POLG_ECHO9
ID POLG_ECHO9 Reviewed; 205 AA.
AC P08490;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1988, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Genome polyprotein;
DE Contains:
DE RecName: Full=Viral protein genome-linked;
DE Short=VPg;
DE AltName: Full=Protein 3B;
DE Short=P3B;
DE Contains:
DE RecName: Full=Protease 3C {ECO:0000255|PROSITE-ProRule:PRU01222};
DE EC=3.4.22.28 {ECO:0000255|PROSITE-ProRule:PRU01222};
DE AltName: Full=Picornain 3C {ECO:0000255|PROSITE-ProRule:PRU01222};
DE Short=P3C {ECO:0000255|PROSITE-ProRule:PRU01222};
DE Flags: Fragment;
OS Echo 9 virus (EV-9) (Coxsackievirus A23).
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC Picornavirales; Picornaviridae; Enterovirus; Enterovirus B.
OX NCBI_TaxID=12060;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=3512851; DOI=10.1128/jvi.57.3.1084-1093.1986;
RA Werner G., Rosenwirt B., Bauer E., Seifert J.-M., Werner F.-J., Besemer J.;
RT "Molecular cloning and sequence determination of the genomic regions
RT encoding protease and genome-linked protein of three picornaviruses.";
RL J. Virol. 57:1084-1093(1986).
CC -!- FUNCTION: [Viral protein genome-linked]: Acts as a primer for viral RNA
CC replication and remains covalently bound to viral genomic RNA. VPg is
CC uridylylated prior to priming replication into VPg-pUpU (By
CC similarity). The oriI viral genomic sequence may act as a template for
CC this. The VPg-pUpU is then used as primer on the genomic RNA poly(A) by
CC the RNA-dependent RNA polymerase to replicate the viral genome (By
CC similarity). Following genome release from the infecting virion in the
CC cytoplasm, the VPg-RNA linkage is probably removed by host TDP2 (By
CC similarity). During the late stage of the replication cycle, host TDP2
CC is excluded from sites of viral RNA synthesis and encapsidation,
CC allowing for the generation of progeny virions (By similarity).
CC {ECO:0000250|UniProtKB:P03300}.
CC -!- FUNCTION: [Protease 3C]: Major viral protease that mediates proteolytic
CC processing of the polyprotein (By similarity). Cleaves host EIF5B,
CC contributing to host translation shutoff (By similarity). Cleaves also
CC host PABPC1, contributing to host translation shutoff (By similarity).
CC {ECO:0000250|UniProtKB:P03300, ECO:0000250|UniProtKB:P03313}.
CC -!- CATALYTIC ACTIVITY: [Protease 3C]:
CC Reaction=Selective cleavage of Gln-|-Gly bond in the poliovirus
CC polyprotein. In other picornavirus reactions Glu may be substituted
CC for Gln, and Ser or Thr for Gly.; EC=3.4.22.28;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU01222};
CC -!- SUBUNIT: [Viral protein genome-linked]: Interacts with RNA-directed RNA
CC polymerase. {ECO:0000250|UniProtKB:P03300}.
CC -!- SUBCELLULAR LOCATION: [Viral protein genome-linked]: Virion
CC {ECO:0000250|UniProtKB:P03300}. Host cytoplasm
CC {ECO:0000250|UniProtKB:Q66478}.
CC -!- SUBCELLULAR LOCATION: [Protease 3C]: Host cytoplasm {ECO:0000305}.
CC -!- PTM: [Genome polyprotein]: Specific enzymatic cleavages in vivo by the
CC viral proteases yield processing intermediates and the mature proteins.
CC {ECO:0000250|UniProtKB:P03300}.
CC -!- PTM: [Viral protein genome-linked]: VPg is uridylylated by the
CC polymerase into VPg-pUpU. This acts as a nucleotide-peptide primer for
CC the genomic RNA replication. {ECO:0000250|UniProtKB:P03300}.
CC -!- SIMILARITY: Belongs to the picornaviruses polyprotein family.
CC {ECO:0000305}.
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DR EMBL; M12165; AAA42979.1; -; Genomic_RNA.
DR EMBL; M12167; AAA42978.1; -; Genomic_RNA.
DR SMR; P08490; -.
DR GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0039618; C:T=pseudo3 icosahedral viral capsid; IEA:UniProtKB-KW.
DR GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:UniProtKB-EC.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0018144; P:RNA-protein covalent cross-linking; IEA:UniProtKB-KW.
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 Gene3D; 2.40.10.10; -; 2.
DR InterPro; IPR044067; PCV_3C_PRO.
DR InterPro; IPR000199; Peptidase_C3A/C3B_picornavir.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR Pfam; PF00548; Peptidase_C3; 1.
DR SUPFAM; SSF50494; SSF50494; 1.
DR PROSITE; PS51874; PCV_3C_PRO; 1.
PE 3: Inferred from homology;
KW Autocatalytic cleavage; Capsid protein; Covalent protein-RNA linkage;
KW Host cytoplasm; Host-virus interaction; Hydrolase; Magnesium;
KW Phosphoprotein; Protease; RNA-binding;
KW T=pseudo3 icosahedral capsid protein; Thiol protease;
KW Viral attachment to host cell; Virion; Virus entry into host cell.
FT CHAIN <1..>205
FT /note="Genome polyprotein"
FT /id="PRO_0000449114"
FT CHAIN 1..22
FT /note="Viral protein genome-linked"
FT /id="PRO_0000039547"
FT CHAIN 23..205
FT /note="Protease 3C"
FT /id="PRO_0000039548"
FT DOMAIN 23..201
FT /note="Peptidase C3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01222"
FT ACT_SITE 62
FT /note="For protease 3C activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01222"
FT ACT_SITE 93
FT /note="For protease 3C activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01222"
FT ACT_SITE 169
FT /note="For protease 3C activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01222"
FT SITE 22..23
FT /note="Cleavage; by picornain 3C"
FT /evidence="ECO:0000250|UniProtKB:P03301"
FT MOD_RES 3
FT /note="O-(5'-phospho-RNA)-tyrosine"
FT /evidence="ECO:0000250|UniProtKB:P03300"
FT NON_TER 1
FT NON_TER 205
SQ SEQUENCE 205 AA; 22716 MW; 6C3F0490E5DAC78E CRC64;
GAYTGMPNKK PKVPTLRQAK VQGPAFEFAV AMMKRNASTV KTEYGEFTML GIYDRWAVLP
RHAKPGPSIL MNDQEVGVLD AKELVDKDGI NLELTLLKLN RNEKFRDIRG FLAREEVEVN
EAVLAINTSK FPNMYIPVGQ VTDYGFLNLG GTPTKRMLMY NFPTRAGQCG GVLMSTGKVL
GIHVGGNGHH GFSAALLRHY FNEEQ
