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[1]
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NUCLEOTIDE SEQUENCE [GENOMIC RNA].
STRAIN=P3/Leon/37;
PubMed=6324200 [NCBI, ExPASy, EBI, Israel, Japan]
Stanway G.,
Hughes P.J.,
Mountford R.C.,
Reeve P.,
Minor P.D.,
Schild G.C.,
Almond J.W.;
"Comparison of the complete nucleotide sequences of the genomes of the neurovirulent poliovirus P3/Leon/37 and its attenuated Sabin vaccine derivative P3/Leon 12a1b.";
Proc. Natl. Acad. Sci. U.S.A. 81:1539-1543(1984).
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[2]
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NUCLEOTIDE SEQUENCE [GENOMIC RNA].
STRAIN=P3/Leon 12A[1]B;
DOI=10.1093/nar/11.16.5629; PubMed=6310508 [NCBI, ExPASy, EBI, Israel, Japan]
Stanway G.,
Cann A.J.,
Hauptmann R.,
Hughes P.J.,
Clarke L.D.,
Mountford R.C.,
Minor P.D.,
Schild G.C.,
Almond J.W.;
"The nucleotide sequence of poliovirus type 3 Leon 12 a1b: comparison with poliovirus type 1.";
Nucleic Acids Res. 11:5629-5643(1983).
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[3]
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X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 1-878.
DOI=10.1016/S0960-9822(00)00176-7; PubMed=7820548 [NCBI, ExPASy, EBI, Israel, Japan]
Grant R.A.,
Hiremath C.N.,
Filman D.J.,
Syed R.,
Andries K.,
Hogle J.M.;
"Structures of poliovirus complexes with anti-viral drugs: implications for viral stability and drug design.";
Curr. Biol. 4:784-797(1994).
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[4]
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X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 1-878.
DOI=10.1107/S090744499401084X; PubMed=15299834 [NCBI, ExPASy, EBI, Israel, Japan]
Hiremath C.N.,
Grant R.A.,
Filman D.J.,
Hogle J.M.;
"Binding of the antiviral drug win51711 to the Sabin strain of type-3 poliovirus -structural comparison with drug-binding in rhinovirus-14.";
Acta Crystallogr. D 51:473-489(1995).
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- FUNCTION: Capsid proteins VP1, VP2, VP3 and VP4 form a closed capsid enclosing the viral positive strand RNA genome. VP4 lies on the inner surface of the protein shell formed by VP1, VP2 and VP3. All the three latter proteins contain a beta-sheet structure called beta-barrel jelly roll. Together they form an icosahedral capsid (T=3) composed of 60 copies of each VP1, VP2, and VP3, with a diameter of approximately 300 Angstroms. VP1 is situated at the 12 fivefold axes, whereas VP2 and VP3 are located at the quasi-sixfold axes. The interaction of five VP1 proteins in the fivefold axes results in a prominent protusion extending to about 25 Angstroms from the capsid shell. The resulting structure appears as a steep plateau encircled by a valley or cleft. This depression also termed canyon is the receptor binding site. The capsid interacts with human PVR at this site to provide virion attachment to target cell (By similarity).
- FUNCTION: VP0 precursor is a component of immature procapsids (By similarity).
- FUNCTION: Protein 2A is a cysteine protease that is responsible for the cleavage between the P1 and P2 regions. It cleaves the host translation initiation factor EIF4G1, in order to shut down the capped cellular mRNA transcription (By similarity).
- FUNCTION: Protein 2B affects membrane integrity and cause an increase in membrane permeability (By similarity).
- FUNCTION: Protein 2C associates with and induces structural rearrangements of intracellular membranes. It displays RNA-binding, nucleotide binding and NTPase activities (By similarity).
- FUNCTION: Protein 3A, via its hydrophobic domain, serves as membrane anchor. It also inhibits endoplasmic reticulum-to-Golgi transport (By similarity).
- FUNCTION: Protein 3C is a cysteine protease that generates mature viral proteins from the precursor polyprotein. In addition to its proteolytic activity, it binds to viral RNA, and thus influences viral genome replication. RNA and substrate bind co-operatively to the protease (By similarity).
