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P06210

- POLG_POL2L

UniProt

P06210 - POLG_POL2L

Protein

Genome polyprotein

Gene
N/A
Organism
Poliovirus type 2 (strain Lansing)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 150 (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 to provide virion attachment to target host cells. This attachment induces virion internalization 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. 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 By similarity.By similarity
    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 By similarity.By similarity
    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 By similarity.By similarity
    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 By similarity.By similarity
    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 By similarity.By similarity
    Protein 2C: Induces and associates with structural rearrangements of intracellular membranes. 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 By similarity.By similarity
    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 By similarity.By similarity
    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 By similarity.By similarity
    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 By similarity.By similarity
    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 By similarity.By similarity
    Protease 3C: cleaves host DDX58/RIG-I and thus contributes to the inhibition of type I interferon production. Cleaves also host PABPC1 By similarity.By similarity
    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 By similarity.PROSITE-ProRule annotation

    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
    Sitei69 – 702Cleavage; by autolysisSequence Analysis
    Sitei340 – 3412Cleavage; by Protease 3CSequence Analysis
    Sitei879 – 8802Cleavage; by Protease 2ASequence Analysis
    Active sitei899 – 8991For Protease 2A activityBy similarity
    Active sitei917 – 9171For Protease 2A activityBy similarity
    Active sitei988 – 9881For Protease 2A activityBy similarity
    Sitei1028 – 10292Cleavage; by Protease 3CSequence Analysis
    Sitei1125 – 11262Cleavage; by Protease 3CSequence Analysis
    Sitei1454 – 14552Cleavage; by Protease 3CSequence Analysis
    Sitei1541 – 15422Cleavage; by Protease 3CSequence Analysis
    Sitei1563 – 15642Cleavage; by Protease 3CSequence Analysis
    Active sitei1603 – 16031For Protease 3C activitySequence Analysis
    Active sitei1634 – 16341For Protease 3C activitySequence Analysis
    Active sitei1710 – 17101For Protease 3C activitySequence Analysis
    Sitei1746 – 17472Cleavage; by Protease 3CSequence Analysis
    Active sitei2074 – 20741For RdRp activityBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi1254 – 12618ATPPROSITE-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. DNA replication 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. receptor-mediated endocytosis of virus by host cell Source: UniProtKB-KW
    7. RNA-protein covalent cross-linking Source: UniProtKB-KW
    8. suppression by virus of host gene expression Source: UniProtKB-KW
    9. suppression by virus of host mRNA export from nucleus Source: UniProtKB-KW
    10. suppression by virus of host RIG-I activity by RIG-I proteolysis Source: UniProtKB
    11. suppression by virus of host translation initiation factor activity Source: UniProtKB
    12. transcription, DNA-templated Source: InterPro
    13. viral RNA genome replication Source: InterPro
    14. 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, Clathrin- and caveolin-independent endocytosis of virus by host, DNA replication, Eukaryotic host gene expression shutoff by virus, Eukaryotic host transcription 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 eukaryotic host transcription initiation by virus, 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 2 (strain Lansing)
    Taxonomic identifieri12084 [NCBI]
    Taxonomic lineageiVirusesssRNA positive-strand viruses, no DNA stagePicornaviralesPicornaviridaeEnterovirusEnterovirus C
    Virus hostiHomo sapiens (Human) [TaxID: 9606]
    ProteomesiUP000007638: Genome

    Subcellular locationi

    Chain Capsid protein VP0 : Virion By similarity. Host cytoplasm By similarity
    Chain Capsid protein VP2 : Virion By similarity. Host cytoplasm By similarity
    Chain Capsid protein VP3 : Virion By similarity. Host cytoplasm By similarity
    Chain Capsid protein VP1 : Virion By similarity. Host cytoplasm By similarity
    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

