VP3_MYRV9
ID VP3_MYRV9 Reviewed; 1065 AA.
AC Q7TDB4;
DT 11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 25-MAY-2022, entry version 41.
DE RecName: Full=Outer capsid protein VP3;
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=S3;
OS Cryphonectria parasitica mycoreovirus 1 (strain 9B21) (CpMYRV-1).
OC Viruses; Riboviria; Orthornavirae; Duplornaviricota; Resentoviricetes;
OC Reovirales; Reoviridae; Spinareovirinae; Mycoreovirus.
OX NCBI_TaxID=230407;
OH NCBI_TaxID=5116; Cryphonectria parasitica (Chestnut blight fungus) (Endothia parasitica).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=14694120; DOI=10.1128/jvi.78.2.892-898.2004;
RA Hillman B.I., Supyani S., Kondo H., Suzuki N.;
RT "A reovirus of the fungus Cryphonectria parasitica that is infectious as
RT particles and related to the coltivirus genus of animal pathogens.";
RL J. Virol. 78:892-898(2004).
RN [2]
RP MUTAGENESIS OF HIS-233; HIS-242; TYR-243; PHE-244 AND PHE-246.
RX PubMed=17170467; DOI=10.1099/vir.0.82318-0;
RA Supyani S., Hillman B.I., Suzuki N.;
RT "Baculovirus expression of the 11 mycoreovirus-1 genome segments and
RT identification of the guanylyltransferase-encoding segment.";
RL J. Gen. Virol. 88:342-350(2007).
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}.
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DR EMBL; AY277890; AAP45579.1; -; Genomic_RNA.
DR RefSeq; YP_001936006.1; NC_010745.1.
DR GeneID; 6336088; -.
DR KEGG; vg:6336088; -.
DR Proteomes; UP000006719; Genome.
DR GO; GO:0019028; C:viral 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 InterPro; IPR045917; VP3-like.
DR Pfam; PF18965; DUF5705; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Capsid protein; GTP-binding; Methyltransferase; mRNA capping;
KW mRNA processing; Multifunctional enzyme; Nucleotide-binding;
KW Nucleotidyltransferase; Reference proteome; S-adenosyl-L-methionine;
KW Transferase; Virion.
FT CHAIN 1..1065
FT /note="Outer capsid protein VP3"
FT /id="PRO_0000403425"
FT MUTAGEN 233
FT /note="H->A: Complete loss of GTP-binding activity."
FT /evidence="ECO:0000269|PubMed:17170467"
FT MUTAGEN 242
FT /note="H->A: Complete loss of GTP-binding activity."
FT /evidence="ECO:0000269|PubMed:17170467"
FT MUTAGEN 243
FT /note="Y->A: Complete loss of GTP-binding activity."
FT /evidence="ECO:0000269|PubMed:17170467"
FT MUTAGEN 244
FT /note="F->A: Complete loss of GTP-binding activity."
FT /evidence="ECO:0000269|PubMed:17170467"
FT MUTAGEN 246
FT /note="F->A: Complete loss of GTP-binding activity."
FT /evidence="ECO:0000269|PubMed:17170467"
SQ SEQUENCE 1065 AA; 120825 MW; 27883B7A0A3589B9 CRC64;
MFDRQYPTVH DLYIPFPVFQ SRLEQPFDTT VTSIRELRTI SSQSTVYGYD LTVNDPLYYD
LEPLLGNSIS LTLDPKLTDS ERLDAVYLDI NNRLANCHGD LLRKFSATSY SIDTSVIPYV
FLPMYRYLLH IMTGSAFNSL FRQMIVNVDA NCANADESLL TSAQHLFALL NKINPSRQLP
APLRHILINA TIADVPYDMQ GKFVPYNVVF LPTSNESLRD ATIARIREPA GYHPRPSIVV
PHYFVFRSTT DALCRFMYLA KRTFLHVNDK TATHTSVRRC ELLRLNFPLD QSFAQLSLLV
QLQLPLSTLS IQRLPHLSTT VNQLITLASS SYSEQAIINL LRVNWNVIGY IELSTLGEPS
LPAIRVYDFT SSMNTRSVTQ GPNVQIRTRS NAIDVHVREF IRFGRYLPLE IPKCRVPRLV
SLQVINYSLN HLLSVTPWPD QYDVTRHRPE RIIENSVKRT IQYQEYDPSV GTWATSSDMT
NYTHIPSDSY YHQFIVTCLR SFCGLRDLPR ENSARYPYVV LLYGLALGHE IAPSRMGLTY
AMTSHMISYV LSTITTGIDV APSEIISRFK LFLIDVPFAD TIIHDLRKVT PNVNVHSTSI
FTSNERGDAR ILTGWVVIRI AVSRFEQQKR SFEYMSYFND ILRFCDGGII HFDIPDATFL
MHVVTSLQCT PNRRVKVLSY FASQSPFSLT LHFYRDTTDP LLPVANIGHW VTRHQMKRYA
YTDRDSTIPL RHEVIPALST VMSRMTAEYS FVCQKSDLPV CLSALSTISN YARVATWTDY
RGIAHWSGSA VIDPLRLLDS SRTGVLATNV PIEPLIAPSH GVPRLERSTY RVVDAFHLCS
LIGPIFIQRE FNIWTASRTS ERTRHVIDVG GRDGAFRGLF PHAMYTVIDP APAPQHMISN
YISEPWDFND FQGSLDRIMD TLGIIDPQDV FLVFSHVFIS ALNRPAAHVN ALEQLGALQC
SSVVSTQTSG SSASTLYSSY VNHNPFLEIR MENAAYLTRT YPSPYPLPTR AEMNEAILNN
ARSRLHQTSA AEILDLAMRF GYAPSYEAIV TLPALCDQHV VYAIQ
