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P03300

- POLG_POL1M

UniProt

P03300 - POLG_POL1M

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Protein

Genome polyprotein

Gene
N/A
Organism
Poliovirus type 1 (strain Mahoney)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Capsid protein VP1: Forms an icosahedral capsid of pseudo T=3 symmetry with capsid proteins VP2 and VP3. The capsid is 300 Angstroms in diameter, composed of 60 copies of each capsid protein and enclosing the viral positive strand RNA genome. Capsid protein VP1 mainly forms the vertices of the capsid. Capsid protein VP1 interacts with host cell receptor PVR to provide virion attachment to target host epithelial cells. This attachment induces virion internalization predominantly through clathrin- and caveolin-independent endocytosis in Hela cells and through caveolin-mediated endocytosis in brain microvascular endothelial cells. Tyrosine kinases are probably involved in the entry process. Virus binding to PVR induces increased junctional permeability and rearrangement of junctional proteins. Modulation of endothelial tight junctions, as well as cytolytic infection of endothelial cells themselves, may result in loss of endothelial integrity which may help the virus to reach the CNS. After binding to its receptor, the capsid undergoes conformational changes. Capsid protein VP1 N-terminus (that contains an amphipathic alpha-helix) and capsid protein VP4 are externalized. Together, they shape a pore in the host membrane through which viral genome is translocated to host cell cytoplasm. After genome has been released, the channel shrinks.
Capsid protein VP2: Forms an icosahedral capsid of pseudo T=3 symmetry with capsid proteins VP2 and VP3. The capsid is 300 Angstroms in diameter, composed of 60 copies of each capsid protein and enclosing the viral positive strand RNA genome.
Capsid protein VP3: Forms an icosahedral capsid of pseudo T=3 symmetry with capsid proteins VP2 and VP3. The capsid is 300 Angstroms in diameter, composed of 60 copies of each capsid protein and enclosing the viral positive strand RNA genome.
Capsid protein VP4: Lies on the inner surface of the capsid shell. After binding to the host receptor, the capsid undergoes conformational changes. Capsid protein VP4 is released, Capsid protein VP1 N-terminus is externalized, and together, they shape a pore in the host membrane through which the viral genome is translocated into the host cell cytoplasm. After genome has been released, the channel shrinks (By similarity).By similarity
Capsid protein VP0: Component of immature procapsids, which is cleaved into capsid proteins VP4 and VP2 after maturation. Allows the capsid to remain inactive before the maturation step (By similarity).By similarity
Protein 2A: Cysteine protease that cleaves viral polyprotein and specific host proteins. It is responsible for the cleavage between the P1 and P2 regions, first cleavage occurring in the polyprotein. Cleaves also the host translation initiation factor EIF4G1, in order to shut down the capped cellular mRNA translation. Inhibits the host nucleus-cytoplasm protein and RNA trafficking by cleaving host members of the nuclear pores including NUP98, NUP62 and NUP153.
Protein 2B: Plays an essential role in the virus replication cycle by acting as a viroporin. Creates a pore in the host reticulum endoplasmic and as a consequence releases Ca2+ in the cytoplasm of infected cell. In turn, high levels of cyctoplasmic calcium may trigger membrane trafficking and transport of viral ER-associated proteins to viroplasms, sites of viral genome replication.
Protein 2C: Induces and associates with structural rearrangements of intracellular membranes. Triggers host autophagy by interacting with host BECN1 and thereby promotes viral replication. Participates in viral replication and interacts with host DHX9. Displays RNA-binding, nucleotide binding and NTPase activities. May play a role in virion morphogenesis and viral RNA encapsidation by interacting with the capsid protein VP3.
Protein 3AB: Localizes the viral replication complex to the surface of membranous vesicles. Together with protein 3CD binds the Cis-Active RNA Element (CRE) which is involved in RNA synthesis initiation. Acts as a cofactor to stimulate the activity of 3D polymerase, maybe through a nucleid acid chaperone activity.
Protein 3A: Localizes the viral replication complex to the surface of membranous vesicles. It inhibits host cell endoplasmic reticulum-to-Golgi apparatus transport and causes the dissassembly of the Golgi complex, possibly through GBF1 interaction. This would result in depletion of MHC, trail receptors and IFN receptors at the host cell surface.
Viral protein genome-linked: acts as a primer for viral RNA replication and remains covalently bound to viral genomic RNA. VPg is uridylylated prior to priming replication into VPg-pUpU. The oriI viral genomic sequence may act as a template for this. The VPg-pUpU is then used as primer on the genomic RNA poly(A) by the RNA-dependent RNA polymerase to replicate the viral genome. VPg may be removed in the cytoplasm by an unknown enzyme termed "unlinkase". VPg is not cleaved off virion genomes because replicated genomic RNA are encapsidated at the site of replication.
Protein 3CD: Is involved in the viral replication complex and viral polypeptide maturation. It exhibits protease activity with a specificity and catalytic efficiency that is different from protease 3C. Protein 3CD lacks polymerase activity. The 3C domain in the context of protein 3CD may have an RNA binding activity.
Protease 3C: May cleave host PABP and contribute to host translation shutoff.
RNA-directed RNA polymerase: Replicates the viral genomic RNA on the surface of intracellular membranes. May form linear arrays of subunits that propagate along a strong head-to-tail interaction called interface-I. Covalently attaches UMP to a tyrosine of VPg, which is used to prime RNA synthesis. The positive stranded RNA genome is first replicated at virus induced membranous vesicles, creating a dsRNA genomic replication form. This dsRNA is then used as template to synthesize positive stranded RNA genomes. ss+RNA genomes are either translated, replicated or encapsidated.

Catalytic activityi

Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1).PROSITE-ProRule annotation
Selective cleavage of Tyr-|-Gly bond in the picornavirus polyprotein.
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.
NTP + H2O = NDP + phosphate.

Enzyme regulationi

RNA-directed RNA polymerase: replication or transcription is subject to high level of random mutations by the nucleotide analog ribavirin.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei25 – 251Involved in the interaction with human RTN3By similarity
Sitei69 – 702Cleavage; by autolysisSequence Analysis
Sitei341 – 3422Cleavage; by Protease 3CSequence Analysis
Sitei881 – 8822Cleavage; by Protease 2ASequence Analysis
Active sitei901 – 9011For Protease 2A activityBy similarity
Active sitei919 – 9191For Protease 2A activityBy similarity
Active sitei990 – 9901For Protease 2A activityBy similarity
Sitei1030 – 10312Cleavage; by Protease 3CSequence Analysis
Sitei1127 – 11282Cleavage; by Protease 3CSequence Analysis
Sitei1456 – 14572Cleavage; by Protease 3CSequence Analysis
Sitei1543 – 15442Cleavage; by Protease 3CSequence Analysis
Sitei1565 – 15662Cleavage; by Protease 3CSequence Analysis
Active sitei1605 – 16051For Protease 3C activitySequence Analysis
Active sitei1636 – 16361For Protease 3C activitySequence Analysis
Active sitei1712 – 17121For Protease 3C activitySequence Analysis
Sitei1748 – 17492Cleavage; by Protease 3CSequence Analysis
Active sitei2076 – 20761For RdRp activity1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi1256 – 12638ATPPROSITE-ProRule annotation

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. cysteine-type endopeptidase activity Source: InterPro
  3. ion channel activity Source: UniProtKB-KW
  4. RNA binding Source: UniProtKB-KW
  5. RNA-directed RNA polymerase activity Source: UniProtKB-KW
  6. RNA helicase activity Source: InterPro
  7. structural molecule activity Source: InterPro

