VP3_ROTPC
ID VP3_ROTPC Reviewed; 692 AA.
AC P26192;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1992, sequence version 1.
DT 03-AUG-2022, entry version 69.
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 (strain RVC/Pig/United States/Cowden/1980) (RV-C).
OC Viruses; Riboviria; Orthornavirae; Duplornaviricota; Resentoviricetes;
OC Reovirales; Reoviridae; Sedoreovirinae; Rotavirus.
OX NCBI_TaxID=10916;
OH NCBI_TaxID=9823; Sus scrofa (Pig).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1310192; DOI=10.1016/0042-6822(92)90035-n;
RA Bremont M., Juste-Lesage P., Chabanne-Vautherot D., Charpilienne A.,
RA Cohen J.;
RT "Sequences of the four larger proteins of a porcine group C rotavirus and
RT comparison with the equivalent group A rotavirus proteins.";
RL Virology 186:684-692(1992).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; M74219; AAA99239.1; -; Genomic_DNA.
DR PIR; C40822; P3XRPC.
DR SMR; P26192; -.
DR Proteomes; UP000008175; Genome.
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 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; Reference proteome; RNA-binding;
KW S-adenosyl-L-methionine; Transferase; Viral immunoevasion; Virion.
FT CHAIN 1..692
FT /note="Protein VP3"
FT /id="PRO_0000149536"
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..558
FT /note="N7-methyltransferase activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04124"
FT REGION 559..692
FT /note="GTase/RTPase activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04124"
SQ SEQUENCE 692 AA; 81378 MW; D679352CF22FE7DE CRC64;
MRVLGLFERG NNLNFADTYI YTWNKQYSYH ENAFLISNQV ATTIIIYLSD TIVNEVDKAF
TLLNSNGIPA LVIRKDHIGI FTSSNFTYDW QHKIVYFHEY TYYKNNEFIV SDEFWLHTNI
HELLPYKLLY YERGMRKLYD GEEYTLYNTA TDDDILYKYI YEKDAIMSGD DYSELYDDKN
FRNFVHFMRL LRMRFAVPFD QLSNRVTRSR AFFKSKIHIG LRNESIPQAL DNINSQWINY
SANGIMISEL KGSGSYSEKR ISEFDIGQFK NYMNFLTLMF YIKNMKKRPS CTIIGAAPGY
WIPSMKRYFT IITYDDKIVD STEHHNRYFS EEDITKVRTN GVYIDVRSDF DKSDWKKRRQ
LVEEETKRWL EISYRLLEGK YVEAVLLKMT AMDIEIPDGY FVHFPTTYRK SEYYLLIDKQ
IIKKQKVKVT KSLMYNAINT IYSDNVFISG KYTLRGKTEG VVALYCLSNT INQKDKVIQY
ANSFSGTCMT VRLNNTYEVN KVINLNNADY TFLPSDFVCP VNTVLTSYRG YAGVFGYAIT
KDLKSDGNNH IYIIPNARDE NNFDTFASHL GLSRYSHSKR FSESATTMSG YLFRDMVSGK
EDMGDTDKAN YASGHVFNAI AHYRFDYTYD IVGWLRLHKN KQFRVKSDIY EEHTSDEVRN
AIEAAYTYYL LDGDRVGKEY AKKIMEIWEA QV
