VP3_ROTBS
ID VP3_ROTBS Reviewed; 695 AA.
AC Q65526;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 54.
DE RecName: Full=Protein VP3 {ECO:0000255|HAMAP-Rule:MF_04124};
DE Includes:
DE RecName: Full=mRNA guanylyltransferase {ECO:0000255|HAMAP-Rule:MF_04124};
DE EC=2.7.7.50 {ECO:0000255|HAMAP-Rule:MF_04124};
DE Includes:
DE RecName: Full=mRNA (guanine-N(7))-methyltransferase {ECO:0000255|HAMAP-Rule:MF_04124};
DE EC=2.1.1.56 {ECO:0000255|HAMAP-Rule:MF_04124};
OS Rotavirus C (isolate RVC/Cow/Japan/Shintoku/1991/G2P[3]) (RV-C).
OC Viruses; Riboviria; Orthornavirae; Duplornaviricota; Resentoviricetes;
OC Reovirales; Reoviridae; Sedoreovirinae; Rotavirus.
OX NCBI_TaxID=33723;
OH NCBI_TaxID=9913; Bos taurus (Bovine).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Jiang B., Gentsch J.R., Tsunemitsu H., Saif L.J., Glass R.I.;
RT "Sequence analysis of VP3 and VP4 genes of a bovine group C rotavirus:
RT molecular evidence for a new P type.";
RL Submitted (MAY-1995) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Multifunctional enzyme involved in mRNA capping. Catalyzes
CC the formation of the 5' cap structure on the viral plus-strand
CC transcripts. Specifically binds to GTP and displays guanylyltransferase
CC and methyltransferase activities. Has affinity for ssRNA but not for
CC dsRNA. Capping activity is non-specific and caps RNAs that initiate
CC with either a G or an A residue. Together with VP1 polymerase, forms a
CC VP1-VP3 complex positioned near the channels situated at each of the
CC five-fold vertices of the core. Following infection, the outermost
CC layer of the virus is lost, leaving a double-layered particle (DLP)
CC made up of the core and VP6 shell. VP1 then catalyzes the transcription
CC of fully conservative plus-strand genomic RNAs that are capped by VP3
CC and extruded through the DLP's channels into the cytoplasm where they
CC function as mRNAs for translation of viral proteins. DLPs probably have
CC an RNA triphosphatase activity as well, whereas open cores do not.
CC {ECO:0000255|HAMAP-Rule:MF_04124}.
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 Evidence={ECO:0000255|HAMAP-Rule:MF_04124};
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; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_04124};
CC -!- SUBUNIT: Interacts with VP1. Interacts with VP2. {ECO:0000255|HAMAP-
CC Rule:MF_04124}.
CC -!- SUBCELLULAR LOCATION: Virion {ECO:0000255|HAMAP-Rule:MF_04124}.
CC Note=Attached inside the inner capsid as a minor component. There are
CC about 11 to 12 copies per virion. {ECO:0000255|HAMAP-Rule:MF_04124}.
CC -!- SIMILARITY: Belongs to the rotavirus VP3 family. {ECO:0000255|HAMAP-
CC Rule:MF_04124}.
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DR EMBL; U26552; AAB01673.1; -; Genomic_DNA.
DR SMR; Q65526; -.
DR GO; GO:0019013; C:viral nucleocapsid; IEA:UniProtKB-UniRule.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004482; F:mRNA (guanine-N7-)-methyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0004484; F:mRNA guanylyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016032; P:viral process; IEA:UniProtKB-UniRule.
DR HAMAP; MF_04124; Rota_VP3; 1.
DR InterPro; IPR011181; VP3_Rotav.
DR Pfam; PF06929; Rotavirus_VP3; 1.
DR PIRSF; PIRSF004015; LigT_rotavirus; 1.
DR PROSITE; PS51589; SAM_MT56_VP3; 1.
PE 3: Inferred from homology;
KW GTP-binding; Host-virus interaction; Methyltransferase; mRNA capping;
KW mRNA processing; Multifunctional enzyme; Nucleotide-binding;
KW Nucleotidyltransferase; RNA-binding; S-adenosyl-L-methionine; Transferase;
KW Viral immunoevasion; Virion.
FT CHAIN 1..695
FT /note="Protein VP3"
FT /id="PRO_0000369871"
FT REGION 187..255
FT /note="N7-methyltransferase activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04124"
FT REGION 256..432
FT /note="2'-O-methyltransferase activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04124"
FT REGION 433..559
FT /note="N7-methyltransferase activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04124"
FT REGION 560..695
FT /note="GTase/RTPase activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04124"
SQ SEQUENCE 695 AA; 81517 MW; 1EF9F1ECFFAD3328 CRC64;
MRVLGLFERG NNLNFADTYV YTWNKQYSFH ENAFLISNQV ATTIIIYLDK EIVNQVNEAF
NLLNSNGIPA LIIKSDHIGI FTSSNFTYDW QNKIIYFHEY TYYKNNEFIV SDEFWLNTSI
QDLLPYKVLF FERGLRKLYE GEEYILYNTA TDDDIIYKYI YEKDVIMSGN DYSKLYDTKS
FKNFVHFMRL LRMRFAVPFD QLSNRVTRSR AFAKSKIHIG LRNESIPQAL DNIHHYWINY
SANGMRVSEL KGSGSYSEKK ISEFDIGQFK NYMNFLTLMF YIKNMKKKPS CTIIGAAPGY
WIPSMKKYFN IVTYDDKHVD STEHYNRYFT DDDIASVKTN GVYIDVRSDF KNYDWKKRRQ
LVEEETMRWL SITYKLLENR YVEAVLLKMT AMDIEIPDGY FVHFPTTYRK SEYYLLVDKQ
TVKRPKIKIT KSLAYGAINT IFSDNVFISG KYSLKGKTEG VLALYCLSNT INPKEKVVQY
ANSFSGTCMT VRLNNTYILN KIIDFKTNAD YTFLPSDFQC SIKTVLTSYR GYAGVFGYAI
TKDLKSDGNN HIYIIPNARD DDNFDTFASH LGLSRYSHSK RFSESATTMS GYLFRDMVSG
KENMEDTDTE NLASGHVFNA IAHYRFDYTY DIVGWLKLHK MRKFRVKSNI YGEHTDDEIR
NAIEAAYVYY LLDGDEVGKE YAKRIMEIWD VQTWG
