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Q66282

- POLG_CXB3W

UniProt

Q66282 - POLG_CXB3W

Protein

Genome polyprotein

Gene
N/A
Organism
Coxsackievirus B3 (strain Woodruff)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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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. 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

    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 Woodruff)
    Taxonomic identifieri103904 [NCBI]
    Taxonomic lineageiVirusesssRNA positive-strand viruses, no DNA stagePicornaviralesPicornaviridaeEnterovirusEnterovirus B
    Virus hostiHomo sapiens (Human) [TaxID: 9606]
    ProteomesiUP000007530: 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 host
    Chaini2 – 21852184Genome polyproteinBy similarityPRO_0000426281Add
    BLAST
    Chaini2 – 848847P1By similarityPRO_0000426282Add
    BLAST
    Chaini2 – 332331Capsid protein VP0Sequence AnalysisPRO_0000426283Add
    BLAST
    Chaini2 – 6968Capsid protein VP4Sequence AnalysisPRO_0000426284Add
    BLAST
    Chaini70 – 332263Capsid protein VP2Sequence AnalysisPRO_0000426285Add
    BLAST
    Chaini333 – 568236Capsid protein VP3Sequence AnalysisPRO_0000426286Add
    BLAST
    Chaini568 – 848281Capsid protein VP1Sequence AnalysisPRO_0000426287Add
    BLAST
    Chaini849 – 1429581P2By similarityPRO_0000426288Add
    BLAST
    Chaini849 – 1001153Protease 2ASequence AnalysisPRO_0000426289Add
    BLAST
    Chaini1002 – 110099Protein 2BSequence AnalysisPRO_0000039598Add
    BLAST
    Chaini1101 – 1429329Protein 2CSequence AnalysisPRO_0000039599Add
    BLAST
    Chaini1430 – 2185756P3By similarityPRO_0000426290Add
    BLAST
    Chaini1430 – 1540111Protein 3ABSequence AnalysisPRO_0000426291Add
    BLAST
    Chaini1430 – 151889Protein 3ASequence AnalysisPRO_0000039600Add
    BLAST
    Chaini1519 – 154022Viral protein genome-linkedSequence AnalysisPRO_0000426292Add
    BLAST
    Chaini1541 – 2185645Protein 3CDSequence AnalysisPRO_0000426293Add
    BLAST
    Chaini1541 – 1722182Protease 3CSequence AnalysisPRO_0000426294Add
    BLAST
    Chaini1723 – 2185463RNA-directed RNA polymeraseBy similarityPRO_0000426295Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Lipidationi2 – 21N-myristoyl glycine; by host1 Publication
    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. 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

    IntActiQ66282. 1 interaction.

    Structurei

    Secondary structure

    1
    2185
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi4 – 74
    Beta strandi26 – 294
    Helixi36 – 383
    Helixi50 – 523
    Beta strandi57 – 593
    Beta strandi83 – 875
    Beta strandi90 – 967
    Turni113 – 1153
    Helixi126 – 1283
    Beta strandi133 – 1408
    Beta strandi147 – 1515
    Turni152 – 1543
    Helixi159 – 1679
    Beta strandi168 – 18013
    Beta strandi188 – 19710
    Beta strandi203 – 2053
    Helixi212 – 2154
    Beta strandi218 – 2203
    Beta strandi225 – 2273
    Helixi241 – 2433
    Turni244 – 2474
    Helixi250 – 2556
    Beta strandi256 – 2627
    Turni263 – 2653
    Beta strandi267 – 2737
    Beta strandi278 – 2803
    Turni284 – 2863
    Beta strandi290 – 30112
    Beta strandi310 – 32617
    Turni340 – 3434
    Beta strandi355 – 3573
    Beta strandi369 – 3746
    Helixi376 – 3794
    Helixi391 – 3955
    Helixi397 – 4004
    Beta strandi402 – 4054
    Beta strandi408 – 4103
    Beta strandi413 – 4197
    Turni421 – 4233
    Turni425 – 4295
    Helixi431 – 4366
    Beta strandi439 – 4435
    Beta strandi446 – 4527
    Beta strandi461 – 4677
    Beta strandi469 – 4713
    Helixi477 – 4804
    Beta strandi483 – 4897
    Beta strandi491 – 4933
    Beta strandi495 – 5006
    Beta strandi505 – 5128
    Beta strandi521 – 5288
    Beta strandi538 – 54811
    Beta strandi553 – 5575
    Beta strandi599 – 6024
    Helixi604 – 6063
    Helixi614 – 6174
    Helixi634 – 6385
    Beta strandi642 – 65413
    Beta strandi656 – 6616
    Helixi668 – 6747
    Beta strandi677 – 69418
    Beta strandi708 – 7147
    Helixi727 – 7304
    Beta strandi732 – 7343
    Beta strandi736 – 7405
    Beta strandi747 – 7504
    Beta strandi755 – 7617
    Beta strandi765 – 7684
    Turni769 – 7713
    Beta strandi772 – 7765
    Helixi777 – 7793
    Beta strandi785 – 7917
    Beta strandi795 – 7973
    Beta strandi799 – 81719
    Beta strandi828 – 8303

