ID C0SUQ3_9HEPC Unreviewed; 1099 AA.
AC C0SUQ3;
DT 26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 26-MAY-2009, sequence version 1.
DT 24-JAN-2024, entry version 67.
DE RecName: Full=Genome polyprotein {ECO:0000256|ARBA:ARBA00020107};
DE Flags: Fragment;
OS Hepatitis C virus subtype 1b.
OC Viruses; Riboviria; Orthornavirae; Kitrinoviricota; Flasuviricetes;
OC Amarillovirales; Flaviviridae; Hepacivirus; Hepacivirus hominis.
OX NCBI_TaxID=31647 {ECO:0000313|EMBL:BAH47686.1};
RN [1] {ECO:0000313|EMBL:BAH47686.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=K4preL-11 {ECO:0000313|EMBL:BAH47686.1};
RX PubMed=19369330; DOI=10.1128/JVI.02674-08;
RA Sugiyama K., Suzuki K., Nakazawa T., Funami K., Hishiki T., Ogawa K.,
RA Saito S., Shimotohno K.W., Suzuki T., Shimizu Y., Tobita R., Hijikata M.,
RA Takaku H., Shimotohno K.;
RT "Genetic analysis of hepatitis C virus with defective genome and its
RT infectivity in vitro.";
RL J. Virol. 83:6922-6928(2009).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13;
CC Evidence={ECO:0000256|ARBA:ARBA00001556};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC Endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004389}; Single-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004389}. Endoplasmic
CC reticulum membrane {ECO:0000256|ARBA:ARBA00004115}; Single-pass type I
CC membrane protein {ECO:0000256|ARBA:ARBA00004115}. Host cytoplasm
CC {ECO:0000256|ARBA:ARBA00004192}. Host endoplasmic reticulum membrane
CC {ECO:0000256|ARBA:ARBA00004517}; Single-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004517}. Host endoplasmic reticulum membrane
CC {ECO:0000256|ARBA:ARBA00004482}; Single-pass type I membrane protein
CC {ECO:0000256|ARBA:ARBA00004482}. Host lipid droplet
CC {ECO:0000256|ARBA:ARBA00004338}. Host mitochondrion membrane
CC {ECO:0000256|ARBA:ARBA00004458}; Single-pass type I membrane protein
CC {ECO:0000256|ARBA:ARBA00004458}. Host nucleus
CC {ECO:0000256|ARBA:ARBA00004147}. Lipid droplet
CC {ECO:0000256|ARBA:ARBA00004502}. Membrane
CC {ECO:0000256|ARBA:ARBA00004167}; Single-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004167}. Membrane
CC {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein
CC {ECO:0000256|ARBA:ARBA00004479}. Mitochondrion membrane
CC {ECO:0000256|ARBA:ARBA00004583}; Single-pass type I membrane protein
CC {ECO:0000256|ARBA:ARBA00004583}. Nucleus
CC {ECO:0000256|ARBA:ARBA00004123}. Virion membrane
CC {ECO:0000256|ARBA:ARBA00004563}; Single-pass type I membrane protein
CC {ECO:0000256|ARBA:ARBA00004563}.
CC -!- SIMILARITY: Belongs to the hepacivirus polyprotein family.
CC {ECO:0000256|ARBA:ARBA00008286}.
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DR EMBL; AB492225; BAH47686.1; -; Genomic_RNA.
DR euHCVdb; AB492225; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0044167; C:host cell endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0044186; C:host cell lipid droplet; IEA:UniProtKB-SubCell.
DR GO; GO:0044191; C:host cell mitochondrial membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005811; C:lipid droplet; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:1990904; C:ribonucleoprotein complex; IEA:UniProtKB-KW.
DR GO; GO:0019031; C:viral envelope; IEA:UniProtKB-KW.
DR GO; GO:0019013; C:viral nucleocapsid; IEA:UniProtKB-KW.
DR GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0008236; F:serine-type peptidase activity; IEA:InterPro.
DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR GO; GO:0075512; P:clathrin-dependent endocytosis of virus by host cell; IEA:UniProtKB-KW.
DR GO; GO:0039654; P:fusion of virus membrane with host endosome membrane; IEA:UniProtKB-KW.
DR GO; GO:0019049; P:mitigation of host antiviral defense response; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0019087; P:transformation of host cell by virus; IEA:InterPro.
DR GO; GO:0019062; P:virion attachment to host cell; IEA:UniProtKB-KW.
DR CDD; cd20903; HCV_p7; 1.
DR Gene3D; 2.40.10.120; -; 1.
DR Gene3D; 6.10.250.1610; -; 1.
DR Gene3D; 6.10.250.1750; -; 1.
DR Gene3D; 3.30.160.890; Hepatitis C virus envelope glycoprotein E1, chain C; 1.
DR Gene3D; 2.30.30.710; Hepatitis C virus non-structural protein NS2, C-terminal domain; 1.
DR Gene3D; 1.20.1280.150; Hepatitis C virus non-structural protein NS2, N-terminal domain; 1.
DR InterPro; IPR002521; HCV_Core_C.
DR InterPro; IPR044896; HCV_core_chain_A.
DR InterPro; IPR002522; HCV_core_N.
DR InterPro; IPR002519; HCV_Env.
DR InterPro; IPR002531; HCV_NS1.
DR InterPro; IPR002518; HCV_NS2.
