ID   VP2_RRSVT               Reviewed;        1192 AA.
AC   O56043;
DT   11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   23-FEB-2022, entry version 56.
DE   RecName: Full=Outer capsid protein VP2;
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;
GN   Name=S2;
OS   Rice ragged stunt virus (isolate Thailand) (RRSV).
OC   Viruses; Riboviria; Orthornavirae; Duplornaviricota; Resentoviricetes;
OC   Reovirales; Reoviridae; Spinareovirinae; Oryzavirus.
OX   NCBI_TaxID=649603;
OH   NCBI_TaxID=4534; Oryza latifolia.
OH   NCBI_TaxID=4536; Oryza nivara (Indian wild rice) (Oryza sativa f. spontanea).
OH   NCBI_TaxID=4529; Oryza rufipogon (Brownbeard rice) (Asian wild rice).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RA   Upadhyaya N.M., Li Z., Ramm K., Yang M., Gellatly J.A., Kositratana W.,
RA   Gerlach W.L., Waterhouse P.M.;
RT   "Rice ragged stunt oryzavirus:complete sequence and genome organization.";
RL   Submitted (AUG-1997) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Outer capsid protein involved in mRNA capping. Catalyzes the
CC       last 3 enzymatic activities for formation of the 5' cap structure on
CC       the viral plus-strand transcripts, namely the RNA guanylyltransferase,
CC       RNA-7N- and RNA-2'O-methyltransferase activities (By similarity).
CC       {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   -!- SUBCELLULAR LOCATION: Virion {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AF020335; AAC04673.1; -; Genomic_RNA.
DR   PIR; T08609; T08609.
DR   RefSeq; NP_620515.1; NC_003750.1.
DR   SMR; O56043; -.
DR   GeneID; 991196; -.
DR   KEGG; vg:991196; -.
DR   Proteomes; UP000000348; Genome.
DR   GO; GO:0039625; C:viral inner capsid; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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.
PE   3: Inferred from homology;
KW   ATP-binding; Capsid protein; GTP-binding; Inner capsid protein;
KW   Methyltransferase; mRNA capping; mRNA processing; Multifunctional enzyme;
KW   Nucleotide-binding; Nucleotidyltransferase; Reference proteome;
KW   S-adenosyl-L-methionine; Transferase; Virion.
FT   CHAIN           1..1192
FT                   /note="Outer capsid protein VP2"
FT                   /id="PRO_0000403635"
FT   REGION          1112..1192
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1125..1185
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1192 AA;  133081 MW;  E44C2EF707F72F7C CRC64;
     MTEYTNLPVK WTNGIVISDE RMMLDPLPSE VSAVLDAPIN YSYRYNELRR THSLKLFGVW
     SGYIPSHADK HLMIFQLLQQ EKELTGDEIR LALRQMQGSI KLPINDKLLD SLDRYSLIFA
     WIAYAGCLDS AFWQQVCADP KCLVYNPDDN LKFSLMFSLA RQYSATTRIC SADGLRIPSQ
     ISPDLGQLAF DLVFNSSVRQ TVWFHANDFP AFDFYTKDVG TMVTFHVNFL YNMTHCVPFK
     TKQSCAEYLI QKAHEAWSVY CGVLNDTIRH RLRLVEGVGI VTLDVDLQIL AAVGWYLPLL
     VYTIRSVSGS DISEWLNVAR REFRDLNCSS MINGEGYVGV PEQFWTIHAT SKARMWPRVK
     KYTCDLTDLY NGDLSSTVLG EGASETGTVK WFDVPLGPKV ENFRVVGTRI GALSRANVIY
     NYEDPSDNCD LARAIGSFVP SLPTSGTRDT NGDLEDAKKM FDYRVSQNVY SICQKGKISS
     LVSRSVKNLR ASLMNGELRV YKGSRLWALR AMLFSDKLRY KSDGQVIDPY ESHRGKITVR
     LNNSSLKMLS AFVTLIELAM AQSSGVEDNM LNGRGLSPLQ VRSDREVSRV VIAGAINEPL
     VGCLRRMYPK LSVIGFGMDA VGENERLTVE GASQRNLACD MLISDIDQTF YSDFTKMCNV
     TVKHALAFSS WSDYVLMKVN YPSSHLLNEI KQALLSRGFS RIVLPVVMCG QNSFTSEVFV
     YIGRAGVGGH VDFKNNWFTK NDILMRRYRH MKAPLITIPQ VVHSVVSKCV TKHDTELFAN
     PGSIVALTVE YASAREVVSL ISEVCSPVWT WRTGAGANKF VNIVGMPSKA RAALTRRTDE
     HYYLKAFERN IVGTSFGMYK GIPRIDALNC VSWVTIFGAA MRECLYWIVD TLKVQYNEVI
     SIGARNMTDI EFIKPSVKLT CYDEYYANPQ DLATHYNVNY ENKYFNWLSP TLVNDSVYVA
     NFVIMAPTEG SESPSATEQL DRIDSVAGAM AKSSITRMTF VGNLYDSRFL ADIALSSLPP
     EGLKVNDTRT TVQIGKYPPC AAVKPSAFLE RMKKYKGVLS YHVYPLGYDR VLKTCADNLW
     IPDVAGSPML AFCQGLSYAF YITKPAIPDE GIDQFMLDDM PDDGSGSVTP TQSPSPSPSP
     SAAANTEAST VVEPIDNLNV VSPTVPGQPS QTPVNPNQST ELQSVAKPGI VR