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Database: UniProt
Entry: C0SUQ3_9HEPC
LinkDB: C0SUQ3_9HEPC
Original site: C0SUQ3_9HEPC 
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
//
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