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Q66790

- POLG_EC16H

UniProt

Q66790 - POLG_EC16H

Protein

Genome polyprotein

Gene
N/A
Organism
Echovirus 16 (strain Harrington)
Status
Reviewed - Annotation score: 4 out of 5- Protein inferred from homologyi
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    • History
      Entry version 87 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    Protein VP1: Forms, together with VP2 and VP3, an icosahedral capsid (pseudo T=3), 300 Angstroms in diameter, composed of 60 copies of each capsid protein and enclosing the viral positive strand RNA genome. Protein VP1 mainly forms the vertices of the capsid. VP1 interacts with host cell receptor to provide virion attachment to target cell. After binding to its receptor, the capsid undergoes conformational changes. VP1 N-terminus (that contains an amphipathic alpha-helix) is externalized, VP4 is released and together, they shape a virion-cell connecting channel and a pore in the host membrane through which RNase-protected transfer of the viral genome takes place. After genome has been released, the channel shrinks By similarity.By similarity
    Protein VP2: Forms, together with VP1 and VP3, an icosahedral capsid (pseudo T=3), 300 Angstroms in diameter, composed of 60 copies of each capsid protein and enclosing the viral positive strand RNA genome.By similarity
    Protein VP3: Forms, together with VP1 and VP2, an icosahedral capsid (pseudo T=3), 300 Angstroms in diameter, composed of 60 copies of each capsid protein and enclosing the viral positive strand RNA genome.By similarity
    Protein VP4: Lies on the inner surface of the capsid shell. After binding to the host receptor, the capsid undergoes conformational changes. VP4 is released, VP1 N-terminus is externalized, and together, they shape a virion-cell connecting channel and a pore in the host membrane through which RNase-protected transfer of the viral genome takes place. After genome has been released, the channel shrinks By similarity.By similarity
    Protein VP0: Protein VP0: VP0 precursor is a component of immature procapsids, which gives rise to VP4 and VP2 after maturation. Allows the capsid to remain inactive before the maturation step By similarity.By similarity
    Protease 2A: cysteine protease that is responsible for the cleavage between the P1 and P2 regions. It cleaves the host translation initiation factor EIF4G1, in order to shut off the capped cellular mRNA transcription By similarity.By similarity

    Catalytic activityi

    Selective cleavage of Tyr-|-Gly bond in the picornavirus polyprotein.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei69 – 702CleavageSequence Analysis
    Sitei331 – 3322Cleavage; by protease 3CSequence Analysis
    Sitei854 – 8552Cleavage; by protease 2ASequence Analysis

    GO - Molecular functioni

    1. cysteine-type peptidase activity Source: UniProtKB-KW
    2. structural molecule activity Source: InterPro
    3. transferase activity Source: UniProtKB-KW

    GO - Biological processi

    1. pore-mediated entry of viral genome into host cell Source: UniProtKB-KW
    2. suppression by virus of host gene expression Source: UniProtKB-KW
    3. virion attachment to host cell Source: UniProtKB-KW

    Keywords - Molecular functioni

    Hydrolase, Protease, Thiol protease, Transferase

    Keywords - Biological processi

    Eukaryotic host gene expression shutoff by virus, Eukaryotic host translation shutoff by virus, Host gene expression shutoff by virus, Host-virus interaction, Pore-mediated penetration of viral genome into host cell, Viral attachment to host cell, Viral penetration into host cytoplasm, Virus entry into host cell

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Genome polyprotein
    Cleaved into the following 6 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):
    Protein 2A
    OrganismiEchovirus 16 (strain Harrington)
    Taxonomic identifieri103910 [NCBI]
    Taxonomic lineageiVirusesssRNA positive-strand viruses, no DNA stagePicornaviralesPicornaviridaeEnterovirusEnterovirus B
    Virus hostiHomo sapiens (Human) [TaxID: 9606]

    Subcellular locationi

    GO - Cellular componenti

    1. host cell cytoplasm Source: UniProtKB-SubCell
    2. viral capsid Source: UniProtKB-KW

    Keywords - Cellular componenti

    Capsid protein, Host cytoplasm, Virion

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed; by hostBy similarity
    Chaini2 – 331330Protein VP0Sequence AnalysisPRO_0000311060Add
    BLAST
    Chaini2 – 6968Protein VP4Sequence AnalysisPRO_0000039725Add
    BLAST
    Chaini70 – 331262Protein VP2Sequence AnalysisPRO_0000039726Add
    BLAST
    Chaini332 – 570239Protein VP3Sequence AnalysisPRO_0000039727Add
    BLAST
    Chaini571 – 854284Protein VP1Sequence AnalysisPRO_0000039728Add
    BLAST
    Chaini855 – ›862›8Protease 2ASequence AnalysisPRO_0000039729

