Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

B1NKT1

- VP3_ROTHP

UniProt

B1NKT1 - VP3_ROTHP

(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)

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

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
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/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
Complete GO annotation...

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

« Hide

        10         20         30         40         50
MKVLALRHSV AQVYADTQTY LHDDSKDEYE NAFLISNLTT HNILYLNYSL
60 70 80 90 100
KTLKILNKSG IAAVEVQSPD ELFALIRCNF TYDYENNIIY LHDYSYYTNN
110 120 130 140 150
EIRTDQHWIT KTDIIDYLLP GWKLTYVGYN GKNTRGHYNF SFSCQNAATD
160 170 180 190 200
DDIIIEYIYS NELDFQNFLL RKIKERMTTS LPIARLSNRV FRDKLFPSIV
210 220 230 240 250
NIYKKVINVG PRNESMFTFL NFPTIKQFSN GAYIVKHTIK LKQEKWLGKR
260 270 280 290 300
VSQFDIGQYK NMLNVVTTIY YYYNLYHSKP IIYMLGSAPS YWIHDIKQYS
310 320 330 340 350
DFTFETWDPL DTPYSTIHHK ELFFDKDVNK LKDNSVLYID IRTDRKNMDW
360 370 380 390 400
KEWRKVVEQQ TVNNLNIAYK YLSTGKAKVC CVKLTAMDLE LPITAKLLHH
410 420 430 440 450
PTTEVRSEFY AILDAWDIIT IKRFIPKGVF YAFINNITTE NVFIQPPFKL
460 470 480 490 500
KASPTDYIVA LYALSNDFNS RQDVINLINK QKQSLITVRM NNTFKDEPKV
510 520 530 540 550
NFKNIYDWTF LPTDFELKDS IITSYDGCLG MFGLSISLSS KPTGNNHLFI
560 570 580 590 600
INGTDKYYKL DQYANHMGIS RRSHQIRFSE SATSYSGYIF RDLSNNNFNL
610 620 630 640 650
IGTNVENSVS GHVYNALIYY RYNYAFDLKR WIYLHSIGKV TVEGGRYYEH
660 670 680 690 700
APIELIYACR SAKEFAILQD DLTVLRYANE IEGYINKVYS ITYADDPNYF
710 720 730 740 750
IGIKFNSIPY EYDVKVPHLT LGVLFISDNM IHDVVTVLKK MKTELFKTEI
760 770 780 790 800
STSYTYMLSD NIYVANASGV LSTYFKLYNM FYRNHITFGQ SRMFIPHITL
810 820 830
SFSNKQTVRI ESTRLKINSI YLRKIKGETV FDMSE
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