ID   VP5_APRVF               Reviewed;        1056 AA.
AC   Q2Y0E6;
DT   11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT   20-DEC-2005, sequence version 1.
DT   23-FEB-2022, entry version 40.
DE   RecName: Full=Outer capsid protein VP5;
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=S5;
OS   Aedes pseudoscutellaris reovirus (isolate France) (ApRV).
OC   Viruses; Riboviria; Orthornavirae; Duplornaviricota; Resentoviricetes;
OC   Reovirales; Reoviridae; Spinareovirinae; Dinovernavirus.
OX   NCBI_TaxID=648170;
OH   NCBI_TaxID=316597; Aedes pseudoscutellaris (Mosquito) (Stegomyia pseudoscutellaris).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=16171838; DOI=10.1016/j.virol.2005.08.028;
RA   Attoui H., Mohd Jaafar F., Belhouchet M., Biagini P., Cantaloube J.F.,
RA   de Micco P., de Lamballerie X.;
RT   "Expansion of family Reoviridae to include nine-segmented dsRNA viruses:
RT   isolation and characterization of a new virus designated Aedes
RT   pseudoscutellaris reovirus assigned to a proposed genus (Dinovernavirus).";
RL   Virology 343:212-223(2005).
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   -!- SIMILARITY: Belongs to the orthoreovirus lambda-2 protein family.
CC       {ECO:0000305}.
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DR   EMBL; DQ087280; AAZ94072.1; -; Genomic_RNA.
DR   RefSeq; YP_443939.1; NC_007670.1.
DR   SMR; Q2Y0E6; -.
DR   PRIDE; Q2Y0E6; -.
DR   GeneID; 5076692; -.
DR   KEGG; vg:5076692; -.
DR   Proteomes; UP000001676; Genome.
DR   GO; GO:0039624; C:viral outer 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; Methyltransferase; mRNA capping;
KW   mRNA processing; Multifunctional enzyme; Nucleotide-binding;
KW   Nucleotidyltransferase; Outer capsid protein; Reference proteome;
KW   S-adenosyl-L-methionine; Transferase; Virion.
FT   CHAIN           1..1056
FT                   /note="Outer capsid protein VP5"
FT                   /id="PRO_0000403279"
SQ   SEQUENCE   1056 AA;  121238 MW;  2F6323BE4904A0F3 CRC64;
     MIDLRLEEDI LTATLPEFLT TRPKYRYAYT NTKQQDLRLL GPMRHVRLTH LYKHTKLWNL
     QYIERELTNI EIDDALDEFM QTFSLPYTIE QGTYKYNMLL GMHAHNIGYQ DDVSELIANN
     PQLLNYLNDN PLASIFELID IDLQIYQYGQ NIFNNEVEHM ILFLKDNTYH GVIQALQKHP
     FSATHVTWHL HKHIFVFHSR EKLLNKLLAT GLEDSQLYQR QKTYSTKRGD RPTERMITYI
     EDDHIRRIQA VLPLLLDNIF DVKLHRDSSM TWLKSYADTI YDSAKNSDST VTPEIRKLYL
     RMYNQYMRVF LPIEQYMLYD TTCWPFSEKI TLKINVRLIS SRENQPVSWK TPIDTENLIS
     IVQPDNPINK LNFTAVPSTM IRLNDNIMMY RSVKDMFAAI EYIPDSDENI PTIEMKEQAL
     SRYISPDSEA QNFFNNQPPY LNSIINVNKQ VFEAVRRGNI QVSTGSAEHL CLCMYVKSGL
     IVGRTVLIDD KVILRRNFNA STAKMITCYV KAVTQLYGEG SLIYPGLRIV FFGVETEPAM
     DVLKLFYGDK ALYIQGFGDR GIGRDRFRTK IEDALTLRIG CDILISDIDQ ADYQDPSEEK
     FDDITEFVCY LTELVISNAT IGLVKISMPT YYLLNKISQN INNKFSKVNI NIVKLSTQKP
     YTYEAYLLLS HGSTLTTKGY AKNPVCDVYL EQISLQPQEI KIISTISNEI NYDKPTLYRL
     VVDKNDITDV SIAMHILSIH CSTIITRSVM VKNDNTGAFV TMSGMKDMKR VAIMNRMTDG
     TNENAYMYED NGKLYLQKVP YLEDLVNAFP NGFGSTHQND YDSSTSVINV NALVRQVVYR
     VISKSIPVAL LESLSRIRIV GGRDLGEMNA VYKLYKTPVE VYDTVGITRE YPHVQISYRA
     QRYQFTESIP NHTLLLANYV IMNDIDRAPI SSAEQINTIK KIISKIGVGS IAYVQVYTDV
     VARHINVMTK NDSFLISANA DKTVFKVQVS GYKAVEMCNY EQLLQLVSDN TGVHIIKLTY
     QDVLESCVLS SGILGDTGSW LLDLVLASTY IIEIRG