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed; by hostBy similarity
    Chaini2 – 22072206Genome polyproteinBy similarityPRO_0000426611Add
    BLAST
    Chaini2 – 879878P1By similarityPRO_0000426612Add
    BLAST
    Chaini2 – 340339Capsid protein VP0Sequence AnalysisPRO_0000426613Add
    BLAST
    Chaini2 – 6968Capsid protein VP4Sequence AnalysisPRO_0000426614Add
    BLAST
    Chaini70 – 340271Capsid protein VP2Sequence AnalysisPRO_0000426615Add
    BLAST
    Chaini341 – 578238Capsid protein VP3Sequence AnalysisPRO_0000426616Add
    BLAST
    Chaini579 – 879301Capsid protein VP1Sequence AnalysisPRO_0000426617Add
    BLAST
    Chaini880 – 1454575P2By similarityPRO_0000426618Add
    BLAST
    Chaini880 – 1028149Protease 2ASequence AnalysisPRO_0000426619Add
    BLAST
    Chaini1029 – 112597Protein 2BSequence AnalysisPRO_0000040107Add
    BLAST
    Chaini1126 – 1454329Protein 2CSequence AnalysisPRO_0000040108Add
    BLAST
    Chaini1455 – 2207753P3By similarityPRO_0000426620Add
    BLAST
    Chaini1455 – 1563109Protein 3ABSequence AnalysisPRO_0000426621Add
    BLAST
    Chaini1455 – 154187Protein 3ASequence AnalysisPRO_0000040109Add
    BLAST
    Chaini1542 – 156322Viral protein genome-linkedSequence AnalysisPRO_0000426622Add
    BLAST
    Chaini1564 – 2207644Protein 3CDSequence AnalysisPRO_0000426623Add
    BLAST
    Chaini1564 – 1745182Protease 3CSequence AnalysisPRO_0000426624Add
    BLAST
    Chaini1746 – 2207462RNA-directed RNA polymeraseBy similarityPRO_0000426625Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Lipidationi2 – 21N-myristoyl glycine; by hostBy similarity
    Modified residuei1544 – 15441O-(5'-phospho-RNA)-tyrosineBy similarity

    Post-translational modificationi

    Specific enzymatic cleavages in vivo by the viral proteases yield a variety of precursors and mature proteins. Polyprotein processing intermediates such as VP0 which is a VP4-VP2 precursor are produced. During virion maturation, non-infectious particles are rendered infectious following cleavage of VP0. This maturation cleavage is followed by a conformational change of the particle By similarity.By similarity
    VPg is uridylylated by the polymerase and is covalently linked to the 5'-end of genomic RNA. This uridylylated form acts as a nucleotide-peptide primer for the polymerase By similarity.By similarity
    Myristoylation of VP4 is required during RNA encapsidation and formation of the mature virus particle.By similarity
    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.By similarity
    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 By similarity.By similarity
    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 By similarity.By similarity

    Keywords - PTMi

    Covalent protein-RNA linkage, Lipoprotein, Myristate, Phosphoprotein

    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 capsid protein VP4 in the mature capsid By similarity. 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 By similarity. 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 By similarity. Capsid protein VP4: Interacts with capsid protein VP1 and capsid protein VP3 By similarity. Protein 2C: interacts with capsid protein VP3; this interaction may be important for virion morphogenesis By similarity. Protein 3AB: interacts with protein 3CD By similarity. Viral protein genome-linked: interacts with RNA-directed RNA polymerase By similarity. 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 similarity.By similarity

    Structurei

    Secondary structure

    1
    2207
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi4 – 74
    Helixi17 – 193
    Helixi23 – 253
    Beta strandi26 – 294
    Helixi36 – 383
    Helixi51 – 544
    Beta strandi57 – 593
    Beta strandi63 – 653
    Beta strandi83 – 875
    Beta strandi90 – 967
    Helixi103 – 1053
    Turni113 – 1153
    Helixi126 – 1283
    Beta strandi138 – 1403
    Beta strandi147 – 1515
    Helixi153 – 1553
    Helixi159 – 1679
    Beta strandi168 – 18013
    Beta strandi187 – 19711
    Beta strandi203 – 2075
    Helixi213 – 2164
    Helixi219 – 2213
    Beta strandi226 – 2283
    Beta strandi235 – 2373
    Helixi246 – 2483
    Turni249 – 2524
    Helixi255 – 2606
    Beta strandi261 – 2677
    Turni268 – 2703
    Beta strandi272 – 2787
    Beta strandi282 – 2876
    Turni289 – 2913
    Beta strandi295 – 30713
    Beta strandi315 – 33117
    Turni348 – 3514
    Beta strandi363 – 3653
    Beta strandi379 – 3824
    Helixi384 – 3874
    Turni399 – 4035
    Helixi405 – 4084
    Beta strandi410 – 4134
    Beta strandi422 – 4276
    Turni429 – 4313
    Turni433 – 4375
    Helixi439 – 4446
    Beta strandi447 – 4526
    Beta strandi454 – 4607
    Beta strandi469 – 4757
    Beta strandi477 – 4793
    Helixi485 – 4884
    Beta strandi491 – 4977
    Beta strandi499 – 5013
    Beta strandi503 – 5086
    Beta strandi513 – 5208
    Beta strandi529 – 5368
    Beta strandi546 – 55611
    Beta strandi561 – 5655
    Helixi625 – 6273
    Helixi635 – 6373
    Helixi655 – 6595
    Beta strandi663 – 6719
    Beta strandi683 – 6875
    Helixi695 – 7006
    Beta strandi703 – 72523
    Beta strandi732 – 7387
    Helixi751 – 7544
    Beta strandi756 – 7583
    Beta strandi760 – 7645
    Beta strandi770 – 7745
    Beta strandi779 – 7857
    Turni800 – 8034
    Beta strandi812 – 8154
    Beta strandi817 – 8226
    Beta strandi831 – 84919
    Beta strandi859 – 8624

