ID SCAF_EHV2 Reviewed; 643 AA. AC P52369; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 11-NOV-2015, entry version 83. DE RecName: Full=Capsid scaffolding protein; DE AltName: Full=Capsid protein P40; DE AltName: Full=Protease precursor; DE Short=pPR; DE Contains: DE RecName: Full=Assemblin; DE EC=3.4.21.97; DE AltName: Full=Protease; DE Contains: DE RecName: Full=Assembly protein; DE AltName: Full=Capsid assembly protein; GN ORFNames=17; OS Equine herpesvirus 2 (strain 86/87) (EHV-2). OC Viruses; dsDNA viruses, no RNA stage; Herpesvirales; Herpesviridae; OC Gammaherpesvirinae; Percavirus. OX NCBI_TaxID=82831; OH NCBI_TaxID=9796; Equus caballus (Horse). RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=7783207; DOI=10.1006/jmbi.1995.0314; RA Telford E.A.R., Watson M.S., Aird H.C., Perry J., Davison A.J.; RT "The DNA sequence of equine herpesvirus 2."; RL J. Mol. Biol. 249:520-528(1995). CC -!- FUNCTION: Capsid scaffolding protein: Acts as a scaffold protein CC by binding major capsid protein VP5 in the cytoplasm, inducing the CC nuclear localization of both proteins. Multimerizes in the nucleus CC such as VP5 forms the icosahedral T=16 capsid. Autocatalytic CC cleavage releases the assembly protein, and subsequently abolishes CC interaction with major capsid protein VP5. Cleavages products are CC evicted from the capsid before or during DNA packaging. CC {ECO:0000250|UniProtKB:P03234}. CC -!- FUNCTION: Assemblin: Protease that plays an essential role in CC virion assembly within the nucleus. Catalyzes the cleavage of the CC assembly protein after formation of the spherical procapsid. By CC that cleavage, the capsid matures and gains its icosahedral shape. CC The cleavage sites seem to include -Ala-|-Ser-, -Ala-|-Ala-, as CC well as Ala-Thr bonds. Assemblin and cleavages products are CC evicted from the capsid before or during DNA packaging. CC {ECO:0000250|UniProtKB:P03234}. CC -!- FUNCTION: Assembly protein: Plays a major role in capsid assembly. CC Acts as a scaffold protein by binding major capsid protein VP5. CC Multimerizes in the nucleus such as VP5 forms the icosahedral T=16 CC capsid. Cleaved by assemblin after capsid completion. The CC cleavages products are evicted from the capsid before or during CC DNA packaging. {ECO:0000250|UniProtKB:P03234}. CC -!- CATALYTIC ACTIVITY: Cleaves -Ala-|-Ser- and -Ala-|-Ala- bonds in CC the scaffold protein. CC -!- SUBUNIT: Capsid scaffolding protein homomultimerizes and interacts CC with major capsid protein. Assemblin exists in a monomer-dimer CC equilibrium with the dimer being the active species. Assembly CC protein homomultimerizes and interacts with major capsid protein CC (By similarity). {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Capsid scaffolding protein: Host cytoplasm CC {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Assemblin: Host nucleus {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Assembly protein: Host nucleus CC {ECO:0000250}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative promoter usage; Named isoforms=2; CC Name=Capsid scaffolding protein; Synonyms=pPR; CC IsoId=P52369-1; Sequence=Displayed; CC Name=pAP; Synonyms=Assembly protein; CC IsoId=P52369-2; Sequence=VSP_037417; CC -!- DOMAIN: Region of interaction between pPR and pAP is called Amino CC conserved domain (ACD). The region of interaction with major CC capsid protein is called carboxyl conserved domain (CCD) (By CC similarity). {ECO:0000250}. CC -!- PTM: Capsid scaffolding protein is cleaved by assemblin after CC formation of the spherical procapsid. As a result, the capsid CC obtains its mature, icosahedral shape. Cleavages occur at two or CC more sites: release and tail site. {ECO:0000250|UniProtKB:P03234}. CC -!- SIMILARITY: Belongs to the herpesviridae capsid scaffolding CC protein family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; U20824; AAC13804.1; -; Genomic_DNA. DR PIR; S55610; S55610. DR RefSeq; NP_042612.1; NC_001650.2. DR ProteinModelPortal; P52369; -. DR MEROPS; S21.006; -. DR GeneID; 1461012; -. DR KEGG; vg:1461012; -. DR Proteomes; UP000007083; 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:0004252; F:serine-type endopeptidase activity; IEA:InterPro. DR GO; GO:0019076; P:viral release from host cell; IEA:UniProtKB-KW. DR InterPro; IPR001847; Peptidase_S21. DR Pfam; PF00716; Peptidase_S21; 1. DR PRINTS; PR00236; HSVCAPSIDP40. PE 3: Inferred from homology; KW Alternative promoter usage; Complete proteome; Host cytoplasm; KW Host nucleus; Hydrolase; Protease; Reference proteome; KW Serine protease; Viral capsid assembly; Virus exit from host cell. FT CHAIN 1 643 Capsid scaffolding protein. FT /FTId=PRO_0000376800. FT CHAIN 1 269 Assemblin. FT /FTId=PRO_0000027263. FT CHAIN 270 643 Assembly protein. FT /FTId=PRO_0000027264. FT REGION 324 343 Interaction with pAP. FT REGION 623 643 Interaction with major capsid protein. FT MOTIF 439 445 Nuclear localization signal. FT {ECO:0000255}. FT ACT_SITE 82 82 Charge relay system. {ECO:0000250}. FT ACT_SITE 151 151 Charge relay system. {ECO:0000250}. FT ACT_SITE 173 173 Charge relay system. {ECO:0000250}. FT SITE 269 270 Cleavage; by assemblin; Release site. FT {ECO:0000250}. FT SITE 621 622 Cleavage; by assemblin; Tail site. FT {ECO:0000250}. FT VAR_SEQ 1 307 Missing (in isoform pAP). {ECO:0000305}. FT /FTId=VSP_037417. SQ SEQUENCE 643 AA; 68394 MW; 1108A7A40E9FCA38 CRC64; MSSPSPSSSS SDHPSSPAPV PAPPGPVPEA AAASRASRAP VYLGGFVDVF SYPKDSRALY LNPADVGAHL PLPGPIPLNV EHLQEAHVGW TLGLHLTRYG LFCVAVITAE EFFTLLDRLC AASSVARTRA DHHLPPNPTL EMLHTWLPEL SLSSIHPDAL PGAKGGDTPI FQHVALCAMG QRRGTVAVYG ESLDWILSKF TSLSPEERGA IAEGYASPAP ESLPEPHFTC SNEILMAKAI DAGFIKNRLE ILKTDKGVAE VKAPTYLKAS VQGLPANLDE VDSARGGEDP PTAAIATTPH PATDATTMNQ QQPFAAQAPA GGCEDLISVP RSTFMTMLQT NLDTMRQTSL GQRFGQPIDA PAAPPAQLRV PPPAAPFPVH PGYYPAPYHP QVDAQAQYLP YVPLPPPGAM PFAPPPLPDF YKYGGIPAPG YSPVAHPARP GKRKRDCDEE FEGPLFPGEI HKDVQSLSKS IAALQSELKD IKNSQQFPQP LPQPQLQPQA QPQPQPAPQL YPAPPQAFYH PAAGDQGYYV RYLNPFQASG GVPCAPGPQG VGEPQAPQVT VTHNGHQAAP QAGGGATGAT AANVEQRQPE GGEACGAQQQ QPPQPQPQQQ QQPQQQAFVE ASTKPSQISQ LQKIFCEELL NKT //