GO - Biological processi

  1. endocytosis involved in viral entry into host cell Source: UniProtKB-KW
  2. induction by virus of host autophagy Source: UniProtKB
  3. pore formation by virus in membrane of host cell Source: UniProtKB-KW
  4. pore-mediated entry of viral genome into host cell Source: UniProtKB-KW
  5. protein oligomerization Source: UniProtKB-KW
  6. RNA-protein covalent cross-linking Source: UniProtKB-KW
  7. suppression by virus of host mRNA export from nucleus Source: UniProtKB
  8. suppression by virus of host RIG-I activity by RIG-I proteolysis Source: UniProtKB
  9. suppression by virus of host translation initiation factor activity Source: UniProtKB
  10. transcription, DNA-templated Source: InterPro
  11. viral RNA genome replication Source: InterPro
  12. virion attachment to host cell Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Helicase, Hydrolase, Ion channel, Nucleotidyltransferase, Protease, RNA-directed RNA polymerase, Thiol protease, Transferase, Viral ion channel

Keywords - Biological processi

Activation of host autophagy by virus, Eukaryotic host gene expression shutoff by virus, Eukaryotic host translation shutoff by virus, Host gene expression shutoff by virus, Host mRNA suppression by virus, Host-virus interaction, Inhibition of host innate immune response by virus, Inhibition of host mRNA nuclear export by virus, Inhibition of host RIG-I by virus, Inhibition of host RLR pathway by virus, Ion transport, Pore-mediated penetration of viral genome into host cell, Transport, Viral attachment to host cell, Viral immunoevasion, Viral penetration into host cytoplasm, Viral RNA replication, Virus endocytosis by host, Virus entry into host cell

Keywords - Ligandi

ATP-binding, Nucleotide-binding, RNA-binding

Protein family/group databases

MEROPSiC03.001.

Names & Taxonomyi

Protein namesi
Recommended name:
Genome polyprotein
Cleaved into the following 17 chains:
Alternative name(s):
VP4-VP2
Alternative name(s):
P1A
Virion protein 4
Alternative name(s):
P1B
Virion protein 2
Alternative name(s):
P1C
Virion protein 3
Alternative name(s):
P1D
Virion protein 1
Protease 2A (EC:3.4.22.29)
Short name:
P2A
Alternative name(s):
Picornain 2A
Protein 2A
Protein 2B
Short name:
P2B
Protein 2C (EC:3.6.1.15)
Short name:
P2C
Protein 3A
Short name:
P3A
Alternative name(s):
Protein 3B
Short name:
P3B
Protease 3C (EC:3.4.22.28)
Short name:
P3C
Alternative name(s):
3D polymerase
Short name:
3Dpol
Protein 3D
Short name:
3D
OrganismiPoliovirus type 1 (strain Mahoney)
Taxonomic identifieri12081 [NCBI]
Taxonomic lineageiVirusesssRNA positive-strand viruses, no DNA stagePicornaviralesPicornaviridaeEnterovirusEnterovirus C
Virus hostiHomo sapiens (Human) [TaxID: 9606]
ProteomesiUP000000356: Genome

Subcellular locationi

Chain Protein 2B : Host cytoplasmic vesicle membrane Curated; Peripheral membrane protein Curated; Cytoplasmic side Curated
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.
Chain Protein 2C : Host cytoplasmic vesicle membrane Curated; Peripheral membrane protein Curated; Cytoplasmic side Curated
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.
Chain Protein 3A : Host cytoplasmic vesicle membrane Curated; Peripheral membrane protein Curated; Cytoplasmic side Curated
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.
Chain Protein 3AB : Host cytoplasmic vesicle membrane Curated; Peripheral membrane protein Curated; Cytoplasmic side Curated
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.
Chain Protein 3CD : Host cytoplasmic vesicle membrane Curated; Peripheral membrane protein Curated; Cytoplasmic side Curated
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.
Chain RNA-directed RNA polymerase : Host cytoplasmic vesicle membrane Curated; Peripheral membrane protein Curated; Cytoplasmic side Curated
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.

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini2 – 15201519CytoplasmicSequence AnalysisAdd
BLAST
Intramembranei1521 – 153616Sequence AnalysisAdd
BLAST
Topological domaini1537 – 2209673CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. host cell cytoplasmic vesicle Source: UniProtKB-KW
  2. integral to membrane of host cell Source: UniProtKB-KW
  3. membrane Source: UniProtKB-KW
  4. T=pseudo3 icosahedral viral capsid Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Capsid protein, Host cytoplasm, Host cytoplasmic vesicle, Host membrane, Membrane, T=pseudo3 icosahedral capsid protein, Virion

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi2 – 21G → A: 100% loss of myristoylation. Impaired viral assembly. 1 Publication
Mutagenesisi3 – 31A → D: 50% loss of myristoylation. Severe reduction in specific infectivity. 1 Publication
Mutagenesisi3 – 31A → G, L or V: No effect on myristoylation and virus growth. 1 Publication
Mutagenesisi3 – 31A → H: No effect on myristoylation. Severe reduction in specific infectivity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed; by hostBy similarity
Chaini2 – 22092208Genome polyproteinPRO_0000424686Add
BLAST
Chaini2 – 881880P1PRO_0000424687Add
BLAST
Chaini2 – 341340Capsid protein VP0Sequence AnalysisPRO_0000424688Add
BLAST
Chaini2 – 6968Capsid protein VP4Sequence AnalysisPRO_0000040080Add
BLAST
Chaini70 – 341272Capsid protein VP2Sequence AnalysisPRO_0000040081Add
BLAST
Chaini342 – 579238Capsid protein VP3Sequence AnalysisPRO_0000040082Add
BLAST
Chaini580 – 881302Capsid protein VP1Sequence AnalysisPRO_0000040083Add
BLAST
Chaini882 – 1456575P2PRO_0000424689Add
BLAST
Chaini882 – 1030149Protease 2ASequence AnalysisPRO_0000040084Add
BLAST
Chaini1031 – 112797Protein 2BSequence AnalysisPRO_0000040085Add
BLAST
Chaini1128 – 1456329Protein 2CSequence AnalysisPRO_0000040086Add
BLAST
Chaini1457 – 2209753P3PRO_0000424690Add
BLAST
Chaini1457 – 1565109Protein 3ABSequence AnalysisPRO_0000424691Add
BLAST
Chaini1457 – 154387Protein 3ASequence AnalysisPRO_0000424692Add
BLAST
Chaini1544 – 156522Viral protein genome-linkedSequence AnalysisPRO_0000040088Add
BLAST
Chaini1566 – 2209644Protein 3CDSequence AnalysisPRO_0000424693Add
BLAST
Chaini1566 – 1747182Protease 3CSequence AnalysisPRO_0000040089Add
BLAST
Chaini1748 – 2209462RNA-directed RNA polymerasePRO_0000040090Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi2 – 21N-myristoyl glycine; by host3 Publications
Modified residuei1546 – 15461O-(5'-phospho-RNA)-tyrosine
Modified residuei1546 – 15461O-UMP-tyrosine; transient2 Publications

Post-translational modificationi

Capsid protein VP0: Myristoylation is required for the formation of pentamers during virus assembly. Further assembly of 12 pentamers and a molecule of genomic RNA generates the provirion (By similarity).By similarity
Genome polyprotein: Specific enzymatic cleavages in vivo by the viral proteases yield processing intermediates and the mature proteins.
Capsid protein VP0: During virion maturation, immature virions are rendered infectious following cleavage of VP0 into VP4 and VP2. This maturation seems to be an autocatalytic event triggered by the presence of RNA in the capsid and it is followed by a conformational change infectious virion.
Viral protein genome-linked: VPg is uridylylated by the polymerase into VPg-pUpU. This acts as a nucleotide-peptide primer for the genomic RNA replication.

Keywords - PTMi

Covalent protein-RNA linkage, Lipoprotein, Myristate, Phosphoprotein

Miscellaneous databases

PMAP-CutDBP03299.

