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P15736

- VP3_ROTS1

UniProt

P15736 - VP3_ROTS1

Protein

Protein VP3

Gene
N/A
Organism
Rotavirus A (strain SA11-Both G3-P5B[2]-I2-R2-C5-M5-A5-N2-T5-E2-H5) (RV-A) (Simian Agent 11 (strain Both))
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 64 (01 Oct 2014)
      Sequence version 2 (01 Aug 1991)
      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 SA11-Both G3-P5B[2]-I2-R2-C5-M5-A5-N2-T5-E2-H5) (RV-A) (Simian Agent 11 (strain Both))
    Taxonomic identifieri37137 [NCBI]
    Taxonomic lineageiVirusesdsRNA virusesReoviridaeSedoreovirinaeRotavirusRotavirus A
    Virus hostiMacaca mulatta (Rhesus macaque) [TaxID: 9544]
    ProteomesiUP000007180: 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_0000149537Add
    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.

    P15736-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKVLALRHSV AQVYADTQVY VHDDIKDSYE NAFLISNLTT HNILYLNYSI    50
    KTLEILNKSG IAAIALQSLE ELFTLIRCNF TYDYELDIIY LHDYSYYTNN 100
    EIRTDQHWIT KTNIEEYLLP GWKLTYVGYN GSETRGHYNF SFKCQNAATD 150
    DDLIIEYIYS EALDFQNFML KKIKERMTTS LPIARLSNRV FRDKLFPSLL 200
    KEHKNVVNVG PRNESMFTFL NYPTIKQFSN GAYLVKDTIK LKQERWLGKR 250
    ISQFDIGQYK NMLNVLTAIY YYYNLYKSKP IIYMIGSAPS YWIYDVRHYS 300
    DFFFETWDPL DTPYSSIHHK ELFFINDVKK LKDNSILYID IRTDRGNADW 350
    KKWRKTVEEQ TINNLDIAYE YLRTGKAKVC CVKMTAMHLE LPISAKLLHH 400
    PTTEIRSEFY LLLDTWDLTN IRRFIPKGVL YSFINNIITE NVFIQQPFKV 450
    KVLNDSYIVA LYALSNDFNN RSEVIKLINN QKQSLITVRI NNTFKDEPKV 500
    GFKNIYDWTF LPTDFDTKEA IITSYDGCLG LFGLSISLAS KPTGNNHLFI 550
    LSGTDKYYKL DQFANHTSIS RRSHQIRFSE SATSYSGYIF RDLSNNNFNL 600
    IGTNIENSVS GHIYNALIYY RYNYSFDLKR WIYLHSIDKV DIEGGKYYEH 650
    APIELIYACR SAKEFATLQD DLTVLRYSNE IENYINTVYS ITYADDPNYF 700
    IGIQFRNIPY KYDVKIPHLT FGVLHISDNM VPDVIDILKI MKNELFKMDI 750
    TTSYTYMLSD GIYVANVSGV LSTYFKIYNV FYKNQITFGQ SRMFIPHITL 800
    SFNNMRTVRI ETTKLQIKSI YLRKIKGDTV FDMVE 835
    Length:835
    Mass (Da):98,141
    Last modified:August 1, 1991 - v2
    Checksum:iD67C329D6A29B680
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti25 – 251I → T in CAA34198. (PubMed:2552420)Curated
    Sequence conflicti136 – 1361G → A in CAA34198. (PubMed:2552420)Curated
    Sequence conflicti388 – 3881H → D in CAA34198. (PubMed:2552420)Curated
    Sequence conflicti613 – 6131I → V in CAA34198. (PubMed:2552420)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X16387 Genomic RNA. Translation: CAA34423.1.
    X16062 Genomic RNA. Translation: CAA34198.1.
    PIRiS06085. P3XRSR.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X16387 Genomic RNA. Translation: CAA34423.1 .
    X16062 Genomic RNA. Translation: CAA34198.1 .
    PIRi S06085. P3XRSR.

    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. "Completion of the genomic sequence of the simian rotavirus SA11: nucleotide sequences of segments 1, 2, and 3."
      Mitchell D.B., Both G.W.
      Virology 177:324-331(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
    2. "Nucleotide sequence of the simian rotavirus SA11 genome segment 3."
      Liu M., Estes M.K.
      Nucleic Acids Res. 17:7991-7991(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].

    Entry informationi

    Entry nameiVP3_ROTS1
    AccessioniPrimary (citable) accession number: P15736
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1990
    Last sequence update: August 1, 1991
    Last modified: October 1, 2014
    This is version 64 of the entry and version 2 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