ID Q4PQQ0_9HEPC Unreviewed; 1644 AA.
AC Q4PQQ0;
DT 19-JUL-2005, integrated into UniProtKB/TrEMBL.
DT 19-JUL-2005, sequence version 1.
DT 27-MAR-2024, entry version 122.
DE RecName: Full=Genome polyprotein {ECO:0000256|ARBA:ARBA00020107};
DE Flags: Fragment;
OS Hepacivirus hominis.
OC Viruses; Riboviria; Orthornavirae; Kitrinoviricota; Flasuviricetes;
OC Amarillovirales; Flaviviridae; Hepacivirus.
OX NCBI_TaxID=3052230 {ECO:0000313|EMBL:AAY82061.1};
RN [1] {ECO:0000313|EMBL:AAY82061.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=AD13c10 {ECO:0000313|EMBL:AAY82061.1};
RX PubMed=15939791; DOI=10.1084/jem.20050122;
RA Ray S.C., Fanning L., Wang X.H., Netski D.M., Kenny-Walsh E., Thomas D.L.;
RT "Divergent and convergent evolution after a common-source outbreak of
RT hepatitis C virus.";
RL J. Exp. Med. 201:1753-1759(2005).
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 -!- CATALYTIC ACTIVITY:
CC Reaction=a ribonucleoside 5'-triphosphate + H2O = a ribonucleoside 5'-
CC diphosphate + H(+) + phosphate; Xref=Rhea:RHEA:23680,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:57930, ChEBI:CHEBI:61557; EC=3.6.1.15;
CC Evidence={ECO:0000256|ARBA:ARBA00001491};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC Endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004477}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004477}. 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:ARBA00004153}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004153}. 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 nucleus
CC {ECO:0000256|ARBA:ARBA00004147}. Lipid droplet
CC {ECO:0000256|ARBA:ARBA00004502}. Membrane
CC {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein
CC {ECO:0000256|ARBA:ARBA00004479}. Nucleus
CC {ECO:0000256|ARBA:ARBA00004123}. Virion membrane
CC {ECO:0000256|ARBA:ARBA00004563}; Single-pass type I membrane protein
CC {ECO:0000256|ARBA:ARBA00004563}.
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DR EMBL; DQ061356; AAY82061.1; -; Genomic_RNA.
DR MEROPS; S29.001; -.
DR euHCVdb; DQ061356; -.
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:0033650; C:host cell mitochondrion; IEA:UniProtKB-KW.
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:0017111; F:ribonucleoside triphosphate phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR GO; GO:0008236; F:serine-type peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR GO; GO:0039654; P:fusion of virus membrane with host endosome membrane; 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:0046718; P:viral entry into host cell; IEA:UniProtKB-KW.
DR GO; GO:0019062; P:virion attachment to host cell; IEA:UniProtKB-KW.
DR CDD; cd17931; DEXHc_viral_Ns3; 1.
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 Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR Gene3D; 1.10.820.10; RNA Helicase Chain A , domain 3; 1.
DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 1.
DR InterPro; IPR011492; Flavi_DEAD.
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; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR004109; HepC_NS3_protease.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR Pfam; PF07652; Flavi_DEAD; 1.
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 SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR PROSITE; PS51693; HCV_NS2_PRO; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS51822; HV_PV_NS3_PRO; 1.
