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P03313

- POLG_CXB3N

UniProt

P03313 - POLG_CXB3N

Protein

Genome polyprotein

Gene
N/A
Organism
Coxsackievirus B3 (strain Nancy)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 156 (01 Oct 2014)
      Sequence version 4 (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 CD55 and CXADR to provide virion attachment to target host cells. This attachment induces virion internalization. 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
    Sitei332 – 3332Cleavage; by Protease 3CSequence Analysis
    Active sitei872 – 8721For Protease 2A activityBy similarity
    Active sitei890 – 8901For Protease 2A activityBy similarity
    Active sitei961 – 9611For Protease 2A activityBy similarity
    Sitei1001 – 10022Cleavage; by Protease 3CSequence Analysis
    Sitei1429 – 14302Cleavage; by Protease 3CSequence Analysis
    Sitei1518 – 15192Cleavage; by Protease 3CSequence Analysis
    Sitei1540 – 15412Cleavage; by Protease 3CSequence Analysis
    Active sitei1580 – 15801For Protease 3C activitySequence Analysis
    Active sitei1611 – 16111For Protease 3C activitySequence Analysis
    Active sitei1687 – 16871For Protease 3C activityBy similarity
    Sitei1723 – 17242Cleavage; by Protease 3CSequence Analysis
    Active sitei2052 – 20521For RdRp activityBy similarity

    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. endocytosis involved in viral entry into host cell Source: UniProtKB-KW
    3. induction by virus of host autophagy Source: UniProtKB
    4. pore formation by virus in membrane of host cell Source: UniProtKB-KW
    5. pore-mediated entry of viral genome into host cell Source: UniProtKB-KW
    6. protein oligomerization 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, DNA replication, 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

    MEROPSiC03.011.

