Detail Information for IndEnz0002009007
IED ID IndEnz0002009007
Enzyme Type ID protease009007
Protein Name Capsid scaffolding protein
Capsid protein P40
Protease precursor
pPR

Cleaved into: Assemblin
EC 3.4.21.97
Protease
; Assembly protein
Capsid assembly protein
Gene Name ORF17
Organism Human herpesvirus 8 type P (isolate GK18) (HHV-8) (Kaposi's sarcoma-associated herpesvirus)
Taxonomic Lineage Viruses Duplodnaviria Heunggongvirae Peploviricota Herviviricetes Herpesvirales Herpesviridae Gammaherpesvirinae Rhadinovirus Human herpesvirus 8 (HHV-8) (Kaposi's sarcoma-associated herpesvirus) Human herpesvirus 8 type P (isolate GK18) (HHV-8) (Kaposi's sarcoma-associated herpesvirus)
Enzyme Sequence MAQGLYVGGFVDVVSCPKLEQELYLDPDQVTDYLPVTEPLPITIEHLPETEVGWTLGLFQVSHGIFCTGAITSPAFLELASRLADTSHVARAPVKNLPKEPLLEILHTWLPGLSLSSIHPRELSQTPSGPVFQHVSLCALGRRRGTVAVYGHDAEWVVSRFSSVSKSERAHILQHVSSCRLEDLSTPNFVSPLETLMAKAIDASFIRDRLDLLKTDRGVASILSPAYLKASQFPVGIQAVTPPRPAMNSSGQEDIISIPKSAFLSMLQSSIDGMKTTAAKMSHTLSGPGLMGCGGQMFPTDHHLPSYVSNPAPPYGYAYKNPYDPWYYSPQLPGYRTGKRKRGAEDDEGHLFPGEEPAYHKDILSMSKNIAEIQSELKEMKLNGWHAGPPPSSSAAAAAVDPHYRPHANSAAPCQFPTMKEHGGTYVHPPIYVQAPHGQFQQAAPILFAQPHVSHPPVSTGLAVVGAPPAEPTPASSTQSIQQQAPETTHTPCAAVEKDAPTPNPTSNRVEASSRSSPKSKIRKMFCEELLNKQ
Enzyme Length 534
Uniprot Accession Number Q2HRB6
Absorption
Active Site ACT_SITE 46; /note=Charge relay system; /evidence=ECO:0000255|HAMAP-Rule:MF_04008; ACT_SITE 114; /note=Charge relay system; /evidence=ECO:0000255|HAMAP-Rule:MF_04008; ACT_SITE 134; /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 (10); Chain (3); Compositional bias (3); Helix (10); Motif (1); Region (4); Site (2)
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 4P2T;
Mapped Pubmed ID -
Motif MOTIF 336..342; /note=Nuclear localization signal; /evidence=ECO:0000250
Gene Encoded By
Mass 57,866
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda