ID   VP1_AQRVC               Reviewed;        1299 AA.
AC   Q8JU62;
DT   08-FEB-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-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 C (isolate Golden shiner/USA/GSRV/1977) (AQRV-C).
OC   Viruses; Riboviria; Orthornavirae; Duplornaviricota; Resentoviricetes;
OC   Reovirales; Reoviridae; Spinareovirinae; Aquareovirus.
OX   NCBI_TaxID=185783;
OH   NCBI_TaxID=28800; Notemigonus crysoleucas (Golden shiner) (Cyprinus crysoleucas).
OH   NCBI_TaxID=90988; Pimephales promelas (Fathead minnow).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=12124458; DOI=10.1099/0022-1317-83-8-1941;
RA   Attoui H., Fang Q., Mohd Jaafar F., Cantaloube J.F., Biagini P.,
RA   de Micco P., de Lamballerie X.;
RT   "Common evolutionary origin of aquareoviruses and orthoreoviruses revealed
RT   by genome characterization of Golden shiner reovirus, Grass carp reovirus,
RT   Striped bass reovirus and golden ide reovirus (genus Aquareovirus, family
RT   Reoviridae).";
RL   J. Gen. Virol. 83:1941-1951(2002).
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; AF403398; AAM92744.1; -; Genomic_RNA.
DR   RefSeq; NP_938060.1; NC_005166.1.
DR   SMR; Q8JU62; -.
DR   GeneID; 2648329; -.
DR   KEGG; vg:2648329; -.
DR   Proteomes; UP000006713; 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.
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; Reference proteome; S-adenosyl-L-methionine;
KW   Transferase; Virion.
FT   CHAIN           1..1299
FT                   /note="Outer capsid protein VP1"
FT                   /id="PRO_0000404185"
SQ   SEQUENCE   1299 AA;  141261 MW;  8330157DFCFB9D17 CRC64;
     MAAVFGIQLV PKLNTSTTRR TFLPLRFDLL LDRLQSTNLH GVLYRALDFN PVDRSATVIQ
     TYPPLNAWSP HPAFIENPLD YRDWTEFIHD RALAFVGVLT QRYPLTQNAQ RYTNPLVLGA
     AFGDFLNARS IDIFLDRLFY GPTQESPITS ITKFPYQWTI DFNVTADSVR TPAGCKYITL
     YGYDPSRPST PATYGKHRPT YATVFYYSTL PARSRLLANL AAGPTVLEHF DSPTYGPHLL
     LPQTGDVLGY SSSLISQAAL LMVESVMDAL RDNANASAST AVTRLDQSYH PVTSFDPSTF
     NTLLQRATNL ALLAVQGVQS ESAIPAIPTM SDVRSFVARL MAEGDPQQWF PYRVDQILYW
     PESPFVPPIG PFYAPFRPVN FPFTTGSYTV VPDASRPLRL LPQYRNATIT VQQADDAYED
     TALSPLITTH GFCVTGGVST SIYDISGDPT AYPPAQLVDT PNDYFDRERM ARRDLFRRLR
     APADRSAIKD RAVFDFLASL VNPTTANPVL DTSFSMAYLG ASSAHANADE PVILADIRSG
     SIPGLPIPRR IVQFGYDVVH GSLLDLSRAV PTGTFGLVYA DLDQVEDAGT DMPAANRAAI
     AMLGTALQMT TAGGVSVLKV NFPTRAFWTQ VFNLYATHAT TLHLVKPTIV NSSEVFLVFG
     GRQSNGALRS TTALQRALLS LYARNAAIDR AVTHIPFFGV PDDGTSDLGI DAVRLFDPMF
     SDAVANLPSN ALASLVSRVV PSSIMFTRVP SNGPVSTTIY GKRTFLSNRR RARLRDVPML
     ITTTLVHQRR FTTPPTFTLF SSEAVPVTTL VAAGYNSFIS EQTRNPNLAH LLDLGTGPEC
     RILSLIPPTL QVTMSDARPC AELMASFDPA LTAYVQGDYS TAAFWNGIRC DSATAIFTLG
     AAAAAAGTDL IAFVQQLIPR IVAAGGTRMW LQLNTPLYEV SSLPDLIDID LRDRVYRFNG
     GERVEPYADP VPLQQAIAAL LPAAALSWHT LSPTCDWLPY IIGVGSPLNL SDINTAISYS
     RLTPILHIDT TTPPLRVNPV PTPLNQQCAI RITSLDPAAV LSVQHNGVEV IGGTPGNVIS
     VAGAAALQYI LANQEFLLQF TPTLPGIFDV FLTTLGQPPV PRGSFTITPP PTTVVLNMPP
     PGQLDFTDVG NDARITCDPY YQLAVCIFKD GQYVRVNPEK ASVVTNAPNR DLHFVLDLAD
     NHVLLYLCDV TPSGLGDRIA FPIVDIYRIA FPRNTPVRAS LPYTGGGAHL TSGGNPFMSL
     TTPPAVLPAG VALAALSTSV ATQYPTYTLP AGVYEYVIE