Interactioni

Subunit structurei

Capsid protein VP1: Interacts with capsid protein VP0, and capsid protein VP3 to form heterotrimeric protomers. Five protomers subsequently associate to form pentamers which serve as building blocks for the capsid. Interacts with human PVR. Interacts with capsid protein VP4 in the mature capsid. Capsid protein VP0: interacts with capsid protein VP1 and capsid protein VP3 to form heterotrimeric protomers. Five protomers subsequently associate to form pentamers which serve as building blocks for the capsid. Capsid protein VP2: Interacts with capsid protein VP1 and capsid protein VP3 in the mature capsid. Capsid protein VP3: interacts with capsid protein VP0 and capsid protein VP1 to form heterotrimeric protomers. Five protomers subsequently associate to form pentamers which serve as building blocks for the capsid. Interacts with capsid protein VP4 in the mature capsid. Capsid protein VP4: Interacts with capsid protein VP1 and capsid protein VP3. Protein 2C: interacts with cellular Vimentin/VIM and BECN1; these interactions play important roles in the viral replication (By similarity). Protein 2C: interacts with capsid protein VP3; this interaction may be important for virion morphogenesis. Protein 2C: interacts with host BECN1 and DHX9 and possibly presents an hexameric ring structure with 6-fold symmetry characteristic of AAA+ ATPases. Protein 2C: N-terminus interacts with human RTN3. This interaction is important for viral replication (By similarity). Protein 3AB: interacts with protein 3CD. Protein 3A: homodimerizes and interacts with host GBF1. Viral protein genome-linked: interacts with RNA-directed RNA polymerase. Protein 3CD: interacts with protein 3AB and with RNA-directed RNA polymerase. RNA-directed RNA polymerase: interacts with Viral protein genome-linked and with protein 3CD.By similarity7 Publications

Structurei

Secondary structure

1
2209
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi3 – 75Combined sources
Beta strandi17 – 237Combined sources
Beta strandi26 – 294Combined sources
Beta strandi33 – 353Combined sources
Helixi36 – 383Combined sources
Helixi51 – 544Combined sources
Beta strandi57 – 593Combined sources
Helixi66 – 694Combined sources
Helixi74 – 763Combined sources
Beta strandi83 – 875Combined sources
Beta strandi90 – 967Combined sources
Beta strandi100 – 1023Combined sources
Helixi103 – 1053Combined sources
Helixi113 – 1153Combined sources
Helixi126 – 1283Combined sources
Beta strandi138 – 1414Combined sources
Beta strandi147 – 1515Combined sources
Helixi153 – 1553Combined sources
Helixi159 – 1679Combined sources
Beta strandi168 – 18013Combined sources
Beta strandi187 – 19711Combined sources
Beta strandi206 – 2105Combined sources
Helixi214 – 2174Combined sources
Helixi220 – 2223Combined sources
Beta strandi227 – 2293Combined sources
Beta strandi236 – 2383Combined sources
Helixi247 – 2493Combined sources
Turni250 – 2534Combined sources
Helixi256 – 2616Combined sources
Beta strandi262 – 2687Combined sources
Turni269 – 2713Combined sources
Beta strandi273 – 2797Combined sources
Beta strandi284 – 2885Combined sources
Turni290 – 2923Combined sources
Beta strandi296 – 30813Combined sources
Beta strandi311 – 3133Combined sources
Beta strandi315 – 33218Combined sources
Turni349 – 3524Combined sources
Beta strandi364 – 3663Combined sources
Beta strandi380 – 3834Combined sources
Helixi384 – 3885Combined sources
Turni400 – 4045Combined sources
Helixi406 – 4094Combined sources
Beta strandi411 – 4144Combined sources
Beta strandi423 – 4286Combined sources
Turni430 – 4323Combined sources
Turni434 – 4385Combined sources
Helixi440 – 4456Combined sources
Beta strandi448 – 4536Combined sources
Beta strandi455 – 4617Combined sources
Beta strandi470 – 4767Combined sources
Beta strandi478 – 4803Combined sources
Helixi486 – 4894Combined sources
Beta strandi492 – 4987Combined sources
Beta strandi500 – 5023Combined sources
Beta strandi504 – 5096Combined sources
Beta strandi514 – 5218Combined sources
Helixi524 – 5263Combined sources
Beta strandi530 – 5378Combined sources
Beta strandi547 – 55711Combined sources
Beta strandi562 – 5665Combined sources
Beta strandi570 – 5723Combined sources
Beta strandi586 – 5894Combined sources
Beta strandi594 – 5963Combined sources
Helixi626 – 6283Combined sources
Helixi636 – 6383Combined sources
Helixi652 – 6543Combined sources
Helixi656 – 6605Combined sources
Beta strandi664 – 67310Combined sources
Beta strandi685 – 6884Combined sources
Beta strandi693 – 6953Combined sources
Helixi696 – 7016Combined sources
Beta strandi704 – 72118Combined sources
Beta strandi723 – 7253Combined sources
Beta strandi733 – 7397Combined sources
Helixi752 – 7554Combined sources
Beta strandi757 – 7593Combined sources
Beta strandi761 – 7655Combined sources
Beta strandi771 – 7755Combined sources
Beta strandi780 – 7867Combined sources
Beta strandi790 – 7934Combined sources
Beta strandi796 – 7994Combined sources
Turni801 – 8044Combined sources
Helixi812 – 8143Combined sources
Beta strandi818 – 8236Combined sources
Beta strandi832 – 85019Combined sources
Beta strandi860 – 8634Combined sources
Helixi1478 – 14847Combined sources
Helixi1487 – 149610Combined sources
Beta strandi1546 – 15505Combined sources
Beta strandi1556 – 15583Combined sources
Helixi1560 – 15645Combined sources
Helixi1567 – 157913Combined sources
Beta strandi1580 – 15856Combined sources
Beta strandi1588 – 159710Combined sources
Beta strandi1599 – 16035Combined sources
Helixi1604 – 16063Combined sources
