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P03301

- POLG_POL1S

UniProt

P03301 - POLG_POL1S

Protein

Genome polyprotein

Gene
N/A
Organism
Poliovirus type 1 (strain Sabin)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 145 (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
    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 activityBy similarity

    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. 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

    MEROPSiC03.020.

    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 Sabin)
    Taxonomic identifieri12082 [NCBI]
    Taxonomic lineageiVirusesssRNA positive-strand viruses, no DNA stagePicornaviralesPicornaviridaeEnterovirusEnterovirus C
    Virus hostiHomo sapiens (Human) [TaxID: 9606]
    ProteomesiUP000000478: 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

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi1605 – 16051H → Y: Complete loss of protease activity. 1 Publication
    Mutagenesisi1636 – 16361E → Q: Complete loss of protease activity. 1 Publication
    Mutagenesisi1650 – 16501D → N: No effect on protease activity; complete loss of autoprocessing ability. 1 Publication
    Mutagenesisi1712 – 17121C → S: Complete loss of protease activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed; by hostBy similarity
    Chaini2 – 22092208Genome polyproteinBy similarityPRO_0000426596Add
    BLAST
    Chaini2 – 881880P1By similarityPRO_0000426597Add
    BLAST
    Chaini2 – 341340Capsid protein VP0Sequence AnalysisPRO_0000426598Add
    BLAST
    Chaini2 – 6968Capsid protein VP4Sequence AnalysisPRO_0000426599Add
    BLAST
    Chaini70 – 341272Capsid protein VP2Sequence AnalysisPRO_0000426600Add
    BLAST
    Chaini342 – 579238Capsid protein VP3Sequence AnalysisPRO_0000426601Add
    BLAST
    Chaini580 – 881302Capsid protein VP1Sequence AnalysisPRO_0000426602Add
    BLAST
    Chaini882 – 1456575P2By similarityPRO_0000426603Add
    BLAST
    Chaini882 – 1030149Protease 2ASequence AnalysisPRO_0000426604Add
    BLAST
    Chaini1031 – 112797Protein 2BSequence AnalysisPRO_0000040096Add
    BLAST
    Chaini1128 – 1456329Protein 2CSequence AnalysisPRO_0000040097Add
    BLAST
    Chaini1457 – 2209753P3By similarityPRO_0000426605Add
    BLAST
    Chaini1457 – 1565109Protein 3ABSequence AnalysisPRO_0000426606Add
    BLAST
    Chaini1457 – 154387Protein 3ASequence AnalysisPRO_0000040098Add
    BLAST
    Chaini1544 – 156522Viral protein genome-linkedSequence AnalysisPRO_0000426607Add
    BLAST
    Chaini1566 – 2209644Protein 3CDSequence AnalysisPRO_0000426608Add
    BLAST
    Chaini1566 – 1747182Protease 3CSequence AnalysisPRO_0000426609Add
    BLAST
    Chaini1748 – 2209462RNA-directed RNA polymeraseBy similarityPRO_0000426610Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Lipidationi2 – 21N-myristoyl glycine; by hostBy similarity
    Modified residuei1546 – 15461O-(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

    Protein-protein interaction databases

    IntActiP03301. 2 interactions.
    MINTiMINT-5224497.

    Structurei

    3D structure databases

    ProteinModelPortaliP03301.
    SMRiP03301. Positions 2-579, 599-1030, 1457-1515, 1566-2209.
    ModBaseiSearch...
    MobiDBiSearch...

    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
    Domaini1232 – 1388157SF3 helicasePROSITE-ProRule annotationAdd
    BLAST
    Domaini1566 – 1731166Peptidase C3Add
    BLAST
    Domaini1975 – 2090116RdRp catalyticPROSITE-ProRule annotationAdd
    BLAST

