SCAF_VZVD
ID SCAF_VZVD Reviewed; 605 AA.
AC P09286; Q65ZF9;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Capsid scaffolding protein {ECO:0000255|HAMAP-Rule:MF_04008};
DE AltName: Full=Protease precursor {ECO:0000255|HAMAP-Rule:MF_04008};
DE Short=pPR {ECO:0000255|HAMAP-Rule:MF_04008};
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=33;
OS Varicella-zoster virus (strain Dumas) (HHV-3) (Human herpesvirus 3).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Alphaherpesvirinae; Varicellovirus.
OX NCBI_TaxID=10338;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=3018124; DOI=10.1099/0022-1317-67-9-1759;
RA Davison A.J., Scott J.E.;
RT "The complete DNA sequence of varicella-zoster virus.";
RL J. Gen. Virol. 67:1759-1816(1986).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 11-231.
RX PubMed=9096314; DOI=10.1073/pnas.94.7.2874;
RA Qiu X., Janson C.A., Culp J.S., Richardson S.B., Debouck C., Smith W.W.,
RA Abdel-Meguid S.S.;
RT "Crystal structure of varicella-zoster virus protease.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:2874-2879(1997).
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;
CC IsoId=P09286-1; Sequence=Displayed;
CC Name=pAP; Synonyms=Assembly protein;
CC IsoId=P09286-2; Sequence=VSP_037420;
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; X04370; CAA27916.1; -; Genomic_DNA.
DR EMBL; X04370; CAH19069.1; -; Genomic_DNA.
DR PIR; G27214; WZBE33.
DR PDB; 1VZV; X-ray; 3.00 A; A=11-231.
DR PDBsum; 1VZV; -.
DR SMR; P09286; -.
DR MEROPS; S21.005; -.
DR PRIDE; P09286; -.
DR EvolutionaryTrace; P09286; -.
DR Proteomes; UP000002602; 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: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 3D-structure; Alternative promoter usage; Host cytoplasm; Host nucleus;
KW Hydrolase; Phosphoprotein; Protease; Reference proteome; Serine protease;
KW Viral capsid assembly; Viral release from host cell.
FT CHAIN 1..605
FT /note="Capsid scaffolding protein"
FT /id="PRO_0000027269"
FT CHAIN 1..236
FT /note="Assemblin"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04008"
FT /id="PRO_0000027270"
FT CHAIN 237..605
FT /note="Assembly protein"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04008"
FT /id="PRO_0000027271"
FT REGION 326..344
FT /note="Interaction with pAP"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04008"
FT REGION 585..605
FT /note="Interaction with major capsid protein"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04008"
FT ACT_SITE 52
FT /note="Charge relay system"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04008"
FT ACT_SITE 120
FT /note="Charge relay system"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04008"
FT ACT_SITE 139
FT /note="Charge relay system"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04008"
FT SITE 236..237
FT /note="Cleavage; by assemblin; Release site"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04008"
FT SITE 578..579
FT /note="Cleavage; by assemblin; Tail site"
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..303
FT /note="Missing (in isoform pAP)"
FT /evidence="ECO:0000305"
FT /id="VSP_037420"
FT STRAND 13..19
FT /evidence="ECO:0007829|PDB:1VZV"
FT TURN 22..25
FT /evidence="ECO:0007829|PDB:1VZV"
FT TURN 27..29
FT /evidence="ECO:0007829|PDB:1VZV"
FT HELIX 33..39
FT /evidence="ECO:0007829|PDB:1VZV"
FT STRAND 47..50
FT /evidence="ECO:0007829|PDB:1VZV"
FT STRAND 57..66
FT /evidence="ECO:0007829|PDB:1VZV"
FT STRAND 68..77
FT /evidence="ECO:0007829|PDB:1VZV"
FT HELIX 80..89
FT /evidence="ECO:0007829|PDB:1VZV"
FT HELIX 97..100
FT /evidence="ECO:0007829|PDB:1VZV"
FT HELIX 106..115
FT /evidence="ECO:0007829|PDB:1VZV"
FT STRAND 118..122
FT /evidence="ECO:0007829|PDB:1VZV"
FT STRAND 139..145
FT /evidence="ECO:0007829|PDB:1VZV"
FT STRAND 154..158
FT /evidence="ECO:0007829|PDB:1VZV"
FT HELIX 159..162
FT /evidence="ECO:0007829|PDB:1VZV"
FT STRAND 167..169
FT /evidence="ECO:0007829|PDB:1VZV"
FT HELIX 171..183
FT /evidence="ECO:0007829|PDB:1VZV"
FT HELIX 195..207
FT /evidence="ECO:0007829|PDB:1VZV"
FT TURN 208..211
FT /evidence="ECO:0007829|PDB:1VZV"
FT HELIX 215..226
FT /evidence="ECO:0007829|PDB:1VZV"
SQ SEQUENCE 605 AA; 66047 MW; 2F2C2FE6AB6D2C17 CRC64;
MAAEADEENC EALYVAGYLA LYSKDEGELN ITPEIVRSAL PPTSKIPINI DHRKDCVVGE
VIAIIEDIRG PFFLGIVRCP QLHAVLFEAA HSNFFGNRDS VLSPLERALY LVTNYLPSVS
LSSKRLSPNE IPDGNFFTHV ALCVVGRRVG TVVNYDCTPE SSIEPFRVLS MESKARLLSL
VKDYAGLNKV WKVSEDKLAK VLLSTAVNNM LLRDRWDVVA KRRREAGIMG HVYLQASTGY
GLARITNVNG VESKLPNAGV INATFHPGGP IYDLALGVGE SNEDCEKTVP HLKVTQLCRN
DSDMASVAGN ASNISPQPPS GVPTGGEFVL IPTAYYSQLL TGQTKNPQVS IGAPNNGQYI
VGPYGSPHPP AFPPNTGGYG CPPGHFGGPY GFPGYPPPNR LEMQMSAFMN ALAAERGIDL
QTPCVNFPDK TDVRRPGKRD FKSMDQRELD SFYSGESQMD GEFPSNIYFP GEPTYITHRR
RRVSPSYWQR RHRVSNGQHE ELAGVVAKLQ QEVTELKSQN GTQMPLSHHT NIPEGTRDPR
ISILLKQLQS VSGLCSSQNT TSTPHTDTVG QDVNAVEASS KAPLIQGSTA DDADMFANQM
MVGRC
