ID   A0A221IRJ8_9REOV        Unreviewed;       835 AA.
AC   A0A221IRJ8;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2017, sequence version 1.
DT   07-OCT-2020, entry version 10.
DE   RecName: Full=Protein VP3 {ECO:0000256|HAMAP-Rule:MF_04128};
DE   Includes:
DE     RecName: Full=2',5'-phosphodiesterase {ECO:0000256|HAMAP-Rule:MF_04128};
DE              EC=3.1.4.- {ECO:0000256|HAMAP-Rule:MF_04128};
DE   Includes:
DE     RecName: Full=mRNA guanylyltransferase {ECO:0000256|HAMAP-Rule:MF_04128};
DE              EC=2.7.7.50 {ECO:0000256|HAMAP-Rule:MF_04128};
DE   Includes:
DE     RecName: Full=mRNA (guanine-N(7)-)-methyltransferase {ECO:0000256|HAMAP-Rule:MF_04128};
DE              EC=2.1.1.56 {ECO:0000256|HAMAP-Rule:MF_04128};
GN   Name=VP3 {ECO:0000313|EMBL:ASM56484.1};
OS   Rotavirus A.
OC   Viruses; Riboviria; Orthornavirae; Duplornaviricota; Resentoviricetes;
OC   Reovirales; Reoviridae; Sedoreovirinae; Rotavirus.
OX   NCBI_TaxID=28875 {ECO:0000313|EMBL:ASM56484.1, ECO:0000313|Proteomes:UP000225826};
RN   [1] {ECO:0000313|EMBL:ASM56484.1, ECO:0000313|Proteomes:UP000225826}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RVA/Human-wt/UGA/MUL-13-166/2013/G3P[6]
RC   {ECO:0000313|EMBL:ASM56484.1, ECO:0000313|Proteomes:UP000225826};
RX   PubMed=28640820;
RA   Bwogi J., Jere K.C., Karamagi C., Byarugaba D.K., Namuwulya P.,
RA   Baliraine F.N., Desselberger U., Iturriza-Gomara M.;
RT   "Whole genome analysis of selected human and animal rotaviruses identified
RT   in Uganda from 2012 to 2014 reveals complex genome reassortment events
RT   between human, bovine, caprine and porcine strains.";
RL   PLoS ONE 12:E0178855-E0178855(2017).
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:0000256|HAMAP-Rule:MF_04128}.
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:0000256|HAMAP-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:0000256|HAMAP-Rule:MF_04128};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 5'-end (5'-triphosphoguanosine)-adenosine in mRNA + S-
CC         adenosyl-L-methionine = a 5'-end (N(7)-methyl 5'-
CC         triphosphoguanosine)-adenosine in mRNA + S-adenosyl-L-homocysteine;
CC         Xref=Rhea:RHEA:60852, Rhea:RHEA-COMP:15680, Rhea:RHEA-COMP:15682,
CC         ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:143973,
CC         ChEBI:CHEBI:143974; EC=2.1.1.56; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_04128};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 5'-end (5'-triphosphoguanosine)-guanosine in mRNA + S-
CC         adenosyl-L-methionine = a 5'-end (N(7)-methyl 5'-
CC         triphosphoguanosine)-guanosine in mRNA + S-adenosyl-L-homocysteine;
CC         Xref=Rhea:RHEA:60856, Rhea:RHEA-COMP:15681, Rhea:RHEA-COMP:15683,
CC         ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:143971,
CC         ChEBI:CHEBI:143975; EC=2.1.1.56; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_04128};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 5'-end diphospho-(purine-ribonucleoside) in mRNA + GTP +
CC         H(+) = a 5'-end (5'-triphosphoguanosine)-(purine-ribonucleotide) in
CC         mRNA + diphosphate; Xref=Rhea:RHEA:54592, Rhea:RHEA-COMP:13407,
CC         Rhea:RHEA-COMP:13929, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:37565, ChEBI:CHEBI:136896, ChEBI:CHEBI:138276;
CC         EC=2.7.7.50; Evidence={ECO:0000256|HAMAP-Rule:MF_04128};
CC   -!- SUBUNIT: Interacts with VP1. Interacts with VP2. {ECO:0000256|HAMAP-
CC       Rule:MF_04128}.
CC   -!- SUBCELLULAR LOCATION: Virion {ECO:0000256|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:0000256|HAMAP-Rule:MF_04128}.
CC   -!- DOMAIN: Contains a bipartite N7-methytransferase domain, a 2'-O-
CC       methytransferase 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:0000256|HAMAP-
CC       Rule:MF_04128}.
CC   -!- SIMILARITY: Belongs to the rotavirus VP3 family. {ECO:0000256|HAMAP-
CC       Rule:MF_04128, ECO:0000256|PIRNR:PIRNR004015}.
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DR   EMBL; KX632278; ASM56484.1; -; mRNA.
