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Q6WVH5

- VP3_ROTHW

UniProt

Q6WVH5 - VP3_ROTHW

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Protein

Protein VP3

Gene
N/A
Organism
Rotavirus A (strain Human/United States/Wa/1974 G1-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

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.

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
Complete GO annotation...

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/Wa/1974 G1-P1A[8]-I1-R1-C1-M1-A1-N1-T1-E1-H1) (RV-A)
Taxonomic identifieri10962 [NCBI]
Taxonomic lineageiVirusesdsRNA virusesReoviridaeSedoreovirinaeRotavirusRotavirus A
Virus hostiHomo sapiens (Human) [TaxID: 9606]
ProteomesiUP000006581: Genome

Subcellular locationi

Virion Reviewed prediction
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 Reviewed prediction.

GO - Cellular componenti

  1. viral nucleocapsid Source: InterPro
Complete GO annotation...

Keywords - Cellular componenti

Virion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 835835Protein VP3PRO_0000368087Add
BLAST

Interactioni

Subunit structurei

Interacts with VP1 Reviewed prediction. Interacts with VP2 By similarity.

Family & Domainsi

Compositional bias

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

Sequence similaritiesi

Belongs to the rotavirus VP3 family.

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.

Q6WVH5-1 [UniParc]FASTAAdd to Basket

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MKVLALRHSV AQVYADTQTY LHDDSKDEYE NAFLISNLTT HNILYLNYSL    50
KTLKILNKSG IAAVEVQSPD ELFALIRCNF TYDYEDNIVY LHDYSYYTNN 100
EIRTDQHWIT KTDIIDYLLP GWKLTYVGYN GKNTRGHYNF SFICQNAATD 150
DDIIIEYIYS NELDFQNFLL RKIKERMTTS LPIARLSNRV FRDKLFPSIV 200
NIHKKVINVG PRNESMFTFL NFPTIKQFSN GAYIVKHTIK LKQEKWLGKR 250
VSQFDIGQYK NMLNVVTTIY YYYNLYYSKP IIYMLGSAPS YWIYDIKQYS 300
DFTFETWDPL DTPYSTTHHK ELFFDKDVNK LKDNSVLYID IRTDRGNMDW 350
KEWRKIVEQQ TVSNLNIAYK YLSTGKAKVC CVKLTAMDLE LPITAKLLHH 400
PTTEVRSEFY AILDVWDIIT IKRFIPKGVF YAFINNVTTE NVFIQPPFKL 450
KTSPTDYIVA LYALSNDLNS RQDVINLINK QKQSLITVRI NNTFKDEPKV 500
NFKNIYDWTF LPTDFELKDS IITSYDGCLG IFGLSISLSS KPTGNNHLFI 550
INGTDKYDKL DQYANHMGVS RRSHQIRFSE SATSYSGYIF RDLSNNNFNL 600
IGTNVENSVS GHVYNALIYY RYNYAFDLKR WIYLHSIGKV AVEGGRYYEH 650
APIELIYACR SAKEFAILQD DLTVLRYANE IEGYINKVYS ITYADDPNYF 700
IGIKFNSIPY EYDVKIPHLT LGVLFISDNM IHDVITVLKK MKTELFKMEI 750
STSYTYMLSD NTYVANASGV LSTYFKLYNM FYRNHITFGQ SRMFIPHITL 800
SFSNKQTVRI ESTKLRINSI YLRKIKGETV FDMSE 835
Length:835
Mass (Da):97,727
Last modified:July 5, 2004 - v1
Checksum:i3B3C6D920E4844CA
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AY267335 Genomic RNA. Translation: AAQ02692.1.
AJ292379 Genomic RNA. Translation: CAB98137.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AY267335 Genomic RNA. Translation: AAQ02692.1 .
AJ292379 Genomic RNA. Translation: CAB98137.1 .

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. "Sequence analysis of the guanylyltransferase (VP3) of group A rotaviruses."
    Cook J.P., McCrae M.A.
    J. Gen. Virol. 85:929-932(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
  2. "Frequent reassortments may explain the genetic heterogeneity of rotaviruses: analysis of Finnish rotavirus strains."
    Maunula L., Von Bonsdorff C.H.
    J. Virol. 76:11793-11800(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 154-267.

Entry informationi

Entry nameiVP3_ROTHW
AccessioniPrimary (citable) accession number: Q6WVH5
Secondary accession number(s): Q9ICZ7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: July 5, 2004
Last modified: April 16, 2014
This is version 29 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

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