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 27-MAR-2024, entry version 76. 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; Sedoreoviridae; Rotavirus; Rotavirus C. 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 5'-cap (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:0019049; P:virus-mediated perturbation of host defense response; IEA:UniProtKB-KW. 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; RNA-binding; S-adenosyl-L-methionine; Transferase; KW 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 //