Beta strandi1610 – 16145Combined sources
Beta strandi1617 – 162812Combined sources
Beta strandi1634 – 164512Combined sources
Helixi1652 – 16543Combined sources
Beta strandi1662 – 16698Combined sources
Beta strandi1671 – 16744Combined sources
Beta strandi1677 – 169216Combined sources
Beta strandi1695 – 170511Combined sources
Beta strandi1715 – 17184Combined sources
Beta strandi1721 – 17299Combined sources
Beta strandi1734 – 17385Combined sources
Helixi1741 – 17444Combined sources
Beta strandi1750 – 17567Combined sources
Turni1757 – 17615Combined sources
Turni1763 – 17664Combined sources
Helixi1770 – 17723Combined sources
Turni1777 – 17815Combined sources
Beta strandi1786 – 17883Combined sources
Beta strandi1792 – 17943Combined sources
Helixi1802 – 18076Combined sources
Helixi1820 – 183415Combined sources
Turni1835 – 18373Combined sources
Helixi1845 – 18506Combined sources
Beta strandi1860 – 18623Combined sources
Turni1866 – 18727Combined sources
Helixi1875 – 18784Combined sources
Turni1881 – 18844Combined sources
Helixi1887 – 18959Combined sources
Beta strandi1902 – 19065Combined sources
Beta strandi1910 – 19123Combined sources
Helixi1913 – 19175Combined sources
Beta strandi1923 – 19264Combined sources
Helixi1929 – 194820Combined sources
Turni1952 – 19554Combined sources
Helixi1962 – 19654Combined sources
Turni1966 – 19683Combined sources
Helixi1969 – 19724Combined sources
Beta strandi1975 – 19784Combined sources
Beta strandi1981 – 19844Combined sources
Helixi1985 – 19884Combined sources
Helixi1991 – 200313Combined sources
Turni2004 – 20063Combined sources
Helixi2007 – 20104Combined sources
Helixi2011 – 20177Combined sources
Beta strandi2018 – 20236Combined sources
Beta strandi2026 – 20327Combined sources
Beta strandi2036 – 20383Combined sources
Helixi2041 – 206020Combined sources
Beta strandi2061 – 20633Combined sources
Helixi2066 – 20683Combined sources
Beta strandi2070 – 20745Combined sources
Beta strandi2077 – 20848Combined sources
Helixi2088 – 209710Combined sources
Beta strandi2102 – 21043Combined sources
Turni2105 – 21073Combined sources
Turni2116 – 21183Combined sources
Beta strandi2124 – 21285Combined sources
Beta strandi2130 – 21323Combined sources
Beta strandi2135 – 21395Combined sources
Helixi2142 – 21498Combined sources
Beta strandi2151 – 21533Combined sources
Helixi2155 – 21573Combined sources
Helixi2158 – 216912Combined sources
Helixi2170 – 21723Combined sources
Helixi2174 – 218411Combined sources
Helixi2188 – 21914Combined sources
Helixi2198 – 220811Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1AL2X-ray2.901580-881[»]
270-341[»]
3342-579[»]
42-69[»]
1AR6X-ray2.901580-881[»]
270-341[»]
3342-579[»]
42-69[»]
1AR7X-ray2.901580-881[»]
270-341[»]
3342-579[»]
42-69[»]
1AR8X-ray2.901580-881[»]
270-341[»]
3342-579[»]
42-69[»]
1AR9X-ray2.901580-881[»]
270-341[»]
3342-579[»]
42-69[»]
1ASJX-ray2.901580-881[»]
270-341[»]
3342-579[»]
42-69[»]
1DGIelectron microscopy22.001599-881[»]
274-341[»]
3342-576[»]
42-69[»]
1FPTX-ray3.00P665-682[»]
1HXSX-ray2.201580-881[»]
270-341[»]
3342-578[»]
42-69[»]
1L1NX-ray2.10A/B1566-1748[»]
1NG7NMR-A/B1457-1515[»]
1NN8electron microscopy15.001580-881[»]
270-341[»]
3342-576[»]
42-69[»]
1PO1X-ray2.901580-881[»]
270-341[»]
3342-579[»]
42-69[»]
1PO2X-ray2.901580-881[»]
270-341[»]
3342-579[»]
42-69[»]
1POVX-ray2.8002-341[»]
1580-881[»]
3342-579[»]
1RA6X-ray2.00A1749-2209[»]
1RA7X-ray2.35A1749-2209[»]
1RAJX-ray2.50A1817-2209[»]
1RDRX-ray2.40A1749-2209[»]
1TQLX-ray2.30A1749-2209[»]
1VBDX-ray2.901580-881[»]
270-341[»]
3342-579[»]
42-69[»]
1XYRelectron microscopy11.001650-881[»]
297-333[»]
3391-572[»]
5342-353[»]
6355-390[»]
782-95[»]
8621-631[»]
2BBLNMR-A1544-1565[»]
2BBPNMR-A1544-1565[»]
2IJDX-ray3.401/21566-2208[»]
2IJFX-ray3.00A1749-2208[»]
2ILYX-ray2.60A1749-2208[»]
2ILZX-ray2.50A1749-2208[»]
2IM0X-ray2.25A1749-2208[»]
2IM1X-ray2.50A1749-2208[»]
2IM2X-ray2.35A1749-2208[»]
2IM3X-ray2.60A1749-2208[»]
2PLVX-ray2.881580-881[»]
270-341[»]
3342-579[»]
42-69[»]
3EPCelectron microscopy8.001599-881[»]
274-341[»]
3342-576[»]
42-69[»]
3IYBelectron microscopy-1647-881[»]
497-341[»]
3IYCelectron microscopy-1647-881[»]
497-341[»]
3J3Oelectron microscopy11.101580-881[»]
270-341[»]
3342-579[»]
42-69[»]
3J3Pelectron microscopy9.101580-881[»]
270-341[»]
3342-579[»]
3J48electron microscopy5.501580-881[»]
270-341[»]
3342-579[»]
3J69electron microscopy4.801580-881[»]
270-341[»]
3342-579[»]
42-69[»]
3J6Aelectron microscopy6.501580-881[»]
270-341[»]
3342-579[»]
42-69[»]
3OL7X-ray2.70A/E/I/M1749-2209[»]
4DCDX-ray1.69A1566-1748[»]
4K4SX-ray2.40A/E1749-2209[»]
4K4TX-ray2.75A/E1749-2209[»]
4K4UX-ray2.85A/E1749-2209[»]
4K4VX-ray2.63A/E1749-2209[»]
4K4WX-ray2.69A/E1749-2209[»]
4NLOX-ray2.20A1749-2209[»]
4NLPX-ray2.20A1749-2209[»]
4NLQX-ray2.30A1749-2209[»]
4NLRX-ray2.00A1749-2209[»]
4NLSX-ray2.00A1749-2209[»]
4NLTX-ray2.50A1749-2209[»]
4NLUX-ray2.10A1749-2209[»]
4NLVX-ray2.30A1749-2209[»]
4NLWX-ray2.10A1749-2209[»]
4NLXX-ray2.60A1749-2209[»]
4NLYX-ray2.30A1749-2209[»]
ProteinModelPortaliP03300.
SMRiP03300. Positions 2-579, 599-1030, 1457-1515, 1566-2209.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP03300.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini882 – 1031150Peptidase C3 1Add
BLAST
Domaini1232 – 1388157SF3 helicasePROSITE-ProRule annotationAdd
BLAST
Domaini1566 – 1731166Peptidase C3 2Add
BLAST
Domaini1975 – 2090116RdRp catalyticPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni580 – 60021Amphipatic alpha-helixSequence AnalysisAdd
BLAST
Regioni1457 – 147923DisorderedAdd
BLAST

