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Genome polyprotein

 E7ELX2_9HEPC            Unreviewed;      3012 AA.
E7ELX2;
08-MAR-2011, integrated into UniProtKB/TrEMBL.
08-MAR-2011, sequence version 1.
30-AUG-2017, entry version 44.
SubName: Full=Polyprotein {ECO:0000313|EMBL:ADV40005.1};
Recombinant Hepatitis C virus J6/JFH1(ED43-NS5A).
Viruses; ssRNA viruses; ssRNA positive-strand viruses, no DNA stage;
Flaviviridae; Hepacivirus.
NCBI_TaxID=945062 {ECO:0000313|EMBL:ADV40005.1, ECO:0000313|Proteomes:UP000129440};
[1] {ECO:0000313|EMBL:ADV40005.1, ECO:0000313|Proteomes:UP000129440}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=J6/JFH1 {ECO:0000313|EMBL:ADV40005.1};
PubMed=21111742; DOI=10.1053/j.gastro.2010.11.036;
Scheel T.K., Gottwein J.M., Mikkelsen L.S., Jensen T.B., Bukh J.;
"Recombinant HCV variants with NS5A from genotypes 1-7 have different
sensitivities to an NS5A inhibitor but not interferon-alpha.";
Gastroenterology 140:1032-1042(2011).
-!- CATALYTIC ACTIVITY: ATP + H(2)O = ADP + phosphate.
{ECO:0000256|SAAS:SAAS00368577}.
-!- CATALYTIC ACTIVITY: NTP + H(2)O = NDP + phosphate.
{ECO:0000256|SAAS:SAAS00368620}.
-!- CATALYTIC ACTIVITY: Nucleoside triphosphate + RNA(n) = diphosphate
+ RNA(n+1). {ECO:0000256|SAAS:SAAS00383097}.
-!- SUBCELLULAR LOCATION: Virion {ECO:0000256|SAAS:SAAS00560857}.
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EMBL; HQ852463; ADV40005.1; -; Other_RNA.
ProteinModelPortal; E7ELX2; -.
Proteomes; UP000129440; Genome.
GO; GO:0033644; C:host cell membrane; IEA:UniProtKB-KW.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0019028; C:viral capsid; IEA:UniProtKB-KW.
GO; GO:0019031; C:viral envelope; IEA:InterPro.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0008026; F:ATP-dependent helicase activity; IEA:InterPro.
GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:InterPro.
GO; GO:0003723; F:RNA binding; IEA:InterPro.
GO; GO:0003968; F:RNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-KW.
GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0039520; P:induction by virus of host autophagy; IEA:UniProtKB-KW.
GO; GO:0019087; P:transformation of host cell by virus; IEA:InterPro.
GO; GO:0046718; P:viral entry into host cell; IEA:UniProtKB-KW.
GO; GO:0039694; P:viral RNA genome replication; IEA:InterPro.
GO; GO:0019062; P:virion attachment to host cell; IEA:UniProtKB-KW.
InterPro; IPR011492; DEAD_Flavivir.
InterPro; IPR002521; HCV_core_C.
InterPro; IPR002522; HCV_core_N.
InterPro; IPR002519; HCV_env.
InterPro; IPR002531; HCV_NS1.
InterPro; IPR002518; HCV_NS2.
InterPro; IPR000745; HCV_NS4a.
InterPro; IPR001490; HCV_NS4b.
InterPro; IPR002868; HCV_NS5a.
InterPro; IPR013193; HCV_NS5a_1B_dom.
InterPro; IPR024350; HCV_NS5a_C.
InterPro; IPR014001; Helicase_ATP-bd.
InterPro; IPR001650; Helicase_C.
InterPro; IPR013192; NS5A_1a.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR009003; Peptidase_S1_PA.
InterPro; IPR004109; Peptidase_S29.
InterPro; IPR007094; RNA-dir_pol_PSvirus.
InterPro; IPR002166; RNA_pol_HCV.
Pfam; PF07652; Flavi_DEAD; 1.
Pfam; PF01543; HCV_capsid; 1.
Pfam; PF01542; HCV_core; 1.
Pfam; PF01539; HCV_env; 1.
