ID   VP1_AQRVA               Reviewed;        1297 AA.
AC   Q8VA43;
DT   08-FEB-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   03-AUG-2022, entry version 59.
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 A (isolate Chum salmon/Japan/CSRV/1981) (AQRV-A).
OC   Viruses; Riboviria; Orthornavirae; Duplornaviricota; Resentoviricetes;
OC   Reovirales; Reoviridae; Spinareovirinae; Aquareovirus.
OX   NCBI_TaxID=928295;
OH   NCBI_TaxID=8018; Oncorhynchus keta (Chum salmon) (Salmo keta).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=3819694; DOI=10.1099/0022-1317-68-2-353;
RA   Winton J.R., Lannan C.N., Fryer J.L., Hedrick R.P., Meyers T.R.,
RA   Plumb J.A., Yamamoto T.;
RT   "Morphological and biochemical properties of four members of a novel group
RT   of reoviruses isolated from aquatic animals.";
RL   J. Gen. Virol. 68:353-364(1987).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RA   Rao S., Carner G.R., Chen W., Winton J.R.;
RT   "Complete genome sequence of the chum salmon virus.";
RL   Submitted (SEP-2001) 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   -!- SIMILARITY: Belongs to the aquareoviridae outer capsid VP1 protein
CC       family. {ECO:0000305}.
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DR   EMBL; AF418294; AAL31496.1; -; Genomic_RNA.
DR   RefSeq; YP_398629.1; NC_007582.1.
DR   SMR; Q8VA43; -.
DR   GeneID; 3773155; -.
DR   KEGG; vg:3773155; -.
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; 3.40.50.150; -; 1.
DR   InterPro; IPR010311; Reovirus_L2.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   Pfam; PF06016; Reovirus_L2; 1.
DR   PIRSF; PIRSF000845; 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; S-adenosyl-L-methionine; Transferase; Virion.
FT   CHAIN           1..1297
FT                   /note="Outer capsid protein VP1"
FT                   /id="PRO_0000404184"
SQ   SEQUENCE   1297 AA;  140925 MW;  672218FB75A327CB CRC64;
     MATVYGIQLT NRLNTATVRR PLRLRRYDSC ITTFTTPNGI SQLYRALDFQ PTSFQASILQ
     TFPPLNAWSP SPQFVPDDLS LSQWKEWITE RMRALATVLQ RAHPLVANAG REVNPITIGL
     ITSSFLNQRP IDGYLPFLFL ARNARDPIAP LVTVDITFSD DTYVSRHVLY TPAGLKYLTL
     SSYDPTKPSS ICTFGKHIPL YATAAFYPDE TARLTILHRY NGGPPLIEHF DQPTYGPHVL
     IPALGSPEGY DTHLNICRLL LAEGLLDSFR LNASAGPSTA VARIDQTYHV VMNGSPDDHT
     QLATRLSNLS LLAVQGCQMT VQVADHPTMS DVGGFLVRLQ GPGDPQRLIA YRTDQILIWQ
     ASPFPFGNNA RYVRRPGRVP FTIGTTTYVP DTKTPLPFLP QYRQATVNKN NAQDSYELNV
     LPSLPIYSPF ALTGGAFFQA RDITGDPANV WPVNTLPGLP RDYFSIQSRQ RRELLSRLRS
     HSDRSYVKDV HNISFASTVL NPVNNQIVLS EGFSMAYLGA ASTHGTTDEP LIIEALKSGT
     VPGVPIPSKI SQFGYDVANG SIMDATLAPP TGTFTFVYSD VDQVEDAGLS IVATNRAAVA
     VTNIALSMTT AGGLTVVKVN FPTPAFWTQL FRNHATDARA LYILKPLIVN SVEVFLLFVS
     RATAGNLVSS PALRQFLVQL FDRSTSLSEV MAHVPLLGDV DTGVTTLGFN ACRLYSPDLP
     TVNITPEIQT LAYQLATIVP STSFIAREDY DGATAVTFYG KRTFLSRNRL DRLVDVPVPA
     TNAINHQTRF TGSPVYQLFP TNPAPVTQLL WLARTTGLYT ASWPRLLLSR WLICGTGPEC
     RILSLMPPAT SVTMIDSRPP AESLAAFNPA MNQYIVGNFL DPAQWVANPH DSLTAIFSLG
     AAFAGAGQDL VVGLTAFLRL IQPSNVQHLW LQLNTTLTST ASLPGLIEID TRTGQYIFNG
     GQRTEPYAAP DAILAAIRLV YPAATTSWLT ASSTMDWTEY VIGLGSSMSL DDVSTMISYS
     GLTPILHIDL TQRPMDVPVP LVVGVQAVIH VAAPVQQTTV IGSMAGVQVF TADGVNAPST
     IGPLAVVWDP VLSRWDLTIT PNQPGVLDVV VDHNGVLLNR GSTTIALPPA TIVITFPQAA
     NRDFTNAGND AAVVCDAFYR LGVFVSVNGA FQPVNPERAA IVTAANARVL HYVYDLSDNH
     VLMYVCDITD NNIGRNVALP LADIFQTLFP NNTPLLASPP YPSASGRLML NGQLFVDLDP
     LPPVLPPGVQ IQALSTAIEP ARQTAEVPGG AYTYVVV