Sequence similaritiesi

Belongs to the picornaviruses polyprotein family.Curated
Contains 2 peptidase C3 domains.Curated
Contains 1 RdRp catalytic domain.PROSITE-ProRule annotation
Contains 1 SF3 helicase domain.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Family and domain databases

Gene3Di2.60.120.20. 3 hits.
4.10.80.10. 2 hits.
InterProiIPR003593. AAA+_ATPase.
IPR000605. Helicase_SF3_ssDNA/RNA_vir.
IPR014759. Helicase_SF3_ssRNA_vir.
IPR027417. P-loop_NTPase.
IPR014838. P3A.
IPR000081. Peptidase_C3.
IPR000199. Peptidase_C3A/C3B_picornavir.
IPR003138. Pico_P1A.
IPR002527. Pico_P2B.
IPR001676. Picornavirus_capsid.
IPR001205. RNA-dir_pol_C.
IPR007094. RNA-dir_pol_PSvirus.
IPR009003. Trypsin-like_Pept_dom.
IPR029053. Viral_coat.
[Graphical view]
PfamiPF08727. P3A. 1 hit.
PF00548. Peptidase_C3. 1 hit.
PF02226. Pico_P1A. 1 hit.
PF00947. Pico_P2A. 1 hit.
PF01552. Pico_P2B. 1 hit.
PF00680. RdRP_1. 1 hit.
PF00073. Rhv. 3 hits.
PF00910. RNA_helicase. 1 hit.
[Graphical view]
ProDomiPD001306. Peptidase_C3. 1 hit.
PD649346. Pico_P2B. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTiSM00382. AAA. 1 hit.
[Graphical view]
SUPFAMiSSF50494. SSF50494. 2 hits.
SSF52540. SSF52540. 1 hit.
SSF89043. SSF89043. 1 hit.
PROSITEiPS50507. RDRP_SSRNA_POS. 1 hit.
PS51218. SF3_HELICASE_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P03300-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MGAQVSSQKV GAHENSNRAY GGSTINYTTI NYYRDSASNA ASKQDFSQDP
60 70 80 90 100
SKFTEPIKDV LIKTAPMLNS PNIEACGYSD RVLQLTLGNS TITTQEAANS
110 120 130 140 150
VVAYGRWPEY LRDSEANPVD QPTEPDVAAC RFYTLDTVSW TKESRGWWWK
160 170 180 190 200
LPDALRDMGL FGQNMYYHYL GRSGYTVHVQ CNASKFHQGA LGVFAVPEMC
210 220 230 240 250
LAGDSNTTTM HTSYQNANPG EKGGTFTGTF TPDNNQTSPA RRFCPVDYLL
260 270 280 290 300
GNGTLLGNAF VFPHQIINLR TNNCATLVLP YVNSLSIDSM VKHNNWGIAI
310 320 330 340 350
LPLAPLNFAS ESSPEIPITL TIAPMCCEFN GLRNITLPRL QGLPVMNTPG
360 370 380 390 400
SNQYLTADNF QSPCALPEFD VTPPIDIPGE VKNMMELAEI DTMIPFDLSA
410 420 430 440 450
TKKNTMEMYR VRLSDKPHTD DPILCLSLSP ASDPRLSHTM LGEILNYYTH
460 470 480 490 500
WAGSLKFTFL FCGFMMATGK LLVSYAPPGA DPPKKRKEAM LGTHVIWDIG
510 520 530 540 550
LQSSCTMVVP WISNTTYRQT IDDSFTEGGY ISVFYQTRIV VPLSTPREMD
560 570 580 590 600
ILGFVSACND FSVRLLRDTT HIEQKALAQG LGQMLESMID NTVRETVGAA
610 620 630 640 650
TSRDALPNTE ASGPTHSKEI PALTAVETGA TNPLVPSDTV QTRHVVQHRS
660 670 680 690 700
RSESSIESFF ARGACVTIMT VDNPASTTNK DKLFAVWKIT YKDTVQLRRK
710 720 730 740 750
LEFFTYSRFD MELTFVVTAN FTETNNGHAL NQVYQIMYVP PGAPVPEKWD
760 770 780 790 800
DYTWQTSSNP SIFYTYGTAP ARISVPYVGI SNAYSHFYDG FSKVPLKDQS
810 820 830 840 850
AALGDSLYGA ASLNDFGILA VRVVNDHNPT KVTSKIRVYL KPKHIRVWCP
860 870 880 890 900
RPPRAVAYYG PGVDYKDGTL TPLSTKDLTT YGFGHQNKAV YTAGYKICNY
910 920 930 940 950
HLATQDDLQN AVNVMWSRDL LVTESRAQGT DSIARCNCNA GVYYCESRRK
960 970 980 990 1000
YYPVSFVGPT FQYMEANNYY PARYQSHMLI GHGFASPGDC GGILRCHHGV
1010 1020 1030 1040 1050
IGIITAGGEG LVAFSDIRDL YAYEEEAMEQ GITNYIESLG AAFGSGFTQQ
1060 1070 1080 1090 1100
ISDKITELTN MVTSTITEKL LKNLIKIISS LVIITRNYED TTTVLATLAL
1110 1120 1130 1140 1150
LGCDASPWQW LRKKACDVLE IPYVIKQGDS WLKKFTEACN AAKGLEWVSN
1160 1170 1180 1190 1200
KISKFIDWLK EKIIPQARDK LEFVTKLRQL EMLENQISTI HQSCPSQEHQ
1210 1220 1230 1240 1250
EILFNNVRWL SIQSKRFAPL YAVEAKRIQK LEHTINNYIQ FKSKHRIEPV
1260 1270 1280 1290 1300
CLLVHGSPGT GKSVATNLIA RAIAERENTS TYSLPPDPSH FDGYKQQGVV
1310 1320 1330 1340 1350
IMDDLNQNPD GADMKLFCQM VSTVEFIPPM ASLEEKGILF TSNYVLASTN
1360 1370 1380 1390 1400
SSRISPPTVA HSDALARRFA FDMDIQVMNE YSRDGKLNMA MATEMCKNCH
1410 1420 1430 1440 1450
QPANFKRCCP LVCGKAIQLM DKSSRVRYSI DQITTMIINE RNRRSNIGNC
1460 1470 1480 1490 1500
MEALFQGPLQ YKDLKIDIKT SPPPECINDL LQAVDSQEVR DYCEKKGWIV
1510 1520 1530 1540 1550
NITSQVQTER NINRAMTILQ AVTTFAAVAG VVYVMYKLFA GHQGAYTGLP
1560 1570 1580 1590 1600
NKKPNVPTIR TAKVQGPGFD YAVAMAKRNI VTATTSKGEF TMLGVHDNVA
1610 1620 1630 1640 1650
ILPTHASPGE SIVIDGKEVE ILDAKALEDQ AGTNLEITII TLKRNEKFRD
1660 1670 1680 1690 1700
IRPHIPTQIT ETNDGVLIVN TSKYPNMYVP VGAVTEQGYL NLGGRQTART
1710 1720 1730 1740 1750
LMYNFPTRAG QCGGVITCTG KVIGMHVGGN GSHGFAAALK RSYFTQSQGE
1760 1770 1780 1790 1800
IQWMRPSKEV GYPIINAPSK TKLEPSAFHY VFEGVKEPAV LTKNDPRLKT
1810 1820 1830 1840 1850
DFEEAIFSKY VGNKITEVDE YMKEAVDHYA GQLMSLDINT EQMCLEDAMY
1860 1870 1880 1890 1900
GTDGLEALDL STSAGYPYVA MGKKKRDILN KQTRDTKEMQ KLLDTYGINL
1910 1920 1930 1940 1950
PLVTYVKDEL RSKTKVEQGK SRLIEASSLN DSVAMRMAFG NLYAAFHKNP
1960 1970 1980 1990 2000
GVITGSAVGC DPDLFWSKIP VLMEEKLFAF DYTGYDASLS PAWFEALKMV
2010 2020 2030 2040 2050
LEKIGFGDRV DYIDYLNHSH HLYKNKTYCV KGGMPSGCSG TSIFNSMINN
2060 2070 2080 2090 2100
LIIRTLLLKT YKGIDLDHLK MIAYGDDVIA SYPHEVDASL LAQSGKDYGL
2110 2120 2130 2140 2150
TMTPADKSAT FETVTWENVT FLKRFFRADE KYPFLIHPVM PMKEIHESIR
2160 2170 2180 2190 2200
WTKDPRNTQD HVRSLCLLAW HNGEEEYNKF LAKIRSVPIG RALLLPEYST

LYRRWLDSF
Length:2,209
Mass (Da):246,540
Last modified:January 23, 2007 - v3
Checksum:iDF1754F87F2E97D6
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti242 – 26423RFCPV…FVFPH → SSARWITSLEMARCWGMPLC SA in CAA24446. (PubMed:6272282)CuratedAdd
BLAST
Sequence conflicti287 – 2871I → L in CAA24446. (PubMed:6272282)Curated
Sequence conflicti309 – 3091A → V in CAA24446. (PubMed:6272282)Curated
Sequence conflicti420 – 4223DDP → AAS in CAA24446. (PubMed:6272282)Curated
Sequence conflicti464 – 4641F → S in CAA24446. (PubMed:6272282)Curated
Sequence conflicti515 – 5151T → S in CAA24446. (PubMed:6272282)Curated
Sequence conflicti855 – 8562AV → QL in CAA24446. (PubMed:6272282)Curated
Sequence conflicti972 – 9721A → V in CAA24446. (PubMed:6272282)Curated
Sequence conflicti985 – 9851A → E in CAA24446. (PubMed:6272282)Curated
Sequence conflicti1140 – 11412NA → QR in CAA24446. (PubMed:6272282)Curated
Sequence conflicti1619 – 16191V → A in CAA24446. (PubMed:6272282)Curated
Sequence conflicti1626 – 16272AL → VF in CAA24446. (PubMed:6272282)Curated
Sequence conflicti1635 – 16351L → F in CAA24446. (PubMed:6272282)Curated
Sequence conflicti1682 – 16821G → R in CAA24446. (PubMed:6272282)Curated
Sequence conflicti1722 – 17309VIGMHVGGN → SSGCMLVD in CAA24446. (PubMed:6272282)Curated
Sequence conflicti1743 – 17431Y → L in CAA24446. (PubMed:6272282)Curated
Sequence conflicti1752 – 17521Q → P in CAA24446. (PubMed:6272282)Curated
Sequence conflicti1759 – 17602EV → DA in CAA24446. (PubMed:6272282)Curated
Sequence conflicti1840 – 18401T → I in CAA24446. (PubMed:6272282)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
V01149 Genomic RNA. Translation: CAA24461.1.
V01148 Genomic RNA. Translation: CAA24446.1.
PIRiA03898. GNNY2P.
A93258. GNNY1P.
RefSeqiNP_041277.1. NC_002058.3.

