Sequence of POLG_HCVJA
EC Number:3.4.21.98
EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
Reaction
Hydrolysis of four peptide bonds in the viral precursor polyprotein, commonly with Asp or Glu in the P6 position, Cys or Thr in P1 and Ser or Ala in P1'
Other sequences found for EC No. 3.4.21.98
General information:
Sequence
0 MSTNPKPQRK TKRNTNRRPQ DVKFPGGGQI VGGVYLLPRR GPRLGVRATR KTSERSQPRG
60 RRQPIPKARR PEGRTWAQPG YPWPLYGNEG MGWAGWLLSP RGSRPSWGPT DPRRRSRNLG
120 KVIDTLTCGF ADLMGYIPLV GAPLGGAARA LAHGVRVLED GVNYATGNLP GCSFSIFLLA
180 LLSCLTIPAS AYEVRNVSGI YHVTNDCSNS SIVYEAADMI MHTPGCVPCV RESNFSRCWV
240 ALTPTLAARN SSIPTTTIRR HVDLLVGAAA LCSAMYVGDL CGSVFLVSQL FTFSPRRYET
300 VQDCNCSIYP GHVSGHRMAW DMMMNWSPTT ALVVSQLLRI PQAVVDMVAG AHWGVLAGLA
360 YYSMVGNWAK VLIVMLLFAG VDGHTHVTGG RVASSTQSLV SWLSQGPSQK IQLVNTNGSW
420 HINRTALNCN DSLQTGFIAA LFYAHRFNAS GCPERMASCR PIDEFAQGWG PITHDMPESS
480 DQRPYCWHYA PRPCGIVPAS QVCGPVYCFT PSPVVVGTTD RFGAPTYSWG ENETDVLLLS
540 NTRPPQGNWF GCTWMNSTGF TKTCGGPPCN IGGVGNNTLV CPTDCFRKHP EATYTKCGSG
600 PWLTPRCMVD YPYRLWHYPC TVNFTVFKVR MYVGGVEHRL NAACNWTRGE RCDLEDRDRS
660 ELSPLLLSTT EWQILPCSFT TLPALSTGLI HLHRNIVDVQ YLYGIGSAVV SFAIKWEYIL
720 LLFLLLADAR VCACLWMMLL IAQAEATLEN LVVLNAASVA GAHGLLSFLV FFCAAWYIKG
780 RLVPGAAYAL YGVWPLLLLL LALPPRAYAM DREMAASCGG AVFVGLVLLT LSPYYKVFLA
840 RLIWWLQYFI TRAEAHLQVW VPPLNVRGGR DAIILLTCAV HPELIFDITK LLLAILGPLM
900 VLQAGITRVP YFVRAQGLIR ACMLVRKVAG GHYVQMAFMK LAALTGTYVY DHLTPLRDWA
960 HAGLRDLAVA VEPVVFSDME TKLITWGADT AACGDIISGL PVSARRGKEI LLGPADSFGE
1020 QGWRLLAPIT AYSQQTRGLL GCIITSLTGR DKNQVDGEVQ VLSTATQSFL ATCVNGVCWT
1080 VYHGAGSKTL AGPKGPITQM YTNVDQDLVG WPAPPGARSM TPCTCGSSDL YLVTRHADVV
1140 PVRRRGDSRG SLLSPRPISY LKGSSGGPLL CPSGHVVGIF RAAVCTRGVA KAVDFIPVES
1200 METTMRSPVF TDNSSPPAVP QTFQVAHLHA PTGSGKSTKV PAAYAAQGYK VLVLNPSVAA
1260 TLGFGAYMSK AHGIEPNIRT GVRTITTGGP ITYSTYCKFL ADGGCSGGAY DIIICDECHS
1320 TDSTTILGIG TVLDQAETAG ARLVVLATAT PPGSITVPHP NIEEVALSNT GEIPFYGKAI
1380 PIEAIKGGRH LIFCHSKKKC DELAAKLTGL GLNAVAYYRG LDVSVIPTSG DVVVVATDAL
1440 MTGFTGDFDS VIDCNTCVTQ TVDFSLDPTF TIETTTLPQD AVSRAQRRGR TGRGRSGIYR
1500 FVTPGERPSG MFDSSVLCEC YDAGCAWYEL TPAETSVRLR AYLNTPGLPV CQDHLEFWES
