ID   SCAF_HHV11              Reviewed;         635 AA.
AC   P10210; O09798;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1989, sequence version 1.
DT   27-MAR-2024, entry version 139.
DE   RecName: Full=Capsid scaffolding protein {ECO:0000255|HAMAP-Rule:MF_04008};
DE   AltName: Full=Capsid protein P40;
DE   AltName: Full=Protease precursor {ECO:0000255|HAMAP-Rule:MF_04008};
DE            Short=pPR {ECO:0000255|HAMAP-Rule:MF_04008};
DE   AltName: Full=Virion structural protein UL26;
DE   Contains:
DE     RecName: Full=Assemblin {ECO:0000255|HAMAP-Rule:MF_04008};
DE              EC=3.4.21.97 {ECO:0000255|HAMAP-Rule:MF_04008};
DE     AltName: Full=Protease {ECO:0000255|HAMAP-Rule:MF_04008};
DE   Contains:
DE     RecName: Full=Assembly protein {ECO:0000255|HAMAP-Rule:MF_04008};
DE     AltName: Full=Capsid assembly protein {ECO:0000255|HAMAP-Rule:MF_04008};
GN   Name=UL26;
OS   Human herpesvirus 1 (strain 17) (HHV-1) (Human herpes simplex virus 1).
OC   Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC   Herpesvirales; Orthoherpesviridae; Alphaherpesvirinae; Simplexvirus;
OC   Simplexvirus humanalpha1; Human herpesvirus 1.
OX   NCBI_TaxID=10299;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2839594; DOI=10.1099/0022-1317-69-7-1531;
RA   McGeoch D.J., Dalrymple M.A., Davison A.J., Dolan A., Frame M.C., McNab D.,
RA   Perry L.J., Scott J.E., Taylor P.;
RT   "The complete DNA sequence of the long unique region in the genome of
RT   herpes simplex virus type 1.";
RL   J. Gen. Virol. 69:1531-1574(1988).
RN   [2]
RP   PROTEIN SEQUENCE OF 11-29; 77-91 AND 223-241.
RX   PubMed=1328483; DOI=10.1099/0022-1317-73-10-2709;
RA   Davison M.D., Rixon F.J., Davison A.J.;
RT   "Identification of genes encoding two capsid proteins (VP24 and VP26) of
RT   herpes simplex virus type 1.";
RL   J. Gen. Virol. 73:2709-2713(1992).
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. {ECO:0000255|HAMAP-
CC       Rule:MF_04008}.
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. {ECO:0000255|HAMAP-Rule:MF_04008}.
CC   -!- FUNCTION: [Assembly protein]: Plays a major role in capsid assembly.
CC       Acts as a scaffold protein by binding major capsid protein.
CC       Multimerizes in the nucleus such as major capsid protein forms the
CC       icosahedral T=16 capsid. Cleaved by assemblin after capsid completion.
CC       The cleavages products are evicted from the capsid before or during DNA
CC       packaging. {ECO:0000255|HAMAP-Rule:MF_04008}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Cleaves -Ala-|-Ser- and -Ala-|-Ala- bonds in the scaffold
CC         protein.; EC=3.4.21.97; Evidence={ECO:0000255|HAMAP-Rule:MF_04008};
CC   -!- SUBUNIT: [Capsid scaffolding protein]: Homomultimer. Interacts with
CC       major capsid protein. {ECO:0000255|HAMAP-Rule:MF_04008}.
CC   -!- SUBUNIT: [Assemblin]: Exists in a monomer-dimer equilibrium with the
CC       dimer being the active species. {ECO:0000255|HAMAP-Rule:MF_04008}.
CC   -!- SUBUNIT: [Assembly protein]: Homomultimer. Interacts with major capsid
CC       protein. {ECO:0000255|HAMAP-Rule:MF_04008}.
CC   -!- INTERACTION:
CC       P10210; P06491: MCP; NbExp=3; IntAct=EBI-8621986, EBI-7608705;
CC       P10210; P10210: UL26; NbExp=2; IntAct=EBI-8621986, EBI-8621986;
CC   -!- SUBCELLULAR LOCATION: [Capsid scaffolding protein]: Host cytoplasm
CC       {ECO:0000255|HAMAP-Rule:MF_04008}.
CC   -!- SUBCELLULAR LOCATION: [Assemblin]: Host nucleus {ECO:0000255|HAMAP-
CC       Rule:MF_04008}.
CC   -!- SUBCELLULAR LOCATION: [Assembly protein]: Host nucleus
CC       {ECO:0000255|HAMAP-Rule:MF_04008}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative promoter usage; Named isoforms=2;
CC       Name=Capsid scaffolding protein; Synonyms=pPR, UL26;
CC         IsoId=P10210-1; Sequence=Displayed;
CC       Name=pAP; Synonyms=Assembly protein, UL26.5 protein;
CC         IsoId=P10210-2; Sequence=VSP_037414;
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). {ECO:0000255|HAMAP-
CC       Rule:MF_04008}.
