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Database: UniProt
Entry: J4AVF1_9HEPC
LinkDB: J4AVF1_9HEPC
Original site: J4AVF1_9HEPC 
ID   J4AVF1_9HEPC            Unreviewed;      1637 AA.
AC   J4AVF1;
DT   31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   31-OCT-2012, sequence version 1.
DT   24-JAN-2024, entry version 64.
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:AFQ54303.1};
RN   [1] {ECO:0000313|EMBL:AFQ54303.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=9055.11 {ECO:0000313|EMBL:AFQ54303.1};
RX   PubMed=22927816; DOI=10.1371/journal.ppat.1002880;
RA   Li H., Stoddard M.B., Wang S., Blair L.M., Giorgi E.E., Parrish E.H.,
RA   Learn G.H., Hraber P., Goepfert P.A., Saag M.S., Denny T.N., Haynes B.F.,
RA   Hahn B.H., Ribeiro R.M., Perelson A.S., Korber B.T., Bhattacharya T.,
RA   Shaw G.M.;
RT   "Elucidation of hepatitis C virus transmission and early diversification by
RT   single genome sequencing.";
RL   PLoS Pathog. 8:e1002880-e1002880(2012).
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; JQ803524; AFQ54303.1; -; Genomic_RNA.
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: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: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   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; NS3_Peptidase_S29.
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   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 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   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        247..270
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        707..728
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        740..767
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        774..793
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        805..824
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        880..902
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          888..1015
FT                   /note="Peptidase C18"
FT                   /evidence="ECO:0000259|PROSITE:PS51693"
FT   DOMAIN          1016..1197
FT                   /note="Peptidase S29"
FT                   /evidence="ECO:0000259|PROSITE:PS51822"
FT   DOMAIN          1206..1358
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          1365..1527
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          25..59
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1466..1489
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        30..52
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:AFQ54303.1"
FT   NON_TER         1637
FT                   /evidence="ECO:0000313|EMBL:AFQ54303.1"
SQ   SEQUENCE   1637 AA;  177129 MW;  134B57E2E4DEC8C9 CRC64;
     RPQDVKFPGG GQIVGGVYVL PRRGPRLGVR ATRKTSERSQ PRGRRQPIPK ARRSEGRSWA
     QPGYPWPLYG NEGCGWAGWL LSPRGSRPSW GPNDPRRRSR NLGKVIDTLT CGFADLMGYI
     PLVGAPVGGV ARALAHGVRA LEDGINFATG NLPGCSFSIF LLALFSCLVH PAASLEWRNA
     SGLYILTNDC SNSSIVYEAD DVILHTPGCV PCVQDGNTSM CWTSVTPTVA VRYVGATTAS
     IRSHVDLLVG AATMCSALYV GDVCGAVFLV GQAFTFRPRR HQTVQTCNCS LYPGHLSGHR
     MAWDMMMNWS PAVGMVVAHV LRLPQTLFDI IAGAHWGILA GLAYYSMQGN WAKVAIIMIM
     FSGVDAGTHV IGGSTARGAS ALTSLLSLGP QQKLQLVRTN GSWHINSTAL NCNDSLNTGF
     IAGLIYYHKF NSTGCPQRLS SCKPITSFGQ GWGPLTDANI TGPSTDKPYC WHYAPRPCDV
     VPASSVCGPV YCFTPSPVVV GTTDERGAPT YTWGANETDV FLLRSLRPPS GQWFGCTWMN
     STGFIKTCGA PPCNIYGGGA GPGNGSSLFC PTDCFRKHPE ATYSRCGAGP WLTPRCMVDY
     PYRLWHYPCT VNFTLFKVRM FVGGIEHRFT AACNWTRGER CDIEDRDRSE QHPLLHSTTE
     FAILPCSFTP MPALSTGLIH LHQNIVDVQY LYGVGSGMVG WALKWEFVIL VFLLLADARV
     CVALWLMLMI SQTEAALENL VTLNAVAAAG THGIGWYLVA FCAAWYVRGK LVPLVTYSLT
     GLWSLALLVL LLPQRAYAWS GEDSATLGAG VLVLFGFFTL SPWYKHWIGR LMWWNQYAIC
     RCESALHVWV PPLLARGSRD GVILLASLLH PSLVFDITKL LIAVLGPLYL IQATITTTPY
     FVRAHVLVRL CMLVRSVMGG KYFQMIILNI GRWFNTYLYD HLAPMQHWAA AGLKDLAVAT
     EPVIFSPMEI KVITWGADTA ACGDILCGLP VSARLGREVL LGPADDYREM GWKLLAPITA
     YAQQTRGLLG TIVTSLTGRD KNVVTGEVQV LSTATQTFLG TTVGGVMWTV YHGAGSRTLA
     GVKHPALQMY TNVDQDLVGW PAPLGAKSLE PCTCGTADLY LVTRDADVIP ARRRGDSTAS
     LLSPRPLACL KGSSGGPVMC PSGHVAGIFR AAVCTRGVAK ALQFIPVETL STQARSPSFS
     DNSTPPAVPQ SYQVGYLHAP TGSGKSTKVP AAYVAQGYNV LVLNPSVAAT LGFGSYMSRA
     YGIDPNVRTG NRTVTTGAKL TYSTYGKFLA DGGCSGGAYD VIICDECHAQ DATSILGIGT
     VLDQAETAGV RLTVLATATP PGSITVPHSN IEEVALGSEG EIPFYGKAIP IALLKGGRHL
     IFCHSKKKCD EVASKLRGMG LNAVAYYRGL DVSVIPTAGD VVVCATDALM TGYTGDFDSV
     IDCNVAVEQY VDFSLDPTFS IETRTAPQDA VSRSQRRGRT GRGRHGTYRY VAPGERPSGM
     FDSVVLCECY DAGCSWYDLQ PAETTVRLRA YLSTPGLPVC QDHLDFWESV FTGLTHIDAH
     FLSQTKQQGL NFSYLTAYQA TVCARAQAPP PSWDESWKCL VRLKPTLHGP TPLLYRLGPV
     QNEICLTHPV TKYIMAC
//
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