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Q65526

- VP3_ROTBS

UniProt

Q65526 - VP3_ROTBS

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Protein

Protein VP3

Gene
N/A
Organism
Rotavirus C (isolate Cow/Japan/Shintoku/1991) (RV-C)
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. 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 C (isolate Cow/Japan/Shintoku/1991) (RV-C)
Taxonomic identifieri33723 [NCBI]
Taxonomic lineageiVirusesdsRNA virusesReoviridaeSedoreovirinaeRotavirus
Virus hostiBos taurus (Bovine) [TaxID: 9913]

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 – 695695Protein VP3PRO_0000369871Add
BLAST

Interactioni

Subunit structurei

Interacts with VP1 (Potential). Interacts with VP2.Curated

Family & Domainsi

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.

Q65526-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MRVLGLFERG NNLNFADTYV YTWNKQYSFH ENAFLISNQV ATTIIIYLDK
60 70 80 90 100
EIVNQVNEAF NLLNSNGIPA LIIKSDHIGI FTSSNFTYDW QNKIIYFHEY
110 120 130 140 150
TYYKNNEFIV SDEFWLNTSI QDLLPYKVLF FERGLRKLYE GEEYILYNTA
160 170 180 190 200
TDDDIIYKYI YEKDVIMSGN DYSKLYDTKS FKNFVHFMRL LRMRFAVPFD
210 220 230 240 250
QLSNRVTRSR AFAKSKIHIG LRNESIPQAL DNIHHYWINY SANGMRVSEL
260 270 280 290 300
KGSGSYSEKK ISEFDIGQFK NYMNFLTLMF YIKNMKKKPS CTIIGAAPGY
310 320 330 340 350
WIPSMKKYFN IVTYDDKHVD STEHYNRYFT DDDIASVKTN GVYIDVRSDF
360 370 380 390 400
KNYDWKKRRQ LVEEETMRWL SITYKLLENR YVEAVLLKMT AMDIEIPDGY
410 420 430 440 450
FVHFPTTYRK SEYYLLVDKQ TVKRPKIKIT KSLAYGAINT IFSDNVFISG
460 470 480 490 500
KYSLKGKTEG VLALYCLSNT INPKEKVVQY ANSFSGTCMT VRLNNTYILN
510 520 530 540 550
KIIDFKTNAD YTFLPSDFQC SIKTVLTSYR GYAGVFGYAI TKDLKSDGNN
560 570 580 590 600
HIYIIPNARD DDNFDTFASH LGLSRYSHSK RFSESATTMS GYLFRDMVSG
610 620 630 640 650
KENMEDTDTE NLASGHVFNA IAHYRFDYTY DIVGWLKLHK MRKFRVKSNI
660 670 680 690
YGEHTDDEIR NAIEAAYVYY LLDGDEVGKE YAKRIMEIWD VQTWG
Length:695
Mass (Da):81,517
Last modified:November 1, 1996 - v1
Checksum:i1EF9F1ECFFAD3328
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U26552 Genomic DNA. Translation: AAB01673.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U26552 Genomic DNA. Translation: AAB01673.1 .

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 VP3 and VP4 genes of a bovine group C rotavirus: molecular evidence for a new P type."
    Jiang B., Gentsch J.R., Tsunemitsu H., Saif L.J., Glass R.I.
    Submitted (MAY-1995) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Entry informationi

Entry nameiVP3_ROTBS
AccessioniPrimary (citable) accession number: Q65526
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: November 1, 1996
Last modified: October 1, 2014
This is version 38 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

Multifunctional enzyme

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3