1560 VFTGLTHIDA HFLSQTKQAG DNLPYLVAYQ ATVCARAQAP PPSWDQMWKC LIRLKPTLHG
1620 PTPLLYRLGA VQNEVTLTHP ITKYIMACMS ADLEVVTSTW VLVGGVLAAL AAYCLTTGSV
1680 VIVGRIILSG RPAVIPDREV LYQEFDEMEE CASHLPYIEQ GMQLAEQFKQ KALGLLQTAT
1740 KQAEAAAPVV ESKWRALEVF WAKHMWNFIS GIQYLAGLST LPGNPAIASL MAFTASITSP
1800 LTTQNTLLFN ILGGWVAAQL APPSAASAFV GAGIAGAAVG SIGLGKVLVD ILAGYGAGVA
1860 GALVAFKVMS GEMPSTEDLV NLLPAILSPG ALVVGVVCAA ILRRHVGPGE GAVQWMNRLI
1920 AFASRGNHVS PTHYVPESDA AARVTQILSS LTITQLLKRL HQWINEDCST PCSGSWLKDV
1980 WDWICTVLSD FKTWLQSKLL PRLPGLPFLS CQRGYKGVWR GDGIMQTTCP CGAQITGHVK
2040 NGSMRIVGPK TCSNTWHGTF PINAYTTGPC TPSPAPNYSR ALWRVAAEEY VEVTRVGDFH
2100 YVTGMTTDNV KCPCQVPAPE FFTEVDGVRL HRYAPVCKPL LREEVVFQVG LNQYLVGSQL
2160 PCEPEPDVAV LTSMLTDPSH ITAETAKRRL ARGSPPSLAS SSASQLSAPS LKATCTTHHD
2220 SPDADLIEAN LLWRQEMGGN ITRVESENKV VILDSFDPIR AVEDEREISV PAEILRKPRK
2280 FPPALPIWAR PDYNPPLLES WKDPDYVPPV VHGCPLPSTK APPIPPPRRK RTVVLTESTV
2340 SSALAELATK TFGSSGSSAV DSGTATGPPD QASDDGDKGS DVESYSSMPP LEGEPGDPDL
2400 SDGSWSTVSG EAGEDVVCCS MSYTWTGALI TPCAAEESKL PINPLSNSLL RHHSMVYSTT
2460 SRSASLRQKK VTFDRLQVLD DHYRDVLKEM KAKASTVKAR LLSIEEACKL TPPHSAKSKF
2520 GYGAKDVRSL SSRAVNHIRS VWEDLLEDTE TPIDTTIMAK NEVFCVQPEK GGRKPARLIV
2580 FPDLGVRVCE KMALYDVVST LPQAVMGPSY GFQYSPGQRV EFLVNTWKSK KCPMGFSYDT
2640 RCFDSTVTEN DIRTEESIYQ CCDLAPEARQ AIRSLTERLY VGGPLTNSKG QNCGYRRCRA
2700 SGVLTTSCGN TLTCYLKATA ACRAAKLQDC TMLVNGDDLV VICESAGTQE DAAALRAFTE
2760 AMTRYSAPPG DPPQPEYDLE LITSCSSNVS VAHDASGKRV YYLTRDPTTP LARAAWETVR
2820 HTPVNSWLGN IIMYAPTLWA RMILMTHFFS ILLAQEQLEK ALDCQIYGAC YSIEPLDLPQ
2880 IIERLHGLSA FSLHSYSPGE INRVASCLRK LGVPPLRVWR HRARSVRAKL LSQGGRAATC
2940 GKYLFNWAVK TKLKLTPIPA ASQLDLSGWF VAGYNGGDIY HSLSRARPRW FMLCLLLLSV
3000 GVGIYLLPNR
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Sequence Reference
Authors
Title
Journal
Volume
Pages
Year
PubMed ID
460651
Kato N.,Hijikata M.,Ootsuyama Y.,Nakagawa M.,Ohkoshi S.,Sugimura T.,Shimotohno K.
Molecular cloning of the human hepatitis C virus genome from Japanese patients with non-A, non-B hepatitis.
Proc. Natl. Acad. Sci. U.S.A.
87
9524-9528
1990
460652
Kato N.,Hijikata M.,Nakagawa M.,Ootsuyama Y.,Muraiso K.,Ohkoshi S.,Shimotohno K.
