AC   MF_04008;
DC   Protein; auto
TR   HAMAP; MF_04008; -; 1; level=0
XX
Names: HSV_SCAF
XX
ID   SCAF
DE   RecName: Full=Capsid scaffolding protein;
DE   AltName: Full=Protease precursor;
DE            Short=pPR;
DE   Contains:
DE     RecName: Full=Assemblin;
DE              EC=3.4.21.97;
DE     AltName: Full=Protease;
DE   Contains:
DE     RecName: Full=Assembly protein;
DE     AltName: Full=Capsid assembly protein;
XX
CC   -!- FUNCTION: Capsid scaffolding protein: Acts as a scaffold protein by
CC       binding major capsid protein in the cytoplasm, inducing the nuclear
CC       localization of both proteins. Multimerizes in the nucleus such as
CC       major capsid protein forms the icosahedral T=16 capsid. Autocatalytic
CC       cleavage releases the assembly protein, and subsequently abolishes
CC       interaction with major capsid protein. Cleavages products are evicted
CC       from the capsid before or during DNA packaging.
CC   -!- FUNCTION: Assemblin: Protease that plays an essential role in virion
CC       assembly within the nucleus. Catalyzes the cleavage of the assembly
CC       protein after formation of the spherical procapsid. By that cleavage,
CC       the capsid matures and gains its icosahedral shape. The cleavage sites
CC       seem to include -Ala-Ser-, -Ala-Ala-, as well as Ala-Thr bonds.
CC       Assemblin and cleavages products are evicted from the capsid before or
CC       during DNA packaging.
CC   -!- FUNCTION: Assembly protein: Plays a major role in capsid assembly. Acts
CC       as a scaffold protein by binding major capsid protein. Multimerizes in
CC       the nucleus such as major capsid protein forms the icosahedral T=16
CC       capsid. Cleaved by assemblin after capsid completion. The cleavages
CC       products are evicted from the capsid before or during DNA packaging.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Cleaves -Ala-|-Ser- and -Ala-|-Ala- bonds in the scaffold
CC         protein.; EC=3.4.21.97;
CC   -!- SUBUNIT: [Capsid scaffolding protein]: Homomultimer. Interacts
CC       with major capsid protein.
CC   -!- SUBUNIT: [Assemblin]: Exists in a monomer-dimer equilibrium with the
CC       dimer being the active species.
CC   -!- SUBUNIT: [Assembly protein]: Homomultimer. Interacts with major
CC       capsid protein.
CC   -!- SUBCELLULAR LOCATION: Capsid scaffolding protein: Host cytoplasm.
CC   -!- SUBCELLULAR LOCATION: Assemblin: Host nucleus.
CC   -!- SUBCELLULAR LOCATION: Assembly protein: Host nucleus.
CC   -!- DOMAIN: Region of interaction between pPR and pAP is called Amino
CC       conserved domain (ACD). The region of interaction with major capsid
CC       protein is called carboxyl conserved domain (CCD).
CC   -!- PTM: Capsid scaffolding protein is cleaved by assemblin after formation
CC       of the spherical procapsid. As a result, the capsid obtains its mature,
CC       icosahedral shape. Cleavages occur at two or more sites: release and
CC       tail site.
CC   -!- SIMILARITY: Belongs to the herpesviridae capsid scaffolding protein
CC       family.
XX
DR   Pfam; PF00716; Peptidase_S21; 1; trigger=no
DR   PRINTS; PR00236; HSVCAPSIDP40; 1; trigger=no
XX
KW   Host cytoplasm
KW   Host nucleus
KW   Hydrolase
KW   Phosphoprotein
KW   Protease
KW   Serine protease
KW   Viral capsid assembly
KW   Viral release from host cell
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GO   GO:0030430; C:host cell cytoplasm
GO   GO:0042025; C:host cell nucleus
GO   GO:0042802; F:identical protein binding
GO   GO:0004252; F:serine-type endopeptidase activity
GO   GO:0019076; P:viral release from host cell
XX
FT   From: SCAF_HHV11 (P10210)
FT   CHAIN           Nter..Cter
FT                   /note="Capsid scaffolding protein"
FT   CHAIN           Nter..247
FT                   /note="Assemblin"
FT   CHAIN           248..Cter
FT                   /note="Assembly protein"
FT   REGION          324..343
FT                   /note="Interaction with pAP"
FT   REGION          Cter-20..Cter
FT                   /note="Interaction with major capsid protein"
FT   ACT_SITE        61
FT                   /note="Charge relay system"
FT   Condition: H
FT   ACT_SITE        129
FT                   /note="Charge relay system"
FT   Condition: S
FT   ACT_SITE        148
FT                   /note="Charge relay system"
FT   Condition: H
FT   SITE            247..248
FT                   /note="Cleavage; by assemblin; Release site"
FT   Condition: A-x
FT   SITE            610..611
FT                   /note="Cleavage; by assemblin; Tail site"
FT   Condition: A-S
XX
Size: 475-726;
Related: None;
Template: P10210;
Scope:
 Viruses; Herpesvirales
Fusion:
 Nter: None
 Cter: None
Duplicate: None
Plasmid: None
Comments: None
XX
# Revision 1.7 2022/07/26
//