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   05-MAY-2009, entry version 64.
DE   RecName: Full=Genome polyprotein;
DE   Contains:
DE     RecName: Full=Protein 3B;
DE              Short=P3B;
DE     AltName: Full=VPg;
DE   Contains:
DE     RecName: Full=Picornain 3C;
DE              EC=3.4.22.28;
DE     AltName: Full=Protease 3C;
DE              Short=P3C;
DE   Flags: Fragment;
OS   Echo 9 virus (EV-9) (Coxsackievirus A23).
OC   Viruses; ssRNA positive-strand viruses, no DNA stage; Picornavirales;
OC   Picornaviridae; Enterovirus.
OX   NCBI_TaxID=12060;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   MEDLINE=86144022; PubMed=3512851;
RA   Werner G., Rosenwirt B., Bauer E., Seifert J.-M., Werner F.-J.,
RA   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: Protein 3C is a cysteine protease that generates mature
CC       viral proteins from the precursor polyprotein. In addition to its
CC       proteolytic activity, it binds to viral RNA, and thus influences
CC       viral genome replication. RNA and substrate bind co-operatively to
CC       the protease (By similarity).
CC   -!- CATALYTIC ACTIVITY: Selective cleavage of Gln-|-Gly bond in the
CC       poliovirus polyprotein. In other picornavirus reactions Glu may be
CC       substituted for Gln, and Ser or Thr for Gly.
CC   -!- SUBCELLULAR LOCATION: Protein 3B: Virion (Potential).
CC   -!- SUBCELLULAR LOCATION: Picornain 3C: Host cytoplasm (Potential).
CC   -!- PTM: Specific enzymatic cleavages in vivo by the viral proteases
CC       yield a variety of precursors and mature proteins. Polyprotein
CC       processing intermediates are produced (By similarity).
CC   -!- PTM: VPg is uridylylated by the polymerase and is covalently
CC       linked to the 5'-end of genomic RNA. This uridylylated form acts
CC       as a nucleotide-peptide primer for the polymerase (By similarity).
CC   -!- SIMILARITY: Belongs to the picornaviruses polyprotein family.
CC   -!- SIMILARITY: Contains 1 peptidase C3 domain.
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DR   EMBL; M12165; AAA42979.1; -; Genomic_RNA.
DR   EMBL; M12167; AAA42978.1; -; Genomic_RNA.
DR   HSSP; P03300; 1L1N.
DR   MEROPS; C03.011; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0019012; C:virion; IEA:UniProtKB-KW.
DR   GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   GO; GO:0018144; P:RNA-protein covalent cross-linking; IEA:UniProtKB-KW.
DR   InterPro; IPR000199; Pept_C3_picorn.
DR   Pfam; PF00548; Peptidase_C3; 1.
DR   ProDom; PD001125; Pept_C3_picorn; 1.
PE   3: Inferred from homology;
KW   Covalent protein-RNA linkage; Cytoplasm; Hydrolase; Phosphoprotein;
KW   Protease; RNA-binding; Thiol protease; Virion.
FT   CHAIN         1     22       Protein 3B (Potential).
FT                                /FTId=PRO_0000039547.
FT   CHAIN        23    205       Picornain 3C (Potential).
FT                                /FTId=PRO_0000039548.
FT   ACT_SITE     62     62       For picornain 3C activity (Potential).
FT   ACT_SITE     93     93       For picornain 3C activity (Potential).
FT   ACT_SITE    169    169       For picornain 3C activity (Potential).
FT   SITE         22     23       Cleavage; by picornain 3C (Potential).
FT   MOD_RES       3      3       O-(5'-phospho-RNA)-tyrosine (By
FT                                similarity).
FT   NON_TER       1      1
FT   NON_TER     205    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
//