Molecular structure of the Japanese hepatitis C viral genome.
FEBS Lett.
280
325-328
1991
460654
Hijikata M.,Mizushima H.,Akagi T.,Mori S.,Kakiuchi N.,Kato N.,Tanaka T.,Kimura K.,Shimotohno K.
Two distinct proteinase activities required for the processing of a putative nonstructural precursor protein of hepatitis C virus.
J. Virol.
67
4665-4675
1993
460655
Hijikata M.,Kato N.,Ootsuyama Y.,Nakagawa M.,Shimotohno K.
Gene mapping of the putative structural region of the hepatitis C virus genome by in vitro processing analysis.
Proc. Natl. Acad. Sci. U.S.A.
88
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1991
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Shih C.-M.,Lo S.J.,Miyamura T.,Chen S.-Y.,Lee Y.-H.W.
Suppression of hepatitis B virus expression and replication by hepatitis C virus core protein in HuH-7 cells.
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67
5823-5832
1993
460657
Bartenschlager R.,Ahlborn-Laake L.,Mous J.,Jacobsen H.
Nonstructural protein 3 of the hepatitis C virus encodes a serine-type proteinase required for cleavage at the NS3/4 and NS4/5 junctions.
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67
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1993
460658
Kaneko T.,Tanji Y.,Satoh S.,Hijikata M.,Asabe S.,Kimura K.,Shimotohno K.
Production of two phosphoproteins from the NS5A region of the hepatitis C viral genome.
Biochem. Biophys. Res. Commun.
205
320-326
1994
460659
Tanji Y.,Kaneko T.,Satoh S.,Shimotohno K.
Phosphorylation of hepatitis C virus-encoded nonstructural protein NS5A.
J. Virol.
69
3980-3986
1995
460660
Asabe S.I.,Tanji Y.,Satoh S.,Kaneko T.,Kimura K.,Shimotohno K.
The N-terminal region of hepatitis C virus-encoded NS5A is important for NS4A-dependent phosphorylation.
J. Virol.
71
790-796
1997
460661
Kato N.,Lan K.H.,Ono-Nita S.K.,Shiratori Y.,Omata M.
Hepatitis C virus nonstructural region 5A protein is a potent transcriptional activator.
J. Virol.
71
8856-8859
1997
460662
Stempniak M.,Hostomska Z.,Nodes B.R.,Hostomsky Z.
The NS3 proteinase domain of hepatitis C virus is a zinc-containing enzyme.
J. Virol.
71
2881-2886
1997
460663
Yasui K.,Wakita T.,Tsukiyama-Kohara K.,Funahashi S.,Ichikawa M.,Kajita T.,Moradpour D.,Wands J.R.,Kohara M.
The native form and maturation process of hepatitis C virus core protein.
J. Virol.
72
6048-6055
1998
460664
Pawlotsky J.-M.,Germanidis G.,Neumann A.U.,Pellerin M.,Frainais P.-O.,Dhumeaux D.
Interferon resistance of hepatitis C virus genotype 1b: relationship to nonstructural 5A gene quasispecies mutations.
J. Virol.
72
2795-2805
1998
460665
Satoh S.,Hirota M.,Noguchi T.,Hijikata M.,Handa H.,Shimotohno K.
Cleavage of hepatitis C virus nonstructural protein 5A by a caspase-like protease(s) in mammalian cells.
Virology
270
476-487
2000
460666
McLauchlan J.
Properties of the hepatitis C virus core protein: a structural protein that modulates cellular processes.
J. Viral Hepat.
7
2-14
2000
460667
Wang Q.M.,Hockman M.A.,Staschke K.,Johnson R.B.,Case K.A.,Lu J.,Parsons S.,Zhang F.,Rathnachalam R.,Kirkegaard K.,Colacino J.M.
Oligomerization and cooperative RNA synthesis activity of hepatitis C virus RNA-dependent RNA polymerase.
J. Virol.
76
3865-3872
2002
460668
Watashi K.,Hijikata M.,Tagawa A.,Doi T.,Marusawa H.,Shimotohno K.
Modulation of retinoid signaling by a cytoplasmic viral protein via sequestration of Sp110b, a potent transcriptional corepressor of retinoic acid receptor, from the nucleus.
Mol. Cell. Biol.