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1COVX-ray3.501571-851[»]
    270-332[»]
    3333-570[»]
    42-69[»]
    1JEWelectron microscopy22.001571-851[»]
    270-332[»]
    3333-570[»]
    42-69[»]
    ProteinModelPortaliQ66282.
    SMRiQ66282. Positions 2-69, 77-570, 583-1001, 1541-2185.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ66282.

    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.

    Q66282-1 [UniParc]FASTAAdd to Basket

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    MGAQVSTQKT GAHETGLNAS GNSIIHYTNI NYYKDAASNS ANRQDFTQDP     50
    SKFTEPVKDI MIKSLPALNS PTVEECGYSD RVRSITLGNS TITTQECANV 100
    VVGYGVWPDY LKDSEATAED QPTQPDVATC RFYTLDSVQW QKTSPGWWWK 150
    LPDALSNLGL FGQNMQYHYL GRTGYTIHVQ CNASKFHQGC LLVVCVPEAE 200
    MGCATLNNTP SSAELLGGDS AKEFADKPVA SGSNKLVQRV VYNAGMGVGV 250
    GNLTIFPHQW INLRTNNSAT IVMPYTNSVP MDNMFRHNNV TLMVIPFVPL 300
    DYCPGSTTYV PITITIAPMC AEYNGLRLAG HQGLPTMNTP GSCQFLTSDD 350
    FQSPSAMPQY DVTPEMRIPG EVKNLMEIAE VDSVVPVQNV GEKVNSMEAY 400
    QIPVRSNEGS GTQVFGFPLQ PGYSSVFSRT LLGEILNYYT HWSGSIKLTF 450
    MFCGSAMATG KFLLAYSPPG AGAPTKRVDA MLGTHVVWDV GLQSSCVLCI 500
    PWISQTHYRY VASDEYTAGG FITCWYQTNI VVPADAQSSC YIMCFVSACN 550
    DFSVRLLKDT PFISQQNFFQ GPVEDAITAA IGRVADTVGT GPTNSEAIPA 600
    LTAAETGHTS QVVPSDTMQT RHVKNYHSRS ESTIENFLCR SACVYFTEYE 650
    NSGAKRYAEW VITPRQAAQL RRKLEFFTYV RFDLELTFVI TSTQQPSTTQ 700
    NQDAQILTHQ IMYVPPGGPV PDKVDSYVWQ TSTNPSVFWT EGNAPPRMSV 750
    PFLSIGNAYS NFYDGWSEFS RNGVYGINTL NNMGTLYARH VNAGSTGPIK 800
    STIRIYFKPK HVKAWIPRPP RLCQYEKAKN VNFQPSGVTT TRQSITTMTN 850
    TGAFGQQSGA VYVGNYRVVN RHLATSADWQ NCVWENYNRD LLVSTTTAHG 900
    CDIIARCRCT TGVYFCASKN KHYPISFEGP GIVEVQESEY YPRRYQSHVL 950
    LAAGFSEPGD CGGILRCEHG VIGIVTMGGE GVVGFADIRD LLWLEDDAME 1000
    QGVKDYVEQL GNAFGSGFTN QICEQVNLLK ESLVGQDSIL EKSLKALVKI 1050
    ISALVIVVRN HDDLITVTAT LALIGCTSSP WRWLKQKVSQ YYGIPMAERQ 1100
    NNGWLKKFTE MTNACKGMEW IAIKIQKFIE WLKVKILPEV REKHEFLNRL 1150
    KQLPLLESQI ATIEQSAPSQ SDQEQLFSNV QYFAHYCRKY APLYASEAKR 1200
    VFSLEKKMSN YIQFKSKCRI EPVCLLLHGS PGAGKSVATN LIGRSLAEKL 1250
    NSSVYSLPPD PDHFDGYKQQ AVVIMDDLCQ KPDGKDVSLF CQMVSSVDFV 1300
    PPMAALEEKG ILFTSPFVLA STNAGSINAP TVSDSRALAR RFHFDMNIEV 1350
    ISMYSQNGKI NMPMSVKTCD EECCPVNFKK CCPLVCGKAI QFIDRRTQVR 1400
    YSLDMLVTEM FREYNHRHSV GATLEALFQG PPVYREIKIS VAPETPPPPR 1450
    IADLLKSVDS EAVREYCKEK GWLVPEVNST LQIEKHVSRA FICLQAITTF 1500
    VSVAGIIYII YKLFAGFQGA YTGIPNQKPK VPTLRQAKVQ GPAFEFAVAM 1550
    MKRNSSTVKT EYGEFTMLGI YDRWAVLPRH AKPGPTILMN DQEVGVLDAK 1600
    ELVDKDGTNL ELTLLKLNRN EKFRDIRGFL AKEEVEVNEA VLAINTSKFP 1650
    NMYIPVGQVT DYGFLNLGGT PTKRMLMYNF PTRAGQCGGV LMSTGKVLGI 1700
    HVGGNGHQGF SAALLKHYFN DEQGEIEFIE SSKEAGFPII NTPSKTKLEP 1750
    SVFHQVFEGD KEPAVLRNGD PRLKVNFEEA IFSKYIGNVN THVDEYMMEA 1800
    VDHYAGQLAT LDISTEPMKL EDAVYGTEGL EALDLTTSAG YPYVALGIKK 1850
    RDILSKKTRD LTKLKECMDK YGLNLPMVTY VKDELRSAEK VAKGKSRLIE 1900
    ASSLNDSVAM RQTFGNLYKT FHLNPGVVTG SAVGCDPDLF WSKIPVMLDG 1950
    HLIAFDYSGY DASLSPVWFA CLKLLLEKLG YSHKETNYID YLCNSHHLYR 2000
    DKHYFVRGGM PSGCSGTSIF NSMINNIIIR TLMLKVYKGI DLDQFRMIAY 2050
    GDDVIASYPW PIDASLLAEA GKDYGLIMTP ADKGECFNEV TWTNVTFLKR 2100
    YFRADEQYPF LVHPVMPMKD IHESIRWTKD PKNTQDHVRS LCLLAWHNGE 2150
    HEYEEFIRKI RSVPVGRCLT LPAFSTIRRK WLDSF 2185
    Length:2,185
    Mass (Da):243,682
    Last modified:January 23, 2007 - v3
    Checksum:iFD93A677904252FA
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U57056 Genomic RNA. Translation: AAB02228.1.

