SCAF_EBVA8
ID SCAF_EBVA8 Reviewed; 605 AA.
AC Q1HVC7; Q1HVC6;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2006, sequence version 1.
DT 03-AUG-2022, entry version 65.
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=Protein EC-RF3/EC-RF3A;
DE AltName: Full=Virion structural protein BVRF2;
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 ORFNames=BVRF2;
OS Epstein-Barr virus (strain AG876) (HHV-4) (Human herpesvirus 4).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Gammaherpesvirinae; Lymphocryptovirus.
OX NCBI_TaxID=82830;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16490228; DOI=10.1016/j.virol.2006.01.015;
RA Dolan A., Addison C., Gatherer D., Davison A.J., McGeoch D.J.;
RT "The genome of Epstein-Barr virus type 2 strain AG876.";
RL Virology 350:164-170(2006).
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 Q1HVC7; P0CK58: BALF1; Xeno; NbExp=2; IntAct=EBI-2621352, EBI-2621293;
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, EC-RF3;
CC IsoId=Q1HVC7-1; Sequence=Displayed;
CC Name=pAP; Synonyms=Assembly protein, EC-RF3A;
CC IsoId=Q1HVC7-2; Sequence=VSP_037729;
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; DQ279927; ABB89280.1; -; Genomic_DNA.
DR EMBL; DQ279927; ABB89281.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; YP_001129501.1; NC_009334.1.
DR SMR; Q1HVC7; -.
DR IntAct; Q1HVC7; 1.
DR MEROPS; S21.003; -.
DR PRIDE; Q1HVC7; -.
DR GeneID; 5176187; -.
DR KEGG; vg:5176187; -.
DR Proteomes; UP000007639; 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 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..605
FT /note="Capsid scaffolding protein"
FT /id="PRO_0000379889"
FT CHAIN 1..235
FT /note="Assemblin"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04008"
FT /id="PRO_0000379890"
FT CHAIN 236..605
FT /note="Assembly protein"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04008"
FT /id="PRO_0000379891"
FT REGION 235..275
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 281..300
FT /note="Interaction with pAP"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04008"
FT REGION 403..432
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 489..588
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 585..605
FT /note="Interaction with major capsid protein"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04008"
FT MOTIF 410..416
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250"
FT COMPBIAS 408..423
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 496..523
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 569..587
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 48
FT /note="Charge relay system"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04008"
FT ACT_SITE 116
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 235..236
FT /note="Cleavage; by assemblin; Release site"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04008"
FT SITE 568..569
FT /note="Cleavage; by assemblin; Tail site"
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..260
FT /note="Missing (in isoform pAP)"
FT /evidence="ECO:0000305"
FT /id="VSP_037729"
SQ SEQUENCE 605 AA; 64154 MW; 60577C4CEDA1ED6C CRC64;
MVQAPSVYVC GFVERPDAPP KDACLHLDPL TVKSQLPLKK PLPLTVEHLP DAPVGSVFGL
YQSRAGLFSA ASITSGVFLS LLDSIYHDCD IAQSQRLPLP REPKLEALHA WLPSLSLASL
HPDIPQTTAD GGKLSFFDHV SICALGRRRG TTAVYGTDLA WVLKHFSDLE PSIAAQIEND
ANAAKRESGC PEDHPLPLTK LIAKAIDAGF LRNRVETLRQ DRGVANIPAE SYLKASDAPD
LQKPDKALQS PPPASTDPDT MLSGNAGEGA TACGGSAAAG QDLISVPRNT FMTLLQTNLD
NKPPRQTPLP YAAPLPPFSH QAIATAPSYG PGAGAVAPAG GYFTSPGGYY AGPAGGDPGA
FLAMDAHTYH PHPHPPPAYF GLPGLFGPPP PVPPYYGSHL RADYVPAPSR SNKRKRDPEE
DEEGGGLFPG EDATLYRKDI AGLSKSVNEL QHTLQALRRE TLSYGHTGVG YCPQQGPCYT
HPGPYGFQPH QSYEVPRYVP HPPPPPTSHQ AAQAQPPPPG TQAPEAHCVA ESTIPEAGAA
GNSGPREDTN PQQPTTEGHH RGKKLVQASA SGVAQSKEPT TPKAKSVSAH LKSIFCEELL
NKRVA