Genome annotation databases

GeneIDi919920.

Cross-referencesi

Web resourcesi

Virus Particle ExploreR db

Icosahedral capsid structure associated with cellular receptor

Virus Particle ExploreR db

Icosahedral capsid structure associated with cellular receptor

Virus Particle ExploreR db

Icosahedral capsid structure in complex with R80633, an inhibitor of viral replication

Virus Particle ExploreR db

Icosahedral capsid structure in complex with R77975, an inhibitor of viral replication

Virus Particle ExploreR db

Icosahedral empty capsid structure

Virus Particle ExploreR db

Icosahedral capsid structure complexed with R78206

Virus Particle ExploreR db

Icosahedral capsid structure

Virus Particle ExploreR db

Icosahedral capsid structure of 135S cell entry intermediate

Virus Particle ExploreR db

Icosahedral capsid structure

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
V01149 Genomic RNA. Translation: CAA24461.1 .
V01148 Genomic RNA. Translation: CAA24446.1 .
PIRi A03898. GNNY2P.
A93258. GNNY1P.
RefSeqi NP_041277.1. NC_002058.3.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1AL2 X-ray 2.90 1 580-881 [» ]
2 70-341 [» ]
3 342-579 [» ]
4 2-69 [» ]
1AR6 X-ray 2.90 1 580-881 [» ]
2 70-341 [» ]
3 342-579 [» ]
4 2-69 [» ]
1AR7 X-ray 2.90 1 580-881 [» ]
2 70-341 [» ]
3 342-579 [» ]
4 2-69 [» ]
1AR8 X-ray 2.90 1 580-881 [» ]
2 70-341 [» ]
3 342-579 [» ]
4 2-69 [» ]
1AR9 X-ray 2.90 1 580-881 [» ]
2 70-341 [» ]
3 342-579 [» ]
4 2-69 [» ]
1ASJ X-ray 2.90 1 580-881 [» ]
2 70-341 [» ]
3 342-579 [» ]
4 2-69 [» ]
1DGI electron microscopy 22.00 1 599-881 [» ]
2 74-341 [» ]
3 342-576 [» ]
4 2-69 [» ]
1FPT X-ray 3.00 P 665-682 [» ]
1HXS X-ray 2.20 1 580-881 [» ]
2 70-341 [» ]
3 342-578 [» ]
4 2-69 [» ]
1L1N X-ray 2.10 A/B 1566-1748 [» ]
1NG7 NMR - A/B 1457-1515 [» ]
1NN8 electron microscopy 15.00 1 580-881 [» ]
2 70-341 [» ]
3 342-576 [» ]
4 2-69 [» ]
1PO1 X-ray 2.90 1 580-881 [» ]
2 70-341 [» ]
3 342-579 [» ]
4 2-69 [» ]
1PO2 X-ray 2.90 1 580-881 [» ]
2 70-341 [» ]
3 342-579 [» ]
4 2-69 [» ]
1POV X-ray 2.80 0 2-341 [» ]
1 580-881 [» ]
3 342-579 [» ]
1RA6 X-ray 2.00 A 1749-2209 [» ]
1RA7 X-ray 2.35 A 1749-2209 [» ]
1RAJ X-ray 2.50 A 1817-2209 [» ]
1RDR X-ray 2.40 A 1749-2209 [» ]
1TQL X-ray 2.30 A 1749-2209 [» ]
1VBD X-ray 2.90 1 580-881 [» ]
2 70-341 [» ]
3 342-579 [» ]
4 2-69 [» ]
1XYR electron microscopy 11.00 1 650-881 [» ]
2 97-333 [» ]
3 391-572 [» ]
5 342-353 [» ]
6 355-390 [» ]
7 82-95 [» ]
8 621-631 [» ]
2BBL NMR - A 1544-1565 [» ]
2BBP NMR - A 1544-1565 [» ]
2IJD X-ray 3.40 1/2 1566-2208 [» ]
2IJF X-ray 3.00 A 1749-2208 [» ]
2ILY X-ray 2.60 A 1749-2208 [» ]
2ILZ X-ray 2.50 A 1749-2208 [» ]
2IM0 X-ray 2.25 A 1749-2208 [» ]
2IM1 X-ray 2.50 A 1749-2208 [» ]
2IM2 X-ray 2.35 A 1749-2208 [» ]
2IM3 X-ray 2.60 A 1749-2208 [» ]
2PLV X-ray 2.88 1 580-881 [» ]
2 70-341 [» ]
3 342-579 [» ]
4 2-69 [» ]
3EPC electron microscopy 8.00 1 599-881 [» ]
2 74-341 [» ]
3 342-576 [» ]
4 2-69 [» ]
3IYB electron microscopy - 1 647-881 [» ]
4 97-341 [» ]
3IYC electron microscopy - 1 647-881 [» ]
4 97-341 [» ]
3J3O electron microscopy 11.10 1 580-881 [» ]
2 70-341 [» ]
3 342-579 [» ]
4 2-69 [» ]
3J3P electron microscopy 9.10 1 580-881 [» ]
2 70-341 [» ]
3 342-579 [» ]
3J48 electron microscopy 5.50 1 580-881 [» ]
2 70-341 [» ]
3 342-579 [» ]
3J69 electron microscopy 4.80 1 580-881 [» ]
2 70-341 [» ]
3 342-579 [» ]
4 2-69 [» ]
3J6A electron microscopy 6.50 1 580-881 [» ]
2 70-341 [» ]
3 342-579 [» ]
4 2-69 [» ]
3OL7 X-ray 2.70 A/E/I/M 1749-2209 [» ]
4DCD X-ray 1.69 A 1566-1748 [» ]
4K4S X-ray 2.40 A/E 1749-2209 [» ]
4K4T X-ray 2.75 A/E 1749-2209 [» ]
4K4U X-ray 2.85 A/E 1749-2209 [» ]
4K4V X-ray 2.63 A/E 1749-2209 [» ]
4K4W X-ray 2.69 A/E 1749-2209 [» ]
4NLO X-ray 2.20 A 1749-2209 [» ]
4NLP X-ray 2.20 A 1749-2209 [» ]
4NLQ X-ray 2.30 A 1749-2209 [» ]
4NLR X-ray 2.00 A 1749-2209 [» ]
4NLS X-ray 2.00 A 1749-2209 [» ]
4NLT X-ray 2.50 A 1749-2209 [» ]
4NLU X-ray 2.10 A 1749-2209 [» ]
4NLV X-ray 2.30 A 1749-2209 [» ]
4NLW X-ray 2.10 A 1749-2209 [» ]
4NLX X-ray 2.60 A 1749-2209 [» ]
4NLY X-ray 2.30 A 1749-2209 [» ]
ProteinModelPortali P03300.
SMRi P03300. Positions 2-579, 599-1030, 1457-1515, 1566-2209.
ModBasei Search...
MobiDBi Search...

Chemistry

BindingDBi P03300.
ChEMBLi CHEMBL5127.

Protein family/group databases

MEROPSi C03.001.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 919920.

Miscellaneous databases

EvolutionaryTracei P03300.
PMAP-CutDB P03299.

