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P29813

- POLG_EC11G

UniProt

P29813 - POLG_EC11G

Protein

Genome polyprotein

Gene
N/A
Organism
Echovirus 11 (strain Gregory)
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 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 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
    Sitei331 – 3322Cleavage; by Protease 3CSequence Analysis
    Active sitei882 – 8821For Protease 2A activityBy similarity
    Active sitei900 – 9001For Protease 2A activityBy similarity
    Active sitei971 – 9711For Protease 2A activityBy similarity
    Sitei1011 – 10122Cleavage; by Protease 3CSequence Analysis
    Sitei1439 – 14402Cleavage; by Protease 3CSequence Analysis
    Sitei1528 – 15292Cleavage; by Protease 3CSequence Analysis
    Sitei1550 – 15512Cleavage; by Protease 3CSequence Analysis
    Active sitei1590 – 15901For Protease 3C activitySequence Analysis
    Active sitei1621 – 16211For Protease 3C activitySequence Analysis
    Active sitei1697 – 16971For Protease 3C activityBy similarity
    Sitei1733 – 17342Cleavage; by Protease 3CSequence Analysis
    Active sitei2062 – 20621For 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
    OrganismiEchovirus 11 (strain Gregory)
    Taxonomic identifieri31705 [NCBI]
    Taxonomic lineageiVirusesssRNA positive-strand viruses, no DNA stagePicornaviralesPicornaviridaeEnterovirusEnterovirus B
    Virus hostiHomo sapiens (Human) [TaxID: 9606]
    ProteomesiUP000002684: 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 – 21952194Genome polyproteinBy similarityPRO_0000426431Add
    BLAST
    Chaini2 – 850849P1By similarityPRO_0000426432Add
    BLAST
    Chaini2 – 331330Capsid protein VP0Sequence AnalysisPRO_0000426433Add
    BLAST
    Chaini2 – 6968Capsid protein VP4Sequence AnalysisPRO_0000426434Add
    BLAST
    Chaini70 – 331262Capsid protein VP2Sequence AnalysisPRO_0000426435Add
    BLAST
    Chaini332 – 567236Capsid protein VP3Sequence AnalysisPRO_0000426436Add
    BLAST
    Chaini567 – 850284Capsid protein VP1Sequence AnalysisPRO_0000426437Add
    BLAST
    Chaini851 – 1439589P2By similarityPRO_0000426438Add
    BLAST
    Chaini851 – 1011161Protease 2ASequence AnalysisPRO_0000426439Add
    BLAST
    Chaini1012 – 111099Protein 2BSequence AnalysisPRO_0000039708Add
    BLAST
    Chaini1111 – 1439329Protein 2CSequence AnalysisPRO_0000039709Add
    BLAST
    Chaini1440 – 2195756P3By similarityPRO_0000426440Add
    BLAST
    Chaini1440 – 1550111Protein 3ABSequence AnalysisPRO_0000426441Add
    BLAST
    Chaini1440 – 152889Protein 3ASequence AnalysisPRO_0000039710Add
    BLAST
    Chaini1529 – 155022Viral protein genome-linkedSequence AnalysisPRO_0000426442Add
    BLAST
    Chaini1551 – 2195645Protein 3CDSequence AnalysisPRO_0000426443Add
    BLAST
    Chaini1551 – 1732182Protease 3CSequence AnalysisPRO_0000426444Add
    BLAST
    Chaini1733 – 2195463RNA-directed RNA polymeraseBy similarityPRO_0000426445Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Lipidationi2 – 21N-myristoyl glycine; by hostBy similarity
    Modified residuei1531 – 15311O-(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

    Proteomic databases

    PRIDEiP29813.

    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. 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
    2195
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi4 – 74
    Beta strandi25 – 295
    Helixi36 – 383
    Helixi50 – 523
    Beta strandi57 – 593
    Beta strandi63 – 653
    Beta strandi83 – 875
    Beta strandi90 – 967
    Beta strandi100 – 1023
    Turni113 – 1153
    Helixi126 – 1283
    Beta strandi138 – 1403
    Beta strandi147 – 1526
    Helixi159 – 1679
    Beta strandi168 – 18013
    Beta strandi188 – 19710
    Beta strandi203 – 2053
    Helixi212 – 2154
    Beta strandi218 – 2203
    Beta strandi225 – 2273
    Beta strandi231 – 2355
    Helixi239 – 2413
    Turni242 – 2443
    Helixi248 – 2536
    Beta strandi254 – 2607
    Turni261 – 2633
    Beta strandi265 – 2717
    Beta strandi276 – 2783
    Turni282 – 2843
    Beta strandi288 – 29912
    Beta strandi308 – 32417
    Turni339 – 3424
    Beta strandi354 – 3563
    Helixi374 – 3785
    Helixi396 – 3994
    Beta strandi401 – 4077
    Beta strandi414 – 4174
    Turni420 – 4223
    Helixi424 – 4274
    Helixi430 – 4356
    Beta strandi438 – 4425
    Beta strandi445 – 4517
    Beta strandi458 – 4669
    Beta strandi468 – 4703
    Helixi476 – 4794
    Beta strandi482 – 4887
    Beta strandi490 – 4923
    Beta strandi494 – 4996
    Beta strandi504 – 5063
    Beta strandi508 – 5114
    Beta strandi520 – 53011
    Beta strandi537 – 54711
    Beta strandi552 – 5565
    Beta strandi565 – 5673
    Helixi603 – 6053
    Helixi613 – 6164
    Helixi629 – 6313
    Helixi633 – 6375
    Beta strandi641 – 65111
    Beta strandi653 – 6553
    Helixi656 – 6583
    Beta strandi659 – 6635
    Helixi670 – 6767
    Beta strandi679 – 69618
    Beta strandi710 – 7167
    Helixi729 – 7324
    Beta strandi734 – 7363
    Beta strandi738 – 7425
    Beta strandi749 – 7524
    Beta strandi757 – 7637
    Beta strandi767 – 7704
    Helixi779 – 7824
    Beta strandi787 – 7948
    Beta strandi801 – 81919
    Beta strandi854 – 8563

