Q2HRB6 · SCAF_HHV8P
- ProteinCapsid scaffolding protein
- GeneORF17
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids534 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
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.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 46 | Charge relay system | ||||
Sequence: H | ||||||
Active site | 114 | Charge relay system | ||||
Sequence: S | ||||||
Active site | 134 | Charge relay system | ||||
Sequence: H | ||||||
Site | 230-231 | Cleavage; by assemblin; Release site | ||||
Sequence: AS | ||||||
Site | 512-513 | Cleavage; by assemblin; Maturation site | ||||
Sequence: AS |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | host cell cytoplasm | |
Cellular Component | host cell nucleus | |
Molecular Function | identical protein binding | |
Molecular Function | serine-type endopeptidase activity | |
Biological Process | nuclear capsid assembly | |
Biological Process | proteolysis | |
Biological Process | viral release from host cell |
Keywords
- Molecular function
- Biological process
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameCapsid scaffolding protein
- Alternative names
- Cleaved into 2 chains
Gene names
Organism names
- Taxonomic lineageViruses > Duplodnaviria > Heunggongvirae > Peploviricota > Herviviricetes > Herpesvirales > Orthoherpesviridae > Gammaherpesvirinae > Rhadinovirus > Rhadinovirus humangamma8 > Human herpesvirus 8
- Virus hosts
Accessions
- Primary accessionQ2HRB6
- Secondary accessions
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Keywords
- Cellular component
Phenotypes & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 114 | Reduced levels of autoproteolysis. | ||||
Sequence: S → A |
Chemistry
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000435878 | 1-230 | Assemblin | |||
Sequence: MAQGLYVGGFVDVVSCPKLEQELYLDPDQVTDYLPVTEPLPITIEHLPETEVGWTLGLFQVSHGIFCTGAITSPAFLELASRLADTSHVARAPVKNLPKEPLLEILHTWLPGLSLSSIHPRELSQTPSGPVFQHVSLCALGRRRGTVAVYGHDAEWVVSRFSSVSKSERAHILQHVSSCRLEDLSTPNFVSPLETLMAKAIDASFIRDRLDLLKTDRGVASILSPAYLKA | ||||||
Chain | PRO_0000423879 | 1-534 | Capsid scaffolding protein | |||
Sequence: MAQGLYVGGFVDVVSCPKLEQELYLDPDQVTDYLPVTEPLPITIEHLPETEVGWTLGLFQVSHGIFCTGAITSPAFLELASRLADTSHVARAPVKNLPKEPLLEILHTWLPGLSLSSIHPRELSQTPSGPVFQHVSLCALGRRRGTVAVYGHDAEWVVSRFSSVSKSERAHILQHVSSCRLEDLSTPNFVSPLETLMAKAIDASFIRDRLDLLKTDRGVASILSPAYLKASQFPVGIQAVTPPRPAMNSSGQEDIISIPKSAFLSMLQSSIDGMKTTAAKMSHTLSGPGLMGCGGQMFPTDHHLPSYVSNPAPPYGYAYKNPYDPWYYSPQLPGYRTGKRKRGAEDDEGHLFPGEEPAYHKDILSMSKNIAEIQSELKEMKLNGWHAGPPPSSSAAAAAVDPHYRPHANSAAPCQFPTMKEHGGTYVHPPIYVQAPHGQFQQAAPILFAQPHVSHPPVSTGLAVVGAPPAEPTPASSTQSIQQQAPETTHTPCAAVEKDAPTPNPTSNRVEASSRSSPKSKIRKMFCEELLNKQ | ||||||
Chain | PRO_0000435879 | 231-534 | Assembly protein | |||
Sequence: SQFPVGIQAVTPPRPAMNSSGQEDIISIPKSAFLSMLQSSIDGMKTTAAKMSHTLSGPGLMGCGGQMFPTDHHLPSYVSNPAPPYGYAYKNPYDPWYYSPQLPGYRTGKRKRGAEDDEGHLFPGEEPAYHKDILSMSKNIAEIQSELKEMKLNGWHAGPPPSSSAAAAAVDPHYRPHANSAAPCQFPTMKEHGGTYVHPPIYVQAPHGQFQQAAPILFAQPHVSHPPVSTGLAVVGAPPAEPTPASSTQSIQQQAPETTHTPCAAVEKDAPTPNPTSNRVEASSRSSPKSKIRKMFCEELLNKQ |
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
- PTM
Expression
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.
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for region, motif, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 253-272 | Interaction with pAP | ||||
Sequence: EDIISIPKSAFLSMLQSSID | ||||||
Motif | 336-342 | Nuclear localization signal | ||||
Sequence: RTGKRKR | ||||||
Region | 337-356 | Disordered | ||||
Sequence: TGKRKRGAEDDEGHLFPGEE | ||||||
Compositional bias | 338-356 | Basic and acidic residues | ||||
Sequence: GKRKRGAEDDEGHLFPGEE | ||||||
Region | 466-524 | Disordered | ||||
Sequence: GAPPAEPTPASSTQSIQQQAPETTHTPCAAVEKDAPTPNPTSNRVEASSRSSPKSKIRK | ||||||
Compositional bias | 472-490 | Polar residues | ||||
Sequence: PTPASSTQSIQQQAPETTH | ||||||
Compositional bias | 501-515 | Polar residues | ||||
Sequence: PTPNPTSNRVEASSR | ||||||
Region | 514-534 | Interaction with major capsid protein | ||||
Sequence: SRSSPKSKIRKMFCEELLNKQ |
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
- Sequence statusComplete
This entry describes 2 isoforms produced by Alternative promoter usage.
Q2HRB6-1
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.
- NameCapsid scaffolding protein
- SynonymspPR
- Length534
- Mass (Da)57,866
- Last updated2006-03-21 v1
- ChecksumEEA75DF8146B0791
Q2HRB6-2
- NamepAP
- SynonymsAssembly protein
- Differences from canonical
- 1-246: Missing
Features
Showing features for alternative sequence, sequence conflict, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_053272 | 1-246 | in isoform pAP | |||
Sequence: Missing | ||||||
Sequence conflict | 226 | in Ref. 1; AAC05223 | ||||
Sequence: A → V | ||||||
Sequence conflict | 235 | in Ref. 1; AAC05223 | ||||
Sequence: V → A | ||||||
Compositional bias | 338-356 | Basic and acidic residues | ||||
Sequence: GKRKRGAEDDEGHLFPGEE | ||||||
Compositional bias | 472-490 | Polar residues | ||||
Sequence: PTPASSTQSIQQQAPETTH | ||||||
Compositional bias | 501-515 | Polar residues | ||||
Sequence: PTPNPTSNRVEASSR | ||||||
Sequence conflict | 510 | in Ref. 1; AAC05223 | ||||
Sequence: V → L | ||||||
Sequence conflict | 529 | in Ref. 1; AAC05223 | ||||
Sequence: E → EL |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF010430 EMBL· GenBank· DDBJ | AAC05223.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF148805 EMBL· GenBank· DDBJ | ABD28867.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF148805 EMBL· GenBank· DDBJ | ABD28868.1 EMBL· GenBank· DDBJ | Genomic DNA |