Pfam; PF01560; HCV_NS1; 1.
Pfam; PF01538; HCV_NS2; 1.
Pfam; PF01006; HCV_NS4a; 1.
Pfam; PF01001; HCV_NS4b; 1.
Pfam; PF01506; HCV_NS5a; 1.
Pfam; PF08300; HCV_NS5a_1a; 1.
Pfam; PF08301; HCV_NS5a_1b; 1.
Pfam; PF12941; HCV_NS5a_C; 1.
Pfam; PF02907; Peptidase_S29; 1.
Pfam; PF00998; RdRP_3; 1.
ProDom; PD001388; HCV_env; 1.
SMART; SM00487; DEXDc; 1.
SUPFAM; SSF50494; SSF50494; 1.
SUPFAM; SSF52540; SSF52540; 2.
PROSITE; PS51693; HCV_NS2_PRO; 1.
PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
PROSITE; PS51194; HELICASE_CTER; 1.
PROSITE; PS50507; RDRP_SSRNA_POS; 1.
4: Predicted;
Activation of host autophagy by virus {ECO:0000256|SAAS:SAAS00445756};
ATP-binding {ECO:0000256|SAAS:SAAS00058020};
Capsid protein {ECO:0000256|SAAS:SAAS00057850};
Complete proteome {ECO:0000313|Proteomes:UP000129440};
Helicase {ECO:0000256|SAAS:SAAS00058020};
Host membrane {ECO:0000256|SAAS:SAAS00445977};
Host-virus interaction {ECO:0000256|SAAS:SAAS00445756,
ECO:0000256|SAAS:SAAS00445995};
Hydrolase {ECO:0000256|PROSITE-ProRule:PRU01030,
ECO:0000256|SAAS:SAAS00058020};
Membrane {ECO:0000256|SAAS:SAAS00445939,
ECO:0000256|SAAS:SAAS00445977, ECO:0000256|SAM:Phobius};
Nucleotide-binding {ECO:0000256|SAAS:SAAS00058020};
Nucleotidyltransferase {ECO:0000256|SAAS:SAAS00510600};
Protease {ECO:0000256|PROSITE-ProRule:PRU01030};
RNA-directed RNA polymerase {ECO:0000256|SAAS:SAAS00510600};
Thiol protease {ECO:0000256|PROSITE-ProRule:PRU01030};
Transferase {ECO:0000256|SAAS:SAAS00510600};
Transmembrane {ECO:0000256|SAAS:SAAS00445939,
ECO:0000256|SAM:Phobius};
Transmembrane helix {ECO:0000256|SAAS:SAAS00445939,
ECO:0000256|SAM:Phobius};
Viral attachment to host cell {ECO:0000256|SAAS:SAAS00445995};
Viral RNA replication {ECO:0000256|SAAS:SAAS00664279};
Virion {ECO:0000256|SAAS:SAAS00057850, ECO:0000256|SAAS:SAAS00445995};
Virus entry into host cell {ECO:0000256|SAAS:SAAS00445995}.
TRANSMEM 722 745 Helical. {ECO:0000256|SAM:Phobius}.
TRANSMEM 757 782 Helical. {ECO:0000256|SAM:Phobius}.
TRANSMEM 788 807 Helical. {ECO:0000256|SAM:Phobius}.
TRANSMEM 819 840 Helical. {ECO:0000256|SAM:Phobius}.
TRANSMEM 877 897 Helical. {ECO:0000256|SAM:Phobius}.
TRANSMEM 1664 1687 Helical. {ECO:0000256|SAM:Phobius}.
TRANSMEM 1828 1849 Helical. {ECO:0000256|SAM:Phobius}.
TRANSMEM 1855 1874 Helical. {ECO:0000256|SAM:Phobius}.
TRANSMEM 1886 1906 Helical. {ECO:0000256|SAM:Phobius}.
TRANSMEM 2993 3011 Helical. {ECO:0000256|SAM:Phobius}.
DOMAIN 907 1030 Peptidase C18.
{ECO:0000259|PROSITE:PS51693}.
DOMAIN 1221 1373 Helicase ATP-binding.
{ECO:0000259|PROSITE:PS51192}.