Family and domain databases

Gene3Di 2.60.120.20. 3 hits.
4.10.80.10. 2 hits.
InterProi IPR003593. AAA+_ATPase.
IPR000605. Helicase_SF3_ssDNA/RNA_vir.
IPR014759. Helicase_SF3_ssRNA_vir.
IPR027417. P-loop_NTPase.
IPR014838. P3A.
IPR000081. Peptidase_C3.
IPR000199. Peptidase_C3A/C3B_picornavir.
IPR003138. Pico_P1A.
IPR002527. Pico_P2B.
IPR001676. Picornavirus_capsid.
IPR001205. RNA-dir_pol_C.
IPR007094. RNA-dir_pol_PSvirus.
IPR009003. Trypsin-like_Pept_dom.
IPR029053. Viral_coat.
[Graphical view ]
Pfami PF08727. P3A. 1 hit.
PF00548. Peptidase_C3. 1 hit.
PF02226. Pico_P1A. 1 hit.
PF00947. Pico_P2A. 1 hit.
PF01552. Pico_P2B. 1 hit.
PF00680. RdRP_1. 1 hit.
PF00073. Rhv. 3 hits.
PF00910. RNA_helicase. 1 hit.
[Graphical view ]
ProDomi PD001306. Peptidase_C3. 1 hit.
PD649346. Pico_P2B. 1 hit.
[Graphical view ] [Entries sharing at least one domain ]
SMARTi SM00382. AAA. 1 hit.
[Graphical view ]
SUPFAMi SSF50494. SSF50494. 2 hits.
SSF52540. SSF52540. 1 hit.
SSF89043. SSF89043. 1 hit.
PROSITEi PS50507. RDRP_SSRNA_POS. 1 hit.
PS51218. SF3_HELICASE_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
  2. "Molecular cloning of poliovirus cDNA and determination of the complete nucleotide sequence of the viral genome."
    Racaniello V.R., Baltimore D.
    Proc. Natl. Acad. Sci. U.S.A. 78:4887-4891(1981) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
  3. "Identification of the initiation site of poliovirus polyprotein synthesis."
    Dorner A.J., Dorner L.F., Larsen G.R., Wimmer E., Anderson C.W.
    J. Virol. 42:1017-1028(1982) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-69.
  4. "The genome-linked protein of picornaviruses. VII. Genetic mapping of poliovirus VPg by protein and RNA sequence studies."
    Kitamura N., Adler C.J., Rothberg P.G., Martinko J., Nathenson S.G., Wimmer E.
    Cell 21:295-302(1980) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 1539-1574, FUNCTION (VIRAL PROTEIN GENOME-LINKED).
  5. "Protein is linked to the 5' end of poliovirus RNA by a phosphodiester linkage to tyrosine."
    Ambros V., Baltimore D.
    J. Biol. Chem. 253:5263-5266(1978) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION (VIRAL PROTEIN GENOME-LINKED), COVALENT RNA-LINKAGE AT TYR-1546 PF VPG.
  6. "An attempt to unify the structure of polymerases."
    Delarue M., Poch O., Tordo N., Moras D., Argos P.
    Protein Eng. 3:461-467(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACTIVE SITE (RNA-DIRECTED RNA POLYMERASE).
  7. "Myristoylation is important at multiple stages in poliovirus assembly."
    Moscufo N., Simons J., Chow M.
    J. Virol. 65:2372-2380(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: MYRISTOYLATION AT GLY-2, MUTAGENESIS OF ALA-3.
  8. "A Gly1 to Ala substitution in poliovirus capsid protein VP0 blocks its myristoylation and prevents viral assembly."
    Marc D., Girard M., van der Werf S.
    J. Gen. Virol. 72:1151-1157(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: MYRISTOYLATION AT GLY-2, MUTAGENESIS OF GLY-2.
  9. "Poliovirus protein 2C has ATPase and GTPase activities."
    Rodriguez P.L., Carrasco L.
    J. Biol. Chem. 268:8105-8110(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION (PROTEIN 2C).
  10. "Interaction of poliovirus polypeptide 3CDpro with the 5' and 3' termini of the poliovirus genome. Identification of viral and cellular cofactors needed for efficient binding."
    Harris K.S., Xiang W., Alexander L., Lane W.S., Paul A.V., Wimmer E.
    J. Biol. Chem. 269:27004-27014(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION OF PROTEIN 3AB WITH PROTEIN 3CD.
  11. "Poliovirus 2A proteinase cleaves directly the eIF-4G subunit of eIF-4F complex."
    Ventoso I., MacMillan S.E., Hershey J.W., Carrasco L.
    FEBS Lett. 435:79-83(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION (PROTEASE 2A).
  12. "Biochemical and genetic studies of the VPg uridylylation reaction catalyzed by the RNA polymerase of poliovirus."
    Paul A.V., Peters J., Mugavero J., Yin J., van Boom J.H., Wimmer E.
    J. Virol. 77:891-904(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION (PROTEIN 3B), COVALENT RNA-LINKAGE AT TYR-1546 OF VPG, URIDYLYLATION AT TYR-1546.
  13. "Towards an understanding of the poliovirus replication complex: the solution structure of the soluble domain of the poliovirus 3A protein."
    Strauss D.M., Glustrom L.W., Wuttke D.S.
    J. Mol. Biol. 330:225-234(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: HOMODIMERIZATION (PROTEIN 3A).
  14. "Poliovirus protein 3A binds and inactivates LIS1, causing block of membrane protein trafficking and deregulation of cell division."
    Kondratova A.A., Neznanov N., Kondratov R.V., Gudkov A.V.
    Cell Cycle 4:1403-1410(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT (PROTEIN 3A), CAUTION.
  15. "Inhibition of cellular protein secretion by picornaviral 3A proteins."
    Choe S.S., Dodd D.A., Kirkegaard K.
    Virology 337:18-29(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION (PROTEIN 3A).
  16. "Intramolecular and intermolecular uridylylation by poliovirus RNA-dependent RNA polymerase."
    Richards O.C., Spagnolo J.F., Lyle J.M., Vleck S.E., Kuchta R.D., Kirkegaard K.
    J. Virol. 80:7405-7415(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION (VIRAL PROTEIN GENOME-LINKED), COVALENT RNA-LINKAGE AT TYR-1546 OF VPG, URIDYLYLATION AT TYR-1546.
  17. "Effects of picornavirus 3A Proteins on Protein Transport and GBF1-dependent COP-I recruitment."
    Wessels E., Duijsings D., Lanke K.H., van Dooren S.H., Jackson C.L., Melchers W.J., van Kuppeveld F.J.
    J. Virol. 80:11852-11860(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION OF PROTEIN 3A WITH HOST GBF1.
  18. "Reticulon 3 binds the 2C protein of enterovirus 71 and is required for viral replication."
    Tang W.-F., Yang S.-Y., Wu B.-W., Jheng J.-R., Chen Y.-L., Shih C.-H., Lin K.-H., Lai H.-C., Tang P., Horng J.-T.
    J. Biol. Chem. 282:5888-5898(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION OF PROTEIN 2C WITH HUMAN RTN3.
  19. "Hijacking components of the cellular secretory pathway for replication of poliovirus RNA."
    Belov G.A., Altan-Bonnet N., Kovtunovych G., Jackson C.L., Lippincott-Schwartz J., Ehrenfeld E.
    J. Virol. 81:558-567(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION (PROTEIN 3A).
  20. Cited for: FUNCTION (CAPSID PROTEIN VP1), FUNCTION (CAPSID PROTEIN VP2), FUNCTION (CAPSID PROTEIN VP3).
  21. "Poliovirus entry into human brain microvascular cells requires receptor-induced activation of SHP-2."
    Coyne C.B., Kim K.S., Bergelson J.M.
    EMBO J. 26:4016-4028(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION (CAPSID PROTEIN VP1), FUNCTION (CAPSID PROTEIN VP2), FUNCTION (CAPSID PROTEIN VP3).
    Strain: Sabin 2.
  22. "Characterization of protein-protein interactions critical for poliovirus replication: analysis of 3AB and VPg binding to the RNA-dependent RNA polymerase."
    Strauss D.M., Wuttke D.S.
    J. Virol. 81:6369-6378(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION OF PROTEIN 3B WITH PROTEIN 3D.
  23. "Membrane topography of the hydrophobic anchor sequence of poliovirus 3A and 3AB proteins and the functional effect of 3A/3AB membrane association upon RNA replication."
    Fujita K., Krishnakumar S.S., Franco D., Paul A.V., London E., Wimmer E.
    Biochemistry 46:5185-5199(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: TOPOLOGY (PROTEIN 3A AND PROTEIN 3AB).
