VP3_ROTHC
ID VP3_ROTHC Reviewed; 693 AA.
AC Q82041;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 67.
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/Human/United Kingdom/Bristol/1989) (RV-C).
OC Viruses; Riboviria; Orthornavirae; Duplornaviricota; Resentoviricetes;
OC Reovirales; Reoviridae; Sedoreovirinae; Rotavirus.
OX NCBI_TaxID=31567;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8972570; DOI=10.1007/bf00568909;
RA Samarbaf-Zadeh A.R., Lambden P.R., Green S.M., Deng Y., Caul E.O.,
RA Clarke I.N.;
RT "The VP3 gene of human group C rotavirus.";
RL Virus Genes 13:169-173(1996).
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; X96697; CAA65469.1; -; mRNA.
DR RefSeq; YP_392516.1; NC_007574.1.
DR SMR; Q82041; -.
DR PRIDE; Q82041; -.
DR GeneID; 3773133; -.
DR KEGG; vg:3773133; -.
DR Proteomes; UP000007664; 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 PIRSF; PIRSF004015; LigT_rotavirus; 1.
DR PROSITE; PS51589; SAM_MT56_VP3; 1.
PE 2: Evidence at transcript level;
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..693
FT /note="Protein VP3"
FT /id="PRO_0000369872"
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..693
FT /note="GTase/RTPase activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04124"
SQ SEQUENCE 693 AA; 81316 MW; BD9AAF4E3533A175 CRC64;
MRVLGLFERG NNLNFADTYV YTWNQQYSYH ENAFLISNQV ATTIILYLDG ININEVNKAF
ELLNSNGIPA LIIKPDHIGI FTSSNFTYDW QYKIVYFHEY TYYKNNEFIV SDEFWLYTNI
NELLPYKILY YERGMRELYA GREYTLYNTA TDDDILYKYI YEKDSIMNGT DYKKLYDTNS
VKNFVHFMRL LRMRFAVPFD QLSNRITRSR VFSKSRIHIG LRNESIPQAL DNIHSQWINY
SANGIVISEL KGLGSYSEKK ISEFGIGQFK NYMNFLTLMF YIKNMKKKPS CTIIGAAPGY
WISSMKKYFT IVTYDNKEVD STEHHNRYFT DDDIVNVKTN GVYIDVRSEF KTNDWRQRRK
LIEEETIKWL EISYKLLENK RVEAILLKMT AMDGEIPDGY CVHSPTTYRK SEYYLLIDKH
IIKRQKIKVT KSLMYNAINT IYSDNVFISG KYSLRGKTEG VLALYCLSNT INQKEKVIQY
ANSFSGTCMT VRLNNTYEVD KIIDFKTNSD HTFLPSDFTC SLNTILTSYR GYAGIFGYAI
TKDLKSNGNN HIYIIPNARD ENNFDTFGSH LGLSRYSHSK RFSESATTMS GYIFRDMVSG
KENMQDTDKD NYASGHVFNA IAHYRFDYTY DIVGWLRLHK TGQFKVKSDI YKEHTDSEIR
NAIESAYVYY LLDGDKVGEK YSKKMMEIWE VQV
