#=GF ID   VP4_2
#=GF AC   PF08935.14
#=GF DE   Viral protein VP4 subunit
#=GF PI   DUF1865;
#=GF AU   Mistry J;0000-0003-2479-5322
#=GF AU   Sammut SJ;0000-0003-4472-904X
#=GF SE   pdb_2bai
#=GF GA   22.20 22.20;
#=GF TC   22.20 27.20;
#=GF NC   21.10 21.00;
#=GF BM   hmmbuild HMM.ann SEED.ann
#=GF SM   hmmsearch -E 1000 --cpu 4 -Z 75585367 HMM pfamseq
#=GF TP   Domain
#=GF WK   Domain_of_unknown_function
#=GF CL   CL0055
#=GF RN   [1]
#=GF RM   9371640
#=GF RT   Dissecting the roles of VP0 cleavage and RNA packaging in
#=GF RT   picornavirus capsid stabilization: the structure of empty
#=GF RT   capsids of foot-and-mouth disease virus.
#=GF RA   Curry S, Fry E, Blakemore W, Abu-Ghazaleh R, Jackson T, King A,
#=GF RA   Lea S, Newman J, Stuart D;
#=GF RL   J Virol. 1997;71:9743-9752.
#=GF RN   [2]
#=GF RM   10627545
#=GF RT   Molecular tectonic model of virus structural transitions: the
#=GF RT   putative cell entry states of poliovirus.
#=GF RA   Belnap DM, Filman DJ, Trus BL, Cheng N, Booy FP, Conway JF,
#=GF RA   Curry S, Hiremath CN, Tsang SK, Steven AC, Hogle JM;
#=GF RL   J Virol. 2000;74:1342-1354.
#=GF DR   INTERPRO; IPR015031;
#=GF DR   SO; 0000417; polypeptide_domain;
#=GF CC   This domain is predominantly found in viral proteins from the
#=GF CC   family Picornaviridae. It is VP4 of the viral polyprotein which,
#=GF CC   in poliovirus, is part of the capsid that consists of 60 copies
#=GF CC   each of four proteins VP1, VP2, VP3, and VP4 arranged on an
#=GF CC   icosahedral lattice [1]. VP4 is on the inside and differs from
#=GF CC   the others in being small, myristoylated and having an extended
#=GF CC   structure. Productive infection involves the externalisation of
#=GF CC   the VP4, which is cleaved from the rest, along with the
#=GF CC   N-terminus of VP1. There thus seem to be three stages of the
#=GF CC   virus, ie a multi-step process for cell entry involving RNA
#=GF CC   translocation through a membrane channel formed by the
#=GF CC   externalised N termini of VP1 [2].
#=GF SQ   6
#=GS F4YYF3_HUNVO/84-163   AC F4YYF3.1
#=GS POLG_EMCVR/67-120     AC Q66765.1
#=GS X2L6K2_MOVA2/453-531  AC X2L6K2.1
#=GS Q9WJ28_PTV1F/119-191  AC Q9WJ28.1
#=GS Q9DLK1_FMDVP/202-285  AC Q9DLK1.1
#=GS Q66776_ERBV1/220-284  AC Q66776.1
F4YYF3_HUNVO/84-163              ....GPGQSKQESGNTNNSGNHGVINYNFYNQQWQNSVDL---EHA.MENNATAygGTGGGDSQHNSNRTENLL---LSGLQAATTILPL-l...............
POLG_EMCVR/67-120                qgns---TSSDKN-NSSSEGNEGVIINNFYSNQYQNSIDL--SANA.AG-----..-----------------------------------sdpprtygqfsn....
X2L6K2_MOVA2/453-531             ....GGGQSKPQQGNVNGSQNQGINVYNYYNQQYQNSVDM---SNApLSVGGSG..GGNQAASNHTNNSHMN-------------------fvttgfnmasnlvplm
Q9WJ28_PTV1F/119-191             ....GTGTSRMENGNTNNSGNTGVINYNFYSNSYTDAVDL---SGA.MSSQESN..AAENAASGPTSLLK--------AGINAAARIGPLL................
Q9DLK1_FMDVP/202-285             ....GAGQSSPTTGSQNQSGNTGSIINNYYMQQYQNSMDTQLGDNA.ISGGSNE..GSTDTTSTHTNNTQNNDWFSKLANTAFSGLFGALL................
Q66776_ERBV1/220-284             ....GAGHSRPEGGHNNESGNNGTIVNNYYMQHYQNSVDL----DG.MTSQNIG..GQPGSSSNP--------------------------fssildilgta.....
#=GC seq_cons                    ....GsGpS+scsGNsNsSGNpGlIl.NaYsQQYQNSVDL...ssA.hostsss..GsssusSs.ss..p.....................................
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