ID VP3_ROTP5 Reviewed; 835 AA. AC Q6WNV8; DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot. DT 05-JUL-2004, sequence version 1. DT 24-JAN-2024, entry version 45. 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/Pig/United States/OSU/1977/G5P9[7]) (RV-A) OS (Rotavirus A (strain Ohio State University)). OC Viruses; Riboviria; Orthornavirae; Duplornaviricota; Resentoviricetes; OC Reovirales; Sedoreoviridae; Rotavirus; Rotavirus A. OX NCBI_TaxID=10915; OH NCBI_TaxID=9823; Sus scrofa (Pig). 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; AY277921; AAQ21048.1; -; Genomic_RNA. DR SMR; Q6WNV8; -. 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 CDD; cd20757; capping_2-OMTase_Rotavirus; 1. 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..835 FT /note="Protein VP3" FT /id="PRO_0000368088" FT REGION 171..245 FT /note="N7-methyltransferase activity" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04128" FT REGION 246..428 FT /note="2'-O-methyltransferase activity" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04128" FT REGION 429..555 FT /note="N7-methyltransferase activity" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04128" FT REGION 556..692 FT /note="GTase/RTPase activity" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04128" FT REGION 693..835 FT /note="2'-5'-phosphodiesterase activity" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04128" FT ACT_SITE 718 FT /note="For 2'-5'-phosphodiesterase activity" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04128" FT ACT_SITE 720 FT /note="For 2'-5'-phosphodiesterase activity" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04128" FT ACT_SITE 797 FT /note="For 2'-5'-phosphodiesterase activity" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04128" FT ACT_SITE 799 FT /note="For 2'-5'-phosphodiesterase activity" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04128" SQ SEQUENCE 835 AA; 97663 MW; 89207782ACE2733A CRC64; MKVLALRHSV AQVYADTQTY VHDDSKDEYE NAFLISNLTT HNILYINYSV KTLKILNKSG IAAVEIQSPD ELFALIRCNF TYDYENNTVY LHDYSYYTNN EIRTDQHWVT KTDIIDYLLP GWKLTYVGYN GKDTRGHYNF SFTCQNAATD DDIIIEYIYS SELDFQTFLL RKIKERMTTS LPIARLSNRV FRDKLFPSIV NIHKRVVNVG PRNESMFTFL NFPTIKQFSN GAYLVKHTIK LKQERWLGKR VSQFDIGQYK NMLNVVTTIY YYYNLHSSKP VIYMLGSAPS YWIYDIRQYS DFTFETWDPL DTPYSTTHHK ELFFDKDVTK LKDNSILYID IRTDRGNMDW KEWRKVVEQQ TVSNLSIAYK YLSTGKAKVC CVKLTAMDLE LPITAKLLHH PTTEIRSEFY AILDVWDIST IKRFVPKGVF YAFINNVTTE NVFIQPPFKL RTLPNDYIVA LYALSNDFNP RQDIINLINK QKQSLITVRI NNTFKDEPKV NFKNIYDWTF LPTDFEIKDS IITSYDGCLG IFGLSTSLSS KPTGNNHLFI INGTDKYYKL DQYANHMGIS RRSHQVRFSE SATSYSGYIF RDLSNNNFNL IGTNIENSVS GHVYNALIYY RYNYAFDLKR WIYLHSIGEV TVEGGKYYEH APIELIYACR SAKEFAALQD DLTVLRYANE IEGYINKVYS ITYADDPNYF IGVRFDSIPY EYDVKVPHLT FGVLFISDNM IHDVITVLKK MKTELFKMEV STSYTYMLSD GIHVANASGV LSTYFKLYNM FYRNHITFGQ SRMFIPHITL SFSNKRTVRI ENTRLKINSI YLRKIKGETV FDMSE //