    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
    OrganismiCoxsackievirus B3 (strain Nancy)
    Taxonomic identifieri103903 [NCBI]
    Taxonomic lineageiVirusesssRNA positive-strand viruses, no DNA stagePicornaviralesPicornaviridaeEnterovirusEnterovirus B
    Virus hostiHomo sapiens (Human) [TaxID: 9606]
    ProteomesiUP000007760: 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. host cell nucleus Source: CACAO
    3. integral to membrane of host cell Source: UniProtKB-KW
    4. membrane Source: UniProtKB-KW
    5. 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 – 21852184Genome polyproteinBy similarityPRO_0000426266Add
    BLAST
    Chaini2 – 848847P1By similarityPRO_0000426267Add
    BLAST
    Chaini2 – 332331Capsid protein VP0Sequence AnalysisPRO_0000426268Add
    BLAST
    Chaini2 – 6968Capsid protein VP4Sequence AnalysisPRO_0000426269Add
    BLAST
    Chaini70 – 332263Capsid protein VP2Sequence AnalysisPRO_0000426270Add
    BLAST
    Chaini333 – 568236Capsid protein VP3Sequence AnalysisPRO_0000426271Add
    BLAST
    Chaini568 – 848281Capsid protein VP1Sequence AnalysisPRO_0000426272Add
    BLAST
    Chaini849 – 1429581P2By similarityPRO_0000426273Add
    BLAST
    Chaini849 – 1001153Protease 2ASequence AnalysisPRO_0000426274Add
    BLAST
    Chaini1002 – 110099Protein 2BSequence AnalysisPRO_0000039587Add
    BLAST
    Chaini1101 – 1429329Protein 2CSequence AnalysisPRO_0000039588Add
    BLAST
    Chaini1430 – 2185756P3By similarityPRO_0000426275Add
    BLAST
    Chaini1430 – 1540111Protein 3ABSequence AnalysisPRO_0000426276Add
    BLAST
    Chaini1430 – 151889Protein 3ASequence AnalysisPRO_0000039589Add
    BLAST
    Chaini1519 – 154022Viral protein genome-linkedSequence AnalysisPRO_0000426277Add
    BLAST
    Chaini1541 – 2185645Protein 3CDSequence AnalysisPRO_0000426278Add
    BLAST
    Chaini1541 – 1722182Protease 3CSequence AnalysisPRO_0000426279Add
    BLAST
    Chaini1723 – 2185463RNA-directed RNA polymeraseBy similarityPRO_0000426280Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Lipidationi2 – 21N-myristoyl glycine; by hostBy similarity
    Modified residuei1521 – 15211O-(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. Interact with host CD55 and CXADR. 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
    2185
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Turni1528 – 15303
    Helixi1542 – 155413
    Beta strandi1555 – 15606
    Beta strandi1563 – 157210
    Beta strandi1574 – 15785
    Helixi1579 – 15813
    Beta strandi1585 – 15895
    Beta strandi1592 – 160312
    Beta strandi1609 – 16179
    Helixi1627 – 16293
    Beta strandi1637 – 16448
    Beta strandi1646 – 16494
    Beta strandi1652 – 166716
    Beta strandi1670 – 168011
    Beta strandi1690 – 16934
    Beta strandi1696 – 170510
    Beta strandi1708 – 17136
    Helixi1716 – 17194
    Beta strandi1725 – 17317
    Helixi1732 – 17354
    Turni1752 – 17565
    Helixi1777 – 17826
    Helixi1795 – 180915
    Helixi1820 – 18256
    Helixi1843 – 18453
    Helixi1850 – 18523
    Turni1856 – 18583
    Helixi1862 – 187110
    Beta strandi1877 – 18815
    Helixi1888 – 18925
    Beta strandi1898 – 19014
    Helixi1904 – 192320
    Turni1927 – 19304
    Helixi1937 – 19404
    Turni1941 – 19433
    Helixi1944 – 19474
    Beta strandi1950 – 19534
    Beta strandi1956 – 19594
    Helixi1960 – 19634
    Helixi1966 – 197813
    Turni1983 – 19864
    Helixi1987 – 19937
    Beta strandi1994 – 19996
    Beta strandi2002 – 20098
    Helixi2017 – 203620
    Helixi2042 – 20443
    Beta strandi2046 – 20505
    Beta strandi2053 – 20608
    Helixi2064 – 20729
    Turni2073 – 20753
    Beta strandi2078 – 20803
    Helixi2081 – 20833
    Turni2092 – 20943
    Beta strandi2100 – 21045
    Beta strandi2106 – 21083
    Beta strandi2111 – 21155
    Helixi2118 – 21258
    Beta strandi2127 – 21293
    Helixi2131 – 21333
    Helixi2134 – 214512
    Helixi2146 – 21483
    Helixi2150 – 216011
    Helixi2164 – 21685
    Helixi2174 – 218411

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2VB0X-ray2.40A1541-1723[»]
    2ZTXX-ray1.72A1541-1723[»]
    2ZTYX-ray1.72A1541-1723[»]
    2ZTZX-ray2.00A/B1541-1723[»]
    2ZU1X-ray1.38A/B1541-1723[»]
    2ZU3X-ray1.75A1541-1723[»]
    3CDUX-ray2.10A1724-2185[»]
    3CDWX-ray2.50A1724-2185[»]
    H1519-1540[»]
    ProteinModelPortaliP03313.
    SMRiP03313. Positions 2-69, 77-570, 583-1001, 1541-2185.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP03313.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini2 – 14951494CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini1512 – 2185674CytoplasmicSequence AnalysisAdd
    BLAST

    Intramembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Intramembranei1496 – 151116Sequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini1205 – 1361157SF3 helicasePROSITE-ProRule annotationAdd
    BLAST
    Domaini1541 – 1706166Peptidase C3Add
    BLAST
    Domaini1950 – 2066117RdRp catalyticPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni568 – 58417Amphipatic alpha-helixSequence AnalysisAdd
    BLAST
    Regioni1430 – 145324DisorderedBy 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.

