ID U5YB81_9HEPC Unreviewed; 667 AA.
AC U5YB81;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE SubName: Full=Polyprotein {ECO:0000313|EMBL:AGZ86410.1};
DE Flags: Fragment;
GN Name=gp1 {ECO:0000313|EMBL:AGZ86410.1};
OS Hepacivirus hominis.
OC Viruses; Riboviria; Orthornavirae; Kitrinoviricota; Flasuviricetes;
OC Amarillovirales; Flaviviridae; Hepacivirus.
OX NCBI_TaxID=3052230 {ECO:0000313|EMBL:AGZ86410.1};
RN [1] {ECO:0000313|EMBL:AGZ86410.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=M003_N_2BC8 {ECO:0000313|EMBL:AGZ86410.1};
RA Honegger J., Kim S., Price A., Mateu G., Kohout J., Prasad M., Lemon S.,
RA Grakoui A., Walker C.;
RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AGZ86410.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=M003_N_2BC8 {ECO:0000313|EMBL:AGZ86410.1};
RX PubMed=24162814;
RA Honegger J.R., Kim S., Price A.A., Kohout J.A., McKnight K.L., Prasad M.R.,
RA Lemon S.M., Grakoui A., Walker C.M.;
RT "Loss of immune escape mutations during persistent HCV infection in
RT pregnancy enhances replication of vertically transmitted viruses.";
RL Nat. Med. 19:1529-1533(2013).
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JQ062258; AGZ86410.1; -; Genomic_RNA.
DR GO; GO:0033644; C:host cell membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0044423; C:virion component; 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: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 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; 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; IPR002531; HCV_NS1.
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; 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 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, ECO:0000256|SAM:Phobius};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius};
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 TRANSMEM 152..175
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 187..212
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 219..236
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 248..269
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 307..336
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 333..460
FT /note="Peptidase C18"
FT /evidence="ECO:0000259|PROSITE:PS51693"
FT DOMAIN 461..642
FT /note="Peptidase S29"
FT /evidence="ECO:0000259|PROSITE:PS51822"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:AGZ86410.1"
FT NON_TER 667
FT /evidence="ECO:0000313|EMBL:AGZ86410.1"
SQ SEQUENCE 667 AA; 72876 MW; 755B79CA143A0E33 CRC64;
PPCVIGGVGN NTLHCPTDCF RKHPEATYSR CGSGPWITPR CMVDYPHRLW HYPCTINYTT
FKVRMYVGGV EHRLDAACNW TRGERCNLED RDRSELSPLL LSTTQWQVLP CSFTTLPALS
TGLTHLHQNV VDVQYLYGVG SSIASWAIKW EYVVLLFLLL ADARVCSCLW MMLLISQVEA
ALENLVVLNA ASLAGTRGLV PFLVFFCFAW YLKGRWAPGV VYALYGMWPL LLLLLALPQR
AYALDTEVAA SCGGVVLVGL MALTLSPYYK RYISWCLWWL QYFLTRAEAQ LHVWVPPLDV
RGGRDAVILL MCVVHPALVF DITKLLLAIL GPLWILQASL LKVPYFMRVQ GLLRVCALAR
KMAGGHYAQM AIIKLGALTG THVYNHLTPL RDWAHNGLRD LAVAVEPVVF SQMETKLITW
GADTAACGDI INGLPVSARR GQEILLGPAD GMVSKGWRLL APITAYAQQT RGLLGCIITS
LTGRDKNQAE GEVQIVSTAA QTFLATCING VCWTVYHGAG TRTIASPKGP VIQMYTNVDK
DLVGWPAPQG TRSLTPCACG SSDLYLVTRH ADVIPVRRRG DSKGSLLSPR PISYLKGSSG
GPLLCPAGHA VGILRAAVCT RGVAKAVDFI PVENLETTMG SPVFTDNSSP PAVPQSFQVA
HLHAPTG
//
