VP3_ROTP5
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 23-FEB-2022, 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/Pig/United States/OSU/1977/G5P9[7]) (RV-A)
OS (Rotavirus A (strain Ohio State University)).
OC Viruses; Riboviria; Orthornavirae; Duplornaviricota; Resentoviricetes;
OC Reovirales; Reoviridae; Sedoreovirinae; 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 PRIDE; 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 (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