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Lipidationi2 – 21N-myristoyl glycine; by hostBy 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
    Myristoylation of VP4 is required during RNA encapsidation and formation of the mature virus particle.By similarity

    Keywords - PTMi

    Lipoprotein, Myristate

    Structurei

    3D structure databases

    ProteinModelPortaliQ66790.
    SMRiQ66790. Positions 2-69, 79-328, 332-853.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the picornaviruses polyprotein family.Curated
    Contains 1 peptidase C3 domain.Curated

    Family and domain databases

    Gene3Di2.60.120.20. 3 hits.
    4.10.80.10. 2 hits.
    InterProiIPR003138. Pico_P1A.
    IPR001676. Picornavirus_capsid.
    IPR029053. Viral_coat.
    [Graphical view]
    PfamiPF02226. Pico_P1A. 1 hit.
    PF00073. Rhv. 3 hits.
    [Graphical view]

    Sequencei

    Sequence statusi: Fragment.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    Q66790-1 [UniParc]FASTAAdd to Basket

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    MGAQVSTQKT GAHETLLEAA QGATINYTNI NYYKDAASNS ANRQDFSQDP    50
    SKFTEPVKDI MIKSMPALNS PSAEECGYSD RVRSITLGNS TITTQESANV 100
    VVAYGRWPKY LEDDQATAED QPTQPDVATC RFYTLESVQW EANSAGWWWK 150
    FPEALKDMGL FGQNMYYHYL GRAGYTIHVQ CNASKFHQGC LLVVCVPEAE 200
    MGCAKPDENV DATNLTNGEN TCELTAGAAP AEKGKVQTAV CNATMGVAVG 250
    NLTIFPHQWI NLRTNNCATI VMPYINSVPM DNMFRHYNFT LMVIPFVPLT 300
    SMGGSTYVPI TVTIAPMCAE YNGLRLSTQH QGLPVMNVPG SNQFLTSDNF 350
    QSPCAMPEYD VTPPLDIPGE VNNLMEVAEV DSVVPVNNLS DNVKTIKAYQ 400
    IPVSAGDSSR PEAVFKFQLD PGSGSVLKHT LLGEIINYYA HWSGSIKLTF 450
    VFCGSAMATG KLLIAYSPPG ASAPATRKDA MLGTHIIWDL GLQSSCVLCV 500
    PWISQTHYRM VERDEYTTAG YISCWYQTNI IVPPDTPSQC YMLCLASACN 550
    DFSVRMLKDT PFIQQEAKLQ GEPGKAIESA ISRVADTISS GPTNSEQVPA 600
    LTAAETGHTS QVVPGDTIQT RHVKNYHSRS ESTIENFLCR SACVHIARYE 650
    AGANASNEDR FVRWEINNKE LVQLRRKCEM FTYLRYDVEV TFVITSQQDQ 700
    GTDLSQDMPV LTHQVMYVPP GGSVTKQGDS YAWQTSTNPS VFWTEGNAPP 750
    RMSIPFISIG NAYSSFYDGW SHFSQKGVYG YNTLNKMGTL FVRHVNKETP 800
    KPVTSTVRVY FKPKHIRAWI PRPPRLCPYK YKANVNFDVT AITDSRLTIT 850
    TVPQVEHNLR TA 862
    Length:862
    Mass (Da):95,399
    Last modified:January 23, 2007 - v3
    Checksum:i59587E197126595C
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Non-terminal residuei862 – 8621

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X89545 Genomic RNA. Translation: CAA61723.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X89545 Genomic RNA. Translation: CAA61723.1 .

    3D structure databases

    ProteinModelPortali Q66790.
    SMRi Q66790. Positions 2-69, 79-328, 332-853.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Family and domain databases

    Gene3Di 2.60.120.20. 3 hits.
    4.10.80.10. 2 hits.
    InterProi IPR003138. Pico_P1A.
    IPR001676. Picornavirus_capsid.
    IPR029053. Viral_coat.
    [Graphical view ]
    Pfami PF02226. Pico_P1A. 1 hit.
    PF00073. Rhv. 3 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The major echovirus group is genetically coherent and related to coxsackie B viruses."
      Huttunen P., Santti J., Pulli T., Hyypiae T.
      J. Gen. Virol. 77:715-725(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].

    Entry informationi

    Entry nameiPOLG_EC16H
    AccessioniPrimary (citable) accession number: Q66790
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 15, 1999
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 87 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programViral Protein Annotation Program

    Miscellaneousi

    Documents

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

    External Data

    Dasty 3