ID   A0A024CFD6_9REOV        Unreviewed;       835 AA.
AC   A0A024CFD6;
DT   09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT   09-JUL-2014, sequence version 1.
DT   07-OCT-2020, entry version 16.
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:AHZ32439.1};
GN   ORFNames=L312_46714gpVP3 {ECO:0000313|EMBL:AHZ32439.1};
OS   Rotavirus A.
OC   Viruses; Riboviria; Orthornavirae; Duplornaviricota; Resentoviricetes;
OC   Reovirales; Reoviridae; Sedoreovirinae; Rotavirus.
OX   NCBI_TaxID=28875 {ECO:0000313|EMBL:AHZ32439.1, ECO:0000313|Proteomes:UP000118715};
RN   [1] {ECO:0000313|EMBL:AHZ32439.1, ECO:0000313|Proteomes:UP000118715}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RVA/Human-wt/ZAF/MRC-DPRU566/2003/G1P[8]
RC   {ECO:0000313|EMBL:AHZ32439.1};
RA   Wentworth D.E., Halpin R.A., Stucker K.M., Akopov A., Fedorova N.,
RA   Tsitrin T., Puri V., Stockwell T., Amedeo P., Bishop B., Gupta N.,
RA   Hoover J., Katzel D., Schobel S., Shrivastava S., Nyaga M.M.,
RA   Magagula N.B., Peenze I., Seheri M.L., Mphahlele J., Steele A.D.,
RA   Mwenda M.J.;
RL   Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
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; KJ751682; AHZ32439.1; -; Genomic_RNA.
DR   Proteomes; UP000118715; 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   3: Inferred from homology;
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;  97722 MW;  22DFA71399ABCB64 CRC64;
     MKVLALRHSV AQVYADTQTY LHDDLKDEYE NAFLISNLTT HNILYLNYSL KTLKILNKSG
     IAAVEVQSPD ELFALIRCNF TYDYENNIVY LHDYSYYTNN EIRTDQHWIT KTDMIDYLLP
     GWKLTYVGYN GKNTRGHYNF SFICQNAATD DDIIIEYIYS NELDFQNFLL RKIKERMTTS
     LPIARLSNRV FRDKLFPSIV NIHKKVINVG PRNESMFTFL NFPTIKQFSN GAYIVKHTIK
     LKQEKWLGKR VSQFDIGQYK NMLNVVTTIY YYYNLYYSKP IIYMLGSAPS YWIYDIKQYS
     DFTFETWDPL DTPYSTTHHK ELFFDKDVNK LKDNSVLYID IRTDRGSMDW KEWRKIVEQQ
     TVSNLNIAYK YLSTGKAKVC CVKLTAMDLE LPITAKLLHH PTTEVRSEFY AILDVWDIIT
     IKRFIPKGVF YAFINNVTTE NVFIQPPFKL KTSPTDYIVA LYALSNDFNS RQDVINLVNK
     QKQSLITVRI NNTFKDEPKV NFKNIYDWTF LPTDFELKDS IITSYDGCLG VFGLSISLPS
     KPTGNNHLFI INGTDKYNKL DQYANHMGIS RRSHQIRFSE SATSYSGYIF RDLSNNNFNL
     IGTNVENSVS GHVYNALIYY RYNYAFDLKR WIYLHSIGKV AIEGGRYYEH APIELIYACR
     SAKEFAILQD DLTVLRYANE IEGYINKVYS ITYADDPNYF IGIKFNSIPY EYDVKIPHLT
     LGVLFISENM INDVITVLKK MKTELFKMEI STSYTYMLSD NTYVANASGV LSTYFKLYNM
     FYRNHITFGQ SRMFIPHITL SFSNKQTVRI ESTKLKISSI YLRKIKGETV FDMSE
//