    Region

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

    P03301-1 [UniParc]FASTAAdd to Basket

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    MGAQVSSQKV GAHENSNRAY GGSTINYTTI NYYRDSASNA ASKQDFSQDP     50
    SKFTEPIKDV LIKTSPMLNS PNIEACGYSD RVLQLTLGNS TITTQEAANS 100
    VVAYGRWPEY LRDSEANPVD QPTEPDVAAC RFYTLDTVSW TKESRGWWWK 150
    LPDALRDMGL FGQNMYYHYL GRSGYTVHVQ CNASKFHQGA LGVFAVPEMC 200
    LAGDSNTTTM HTSYQNANPG EKGGTFTGTF TPDDNQTSPA RRFCPVDYLF 250
    GNGTLLGNAF VFPHQIINLR TNNCATLVLP YVNSLSIDSM VKHNNWGIAI 300
    LPLAPLNFAS ESSPEIPITL TIAPMCCEFN GLRNITLPRL QGLPVMNTPG 350
    SNQYLTADNF QSPCALPEFD VTPPIDIPGE VKNMMELAEI DTMIPFDLSA 400
    KKKNTMEMYR VRLSDKPHTD DPILCLSLSP ASDPRLSHTM LGEILNYYTH 450
    WAGSLKFTFL FCGSMMATGK LLVSYAPPGA DPPKKRKEAM LGTHVIWDIG 500
    LQSSCTMVVP WISNTTYRQT IDDSFTEGGY ISVFYQTRIV VPLSTPREMD 550
    ILGFVSACND FSVRLMRDTT HIEQKALAQG LGQMLESMID NTVRETVGAA 600
    TSRDALPNTE ASGPAHSKEI PALTAVETGA TNPLVPSDTV QTRHVVQHRS 650
    RSESSIESFF ARGACVAIIT VDNSASTKNK DKLFTVWKIT YKDTVQLRRK 700
    LEFFTYSRFD MEFTFVVTAN FTETNNGHAL NQVYQIMYVP PGAPVPEKWD 750
    DYTWQTSSNP SIFYTYGTAP ARISVPYVGI SNAYSHFYDG FSKVPLKDQS 800
    AALGDSLYGA ASLNDFGILA VRVVNDHNPT KVTSKIRVYL KPKHIRVWCP 850
    RPPRAVAYYG PGVDYKDGTL TPLSTKDLTT YGFGHQNKAV YTAGYKICNY 900
    HLATQEDLQN AVNVMWNRDL LVTESRAQGT DSIARCNCNA GVYYCESRRK 950
    YYPVSFVGPT FQYMEANNYY PARYQSHMLI GHGFASPGDC GGILRCHHGV 1000
    IGIITAGGEG LVAFTDIRDL YAYEEEAMEQ GITNYIESLG AAFGSGFTQQ 1050
    IGDKITELTN MVTSTITEKL LKNLIKIISS LVIITRNYED TTTVLATLAL 1100
    LGCDASPWQW LRKKACDVLE IPYVTKQGDS 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
    NFEEAIFSKY VGNKITEVDE HMKEAVDHYA GQLMSLDINT EQMCLEDAMY 1850
    GTDGLEALDL STSAGYPYVA MGKKKRDILN KQTRDTKEMQ KLLDTYGINL 1900
    PLVTYVKDEL RSKTKVEQGK SRLIEASSLN DSVAMRMAFG NLYAAFHKNP 1950
    GVITGSAVGC DPDLFWSKIP VLMEEKLFAF DYTGYDASLS PAWFEALEMV 2000
    LEKIGFGDRV DYIDYLNHSH HLYKNKTYCV KGGMPSGCSG TSIFNSMINN 2050
    LIIRTLLLKT YKGIDLDHLK MIAYGDDVIA SYPHEVDASL LAQSGKDYGL 2100
    TMTPADKSAI FETVTWENVT FLKRFFRADE KYPFLIHPVM PMKEIHESIR 2150
    WTKDPRNTQD HVRSLCLLAW HNGEEEYNKF LAKIRSVPIG RALLLPEYST 2200
    LYRRWLDSF 2209
    Length:2,209
    Mass (Da):246,578
    Last modified:January 23, 2007 - v3
    Checksum:i9EC1EF4D174A28A4
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    V01150 Genomic RNA. Translation: CAA24465.1.
    PIRiA03899. GNNY3P.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    V01150 Genomic RNA. Translation: CAA24465.1 .
    PIRi A03899. GNNY3P.

    3D structure databases

    ProteinModelPortali P03301.
    SMRi P03301. Positions 2-579, 599-1030, 1457-1515, 1566-2209.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P03301. 2 interactions.
    MINTi MINT-5224497.

    Protein family/group databases

    MEROPSi C03.020.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    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. "Complete nucleotide sequence of the attenuated poliovirus Sabin 1 strain genome."
      Nomoto A., Omata T., Toyoda H., Kuge S., Horie H., Kataoka Y., Genba Y., Nakano Y., Imura N.
      Proc. Natl. Acad. Sci. U.S.A. 79:5793-5797(1982) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
    2. "Site-directed mutagenesis of the putative catalytic triad of poliovirus 3C proteinase."
      Haemmerle T., Hellen C.U.T., Wimmer E.
      J. Biol. Chem. 266:5412-5416(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACTIVE SITE OF P3C, MUTAGENESIS OF HIS-1605; GLU-1636; ASP-1650 AND CYS-1712.

    Entry informationi

    Entry nameiPOLG_POL1S
    AccessioniPrimary (citable) accession number: P03301
    Secondary accession number(s): Q84881
    , Q84882, Q84883, Q84884, Q84885, Q84886, Q84887, Q84888, Q84889, Q84890
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 145 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programViral Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    This virus is a live vaccine strain derived from the mahoney strain by spontaneous mutations during the attenuation process.

    Keywords - Technical termi

    Complete proteome

    Documents

    1. Peptidase families
      Classification of peptidase families and list of entries
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3