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B1NKU3

- VP3_ROTWI

UniProt

B1NKU3 - VP3_ROTWI

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Protein

Protein VP3

Gene
N/A
Organism
Rotavirus A (isolate Human/United States/WI61/1983 G9-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 (isolate Human/United States/WI61/1983 G9-P1A[8]-I1-R1-C1-M1-A1-N1-T1-E1-H1) (RV-A)
Taxonomic identifieri578830 [NCBI]
Taxonomic lineageiVirusesdsRNA virusesReoviridaeSedoreovirinaeRotavirusRotavirus A
Virus hostiHomo sapiens (Human) [TaxID: 9606]
ProteomesiUP000006580: 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_0000368070Add
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.

B1NKU3-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MKVLALRHSV AQVYADTQTY LHDDSKDEYE NAFLISNLTT HNILYLNYSL
60 70 80 90 100
KTLKILNKSG IAAVEVQSLD ELFALIRCNF TYDYENNIVY LHDYSYYTNN
110 120 130 140 150
EIRTDQHWIT KTDITEYLLP GWKLTYVGYN GKNTRGHYNF SFSCQNAATD
160 170 180 190 200
DDIIVEYIYS NELDFQNFLL RKIKERMTTS LPIARLSNRV FRDKLFPSIM
210 220 230 240 250
NIHKKVINVG PRNESMFTFL NFPTIKQFSN GAYIVKHTIK LKQEKWLGKR
260 270 280 290 300
VSQFDIGQYK NMLNIVTTIY YYYNLYHSKP IIYMLGSAPS YWIHDIKQYS
310 320 330 340 350
DFTFETWDPL DTPYSTIHHK ELFFDKDVNK LRDNSVLYID IRTDRKNIDW
360 370 380 390 400
KEWRKIVEQQ TVSNLNIAYK YLATGKAKVC CVKLTAMDLE LPITAKLLHH
410 420 430 440 450
PTTEVRSEFY AILDVWDIIN IKRFIPKGVF YAFINNITTD NVFIQPPFKL
460 470 480 490 500
KASPTDYIVA LYALSNDFNS RQDVINLINK QKQSLITVRI NNTFKDEPKV
510 520 530 540 550
NFKNIYDWTF LPTDFELKDS VITSYDGCLG MFGLSISLSS KPTGNNHLFI
560 570 580 590 600
INGTDKYYKL DQYANHMSIS RRSHQIRFSE SATSYSGYIF RDLSNNNFNL
610 620 630 640 650
IGTNVENSVS GHVYNALIYY RYNYTFDLKR WIYLHSIGKV AVQGGRYYEH
660 670 680 690 700
APIELIYACR SAREFAILQD DLTVLRYANE IEEYINKVYS ITYADDPNYF
710 720 730 740 750
IGIKFNSIPY EYDVKVPHLT LGVLFISDNM IHDVVTVLKK MKTELFKTEI
760 770 780 790 800
STSYTYMLSD NMYVANASGV LSTYFKLYNM FYRNHITFGQ SRMFIPHITL
810 820 830
SFSNKQTVRI ESTRLKINSI YLRKIKGETV FDMSE
Length:835
Mass (Da):97,989
Last modified:April 29, 2008 - v1
Checksum:iA991BF11DC1BB8C8
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti230 – 2301N → K in AAQ21044. (PubMed:15039535)Curated
Sequence conflicti247 – 2471L → I in AAQ21044. (PubMed:15039535)Curated
Sequence conflicti567 – 5671M → V in AAQ21044. (PubMed:15039535)Curated
Sequence conflicti643 – 6431Q → E in AAQ21044. (PubMed:15039535)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AY277917 Genomic RNA. Translation: AAQ21044.1.
EF583051 Genomic RNA. Translation: ABU87860.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AY277917 Genomic RNA. Translation: AAQ21044.1 .
EF583051 Genomic RNA. Translation: ABU87860.1 .

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. "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].

Entry informationi

Entry nameiVP3_ROTWI
AccessioniPrimary (citable) accession number: B1NKU3
Secondary accession number(s): Q6WNW2
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