DR InterPro; IPR042205; HCV_NS2_C.
DR InterPro; IPR042209; HCV_NS2_N.
DR InterPro; IPR004109; NS3_Peptidase_S29.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR Pfam; PF01543; HCV_capsid; 1.
DR Pfam; PF01542; HCV_core; 1.
DR Pfam; PF01539; HCV_env; 1.
DR Pfam; PF01560; HCV_NS1; 1.
DR Pfam; PF01538; HCV_NS2; 1.
DR Pfam; PF02907; Peptidase_S29; 1.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR PROSITE; PS51693; HCV_NS2_PRO; 1.
DR PROSITE; PS51822; HV_PV_NS3_PRO; 1.
PE 3: Inferred from homology;
KW Acetylation {ECO:0000256|ARBA:ARBA00022990};
KW Apoptosis {ECO:0000256|ARBA:ARBA00022703};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Clathrin-mediated endocytosis of virus by host
KW {ECO:0000256|ARBA:ARBA00022570};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Host lipid droplet {ECO:0000256|ARBA:ARBA00023190};
KW Host membrane {ECO:0000256|ARBA:ARBA00022870};
KW Host mitochondrion {ECO:0000256|ARBA:ARBA00023147};
KW Host-virus interaction {ECO:0000256|ARBA:ARBA00022581};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022840};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Ribonucleoprotein {ECO:0000256|ARBA:ARBA00023274};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|ARBA:ARBA00022448};
KW Ubl conjugation {ECO:0000256|ARBA:ARBA00022843};
KW Viral attachment to host cell {ECO:0000256|ARBA:ARBA00022804};
KW Viral envelope protein {ECO:0000256|ARBA:ARBA00022879};
KW Viral nucleoprotein {ECO:0000256|ARBA:ARBA00023086};
KW Viral penetration into host cytoplasm {ECO:0000256|ARBA:ARBA00022570};
KW Virion {ECO:0000256|ARBA:ARBA00022844};
KW Virus endocytosis by host {ECO:0000256|ARBA:ARBA00022890};
KW Virus entry into host cell {ECO:0000256|ARBA:ARBA00023296}.
FT TRANSMEM 718..740
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 752..778
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 784..803
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 815..835
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 891..913
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 903..1026
FT /note="Peptidase C18"
FT /evidence="ECO:0000259|PROSITE:PS51693"
FT DOMAIN 1027..1099
FT /note="Peptidase S29"
FT /evidence="ECO:0000259|PROSITE:PS51822"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 41..76
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 47..69
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1099
FT /evidence="ECO:0000313|EMBL:BAH47686.1"
SQ SEQUENCE 1099 AA; 120351 MW; 57B9C8CB04D33CC6 CRC64;
MSTNPKPQRK TYRNINRRPQ DVKFPGGGQI VGGVYLLPRR GPRLGVRATR KTSERSQPRG
RRQPIPKARR PEGRTWAQPG YPWPLYGNEG LGWAGWLLSP RGSRPNWGPT DPRRRSRNLG
RVIDTLTCGF ADLMGYIPLV GAPLGGVARA LAHGVRVLED GVNYATGNLP GCSFSIFLLA
LLSCLTIPAS AYEVRNVSGV YHVTNDCSNS SIVYEAADMI MHSPGGVPCV RENNSSRCWV
ALTPTLAARN NSVPTTAIRR HVDLLVGAAT LCSAMYVGDL CGSVFLVSQL FTFSPRRHET
VQDCNCSIYP GHVSGHRMAW DMMMNWSPTA ALVVSQLLRI PQAVMDMVAG AHWGVLAGLA
YYSMVGNWAK VLIVMLLFSG VDGGTHTVGG TSAHTTRGLT SLFTSGPSQK IQLVNTNGSW
HINRTALNCN DSLQTGFLAA LFYTHRFNAS GCPDRMAKCR PIDTFDQGWG PITYAEPNNV
DQRPYCWHYA PRPCGVVPAS EVCGPVYCFT PSPVVVGTTD RLGHPTYNWG ENETDVLLLN
NTRPPHGNWF GCTWMNSTGF TKTCGGPPCN IGGVGNNTLT CPTDCFRKHP EATYTKCGSG
PWLTPRCLVH YPYRLWHYPC TVNFTIFKVR MYVGGVEHRL DAACNWTRGE RCDLEDRDRS
ELSPLLLSTT EWQILPCSYT TLPALSTGLI HLHRNIVDVQ YLYGIGSVVV SFAIKWEYIV
LLFLLLADAR VCACLWMMLL IAQAEAALEN LVVLNAASVA GAHGILSFLV FFCAAWYIKG
RLVPGAAYAF YGVWPLLLLL LALPQRAYAT DREMAASCGG AVFIGLAILT LSPYYKVFLA
KLIWWLQYFI TRAEAHLQVW VPPLNVRGGR DAIILLMCAV HPELIFDITK LLLAILGPLM
VLQASITRVP YFVRAQGLIR ACMLVRKVAG GHYVQMAFVK LAALTGTYVY DHLAPLKYWA
HAGLRDLAVA VEPVVFSDME TKIITWGADT AACGDIISGL PVSARRGREV LLGPADSFEG
QGWRLLAPIT AYSQQTRGLL GCIITSLTGR DKNQVEGEVQ VVSTATQSFL ATCVNGVCWT
VFHGAGSKTL AGPKGPITQ
//