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P03300

- POLG_POL1M

UniProt

P03300 - POLG_POL1M

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
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    • History
      Entry version 169 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
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    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

    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.

    GO - Cellular componenti

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

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

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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.

    Topological domain

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

    Intramembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Intramembranei1521 – 153616Sequence AnalysisAdd
    BLAST

    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

    MGAQVSSQKV GAHENSNRAY GGSTINYTTI NYYRDSASNA ASKQDFSQDP     50
    SKFTEPIKDV LIKTAPMLNS PNIEACGYSD RVLQLTLGNS TITTQEAANS 100
    VVAYGRWPEY LRDSEANPVD QPTEPDVAAC RFYTLDTVSW TKESRGWWWK 150
    LPDALRDMGL FGQNMYYHYL GRSGYTVHVQ CNASKFHQGA LGVFAVPEMC 200
    LAGDSNTTTM HTSYQNANPG EKGGTFTGTF TPDNNQTSPA RRFCPVDYLL 250
    GNGTLLGNAF VFPHQIINLR TNNCATLVLP YVNSLSIDSM VKHNNWGIAI 300
    LPLAPLNFAS ESSPEIPITL TIAPMCCEFN GLRNITLPRL QGLPVMNTPG 350
    SNQYLTADNF QSPCALPEFD VTPPIDIPGE VKNMMELAEI DTMIPFDLSA 400
    TKKNTMEMYR VRLSDKPHTD DPILCLSLSP ASDPRLSHTM LGEILNYYTH 450
    WAGSLKFTFL FCGFMMATGK LLVSYAPPGA DPPKKRKEAM LGTHVIWDIG 500
    LQSSCTMVVP WISNTTYRQT IDDSFTEGGY ISVFYQTRIV VPLSTPREMD 550
    ILGFVSACND FSVRLLRDTT HIEQKALAQG LGQMLESMID NTVRETVGAA 600
    TSRDALPNTE ASGPTHSKEI PALTAVETGA TNPLVPSDTV QTRHVVQHRS 650
    RSESSIESFF ARGACVTIMT VDNPASTTNK DKLFAVWKIT YKDTVQLRRK 700
    LEFFTYSRFD MELTFVVTAN FTETNNGHAL NQVYQIMYVP PGAPVPEKWD 750
    DYTWQTSSNP SIFYTYGTAP ARISVPYVGI SNAYSHFYDG FSKVPLKDQS 800
    AALGDSLYGA ASLNDFGILA VRVVNDHNPT KVTSKIRVYL KPKHIRVWCP 850
    RPPRAVAYYG PGVDYKDGTL TPLSTKDLTT YGFGHQNKAV YTAGYKICNY 900
    HLATQDDLQN AVNVMWSRDL LVTESRAQGT DSIARCNCNA GVYYCESRRK 950
    YYPVSFVGPT FQYMEANNYY PARYQSHMLI GHGFASPGDC GGILRCHHGV 1000
    IGIITAGGEG LVAFSDIRDL YAYEEEAMEQ GITNYIESLG AAFGSGFTQQ 1050
    ISDKITELTN MVTSTITEKL LKNLIKIISS LVIITRNYED TTTVLATLAL 1100
    LGCDASPWQW LRKKACDVLE IPYVIKQGDS WLKKFTEACN AAKGLEWVSN 1150
    KISKFIDWLK EKIIPQARDK LEFVTKLRQL EMLENQISTI HQSCPSQEHQ 1200
    EILFNNVRWL SIQSKRFAPL YAVEAKRIQK LEHTINNYIQ FKSKHRIEPV 1250
    CLLVHGSPGT GKSVATNLIA RAIAERENTS TYSLPPDPSH FDGYKQQGVV 1300
    IMDDLNQNPD GADMKLFCQM VSTVEFIPPM ASLEEKGILF TSNYVLASTN 1350
    SSRISPPTVA HSDALARRFA FDMDIQVMNE YSRDGKLNMA MATEMCKNCH 1400
    QPANFKRCCP LVCGKAIQLM DKSSRVRYSI DQITTMIINE RNRRSNIGNC 1450
    MEALFQGPLQ YKDLKIDIKT SPPPECINDL LQAVDSQEVR DYCEKKGWIV 1500
    NITSQVQTER NINRAMTILQ AVTTFAAVAG VVYVMYKLFA GHQGAYTGLP 1550
    NKKPNVPTIR TAKVQGPGFD YAVAMAKRNI VTATTSKGEF TMLGVHDNVA 1600
    ILPTHASPGE SIVIDGKEVE ILDAKALEDQ AGTNLEITII TLKRNEKFRD 1650
    IRPHIPTQIT ETNDGVLIVN TSKYPNMYVP VGAVTEQGYL NLGGRQTART 1700
    LMYNFPTRAG QCGGVITCTG KVIGMHVGGN GSHGFAAALK RSYFTQSQGE 1750
    IQWMRPSKEV GYPIINAPSK TKLEPSAFHY VFEGVKEPAV LTKNDPRLKT 1800
    DFEEAIFSKY VGNKITEVDE YMKEAVDHYA GQLMSLDINT EQMCLEDAMY 1850
    GTDGLEALDL STSAGYPYVA MGKKKRDILN KQTRDTKEMQ KLLDTYGINL 1900
    PLVTYVKDEL RSKTKVEQGK SRLIEASSLN DSVAMRMAFG NLYAAFHKNP 1950
    GVITGSAVGC DPDLFWSKIP VLMEEKLFAF DYTGYDASLS PAWFEALKMV 2000
    LEKIGFGDRV DYIDYLNHSH HLYKNKTYCV KGGMPSGCSG TSIFNSMINN 2050
    LIIRTLLLKT YKGIDLDHLK MIAYGDDVIA SYPHEVDASL LAQSGKDYGL 2100
    TMTPADKSAT FETVTWENVT FLKRFFRADE KYPFLIHPVM PMKEIHESIR 2150
    WTKDPRNTQD HVRSLCLLAW HNGEEEYNKF LAKIRSVPIG RALLLPEYST 2200
    LYRRWLDSF 2209
    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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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:
    PDBe
    RCSB PDB
    PDBj
    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: October 1, 2014
    This is version 169 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