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Q6LE89

- VP6_ROTSR

UniProt

Q6LE89 - VP6_ROTSR

Protein

Intermediate capsid protein VP6

Gene
N/A
Organism
Rotavirus A (strain SA11-Ramig G3-Px[x]-Ix-Rx-Cx-Mx-Ax-Nx-Tx-Ex-Hx) (RV-A) (Simian Agent 11 (strain Ramig))
Status
Reviewed - Annotation score: 2 out of 5- Protein inferred from homologyi
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    • History
      Entry version 42 (01 Oct 2014)
      Sequence version 1 (05 Jul 2004)
      Previous versions | rss
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    Functioni

    Intermediate capsid protein that self assembles to form an icosahedral capsid with a T=13 symmetry, which consists of 230 trimers of VP6, with channels at each of its five-fold vertices. This capsid constitutes the middle concentric layer of the viral mature particle. The innermost VP2 capsid and the intermediate VP6 capsid remain intact following cell entry to protect the dsRNA from degradation and to prevent unfavorable antiviral responses in the host cell during all the replication cycle of the virus. Nacent transcripts are transcribed within the structural confines of this double-layered particle (DLP) and are extruded through the channels at the five-fold axes. VP6 is required for the transcription activity of the DLP By similarity.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi153 – 1531Zinc; shared with all trimeric partnersBy similarity

    GO - Molecular functioni

    1. metal ion binding Source: UniProtKB-KW
    2. structural molecule activity Source: InterPro

    GO - Biological processi

    1. fusion of virus membrane with host plasma membrane Source: InterPro

    Keywords - Ligandi

    Metal-binding, Zinc

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Intermediate capsid protein VP6
    OrganismiRotavirus A (strain SA11-Ramig G3-Px[x]-Ix-Rx-Cx-Mx-Ax-Nx-Tx-Ex-Hx) (RV-A) (Simian Agent 11 (strain Ramig))
    Taxonomic identifieri36435 [NCBI]
    Taxonomic lineageiVirusesdsRNA virusesReoviridaeSedoreovirinaeRotavirusRotavirus A
    Virus hostiMacaca mulatta (Rhesus macaque) [TaxID: 9544]

    Subcellular locationi

    Virion
    Note: Component of the intermediate capsid. Also found in spherical cytoplasmic structures, called virus factories, that appear early after infection and are the site of viral replication and packaging By similarity.By similarity

    GO - Cellular componenti

    1. viral envelope Source: InterPro
    2. viral intermediate capsid Source: UniProtKB-KW

    Keywords - Cellular componenti

    Capsid protein, Intermediate capsid protein, Virion

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 397397Intermediate capsid protein VP6PRO_0000368184Add
    BLAST

    Post-translational modificationi

    The N-terminus is blocked.By similarity

    Interactioni

    Subunit structurei

    Homotrimer. Interacts with VP2 By similarity.By similarity

    Structurei

    3D structure databases

    ProteinModelPortaliQ6LE89.
    SMRiQ6LE89. Positions 1-397.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the rotavirus VP6 family.Curated

    Family and domain databases

    InterProiIPR008980. Capsid_hemagglutn.
    IPR001385. Rotavirus_A/C_VP6.
    IPR008935. Virus_capsid_a-hlx_vir.
    [Graphical view]
    PfamiPF00980. Rota_Capsid_VP6. 1 hit.
    [Graphical view]
    ProDomiPD001812. Rota_Capsid_VP6. 1 hit.
    [Graphical view] [Entries sharing at least one domain]
    SUPFAMiSSF48345. SSF48345. 2 hits.
    SSF49818. SSF49818. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Q6LE89-1 [UniParc]FASTAAdd to Basket

    « Hide

    MDVLYSLSKT LKDARDKIVE GTLYSNVSDL IQQFNQMIIT MNGNEFQTGG    50
    IGNLPIRNWN FNFGLLGTTL LNLDANYVET ARNTIDYFVD FVDNVCMDEM 100
    VRESQRNGIA PQSDSLRKLS AIKFKRINFD NSSEYIENWN LQNRRQRTGF 150
    TFHKPNIFPY SASFTLNRSQ PAHDNLMGTM WLNAGSEIQV AGFDYSCAIN 200
    APANIQQFEH IVPLRRVLTT ATITLLPDAE RFSFPRVINS ADGATTWFFN 250
    PVILRPNNVE VEFLLNGQII NTYQARFGTI VARNFDTIRL SFQLMRPPNM 300
    TPAVAVLFPN AQPFEHHATV GLTLRIESAV CESVLADASE TLLANVTSVR 350
    QEYAIPVGPV FPPGMNWTDL ITNYSPSRED NLQRVFTVAS IRSMLIK 397
    Length:397
    Mass (Da):44,873
    Last modified:July 5, 2004 - v1
    Checksum:i39FAC6E17AE42A46
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L33365 Genomic RNA. Translation: AAA60953.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L33365 Genomic RNA. Translation: AAA60953.1 .

    3D structure databases

    ProteinModelPortali Q6LE89.
    SMRi Q6LE89. Positions 1-397.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Family and domain databases

    InterProi IPR008980. Capsid_hemagglutn.
    IPR001385. Rotavirus_A/C_VP6.
    IPR008935. Virus_capsid_a-hlx_vir.
    [Graphical view ]
    Pfami PF00980. Rota_Capsid_VP6. 1 hit.
    [Graphical view ]
    ProDomi PD001812. Rota_Capsid_VP6. 1 hit.
    [Graphical view ] [Entries sharing at least one domain ]
    SUPFAMi SSF48345. SSF48345. 2 hits.
    SSF49818. SSF49818. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Temperature-sensitive lesions in the capsid proteins of the rotavirus mutants tsF and tsG that affect virion assembly."
      Mansell E.A., Ramig R.F., Patton J.T.
      Virology 204:69-81(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].

    Entry informationi

    Entry nameiVP6_ROTSR
    AccessioniPrimary (citable) accession number: Q6LE89
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 14, 2009
    Last sequence update: July 5, 2004
    Last modified: October 1, 2014
    This is version 42 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programViral Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    The zinc ion is not essential for either trimerization or transcription activity of the DLP. Zinc-depleted VP6 has an increased sensitivity to proteases By similarity.By similarity

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3