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Database: UniProt
Entry: R4UZ48_9ENTO
LinkDB: R4UZ48_9ENTO
Original site: R4UZ48_9ENTO 
ID   R4UZ48_9ENTO            Unreviewed;       174 AA.
AC   R4UZ48;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   27-MAR-2024, entry version 36.
DE   RecName: Full=Genome polyprotein {ECO:0000256|ARBA:ARBA00020107};
DE   Flags: Fragment;
OS   Echovirus E6.
OC   Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC   Picornavirales; Picornaviridae; Ensavirinae; Enterovirus; Enterovirus B.
OX   NCBI_TaxID=12062 {ECO:0000313|EMBL:AGM34249.1};
RN   [1] {ECO:0000313|EMBL:AGM34249.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=MA3806NE08 {ECO:0000313|EMBL:AGM34249.1};
RA   Cabrerizo M., Trallero G., Simmonds P.;
RT   "Recombination and evolutionary dynamics of human echovirus 6.";
RL   Submitted (FEB-2013) 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   -!- SUBUNIT: Interacts with RNA-directed RNA polymerase.
CC       {ECO:0000256|ARBA:ARBA00011124}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Host
CC       cytoplasm {ECO:0000256|ARBA:ARBA00004192}.
CC   -!- SIMILARITY: Belongs to the picornaviruses polyprotein family.
CC       {ECO:0000256|ARBA:ARBA00008303}.
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DR   EMBL; KC679961; AGM34249.1; -; Genomic_RNA.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR   GO; GO:0003968; F:RNA-dependent RNA polymerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006351; P:DNA-templated transcription; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; 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; 4.10.880.10; Poliovirus 3D polymerase Domain 1 (Nucleotidyltransferase); 1.
DR   Gene3D; 2.40.10.10; Trypsin-like serine proteases; 1.
DR   InterPro; IPR043502; DNA/RNA_pol_sf.
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   InterPro; IPR001205; RNA-dir_pol_C.
DR   Pfam; PF00548; Peptidase_C3; 1.
DR   Pfam; PF00680; RdRP_1; 1.
DR   SUPFAM; SSF56672; DNA/RNA polymerases; 1.
DR   SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR   PROSITE; PS51874; PCV_3C_PRO; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Capsid protein {ECO:0000256|ARBA:ARBA00022706};
KW   Covalent protein-RNA linkage {ECO:0000256|ARBA:ARBA00022520};
KW   Host cytoplasm {ECO:0000256|ARBA:ARBA00023200};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695};
KW   Protease {ECO:0000256|ARBA:ARBA00022670};
KW   RNA-directed RNA polymerase {ECO:0000256|ARBA:ARBA00022484};
KW   T=pseudo3 icosahedral capsid protein {ECO:0000256|ARBA:ARBA00022706};
KW   Thiol protease {ECO:0000256|ARBA:ARBA00022807};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Virion {ECO:0000256|ARBA:ARBA00022706}.
FT   DOMAIN          1..38
FT                   /note="Peptidase C3"
FT                   /evidence="ECO:0000259|PROSITE:PS51874"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:AGM34249.1"
FT   NON_TER         174
FT                   /evidence="ECO:0000313|EMBL:AGM34249.1"
SQ   SEQUENCE   174 AA;  19016 MW;  6F93DBE1074B4B53 CRC64;
     YRAGQCGGVL MSTGKVLGIH VGGNGHQGFS AALLRHYFND EQGEIEFIES SKEAGFPIIN
     TPSKTKLEPS VFHHVFEGNK EPAVLRNGDP RLRANFEEAI FSKYIGNVNT HVDEYMLEAV
     DHYAGQLATL DISTEPMKLE DAVYGTEGLE ALDLTTSAGY PYVALGIKKR DIPS
//
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