ID VP40_EHV2 Reviewed; 643 AA. AC P52369; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 04-NOV-2008, entry version 52. DE RecName: Full=Capsid protein P40; DE Contains: DE RecName: Full=Assemblin; DE AltName: Full=Protease; DE EC=3.4.21.97; DE Contains: DE RecName: 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 MEDLINE=95302501; 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: The capsid assembly protein is component of the capsid CC core involved in processing and packaging of progeny DNA. CC -!- FUNCTION: Assemblin is a protease which can proteolytically cleave CC itself and the capsid assembly protein at the C-terminus. CC -!- CATALYTIC ACTIVITY: Cleaves -Ala-|-Ser- and -Ala-|-Ala- bonds in CC the scaffold protein. CC -!- SUBCELLULAR LOCATION: Virion (Potential). CC -!- SIMILARITY: Belongs to the peptidase S21 family. 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; -. DR HSSP; P03234; 1O6E. DR MEROPS; S21.006; -. DR GeneID; 1461012; -. DR GO; GO:0019028; C:viral capsid; IEA:UniProtKB-KW. DR GO; GO:0005198; F:structural molecule activity; IEA:UniProtKB-KW. DR GO; GO:0006323; P:DNA packaging; IEA:UniProtKB-KW. DR InterPro; IPR001847; Peptidase_S21. DR Gene3D; G3DSA:3.20.16.10; Peptidase_S21; 1. DR Pfam; PF00716; Peptidase_S21; 1. DR PRINTS; PR00236; HSVCAPSIDP40. PE 3: Inferred from homology; KW Capsid protein; DNA packaging; Hydrolase; Protease; Serine protease; KW Virion. FT CHAIN 1 269 Assemblin. FT /FTId=PRO_0000027263. FT CHAIN 270 643 Capsid assembly protein. FT /FTId=PRO_0000027264. FT ACT_SITE 82 82 Charge relay system (By similarity). FT ACT_SITE 151 151 Charge relay system (By similarity). FT ACT_SITE 173 173 Charge relay system (By similarity). FT SITE 269 270 Cleavage; by the protease (Probable). 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 //