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1EAHX-ray2.901579-879[»]
    270-340[»]
    3341-578[»]
    42-69[»]
    3EPFelectron microscopy9.001602-879[»]
    279-340[»]
    3341-575[»]
    42-69[»]
    ProteinModelPortaliP06210.
    SMRiP06210. Positions 2-575, 602-1028, 1455-1513, 1564-2207.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP06210.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini2 – 15181517CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini1535 – 2207673CytoplasmicSequence AnalysisAdd
    BLAST

    Intramembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Intramembranei1519 – 153416Sequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini1230 – 1386157SF3 helicasePROSITE-ProRule annotationAdd
    BLAST
    Domaini1564 – 1729166Peptidase C3Add
    BLAST
    Domaini1973 – 2088116RdRp catalyticPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni579 – 59921Amphipatic alpha-helixSequence AnalysisAdd
    BLAST
    Regioni1455 – 147723DisorderedBy similarityAdd
    BLAST

    Sequence similaritiesi

    Belongs to the picornaviruses polyprotein family.Curated
    Contains 1 peptidase C3 domain.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.

    P06210-1 [UniParc]FASTAAdd to Basket

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    MGAQVSSQKV GAHENSNRAY GGSTINYTTI NYYRDSASNA ASKQDFAQDP     50
    SKFTEPIKDV LIKTAPTLNS PNIEACGYSD RVMQLTLGNS TITTQEAANS 100
    VVAYGRWPEY IKDSEANPVD QPTEPDVAAC RFYTLDTVTW RKESRGWWWK 150
    LPDALKDMGL FGQNMFYHYL GRAGYTVHVQ CNASKFHQGA LGVFAVPEMC 200
    LAGDSTTHMF TKYENANPGE KGGEFKGSFT LDTNATNPAR NFCPVDYLFG 250
    SGVLAGNAFV YPHQIINLRT NNCATLVLPY VNSLSIDSMT KHNNWGIAIL 300
    PLAPLDFATE SSTEIPITLT IAPMCCEFNG LRNITVPRTQ GLPVLNTPGS 350
    NQYLTADNYQ SPCAIPEFDV TPPIDIPGEV RNMMELAEID TMIPLNLTNQ 400
    RKNTMDMYRV ELNDAAHSDT PILCLSLSPA SDPRLAHTML GEILNYYTHW 450
    AGSLKFTFLF CGSMMATGKL LVSYAPPGAE APKSRKEAML GTHVIWDIGL 500
    QSSCTMVVPW ISNTTYRQTI NDSFTEGGYI SMFYQTRVVV PLSTPRKMDI 550
    LGFVSACNDF SVRLLRDTTH ISQEAMPQGL GDLIEGVVEG VTRNALTPLT 600
    PANNLPDTQS SGPAHSKETP ALTAVETGAT NPLVPSDTVQ TRHVIQKRTR 650
    SESTVESFFA RGACVAIIEV DNDAPTKRAS KLFSVWKITY KDTVQLRRKL 700
    EFFTYSRFDM EFTFVVTSNY TDANNGHALN QVYQIMYIPP GAPIPGKWND 750
    YTWQTSSNPS VFYTYGAPPA RISVPYVGIA NAYSHFYDGF AKVPLAGQAS 800
    TEGDSLYGAA SLNDFGSLAV RVVNDHNPTK LTSKIRVYMK PKHVRVWCPR 850
    PPRAVPYYGP GVDYKDGLAP LPGKGLTTYG FGHQNKAVYT AGYKICNYHL 900
    ATQEDLQNAV NIMWIRDLLV VESKAQGIDS IARCNCHTGV YYCESRRKYY 950
    PVSFTGPTFQ YMEANEYYPA RYQSHMLIGH GFASPGDCGG ILRCQHGVIG 1000
    IITAGGEGLV AFSDIRDLYA YEEEAMEQGV SNYIESLGAA FGSGFTQQIG 1050
    NKISELTSMV TSTITEKLLK NLIKIISSLV IITRNYEDTT TVLATLALLG 1100
    CDASPWQWLK KKACDILEIP YIMRQGDSWL KKFTEACNAA KGLEWVSNKI 1150
    SKFIDWLKEK IIPQARDKLE FVTKLKQLEM LENQIATIHQ SCPSQEHQEI 1200
    LFNNVRWLSI QSKRFAPLYA VEAKRIQKLE HTINNYVQFK SKHRIEPVCL 1250
