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 03-AUG-2022, entry version 100. 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 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=17; OS Equine herpesvirus 2 (strain 86/87) (EHV-2). OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes; OC Herpesvirales; Herpesviridae; 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 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=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 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}. 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 SMR; 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: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..643 FT /note="Capsid scaffolding protein" FT /id="PRO_0000376800" FT CHAIN 1..269 FT /note="Assemblin" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04008" FT /id="PRO_0000027263" FT CHAIN 270..643 FT /note="Assembly protein" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04008" FT /id="PRO_0000027264" FT REGION 1..31 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 283..306 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 324..343 FT /note="Interaction with pAP" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04008" FT REGION 485..519 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 544..625 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 623..643 FT /note="Interaction with major capsid protein" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04008" FT MOTIF 439..445 FT /note="Nuclear localization signal" FT /evidence="ECO:0000250" FT COMPBIAS 1..15 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 491..515 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 593..625 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 82 FT /note="Charge relay system" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04008" FT ACT_SITE 151 FT /note="Charge relay system" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04008" FT ACT_SITE 173 FT /note="Charge relay system" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04008" FT SITE 269..270 FT /note="Cleavage; by assemblin; Release site" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04008" FT SITE 621..622 FT /note="Cleavage; by assemblin; Tail site" FT /evidence="ECO:0000250" FT VAR_SEQ 1..307 FT /note="Missing (in isoform pAP)" FT /evidence="ECO:0000305" FT /id="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 //