DOMAIN 1365 1542 Helicase C-terminal.
{ECO:0000259|PROSITE:PS51194}.
DOMAIN 2635 2753 RdRp catalytic.
{ECO:0000259|PROSITE:PS50507}.
ACT_SITE 956 956 For protease NS2-3 activity; shared with
dimeric partner. {ECO:0000256|PROSITE-
ProRule:PRU01030}.
ACT_SITE 976 976 For protease NS2-3 activity; shared with
dimeric partner. {ECO:0000256|PROSITE-
ProRule:PRU01030}.
ACT_SITE 997 997 For protease NS2-3 activity; shared with
dimeric partner. {ECO:0000256|PROSITE-
ProRule:PRU01030}.
SITE 1030 1031 Cleavage; by protease NS2-3.
{ECO:0000256|PROSITE-ProRule:PRU01030}.
SEQUENCE 3012 AA; 327576 MW; 74BB1F71D4A2AAF7 CRC64;
MSTNPKPQRK TKRNTNRRPQ DVKFPGGGQI VGGVYLLPRR GPRLGVRATR KTSERSQPRG
RRQPIPKDRR STGKSWGKPG YPWPLYGNEG LGWAGWLLSP RGSRPSWGPN DPRHRSRNVG
KVIDTLTCGF ADLMGYIPVV GAPLGGVARA LAHGVRVLED GVNFATGNLP GCSFSIFLLA
LLSCITTPVS AAEVKNISTG YMVTNDCTND SITWQLQAAV LHVPGCVPCE KVGNASQCWI
PVSPNVAVQR PGALTQGLRT HIDMVVMSAT LCSALYVGDL CGGVMLAAQM FIVSPQHHWF
VQDCNCSIYP GTITGHRMAW DMMMNWSPTA TMILAYAMRV PEVIIDIISG AHWGVMFGLA
YFSMQGAWAK VVVILLLAAG VDARTHTVGG SAAQTTGRLT SLFDMGPRQK IQLVNTNGSW
HINRTALNCN DSLHTGFIAS LFYTHSFNSS GCPERMSACR SIEAFRVGWG ALQYEDNVTN
PEDMRPYCWH YPPRQCGVVS AKTVCGPVYC FTPSPVVVGT TDRLGAPTYT WGENETDVFL
LNSTRPPLGS WFGCTWMNSS GYTKTCGAPP CRTRADFNAS TDLLCPTDCF RKHPDTTYLK
CGSGPWLTPR CLIDYPYRLW HYPCTVNYTI FKIRMYVGGV EHRLTAACNF TRGDRCNLED
RDRSQLSPLL HSTTEWAILP CSYSDLPALS TGLLHLHQNI VDVQFMYGLS PALTKYIVRW
EWVILLFLLL ADARVCACLW MLILLGQAEA ALEKLVILHA ASAASCNGFL YFVIFFVAAW
YIKGRVVPLA TYSLTGLWSF SLLLLALPQQ AYAYDASVHG QIGAALLVMI TLFTLTPGYK
TLLSRFLWWL CYLLTLGEAM VQEWAPPMQV RGGRDGIIWA VAIFYPGVVF DITKWLLAVL
GPAYLLKGAL TRVPYFVRAH ALLRMCTMAR HLAGGRYVQM ALLALGRWTG TYIYDHLTPM
SDWAASGLRD LAVAVEPIIF SPMEKKVIVW GAETAACGDI LHGLPVSARL GREVLLGPAD
GYTSKGWSLL APITAYAQQT RGLLGAIVVS MTGRDRTEQA GEVQILSTVS QSFLGTTISG
VLWTVYHGAG NKTLAGLRGP VTQMYSSAEG DLVGWPSPPG TKSLEPCKCG AVDLYLVTRN
ADVIPARRRG DKRGALLSPR PISTLKGSSG GPVLCPRGHV VGLFRAAVCS RGVAKSIDFI
PVETLDVVTR SPTFSDNSTP PAVPQTYQVG YLHAPTGSGK STKVPVAYAA QGYKVLVLNP
