Reviewed, UniProtKB/Swiss-Prot A2T3S5 (VP3_ROTSH)

Names and origin

Protein names	Recommended name:     Protein VP3 Including the following 2 domains:     1- Recommended name:             mRNA guanylyltransferase               EC=2.7.7.50     2- Recommended name:             mRNA (guanine-N(7)-)-methyltransferase               EC=2.1.1.56
Organism	Rotavirus A (isolate Monkey/South Africa/SA11-H96/1958 G3-P5B[2]-I2-R2-C5-M5-A5-N5-T5-E2-H5) (RV-A) (Simian Agent 11 (isolate SI/South Africa/H96/58))
Taxonomic identifier	450149 [NCBI]
Taxonomic lineage	Viruses › dsRNA viruses › Reoviridae › Rotavirus › Rotavirus A
Virus host	Cercopithecus pygerythrus (Vervet monkey) [TaxID: 60710]

Protein attributes

Sequence length	835 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

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. 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.
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	Core protein Virion
Ligand	GTP-binding Nucleotide-binding RNA-binding S-adenosyl-L-methionine
Molecular function	Methyltransferase Nucleotidyltransferase Transferase
Technical term	Complete proteome Multifunctional enzyme Virus reference strain
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: UniProtKB-KW
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 – 835	835	Protein VP3		PRO_0000367814
Regions
	Compositional bias	270 – 273	4	Poly-Tyr

Sequences

	Sequence		Length	Mass (Da)
	A2T3S5-1 [UniParc]. Last modified March 6, 2007. Version 1. Checksum: B761FCA189B7FBB5	FASTA	835	98,069
	10 20 30 40 50 60 MKVLALRHSV AQVYADTQVY VHDDTKDSYE NAFLISNLTT HNILYLNYSI KTLEILNKSG 70 80 90 100 110 120 IAAIALQSLE ELFTLIRCNF TYDYELDIIY LHDYSYYTNN EIRTDQHWIT KTNIEEYLLP 130 140 150 160 170 180 GWKLTYVGYN GSETRGHYNF SFKCQNAATD DDLIIEYIYS EALDFQNFML KKIKERMTTS 190 200 210 220 230 240 LPIARLSNRV FRDKLFPSLL KEHKNVVNVG PRNESMFTFL NYPTIKQFSN GAYLVKDTIK 250 260 270 280 290 300 LKQERWLGKR ISQFDIGQYK NMLNVLTAIY YYYNLYKSKP IIYMIGSAPS YWIYDVRHYS 310 320 330 340 350 360 DFFFETWDPL DTPYSSIHHK ELFFINDVKK LKDNSILYID IRTDRGNADW KKWRKTVEEQ 370 380 390 400 410 420 TINNLDIAYE YLRTGKAKVC CVKMTAMDLE LPISAKLLHH PTTEIRSEFY LLLDTWDLTN 430 440 450 460 470 480 IRRFIPKGVL YSFINNIITE NVFIQQPFKV KVLNDSYIVA LYALSNDFNN RSEVIKLINN 490 500 510 520 530 540 QKQSLITVRI NNTFKDEPKV GFKNIYDWTF LPTDFDTKEA IITSYDGCLG LFGLSISLAS 550 560 570 580 590 600 KPTGNNHLFI LSGTDKYYKL DQFANHTSIS RRSHQIRFSE SATSYSGYIF RDLSNNNFNL 610 620 630 640 650 660 IGTNIENSVS GHVYNALIYY RYNYSFDLKR WIYLHSIDKV DIEGGKYYEL APIELIYACR 670 680 690 700 710 720 SAKEFATLQD DLTVLRYSNE IENYINTVYS ITYADDPNYF IGIQFRNIPY KYDVKIPHLT 730 740 750 760 770 780 FGVLHISDNM VPDVIDILKI MKNELFKMDI TTSYTYMLSD GIYVANVSGV LSTYFKIYNV 790 800 810 820 830 FYKNQITFGQ SRMFIPHITL SFNNMRTVRI ETTKLQIKSI YLRKIKGDTV FDMVE

References

[1]	"Genome heterogeneity of SA11 rotavirus due to reassortment with 'O' agent." Small C., Barro M., Brown T.L., Patton J.T. Virology 359:415-424(2007) [PubMed: 17059839] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
[2]	"The N terminus of rotavirus VP2 is necessary for encapsidation of VP1 and VP3." Zeng C.Q.-Y., Estes M.K., Charpilienne A., Cohen J. J. Virol. 72:201-208(1998) [PubMed: 9420216] [Abstract] Cited for: INTERACTION WITH VP2.
[3]	"Rotavirus open cores catalyze 5'-capping and methylation of exogenous RNA: evidence that VP3 is a methyltransferase." Chen D., Luongo C.L., Nibert M.L., Patton J.T. Virology 265:120-130(1999) [PubMed: 10603323] [Abstract] Cited for: FUNCTION.

Cross-references

Sequence databases
EMBLGenBankDDBJ	DQ838645 Genomic RNA. Translation: ABG75824.1.
RefSeq	YP_002302228.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	7011370.
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_ROTSH

Accession

Primary (citable) accession number: A2T3S5

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 24, 2009
Last sequence update:	March 6, 2007
Last modified:	June 16, 2009
This is version 14 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

Virus (Virus annotation project)