ID I7AJF1_9ENTO Unreviewed; 211 AA.
AC I7AJF1;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE RecName: Full=Genome polyprotein {ECO:0000256|ARBA:ARBA00020107};
DE Flags: Fragment;
OS Poliovirus 1.
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC Picornavirales; Picornaviridae; Ensavirinae; Enterovirus; Enterovirus C.
OX NCBI_TaxID=12080 {ECO:0000313|EMBL:AFN85085.1};
RN [1] {ECO:0000313|EMBL:AFN85085.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=GHA-WES-JOM-03-001 {ECO:0000313|EMBL:AFN85085.1};
RX PubMed=22829642; DOI=10.1093/infdis/jis474;
RA Odoom J.K., Forrest L., Dunn G., Osei-Kwasi M., Obodai E., Arthur-Quarm J.,
RA Barnor J., Minor P.D., Martin J.;
RT "Interruption of poliovirus transmission in Ghana: molecular epidemiology
RT of wild-type 1 poliovirus isolated from 1995 to 2008.";
RL J. Infect. Dis. 206:1111-1120(2012).
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; JN393193; AFN85085.1; -; 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..43
FT /note="Peptidase C3"
FT /evidence="ECO:0000259|PROSITE:PS51874"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:AFN85085.1"
FT NON_TER 211
FT /evidence="ECO:0000313|EMBL:AFN85085.1"
SQ SEQUENCE 211 AA; 23483 MW; 70B468FAA04DB0DD CRC64;
MYNFPTRAGQ CGGVITCTGK VIGMHVGGNG SHGFAAALKR SYFTQSQGEI QWMRPSKEVG
YPVINAPSKT KLEPSAFHYV FEGVKEPAVL SKSDPRLKVD FEEAIFSKYV GNKITEVDVY
MKEAVDHYAG QLMSLDINTE QMCLEDAMYG TDGLEALDLT TSAGYPYVAL GKKKRDILNK
QTRDTKEMQR LLDTYGINLP LVTYVKDELR S
//
