#=GF ID   PsV_CP_C
#=GF AC   PF22408.2
#=GF DE   PsV, capsid protein, C-terminal domain
#=GF AU   Bateman A;0000-0002-6982-4660
#=GF AU   Lazaro Pinto Beatriz;0000-0001-6837-2941
#=GF SE   ECOD:EF19431
#=GF GA   27.00 27.00;
#=GF TC   27.10 50.40;
#=GF NC   25.60 19.40;
#=GF BM   hmmbuild  HMM.ann SEED.ann
#=GF SM   hmmsearch -E 1000 --cpu 8 -Z 90746521 HMM pfamseq
#=GF TP   Domain
#=GF RC   Paper describing PDB structure 3es5
#=GF RN   [1]
#=GF RM   19246376
#=GF RT   Atomic structure reveals the unique capsid organization of a
#=GF RT   dsRNA virus.
#=GF RA   Pan J, Dong L, Lin L, Ochoa WF, Sinkovits RS, Havens WM, Nibert
#=GF RA   ML, Baker TS, Ghabrial SA, Tao YJ;
#=GF RL   Proc Natl Acad Sci U S A. 2009;106:4225-4230.
#=GF DR   INTERPRO; IPR055062;
#=GF DR   SO; 0000417; polypeptide_domain;
#=GF CC   This domain is found at the C-terminal end of the putative
#=GF CC   capsid protein from Penicillium stoloniferum virus F (CP,
#=GF CC   Swiss:Q4G3H1). This protein has a disordered N-terminal end that
#=GF CC   interacts with the dsRNA genome and probably participates in its
#=GF CC   packaging or transcription, and a C-terminal domain (this entry)
#=GF CC   that shows a helix-loop-helix motif involved in the formation
#=GF CC   flexible channels thought to be involved in RNA synthesis
#=GF CC   activity [1].
#=GF SQ   4
#=GS Q4G3H1_9VIRU/335-385      AC Q4G3H1.1
#=GS A0A2Z5ZAM9_9VIRU/341-391  AC A0A2Z5ZAM9.1
#=GS A0A2V3J613_9FLOR/323-372  AC A0A2V3J613.1
#=GS A0A0B1NYZ1_UNCNE/2-53     AC A0A0B1NYZ1.1
Q4G3H1_9VIRU/335-385                 .WRVESIFKVGPPPAGTTGYGAQTVSS-TGNTARWQFPLSDADINIGYLFSPS
A0A2Z5ZAM9_9VIRU/341-391             .IHIQTVFHLGEPPATERGFASQLVASDDV-TARFGLPLSDADKALGFMFNPR
A0A2V3J613_9FLOR/323-372             l--VEEAFEVAEPVATGFGNACQTVSSDDL-QATFALPLSDQDISMGFMYNPA
A0A0B1NYZ1_UNCNE/2-53                .WRIESTFKVGPPPAGNTGYGAQTVQSHETNLARWQFPSSDADVSIGFLFSPA
#=GC seq_cons                        .h+lEosF+VG.PPAsspGauuQTVuSc-s.pARathPLSDADlulGFhFsPu
//