ID   VP4_LDCPR               Reviewed;        1058 AA.
AC   Q91ID8;
DT   11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   02-JUN-2021, entry version 45.
DE   RecName: Full=Outer capsid protein VP4;
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=S4;
OS   Lymantria dispar cypovirus 1 (isolate Rao) (LdCPV-1).
OC   Viruses; Riboviria; Orthornavirae; Duplornaviricota; Resentoviricetes;
OC   Reovirales; Reoviridae; Spinareovirinae; Cypovirus.
OX   NCBI_TaxID=648169;
OH   NCBI_TaxID=13123; Lymantria dispar (Gypsy moth) (Porthetria dispar).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RA   Rao S., Shapiro M., Lynn D., Hagiwara K., Blackmon B., Fang G.,
RA   Carner G.R.;
RT   "Identification of dsRNA electrophoretypes of two cypoviruses from a dual
RT   infection in gypsy moth, Lymantria dispar.";
RL   Submitted (JUN-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 orthoreovirus lambda-2 protein family.
CC       {ECO:0000305}.
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DR   EMBL; AF389465; AAK73523.1; -; Genomic_RNA.
DR   RefSeq; NP_149149.1; NC_003019.1.
DR   SMR; Q91ID8; -.
DR   GeneID; 2598191; -.
DR   KEGG; vg:2598191; -.
DR   Proteomes; UP000006712; 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..1058
FT                   /note="Outer capsid protein VP4"
FT                   /id="PRO_0000403207"
SQ   SEQUENCE   1058 AA;  119369 MW;  8395151EBB7F0098 CRC64;
     MWHYTSINND TRVALDPKPN QIRTITKPNT VPQLGTDYLY TFNPQRRSHT LRLLGPFQYF
     NFSETDRGHP LFRLPLKYPS KTIPTDELVD NLHSWMRSVH LLHTRSDDNS LRYNWMLGVY
     ARSTNYTTPV GQLVVKTPAI LNYANPQDAF NSVFIALGID YIDIPITNSN IFDDGSTPYN
     VRIWHAPTMT EVNHILTLMR KSTLVSTHSS WHWNVLHTFH YRSESDMIDH FSAKILEDWR
     QKEKFDKGAL VEADRVIQRL IPLSSSTYVQ RLAAIGALYP NEFTENVLDL SRLSTALLQL
     SDTYYQHAND QLKRLYRRMY NDSRTLYMTA RHQELLLAQV AANPNILLYP YTHIFTTAHI
     TASYISNTGQ GRIKHSLAVT GTTEHSTVPD IILGPTSEDV ITISMVEPMS IAAEDMYGYV
     IDTPTRDIWP ADEQVEQKGD AVALYDTKTS RALGMFNNTV RIDDLLSPLL GRVYRTYAKG
     DTMAMTQGSL DHQTLCAAVD SDITFVGNRM IAPLAEGYVP RAMHRNNSTM KMLSLYVAIK
     KLENFAANSY LMSPDTSIIL LGAEREPAVN ILRRFNSSVS NVRIIGMGDR AVEPNIRVRV
     PFPIDKNISA DFVICDINSY EDQSFESMFG ETMSVVTTCA SAATRSLVKI NHPSEYMINS
     VIERLSKLGG VFYHTALLKT ASQNTYSYET YIYITPIAAA VGFLFYNNSA IINRYMTAVA
     DDEAPVIPSI HTIIKEHSNT YSPGLFCGCI DVQSAPLALS QLKSYCSEAT TWRVDSDDNL
     VNIIARIDPA RIALEFRTRS NTSAHHEYQR CVPNGLGFKI RKTREFRYMH REVTFIHKLM
     MYALIREQIS LTESMTQVVS IGGRNLADIS VVPLTMKYIV IDPAARIETL TQEKKNIEIQ
     ARAFQFDAST MDLENNSIYL FIAVIMNEPN GAATPAQTQI DKIRNVATAM LTRTNCVAYI
     SFYESGIITR LSQSTAHKTI RVEDGRLKVA NYVPVDTLPE ADVTLMLRDI GITYEIIRPS
     TPELVNACSS YGIRLGSTGG AVLDVFNHYS PVIKLVRS