#=GF ID HCV_NS5a_1a
#=GF AC PF08300.17
#=GF DE Hepatitis C virus non-structural 5a zinc finger domain
#=GF AU Paterson M;
#=GF AU Bateman A;0000-0002-6982-4660
#=GF SE Bateman A
#=GF GA 25.00 25.00;
#=GF TC 25.50 96.70;
#=GF NC 24.90 22.50;
#=GF BM hmmbuild HMM.ann SEED.ann
#=GF SM hmmsearch -E 1000 --cpu 4 -Z 75585367 HMM pfamseq
#=GF TP Domain
#=GF RN [1]
#=GF RM 9710605
#=GF RT Control of PKR protein kinase by hepatitis C virus nonstructural
#=GF RT 5A protein: molecular mechanisms of kinase regulation.
#=GF RA Gale M Jr, Blakely CM, Kwieciszewski B, Tan SL, Dossett M, Tang
#=GF RA NM, Korth MJ, Polyak SJ, Gretch DR, Katze MG;
#=GF RL Mol Cell Biol 1998;18:5208-5218.
#=GF RN [2]
#=GF RM 9143277
#=GF RT Evidence that hepatitis C virus resistance to interferon is
#=GF RT mediated through repression of the PKR protein kinase by the
#=GF RT nonstructural 5A protein.
#=GF RA Gale MJ Jr, Korth MJ, Tang NM, Tan SL, Hopkins DA, Dever TE,
#=GF RA Polyak SJ, Gretch DR, Katze MG;
#=GF RL Virology 1997;230:217-227.
#=GF RN [3]
#=GF RM 15902263
#=GF RT Structure of the zinc-binding domain of an essential component
#=GF RT of the hepatitis C virus replicase.
#=GF RA Tellinghuisen TL, Marcotrigiano J, Rice CM;
#=GF RL Nature 2005;435:374-379.
#=GF DR INTERPRO; IPR013192;
#=GF DR SO; 0000417; polypeptide_domain;
#=GF CC The molecular function of the non-structural 5a protein is
#=GF CC uncertain. The NS5a protein is phosphorylated when expressed in
#=GF CC mammalian cells. It is thought to interact with the ds RNA
#=GF CC dependent (interferon inducible) kinase PKR, Swiss:P19525 [1,2].
#=GF CC This domain corresponds to the N-terminal zinc binding domain
#=GF CC [3].
#=GF SQ 2
#=GS POLG_HCV77/2006-2067 AC P27958.3
#=GS O41892_PEGIA/1972-2025 AC O41892.1
POLG_HCV77/2006-2067 IPFVSCQRGYRGVWRGDGIMHTRCHCGAEITGHVKNGTMRIVGPRTCKNMWSGTFFINAYTT..
O41892_PEGIA/1972-2025 IPLMGCSKGWAGPWEGNGHVEARCTCGCVITGEIYDGELH--------DMVYSTFFCSHY--lr
#=GC seq_cons IPhhuCp+GatGsWcGsGhhcsRCpCGs.ITGclhsGph+........sMh.uTFFhstY....
//