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B1NKT1

- VP3_ROTHP

UniProt

B1NKT1 - VP3_ROTHP

Protein

Protein VP3

Gene
N/A
Organism
Rotavirus A (strain Human/United States/P/1974 G3-P1A[8]-I1-R1-C1-M1-A1-N1-T1-E1-H1) (RV-A)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 21 (01 Oct 2014)
      Sequence version 1 (29 Apr 2008)
      Previous versions | rss
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    Functioni

    Multifunctional enzyme involved in mRNA capping. Catalyzes the formation of the 5' cap structure on the viral plus-strand transcripts. Specifically binds to GTP and displays guanylyltransferase and methyltransferase activities. Has affinity for ssRNA but not for dsRNA. Capping activity is non-specific and caps RNAs that initiate with either a G or an A residue. Together with VP1 polymerase, forms an enzyme complex positioned near the channels situated at each of the five-fold vertices of the core. Following infection, the outermost layer of the virus is lost, leaving a double-layered particle (DLP) made up of the core and VP6 shell. VP1 then catalyzes the transcription of fully conservative plus-strand genomic RNAs that are capped by VP3 and extruded through the DLP's channels into the cytoplasm where they function as mRNAs for translation of viral proteins. DLPs probably have an RNA triphosphatase activity as well, whereas open cores don't By similarity.By similarity

    Catalytic activityi

    GTP + (5')pp-Pur-mRNA = diphosphate + G(5')ppp-Pur-mRNA.
    S-adenosyl-L-methionine + G(5')pppR-RNA = S-adenosyl-L-homocysteine + m7G(5')pppR-RNA.

    GO - Molecular functioni

    1. GTP binding Source: UniProtKB-KW
    2. mRNA (guanine-N7-)-methyltransferase activity Source: UniProtKB-EC
    3. mRNA guanylyltransferase activity Source: UniProtKB-EC
    4. RNA binding Source: UniProtKB-KW

    GO - Biological processi

    1. viral process Source: InterPro

    Keywords - Molecular functioni

    Methyltransferase, Nucleotidyltransferase, Transferase

    Keywords - Biological processi

    mRNA capping, mRNA processing

    Keywords - Ligandi

    GTP-binding, Nucleotide-binding, RNA-binding, S-adenosyl-L-methionine

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Protein VP3
    Including the following 2 domains:
    mRNA guanylyltransferase (EC:2.7.7.50)
    mRNA (guanine-N(7)-)-methyltransferase (EC:2.1.1.56)
    OrganismiRotavirus A (strain Human/United States/P/1974 G3-P1A[8]-I1-R1-C1-M1-A1-N1-T1-E1-H1) (RV-A)
    Taxonomic identifieri10957 [NCBI]
    Taxonomic lineageiVirusesdsRNA virusesReoviridaeSedoreovirinaeRotavirusRotavirus A
    Virus hostiHomo sapiens (Human) [TaxID: 9606]
    ProteomesiUP000007047: Genome

    Subcellular locationi

    Virion Curated
    Note: Attached inside the inner capsid as a minor component. Also found in spherical cytoplasmic structures, called virus factories, that appear early after infection and are the site of viral replication and packaging Potential.Curated

    GO - Cellular componenti

    1. viral nucleocapsid Source: InterPro

    Keywords - Cellular componenti

    Virion

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 835835Protein VP3PRO_0000368086Add
    BLAST

    Interactioni

    Subunit structurei

    Interacts with VP1 Potential. Interacts with VP2 By similarity.By similarityCurated

    Family & Domainsi

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi270 – 2734Poly-Tyr

    Sequence similaritiesi

    Belongs to the rotavirus VP3 family.Curated

    Family and domain databases

    InterProiIPR011181. VP3_Rotav.
    [Graphical view]
    PfamiPF06929. Rotavirus_VP3. 1 hit.
    [Graphical view]
    PIRSFiPIRSF004015. LigT_rotavirus. 1 hit.
    PROSITEiPS51589. SAM_MT56_VP3. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    B1NKT1-1 [UniParc]FASTAAdd to Basket

