#=GF ID   PM2_P3
#=GF AC   PF20812.1
#=GF DE   Bacteriophage PM2, Viral membrane protein P3
#=GF AU   Lazaro Pinto Beatriz;0000-0001-6837-2941
#=GF AU   Bateman A;0000-0002-6982-4660
#=GF SE   ECOD:3506.1.1
#=GF GA   27.00 27.00;
#=GF TC   34.20 36.80;
#=GF NC   25.30 19.90;
#=GF BM   hmmbuild HMM.ann SEED.ann
#=GF SM   hmmsearch --cpu 4 -Z 75585367 -E 1000 HMM pfamseq
#=GF TP   Domain
#=GF RC   Paper describing PDB structure 2w0c
#=GF RN   [1]
#=GF RM   18775333
#=GF RT   Insights into virus evolution and membrane biogenesis from the
#=GF RT   structure of the marine lipid-containing bacteriophage PM2.
#=GF RA   Abrescia NG, Grimes JM, Kivela HM, Assenberg R, Sutton GC,
#=GF RA   Butcher SJ, Bamford JK, Bamford DH, Stuart DI;
#=GF RL   Mol Cell. 2008;31:749-761.
#=GF DR   SO; 0000417; polypeptide_domain;
#=GF CC   Viral membrane protein P3 assemblies into dimers. Each P3
#=GF CC   subunit comprise a core of two perpendicular alpha    helices,
#=GF CC   and subunits are bound together by a parallel two-stranded beta
#=GF CC   sheet. 120 asymmetric dimers form a layer below the outer capsid
#=GF CC   shell in an almost planar structure. This protein family is
#=GF CC   found in Bacteriophage PM2 and similar PRD1-adenovirus [1].
#=GF SQ   2
#=GS P3_BPPM2/7-67           AC Q9XJR6.1
#=GS A0A7X0NG63_9GAMM/10-72  AC A0A7X0NG63.1
P3_BPPM2/7-67                      ............TSVPTNQSVWGNVSTGLDALISGWARVEQIKAAKASTGQGRVEQAMTPELDNGAAVVVEAP..
A0A7X0NG63_9GAMM/10-72             pvatqnsgsgwl----------DTINTGLSNALDLWGRVEQIKAQKSSQGGDLTQAKLTSELTNGSATVLD--sd
#=GC seq_cons                      ......................sslsTGLsshlshWuRVEQIKAtKuSpGtshsptthTsELsNGuAsVl-....
//