    Cross-referencesi

    Web resourcesi

    Virus Particle ExploreR db

    Icosahedral capsid structure

    Virus Particle ExploreR db

    Icosahedral capsid structure

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U57056 Genomic RNA. Translation: AAB02228.1 .

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1COV X-ray 3.50 1 571-851 [» ]
    2 70-332 [» ]
    3 333-570 [» ]
    4 2-69 [» ]
    1JEW electron microscopy 22.00 1 571-851 [» ]
    2 70-332 [» ]
    3 333-570 [» ]
    4 2-69 [» ]
    ProteinModelPortali Q66282.
    SMRi Q66282. Positions 2-69, 77-570, 583-1001, 1541-2185.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi Q66282. 1 interaction.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Miscellaneous databases

    EvolutionaryTracei Q66282.

    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. "A mutation in the puff region of VP2 attenuates the myocarditic phenotype of an infectious cDNA of the Woodruff virus."
      Knowlton K.U., Jeon E.S., Berkley R.W., Wessely R., Huber S.
      Submitted (APR-1996) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
    2. Cited for: STRUCTURE BY ELECTRON MICROSCOPY (3.5 ANGSTROMS) OF 70-851, MYRISTOYLATION AT GLY-2.

    Entry informationi

    Entry nameiPOLG_CXB3W
    AccessioniPrimary (citable) accession number: Q66282
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 15, 1999
    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

    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