23
7498-7509
2003
460669
Okamoto K.,Moriishi K.,Miyamura T.,Matsuura Y.
Intramembrane proteolysis and endoplasmic reticulum retention of hepatitis C virus core protein.
J. Virol.
78
6370-6380
2004
460670
Penin F.,Dubuisson J.,Rey F.A.,Moradpour D.,Pawlotsky J.-M.
Structural biology of hepatitis C virus.
Hepatology
39
5-19
2004
460671
Boni S.,Lavergne J.-P.,Boulant S.,Cahour A.
Hepatitis C virus core protein acts as a trans-modulating factor on internal translation initiation of the viral RNA.
J. Biol. Chem.
280
17737-17748
2005
460672
Lin W.,Choe W.H.,Hiasa Y.,Kamegaya Y.,Blackard J.T.,Schmidt E.V.,Chung R.T.
Hepatitis C virus expression suppresses interferon signaling by degrading STAT1.
Gastroenterology
128
1034-1041
2005
460673
Suzuki R.,Sakamoto S.,Tsutsumi T.,Rikimaru A.,Tanaka K.,Shimoike T.,Moriishi K.,Iwasaki T.,Mizumoto K.,Matsuura Y.,Miyamura T.,Suzuki T.
Molecular determinants for subcellular localization of hepatitis C virus core protein.
J. Virol.
79
1271-1281
2005
460674
Huang L.,Hwang J.,Sharma S.D.,Hargittai M.R.,Chen Y.,Arnold J.J.,Raney K.D.,Cameron C.E.
Hepatitis C virus nonstructural protein 5A (NS5A) is an RNA-binding protein.
J. Biol. Chem.
280
36417-36428
2005
460675
Hamamoto I.,Nishimura Y.,Okamoto T.,Aizaki H.,Liu M.,Mori Y.,Abe T.,Suzuki T.,Lai M.M.,Miyamura T.,Moriishi K.,Matsuura Y.
Human VAP-B is involved in hepatitis C virus replication through interaction with NS5A and NS5B.
J. Virol.
79
13473-13482
2005
460676
Kalamvoki M.,Georgopoulou U.,Mavromara P.
The NS5A protein of the hepatitis C virus genotype 1a is cleaved by caspases to produce C-terminal-truncated forms of the protein that reside mainly in the cytosol.
J. Biol. Chem.
281
13449-13462
2006
460677
Lin W.,Kim S.S.,Yeung E.,Kamegaya Y.,Blackard J.T.,Kim K.A.,Holtzman M.J.,Chung R.T.
Hepatitis C virus core protein blocks interferon signaling by interaction with the STAT1 SH2 domain.
J. Virol.
80
9226-9235
2006
460678
Wang J.,Tong W.,Zhang X.,Chen L.,Yi Z.,Pan T.,Hu Y.,Xiang L.,Yuan Z.
Hepatitis C virus non-structural protein NS5A interacts with FKBP38 and inhibits apoptosis in Huh7 hepatoma cells.
FEBS Lett.
580
4392-4400
2006
460679
Yan X.B.,Battaglia S.,Boucreux D.,Chen Z.,Brechot C.,Pavio N.
Mapping of the interacting domains of hepatitis C virus core protein and the double-stranded RNA-activated protein kinase PKR.
Virus Res.
125
79-87
2007
460680
Veillon P.,Payan C.,Le Guillou-Guillemette H.,Gaudy C.,Lunel F.
Quasispecies evolution in NS5A region of hepatitis C virus genotype 1b during interferon or combined interferon-ribavirin therapy.
World J. Gastroenterol.
13
1195-1203
2007
460681
Huang Z.S.,Wang C.C.,Wu H.N.
HCV NS3 protein helicase domain assists RNA structure conversion.
FEBS Lett.
584
2356-2362
2010
460682
Braeutigam J.,Scheidig A.J.,Egge-Jacobsen W.
Mass spectrometric analysis of hepatitis C viral envelope protein E2 reveals extended microheterogeneity of mucin-type O-linked glycosylation.
Glycobiology
23
453-474
2013
460683
Salloum S.,Wang H.,Ferguson C.,Parton R.G.,Tai A.W.
Rab18 binds to hepatitis C virus NS5A and promotes interaction between sites of viral replication and lipid droplets.
PLoS Pathog.