  24. "Cleavage of poly(A)-binding protein by poliovirus 3C proteinase inhibits viral internal ribosome entry site-mediated translation."
    Bonderoff J.M., Larey J.L., Lloyd R.E.
    J. Virol. 82:9389-9399(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION (PROTEASE 3C).
  25. "New (fluorescent) light on poliovirus entry."
    Bergelson J.M.
    Trends Microbiol. 16:44-47(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION (CAPSID PROTEIN VP1), FUNCTION (CAPSID PROTEIN VP2), FUNCTION (CAPSID PROTEIN VP3).
  26. "Functional analysis of picornavirus 2B proteins: effects on calcium homeostasis and intracellular protein trafficking."
    de Jong A.S., de Mattia F., Van Dommelen M.M., Lanke K., Melchers W.J., Willems P.H., van Kuppeveld F.J.
    J. Virol. 82:3782-3790(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW (PROTEIN 2B).
  27. "Picornavirus genome replication. Identification of the surface of the poliovirus (PV) 3C dimer that interacts with PV 3Dpol during VPg uridylylation and construction of a structural model for the PV 3C2-3Dpol complex."
    Shen M., Reitman Z.J., Zhao Y., Moustafa I., Wang Q., Arnold J.J., Pathak H.B., Cameron C.E.
    J. Biol. Chem. 283:875-888(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION (PROTEASE 3C).
  28. "RNA nuclear export is blocked by poliovirus 2A protease and is concomitant with nucleoporin cleavage."
    Castello A., Izquierdo J.M., Welnowska E., Carrasco L.
    J. Cell Sci. 122:3799-3809(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION (PROTEIN 2A).
  29. "Poliovirus 2C protein forms homo-oligomeric structures required for ATPase activity."
    Adams P., Kandiah E., Effantin G., Steven A.C., Ehrenfeld E.
    J. Biol. Chem. 284:22012-22021(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION (PROTEIN 2C).
  30. Cited for: REVIEW (RNA-DIRECTED RNA POLYMERASE).
  31. "Direct interaction between two viral proteins, the nonstructural protein 2C and the capsid protein VP3, is required for enterovirus morphogenesis."
    Liu Y., Wang C., Mueller S., Paul A.V., Wimmer E., Jiang P.
    PLoS Pathog. 6:E1001066-E1001066(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION OF CAPSID PROTEIN VP3 WITH PROTEIN 2C, FUNCTION OF CAPSID PROTEIN VP3.
  32. "NMR solution structure of poliovirus uridylyated peptide linked to the genome (VPgpU)."
    Schein C.H., Oezguen N., van der Heden van Noort G.J., Filippov D.V., Paul A., Kumar E., Braun W.
    Peptides 31:1441-1448(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION (VIRAL PROTEIN GENOME-LINKED).
  33. "The twenty-nine amino acid C-terminal cytoplasmic domain of poliovirus 3AB is critical for nucleic acid chaperone activity."
    Gangaramani D.R., Eden E.L., Shah M., Destefano J.J.
    RNA Biol. 7:820-829(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION (PROTEIN 3AB).
  34. Cited for: TOPOLOGY (PROTEIN 2B).
  35. "Analysis of poliovirus protein 3A interactions with viral and cellular proteins in infected cells."
    Teterina N.L., Pinto Y., Weaver J.D., Jensen K.S., Ehrenfeld E.
    J. Virol. 85:4284-4296(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT OF PROTEIN 3A AND PROTEIN 3AB.
  36. "Alanine scanning of poliovirus 2CATPase reveals new genetic evidence that capsid protein/2CATPase interactions are essential for morphogenesis."
    Wang C., Jiang P., Sand C., Paul A.V., Wimmer E.
    J. Virol. 86:9964-9975(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION (PROTEIN 2C).
  37. "Investigation of a predicted N-terminal amphipathic alpha-helix using atomistic molecular dynamics simulation of a complete prototype poliovirus virion."
    Roberts J.A., Kuiper M.J., Thorley B.R., Smooker P.M., Hung A.
    J. Mol. Graph. Model. 38:165-173(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION OF N-TERMINUS (CAPSID PROTEIN VP1).
  38. "RNA transfer from poliovirus 135S particles across membranes is mediated by long umbilical connectors."
    Strauss M., Levy H.C., Bostina M., Filman D.J., Hogle J.M.
    J. Virol. 87:3903-3914(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION (CAPSID PROTEIN VP1 AND CAPSID PROTEIN VP4).
  39. "Surface for catalysis by poliovirus RNA-dependent RNA polymerase."
    Wang J., Lyle J.M., Bullitt E.
    J. Mol. Biol. 425:2529-2540(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: MULTIMERIZATION (RNA-DIRECTED RNA POLYMERASE).
  40. "Three-dimensional structure of poliovirus at 2.9-A resolution."
    Hogle J.M., Chow M., Filman D.J.
    Science 229:1358-1365(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 1-881.
  41. "Structural factors that control conformational transitions and serotype specificity in type 3 poliovirus."
    Filman D.J., Syed R., Chow M., Macadam A.J., Minor P.D., Hogle J.M.
    EMBO J. 8:1567-1579(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.88 ANGSTROMS) OF 2-880.
  42. "Role and mechanism of the maturation cleavage of VP0 in poliovirus assembly: structure of the empty capsid assembly intermediate at 2.9 A resolution."
    Basavappa R., Syed R., Flore O., Icenogle J.P., Filman D.J., Hogle J.M.
    Protein Sci. 3:1651-1669(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 2-880.
  43. "Structures of poliovirus complexes with anti-viral drugs: implications for viral stability and drug design."
    Grant R.A., Hiremath C.N., Filman D.J., Syed R., Andries K., Hogle J.M.
    Curr. Biol. 4:784-797(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 1-881.
  44. Cited for: STRUCTURE BY ELECTRON MICROSCOPY (2.0 ANGSTROMS) OF 1-881, MYRISTOYLATION AT GLY-2.
  45. "Complexes of poliovirus serotypes with their common cellular receptor, CD155."
    He Y., Mueller S., Chipman P.R., Bator C.M., Peng X., Bowman V.D., Mukhopadhyay S., Wimmer E., Kuhn R.J., Rossmann M.G.
    J. Virol. 77:4827-4835(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY ELECTRON MICROSCOPY (15.0 ANGSTROMS) OF 2-881.
  46. "The structure of the poliovirus 135S cell entry intermediate at 10-angstrom resolution reveals the location of an externalized polypeptide that binds to membranes."
    Bubeck D., Filman D.J., Cheng N., Steven A.C., Hogle J.M., Belnap D.M.
    J. Virol. 79:7745-7755(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY ELECTRON MICROSCOPY (11.0 ANGSTROMS) OF 97-880.
  47. "Crystal structure of CD155 and electron microscopic studies of its complexes with polioviruses."
    Zhang P., Mueller S., Morais M.C., Bator C.M., Bowman V.D., Hafenstein S., Wimmer E., Rossmann M.G.
    Proc. Natl. Acad. Sci. U.S.A. 105:18284-18289(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY ELECTRON MICROSCOPY (8.0 ANGSTROMS) OF 2-881.
  48. "Catching a virus in the act of RNA release: a novel poliovirus uncoating intermediate characterized by cryo-electron microscopy."
    Levy H.C., Bostina M., Filman D.J., Hogle J.M.
    J. Virol. 84:4426-4441(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY ELECTRON MICROSCOPY OF 97-341 AND 647-881.

Entry informationi

Entry nameiPOLG_POL1M
AccessioniPrimary (citable) accession number: P03300
Secondary accession number(s): P03299
, Q84879, Q84880, Q89679
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: November 26, 2014
This is version 171 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

Caution

Protein 3A: Has been proposed to interact with host LIS1/NUF (PubMed:16138011), but this has not been confirmed by other studies (PubMed:21345960).2 Publications

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3