VP3_ROTS1
ID VP3_ROTS1 Reviewed; 835 AA.
AC P15736;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1991, sequence version 2.
DT 23-FEB-2022, entry version 90.
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/SA11-Both/G3P5B[2]) (RV-A) (Simian Agent 11 (strain
OS Both)).
OC Viruses; Riboviria; Orthornavirae; Duplornaviricota; Resentoviricetes;
OC Reovirales; Reoviridae; Sedoreovirinae; Rotavirus; Rotavirus A.
OX NCBI_TaxID=37137;
OH NCBI_TaxID=9544; Macaca mulatta (Rhesus macaque).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=2162107; DOI=10.1016/0042-6822(90)90487-c;
RA Mitchell D.B., Both G.W.;
RT "Completion of the genomic sequence of the simian rotavirus SA11:
RT nucleotide sequences of segments 1, 2, and 3.";
RL Virology 177:324-331(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=2552420; DOI=10.1093/nar/17.19.7991;
RA Liu M., Estes M.K.;
RT "Nucleotide sequence of the simian rotavirus SA11 genome segment 3.";
RL Nucleic Acids Res. 17:7991-7991(1989).
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; X16387; CAA34423.1; -; Genomic_RNA.
DR EMBL; X16062; CAA34198.1; -; Genomic_RNA.
DR PIR; S06085; P3XRSR.
DR SMR; P15736; -.
DR Proteomes; UP000007180; 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; IPR039573; NS2A-like.
DR InterPro; IPR011181; VP3_Rotav.
DR Pfam; PF05213; Corona_NS2A; 1.
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; Reference proteome; RNA-binding;
KW S-adenosyl-L-methionine; Transferase; Viral immunoevasion; Virion.
FT CHAIN 1..835
FT /note="Protein VP3"
FT /id="PRO_0000149537"
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 25
FT /note="I -> T (in Ref. 2; CAA34198)"
FT /evidence="ECO:0000305"
FT CONFLICT 136
FT /note="G -> A (in Ref. 2; CAA34198)"
FT /evidence="ECO:0000305"
FT CONFLICT 388
FT /note="H -> D (in Ref. 2; CAA34198)"
FT /evidence="ECO:0000305"
FT CONFLICT 613
FT /note="I -> V (in Ref. 2; CAA34198)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 835 AA; 98141 MW; D67C329D6A29B680 CRC64;
MKVLALRHSV AQVYADTQVY VHDDIKDSYE NAFLISNLTT HNILYLNYSI KTLEILNKSG
IAAIALQSLE ELFTLIRCNF TYDYELDIIY LHDYSYYTNN EIRTDQHWIT KTNIEEYLLP
GWKLTYVGYN GSETRGHYNF SFKCQNAATD DDLIIEYIYS EALDFQNFML KKIKERMTTS
LPIARLSNRV FRDKLFPSLL KEHKNVVNVG PRNESMFTFL NYPTIKQFSN GAYLVKDTIK
LKQERWLGKR ISQFDIGQYK NMLNVLTAIY YYYNLYKSKP IIYMIGSAPS YWIYDVRHYS
DFFFETWDPL DTPYSSIHHK ELFFINDVKK LKDNSILYID IRTDRGNADW KKWRKTVEEQ
TINNLDIAYE YLRTGKAKVC CVKMTAMHLE LPISAKLLHH PTTEIRSEFY LLLDTWDLTN
IRRFIPKGVL YSFINNIITE NVFIQQPFKV KVLNDSYIVA LYALSNDFNN RSEVIKLINN
QKQSLITVRI NNTFKDEPKV GFKNIYDWTF LPTDFDTKEA IITSYDGCLG LFGLSISLAS
KPTGNNHLFI LSGTDKYYKL DQFANHTSIS RRSHQIRFSE SATSYSGYIF RDLSNNNFNL
IGTNIENSVS GHIYNALIYY RYNYSFDLKR WIYLHSIDKV DIEGGKYYEH APIELIYACR
SAKEFATLQD DLTVLRYSNE IENYINTVYS ITYADDPNYF IGIQFRNIPY KYDVKIPHLT
FGVLHISDNM VPDVIDILKI MKNELFKMDI TTSYTYMLSD GIYVANVSGV LSTYFKIYNV
FYKNQITFGQ SRMFIPHITL SFNNMRTVRI ETTKLQIKSI YLRKIKGDTV FDMVE
