VP3_ROTHL
ID VP3_ROTHL Reviewed; 835 AA.
AC B1NKS7;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2008, sequence version 1.
DT 23-FEB-2022, entry version 39.
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/Philippines/L26/1987/G12P1B[4]) (RV-A).
OC Viruses; Riboviria; Orthornavirae; Duplornaviricota; Resentoviricetes;
OC Reovirales; Reoviridae; Sedoreovirinae; Rotavirus; Rotavirus A.
OX NCBI_TaxID=10953;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
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; EF583035; ABU87844.1; -; Genomic_RNA.
DR SMR; B1NKS7; -.
DR Proteomes; UP000001459; 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_0000368082"
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; 98004 MW; FB5B1097BAC863CF CRC64;
MKVLALRHSV AQVYADTQVY THDNSKDEYE NAFLISNLTT HNILYLNYSV KTLQILNKSG
IAAIEIQKMD ELFTLIRCNF TYDYIDDVVY LHDYSYYTNN EIRTDQHWVT KTNIEDYLLP
GWKLTYVGYN GSDTRGHYNF SFRCQNAATD DDAIIEYIYS DELDFQSFIL KKIKERMTTS
LPIARLSNRV FRDKLFKTLS VNHDKVVNVG PRNESMFTFL DYPSIKQFSN GPYLVKDTIK
LKQERWLGKR LSQFDIGQYK NMLNVLTTLY QYYDMYHEKP IVYMIGSAPS YWIYDVKQYS
DLKFETWDPL DTPYSNLHHK ELFYINDVQK LKDNSILYID IRTDRGNMDW KEWRKVVERQ
TADNLYIAYK YLSTGRAKIC CVKMTAMDLE LPISAKLLHH PTTEIRSEFY LMMDIWDSKN
IKRFIPKGVL YSYINNIITE NVFIQQPFKL KTLKNEYVIA LYALSNDLNN REDVIKLINN
QKKALITVRI NNTFKDEPKV GFKNIYDWTF LPTDFETSES IITSYDGCLG IFGLSISLAS
KPTGNNHLFI LSGTDKYFKL DQFANHMSIS RRSHQIRFSE SATSYSGYIF RDLSNNNFNL
IGTNVENSVS GHVYNALIYY RYNYSFDLKR WIYLHSTGKA SIEGGRYYEH APIELIYACR
SAREFAKLQD DLTVLRYSNE IENYINKVYS ITYADDPNYF IGVKFKNIPY KYNVKVPHLT
FGVLNISEQM LPDAIAILKK FKNELFGMDI TTSYTYMLSD EVYVANISGV LSTYFKIYNA
FYKEQITFGQ SRMFIPHVTL SFSNEKTVRI DTTKLYIDSI YLRKIKGDTV FDMTG
