SCAF_HHV11
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 03-AUG-2022, entry version 134.
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; Herpesviridae; Alphaherpesvirinae; Simplexvirus.
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 homomultimerizes and interacts with
CC major capsid protein. Assemblin exists in a monomer-dimer equilibrium
CC with the dimer being the active species. Assembly protein
CC homomultimerizes and interacts with major capsid protein.
CC {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}.
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DR EMBL; X14112; CAA32318.1; -; Genomic_DNA.
DR EMBL; X14112; CAA32319.1; -; Genomic_DNA.
DR PIR; H30084; WMBEW6.
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 PRIDE; P10210; -.
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; -; 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.
PE 1: Evidence at protein level;
KW Alternative promoter usage; Direct protein sequencing; Host cytoplasm;
KW Host nucleus; Hydrolase; Phosphoprotein; Protease; Reference proteome;
KW Serine protease; Viral capsid assembly; 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