PE 4: Predicted;
KW Acetylation {ECO:0000256|ARBA:ARBA00022990};
KW Apoptosis {ECO:0000256|ARBA:ARBA00022703};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Capsid protein {ECO:0000256|ARBA:ARBA00022561};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Fusion of virus membrane with host endosomal membrane
KW {ECO:0000256|ARBA:ARBA00022510};
KW Fusion of virus membrane with host membrane
KW {ECO:0000256|ARBA:ARBA00022506};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Host cytoplasm {ECO:0000256|ARBA:ARBA00023200};
KW Host endoplasmic reticulum {ECO:0000256|ARBA:ARBA00023184};
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 Serine protease {ECO:0000256|ARBA:ARBA00022825};
KW Thiol protease {ECO:0000256|ARBA:ARBA00022807};
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 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:ARBA00022595};
KW Viral RNA replication {ECO:0000256|ARBA:ARBA00022953};
KW Virion {ECO:0000256|ARBA:ARBA00022844};
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..836
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 873..901
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..1208
FT /note="Peptidase S29"
FT /evidence="ECO:0000259|PROSITE:PS51822"
FT DOMAIN 1217..1369
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 1361..1538
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
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 1644
FT /evidence="ECO:0000313|EMBL:AAY82061.1"
SQ SEQUENCE 1644 AA; 178628 MW; 017CAAF3655C56DA CRC64;
MSTNPKPQRK TKRNTNRRPQ DVKFPGGGQI VGGVYLLPRR GPRLGVRATR KTSERSQPRG
RRQPIPKARR PEGRTWAQPG YPWPLYGNEG MGWAGWLLSP RGSRPSWGPT DPRRRSRNLG
KVIDTLTCGL ADLMGYIPLV GAPLGGAARA LAHGVRVLED GVNYATGNLP GCSFSIFLLA
LLSCLTIPAS AIEVRNVSGV YHVTNDCSNA SIVYEAADMI MHTPGCVPCV RENNSSRCWV
ALTPTLAARN SSIPTTTIRR HVDLLVGTAA FCSAMYVGDL CGSVFLVSQL FTFSPRRHET
VQDCNCSIYP GHVTGHRMAW DMMMNWSPTT ALVVSQLLRI PQAVVDVVAG AHWGILAGLA
YYSMVGNWAK VLIVMLLFAG VDGSTYTTGG AQARTAYGIA SLFTRGAQQR IQLINTNGSW
HINRTALNCN DSLNTGFIAA LFYATSFNST GCLERMASCR PIDKFAQGWG PITYTKPSIL
DQRPYCWHYA PQPCGIVPAS QVCGPVYCFT PSPVVVGTTD RFGVPTYRWG ENETDVLLLN
NTRPPQGNWF GCTWMNSTGF TKTCGGPPCN IGGVGNDTLI CPTDCFRKHP EATYTKCGSG
PWLTPRCMVH YPYRLWHYPC TVNFTIFKVR MYVGGVEHRL EAACNWTRGE RCDLEDRDRS
ELSPLLLSTT EWQVLPCSFT TLPALSTGLI HLHRNIVDVQ YLYGIGSAVV SYAIKWEYVL
LLFLFLADAR VCACLWMMLL IAQAEAALEN LVVLNAASVA GTHGILPFLA FFCAAWYIKG
RLVPGAAYAF YGVWPLLLLL LALPPRAYAM DREMAASCGG AVFIGLAFLT LSPHYKLFLA
RLIWWLQYFI TRAEANLQVW IPPLNVRGGR DAIILLMCVI HPELIFVITK ILLAILGPLM
VLQAGLTRVP YFVRAHGLIR ACLLVRKVAG GHYVQMAFMR LAALTGTYVY NHLTPLSDWA
HEGLRDLAVA VEPVVFSDME TKIITWGADT AACGDIILGL PVSARRGREI LLGPADSLEG
QGWRLLAPIT AYAQQTRGLL GCIVTSLTGR DKNQVEGEVQ VVSTATQSFL ATCVNGVCWT
VYHGAGTKTL AGQKGPITQM YTNVDQDLVG WQAPPGARSL TPCTCGSSDL YLVTRHADVI
PVRRRGDSRG SLLSPRPVSY LKGSSGGPLL CPSGHAAGIF RAAVCTRGVA KAVDFVPVES
METTMRSPVF TDNSSPPAVP QTFQVAHLHA PTGSGKSTKV PAAYAAQGYK VLVLNPSVAA
TLGFGAYMSK AHGVDPNIRT GVRTITTGAP ITYSTYGKFL ADGGCSGGAY DIIICDECHS
TDSTTILGIG TVLDQAETAG ARLVVLATAT PPGSVTVPHS NIEEVALSNM GEIPFYGKAI
PIETIKGGRH LIFRHSRKKC DELAAKLSGL GLNAVAYYRG LDVSVIPTSG DVVVVATDAL
MTGFTGDFDS VIDCNTCVTQ TVDFSLDPTF TIETTTVPQD AVSRSQRRGR TGRGRAGIYR
FVTPGERPSG MFDSSVLCEC YDAGCAWYEL TPAETTVRLR AYLNTPGLPV CQDHLEFWEG
VFTGLTHIDA HFLSQTKQAG DNFPYLVAYQ ATVCARAQAP PPSWDQMWKC LIRLKPTLHG
PTPLLYRLGA VQNEVTLTHP ITKY
//
