ID VP3_ROTCC Reviewed; 829 AA. AC Q6WNV6; DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot. DT 05-JUL-2004, sequence version 1. DT 24-JAN-2024, entry version 42. DE RecName: Full=Protein VP3 {ECO:0000255|HAMAP-Rule:MF_04128}; DE Includes: DE RecName: Full=2',5'-phosphodiesterase {ECO:0000255|HAMAP-Rule:MF_04128}; DE EC=3.1.4.- {ECO:0000255|HAMAP-Rule:MF_04128}; DE Includes: DE RecName: Full=mRNA guanylyltransferase {ECO:0000255|HAMAP-Rule:MF_04128}; DE EC=2.7.7.50 {ECO:0000255|HAMAP-Rule:MF_04128}; DE Includes: DE RecName: Full=mRNA (guanine-N(7))-methyltransferase {ECO:0000255|HAMAP-Rule:MF_04128}; DE EC=2.1.1.56 {ECO:0000255|HAMAP-Rule:MF_04128}; OS Rotavirus A (strain RVA/Chicken/Ireland/Ch2/1979/G7P[X]) (RV-A) (Rotavirus OS A (strain Ch-2)). OC Viruses; Riboviria; Orthornavirae; Duplornaviricota; Resentoviricetes; OC Reovirales; Sedoreoviridae; Rotavirus; Rotavirus A. OX NCBI_TaxID=31589; OH NCBI_TaxID=9031; Gallus gallus (Chicken). RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC RNA]. RX PubMed=15039535; DOI=10.1099/vir.0.19629-0; RA Cook J.P., McCrae M.A.; RT "Sequence analysis of the guanylyltransferase (VP3) of group A RT rotaviruses."; RL J. Gen. Virol. 85:929-932(2004). CC -!- FUNCTION: Multifunctional enzyme involved in mRNA capping. Catalyzes CC the formation of the 5' cap structure on the viral plus-strand CC transcripts. Specifically binds to GTP and displays guanylyltransferase CC and methyltransferase activities. Has affinity for ssRNA but not for CC dsRNA. Capping activity is non-specific and caps RNAs that initiate CC with either a G or an A residue. Together with VP1 polymerase, forms a CC VP1-VP3 complex positioned near the channels situated at each of the CC five-fold vertices of the core. Following infection, the outermost CC layer of the virus is lost, leaving a double-layered particle (DLP) CC made up of the core and VP6 shell. VP1 then catalyzes the transcription CC of fully conservative plus-strand genomic RNAs that are capped by VP3 CC and extruded through the DLP's channels into the cytoplasm where they CC function as mRNAs for translation of viral proteins. DLPs probably have CC an RNA triphosphatase activity as well, whereas open cores do not. CC {ECO:0000255|HAMAP-Rule:MF_04128}. CC -!- FUNCTION: Counteracts the host innate immune response thanks to its CC phosphodiesterase that degrades the 5'-triphosphorylated, 2'-5' linked CC adenylate oligomers produced by the host cell IFN-inducible 2',5'- CC oligoadenylate synthetase (OAS). The host RNaseL is therefore not CC activated. {ECO:0000255|HAMAP-Rule:MF_04128}. CC -!- CATALYTIC ACTIVITY: CC Reaction=a 5'-end diphospho-ribonucleoside in mRNA + GTP + H(+) = a 5'- CC end (5'-triphosphoguanosine)-(ribonucleoside) in mRNA + diphosphate; CC Xref=Rhea:RHEA:67012, Rhea:RHEA-COMP:17165, Rhea:RHEA-COMP:17166, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:37565, CC ChEBI:CHEBI:167616, ChEBI:CHEBI:167617; EC=2.7.7.50; CC Evidence={ECO:0000255|HAMAP-Rule:MF_04128}; CC -!- CATALYTIC ACTIVITY: CC Reaction=a 5'-end (5'-triphosphoguanosine)-(ribonucleoside) in mRNA + CC S-adenosyl-L-methionine = a 5'-end (N(7)-methyl 5'- CC triphosphoguanosine)-ribonucleoside in mRNA + S-adenosyl-L- CC homocysteine; Xref=Rhea:RHEA:67008, Rhea:RHEA-COMP:17166, Rhea:RHEA- CC COMP:17167, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:156461, CC ChEBI:CHEBI:167617; EC=2.1.1.56; Evidence={ECO:0000255|HAMAP- CC Rule:MF_04128}; CC -!- CATALYTIC ACTIVITY: CC Reaction=5'-triphosphoadenylyl-(2'->5')-adenylyl-(2'->5')-adenosine + 2 CC H2O = 2 AMP + ATP + 2 H(+); Xref=Rhea:RHEA:45964, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:67143, CC ChEBI:CHEBI:456215; Evidence={ECO:0000255|HAMAP-Rule:MF_04128}; CC -!- SUBUNIT: Interacts with VP1. Interacts with VP2. {ECO:0000255|HAMAP- CC Rule:MF_04128}. CC -!