ID F6ME03_9ENTO Unreviewed; 1217 AA.
AC F6ME03;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 27-JUL-2011, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE RecName: Full=Genome polyprotein {ECO:0000256|ARBA:ARBA00020107};
DE Flags: Fragment;
OS Coxsackievirus B4.
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC Picornavirales; Picornaviridae; Ensavirinae; Enterovirus; Enterovirus B.
OX NCBI_TaxID=12073 {ECO:0000313|EMBL:AEG47273.1};
RN [1] {ECO:0000313|EMBL:AEG47273.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=EPIHFMD-close contact-11 {ECO:0000313|EMBL:AEG47273.1};
RA Zha J.;
RT "Sequence from Human coxsackievirus B4 genomics including complete P1
RT domain, P2-A domain, P2-B domain and 5'region of P2-C domain.";
RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Acts as a primer for viral RNA replication and remains
CC covalently bound to viral genomic RNA. VPg is uridylylated prior to
CC priming replication into VPg-pUpU (By similarity). The oriI viral
CC genomic sequence may act as a template for this. The VPg-pUpU is then
CC used as primer on the genomic RNA poly(A) by the RNA-dependent RNA
CC polymerase to replicate the viral genome (By similarity). Following
CC genome release from the infecting virion in the cytoplasm, the VPg-RNA
CC linkage is probably removed by host TDP2 (By similarity). During the
CC late stage of the replication cycle, host TDP2 is excluded from sites
CC of viral RNA synthesis and encapsidation, allowing for the generation
CC of progeny virions. {ECO:0000256|ARBA:ARBA00024846}.
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; JF794741; AEG47273.1; -; mRNA.
DR MEROPS; N08.001; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0019028; C:viral capsid; IEA:InterPro.
DR GO; GO:0008233; F:peptidase activity; 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:0006508; P:proteolysis; 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 Gene3D; 2.40.10.10; Trypsin-like serine proteases; 2.
DR InterPro; IPR000081; Peptidase_C3.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR003138; Pico_P1A.
DR InterPro; IPR036988; Pico_P1A_sf.
DR InterPro; IPR002527; Pico_P2B.
DR InterPro; IPR001676; Picornavirus_capsid.
DR InterPro; IPR033703; Rhv-like.
DR InterPro; IPR029053; Viral_coat.
DR Pfam; PF02226; Pico_P1A; 1.
DR Pfam; PF00947; Pico_P2A; 1.
DR Pfam; PF01552; Pico_P2B; 1.
DR Pfam; PF00073; Rhv; 3.
DR SUPFAM; SSF88633; Positive stranded ssRNA viruses; 2.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
PE 2: Evidence at transcript level;
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 cytoplasm {ECO:0000256|ARBA:ARBA00023200};
KW Host gene expression shutoff by virus {ECO:0000256|ARBA:ARBA00022995};
KW Host-virus interaction {ECO:0000256|ARBA:ARBA00022581};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
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}; Protease {ECO:0000256|ARBA:ARBA00022670};
KW Thiol protease {ECO:0000256|ARBA:ARBA00022807};
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..782
FT /note="Picornavirus capsid"
FT /evidence="ECO:0000259|Pfam:PF00073"
FT DOMAIN 868..994
FT /note="Peptidase C3 picornavirus core protein 2A"
FT /evidence="ECO:0000259|Pfam:PF00947"
FT DOMAIN 999..1098
FT /note="Picornavirus 2B protein"
FT /evidence="ECO:0000259|Pfam:PF01552"
FT NON_TER 1217
FT /evidence="ECO:0000313|EMBL:AEG47273.1"
SQ SEQUENCE 1217 AA; 135819 MW; 48635C78BEE2CED8 CRC64;
MGAQVSTQKT GAHETSLSAT GNSIIHYTNI NYYKDAASNS ANRQDFTQDP SKFTEPVKDV
MIKSLPALNS PTVEECGYSD RVRSITLGNS TITTQECANV VVGYGVWPDY LSDEEATAED
QPTQPDVATC RFYTLNSVKW EMQSAGWWWK FPDALSEMGL FGQNMQYHYL GRSGYTIHVQ
CNASKFHQGC LLVVCVPEAE MGCTNVENAP AYGDLCGGET AKSFEQNAAT GETAVQTAVC
NAGMGVGVGN LTIYPHQWIN LRTNNSATIV MPYINSVPMD NMFRHNNFTL MIIPFAPLDY
VTGASSYIPI TVTVAPMSAE YNGLRLAGHQ GLPTMLTPGS TQFLTSDDFQ SPSAMPQFDV
TPEMNIPGQV RNLMEIAEVD SVVPLNNLKA NLMTMEAYRV QVRSTDEMGG QIFGFPLQPG
ASSVLQRTLL GEILNYYTHW SGSLKLTFVF CGSAMATGKF LLAYSPPGAG APDSRKNAML
GTHVIWDVGL QSSCVLCVPW ISQTHYRYVV DDKYTASGFI SCWYQTNVIV PAEAQKSCYI
RCFVSACNDF SVRMLRDTQF IKQENFYQGP TEEAVERAMG RVADTIARGP SNSEQIPALT
AVETGHTSQV DPSDTMQTRH VHNYHSRSES SVENFLCRSA CVIYIKYSSA ESNNLKRYAE
WVIDTRQVAQ LRRKMEMFTY IRCDMELTFV ITSHQEMSTA TNSDVPVQTH QIMYVPPGGP
VPTSVNDYVW QTSTNPSIFW TEGNAPPRMS IPFMSIGNAY TMFYDGWSNF SRDGIYGYNS
LNNMGTIYAR HVNDSSPGGL TSTIRIYFKP KHVKAYVPRP PRLCQYKKAK NVNFDVEAIT
AERASLITTG LQGQQAGAVY VGNYKIVNRH LATHTDWQSC VWEDYNRDLL VSTTTAHGCD
TIARCQCTTG VYYCASRHKH YPVSFEGPGL VEVQESEYYP KRYQSHVLLA AGFSEPGDCG
GILRCEHGVI GLVTMGGEGI VGFADVRDLL WLEDDAMEQG VKDYVEQLGN AFGSGFTNQI
CEQVNLLKES LVGLDSILEK SLKSLVKIIS ALVIVVRNHD DLITVTATLA LIGCTSSPWR
WLKQKVSQYY GIPMAERQNN GWLKKFTEMT NACKGMEWIA IKIQKFIEWL KVKILPEVRE
KHEFLNRLKQ LPLLESQIAT IEQSAPSQSD QEQLFSNVQY FAHYCRKYAP LYAAEAKRVF
SLEKKMSNYI QFKSKCR
//