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2C8Ielectron microscopy14.00A570-857[»]
    B79-328[»]
    C332-569[»]
    D2-69[»]
    ProteinModelPortaliP29813.
    SMRiP29813. Positions 2-69, 79-330, 332-858, 862-1011, 1551-2195.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP29813.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini2 – 15051504CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini1522 – 2195674CytoplasmicSequence AnalysisAdd
    BLAST

    Intramembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Intramembranei1506 – 152116Sequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini1215 – 1371157SF3 helicasePROSITE-ProRule annotationAdd
    BLAST
    Domaini1551 – 1716166Peptidase C3Add
    BLAST
    Domaini1960 – 2076117RdRp catalyticPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni567 – 58317Amphipatic alpha-helixSequence AnalysisAdd
    BLAST
    Regioni1440 – 146324DisorderedBy 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.

    P29813-1 [UniParc]FASTAAdd to Basket

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    MGAQVSTQKT GAHETGLNAS GSSIIHYTNI NYYKDAASNS ANRQEFSQDP     50
    GKFTEPVKDI MVKSLPALNS PSAEECGYSD RVRSITLGNS TITTQESANV 100
    VVGYGRWPEY LKDNEATAED QPTQPDVATC RFYTLESVTW ERDSPGWWWK 150
    FPDALKDMGL FGQNMYYHYL GRAGYTLHVQ CNASKFHQGC LLVVCVPEAE 200
    MGCSQVDGTV NEHGLSEGET AKKFSSTSTN GTNTVQTIVT NAGMGVGVGN 250
    LTIYPHQWIN LRTNNCATIV MPYINNVPMD NMFRHHNFTL MIIPFVPLDY 300
    SSDSSTYVPI TVTVAPMCAE YNGLRLSTSL QGLPVMNTPG SNQFLTSDDF 350
    QSPSAMPQFD VTPELNIPGE VQNLMEIAEV DSVVPVNNVE GKLDTMEVYR 400
    IPVQSGNHQS DQVFGFQVQP GLDSVFKHTL LGEILNYFAH WSGSIKLTFV 450
    FCGSAMATGK FLLAYAPPGA NAPKNRKDAM LGTHIIWDVG LQSSCVLCVP 500
    WISQTHYRLV QQDEYTSAGN VTCWYQTGIV VPAGTPTSCS IMCFVSACND 550
    FSVRLLKDTP FIEQTALLQG DVVEAVENAV ARVADTIGSG PSNSQAVPAL 600
    TAVETGHTSQ VTPSDTMQTR HVKNYHSRSE SSIENFLSRS ACVYMGGYHT 650
    TNTDQTKLFA SWTISARRMV QMRRKLEIFT YVRFDVEVTF VITSKQDQGS 700
    RLGQDMPPLT HQIMYIPPGG PIPKSVTDYA WQTSTNPSIF WTEGNAPPRM 750
    SIPFISIGNA YSNFYDGWSH FSQNGVYGYN TLNHMGQIYV RHVNGSSPLP 800
    MTSTVRMYFK PKHVKAWVPR PPRLCQYKNA STVNFTPTNV TDKRTSINYI 850
    PETVKPDLSN YGAFGYQSGA VYVVNYRVVN RHLATHTDWQ NCVWEDYNRD 900
    LLISTTTAHG CDVIARCRCS TGVYYCQSKG KHYPVNFEGP GLVEVQESEY 950
    YPKRYQSHVL LAAGFSEPGD CGGILRCEHG VIGIVTMGGE GVVGFADVRD 1000
    LLWLEDDAME QGVKDYVEQL GNAFGSGFTN QICEQVNLLK ESLVGQDSIL 1050
    EKSLKALVKI ISALVIVVRN HDDLITVTAT LALIGCTSSP WRWLKQKVSQ 1100
    YYGIPMAERQ NNGWLKKFTE MTNSCKGMEW ISIKIQKFIE WLKVKILPEV 1150
    REKHEFLNRL KQLPLLESQI ATIEQSAPSQ SDQEQLFSNV QYFAHYCRKY 1200
    APLYASEAKR VFSLEKKMSN YIQFKSKCRI EPVCLLLHGS PGAGKSVATN 1250
    LIGRSLAEKL NSSVYTLPPD PDHFDGYKQQ AVVIVDDLCQ NPDGKDVSLF 1300
    CQMVSSVDFV PPMAALEEKG ILFTSLFVLA STNAGSINAP TVSDSRALAR 1350
    RFHFDMNIEV ISMYSQNGKI NMPMSEKTCD EECCPVNFKR CCPLVCGKAI 1400
    QFIDRRTQVR YSLDMLVTEM FREYNHRHSV GATLEALFQG PPIYREIKIS 1450
    VAPETPPPPA IADLLKSVDS EAVREYCKEK GWLVPEVNST LQIEKHVSRA 1500
    FICLQALTTF VSVAGIIYII YKLFAGFQGA YTGMPNQKPK VPTLRQAKVQ 1550
    GPAFEFAVAM MKRNSSTVKT EYREFTMLGI YDRWAVLPRH AKPGPTILMN 1600
    NQEVGVLDAK ELVDKDGTNL ELTLLKLNRN EKFRDIRGFL AKEEVEANQA 1650