- SUBCELLULAR LOCATION: Virion {ECO:0000255|HAMAP-Rule:MF_04128}. CC Note=Attached inside the inner capsid as a minor component. There are CC about 11 to 12 copies per virion. {ECO:0000255|HAMAP-Rule:MF_04128}. CC -!- DOMAIN: Contains a bipartite N7-methyltransferase domain, a 2'-O- CC methyltransferase domain and a GTase/RTPase domain. The C-terminus CC contains a phosphodiesterase domain that degrades the 5'- CC triphosphorylated, 2'-5' linked adenylate oligomers produced by the CC host cell in response to IFN stimulation. {ECO:0000255|HAMAP- CC Rule:MF_04128}. CC -!- SIMILARITY: Belongs to the rotavirus VP3 family. {ECO:0000255|HAMAP- CC Rule:MF_04128}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AY277923; AAQ21050.1; -; Genomic_RNA. DR SMR; Q6WNV6; -. DR GO; GO:0019013; C:viral nucleocapsid; IEA:UniProtKB-UniRule. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule. DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW. DR GO; GO:0004482; F:mRNA 5'-cap (guanine-N7-)-methyltransferase activity; IEA:UniProtKB-UniRule. DR GO; GO:0004484; F:mRNA guanylyltransferase activity; IEA:UniProtKB-UniRule. DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule. DR GO; GO:0039503; P:suppression by virus of host innate immune response; IEA:UniProtKB-KW. DR HAMAP; MF_04124; Rota_VP3; 1. DR HAMAP; MF_04128; Rota_VP3_A; 1. DR InterPro; IPR011181; VP3_Rotav. DR Pfam; PF06929; Rotavirus_VP3; 1. DR PIRSF; PIRSF004015; LigT_rotavirus; 1. DR PROSITE; PS51589; SAM_MT56_VP3; 1. PE 3: Inferred from homology; KW GTP-binding; Host-virus interaction; Hydrolase; KW Inhibition of host innate immune response by virus; Methyltransferase; KW mRNA capping; mRNA processing; Multifunctional enzyme; Nucleotide-binding; KW Nucleotidyltransferase; RNA-binding; S-adenosyl-L-methionine; Transferase; KW Viral immunoevasion; Virion. FT CHAIN 1..829 FT /note="Protein VP3" FT /id="PRO_0000368072" FT REGION 171..242 FT /note="N7-methyltransferase activity" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04128" FT REGION 243..425 FT /note="2'-O-methyltransferase activity" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04128" FT REGION 426..551 FT /note="N7-methyltransferase activity" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04128" FT REGION 552..688 FT /note="GTase/RTPase activity" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04128" FT REGION 689..829 FT /note="2'-5'-phosphodiesterase activity" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04128" FT ACT_SITE 714 FT /note="For 2'-5'-phosphodiesterase activity" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04128" FT ACT_SITE 716 FT /note="For 2'-5'-phosphodiesterase activity" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04128" FT ACT_SITE 793 FT /note="For 2'-5'-phosphodiesterase activity" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04128" FT ACT_SITE 795 FT /note="For 2'-5'-phosphodiesterase activity" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04128" SQ SEQUENCE 829 AA; 97789 MW; A45EE6B3F66379E1 CRC64; MKVIALRRDL VSSYADTQVY EHDVDKDYYE NAYLISNITA HNVLYVDYSI QVIEILNKSG IASLIAINKD KLEILIKSNY TYDYYKNIVY LHDYSYYNLN ELRTDQYWLT TTNIEEYILP GWKLTYVGQL GIKTRGHYTY SFICQNTATD DDIIYDYIYS NEVDFLPFLL QALNKRLTTA VNFHRLSNRI FREYLYSKVP KDTINIGPRN ESMFTLLRYP YITNYAANEF KVSDLIRLTQ EKWIGAENSQ FDIGQFKNMC NVLSTIYYYY NKYHAYPRIY MLGSAPSYWL YDLLQVYNFD IETWDPLDTP FSKRHHKAMF AISDTEKLSD NSILYIDIRS DRNGADWREW RQRVEDETKI NLEIMRKYLQ RGKTRICCCK ITAMDIELPA TSILLHFPTT KIQSECYVIC TQEMLQDKKR FVPKGAFYSF INNTKTDNVF VSPVYKVKPT NKFVVALYSL SNENNDRDKV IDFTQKQKRG IITLRMNNTF NYEYRLQFKS TYDYLYLPSE VSREGTIVTS YDGYIAMHNL SLSLESKATG NNHLFISFSD ANYGQIDSYC THMGISRRSH SVRFSEAATT LSGYMFRDIT NGKFNLINTN VENAVSGHVY NALVYFRYNY RFDLLRWINL HAKDEVMIQG GRYYEHAPPE LLYACQSALV FAKLQNDLTL IEYVNSVNRY ILNKYNLKYA DDPNYYIHID FVDLPFKYTV PDPHLTGGLL FLNDFDIQNT ITILRSVKED LIALNLLTQY TYMLTDSIYV ANVDGYLQFY YKLYMKFYRK QIVFGQSRMF LPHITLSKEK KKPVRIDATK LVIKSIKLRK IKSDVEYCI //