    P03313-1 [UniParc]FASTAAdd to Basket

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    MGAQVSTQKT GAHETRLNAS GNSIIHYTNI NYYKDAASNS ANRQDFTQDP     50
    GKFTEPVKDI MIKSLPALNS PTVEECGYSD RARSITLGNS TITTQECANV 100
    VVGYGVWPDY LKDSEATAED QPTQPDVATC RFYTLDSVQW QKTSPGWWWK 150
    LPDALSNLGL FGQNMQYHYL GRTGYTVHVQ CNASKFHQGC LLVVCVPEAE 200
    MGCATLDNTP SSAELLGGDT AKEFADKPVA SGSNKLVQRV VYNAGMGVGV 250
    GNLTIFPHQW INLRTNNSAT IVMPYTNSVP MDNMFRHNNV TLMVIPFVPL 300
    DYCPGSTTYV PITVTIAPMC AEYNGLRLAG HQGLPTMNTP GSCQFLTSDD 350
    FQSPSAMPQY DVTPEMRIPG EVKNLMEIAE VDSVVPVQNV GEKVNSMEAY 400
    QIPVRSNEGS GTQVFGFPLQ PGYSSVFSRT LLGEILNYYT HWSGSIKLTF 450
    MFCGSAMATG KFLLAYSPPG AGAPTKRVDA MLGTHVIWDV GLQSSCVLCI 500
    PWISQTHYRF VASDEYTAGG FITCWYQTNI VVPADAQSSC YIMCFVSACN 550
    DFSVRLLKDT PFISQQNFFQ GPVEDAITAA IGRVADTVGT GPTNSEAIPA 600
    LTAAETGHTS QVVPGDTMQT RHVKNYHSRS ESTIENFLCR SACVYFTEYK 650
    NSGAKRYAEW VLTPRQAAQL RRKLEFFTYV RFDLELTFVI TSTQQPSTTQ 700
    NQDAQILTHQ IMYVPPGGPV PDKVDSYVWQ TSTNPSVFWT EGNAPPRMSI 750
    PFLSIGNAYS NFYDGWSEFS RNGVYGINTL NNMGTLYARH VNAGSTGPIK 800
    STIRIYFKPK HVKAWIPRPP RLCQYEKAKN VNFQPSGVTT TRQSITTMTN 850
    TGAFGQQSGA VYVGNYRVVN RHLATSADWQ NCVWESYNRD LLVSTTTAHG 900
    CDIIARCQCT TGVYFCASKN KHYPISFEGP GLVEVQESEY YPRRYQSHVL 950
    LAAGFSEPGD CGGILRCEHG VIGIVTMGGE GVVGFADIRD LLWLEDDAME 1000
    QGVKDYVEQL GNAFGSGFTN QICEQVNLLK ESLVGQDSIL EKSLKALVKI 1050
    ISALVIVVRN HDDLITVTAT LALIGCTSSP WRWLKQKVSQ YYGIPMAERQ 1100
    NNSWLKKFTE MTNACKGMEW IAVKIQKFIE WLKVKILPEV REKHEFLNRL 1150
    KQLPLLESQI ATIEQSAPSQ SDQEQLFSNV QYFAHYCRKY APLYAAEAKR 1200
    VFSLEKKMSN YIQFKSKCRI EPVCLLLHGS PGAGKSVATN LIGRSLAEKL 1250
    NSSVYSLPPD PDHFDGYKQQ AVVIMDDLCQ NPDGKDVSLF CQMVSSVDFV 1300
    PPMAALEEKG ILFTSPFVLA STNAGSINAP TVSDSRALAR RFHFDMNIEV 1350
    ISMYSQNGKI NMPMSVKTCD DECCPVNFKK CCPLVCGKAI QFIDRRTQVR 1400
    YSLDMLVTEM FREYNHRHSV GTTLEALFQG PPVYREIKIS VAPETPPPPA 1450
    IADLLKSVDS EAVREYCKEK GWLVPEINST LQIEKHVSRA FICLQALTTF 1500
    VSVAGIIYII YKLFAGFQGA YTGVPNQKPR VPTLRQAKVQ GPAFEFAVAM 1550
    MKRNSSTVKT EYGEFTMLGI YDRWAVLPRH AKPGPTILMN DQEVGVLDAK 1600
    ELVDKDGTNL ELTLLKLNRN EKFRDIRGFL AKEEVEVNEA VLAINTSKFP 1650
    NMYIPVGQVT EYGFLNLGGT PTKRMLMYNF PTRAGQCGGV LMSTGKVLGI 1700
    HVGGNGHQGF SAALLKHYFN DEQGEIEFIE SSKDAGFPVI NTPSKTKLEP 1750
    SVFHQVFEGN KEPAVLRSGD PRLKANFEEA IFSKYIGNVN THVDEYMLEA 1800
    VDHYAGQLAT LDISTEPMKL EDAVYGTEGL EALDLTTSAG YPYVALGIKK 1850
    RDILSKKTKD LTKLKECMDK YGLNLPMVTY VKDELRSIEK VAKGKSRLIE 1900
    ASSLNDSVAM RQTFGNLYKT FHLNPGVVTG SAVGCDPDLF WSKIPVMLDG 1950
    HLIAFDYSGY DASLSPVWFA CLKMLLEKLG YTHKETNYID YLCNSHHLYR 2000
    DKHYFVRGGM PSGCSGTSIF NSMINNIIIR TLMLKVYKGI DLDQFRMIAY 2050
    GDDVIASYPW PIDASLLAEA GKGYGLIMTP ADKGECFNEV TWTNATFLKR 2100
    YFRADEQYPF LVHPVMPMKD IHESIRWTKD PKNTQDHVRS LCLLAWHNGE 2150
    HEYEEFIRKI RSVPVGRCLT LPAFSTLRRK WLDSF 2185
    Length:2,185
    Mass (Da):243,453
    Last modified:January 23, 2007 - v4
    Checksum:i1B5ECE3DA47338FF
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti16 – 161R → G in AAA74400. (PubMed:3027968)Curated
    Sequence conflicti177 – 1771V → D in AAA74400. (PubMed:3027968)Curated
    Sequence conflicti469 – 4691P → L in AAA74400. (PubMed:3027968)Curated
    Sequence conflicti487 – 4871I → V in AAA74400. (PubMed:3027968)Curated
    Sequence conflicti510 – 5101F → Y in AAA74400. (PubMed:3027968)Curated
