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Database: Pfam
Entry: Peptidase_S29
LinkDB: Peptidase_S29
Original site: Peptidase_S29 
#=GF ID   Peptidase_S29
#=GF AC   PF02907.13
#=GF DE   Hepatitis C virus NS3 protease
#=GF PI   HCV_NS3; 
#=GF AU   Griffiths-Jones SR, Knutson S
#=GF SE   Structural domain
#=GF GA   20.50 20.50;
#=GF TC   20.50 20.50;
#=GF NC   20.40 20.40;
#=GF BM   hmmbuild HMM.ann SEED.ann
#=GF SM   hmmsearch -Z 17690987 -E 1000 --cpu 4 HMM pfamseq
#=GF TP   Domain
#=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 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   4
#=GS A0A0E0MPM7_ORYPU/6-63  AC A0A0E0MPM7.1
#=GS POLG_HCVH/1056-1204    AC P27958.3
#=GS POLG_HCVH/1056-1204    DR PDB; 2OC8 A; 30-178;
#=GS POLG_HCVH/1056-1204    DR PDB; 2XNI B; 30-178;
#=GS POLG_HCVH/1056-1204    DR PDB; 2F9V C; 30-178;
#=GS POLG_HCVH/1056-1204    DR PDB; 2OC8 C; 30-178;
#=GS POLG_HCVH/1056-1204    DR PDB; 2OBQ C; 30-178;
#=GS POLG_HCVH/1056-1204    DR PDB; 2OC0 A; 30-178;
#=GS POLG_HCVH/1056-1204    DR PDB; 2OC1 C; 30-178;
#=GS POLG_HCVH/1056-1204    DR PDB; 2XNI A; 30-178;
#=GS POLG_HCVH/1056-1204    DR PDB; 1A1R B; 56-204;
#=GS POLG_HCVH/1056-1204    DR PDB; 2F9V A; 30-178;
#=GS POLG_HCVH/1056-1204    DR PDB; 2O8M A; 30-178;
#=GS POLG_HCVH/1056-1204    DR PDB; 2OC7 A; 30-178;
#=GS POLG_HCVH/1056-1204    DR PDB; 2OIN B; 1056-1204;
#=GS POLG_HCVH/1056-1204    DR PDB; 2O8M B; 30-178;
#=GS POLG_HCVH/1056-1204    DR PDB; 2OIN A; 56-204;
#=GS POLG_HCVH/1056-1204    DR PDB; 1RGQ A; 33-181;
#=GS POLG_HCVH/1056-1204    DR PDB; 2OC7 C; 30-178;
#=GS POLG_HCVH/1056-1204    DR PDB; 1N1L A; 30-178;
#=GS POLG_HCVH/1056-1204    DR PDB; 1RGQ B; 33-181;
#=GS POLG_HCVH/1056-1204    DR PDB; 2A4R A; 30-178;
#=GS POLG_HCVH/1056-1204    DR PDB; 2A4R C; 30-178;
#=GS POLG_HCVH/1056-1204    DR PDB; 1N1L B; 30-178;
#=GS POLG_HCVH/1056-1204    DR PDB; 2OC1 A; 30-178;
#=GS POLG_HCVH/1056-1204    DR PDB; 2OC0 C; 30-178;
#=GS POLG_HCVH/1056-1204    DR PDB; 2OBQ A; 30-178;
#=GS POLG_HCVH/1056-1204    DR PDB; 1A1R A; 56-204;
#=GS O41892_PEGIA/991-1138  AC O41892.1
#=GS W9R5F6_9ROSA/3-51      AC W9R5F6.1
A0A0E0MPM7_ORYPU/6-63             ........................gvkaye----------------------------------------------------------------------------------------------------LELKHNQGNSGGPLIDSYGHVIGVNTATFTRK..GTgiSSGVNFAiPIDTV---vqs..............
POLG_HCVH/1056-1204               ..............................EGEVQIVSTATQTFLATCINGVCWTVYHGAGTRTIASPKGPVIQTYTNVDQDLVGWPAPQGSRSLTPCTCGSSDLYLVTRHADVIPVRRRGDSRGSLLSPRPISYLKGSSGGPLLCPTGHAVGLFRAAVCTR..GV..AKAVDFI.PVENLET-t................
#=GR POLG_HCVH/1056-1204    SS    ..............................-CSEEEEE-SS-EEEEEEETTEEEEEHHHHTT-EEEETTSEB--SEEETTTTEEEEE--TTB--B-B-SS--SEEEEE-TTS-EEEEEEECTTEEEEEEEEEHHHHTT-TT-EEEETTSEEEEEEEEEEEET..TE..EEEEEEE.EHHHHHH-H................
#=GR POLG_HCVH/1056-1204    AS    .........................................................*.......................*.........................................................*.............................................................
O41892_PEGIA/991-1138             .............................c-GNVVVLGTSTTRSMGTCVNGVMYATYHGTNGRTMAGPMGPVNARWWSTSDDVCVYPLPMGATCLEPCKCSPQGVWVVRNDGALCHGT-LGK-TVELDLPAELCDFRGSSGSPILCDEGHAVGMLVSVLHRG..NR..VTGIRYTkPWETLPR-e................
#=GR O41892_PEGIA/991-1138  pAS   .........................................................*.......................*.........................................................*.............................................................
W9R5F6_9ROSA/3-51                 ..........................gtri-----------------------------------------------------------------------------------------------------------GNSGGPLIDSYGHVIGVNTATFTRKgtGV..SSGVNFAiPIDTV---vrt..............
#=GC SS_cons                      ..............................-CSEEEEE-SS-EEEEEEETTEEEEEHHHHTT-EEEETTSEB--SEEETTTTEEEEE--TTB--B-B-SS--SEEEEE-TTS-EEEEEEECTTEEEEEEEEEHHHHTT-TT-EEEETTSEEEEEEEEEEEET..TE..EEEEEEE.EHHHHHH-H................
#=GC seq_cons                     ..................................................................................................................................h.lp..pGsSGGPLlsshGHslGl.sAshsR+..Gs..uoGVsFshPl-Tl...s................
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