9
0-0
2013
460684
Maqbool M.A.,Imache M.R.,Higgs M.R.,Carmouse S.,Pawlotsky J.M.,Lerat H.
Regulation of hepatitis C virus replication by nuclear translocation of nonstructural 5A protein and transcriptional activation of host genes.
J. Virol.
87
5523-5539
2013
460685
Han S.H.,Kim S.J.,Kim E.J.,Kim T.E.,Moon J.S.,Kim G.W.,Lee S.H.,Cho K.,Yoo J.S.,Son W.S.,Rhee J.K.,Han S.H.,Oh J.W.
Phosphorylation of hepatitis C virus RNA polymerases ser29 and ser42 by protein kinase C-related kinase 2 regulates viral RNA replication.
J. Virol.
88
11240-11252
2014
460686
Kandangwa M.,Liu Q.
HCV NS5A hyperphosphorylation is involved in viral translation modulation.
Biochem. Biophys. Res. Commun.
520
192-197
2019
460687
Di Marco S.,Rizzi M.,Volpari C.,Walsh M.A.,Narjes F.,Colarusso S.,De Francesco R.,Matassa V.G.,Sollazzo M.
Inhibition of the hepatitis C virus NS3/4A protease. The crystal structures of two protease-inhibitor complexes.
J. Biol. Chem.
275
7152-7157
2000
460688
Ontoria J.M.,Di Marco S.,Conte I.,Di Francesco M.E.,Gardelli C.,Koch U.,Matassa V.G.,Poma M.,Steinkuehler C.,Volpari C.,Harper S.
The design and enzyme-bound crystal structure of indoline based peptidomimetic inhibitors of hepatitis C virus NS3 protease.
J. Med. Chem.
47
6443-6446
2004
460689
Montserret R.,Saint N.,Vanbelle C.,Salvay A.G.,Simorre J.P.,Ebel C.,Sapay N.,Renisio J.G.,Bockmann A.,Steinmann E.,Pietschmann T.,Dubuisson J.,Chipot C.,Penin F.
NMR structure and ion channel activity of the p7 protein from hepatitis C virus.
J. Biol. Chem.
285
31446-31461
2010
460690
Lemke C.T.,Goudreau N.,Zhao S.,Hucke O.,Thibeault D.,Llinas-Brunet M.,White P.W.
Combined X-ray, NMR, and kinetic analyses reveal uncommon binding characteristics of the hepatitis C virus NS3-NS4A protease inhibitor BI 201335.
J. Biol. Chem.
286
11434-11443
2011
460691
Hagel M.,Niu D.,St Martin T.,Sheets M.P.,Qiao L.,Bernard H.,Karp R.M.,Zhu Z.,Labenski M.T.,Chaturvedi P.,Nacht M.,Westlin W.F.,Petter R.C.,Singh J.
Selective irreversible inhibition of a protease by targeting a noncatalytic cysteine.
Nat. Chem. Biol.
7
22-24
2011
460692
Kugler J.,Schmelz S.,Gentzsch J.,Haid S.,Pollmann E.,van den Heuvel J.,Franke R.,Pietschmann T.,Heinz D.W.,Collins J.
High affinity peptide inhibitors of the hepatitis C virus NS3-4A protease refractory to common resistant mutants.
J. Biol. Chem.
287
39224-39232
2012
460693
O'Meara J.A.,Lemke C.T.,Godbout C.,Kukolj G.,Lagace L.,Moreau B.,Thibeault D.,White P.W.,Llinas-Brunet M.
Molecular mechanism by which a potent hepatitis C virus NS3-NS4A protease inhibitor overcomes emergence of resistance.
J. Biol. Chem.
288
5673-5681
2013
460695
Jiang Y.,Andrews S.W.,Condroski K.R.,Buckman B.,Serebryany V.,Wenglowsky S.,Kennedy A.L.,Madduru M.R.,Wang B.,Lyon M.,Doherty G.A.,Woodard B.T.,Lemieux C.,Geck Do M.,Zhang H.,Ballard J.,Vigers G.,Brandhuber B.J.,Stengel P.,Josey J.A.,Beigelman L.,Blatt L.,Seiwert S.D.
Discovery of danoprevir (ITMN-191/R7227), a highly selective and potent inhibitor of hepatitis C virus (HCV) NS3/4A protease.
J. Med. Chem.
57
1753-1769
2014