- FUNCTION: RNA-directed RNA polymerase 3D-POL replicates genomic and antigenomic RNA by recognizing replications specific signals (By similarity).
- CATALYTIC ACTIVITY: Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1).
- CATALYTIC ACTIVITY: Selective cleavage of Tyr-|-Gly bond in the picornavirus polyprotein.
- CATALYTIC ACTIVITY: Selective cleavage of Gln-|-Gly bond in the poliovirus polyprotein. In other picornavirus reactions Glu may be substituted for Gln, and Ser or Thr for Gly.
- CATALYTIC ACTIVITY: NTP + H2O = NDP + phosphate.
- SUBCELLULAR LOCATION: Protein VP2: Virion. Cytoplasm (Potential).
- SUBCELLULAR LOCATION: Protein VP3: Virion. Cytoplasm (Potential).
- SUBCELLULAR LOCATION: Protein VP1: Virion. Cytoplasm (Potential).
- SUBCELLULAR LOCATION: Protein 2B: Cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side (Potential). Note=Probably localizes to the surface of intracellular membrane vesicles that are induced after virus infection as the site for viral RNA replication. These vesicles are derived from the endoplasmic reticulum (By similarity).
- SUBCELLULAR LOCATION: Protein 2C: Cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side (Potential). Note=Probably localizes to the surface of intracellular membrane vesicles that are induced after virus infection as the site for viral RNA replication. These vesicles are derived from the endoplasmic reticulum (By similarity).
- SUBCELLULAR LOCATION: Protein 3A: Cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side (Potential). Note=Probably localizes to the surface of intracellular membrane vesicles that are induced after virus infection as the site for viral RNA replication. These vesicles are derived from the endoplasmic reticulum (By similarity).
- SUBCELLULAR LOCATION: Protein 3B: Virion (Potential).
- SUBCELLULAR LOCATION: Picornain 3C: Cytoplasm (Potential).
- SUBCELLULAR LOCATION: RNA-directed RNA polymerase 3D-POL: Cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side (Potential). Note=Probably localizes to the surface of intracellular membrane vesicles that are induced after virus infection as the site for viral RNA replication. These vesicles are derived from the endoplasmic reticulum (By similarity).
- PTM: Specific enzymatic cleavages in vivo by the viral proteases yield a variety of precursors and mature proteins. Polyprotein processing intermediates such as VP0 which is a VP4-VP2 precursor are produced. During virion maturation, non-infectious particles are rendered infectious following cleavage of VP0. This maturation cleavage is followed by a conformational change of the particle (By similarity).
- PTM: VPg is covalently linked to the genomic RNA (By similarity).
- PTM: Myristoylation of VP4 is required during RNA encapsidation and formation of the mature virus particle (By similarity).
- MISCELLANEOUS: The sequence of strain Sabin vaccine P3/Leon/37 is shown.
- MISCELLANEOUS: The strain Sabin vaccine P3/Leon/37 is the progenitor of the strain Sabin vaccine P3/Leon 12a[1]b.
- SIMILARITY: Belongs to the picornaviruses polyprotein family.
- SIMILARITY: Contains 2 peptidase C3 domains [view classification].
- SIMILARITY: Contains 1 RdRp catalytic domain.
- SIMILARITY: Contains 1 SF3 helicase domain.
- WEB RESOURCE: Name=Virus Particle ExploreR db; Note= Icosahedral capsid structure in complex with antiviral compound R78206; URL="http://viperdb.scripps.edu/info_page.php?VDB=1vba";.
- WEB RESOURCE: Name=Virus Particle ExploreR db; Note= Icosahedral capsid structure in complex with antiviral compound R80633; URL="http://viperdb.scripps.edu/info_page.php?VDB=1vbb";.
- WEB RESOURCE: Name=Virus Particle ExploreR db; Note= Icosahedral capsid structure in complex with antiviral compound R77975; URL="http://viperdb.scripps.edu/info_page.php?VDB=1vbc";.
