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P23069

- POLG_POL2W

UniProt

P23069 - POLG_POL2W

Protein

Genome polyprotein

Gene
N/A
Organism
Poliovirus type 2 (strain W-2)
Status
Reviewed - Annotation score: 5 out of 5- Protein inferred from homologyi
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    • History
      Entry version 135 (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
    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 sitei2072 – 20721For 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 W-2)
    Taxonomic identifieri12085 [NCBI]
    Taxonomic lineageiVirusesssRNA positive-strand viruses, no DNA stagePicornaviralesPicornaviridaeEnterovirusEnterovirus C
    Virus hostiHomo sapiens (Human) [TaxID: 9606]
    ProteomesiUP000008165: 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 – 22052204Genome polyproteinBy similarityPRO_0000426626Add
    BLAST
    Chaini2 – 879878P1By similarityPRO_0000426627Add
    BLAST
    Chaini2 – 340339Capsid protein VP0Sequence AnalysisPRO_0000426628Add
    BLAST
    Chaini2 – 6968Capsid protein VP4Sequence AnalysisPRO_0000426629Add
    BLAST
    Chaini70 – 340271Capsid protein VP2Sequence AnalysisPRO_0000426630Add
    BLAST
    Chaini341 – 578238Capsid protein VP3Sequence AnalysisPRO_0000426631Add
    BLAST
    Chaini579 – 879301Capsid protein VP1Sequence AnalysisPRO_0000426632Add
    BLAST
    Chaini880 – 1454575P2By similarityPRO_0000426633Add
    BLAST
    Chaini880 – 1028149Protease 2ASequence AnalysisPRO_0000426634Add
    BLAST
    Chaini1029 – 112597Protein 2BSequence AnalysisPRO_0000040118Add
    BLAST
    Chaini1126 – 1454329Protein 2CSequence AnalysisPRO_0000040119Add
    BLAST
    Chaini1455 – 2205751P3By similarityPRO_0000426635Add
    BLAST
    Chaini1455 – 1563109Protein 3ABSequence AnalysisPRO_0000426636Add
    BLAST
    Chaini1455 – 154187Protein 3ASequence AnalysisPRO_0000040120Add
    BLAST
    Chaini1542 – 156322Viral protein genome-linkedSequence AnalysisPRO_0000426637Add
    BLAST
    Chaini1564 – 2205642Protein 3CDSequence AnalysisPRO_0000426638Add
    BLAST
    Chaini1564 – 1745182Protease 3CSequence AnalysisPRO_0000426639Add
    BLAST
    Chaini1746 – 2205460RNA-directed RNA polymeraseBy similarityPRO_0000426640Add
    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

    3D structure databases

    ProteinModelPortaliP23069.
    SMRiP23069. Positions 2-574, 603-1028, 1456-1513, 1564-2205.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini2 – 15181517CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini1535 – 2205671CytoplasmicSequence 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
    Domaini1971 – 2086116RdRp 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.

