SCAF_EBVB9
ID SCAF_EBVB9 Reviewed; 605 AA.
AC P03234; Q66541; Q777B6;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 130.
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 B95-8) (HHV-4) (Human herpesvirus 4).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Gammaherpesvirinae; Lymphocryptovirus.
OX NCBI_TaxID=10377;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6092825;
RA Bankier A.T., Deininger P.L., Farrell P.J., Barrell B.G.;
RT "Sequence analysis of the 17,166 base-pair EcoRI fragment C of B95-8
RT Epstein-Barr virus.";
RL Mol. Biol. Med. 1:21-45(1983).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=6087149; DOI=10.1038/310207a0;
RA Baer R., Bankier A.T., Biggin M.D., Deininger P.L., Farrell P.J.,
RA Gibson T.J., Hatfull G., Hudson G.S., Satchwell S.C., Seguin C.,
RA Tuffnell P.S., Barrell B.G.;
RT "DNA sequence and expression of the B95-8 Epstein-Barr virus genome.";
RL Nature 310:207-211(1984).
RN [3]
RP FUNCTION.
RX PubMed=19158247; DOI=10.1128/jvi.01733-08;
RA Henson B.W., Perkins E.M., Cothran J.E., Desai P.;
RT "Self-assembly of Epstein-Barr virus capsids.";
RL J. Virol. 83:3877-3890(2009).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 1-235.
RX PubMed=12421561; DOI=10.1016/s0022-2836(02)01040-9;
RA Buisson M., Hernandez J.F., Lascoux D., Schoehn G., Forest E., Arlaud G.,
RA Seigneurin J.M., Ruigrok R.W., Burmeister W.P.;
RT "The crystal structure of the Epstein-Barr virus protease shows
RT rearrangement of the processed C terminus.";
RL J. Mol. Biol. 324:89-103(2002).
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, ECO:0000269|PubMed:19158247}.
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 ECO:0000269|PubMed:19158247}.
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 ECO:0000269|PubMed:19158247}.
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, EC-RF3;
CC IsoId=P03234-1; Sequence=Displayed;
CC Name=pAP; Synonyms=Assembly protein, EC-RF3A;
CC IsoId=P03234-2; Sequence=VSP_018865;
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; V01555; CAA24801.1; -; Genomic_DNA.
DR EMBL; V01555; CAA24802.1; -; Genomic_DNA.
DR EMBL; AJ507799; CAD53454.1; -; Genomic_DNA.
DR EMBL; AJ507799; CAD53455.1; -; Genomic_DNA.
DR PIR; A03798; QQBE3R.
DR RefSeq; YP_401704.1; NC_007605.1.
DR RefSeq; YP_401705.1; NC_007605.1.
DR PDB; 1O6E; X-ray; 2.30 A; A/B=1-235.
DR PDBsum; 1O6E; -.
DR SMR; P03234; -.
DR BindingDB; P03234; -.
DR ChEMBL; CHEMBL4013; -.
DR DrugBank; DB03976; Phosphorylisopropane.
DR MEROPS; S21.003; -.
DR PRIDE; P03234; -.
DR DNASU; 3783696; -.
DR DNASU; 3783733; -.
DR GeneID; 3783696; -.
DR GeneID; 3783733; -.
DR KEGG; vg:3783696; -.
DR KEGG; vg:3783733; -.
DR EvolutionaryTrace; P03234; -.
DR Proteomes; UP000153037; 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 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_0000027279"
FT CHAIN 1..235
FT /note="Assemblin"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04008"
FT /id="PRO_0000027280"
FT CHAIN 236..605
FT /note="Assembly protein"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04008"
FT /id="PRO_0000027281"
FT REGION 235..274
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_018865"
FT STRAND 7..14
FT /evidence="ECO:0007829|PDB:1O6E"
FT STRAND 21..23
FT /evidence="ECO:0007829|PDB:1O6E"
FT HELIX 29..35
FT /evidence="ECO:0007829|PDB:1O6E"
FT STRAND 42..46
FT /evidence="ECO:0007829|PDB:1O6E"
FT STRAND 49..62
FT /evidence="ECO:0007829|PDB:1O6E"
FT STRAND 67..73
FT /evidence="ECO:0007829|PDB:1O6E"
FT HELIX 76..79
FT /evidence="ECO:0007829|PDB:1O6E"
FT HELIX 81..86
FT /evidence="ECO:0007829|PDB:1O6E"
FT HELIX 90..93
FT /evidence="ECO:0007829|PDB:1O6E"
FT HELIX 103..111
FT /evidence="ECO:0007829|PDB:1O6E"
FT STRAND 114..120
FT /evidence="ECO:0007829|PDB:1O6E"
FT STRAND 136..145
FT /evidence="ECO:0007829|PDB:1O6E"
FT STRAND 147..150
FT /evidence="ECO:0007829|PDB:1O6E"
FT STRAND 154..157
FT /evidence="ECO:0007829|PDB:1O6E"
FT HELIX 159..164
FT /evidence="ECO:0007829|PDB:1O6E"
FT HELIX 171..184
FT /evidence="ECO:0007829|PDB:1O6E"
FT HELIX 198..207
FT /evidence="ECO:0007829|PDB:1O6E"
FT HELIX 214..224
FT /evidence="ECO:0007829|PDB:1O6E"
FT STRAND 229..232
FT /evidence="ECO:0007829|PDB:1O6E"
SQ SEQUENCE 605 AA; 64102 MW; FC2D355F8A389708 CRC64;
MVQAPSVYVC GFVERPDAPP KDACLHLDPL TVKSQLPLKK PLPLTVEHLP DAPVGSVFGL
YQSRAGLFSA ASITSGDFLS LLDSIYHDCD IAQSQRLPLP REPKVEALHA WLPSLSLASL
HPDIPQTTAD GGKLSFFDHV SICALGRRRG TTAVYGTDLA WVLKHFSDLE PSIAAQIEND
ANAAKRESGC PEDHPLPLTK LIAKAIDAGF LRNRVETLRQ DRGVANIPAE SYLKASDAPD
LQKPDKALQS PPPASTDPAT MLSGNAGEGA TACGGSAAAG QDLISVPRNT FMTLLQTNLD
NKPPRQTPLP YAAPLPPFSH QAIATAPSYG PGAGAVAPAG GYFTSPGGYY AGPAGGDPGA
FLAMDAHTYH PHPHPPPAYF GLPGLFGPPP PVPPYYGSHL RADYVPAPSR SNKRKRDPEE
DEEGGGLFPG EDATLYRKDI AGLSKSVNEL QHTLQALRRE TLSYGHTGVG YCPQQGPCYT
HSGPYGFQPH QSYEVPRYVP HPPPPPTSHQ AAQAQPPPPG TQAPEAHCVA ESTIPEAGAA
GNSGPREDTN PQQPTTEGHH RGKKLVQASA SGVAQSKEPT TPKAKSVSAH LKSIFCEELL
NKRVA
