ID   A0A221IRJ8_9REOV        Unreviewed;       835 AA.
AC   A0A221IRJ8;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2017, sequence version 1.
DT   16-OCT-2019, entry version 7.
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; 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
RT   identified in Uganda from 2012 to 2014 reveals complex genome
RT   reassortment events between human, bovine, caprine and porcine
RT   strains.";
RL   PLoS ONE 12:E0178855-E0178855(2017).
CC   -!- FUNCTION: Counteracts the host innate immune response thanks to
CC       its phosphodiesterase that degrades the 5'-triphosphorylated, 2'-
CC       5' linked adenylate oligomers produced by the host cell IFN-
CC       inducible 2',5'-oligoadenylate synthetase (OAS). The host RNaseL
CC       is therefore not activated. {ECO:0000256|HAMAP-Rule:MF_04128}.
CC   -!- FUNCTION: Multifunctional enzyme involved in mRNA capping.
CC       Catalyzes the formation of the 5' cap structure on the viral plus-
CC       strand transcripts. Specifically binds to GTP and displays
CC       guanylyltransferase and methyltransferase activities. Has affinity
CC       for ssRNA but not for dsRNA. Capping activity is non-specific and
CC       caps RNAs that initiate with either a G or an A residue. Together
CC       with VP1 polymerase, forms a VP1-VP3 complex positioned near the
CC       channels situated at each of the five-fold vertices of the core.
CC       Following infection, the outermost layer of the virus is lost,
CC       leaving a double-layered particle (DLP) made up of the core and
CC       VP6 shell. VP1 then catalyzes the transcription of fully
CC       conservative plus-strand genomic RNAs that are capped by VP3 and
CC       extruded through the DLP's channels into the cytoplasm where they
CC       function as mRNAs for translation of viral proteins. DLPs probably
CC       have an RNA triphosphatase activity as well, whereas open cores do
CC       not. {ECO:0000256|HAMAP-Rule:MF_04128}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=5'-triphosphoadenylyl-(2'->5')-adenylyl-(2'->5')-
CC         adenosine + 2 H2O = 2 AMP + ATP + 2 H(+); Xref=Rhea:RHEA:45964,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:67143, ChEBI:CHEBI:456215;
CC         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-
CC         homocysteine; Xref=Rhea:RHEA:60852, Rhea:RHEA-COMP:15680,
CC         Rhea:RHEA-COMP:15682, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC         ChEBI:CHEBI:143973, ChEBI:CHEBI:143974; EC=2.1.1.56;
CC         Evidence={ECO:0000256|HAMAP-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-
CC         homocysteine; Xref=Rhea:RHEA:60856, Rhea:RHEA-COMP:15681,
CC         Rhea:RHEA-COMP:15683, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC         ChEBI:CHEBI:143971, ChEBI:CHEBI:143975; EC=2.1.1.56;
CC         Evidence={ECO:0000256|HAMAP-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-
CC         ribonucleotide) in mRNA + diphosphate; Xref=Rhea:RHEA:54592,
CC         Rhea:RHEA-COMP:13407, Rhea:RHEA-COMP:13929, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:37565, ChEBI:CHEBI:136896,
CC         ChEBI:CHEBI:138276; EC=2.7.7.50; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_04128};
CC   -!- SUBUNIT: Interacts with VP1. Interacts with VP2.
CC       {ECO:0000256|HAMAP-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
CC       are about 11 to 12 copies per virion. {ECO:0000256|HAMAP-
CC       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
CC       the host cell in response to IFN stimulation. {ECO:0000256|HAMAP-
CC       Rule:MF_04128}.
CC   -!- SIMILARITY: Belongs to the rotavirus VP3 family.
CC       {ECO:0000256|HAMAP-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   Complete proteome {ECO:0000313|Proteomes:UP000225826};
KW   GTP-binding {ECO:0000256|HAMAP-Rule:MF_04128,
KW   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|HAMAP-Rule:MF_04128,
KW   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,
KW   ECO:0000256|PIRNR:PIRNR004015}.
FT   REGION      171    245       N7-methyltransferase activity.
FT                                {ECO:0000256|HAMAP-Rule:MF_04128}.
FT   REGION      246    428       2'-O-methyltransferase activity.
FT                                {ECO:0000256|HAMAP-Rule:MF_04128}.
FT   REGION      429    555       N7-methyltransferase activity.
FT                                {ECO:0000256|HAMAP-Rule:MF_04128}.
FT   REGION      556    692       GTase/RTPase activity.
FT                                {ECO:0000256|HAMAP-Rule:MF_04128}.
FT   REGION      693    835       2'-5'-phosphodiesterase activity.
FT                                {ECO:0000256|HAMAP-Rule:MF_04128}.
FT   ACT_SITE    718    718       For 2'-5'-phosphodiesterase activity.
FT                                {ECO:0000256|HAMAP-Rule:MF_04128}.
FT   ACT_SITE    720    720       For 2'-5'-phosphodiesterase activity.
FT                                {ECO:0000256|HAMAP-Rule:MF_04128}.
FT   ACT_SITE    797    797       For 2'-5'-phosphodiesterase activity.
FT                                {ECO:0000256|HAMAP-Rule:MF_04128}.
FT   ACT_SITE    799    799       For 2'-5'-phosphodiesterase activity.
FT                                {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
//