VP3_ROTBU
ID VP3_ROTBU Reviewed; 835 AA.
AC Q6WAT6;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 23-FEB-2022, entry version 46.
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/Cow/United Kingdom/UK/1975/G6P7[5]) (RV-A).
OC Viruses; Riboviria; Orthornavirae; Duplornaviricota; Resentoviricetes;
OC Reovirales; Reoviridae; Sedoreovirinae; Rotavirus; Rotavirus A.
OX NCBI_TaxID=10934;
OH NCBI_TaxID=9913; Bos taurus (Bovine).
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 INTERACTION WITH RNA-DIRECTED RNA POLYMERASE VP1, FUNCTION, AND SUBCELLULAR
RP LOCATION.
RX PubMed=20122940; DOI=10.1016/j.jmb.2010.01.055;
RA McClain B., Settembre E., Temple B.R., Bellamy A.R., Harrison S.C.;
RT "X-ray crystal structure of the rotavirus inner capsid particle at 3.8 A
RT resolution.";
RL J. Mol. Biol. 397:587-599(2010).
CC -!- FUNCTION: Multifunctional enzyme involved in mRNA capping. Catalyzes
CC the formation of the 5' cap structure on the viral plus-strand
CC transcripts (By similarity). Specifically binds to GTP and displays
CC guanylyltransferase and methyltransferase activities (By similarity).
CC Has affinity for ssRNA but not for dsRNA (By similarity). Capping
CC activity is non-specific and caps RNAs that initiate with either a G or
CC an A residue (By similarity). 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 (PubMed:20122940). Following infection,
CC the outermost layer of the virus is lost, leaving a double-layered
CC particle (DLP) made up of the core and VP6 shell (By similarity). VP1
CC then catalyzes the transcription of fully conservative plus-strand
CC genomic RNAs that are capped by VP3 and extruded through the DLP's
CC channels into the cytoplasm where they function as mRNAs for
CC translation of viral proteins (By similarity). DLPs probably have an
CC RNA triphosphatase activity as well, whereas open cores do not (By
CC similarity). {ECO:0000255|HAMAP-Rule:MF_04128,
CC ECO:0000269|PubMed:20122940}.
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 (PubMed:20122940). Interacts with VP2 (By
CC similarity). {ECO:0000255|HAMAP-Rule:MF_04128,
CC ECO:0000269|PubMed:20122940}.
CC -!- SUBCELLULAR LOCATION: Virion {ECO:0000255|HAMAP-Rule:MF_04128,
CC ECO:0000269|PubMed:20122940}. Note=Attached inside the inner capsid as
CC a minor component. There are about 11 to 12 copies per virion.
CC {ECO:0000255|HAMAP-Rule:MF_04128, ECO:0000305}.
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, ECO:0000305}.
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DR EMBL; AY300923; AAQ74387.1; -; Genomic_RNA.
DR SMR; Q6WAT6; -.
DR Proteomes; UP000008657; 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 1: Evidence at protein level;
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_0000368074"
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; 98045 MW; C47E642ABA171312 CRC64;
MKVLALRHSV AQVYADTQIY IHDETKDDYE NAFFISNLTT HNILYLNYSV KTLQILNKSG
IAAVEIQKMD KLFTLIRCNF TYDYIDDVVY LHDYSYYTNN EIRTDQHWVT KTNIEDYLLP
GWKLTYVGYN GNDTRGHYNF SFKCQNAATD DDAIIEYIYS NELDFQNFIL KKIKERMTTS
LPIARLSNRV FRDKLFKTLV SDHSKIVNVG PRNESMFTFL DHPSIKQFSN GPYLVKDTIK
LKQERWLGKR LSQFDIGQYK NYVKCINNLI SIYDMYHEKP IIYMLGSAPS YWIHDVKQYS
NLKFETWDPL DTPYSDLHHK ELFYISDVTK LKDNSILYID IRTDRENADW KTWRKIVEEQ
TVNNLNIAYK YLSTGKAKVC CVKMTAMDLE LPISAKLLHH PTTEIRSEFY LIMDIWDSKN
IKRFIPKGVL YSYINNIITE NVFIQQPFKL KTLRNEYVVA LYALSNDFNN REDVIKLINN
QKNALITVRI NNTFKDEPKV GFKDIYDWTF LPTDFETNES IITSYDGCLG VFGLSISLAS
KPTGNNHLFM LSGTNKYFNM DQFANHMSIS RRSHQIRFSE SATSYSGYIF RDLSNNNFNL
IGTNVENSVS GHVYNALIYY RYNYSFDLKR WIYLHSTNKA SIEGGRYYEH APIELIYACR
SAREFAKLQD DLTVLRYSNE IENYINKVYS ITYADDPNYF IGIKFKNIPY EYDVKVPHLT
FGVLNISDSM VPDVVVILKK FKSELFRMDV TTSYTYMLSD EIYVANVSGV LSTYFKLYNA
FYKEQITFGQ SRMFIPHITL SFSNKKVVRI DSTRLNIDFI YLRKIKGDTV FDMAE
