ID VP40_HSVE2 STANDARD; PRT; 643 AA. AC P52369; DT 01-OCT-1996 (REL. 34, CREATED) DT 01-OCT-1996 (REL. 34, LAST SEQUENCE UPDATE) DT 01-OCT-1996 (REL. 34, LAST ANNOTATION UPDATE) DE CAPSID PROTEIN P40 [CONTAINS: ASSEMBLIN (PROTEASE) (EC 3.4.21.-); DE CAPSID ASSEMBLY PROTEIN]. GN 17. OS EQUINE HERPESVIRUS TYPE 2 (STRAIN 86/87) (EHV-2). OC VIRUSES; DSDNA VIRUSES, NO RNA STAGE; HERPESVIRIDAE; OC BETAHERPESVIRINAE. RN [1] RP SEQUENCE FROM N.A. RX MEDLINE; 95302501. RA TELFORD E.A., 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: PREFERENTIALLY CLEAVES AT ALA-|-SER OR ALA-|- CC ALA. CC -!- SIMILARITY: BELONGS TO PEPTIDASE FAMILY S21 (SERINE PROTEASE). CC -!- SIMILARITY: TO OTHER HERPESVIRUSES CAPSID PROTEIN VP40. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- 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; G695188; -. DR PFAM; PF00716; Peptidase_S21; 1. DR HSSP; P16753; 1CMV. KW COAT PROTEIN; HYDROLASE; SERINE PROTEASE. FT CHAIN 1 269 ASSEMBLIN (PROTEASE). FT CHAIN 270 643 CAPSID ASSEMBLY PROTEIN. FT SITE 269 270 CLEAVAGE (BY THE PROTEASE) (PROBABLE). 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). SQ SEQUENCE 643 AA; 68394 MW; 6016B306 CRC32; 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 //