    Sequence conflicti516 – 5161Y → C in AAA74400. (PubMed:3027968)Curated
    Sequence conflicti566 – 5661Q → E in AAA74400. (PubMed:3027968)Curated
    Sequence conflicti593 – 5931T → N in AAA74400. (PubMed:3027968)Curated
    Sequence conflicti650 – 6501K → E in AAA74400. (PubMed:3027968)Curated
    Sequence conflicti854 – 86512FGQQS…VYVGN → IWTTIRGSVCGD in AAA74400. (PubMed:3027968)CuratedAdd
    BLAST
    Sequence conflicti873 – 8731L → S in AAA74400. (PubMed:3027968)Curated
    Sequence conflicti1097 – 10971A → P in AAA74400. (PubMed:3027968)Curated
    Sequence conflicti1280 – 12801Q → H in AAA74400. (PubMed:3027968)Curated
    Sequence conflicti1437 – 14371I → F in AAA74400. (PubMed:3027968)Curated
    Sequence conflicti1503 – 15031V → M in AAA74400. (PubMed:3027968)Curated
    Sequence conflicti1616 – 16161K → E in AAA74400. (PubMed:3027968)Curated
    Sequence conflicti1624 – 16241R → G in AAA74400. (PubMed:3027968)Curated
    Sequence conflicti1627 – 16271R → G in AAA74400. (PubMed:3027968)Curated
    Sequence conflicti1630 – 16301L → V in AAA74400. (PubMed:3027968)Curated
    Sequence conflicti1718 – 17181Y → N in AAA74400. (PubMed:3027968)Curated
    Sequence conflicti1734 – 17341D → V in AAA74400. (PubMed:3027968)Curated
    Sequence conflicti1758 – 17581E → V(PubMed:3027968)Curated
    Sequence conflicti1758 – 17581E → V(PubMed:6088796)Curated
    Sequence conflicti1824 – 18241V → R(PubMed:3027968)Curated
    Sequence conflicti1824 – 18241V → R(PubMed:6088796)Curated
    Sequence conflicti1867 – 18671C → R(PubMed:3027968)Curated
    Sequence conflicti1867 – 18671C → R(PubMed:6088796)Curated
    Sequence conflicti1880 – 18801Y → H(PubMed:3027968)Curated
    Sequence conflicti1880 – 18801Y → H(PubMed:6088796)Curated
    Sequence conflicti2001 – 20011D → N(PubMed:3027968)Curated
    Sequence conflicti2001 – 20011D → N(PubMed:6088796)Curated
    Sequence conflicti2095 – 20951A → V(PubMed:3027968)Curated
    Sequence conflicti2095 – 20951A → V(PubMed:6088796)Curated
    Sequence conflicti2115 – 21151V → A(PubMed:3027968)Curated
    Sequence conflicti2115 – 21151V → A(PubMed:6088796)Curated
    Sequence conflicti2175 – 21751S → T(PubMed:3027968)Curated
    Sequence conflicti2175 – 21751S → T(PubMed:6088796)Curated
    Sequence conflicti2178 – 21781R → G(PubMed:3027968)Curated
    Sequence conflicti2178 – 21781R → G(PubMed:6088796)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M33854 Genomic RNA. Translation: AAA42931.1.
    K02709 Genomic RNA. Translation: AAA42932.1.
    M16572 Genomic RNA. Translation: AAA74400.1.
    PIRiA26354. GNNYB3.
    A34664. GNNYBT.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M33854 Genomic RNA. Translation: AAA42931.1 .
    K02709 Genomic RNA. Translation: AAA42932.1 .
    M16572 Genomic RNA. Translation: AAA74400.1 .
    PIRi A26354. GNNYB3.
    A34664. GNNYBT.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2VB0 X-ray 2.40 A 1541-1723 [» ]
    2ZTX X-ray 1.72 A 1541-1723 [» ]
    2ZTY X-ray 1.72 A 1541-1723 [» ]
    2ZTZ X-ray 2.00 A/B 1541-1723 [» ]
    2ZU1 X-ray 1.38 A/B 1541-1723 [» ]
    2ZU3 X-ray 1.75 A 1541-1723 [» ]
    3CDU X-ray 2.10 A 1724-2185 [» ]
    3CDW X-ray 2.50 A 1724-2185 [» ]
    H 1519-1540 [» ]
    ProteinModelPortali P03313.
    SMRi P03313. Positions 2-69, 77-570, 583-1001, 1541-2185.
    ModBasei Search...
    MobiDBi Search...

