Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

A2T3S5

- VP3_ROTSH

UniProt

A2T3S5 - VP3_ROTSH

Protein

Protein VP3

Gene
N/A
Organism
Rotavirus A (isolate Monkey/South Africa/SA11-H96/1958 G3-P5B[2]-I2-R2-C5-M5-A5-N5-T5-E2-H5) (RV-A) (Simian Agent 11 (isolate SI/South Africa/H96/58))
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 31 (01 Oct 2014)
      Sequence version 1 (06 Mar 2007)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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 (isolate Monkey/South Africa/SA11-H96/1958 G3-P5B[2]-I2-R2-C5-M5-A5-N5-T5-E2-H5) (RV-A) (Simian Agent 11 (isolate SI/South Africa/H96/58))
    Taxonomic identifieri450149 [NCBI]
    Taxonomic lineageiVirusesdsRNA virusesReoviridaeSedoreovirinaeRotavirusRotavirus A
    Virus hostiCercopithecus pygerythrus (Vervet monkey) [TaxID: 60710]
    ProteomesiUP000001119: 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_0000367814Add
    BLAST

    Interactioni

    Subunit structurei

    Interacts with VP1 Potential. Interacts with VP2.1 PublicationCurated

    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.

    A2T3S5-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKVLALRHSV AQVYADTQVY VHDDTKDSYE 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 CVKMTAMDLE 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 GHVYNALIYY RYNYSFDLKR WIYLHSIDKV DIEGGKYYEL 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):98,069
    Last modified:March 6, 2007 - v1
    Checksum:iB761FCA189B7FBB5
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    DQ838645 Genomic RNA. Translation: ABG75824.1.
    RefSeqiYP_002302228.1. NC_011508.2.

    Genome annotation databases

    GeneIDi7011370.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    DQ838645 Genomic RNA. Translation: ABG75824.1 .
    RefSeqi YP_002302228.1. NC_011508.2.

    3D structure databases

    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 7011370.

    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. "Genome heterogeneity of SA11 rotavirus due to reassortment with 'O' agent."
      Small C., Barro M., Brown T.L., Patton J.T.
      Virology 359:415-424(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
    2. "The N terminus of rotavirus VP2 is necessary for encapsidation of VP1 and VP3."
      Zeng C.Q.-Y., Estes M.K., Charpilienne A., Cohen J.
      J. Virol. 72:201-208(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH VP2.
    3. "Rotavirus open cores catalyze 5'-capping and methylation of exogenous RNA: evidence that VP3 is a methyltransferase."
      Chen D., Luongo C.L., Nibert M.L., Patton J.T.
      Virology 265:120-130(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.

    Entry informationi

    Entry nameiVP3_ROTSH
    AccessioniPrimary (citable) accession number: A2T3S5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 24, 2009
    Last sequence update: March 6, 2007
    Last modified: October 1, 2014
    This is version 31 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, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3