    P23069-1 [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 GRASYTVHVQ CNASKFHQGA LGVFAVPEMC 200
    LAGDSATHML TKYENANPGE KGGEFKGSFT LDTNATNPAR NFCPVDYLFG 250
    SGVLAGNAFV YPHQIINLRT NNCATLVLPY VNSLSIDSMT KHNNWGIAIL 300
    PLAPLDFATE SSTEIPITLT IAPMCCEFNG LRNITVPRTQ GLPVLNTPGS 350
    NQYLTADNYQ SPCAIPEFDV TPPIDIPGEV RNMMELAEID TMIPLNLTSQ 400
    RKNTMDMYRV ELNDAAHSDT PILCLSLSPA SDPRLAHTML GEILNYYTHW 450
    AGSLKFTFLF CGSMMATGKL LVSYAPPGAK APESRKEAML GTHVIWDIGL 500
    QSSCTMVVPW ISNTTYRQTI NDSFTEGGYI SMFYQTRVVV PLSTPRKMDI 550
    LGFVSACNDF SVRLLRDTTH ISQEVMPQGL GDLIEGVVEG VTRNALTPLT 600
    PVNNLPDTRS SGPAHSKETP ALTAVETGAT NPLVPSDTVQ TRHVIQKRTR 650
    SESTVESFFA RGACVAIIEV DNDAPTRRAS KLFSVWKITY KDTVQLRRKL 700
    EFFTYSRFDM EFTFVVTSNY TDANNGHALN QVYQIMYIPP GAPIPGKRND 750
    YTWQTSSNPS VFYTYGAPPA RISVPYVGIA NAYSHFYDGF AKVPLAGQAS 800
    TEGDSLYGAA SLNDFGSLAV RVVNDHNPTK LTSKIRVYMK PKHVRVWCPR 850
    PPRAVPYYGP GVDYKDGLTP LPEKGLITYG FGHQNKAVYT AGYKICNYHL 900
    ATQEDLQNAI NIMWIRDLLV VESKAQGIDS IARCNCHTGV YYCESRRKYY 950
    PVSFVGPTFQ YMEANEYYPA RYQSHMLIGH GFASPGDCGG ILRCQHGVIG 1000
    IITAGGEGLV AFSDIRDLYA YEVEAMEQGV SNYIESLGAA FGSGFTQQIG 1050
    NKISELTSMV TSTITEKLLK NLIKIISSLV IITRNYEDTT TVLATLALLG 1100
    CDASPWQWLK KKACDILEIP YIMRQGDSWL KKFTEACNAA KGLEWVSNKI 1150
    SKFIDWLKEK IIPQARDKLE FVTKLKQLEM LENQIATIHQ SCPSQEHQEI 1200
    LFNNVRWLSI QSRRFAPLYA VEAKRIQKLE HTINNYVQFK SKHRIEPVCL 1250
    LVHGSPGTGK SVATNLIARA IAEKENTSTY SLPPDPSHFD GYKQQGVVIM 1300
    DDLNQNPDGA DMKLFCQMVS TVEFIPPMAS LEEKGILFTS NYVLASTNSS 1350
    RITPPTVAHS DALARRFAFD MDIQIMSEYS RDGKLNMAMA TEMCKNCHQP 1400
    ANFKRCCPLV CGKAIQLMDK SSRVRYSIDQ ITTMIINERN RRSSIGNCME 1450
    ALFQSPLQYK DLKIDIKTTP PPECINDLLH AVDSQEVRDY CEKKGWIADI 1500
    TSQVQTERNI NRAMTILQAV TTFAAVAGVV YVMYKLFAGH QGAYTGLPNK 1550
    RPNVPTIRTA KVQGPGFDYA VAMAKRNILT ATTIKGEFTM LGVHDNVAIL 1600
    PTHASPGETI VIDGKEVEVL DAKALEDQAG TNLEITIVTL KRNEKFRDIR 1650
    PHIPTQITET NDGVLIVNTS KYPNMYVPVG AVTEQGYLNL GGRQTARTLM 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 MEEKLFDYTG YDASLSPAWF EALKMVLEKI 2000
    GFGDRVDYID YLNHSHHLYK NKTYCVKGGM PSGCSGTSIF NSMINNLIIR 2050
    TLLLKTYKGI DLDHLKMIAY GDDVIASYPH EVDASLLAQS GKDYGLTMTP 2100
    ADKSATFETV TWENVTFLKR FFRADEKYPF LVHPVMPMKE IHESIRWTKD 2150
    PRNTQDHVRS LCLLAWHSGE EEYNKFLAKI RSVPIGRALL LPEYSTLYRR 2200
    WLDSF 2205
    Length:2,205
    Mass (Da):245,703
    Last modified:January 23, 2007 - v3
    Checksum:i2A42AB039E0254AD
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D00625 Genomic RNA. Translation: BAA00516.1. Sequence problems.
    PIRiA34032. GNNY2W.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D00625 Genomic RNA. Translation: BAA00516.1 . Sequence problems.
    PIRi A34032. GNNY2W.

    3D structure databases

    ProteinModelPortali P23069.
    SMRi P23069. Positions 2-574, 603-1028, 1456-1513, 1564-2205.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    MEROPSi C03.001.

    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. "Localization of genomic regions specific for the attenuated, mouse-adapted poliovirus type 2 strain W-2."
      Pevear D.C., Oh C.K., Cunningham L.L., Calenoff M., Jubelt B.
      J. Gen. Virol. 71:43-52(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].

    Entry informationi

    Entry nameiPOLG_POL2W
    AccessioniPrimary (citable) accession number: P23069
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1991
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 135 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

    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