DR   Proteomes; UP000225826; 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   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   2: Evidence at transcript level;
KW   GTP-binding {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|HAMAP-
KW   Rule:MF_04128, ECO:0000256|PIRNR:PIRNR004015};
KW   Host-virus interaction {ECO:0000256|HAMAP-Rule:MF_04128};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_04128};
KW   Inhibition of host innate immune response by virus {ECO:0000256|HAMAP-
KW   Rule:MF_04128};
KW   Methyltransferase {ECO:0000256|HAMAP-Rule:MF_04128,
KW   ECO:0000256|PIRNR:PIRNR004015};
KW   mRNA capping {ECO:0000256|HAMAP-Rule:MF_04128,
KW   ECO:0000256|PIRNR:PIRNR004015};
KW   mRNA processing {ECO:0000256|HAMAP-Rule:MF_04128,
KW   ECO:0000256|PIRNR:PIRNR004015};
KW   Multifunctional enzyme {ECO:0000256|HAMAP-Rule:MF_04128};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_04128,
KW   ECO:0000256|PIRNR:PIRNR004015};
KW   Nucleotidyltransferase {ECO:0000256|HAMAP-Rule:MF_04128,
KW   ECO:0000256|PIRNR:PIRNR004015};
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|HAMAP-
KW   Rule:MF_04128, ECO:0000256|PIRNR:PIRNR004015};
KW   S-adenosyl-L-methionine {ECO:0000256|HAMAP-Rule:MF_04128,
KW   ECO:0000256|PIRNR:PIRNR004015};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_04128,
KW   ECO:0000256|PIRNR:PIRNR004015};
KW   Viral immunoevasion {ECO:0000256|HAMAP-Rule:MF_04128};
KW   Virion {ECO:0000256|HAMAP-Rule:MF_04128, ECO:0000256|PIRNR:PIRNR004015}.
FT   REGION          171..245
FT                   /note="N7-methyltransferase activity"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_04128"
FT   REGION          246..428
FT                   /note="2'-O-methyltransferase activity"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_04128"
FT   REGION          429..555
FT                   /note="N7-methyltransferase activity"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_04128"
FT   REGION          556..692
FT                   /note="GTase/RTPase activity"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_04128"
FT   REGION          693..835
FT                   /note="2'-5'-phosphodiesterase activity"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_04128"
FT   ACT_SITE        718
FT                   /note="For 2'-5'-phosphodiesterase activity"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_04128"
FT   ACT_SITE        720
FT                   /note="For 2'-5'-phosphodiesterase activity"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_04128"
FT   ACT_SITE        797
FT                   /note="For 2'-5'-phosphodiesterase activity"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_04128"
FT   ACT_SITE        799
FT                   /note="For 2'-5'-phosphodiesterase activity"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_04128"
SQ   SEQUENCE   835 AA;  98225 MW;  AA5E18234705DD20 CRC64;
     MKVLALRHSV AQVYADTQMY THDDSKDEYE NAFLISNLTT HNILYFNYNV KTLQILNKSG
     IAAIEIQEID ELFTLIRCNF TYDYIENVVY LHDYSYYTNN EIRTDQHWIT KTNIEDYLLP
     GWKLTYVGYN GSDTRGHYNF SFRCQNAATD DDAIIEYIYS DELDFQSFIL KKIKERMTTS
     LPIARLSNRV FRDKLFETVS VNHDKVVNIG PRNESMFTFL DYPSIKQFSN GPYLVKDTIK
     LKQERWLGKR LSQFDIGQYK NMLNVLTTLY QYYDIYHEKP IVYMIGSAPS YWIYDVKQYS
     NLKFETWDPL DTPYSNLHHK ELFYINDVQK LKDNSILYID IRTDRGTVDW KEWRKIVERQ
     TIDNLHIAYK YLSTGKAKVC CVKMTAMDLE LPISAKLLHH PTTEIRSEFY LVMDIWDSKN
     IKRFIPKGVL YSYINNIITE NVFIQQPFKL KTLKNEYIIA LYALSNDLNN REDVVKLINN
     QKKALMTVRI NNTFKDEPKV GFKNIYDWTF LPTDFETNES IITSYDGCLG IFGLSISLAS
     KPTGNNHLFI LSGTDKYFKL DQFANHMSIS RRSHQIRFSE SATSYSGYIF RDLSNNNFNL
     IGTNVENSVS GHVYNALIYY RYNYSFDLKR WIYLHSTGKA SIEGGKYYEH APIELIYACR
     SAREFAKLQD DLTVLRYSNE IENYINKVYS ITYADDPNYF IGVKFKNIPY KYNVKVPHLT
     FGVLNISEQM LSDVITILKR FKNELFRMEI TTSYTYMLSD EVYVANISGV LSTYFKMYNA
     FYKEQITFGQ SRMFIPHVTL SFSNEKTVRI DTTKLYIDSI YLRKIKGDTV FDMTG
//