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Database: UniProt
Entry: C0SUL6_9HEPC
LinkDB: C0SUL6_9HEPC
Original site: C0SUL6_9HEPC 
ID   C0SUL6_9HEPC            Unreviewed;       426 AA.
AC   C0SUL6;
DT   26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   26-MAY-2009, sequence version 1.
DT   27-MAR-2024, entry version 61.
DE   SubName: Full=Polyprotein {ECO:0000313|EMBL:BAH47649.1};
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:BAH47649.1};
RN   [1] {ECO:0000313|EMBL:BAH47649.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=T5S-5 {ECO:0000313|EMBL:BAH47649.1};
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}. Host
CC       cytoplasm {ECO:0000256|ARBA:ARBA00004192}.
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DR   EMBL; AB492188; BAH47649.1; -; Genomic_RNA.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0033644; C:host cell membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0019028; C:viral capsid; IEA:InterPro.
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:0006508; P:proteolysis; IEA:InterPro.
DR   GO; GO:0019087; P:transformation of host cell by virus; IEA:InterPro.
DR   GO; GO:0046718; P:viral entry into host cell; IEA:UniProtKB-KW.
DR   GO; GO:0019062; P:virion attachment to host cell; IEA:UniProtKB-KW.
DR   Gene3D; 2.40.10.120; -; 1.
DR   Gene3D; 6.10.250.1610; -; 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; IPR002518; HCV_NS2.
DR   InterPro; IPR042205; HCV_NS2_C.
DR   InterPro; IPR042209; HCV_NS2_N.
DR   InterPro; IPR004109; HepC_NS3_protease.
DR   InterPro; IPR009003; Peptidase_S1_PA.
DR   Pfam; PF01543; HCV_capsid; 1.
DR   Pfam; PF01542; HCV_core; 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   4: Predicted;
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Host membrane {ECO:0000256|ARBA:ARBA00022870};
KW   Host-virus interaction {ECO:0000256|ARBA:ARBA00022581};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989};
KW   Viral attachment to host cell {ECO:0000256|ARBA:ARBA00022804};
KW   Virion {ECO:0000256|ARBA:ARBA00022844};
KW   Virus entry into host cell {ECO:0000256|ARBA:ARBA00023296}.
FT   DOMAIN          230..353
FT                   /note="Peptidase C18"
FT                   /evidence="ECO:0000259|PROSITE:PS51693"
FT   DOMAIN          354..426
FT                   /note="Peptidase S29"
FT                   /evidence="ECO:0000259|PROSITE:PS51822"
FT   REGION          1..78
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         426
FT                   /evidence="ECO:0000313|EMBL:BAH47649.1"
SQ   SEQUENCE   426 AA;  45914 MW;  48CEE7557C34BD24 CRC64;
     MSTNPKPQRK TKRNTNRRPQ DVKFPGGGQI VGGVYLLPRR GPRLGVRATR KTSERSQPRG
     RRQPIPKARR PEGRTWAQPG YPWPLYGNEG LGWAGWLLSP RGSRPSWGPT DPRRRSRNLG
     KVIDTLTCGF ADLMGYIPLV GAPLGGAARA LAHGVRVLED SVNYATGNLP GCSFSIFLLA
     LLSCLTVPAS ACEVRNVSGV YHATADCSNL SIFDITKLLL AIFGPVMVLQ AGLVRVPYFV
     RAQGLIRACM LARKVAGGHY VQMALLKLAA LTGTYVYNHL TPLRDWAHEG LRDLAVAVEP
     VVFSDMETKI ITWGADTAAC GDIISGLPVS ARRGREILLG PADSLQGQGW RLLAPITAYS
     QQTRGLLGCI ITSLTGRDKN QVEGEVQVVS TATQSFLATC INGVCWTVYH GAGSKTLAGP
     KGPITQ
//
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