VP3_ROTHT
ID VP3_ROTHT Reviewed; 835 AA.
AC B1NKT9; Q6WNW0;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2008, sequence version 1.
DT 23-FEB-2022, entry version 37.
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/Human/United Kingdom/ST3/1975/G4P2A[6]) (RV-A)
OS (Rotavirus A (strain St. Thomas 3)).
OC Viruses; Riboviria; Orthornavirae; Duplornaviricota; Resentoviricetes;
OC Reovirales; Reoviridae; Sedoreovirinae; Rotavirus; Rotavirus A.
OX NCBI_TaxID=10960;
OH NCBI_TaxID=9606; Homo sapiens (Human).
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).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=18216098; DOI=10.1128/jvi.02257-07;
RA Matthijnssens J., Ciarlet M., Heiman E.M., Arijs I., Delbeke T.,
RA McDonald S.M., Palombo E.A., Iturriza-Gomara M., Maes P., Patton J.T.,
RA Rahman M., Van Ranst M.;
RT "Full genome-based classification of rotaviruses reveals a common origin
RT between human Wa-Like and porcine rotavirus strains and human DS-1-like and
RT bovine rotavirus strains.";
RL J. Virol. 82:3204-3219(2008).
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}.
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DR EMBL; AY277919; AAQ21046.1; -; Genomic_RNA.
DR EMBL; EF583047; ABU87856.1; -; Genomic_RNA.
DR SMR; B1NKT9; -.
DR PRIDE; B1NKT9; -.
DR Proteomes; UP000007048; 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 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_0000368083"
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"
FT CONFLICT 347
FT /note="N -> D (in Ref. 1; AAQ21046)"
FT /evidence="ECO:0000305"
FT CONFLICT 695
FT /note="D -> A (in Ref. 1; AAQ21046)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 835 AA; 97944 MW; 2B56CDF0C85D5A58 CRC64;
MKVLALRHSV AQVYADTQIY LHDDSKDEYE NAFLISNLTT HNILYLNYSL KTLKILNKSG
IAAVEVQSPD ELFALIRCNF TYDYENNIIY LHDYSYYTNN EIRTDQHWIT KTDIIDYLLP
GWKLTYVGYN GKNTRGHYNF SFSCQNAATD DDIIIEYIYS NELDFQNFLL RKIKERMTTS
LPIARLSNRV FRDKLFPSIV NIYKKVINVG PRNESMFTFL NFPTIKQFSN GAYIVKHTIK
LKQEKWLGKR VSQFDIGQYK NMLNVVTTIY YYYNLYHSKP IIYMLGSAPS HWIHDIKQYS
DFTFETWDPL DTPYSTIHHK ELFFYKDVNK LKDNSILYID IRTDRKNMDW KEWRKVVEQQ
TVNNLNIAYK YLSTGKAKVC CVKLTAMDLE LPITAKLLHH PTTEVRSEFY AILDVWDIIT
IKRFIPKGVF YAFINNITTE NVFIQPPFKL KASPTDYIVA LYALSNDFNS RQDVINLINK
QKQSLITVRM NNTFKDEPKV NFKNIYDWTF LPTDFELKDS IITSYDGCLG MFGLSISLSS
KPTGNNHLFI INGNDKYYKL DQYANHMGIS RRSHQIRFSE SATSYSGYIF RDLSNNNFNL
IGTNVENSVS GHVYNALIYY RYNYAFDLKR WIYLHSIGKV AIEGGRYYEH APIELIYACR
SAREFAILQD DLTVLRYADE IEGYINKVYS ITYADDPNYF IGIKFNSIPY EYDVKVPHLT
LGVLFISDNM IHNVVTVLKK MKTELFKTEI STSYTYMLSD NIYVANASGV LSTYFKLYNM
FYRNHITFGQ SRMFIPHITL SFSTKQTVRI ESTRLKINSI YLRKIKGETV FDMSE
