ID A0A221IRJ8_9REOV Unreviewed; 835 AA. AC A0A221IRJ8; DT 25-OCT-2017, integrated into UniProtKB/TrEMBL. DT 25-OCT-2017, sequence version 1. DT 12-AUG-2020, entry version 9. DE RecName: Full=Protein VP3 {ECO:0000256|HAMAP-Rule:MF_04128}; DE Includes: DE RecName: Full=2',5'-phosphodiesterase {ECO:0000256|HAMAP-Rule:MF_04128}; DE EC=3.1.4.- {ECO:0000256|HAMAP-Rule:MF_04128}; DE Includes: DE RecName: Full=mRNA guanylyltransferase {ECO:0000256|HAMAP-Rule:MF_04128}; DE EC=2.7.7.50 {ECO:0000256|HAMAP-Rule:MF_04128}; DE Includes: DE RecName: Full=mRNA (guanine-N(7)-)-methyltransferase {ECO:0000256|HAMAP-Rule:MF_04128}; DE EC=2.1.1.56 {ECO:0000256|HAMAP-Rule:MF_04128}; GN Name=VP3 {ECO:0000313|EMBL:ASM56484.1}; OS Rotavirus A. OC Viruses; Riboviria; Orthornavirae; Duplornaviricota; Resentoviricetes; OC Reovirales; Reoviridae; Sedoreovirinae; Rotavirus. OX NCBI_TaxID=28875 {ECO:0000313|EMBL:ASM56484.1, ECO:0000313|Proteomes:UP000225826}; RN [1] {ECO:0000313|EMBL:ASM56484.1, ECO:0000313|Proteomes:UP000225826} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=RVA/Human-wt/UGA/MUL-13-166/2013/G3P[6] RC {ECO:0000313|EMBL:ASM56484.1, ECO:0000313|Proteomes:UP000225826}; RX PubMed=28640820; RA Bwogi J., Jere K.C., Karamagi C., Byarugaba D.K., Namuwulya P., RA Baliraine F.N., Desselberger U., Iturriza-Gomara M.; RT "Whole genome analysis of selected human and animal rotaviruses identified RT in Uganda from 2012 to 2014 reveals complex genome reassortment events RT between human, bovine, caprine and porcine strains."; RL PLoS ONE 12:E0178855-E0178855(2017). 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:0000256|HAMAP-Rule:MF_04128}. 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:0000256|HAMAP-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:0000256|HAMAP-Rule:MF_04128}; CC -!- CATALYTIC ACTIVITY: CC Reaction=a 5'-end (5'-triphosphoguanosine)-adenosine in mRNA + S- CC adenosyl-L-methionine = a 5'-end (N(7)-methyl 5'- CC triphosphoguanosine)-adenosine in mRNA + S-adenosyl-L-homocysteine; CC Xref=Rhea:RHEA:60852, Rhea:RHEA-COMP:15680, Rhea:RHEA-COMP:15682, CC ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:143973, CC ChEBI:CHEBI:143974; EC=2.1.1.56; Evidence={ECO:0000256|HAMAP- CC Rule:MF_04128}; CC -!- CATALYTIC ACTIVITY: CC Reaction=a 5'-end (5'-triphosphoguanosine)-guanosine in mRNA + S- CC adenosyl-L-methionine = a 5'-end (N(7)-methyl 5'- CC triphosphoguanosine)-guanosine in mRNA + S-adenosyl-L-homocysteine; CC Xref=Rhea:RHEA:60856, Rhea:RHEA-COMP:15681, Rhea:RHEA-COMP:15683, CC ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:143971, CC ChEBI:CHEBI:143975; EC=2.1.1.56; Evidence={ECO:0000256|HAMAP- CC Rule:MF_04128}; CC -!- CATALYTIC ACTIVITY: CC Reaction=a 5'-end diphospho-(purine-ribonucleoside) in mRNA + GTP + CC H(+) = a 5'-end (5'-triphosphoguanosine)-(purine-ribonucleotide) in CC mRNA + diphosphate; Xref=Rhea:RHEA:54592, Rhea:RHEA-COMP:13407, CC Rhea:RHEA-COMP:13929, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, CC ChEBI:CHEBI:37565, ChEBI:CHEBI:136896, ChEBI:CHEBI:138276; CC EC=2.7.7.50; Evidence={ECO:0000256|HAMAP-Rule:MF_04128}; CC -!- SUBUNIT: Interacts with VP1. Interacts with VP2. {ECO:0000256|HAMAP- CC Rule:MF_04128}. CC -!- SUBCELLULAR LOCATION: Virion {ECO:0000256|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:0000256|HAMAP-Rule:MF_04128}. CC -!- DOMAIN: Contains a bipartite N7-methytransferase domain, a 2'-O- CC methytransferase 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:0000256|HAMAP- CC Rule:MF_04128}. CC -!