Q65526 (VP3_ROTBS) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names	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
Organism	Rotavirus C (isolate Cow/Japan/Shintoku/1991) (RV-C)
Taxonomic identifier	33723 [NCBI]
Taxonomic lineage	Viruses › dsRNA viruses › Reoviridae › Sedoreovirinae › Rotavirus
Virus host	Bos taurus (Bovine) [TaxID: 9913]

Protein attributes

Sequence length	695 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	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.
Catalytic activity	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.
Subunit structure	Interacts with VP1 Potential. Interacts with VP2.
Subcellular location	Virion Potential. 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.
Sequence similarities	Belongs to the rotavirus VP3 family.

Ontologies

Keywords
Biological process	mRNA capping mRNA processing
Cellular component	Virion
Ligand	GTP-binding Nucleotide-binding RNA-binding S-adenosyl-L-methionine
Molecular function	Methyltransferase Nucleotidyltransferase Transferase
Technical term	Multifunctional enzyme
Gene Ontology (GO)
Biological process	mRNA capping Inferred from electronic annotation. Source: UniProtKB-KW viral reproduction Inferred from electronic annotation. Source: InterPro
Cellular component	viral nucleocapsid Inferred from electronic annotation. Source: InterPro
Molecular function	GTP binding Inferred from electronic annotation. Source: UniProtKB-KW RNA binding Inferred from electronic annotation. Source: UniProtKB-KW mRNA (guanine-N7-)-methyltransferase activity Inferred from electronic annotation. Source: EC mRNA guanylyltransferase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 695	695	Protein VP3		PRO_0000369871

Sequences

	Sequence		Length	Mass (Da)
	Q65526 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: 1EF9F1ECFFAD3328	FASTA	695	81,517
	10 20 30 40 50 60 MRVLGLFERG NNLNFADTYV YTWNKQYSFH ENAFLISNQV ATTIIIYLDK EIVNQVNEAF 70 80 90 100 110 120 NLLNSNGIPA LIIKSDHIGI FTSSNFTYDW QNKIIYFHEY TYYKNNEFIV SDEFWLNTSI 130 140 150 160 170 180 QDLLPYKVLF FERGLRKLYE GEEYILYNTA TDDDIIYKYI YEKDVIMSGN DYSKLYDTKS 190 200 210 220 230 240 FKNFVHFMRL LRMRFAVPFD QLSNRVTRSR AFAKSKIHIG LRNESIPQAL DNIHHYWINY 250 260 270 280 290 300 SANGMRVSEL KGSGSYSEKK ISEFDIGQFK NYMNFLTLMF YIKNMKKKPS CTIIGAAPGY 310 320 330 340 350 360 WIPSMKKYFN IVTYDDKHVD STEHYNRYFT DDDIASVKTN GVYIDVRSDF KNYDWKKRRQ 370 380 390 400 410 420 LVEEETMRWL SITYKLLENR YVEAVLLKMT AMDIEIPDGY FVHFPTTYRK SEYYLLVDKQ 430 440 450 460 470 480 TVKRPKIKIT KSLAYGAINT IFSDNVFISG KYSLKGKTEG VLALYCLSNT INPKEKVVQY 490 500 510 520 530 540 ANSFSGTCMT VRLNNTYILN KIIDFKTNAD YTFLPSDFQC SIKTVLTSYR GYAGVFGYAI 550 560 570 580 590 600 TKDLKSDGNN HIYIIPNARD DDNFDTFASH LGLSRYSHSK RFSESATTMS GYLFRDMVSG 610 620 630 640 650 660 KENMEDTDTE NLASGHVFNA IAHYRFDYTY DIVGWLKLHK MRKFRVKSNI YGEHTDDEIR 670 680 690 NAIEAAYVYY LLDGDEVGKE YAKRIMEIWD VQTWG

References

[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].

Cross-references

Sequence databases
EMBL GenBank DDBJ	U26552 Genomic DNA. Translation: AAB01673.1.
3D structure databases
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Family and domain databases
InterPro	IPR011181. Pesterase_Rotav. IPR009697. Rotavirus_VP3. [Graphical view]
Pfam	PF06929. Rotavirus_VP3. 1 hit. [Graphical view]
PIRSF	PIRSF004015. LigT_rotavirus. 1 hit.
ProtoNet	Search...

Entry information

Entry name

VP3_ROTBS

Accession

Primary (citable) accession number: Q65526

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 14, 2009
Last sequence update:	November 1, 1996
Last modified:	February 8, 2011
This is version 30 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Viral Protein Annotation Program