ID C6ZFI1_9ENTO Unreviewed; 136 AA.
AC C6ZFI1;
DT 22-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 22-SEP-2009, sequence version 1.
DT 24-JAN-2024, entry version 39.
DE RecName: Full=Genome polyprotein {ECO:0000256|ARBA:ARBA00020107};
DE Flags: Fragment;
OS Human rhinovirus sp.
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC Picornavirales; Picornaviridae; Ensavirinae; Enterovirus.
OX NCBI_TaxID=169066 {ECO:0000313|EMBL:ACU27070.1};
RN [1] {ECO:0000313|EMBL:ACU27070.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CL-073908 {ECO:0000313|EMBL:ACU27070.1};
RX PubMed=19402957; DOI=10.3201/eid1505.081286;
RA Tapparel C., Junier T., Gerlach D., Van-Belle S., Turin L., Cordey S.,
RA Muhlemann K., Regamey N., Aubert J.D., Soccal P.M., Eigenmann P.,
RA Zdobnov E., Kaiser L.;
RT "New respiratory enterovirus and recombinant rhinoviruses among circulating
RT picornaviruses.";
RL Emerg. Infect. Dis. 15:719-726(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 -!- SIMILARITY: Belongs to the picornaviruses polyprotein family.
CC {ECO:0000256|ARBA:ARBA00008303}.
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; EU840930; ACU27070.1; -; Genomic_RNA.
DR GO; GO:0019028; C:viral capsid; IEA:UniProtKB-KW.
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 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:ARBA00022804};
KW Virus entry into host cell {ECO:0000256|ARBA:ARBA00023296}.
FT DOMAIN 93..135
FT /note="Picornavirus capsid"
FT /evidence="ECO:0000259|Pfam:PF00073"
FT REGION 115..136
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 121..136
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 136
FT /evidence="ECO:0000313|EMBL:ACU27070.1"
SQ SEQUENCE 136 AA; 14737 MW; 75D9B1049F18DBAE CRC64;
MGAQVSRQNV GTHSTQNSVS NGSSLNYFNI NYFKDAASSG ASKLEFSQDP SKFTDPVKDV
LEKGIPTLQS PTVEACGYSD RIIQITRGDS TITSQDVANA VVGYGVWPHY LTPQDATAID
KPSHPDTSSN RFYTLE
//