplodnaviria Heunggongvirae Peploviricota Herviviricetes Herpesvirales Herpesviridae Alphaherpesvirinae Varicellovirus Human herpesvirus 3 (HHV-3) (Varicella-zoster virus) Varicella-zoster virus (strain Dumas) (HHV-3) (Human herpesvirus 3) |
| Enzyme Sequence | MAAEADEENCEALYVAGYLALYSKDEGELNITPEIVRSALPPTSKIPINIDHRKDCVVGEVIAIIEDIRGPFFLGIVRCPQLHAVLFEAAHSNFFGNRDSVLSPLERALYLVTNYLPSVSLSSKRLSPNEIPDGNFFTHVALCVVGRRVGTVVNYDCTPESSIEPFRVLSMESKARLLSLVKDYAGLNKVWKVSEDKLAKVLLSTAVNNMLLRDRWDVVAKRRREAGIMGHVYLQASTGYGLARITNVNGVESKLPNAGVINATFHPGGPIYDLALGVGESNEDCEKTVPHLKVTQLCRNDSDMASVAGNASNISPQPPSGVPTGGEFVLIPTAYYSQLLTGQTKNPQVSIGAPNNGQYIVGPYGSPHPPAFPPNTGGYGCPPGHFGGPYGFPGYPPPNRLEMQMSAFMNALAAERGIDLQTPCVNFPDKTDVRRPGKRDFKSMDQRELDSFYSGESQMDGEFPSNIYFPGEPTYITHRRRRVSPSYWQRRHRVSNGQHEELAGVVAKLQQEVTELKSQNGTQMPLSHHTNIPEGTRDPRISILLKQLQSVSGLCSSQNTTSTPHTDTVGQDVNAVEASSKAPLIQGSTADDADMFANQMMVGRC |
| Enzyme Length | 605 |
| Uniprot Accession Number | P09286 |
| Absorption | |
| Active Site | ACT_SITE 52; /note=Charge relay system; /evidence=ECO:0000255|HAMAP-Rule:MF_04008; ACT_SITE 120; /note=Charge relay system; /evidence=ECO:0000255|HAMAP-Rule:MF_04008; ACT_SITE 139; /note=Charge relay system; /evidence=ECO:0000255|HAMAP-Rule:MF_04008 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Cleaves -Ala-|-Ser- and -Ala-|-Ala- bonds in the scaffold protein.; EC=3.4.21.97; Evidence={ECO:0000255|HAMAP-Rule:MF_04008}; |
| DNA Binding | |
| EC Number | 3.4.21.97 |
| Enzyme 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. {ECO:0000255|HAMAP-Rule:MF_04008}.; 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. {ECO:0000255|HAMAP-Rule:MF_04008}.; FUNCTION: [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. {ECO:0000255|HAMAP-Rule:MF_04008}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Alternative sequence (1); Beta strand (8); Chain (3); Helix (8); Region (2); Site (2); Turn (3) |
| Keywords | 3D-structure;Alternative promoter usage;Host cytoplasm;Host nucleus;Hydrolase;Phosphoprotein;Protease;Reference proteome;Serine protease;Viral capsid assembly;Viral release from host cell |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: [Capsid scaffolding protein]: Host cytoplasm {ECO:0000255|HAMAP-Rule:MF_04008}.; SUBCELLULAR LOCATION: [Assemblin]: Host nucleus {ECO:0000255|HAMAP-Rule:MF_04008}.; SUBCELLULAR LOCATION: [Assembly protein]: Host nucleus {ECO:0000255|HAMAP-Rule:MF_04008}. |
| Modified Residue | |
| Post Translational Modification | PTM: 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 and tail site. {ECO:0000255|HAMAP-Rule:MF_04008}. |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (1) |
| Cross Reference PDB | 1VZV; |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 66,047 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |