ID   VP1_AQRVG               Reviewed;        1298 AA.
AC   B2BND9;
DT   08-FEB-2011, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 1.
DT   03-AUG-2022, entry version 50.
DE   RecName: Full=Outer capsid protein VP1;
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=S1;
OS   Aquareovirus G (isolate American grass carp/USA/PB01-155/-) (AQRV-G).
OC   Viruses; Riboviria; Orthornavirae; Duplornaviricota; Resentoviricetes;
OC   Reovirales; Reoviridae; Spinareovirinae; Aquareovirus.
OX   NCBI_TaxID=648234;
OH   NCBI_TaxID=7959; Ctenopharyngodon idella (Grass carp) (Leuciscus idella).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=18191982; DOI=10.1016/j.virol.2007.12.006;
RA   Mohd Jaafar F., Goodwin A.E., Belhouchet M., Merry G., Fang Q.,
RA   Cantaloube J.F., Biagini P., de Micco P., Mertens P.P., Attoui H.;
RT   "Complete characterisation of the American grass carp reovirus genome
RT   (genus Aquareovirus: family Reoviridae) reveals an evolutionary link
RT   between aquareoviruses and coltiviruses.";
RL   Virology 373:310-321(2008).
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 aquareoviridae outer capsid VP1 protein
CC       family. {ECO:0000305}.
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DR   EMBL; EF589098; ABV01039.1; -; Genomic_RNA.
DR   RefSeq; YP_001837094.1; NC_010584.1.
DR   SMR; B2BND9; -.
DR   GeneID; 6218799; -.
DR   KEGG; vg:6218799; -.
DR   Proteomes; UP000001674; 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.
DR   Gene3D; 2.60.40.10; -; 1.
DR   Gene3D; 3.40.50.150; -; 1.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR010311; Reovirus_L2.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   Pfam; PF06016; Reovirus_L2; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Capsid protein; GTP-binding; Methyltransferase; mRNA capping;
KW   mRNA processing; Multifunctional enzyme; Nucleotide-binding;
KW   Outer capsid protein; Reference proteome; S-adenosyl-L-methionine;
KW   Transferase; Virion.
FT   CHAIN           1..1298
FT                   /note="Outer capsid protein VP1"
FT                   /id="PRO_0000404186"
SQ   SEQUENCE   1298 AA;  141101 MW;  28868AF6DE04AB09 CRC64;
     MAAVYGIQLV NKLNTATVRR TYLPNRYDIL IDRLTNHTQH NVLHRALDFN ATTREATVVQ
     LYPPLNAWTP SSATNVTDYT YLEWVDFIQE RSTTFSEVLR QRYPITTYAN RFVNPLVVGA
     AFSDFLNADD ISVYLEHLFY DPRVESPVQA ILSFPYQWTP RFHVFQEFIR TGAGCKYARS
     SRDMTPPTPA RLPRYGKHRP AYATVFYYNT LAARSTILAG ISAGPTALEH FDSPTYGPHI
     ILPQAGDVLG YHSRPVSQAD LLMTESVMDC LRENSQASAS TAVARLDQTY HPVANFDPTN
     EDSMMSRLTN LALLVVQGAQ AELAIPTVPT NDDVRGFVAR LMSEGQRQRW FPYRTDRVLI
     HPDSPFVLPP GDFYAAYRVA NFPFTSGTYT SVPNATKPLR VLPQYRAATI LPAQATQAYE
     DHVIAPININ HGYCISGGVY FTADDISIDP TPFPARDLAQ LPQNYFDPNR MARRELLRRL
     RVPSDRSYLK DNAVFTFLAS LVNPATALPA LQPGFSLAYL GASAAHAKSD EPTILADLRN
     GSIPGLPIPS RIAQFGYDVV HGSLLDLTRA VPTGTFGLVY ADLDQVEDAG TDLPAANRAA
     LAMLGTTLQM CTAGGVAVLK VNFPTVEFWT QLFNQYATFA TTLHVVKPIV VNSSEVFVVM
     SGRQSAGNLT CTTSLQRALL AMYARNAAID QTMTHVPMLG QADDGTSALG MEAIRLFDPL
     FVEGNPNAAT SALATLMANV VPSSIHMSRL PVNGPVSTTI FGKRTFLSTR RRDRLLEYPL
     PMVTAINHQR RFTAPPSFSI YPTEPVNVTT LVAAGYNAYV HTVITSAQPA HLFDLGTGPE
     CRILSLVPQN TRVTMVDSRP CAELMQAYDP NTTAYEQADY TLAAFWNGRQ CDAVSAIFTL
     GAAAASNAVT IDALLANLLP SIANAGTTRL WLQVNAPLAG PTPIPGLIDI DTRAGTYTFN
     NGERTEPYID PQVMQATVLA HFPNATLSWY TLPPTCEWLD YIIGAGSSLD LSTIPTALQY
     SQLTPILSID TNVAPLRVNP IPTPLGQQCA IRIPTNDPAA VLDAKHRGVP VITGTPAALT
     SLMGNAALQY IQANNEFLLQ LTPTLAGIFD VTLTSAGQPP IPRGSFTITA PPPTAAVTMP
     ANIDYTDAGN DGPIACDPYY NLAVCIMRNG QYVRVNPEKA RVETVAAGRA LHFVLDLADN
     HVLMYLCDVT PAAIGAIIAH PLADIYQLVF PNNTPLRASL PYIGGGARVE LNNQPYLSLT
     NPPPVLPAGT ALAALATAAS VGQPTYTLPA GAYRYVLE