SVAATLGFGA YLSKAHGINP NIRTGVRTVM TGEAITYSTY GKFLADGGCA SGAYDIIICD
ECHAVDATSI LGIGTVLDQA ETAGVRLTVL ATATPPGSVT TPHPDIEEVG LGREGEIPFY
GRAIPLSCIK GGRHLIFCHS KKKCDELAAA LRGMGLNAVA YYRGLDVSII PAQGDVVVVA
TDALMTGYTG DFDSVIDCNV AVTQAVDFSL DPTFTITTQT VPQDAVSRSQ RRGRTGRGRQ
GTYRYVSTGE RASGMFDSVV LCECYDAGAA WYDLTPAETT VRLRAYFNTP GLPVCQDHLE
FWEAVFTGLT HIDAHFLSQT KQAGENFAYL VAYQATVCAR AKAPPPSWDA MWKCLARLKP
TLAGPTPLLY RLGPITNEVT LTHPGTKYIA TCMQADLEVM TSTWVLAGGV LAAVAAYCLA
TGCVSIIGRL HVNQRVVVAP DKEVLYEAFD EMEECASRAA LIEEGQRIAE MLKSKIQGLL
QQASKQAQDI QPAMQASWPK VEQFWARHMW NFISGIQYLA GLSTLPGNPA VASMMAFSAA
LTSPLSTSTT ILLNIMGGWL ASQIAPPAGA TGFVVSGLVG AAVGSIGLGK VLVDILAGYG
AGISGALVAF KIMSGEKPSM EDVINLLPGI LSPGALVVGV ICAAILRRHV GPGEGAVQWM
NRLIAFASRG NHVAPTHYVT ESDASQRVTQ LLGSLTITSL LRRLHNWITE DCPIPCAESW
LWEVWDWVCT VLSDFKTWLK AKLLPLMPGI PFLSCQRGYK GEWRGDGVMH TTCPCGADLA
GHIKNGSMRI TGPKTCSNTW HGTFPINAYT TGPGVPIPAP NYKFALWRVS AEDYVEVRRV
GDFHYVTGVT QDNIKCPCQV PAPEFFTEVD GIRLHRHAPK CKPLLRDEVS FSVGLNSFVV
GSQLPCEPEP DVAVLTSMLT DPSHITAESA RRRLARGSRP SLASSSASQL SAPSLKATCT
APHDSPGTDL LEANLLWGST ATRVETDEKV IILDSFESCV AEPNDDREVS VAAEILRPTK
KFPPALPIWA RPDYNPPLTE TWKQQDYKPP TVHGCALPPG KQPPVPPPRR KRTVQLTESV
VSTALAELAA KTFGQSEPSS DRDTDLTTPT ETTDSGPIVV DDASDDGSYS SMPPLEGEPG
DPDLTSDSWS TVSGSEDVVC CSMSYSWTGA LITPCSPEEE KLPINPLSNS LLRYHNKVYC
TTSKSASQRA KKVTFDRTQV LDAHYDSVLK DIKLAASKVS ARLLTLEEAC QLTPPHSARS
KYGFGAKEVR SLSGRAVNHI KSVWKDLLED PQTPIPTTIM AKNEVFCVDP AKGGKKPARL
IVYPDLGVRV CEKMALYDIT QKLPQAVMGA SYGFQYSPAQ RVEYLLKAWA EKKDPMGFSY
DTRCFDSTVT ERDIRTEESI YQACSLPEEA RTAIHSLTER LYVGGPMFNS KGQTCGYRRC
RASGVLTTSM GNTITCYVKA LAACKAAGIV APTMLVCGDD LVVISESQGT EEDERNLRAF
TEAMTRYSAP PGDPPRPEYD LELITSCSSN VSVALGPRGR RRYYLTRDPT TPLARAAWET
VRHSPINSWL GNIIQYAPTI WVRMVLMTHF FSILMVQDTL DQNLNFEMYG SVYSVNPLDL
PAIIERLHGL DAFSMHTYSH HELTRVASAL RKLGAPPLRV WKSRARAVRA SLISRGGKAA
VCGRYLFNWA VKTKLKLTPL PEARLLDLSS WFTVGAGGGD IFHSVSRARP RSLLFGLLLL
FVGVGLFLLP AR


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