    VLAINTSKFP NMYIPVGQVT DYGFLNLGGT PTKRMLMSNF PTRAGQCGGV 1700
    LMSTGKVLGI HVGGNGHQGF SAALLKHYFN DEQGEIEFIE SSKDAGFPII 1750
    NTPSKTKLEP SVFHQVFEGD KEPAVLRNGD PRLKANFEEA IFSKYIGNVN 1800
    THVDEYMLEA VDHYAGQLAT LDISTEPMRL EDAVYGTEGL EALDLTTSAG 1850
    YPYVALGIKK RDILSRRTRD LTKLKECMDK YGLNLPMVTY VKDELRSADK 1900
    VAKGKSRLIE ASSLNDSVAM RQTFGNLYRT FHLNPGIVTG SAVGCDPDLF 1950
    WSKIPVMLDG HLIAFDYSGY DASLSPVWFA CLKLLLEKLG YTHKETNYID 2000
    YLCNSHHLYR DKHYFERGGM PSGYSGTSMF NSMINNIIIR TLMLKVYKGI 2050
    DLDQFRMIAY GDDVIASYPW PIDASLLAET GKGYGLIMTP ADKGECFNEV 2100
    TWTNVTFLKR YFRADEQYPF LVHPVMPMKD IHESIRWTKD PKNTQDHVRS 2150
    LCLLAWHNGE HEYEEFIRKI RSVPVGRCLT LPAFSTLRRK WLDSF 2195
    Length:2,195
    Mass (Da):245,407
    Last modified:January 23, 2007 - v4
    Checksum:i1CFC5DF288831AF0
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti823 – 8275RLCQY → SYANT in BAA01439. (PubMed:2170575)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X80059 Genomic RNA. Translation: CAA56365.1.
    D10582 Genomic RNA. Translation: BAA01439.1.
    PIRiA36642. GNNYEC.

    Cross-referencesi

    Web resourcesi

    Virus Particle ExploreR db

    Icosahedral capsid structure

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X80059 Genomic RNA. Translation: CAA56365.1 .
    D10582 Genomic RNA. Translation: BAA01439.1 .
    PIRi A36642. GNNYEC.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2C8I electron microscopy 14.00 A 570-857 [» ]
    B 79-328 [» ]
    C 332-569 [» ]
    D 2-69 [» ]
    ProteinModelPortali P29813.
    SMRi P29813. Positions 2-69, 79-330, 332-858, 862-1011, 1551-2195.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    MEROPSi C03.011.

    Proteomic databases

    PRIDEi P29813.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Miscellaneous databases

    EvolutionaryTracei P29813.

    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. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
    2. "Echoviruses include genetically distinct serotypes."
      Auvinen P., Hyypiae T.
      J. Gen. Virol. 71:2133-2139(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 822-2195.
    3. "Decay-accelerating factor (CD55), a glycosylphosphatidylinositol-anchored complement regulatory protein, is a receptor for several echoviruses."
      Bergelson J.M., Chan M., Solomon K.R., St John N.F., Lin H., Finberg R.W.
      Proc. Natl. Acad. Sci. U.S.A. 91:6245-6248(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH HOST CD55.
    4. "Determination of the structure of a decay accelerating factor-binding clinical isolate of echovirus 11 allows mapping of mutants with altered receptor requirements for infection."
      Stuart A.D., McKee T.A., Williams P.A., Harley C., Shen S., Stuart D.I., Brown T.D., Lea S.M.
      J. Virol. 76:7694-7704(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 1-859.
      Strain: Isolate clinical EV11-207.

    Entry informationi

    Entry nameiPOLG_EC11G
    AccessioniPrimary (citable) accession number: P29813
    Secondary accession number(s): Q66785
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1993
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 135 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