    Chemistry

    ChEMBLi CHEMBL2396505.

    Protein family/group databases

    MEROPSi C03.011.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Miscellaneous databases

    EvolutionaryTracei P03313.

    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 infectious Coxsackievirus B3 cDNA: two initial 5' uridine residues are regained during plus-strand RNA synthesis."
      Klump W.M., Bergmann I., Mueller B.C., Ameis D., Kandolf R.
      J. Virol. 64:1573-1583(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
    2. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
    3. "Replicase gene of coxsackievirus B3."
      Staalhandske P.O.K., Lindberg A.M., Pettersson U.
      J. Virol. 51:742-746(1984) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 1724-2185.
    4. "Coxsackieviruses B1, B3, and B5 use decay accelerating factor as a receptor for cell attachment."
      Shafren D.R., Bates R.C., Agrez M.V., Herd R.L., Burns G.F., Barry R.D.
      J. Virol. 69:3873-3877(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH HOST CD55.
    5. "The coxsackie-adenovirus receptor (CAR) is used by reference strains and clinical isolates representing all six serotypes of coxsackievirus group B and by swine vesicular disease virus."
      Martino T.A., Petric M., Weingartl H., Bergelson J.M., Opavsky M.A., Richardson C.D., Modlin J.F., Finberg R.W., Kain K.C., Willis N., Gauntt C.J., Liu P.P.
      Virology 271:99-108(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH HOST CXADR.
    6. "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: FUNCTION OF PROTEIN 3A.

    Entry informationi

    Entry nameiPOLG_CXB3N
    AccessioniPrimary (citable) accession number: P03313
    Secondary accession number(s): Q66322
    , Q66323, Q66324, Q66325, Q66326, Q66327, Q66328, Q83744
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 156 of the entry and version 4 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