ID S6DKP8_9ENTO Unreviewed; 345 AA.
AC S6DKP8;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=Genome polyprotein {ECO:0000256|ARBA:ARBA00020107};
DE Flags: Fragment;
OS Coxsackievirus B5.
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC Picornavirales; Picornaviridae; Ensavirinae; Enterovirus; Enterovirus B.
OX NCBI_TaxID=12074 {ECO:0000313|EMBL:CCW33655.1};
RN [1] {ECO:0000313|EMBL:CCW33655.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CF641_FRA_79 {ECO:0000313|EMBL:CCW33655.1};
RX PubMed=24006446; DOI=10.1128/JVI.02075-13;
RA Henquell C., Mirand A., Richter J., Schuffenecker I., Bottiger B.,
RA Diedrich S., Terletskaia-Ladwig E., Christodoulou C., Peigue-Lafeuille H.,
RA Bailly J.L.;
RT "Phylogenetic Patterns of Human Coxsackievirus B5 Arise from Population
RT Dynamics between Two Genogroups and Reveal Evolutionary Factors of
RT Molecular Adaptation and Transmission.";
RL J. Virol. 87:12249-12259(2013).
RN [2] {ECO:0000313|EMBL:CCW33655.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CF641_FRA_79 {ECO:0000313|EMBL:CCW33655.1};
RA Bailly J.;
RL Submitted (MAR-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; HF948280; CCW33655.1; -; 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; 2.
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..130
FT /note="Peptidase C3"
FT /evidence="ECO:0000259|PROSITE:PS51874"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:CCW33655.1"
FT NON_TER 345
FT /evidence="ECO:0000313|EMBL:CCW33655.1"
SQ SEQUENCE 345 AA; 38109 MW; 4E2B06B5790DA56B CRC64;
NDQEVGVLDA KELVDKDGTN LELTLLKLNR NEKFRDIRGF LAREEVEVNE AVLAINTSKF
PNMYIPVGQV NDYGFLNLGG IPTKRMLMYN FPTRAGQCGG VLMSTGKVLG IHVGGNGHQG
FSAALLRHYF NEEQGEIEFI ESSKDAGFPV INTPSKTKLE PSVFHQVFEG NKEPAVLRNG
DPRLKANFEE AIFSKYIGNV NTHVDEYMQE AVDHYAGQLA TLDISTEPMK LEDAVYGTEG
LEALDLTTSA GYPYVALGIK KRDILSKKTK DLTKLKECMD KYGLNLPMVT YVKDELRSAE
KVAKGKSRLI EASSLNDSVA MRQTFGNLYK TFHLNPGIVT GSAVG
//
