ID A0A024CFD6_9REOV Unreviewed; 835 AA. AC A0A024CFD6; DT 09-JUL-2014, integrated into UniProtKB/TrEMBL. DT 09-JUL-2014, sequence version 1. DT 11-DEC-2019, entry version 14. 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:AHZ32439.1}; GN ORFNames=L312_46714gpVP3 {ECO:0000313|EMBL:AHZ32439.1}; OS Rotavirus A. OC Viruses; Riboviria; Reoviridae; Sedoreovirinae; Rotavirus. OX NCBI_TaxID=28875 {ECO:0000313|EMBL:AHZ32439.1, ECO:0000313|Proteomes:UP000118715}; RN [1] {ECO:0000313|EMBL:AHZ32439.1, ECO:0000313|Proteomes:UP000118715} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=RVA/Human-wt/ZAF/MRC-DPRU566/2003/G1P[8] RC {ECO:0000313|EMBL:AHZ32439.1}; RA Wentworth D.E., Halpin R.A., Stucker K.M., Akopov A., Fedorova N., RA Tsitrin T., Puri V., Stockwell T., Amedeo P., Bishop B., Gupta N., RA Hoover J., Katzel D., Schobel S., Shrivastava S., Nyaga M.M., RA Magagula N.B., Peenze I., Seheri M.L., Mphahlele J., Steele A.D., RA Mwenda M.J.; RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases. 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; KJ751682; AHZ32439.1; -; Genomic_RNA. DR Proteomes; UP000118715; 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 3: Inferred from homology; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_04128, KW 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|HAMAP-Rule:MF_04128, KW ECO:0000256|PIRNR:PIRNR004015}; KW Nucleotidyltransferase {ECO:0000256|HAMAP-Rule:MF_04128, KW ECO:0000256|PIRNR:PIRNR004015}; KW RNA-binding {ECO:0000256|HAMAP-Rule:MF_04128, KW 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; 97722 MW; 22DFA71399ABCB64 CRC64; MKVLALRHSV AQVYADTQTY LHDDLKDEYE NAFLISNLTT HNILYLNYSL KTLKILNKSG IAAVEVQSPD ELFALIRCNF TYDYENNIVY LHDYSYYTNN EIRTDQHWIT KTDMIDYLLP GWKLTYVGYN GKNTRGHYNF SFICQNAATD DDIIIEYIYS NELDFQNFLL RKIKERMTTS LPIARLSNRV FRDKLFPSIV NIHKKVINVG PRNESMFTFL NFPTIKQFSN GAYIVKHTIK LKQEKWLGKR VSQFDIGQYK NMLNVVTTIY YYYNLYYSKP IIYMLGSAPS YWIYDIKQYS DFTFETWDPL DTPYSTTHHK ELFFDKDVNK LKDNSVLYID IRTDRGSMDW KEWRKIVEQQ TVSNLNIAYK YLSTGKAKVC CVKLTAMDLE LPITAKLLHH PTTEVRSEFY AILDVWDIIT IKRFIPKGVF YAFINNVTTE NVFIQPPFKL KTSPTDYIVA LYALSNDFNS RQDVINLVNK QKQSLITVRI NNTFKDEPKV NFKNIYDWTF LPTDFELKDS IITSYDGCLG VFGLSISLPS KPTGNNHLFI INGTDKYNKL DQYANHMGIS RRSHQIRFSE SATSYSGYIF RDLSNNNFNL IGTNVENSVS GHVYNALIYY RYNYAFDLKR WIYLHSIGKV AIEGGRYYEH APIELIYACR SAKEFAILQD DLTVLRYANE IEGYINKVYS ITYADDPNYF IGIKFNSIPY EYDVKIPHLT LGVLFISENM INDVITVLKK MKTELFKMEI STSYTYMLSD NTYVANASGV LSTYFKLYNM FYRNHITFGQ SRMFIPHITL SFSNKQTVRI ESTKLKISSI YLRKIKGETV FDMSE //