SCAF_HHV2H
ID SCAF_HHV2H Reviewed; 637 AA.
AC P89449; P90341;
DT 05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 85.
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=Capsid protein VP24;
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};
DE AltName: Full=Capsid protein VP22A;
GN Name=UL26;
OS Human herpesvirus 2 (strain HG52) (HHV-2) (Human herpes simplex virus 2).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Alphaherpesvirinae; Simplexvirus.
OX NCBI_TaxID=10315;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=1662697; DOI=10.1099/0022-1317-72-12-3057;
RA McGeoch D.J., Cunningham C., McIntyre G., Dolan A.;
RT "Comparative sequence analysis of the long repeat regions and adjoining
RT parts of the long unique regions in the genomes of herpes simplex viruses
RT types 1 and 2.";
RL J. Gen. Virol. 72:3057-3075(1991).
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 -!- 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=P89449-1; Sequence=Displayed;
CC Name=pAP; Synonyms=Assembly protein, UL26.5 protein;
CC IsoId=P89449-2; Sequence=VSP_040777;
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; Z86099; CAB06750.1; -; Genomic_DNA.
DR EMBL; Z86099; CAB06751.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; YP_009137177.1; NC_001798.2.
DR RefSeq; YP_009137178.1; NC_001798.2.
DR SMR; P89449; -.
DR BindingDB; P89449; -.
DR ChEMBL; CHEMBL3416; -.
DR MEROPS; S21.001; -.
DR PRIDE; P89449; -.
DR DNASU; 1487310; -.
DR GeneID; 1487310; -.
DR GeneID; 1487311; -.
DR KEGG; vg:1487310; -.
DR KEGG; vg:1487311; -.
DR Proteomes; UP000001874; Genome.
DR GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0042802; F:identical protein binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
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 3: Inferred from homology;
KW Alternative promoter usage; Host cytoplasm; Host nucleus; Hydrolase;
KW Phosphoprotein; Protease; Reference proteome; Serine protease;
KW Viral capsid assembly; Viral release from host cell.
FT CHAIN 1..637
FT /note="Capsid scaffolding protein"
FT /id="PRO_0000406172"
FT CHAIN 1..247
FT /note="Assemblin"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04008"
FT /id="PRO_0000406173"
FT CHAIN 248..637
FT /note="Assembly protein"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04008"
FT /id="PRO_0000406174"
FT REGION 262..326
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 326..345
FT /note="Interaction with pAP"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04008"
FT REGION 414..479
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 502..608
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 617..637
FT /note="Interaction with major capsid protein"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04008"
FT MOTIF 428..431
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250"
FT COMPBIAS 291..308
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 423..467
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 531..598
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 612..613
FT /note="Cleavage; by assemblin; Tail site"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04008"
FT VAR_SEQ 1..308
FT /note="Missing (in isoform pAP)"
FT /evidence="ECO:0000305"
FT /id="VSP_040777"
SQ SEQUENCE 637 AA; 66941 MW; 96B9D1F68C8DAB9C CRC64;
MASAEMRERL EAPLPDRAVP IYVAGFLALY DSGDPGELAL DPDTVRAALP PENPLPINVD
HRARCEVGRV LAVVNDPRGP FFVGLIACVQ LERVLETAAS AAIFERRGPA LSREERLLYL
ITNYLPSVSL STKRRGDEVP PDRTLFAHVA LCAIGRRLGT IVTYDTSLDA AIAPFRHLDP
ATREGVRREA AEAELALAGR TWAPGVEALT HTLLSTAVNN MMLRDRWSLV AERRRQAGIA
GHTYLQASEK FKIWGAESAP APERGYKTGA PGAMDTSPAA SVPAPQVAVR ARQVASSSSS
SSFPAPADMN PVSASGAPAP PPPGDGSYLW IPASHYNQLV TGQSAPRHPP LTACGLPAAG
TVAYGHPGAG PSPHYPPPPA HPYPGMLFAG PSPLEAQIAA LVGAIAADRQ AGGLPAAAGD
HGIRGSAKRR RHEVEQPEYD CGRDEPDRDF PYYPGEARPE PRPVDSRRAA RQASGPHETI
TALVGAVTSL QQELAHMRAR THAPYGPYPP VGPYHHPHAD TETPAQPPRY PAKAVYLPPP
HIAPPGPPLS GAVPPPSYPP VAVTPGPAPP LHQPSPAHAH PPPPPPGPTP PPAASLPQPE
APGAEAGALV NASSAAHVNV DTARAADLFV SQMMGSR
