ID B7VBZ1_9ENTO Unreviewed; 217 AA.
AC B7VBZ1;
DT 10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT 10-FEB-2009, sequence version 1.
DT 27-MAR-2024, entry version 63.
DE SubName: Full=Polyprotein {ECO:0000313|EMBL:CAR78891.1};
DE Flags: Fragment;
OS Echovirus E30.
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC Picornavirales; Picornaviridae; Ensavirinae; Enterovirus; Enterovirus B.
OX NCBI_TaxID=41846 {ECO:0000313|EMBL:CAR78891.1};
RN [1] {ECO:0000313|EMBL:CAR78891.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Reims-2005 {ECO:0000313|EMBL:CAR78891.1};
RX PubMed=20381415; DOI=10.1016/j.jcv.2010.03.011;
RA Leveque N., Jacques J., Renois F., Antona D., Abely M., Chomel J.J.,
RA Andreoletti L.;
RT "Phylogenetic analysis of Echovirus 30 isolated during the 2005 outbreak in
RT France reveals existence of multiple lineages and suggests frequent
RT recombination events.";
RL J. Clin. Virol. 48:137-141(2010).
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 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Host
CC cytoplasm {ECO:0000256|ARBA:ARBA00004192}.
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DR EMBL; FM211739; CAR78891.1; -; 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: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; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR001205; RNA-dir_pol_C.
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 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Host cytoplasm {ECO:0000256|ARBA:ARBA00023200};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
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 Thiol protease {ECO:0000256|ARBA:ARBA00022807};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 1..29
FT /note="Peptidase C3"
FT /evidence="ECO:0000259|PROSITE:PS51874"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:CAR78891.1"
FT NON_TER 217
FT /evidence="ECO:0000313|EMBL:CAR78891.1"
SQ SEQUENCE 217 AA; 24038 MW; E3901E773787A8F2 CRC64;
LMSTGKVLGI HCCGNGHQGF SAALLRHYFN EEQGEIEFIE SSRDAGFPVI NTPSKTKLEP
SVFHQVFEGN KEPAVLRNGD PRLKANFEEA IFSKYIGNVN THVDEYMLEA VDHYAGQLAT
LDISTEPMKL EDAVYGTEGL EALDLTTSAG YPYVALGIKK RDILSKKTKD LTKLKECMDK
YGLNLPMVTY VKDELRSAEK VAKGKSRLIE ASSLTTQ
//