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. {ECO:0000255|HAMAP-Rule:MF_04008}.
CC   -!- SIMILARITY: Belongs to the herpesviridae capsid scaffolding protein
CC       family. {ECO:0000255|HAMAP-Rule:MF_04008}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; X14112; CAA32318.1; -; Genomic_DNA.
DR   EMBL; X14112; CAA32319.1; -; Genomic_DNA.
DR   PIR; H30084; WMBEW6.
DR   PDB; 8BQ1; X-ray; 2.32 A; A=1-247.
DR   PDBsum; 8BQ1; -.
DR   SMR; P10210; -.
DR   BioGRID; 971467; 1.
DR   DIP; DIP-1096N; -.
DR   IntAct; P10210; 1.
DR   MINT; P10210; -.
DR   BindingDB; P10210; -.
DR   ChEMBL; CHEMBL3518; -.
DR   DrugCentral; P10210; -.
DR   MEROPS; S21.001; -.
DR   Proteomes; UP000009294; Genome.
DR   GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0042025; C:host cell nucleus; IDA:CAFA.
DR   GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0039708; P:nuclear capsid assembly; IDA:UniProtKB.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   GO; GO:0019076; P:viral release from host cell; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.20.16.10; Herpesvirus/Caudovirus protease domain; 1.
DR   HAMAP; MF_04008; HSV_SCAF; 1.
DR   InterPro; IPR035443; Herpes_virus_sf.
DR   InterPro; IPR001847; Peptidase_S21.
DR   Pfam; PF00716; Peptidase_S21; 1.
DR   PRINTS; PR00236; HSVCAPSIDP40.
DR   SUPFAM; SSF50789; Herpes virus serine proteinase, assemblin; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative promoter usage; Direct protein sequencing;
KW   Host cytoplasm; Host nucleus; Hydrolase; Phosphoprotein; Protease;
KW   Reference proteome; Serine protease; Viral capsid assembly;
KW   Viral release from host cell.
FT   CHAIN           1..635
FT                   /note="Capsid scaffolding protein"
FT                   /id="PRO_0000027244"
FT   CHAIN           1..247
FT                   /note="Assemblin"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04008"
FT                   /id="PRO_0000027245"
FT   CHAIN           248..635
FT                   /note="Assembly protein"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04008"
FT                   /id="PRO_0000027246"
FT   REGION          324..343
FT                   /note="Interaction with pAP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04008"
FT   REGION          409..476
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          514..606
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          615..635
FT                   /note="Interaction with major capsid protein"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04008"
FT   MOTIF           426..429
FT                   /note="Nuclear localization signal"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        422..436
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        531..590
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        61
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04008"
FT   ACT_SITE        129
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04008"
FT   ACT_SITE        148
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04008"
FT   SITE            247..248
FT                   /note="Cleavage; by assemblin; Release site"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04008"
FT   SITE            610..611
FT                   /note="Cleavage; by assemblin; Tail site"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04008"
FT   VAR_SEQ         1..306
FT                   /note="Missing (in isoform pAP)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_037414"
SQ   SEQUENCE   635 AA;  66471 MW;  F3B3C7D42F3D062D CRC64;
     MAADAPGDRM EEPLPDRAVP IYVAGFLALY DSGDSGELAL DPDTVRAALP PDNPLPINVD
     HRAGCEVGRV LAVVDDPRGP FFVGLIACVQ LERVLETAAS AAIFERRGPP LSREERLLYL
     ITNYLPSVSL ATKRLGGEAH PDRTLFAHVA LCAIGRRLGT IVTYDTGLDA AIAPFRHLSP
     ASREGARRLA AEAELALSGR TWAPGVEALT HTLLSTAVNN MMLRDRWSLV AERRRQAGIA
     GHTYLQASEK FKMWGAEPVS APARGYKNGA PESTDIPPGS IAAAPQGDRC PIVRQRGVAL
     SPVLPPMNPV PTSGTPAPAP PGDGSYLWIP ASHYNQLVAG HAAPQPQPHS AFGFPAAAGS
     VAYGPHGAGL SQHYPPHVAH QYPGVLFSGP SPLEAQIAAL VGAIAADRQA GGQPAAGDPG
     VRGSGKRRRY EAGPSESYCD QDEPDADYPY YPGEARGAPR GVDSRRAARH SPGTNETITA
     LMGAVTSLQQ ELAHMRARTS APYGMYTPVA HYRPQVGEPE PTTTHPALCP PEAVYRPPPH
     SAPYGPPQGP ASHAPTPPYA PAACPPGPPP PPCPSTQTRA PLPTEPAFPP AATGSQPEAS
     NAEAGALVNA SSAAHVDVDT ARAADLFVSQ MMGAR
//