- WEB RESOURCE: Name=Virus Particle ExploreR db; Note= Icosahedral capsid structure of mutant F700L, F710L in complex with antiviral compound R78206; URL="http://viperdb.scripps.edu/info_page.php?VDB=1vbe";.
- WEB RESOURCE: Name=Virus Particle ExploreR db; Note= Icosahedral capsid structure in complex with antiviral compound WIN51711; URL="http://viperdb.scripps.edu/info_page.php?VDB=1piv";.
- WEB RESOURCE: Name=Virus Particle ExploreR db; Note= Icosahedral capsid structure; URL="http://viperdb.scripps.edu/info_page.php?VDB=1pvc";.
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Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms.
Distributed under the Creative Commons Attribution-NoDerivs License.
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| Sequence databases |
| EMBL |
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| PIR |
A93987; GNNY4P. |
| 3D structure databases |
| PDB |
| 1PIV; X-ray; 2.90 A; 1=578-878, 2=70-340, 3=341-578, 4=1-69. | [ExPASy / RCSB / EBI] |
| 1PVC; X-ray; 2.40 A; 1=578-878, 2=70-340, 3=-, 4=2-69. | [ExPASy / RCSB / EBI] |
| 1VBA; X-ray; 2.90 A; 1=579-878, 2=70-340, 3=341-575, 4=1-69. | [ExPASy / RCSB / EBI] |
| 1VBB; X-ray; 2.80 A; 1=579-878, 2=70-340, 3=341-575, 4=1-69. | [ExPASy / RCSB / EBI] |
| 1VBC; X-ray; 2.80 A; 1=579-878, 2=70-340, 3=341-575, 4=1-69. | [ExPASy / RCSB / EBI] |
| 1VBE; X-ray; 2.80 A; 1=579-878, 2=70-340, 3=341-575, 4=1-69. | [ExPASy / RCSB / EBI] |
Detailed list of linked structures. |
| PDBsum |
1PIV; -.
1PVC; -.
1VBA; -.
1VBB; -.
1VBC; -.
1VBE; -. |
| SMR |
P03302; 12-339, 13-340, 1562-1741, 1563-2206. |
| ModBase |
P03302. |
| Protein family/group databases |
| MEROPS |
C03.020; -. |
| Ontologies |
| GO |
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| Family and domain databases |
| InterPro |
IPR003593; AAA+_ATPase_core.
IPR004004; Helicase/Pol/Pept_Calicivir.
IPR000605; Helicase_SF3_ssDNA/RNA_vir.
IPR014759; Helicase_SF3_ssRNA_vir.
IPR014838; P3A.
IPR000199; Pept_C3_picorn.
IPR000081; Peptidase_C3.
IPR003138; Pico_P1A.
IPR002527; Pico_P2B.
IPR001676; Picornavirus_capsid.
IPR001205; RNA_pol_P3D.
IPR007094; RNA_pol_PSvir.
Graphical view of domain structure. |
| Pfam |
PF08727; P3A; 1.
PF00548; Peptidase_C3; 1.
PF02226; Pico_P1A; 1.
PF00947; Pico_P2A; 1.
PF01552; Pico_P2B; 1.
PF00680; RdRP_1; 1.
PF00073; Rhv; 3.
PF00910; RNA_helicase; 1.
Pfam graphical view of domain structure. |
| PRINTS |
PR00918; CALICVIRUSNS. |
| ProDom |
PD001125; Pept_C3_picorn; 1.
PD001306; Peptidase_C3_2; 1.
PD001274; Pico_P2B; 1.
[Domain structure / List of seq. sharing at least 1 domain] |
| SMART |
SM00382; AAA; 1.
SMART graphical view of domain structure. |
| PROSITE |
PS50507; RDRP_SSRNA_POS; 1.
PS51218; SF3_HELICASE_2; 1.
PROSITE graphical view of domain structure (profiles). |
| BLOCKS |
P03302. |
| ProtoNet |
P03302. |
| Other |
| LinkHub |
P03302; -. |
| UniRef |
View cluster of proteins with at least 50% / 90% / 100% identity. |
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