Detail Information for IndEnz0002001949
IED ID IndEnz0002001949
Enzyme Type ID protease001949
Protein Name Capsid scaffolding protein
Capsid protein P40
Protease precursor
pPR

Cleaved into: Assemblin
EC 3.4.21.97
Capsid protein VP24
Protease
; Assembly protein
Capsid assembly protein
Capsid protein VP22A
Gene Name 17
Organism Saimiriine herpesvirus 2 (strain 11) (SaHV-2) (Herpesvirus saimiri)
Taxonomic Lineage Viruses Duplodnaviria Heunggongvirae Peploviricota Herviviricetes Herpesvirales Herpesviridae Gammaherpesvirinae Rhadinovirus Saimiriine herpesvirus 2 (SaHV-2) (Herpesvirus saimiri) Saimiriine herpesvirus 2 (strain 11) (SaHV-2) (Herpesvirus saimiri)
Enzyme Sequence MSIVYVAGFVDVVAYPKVDPVLYLNLDDVSKCLPLTKPIPLNIEHLPESTIGHTIGLYAVTHGVFCVGVIHSEKFLHLTENLFSNSCVAQATSKFLPYQPLLEMLHTWLPALSLSSLCPTAQNAANTNMFQHVSLCALGRRRGTVAVYSMNLEDAISQFCSISQAEVENIYQDSKNVDINSLPKPVFNIDPHILMAKAIDAGFIKDRLQLLKTDKGVAKIKKLTYLKASEIGKPVTEDISEDMNQHGIVPQGSDDLISVPKSTFLSMLQNNLDNFKQHPRPACFPQYFSPQGAYMPYELYPPQPYSGDNIGYMLPSGSYVPAMFPSRPNKRKREDFDDCVFPGESSLYKDVLNLTKNISQLQDDLKDLKQAAINQPNRYPPHHFSNPYSLDPGHASYFRYAPYGAPKPDQHLLQPLACVQQAPVVQPNYAPPPTEGASNEAPKPSVQEPVHIDASFAQDPVSKLQKMFCDELLNK
Enzyme Length 475
Uniprot Accession Number Q01002
Absorption
Active Site ACT_SITE 45; /note=Charge relay system; /evidence=ECO:0000255|HAMAP-Rule:MF_04008; ACT_SITE 113; /note=Charge relay system; /evidence=ECO:0000255|HAMAP-Rule:MF_04008; ACT_SITE 132; /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); Chain (3); Motif (1); Region (3); Site (2)
Keywords 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
Cross Reference PDB -
Mapped Pubmed ID -
Motif MOTIF 327..333; /note=Nuclear localization signal; /evidence=ECO:0000250
Gene Encoded By
Mass 52,820
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda