ID   VP3_ROTJ1               Reviewed;         719 AA.
AC   Q45UF7;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   29-SEP-2021, entry version 53.
DE   RecName: Full=Protein VP3;
DE   Includes:
DE     RecName: Full=mRNA guanylyltransferase;
DE              EC=2.7.7.50;
DE   Includes:
DE     RecName: Full=mRNA (guanine-N(7))-methyltransferase;
DE              EC=2.1.1.56;
OS   Rotavirus X (strain RVX/Human/China/NADRV-J19/1997/GXP[X]) (RV ADRV-N)
OS   (Rotavirus (isolate novel adult diarrhea rotavirus-J19)).
OC   Viruses; Riboviria; Orthornavirae; Duplornaviricota; Resentoviricetes;
OC   Reovirales; Reoviridae; Sedoreovirinae; Rotavirus.
OX   NCBI_TaxID=335103;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=18796732; DOI=10.1099/vir.0.2008/001933-0;
RA   Jiang S., Ji S., Tang Q., Cui X., Yang H., Kan B., Gao S.;
RT   "Molecular characterization of a novel adult diarrhoea rotavirus strain J19
RT   isolated in China and its significance for the evolution and origin of
RT   group B rotaviruses.";
RL   J. Gen. Virol. 89:2622-2629(2008).
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. Together with VP1 polymerase, forms
CC       an enzyme 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 don't (By
CC       similarity). {ECO:0000250}.
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   -!- 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;
CC   -!- SUBUNIT: Interacts with VP1. Interacts with VP2. {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: Virion {ECO:0000305}. Note=Attached inside the
CC       inner capsid as a minor component. Also found in spherical cytoplasmic
CC       structures, called virus factories, that appear early after infection
CC       and are the site of viral replication and packaging (Potential).
CC       {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the rotavirus VP3 family. {ECO:0000305}.
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DR   EMBL; DQ113900; AAZ03488.1; -; Genomic_RNA.
DR   RefSeq; YP_392493.1; NC_007551.1.
DR   PRIDE; Q45UF7; -.
DR   GeneID; 5076653; -.
DR   KEGG; vg:5076653; -.
DR   Proteomes; UP000007663; Genome.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004482; F:mRNA (guanine-N7-)-methyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004484; F:mRNA guanylyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
PE   3: Inferred from homology;
KW   GTP-binding; Methyltransferase; mRNA capping; mRNA processing;
KW   Multifunctional enzyme; Nucleotide-binding; Nucleotidyltransferase;
KW   Reference proteome; RNA-binding; S-adenosyl-L-methionine; Transferase;
KW   Virion.
FT   CHAIN           1..719
FT                   /note="Protein VP3"
FT                   /id="PRO_0000369837"
SQ   SEQUENCE   719 AA;  84711 MW;  F896921F3AC92D24 CRC64;
     MAKLIIINSE KGEKVETHED IFKLSNLQQR EIYAITNERT KSILLNQTFY TILDIENEPK
     DKVAFDSYNS LFPTSIFSYS RQDRLFGTCN HVLDNNIHYS FALFDSMVDN LSTYLPNDWN
     IIKISDSIDY PIGNDLLFYV FDNLVHMTID QFVNSEEKQM NTVPKCKESQ DKIKEVFTDI
     MSHLYMPAID YDPQSYNYRV SRREIGNLVR DQVFSLVKGH IHLIGPEMES LRNIIMFLHA
     GNSITFHTID TSTKSSYIKE LEFNKKTKLT MASVLVNQRK NMNNFFKGLI RHYITYGIPR
     KVYYIGAYPS YWLELITWVP FNIVAYDPKY RRVDNDKIIW YDRLFDRNDI ETIESKSYIY
     IDIRTDVRNL DTTKKQRIFK EEDDMIVDMA IKLASKQCTV MFKRKIFPGN NMSFGDPLFH
     PKLTQLGREY YNCITTIVSP SVYKESELYS LLLSARSNNV SNYVYGGSKF DQFSIVNCNS
     TVVALYSLSN TVNSLKTIEH AIKYNHIITF PHRTDRGDWR NIEELDNSSP FQNRKRQLEF
     EDWSIDPKNY VMKFRCEMVS ESVFLQLGHS RALIPDLYNH MISLRMEMPL FYSDRFFSHI
     GIRQPSIFKR DSYMTSRLSA YISRQLTHSI NLSVLKRNHF EGYSGHLIAI ETSFSSLVFT
     MSPYRWLIRA KKLLTKNKMR DKFKIGDGQP HTREEFENTY DYLKINRLVN STFRSLLLD