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P15736

- VP3_ROTS1

UniProt

P15736 - VP3_ROTS1

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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

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 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
Complete GO annotation...

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

        10         20         30         40         50
MKVLALRHSV AQVYADTQVY VHDDIKDSYE NAFLISNLTT HNILYLNYSI
60 70 80 90 100
KTLEILNKSG IAAIALQSLE ELFTLIRCNF TYDYELDIIY LHDYSYYTNN
110 120 130 140 150
EIRTDQHWIT KTNIEEYLLP GWKLTYVGYN GSETRGHYNF SFKCQNAATD
160 170 180 190 200
DDLIIEYIYS EALDFQNFML KKIKERMTTS LPIARLSNRV FRDKLFPSLL
210 220 230 240 250
KEHKNVVNVG PRNESMFTFL NYPTIKQFSN GAYLVKDTIK LKQERWLGKR
260 270 280 290 300
ISQFDIGQYK NMLNVLTAIY YYYNLYKSKP IIYMIGSAPS YWIYDVRHYS
310 320 330 340 350
DFFFETWDPL DTPYSSIHHK ELFFINDVKK LKDNSILYID IRTDRGNADW
360 370 380 390 400
KKWRKTVEEQ TINNLDIAYE YLRTGKAKVC CVKMTAMHLE LPISAKLLHH
410 420 430 440 450
PTTEIRSEFY LLLDTWDLTN IRRFIPKGVL YSFINNIITE NVFIQQPFKV
460 470 480 490 500
KVLNDSYIVA LYALSNDFNN RSEVIKLINN QKQSLITVRI NNTFKDEPKV
510 520 530 540 550
GFKNIYDWTF LPTDFDTKEA IITSYDGCLG LFGLSISLAS KPTGNNHLFI
560 570 580 590 600
LSGTDKYYKL DQFANHTSIS RRSHQIRFSE SATSYSGYIF RDLSNNNFNL
610 620 630 640 650
IGTNIENSVS GHIYNALIYY RYNYSFDLKR WIYLHSIDKV DIEGGKYYEH
660 670 680 690 700
APIELIYACR SAKEFATLQD DLTVLRYSNE IENYINTVYS ITYADDPNYF
710 720 730 740 750
IGIQFRNIPY KYDVKIPHLT FGVLHISDNM VPDVIDILKI MKNELFKMDI
760 770 780 790 800
TTSYTYMLSD GIYVANVSGV LSTYFKIYNV FYKNQITFGQ SRMFIPHITL
810 820 830
SFNNMRTVRI ETTKLQIKSI YLRKIKGDTV FDMVE
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