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Database: UniProt
Entry: H9BCJ5_9ENTO
LinkDB: H9BCJ5_9ENTO
Original site: H9BCJ5_9ENTO 
ID   H9BCJ5_9ENTO            Unreviewed;       719 AA.
AC   H9BCJ5;
DT   16-MAY-2012, integrated into UniProtKB/TrEMBL.
DT   16-MAY-2012, sequence version 1.
DT   27-MAR-2024, entry version 38.
DE   RecName: Full=Genome polyprotein {ECO:0000256|ARBA:ARBA00020107};
DE   Flags: Fragment;
OS   Coxsackievirus A9.
OC   Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC   Picornavirales; Picornaviridae; Ensavirinae; Enterovirus; Enterovirus B.
OX   NCBI_TaxID=12067 {ECO:0000313|EMBL:AFD33731.1};
RN   [1] {ECO:0000313|EMBL:AFD33731.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=1857 {ECO:0000313|EMBL:AFD33731.1};
RX   PubMed=22855495; DOI=10.1128/JVI.00640-12;
RA   McLeish N.J., Williams C.H., Kaloudas D., Roivainen M.M., Stanway G.;
RT   "Symmetry-related clustering of positive charges is a common mechanism for
RT   heparan sulfate binding in enteroviruses.";
RL   J. Virol. 86:11163-11170(2012).
CC   -!- FUNCTION: Component of immature procapsids, which is cleaved into
CC       capsid proteins VP4 and VP2 after maturation (By similarity). Allows
CC       the capsid to remain inactive before the maturation step.
CC       {ECO:0000256|ARBA:ARBA00025202}.
CC   -!- SUBUNIT: Interacts with capsid protein VP1 and capsid protein VP3 to
CC       form heterotrimeric protomers. {ECO:0000256|ARBA:ARBA00011474}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Host
CC       cytoplasm {ECO:0000256|ARBA:ARBA00004192}. Virion
CC       {ECO:0000256|ARBA:ARBA00004328}.
CC   -!- SIMILARITY: Belongs to the picornaviruses polyprotein family.
CC       {ECO:0000256|ARBA:ARBA00008303}.
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DR   EMBL; JN996515; AFD33731.1; -; Genomic_RNA.
DR   MEROPS; N08.001; -.
DR   GO; GO:0019028; C:viral capsid; IEA:InterPro.
DR   GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR   GO; GO:0044694; P:pore-mediated entry of viral genome into host cell; IEA:UniProtKB-KW.
DR   GO; GO:0039657; P:suppression by virus of host gene expression; IEA:UniProtKB-KW.
DR   GO; GO:0019062; P:virion attachment to host cell; IEA:UniProtKB-KW.
DR   CDD; cd00205; rhv_like; 3.
DR   Gene3D; 2.60.120.20; -; 3.
DR   Gene3D; 4.10.80.10; Picornavirus coat protein VP4; 1.
DR   InterPro; IPR003138; Pico_P1A.
DR   InterPro; IPR036988; Pico_P1A_sf.
DR   InterPro; IPR001676; Picornavirus_capsid.
DR   InterPro; IPR033703; Rhv-like.
DR   InterPro; IPR029053; Viral_coat.
DR   Pfam; PF02226; Pico_P1A; 1.
DR   Pfam; PF00073; Rhv; 3.
DR   SUPFAM; SSF88633; Positive stranded ssRNA viruses; 2.
PE   3: Inferred from homology;
KW   Capsid protein {ECO:0000256|ARBA:ARBA00022561};
KW   Eukaryotic host gene expression shutoff by virus
KW   {ECO:0000256|ARBA:ARBA00023247};
KW   Eukaryotic host translation shutoff by virus
KW   {ECO:0000256|ARBA:ARBA00022809};
KW   Host gene expression shutoff by virus {ECO:0000256|ARBA:ARBA00022995};
KW   Host-virus interaction {ECO:0000256|ARBA:ARBA00022581};
KW   Lipoprotein {ECO:0000256|ARBA:ARBA00023288};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Myristate {ECO:0000256|ARBA:ARBA00022707};
KW   Pore-mediated penetration of viral genome into host cell
KW   {ECO:0000256|ARBA:ARBA00023255};
KW   Viral attachment to host cell {ECO:0000256|ARBA:ARBA00022804};
KW   Viral penetration into host cytoplasm {ECO:0000256|ARBA:ARBA00022595};
KW   Virion {ECO:0000256|ARBA:ARBA00022561};
KW   Virus entry into host cell {ECO:0000256|ARBA:ARBA00023296}.
FT   DOMAIN          93..300
FT                   /note="Picornavirus capsid"
FT                   /evidence="ECO:0000259|Pfam:PF00073"
FT   DOMAIN          359..524
FT                   /note="Picornavirus capsid"
FT                   /evidence="ECO:0000259|Pfam:PF00073"
FT   DOMAIN          613..718
FT                   /note="Picornavirus capsid"
FT                   /evidence="ECO:0000259|Pfam:PF00073"
FT   NON_TER         719
FT                   /evidence="ECO:0000313|EMBL:AFD33731.1"
SQ   SEQUENCE   719 AA;  79713 MW;  066F291D2A033E0A CRC64;
     MGAQVSTQKT GAHETSLSAT GNSTIHYTNI NYYKDAASNS ANRQDFTQDP SKFTEPVKDV
     MIKSLPALNS PTVEECGFSD RVRSITLGNS TITTQECANV VVGYGRWPSY LRDDEATAED
     QPTQPDVATC RFYTLDSIKW EKGSVGWWWK FPEALSDMGL FGQNMQYHYL GRAGYTIHVQ
     CNASKFHQGC LLVVCVPEAE MGGAVVGQAF PSSAMADGDK AYEFTSTNQS DQTKVQTAVH
     NAGMGVGVGN LTIFPHQWIN LRTNNSATIV MPYINSVPMD NMFRHYNFTL MVIPFVKLDY
     ADTASTYVPI TVTVAPMCAE YNGLRLAQAQ GLPTMNTPGS TQFLTSDDFQ SPCALPQFDV
     TPSMNIPGEV KNLMEIAEVD SVVPVNNVQD TTDQMSKIMT SVHIVAQHWQ RVFGLKFLVG
     LDIDLQRTLL GEILNYYAAR SHSMKDIGLQ SSSAMAVPWI LIAYSPPGAN PPKTRKDAML
     GTHIIWDIGL QSSCVLCVPW ISQTHYRLVQ QDEYTSAGFV TCWYQTGMIV PPGNPNSSSI
     MCFASACNDF SVRMLRDTPF ISQDNKLQGD VEEAIERAVV HVADTMRSGP SNSESIPALT
     AVETGHTSQV TPSDTMQTRH VKNYHSRSES TIENFLGRSA CVYMEEYKTT DSDTNKKFVA
     WPINTKQMVQ MRRKLEMFTY LRFDMEVTFV ITSRQDPGTT LAQDMPVLTH QIMYVPPGG
//
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