#=GF ID   Vp24_capsid
#=GF AC   PF23371.1
#=GF DE   Capsid protein Vp24
#=GF AU   Chuguransky S;0000-0002-0520-0736
#=GF SE   ECOD, PDB:7chk
#=GF GA   27.00 27.00;
#=GF TC   279.10 278.40;
#=GF NC   23.60 19.60;
#=GF BM   hmmbuild  HMM.ann SEED.ann
#=GF SM   hmmsearch -E 1000 -Z 90746521 --cpu 8 HMM pfamseq
#=GF TP   Family
#=GF CL   CL0159
#=GF RN   [1]
#=GF RM   32887929
#=GF RT   Apple latent spherical virus structure with stable capsid frame
#=GF RT   supports  quasi-stable protrusions expediting genome release.
#=GF RA   Naitow H, Hamaguchi T, Maki-Yonekura S, Isogai M, Yoshikawa N,
#=GF RA   Yonekura K;
#=GF RL   Commun Biol. 2020;3:488.
#=GF DR   INTERPRO; IPR056476;
#=GF DR   SO; 0100021; polypeptide_conserved_region;
#=GF CC   This entry represents the capsid Vp24 protein from apple-latent
#=GF CC   spherical virus (ALSV) and related picorna-like plant viruses.
#=GF CC   This protein is encoded in a polyprotein that is cleaved into
#=GF CC   three proteins, Vp25, Vp20 and Vp24 which all have jellyroll
#=GF CC   fold and form one protomer; 60 copies of this unit compose one
#=GF CC   virion. Vp25, Vp20 and Vp24 contribute to capsid stabilization
#=GF CC   [1]. Vp24 form a pentameric protrusion around a fivefold axis,
#=GF CC   and the protrusion sits on a base of Vp25 and Vp20. Vp24 is more
#=GF CC   loosely held and is supported by Vp25 nd Vp20 [1].
#=GF SQ   1
#=GS POL2_CRLVP/768-960  AC Q6EWG8.1
POL2_CRLVP/768-960             GPDPFSFHLFYLHCGTLKTESLNKGGMWCVPVSPINLAAMKHgTGSSLVFNESFVSKTHNWLHYMASCTAYWRGTLTYELRVTYNSRVNAVANLVAFYTSQVEDLFGFSDKAVGDTGIASICGDAFSVRISIPFVTPTLWLRTYRNAYDVFTSCNGSLYFHLPTSGVKSVQLFVRAESDFSFERFRALKAEYT
#=GC seq_cons                  GPDPFSFHLFYLHCGTLKTESLNKGGMWCVPVSPINLAAMKHGTGSSLVFNESFVSKTHNWLHYMASCTAYWRGTLTYELRVTYNSRVNAVANLVAFYTSQVEDLFGFSDKAVGDTGIASICGDAFSVRISIPFVTPTLWLRTYRNAYDVFTSCNGSLYFHLPTSGVKSVQLFVRAESDFSFERFRALKAEYT
//