- SIMILARITY: Belongs to the rotavirus VP3 family. {ECO:0000256|HAMAP- CC Rule:MF_04128, ECO:0000256|PIRNR:PIRNR004015}. 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; KX632278; ASM56484.1; -; mRNA. DR Proteomes; UP000225826; Genome. 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 (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 2: Evidence at transcript level; KW GTP-binding {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|HAMAP- KW Rule:MF_04128, ECO:0000256|PIRNR:PIRNR004015}; KW Host-virus interaction {ECO:0000256|HAMAP-Rule:MF_04128}; KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_04128}; KW Inhibition of host innate immune response by virus {ECO:0000256|HAMAP- KW Rule:MF_04128}; KW Methyltransferase {ECO:0000256|HAMAP-Rule:MF_04128, KW ECO:0000256|PIRNR:PIRNR004015}; KW mRNA capping {ECO:0000256|HAMAP-Rule:MF_04128, KW ECO:0000256|PIRNR:PIRNR004015}; KW mRNA processing {ECO:0000256|HAMAP-Rule:MF_04128, KW ECO:0000256|PIRNR:PIRNR004015}; KW Multifunctional enzyme {ECO:0000256|HAMAP-Rule:MF_04128}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP- KW Rule:MF_04128, ECO:0000256|PIRNR:PIRNR004015}; KW Nucleotidyltransferase {ECO:0000256|HAMAP-Rule:MF_04128, KW ECO:0000256|PIRNR:PIRNR004015}; KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|HAMAP- KW Rule:MF_04128, ECO:0000256|PIRNR:PIRNR004015}; KW S-adenosyl-L-methionine {ECO:0000256|HAMAP-Rule:MF_04128, KW ECO:0000256|PIRNR:PIRNR004015}; KW Transferase {ECO:0000256|HAMAP-Rule:MF_04128, KW ECO:0000256|PIRNR:PIRNR004015}; KW Viral immunoevasion {ECO:0000256|HAMAP-Rule:MF_04128}; KW Virion {ECO:0000256|HAMAP-Rule:MF_04128, ECO:0000256|PIRNR:PIRNR004015}. FT REGION 171..245 FT /note="N7-methyltransferase activity" FT /evidence="ECO:0000256|HAMAP-Rule:MF_04128" FT REGION 246..428 FT /note="2'-O-methyltransferase activity" FT /evidence="ECO:0000256|HAMAP-Rule:MF_04128" FT REGION 429..555 FT /note="N7-methyltransferase activity" FT /evidence="ECO:0000256|HAMAP-Rule:MF_04128" FT REGION 556..692 FT /note="GTase/RTPase activity" FT /evidence="ECO:0000256|HAMAP-Rule:MF_04128" FT REGION 693..835 FT /note="2'-5'-phosphodiesterase activity" FT /evidence="ECO:0000256|HAMAP-Rule:MF_04128" FT ACT_SITE 718 FT /note="For 2'-5'-phosphodiesterase activity" FT /evidence="ECO:0000256|HAMAP-Rule:MF_04128" FT ACT_SITE 720 FT /note="For 2'-5'-phosphodiesterase activity" FT /evidence="ECO:0000256|HAMAP-Rule:MF_04128" FT ACT_SITE 797 FT /note="For 2'-5'-phosphodiesterase activity" FT /evidence="ECO:0000256|HAMAP-Rule:MF_04128" FT ACT_SITE 799 FT /note="For 2'-5'-phosphodiesterase activity" FT /evidence="ECO:0000256|HAMAP-Rule:MF_04128" SQ SEQUENCE 835 AA; 98225 MW; AA5E18234705DD20 CRC64; MKVLALRHSV AQVYADTQMY THDDSKDEYE NAFLISNLTT HNILYFNYNV KTLQILNKSG IAAIEIQEID ELFTLIRCNF TYDYIENVVY LHDYSYYTNN EIRTDQHWIT KTNIEDYLLP GWKLTYVGYN GSDTRGHYNF SFRCQNAATD DDAIIEYIYS DELDFQSFIL KKIKERMTTS LPIARLSNRV FRDKLFETVS VNHDKVVNIG PRNESMFTFL DYPSIKQFSN GPYLVKDTIK LKQERWLGKR LSQFDIGQYK NMLNVLTTLY QYYDIYHEKP IVYMIGSAPS YWIYDVKQYS NLKFETWDPL DTPYSNLHHK ELFYINDVQK LKDNSILYID IRTDRGTVDW KEWRKIVERQ TIDNLHIAYK YLSTGKAKVC CVKMTAMDLE LPISAKLLHH PTTEIRSEFY LVMDIWDSKN IKRFIPKGVL YSYINNIITE NVFIQQPFKL KTLKNEYIIA LYALSNDLNN REDVVKLINN QKKALMTVRI NNTFKDEPKV GFKNIYDWTF LPTDFETNES IITSYDGCLG IFGLSISLAS KPTGNNHLFI LSGTDKYFKL DQFANHMSIS RRSHQIRFSE SATSYSGYIF RDLSNNNFNL IGTNVENSVS GHVYNALIYY RYNYSFDLKR WIYLHSTGKA SIEGGKYYEH APIELIYACR SAREFAKLQD DLTVLRYSNE IENYINKVYS ITYADDPNYF IGVKFKNIPY KYNVKVPHLT FGVLNISEQM LSDVITILKR FKNELFRMEI TTSYTYMLSD EVYVANISGV LSTYFKMYNA FYKEQITFGQ SRMFIPHVTL SFSNEKTVRI DTTKLYIDSI YLRKIKGDTV FDMTG //