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    MKVLALRHSV AQVYADTQTY LHDDSKDEYE NAFLISNLTT HNILYLNYSL    50
    KTLKILNKSG IAAVEVQSPD ELFALIRCNF TYDYENNIIY LHDYSYYTNN 100
    EIRTDQHWIT KTDIIDYLLP GWKLTYVGYN GKNTRGHYNF SFSCQNAATD 150
    DDIIIEYIYS NELDFQNFLL RKIKERMTTS LPIARLSNRV FRDKLFPSIV 200
    NIYKKVINVG PRNESMFTFL NFPTIKQFSN GAYIVKHTIK LKQEKWLGKR 250
    VSQFDIGQYK NMLNVVTTIY YYYNLYHSKP IIYMLGSAPS YWIHDIKQYS 300
    DFTFETWDPL DTPYSTIHHK ELFFDKDVNK LKDNSVLYID IRTDRKNMDW 350
    KEWRKVVEQQ TVNNLNIAYK YLSTGKAKVC CVKLTAMDLE LPITAKLLHH 400
    PTTEVRSEFY AILDAWDIIT IKRFIPKGVF YAFINNITTE NVFIQPPFKL 450
    KASPTDYIVA LYALSNDFNS RQDVINLINK QKQSLITVRM NNTFKDEPKV 500
    NFKNIYDWTF LPTDFELKDS IITSYDGCLG MFGLSISLSS KPTGNNHLFI 550
    INGTDKYYKL DQYANHMGIS RRSHQIRFSE SATSYSGYIF RDLSNNNFNL 600
    IGTNVENSVS GHVYNALIYY RYNYAFDLKR WIYLHSIGKV TVEGGRYYEH 650
    APIELIYACR SAKEFAILQD DLTVLRYANE IEGYINKVYS ITYADDPNYF 700
    IGIKFNSIPY EYDVKVPHLT LGVLFISDNM IHDVVTVLKK MKTELFKTEI 750
    STSYTYMLSD NIYVANASGV LSTYFKLYNM FYRNHITFGQ SRMFIPHITL 800
    SFSNKQTVRI ESTRLKINSI YLRKIKGETV FDMSE 835
    Length:835
    Mass (Da):97,856
    Last modified:April 29, 2008 - v1
    Checksum:i134FE1363B1F05ED
    GO

    Sequence cautioni

    The sequence ABB18255.1 differs from that shown. Reason: Frameshift at position 139.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti294 – 2941H → Y in ABB18255. (PubMed:16972027)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    EF583039 Genomic RNA. Translation: ABU87848.1.
    DQ200932 Genomic RNA. Translation: ABB18255.1. Frameshift.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    EF583039 Genomic RNA. Translation: ABU87848.1 .
    DQ200932 Genomic RNA. Translation: ABB18255.1 . Frameshift.

    3D structure databases

    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Family and domain databases

    InterProi IPR011181. VP3_Rotav.
    [Graphical view ]
    Pfami PF06929. Rotavirus_VP3. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF004015. LigT_rotavirus. 1 hit.
    PROSITEi PS51589. SAM_MT56_VP3. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Full genome-based classification of rotaviruses reveals a common origin between human Wa-Like and porcine rotavirus strains and human DS-1-like and bovine rotavirus strains."
      Matthijnssens J., Ciarlet M., Heiman E.M., Arijs I., Delbeke T., McDonald S.M., Palombo E.A., Iturriza-Gomara M., Maes P., Patton J.T., Rahman M., Van Ranst M.
      J. Virol. 82:3204-3219(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
    2. "Genetic characterization of VP3 gene of group A rotaviruses."
      Subodh S., Bhan M.K., Ray P.
      Virus Genes 33:143-145(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 138-294.

    Entry informationi

    Entry nameiVP3_ROTHP
    AccessioniPrimary (citable) accession number: B1NKT1
    Secondary accession number(s): Q1ADF3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 14, 2009
    Last sequence update: April 29, 2008
    Last modified: October 1, 2014
    This is version 21 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programViral Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Multifunctional enzyme

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3