    LVHGSPGTGK SVATNLIARA IAEKENTSTY SLPPDPSHFD GYKQQGVVIM 1300
    DDLNQNPDGA DMKLFCQMVS TVEFIPPMAS LEEKGILFTS NYVLASTNSS 1350
    RITPPTVAHS DALARRFAFD MDIQIMSEYS RDGKLNMAMA TEMCKNCHHP 1400
    ANFKRCCPLV CGKAIQLMDK SSRVRYSIDQ ITTMIINERN RRSSIGNCME 1450
    ALFQGPLQYK DLKIDIKTTP PPECINDLLQ AVDSQEVRDY CEKKGWIVDI 1500
    TSQVQTERNI NRAMTILQAV TTFAAVAGVV YVMYKLFAGH QGAYTGLPNK 1550
    RPNVPTIRTA KVQGPGFDYA VAMAKRNILT ATTIKGEFTM LGVHDNVAIL 1600
    PTHASPGETI VIDGKEVEVL DAKALEDQAG TNLEITIVTL KRNEKFRDIR 1650
    PHIPTQITET NDGVLIVNTS KYPNMYVPVG AVTEQGYLNL SGRQTARTLM 1700
    YNFPTRAGQC GGVITCTGKV IGMHVGGNGS HGFAAALKRS YFTQSQGEIQ 1750
    WMRPSKEVGY PVINAPSKTK LEPSAFHYVF EGVKEPAVLT KSDPRLKTDF 1800
    EEAIFSKYVG NKITEVDEYM KEAVDHYAGQ LMSLDINTEQ MCLEDAMYGT 1850
    DGLEALDLST SAGYPYVAMG KKKRDILNKQ TRDTKEMQRL LDTYGINLPL 1900
    VTYVKDELRS KTKVEQGKSR LIEASSLNDS VAMRMAFGNL YAAFHKNPGV 1950
    VTGSAVGCDP DLFWSKIPVL MEEKLFAFDY TGYDASLSPA WFEALKMVLE 2000
    KIGFGDRVDY IDYLNHSHHL YKNKTYCVKG GMPSGCSGTS IFNSMINNLI 2050
    IRTLLLKTYK GIDLDHLKMI AYGDDVIASY PHEVDASLLA QSGKDYGLTM 2100
    TPADKSATFE TVTWENVTFL KRFFRADEKY PFLVHPVMPM KEIHESIRWT 2150
    KDPRNTQDHV RSLCLLAWHN GEEEYNKFLA KIRSVPIGRA LLLPEYSTLY 2200
    RRWLDSF 2207
    Length:2,207
    Mass (Da):245,831
    Last modified:January 23, 2007 - v3
    Checksum:i2B1E2070B7D44F99
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M12197 Genomic RNA. Translation: AAA46912.1.
    PIRiA29507. GNNY5P.

    Cross-referencesi

    Web resourcesi

    Virus Particle ExploreR db

    Icosahedral capsid structure

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M12197 Genomic RNA. Translation: AAA46912.1 .
    PIRi A29507. GNNY5P.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1EAH X-ray 2.90 1 579-879 [» ]
    2 70-340 [» ]
    3 341-578 [» ]
    4 2-69 [» ]
    3EPF electron microscopy 9.00 1 602-879 [» ]
    2 79-340 [» ]
    3 341-575 [» ]
    4 2-69 [» ]
    ProteinModelPortali P06210.
    SMRi P06210. Positions 2-575, 602-1028, 1455-1513, 1564-2207.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    MEROPSi C03.001.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Miscellaneous databases

    EvolutionaryTracei P06210.

    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. "Mapping of sequences required for mouse neurovirulence of poliovirus type 2 Lansing."
      la Monica N., Meriam C., Racaniello V.R.
      J. Virol. 57:515-525(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].

    Entry informationi

    Entry nameiPOLG_POL2L
    AccessioniPrimary (citable) accession number: P06210
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 1, 1988
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 150 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programViral Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete 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