ID   VP3_ROTB2               Reviewed;         719 AA.
AC   A9Q1K9;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 1.
DT   03-AUG-2022, entry version 47.
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 (isolate RVX/Human/Bangladesh/NADRV-B219/2002/GXP[X]) (RV
OS   ADRV-N) (Rotavirus (isolate novel adult diarrhea rotavirus-B219)).
OC   Viruses; Riboviria; Orthornavirae; Duplornaviricota; Resentoviricetes;
OC   Reovirales; Reoviridae; Sedoreovirinae; Rotavirus; unclassified Rotavirus.
OX   NCBI_TaxID=348136;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=18814255; DOI=10.1002/jmv.21286;
RA   Nagashima S., Kobayashi N., Ishino M., Alam M.M., Ahmed M.U., Paul S.K.,
RA   Ganesh B., Chawla-Sarkar M., Krishnan T., Naik T.N., Wang Y.-H.;
RT   "Whole genomic characterization of a human rotavirus strain B219 belonging
RT   to a novel group of the genus Rotavirus.";
RL   J. Med. Virol. 80:2023-2033(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; EF453357; ABR32124.1; -; mRNA.
DR   PRIDE; A9Q1K9; -.
DR   Proteomes; UP000174021; 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   2: Evidence at transcript level;
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_0000369836"
SQ   SEQUENCE   719 AA;  84556 MW;  6EE2CE8A87F5CC93 CRC64;
     MAKLIIINSE KGEKVETHED IFKLSNLQQR EIYAITNERT KSILLNQTFY TILDIENEPK
     DRVAFDSYNS LFPTSIFSYN RQDRLFGTCN HVLDNNIHYS FALFDSMVDN LSTYLPNDWN
     IIKIPDSIDY PIGNDLLFYV FDNLVHMTID QFVNSEEKQM NTVPKCKESQ DRIKEVFTDI
     MSHLYMPAID YDPQSYNYRI SRREIGNLVR DQVFSLVKGH IHLIGPEMES LRNIIMFLHA
     GNSITFHTID TSKKSNYIKE LEFNKKTKLT MANVLINQRK NMNNFFKGLI KHYMTYGIPN
     KVYYIGAYPS YWLELITWVP FNIITYDPKY RHVDNDKIIW HDKLFDRNDI ETIESKSYIY
     IDIRTDIRKL DMTKKQRIFK EEDDMIVEIA TKLASKQCTV MFKRKIFPGN NMSFGDPLFH
     PKLTQLGREY YNCITTIVSP SIYKESELYS LLLSARSNNV SNYVYGGSKF DQSSIVNYNS
     TVIALYSLSN TVNSLETIEH AIKFNHIITF PHRTDRGDWR NIEELNNLSP FQNKKRQLEF
     EDWSIDPKNY AMKFGCEIVS ESVFLQLGHS RALIPDLYNH IISIRMEMPL FYPDRFFSHI
     GIRQPSIFKR DSYMTSRLSA YISRQLTHSI DLSVLKKNHF EGYSGHLIAI ETSFSSLVFT
     MSPYRWLIRA KKSLTKSKIR DKFKIGDGQP HTREEFENTY DYLKINRLVN STFHSLLLG