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Database: UniProt
Entry: D2Y2R8_9ENTO
LinkDB: D2Y2R8_9ENTO
Original site: D2Y2R8_9ENTO 
ID   D2Y2R8_9ENTO            Unreviewed;       138 AA.
AC   D2Y2R8;
DT   02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT   02-MAR-2010, sequence version 1.
DT   27-MAR-2024, entry version 40.
DE   RecName: Full=Genome polyprotein {ECO:0000256|ARBA:ARBA00020107};
DE   Flags: Fragment;
OS   Rhinovirus C.
OC   Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC   Picornavirales; Picornaviridae; Ensavirinae; Enterovirus.
OX   NCBI_TaxID=463676 {ECO:0000313|EMBL:ADB20052.1};
RN   [1] {ECO:0000313|EMBL:ADB20052.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Resp_2784/07 {ECO:0000313|EMBL:ADB20052.1};
RX   PubMed=20041158; DOI=10.1371/journal.pone.0008518;
RA   Wisdom A., Kutkowska A.E., McWilliam Leitch E.C., Gaunt E., Templeton K.,
RA   Harvala H., Simmonds P.;
RT   "Genetics, recombination and clinical features of human rhinovirus species
RT   C (HRV-C) infections; interactions of HRV-C with other respiratory
RT   viruses.";
RL   PLoS ONE 4:E8518-E8518(2009).
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; GU294339; ADB20052.1; -; Genomic_RNA.
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   Gene3D; 2.60.120.20; -; 1.
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; IPR029053; Viral_coat.
DR   Pfam; PF02226; Pico_P1A; 1.
DR   Pfam; PF00073; Rhv; 1.
DR   SUPFAM; SSF88633; Positive stranded ssRNA viruses; 1.
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          91..138
FT                   /note="Picornavirus capsid"
FT                   /evidence="ECO:0000259|Pfam:PF00073"
FT   NON_TER         138
FT                   /evidence="ECO:0000313|EMBL:ADB20052.1"
SQ   SEQUENCE   138 AA;  15061 MW;  554235E4C0F4A5E6 CRC64;
     MGAQVSKQNV GSHESGISAS SGSVIKYFNI NYYKDSASSG LSKQDFSMDP EKFTKPIAEA
     MTNPALMSPS IEACGFSDRL KQITIGSSTI TTQDTLNTIV AYGEWPEYLK DIDASAVDKP
     THPETSTDRF YTLTSVKW
//
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