#=GF ID Peptidase_S29
#=GF AC PF02907.19
#=GF DE Hepatitis C virus NS3 protease
#=GF PI HCV_NS3;
#=GF AU Griffiths-Jones SR;0000-0001-6043-807X
#=GF AU Knutson S;
#=GF SE Structural domain
#=GF GA 25.00 25.00;
#=GF TC 25.00 25.10;
#=GF NC 24.90 24.80;
#=GF BM hmmbuild HMM.ann SEED.ann
#=GF SM hmmsearch -Z 75585367 -E 1000 --cpu 4 HMM pfamseq
#=GF TP Domain
#=GF CL CL0124
#=GF RN [1]
#=GF RM 9568891
#=GF RT Complex of NS3 protease and NS4A peptide of BK strain hepatitis
#=GF RT C virus: a 2.2 A resolution structure in a hexagonal crystal
#=GF RT form.
#=GF RA Yan Y, Li Y, Munshi S, Sardana V, Cole JL, Sardana M,
#=GF RA Steinkuehler C, Tomei L, De Francesco R, Kuo LC, Chen Z;
#=GF RL Protein Sci 1998;7:837-847.
#=GF RN [2]
#=GF RM 8861916
#=GF RT The crystal structure of hepatitis C virus NS3 proteinase
#=GF RT reveals a trypsin-like fold and a structural zinc binding site.
#=GF RA Love RA, Parge HE, Wickersham JA, Hostomsky Z, Habuka N, Moomaw
#=GF RA EW, Adachi T, Hostomska Z;
#=GF RL Cell 1996;87:331-342.
#=GF RN [3]
#=GF RM 9083052
#=GF RT Substrate specificity of the hepatitis C virus serine protease
#=GF RT NS3.
#=GF RA Urbani A, Bianchi E, Narjes F, Tramontano A, De Francesco R,
#=GF RA Steinkuhler C, Pessi A;
#=GF RL J Biol Chem 1997;272:9204-9209.
#=GF DR INTERPRO; IPR004109;
#=GF DR SCOP; 1a1r; fa;
#=GF DR MEROPS; S29;
#=GF DR SO; 0000417; polypeptide_domain;
#=GF CC Hepatitis C virus NS3 protein is a serine protease which has a
#=GF CC trypsin-like fold. The non-structural (NS) protein NS3 is one
#=GF CC of the NS proteins involved in replication of the HCV genome.
#=GF CC NS2-3 proteinase, a zinc-dependent enzyme, performs a single
#=GF CC proteolytic cut to release the N-terminus of NS3. The action of
#=GF CC NS3 proteinase (NS3P), which resides in the N-terminal one-third
#=GF CC of the NS3 protein, then yields all remaining non-structural
#=GF CC proteins. The C-terminal two-thirds of the NS3 protein contain
#=GF CC a helicase. The functional relationship between the proteinase
#=GF CC and helicase domains is unknown. NS3 has a structural
#=GF CC zinc-binding site and requires cofactor NS4A.
#=GF SQ 2
#=GS O41892_PEGIA/991-1138 AC O41892.1
#=GS POLG_HCV77/1056-1204 AC P27958.3
O41892_PEGIA/991-1138 ......c-GNVVVLGTSTTRSMGTCVNGVMYATYHGTNGR..TMAGP.MGPVNARWWSTSDDVCVYPLPMGATCLEPCKCSPQGVWVVRNDGALCHGT-LGK-TVELDLPAELCDFRGSSGSPILCDEGHAVGMLVSVLHRGNRVTGIRYTkPWETLPR-e..
#=GR O41892_PEGIA/991-1138 pAS ..................................*..........................*.........................................................*...........................................
POLG_HCV77/1056-1204 .......EGEVQIVSTATQTFLATCINGVCWTVYHGAGTR..TIASP.KGPVIQTYTNVDQDLVGWPAPQGSRSLTPCTCGSSDLYLVTRHADVIPVRRRGDSRGSLLSPRPISYLKGSSGGPLLCPTGHAVGLFRAAVCTRGVAKAVDFI.PVENLET-t..
#=GR POLG_HCV77/1056-1204 AS ..................................*..........................*.........................................................*...........................................
#=GC seq_cons ........GpV.lluTuTpp.huTClNGVhassYHGsssR..ThAuP.hGPV.tpahssspDlssaPhP.GupsLpPCpCuspslalVppcuslh.sp.hGc.pspL..Pt.ls.h+GSSGuPlLCspGHAVGhhhuslpptshspulcah.PhEsL.p.p..
//
