ID RDRP_ROTTU Reviewed; 1088 AA. AC B3F2X5; DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot. DT 22-JUL-2008, sequence version 1. DT 22-FEB-2023, entry version 43. DE RecName: Full=RNA-directed RNA polymerase; DE EC=2.7.7.48; DE AltName: Full=Protein VP1; OS Rotavirus A (isolate RVA/Monkey/United States/TUCH/2003/G3P[24]) (RV-A). OC Viruses; Riboviria; Orthornavirae; Duplornaviricota; Resentoviricetes; OC Reovirales; Sedoreoviridae; Rotavirus; Rotavirus A. OX NCBI_TaxID=444186; OH NCBI_TaxID=9544; Macaca mulatta (Rhesus macaque). RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC RNA]. RA Brown T.L., Yang H., Patton J.T.; RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: RNA-directed RNA polymerase that is involved in both CC transcription and genome replication. Together with VP3 capping enzyme, CC forms an enzyme complex positioned near the channels situated at each CC of the five-fold vertices of the core. Following infection, the CC outermost layer of the virus is lost, leaving a double-layered particle CC (DLP) made up of the core and VP6 shell. VP1 then catalyzes the CC transcription of fully conservative plus-strand genomic RNAs that are CC extruded through the DLP's channels into the cytoplasm where they CC function as mRNAs for translation of viral proteins. One copy of each CC of the viral (+)RNAs is also recruited during core assembly, together CC with newly synthesized polymerase complexes and VP2. The polymerase of CC these novo-formed particles catalyzes the synthesis of complementary CC minus-strands leading to dsRNA formation. To do so, the polymerase CC specifically recognizes and binds 4 bases 5'-UGUG-3' in the conserved CC 3'-sequence of plus-strand RNA templates. VP2 presumably activates the CC autoinhibited VP1-RNA complex to coordinate packaging and genome CC replication. Once dsRNA synthesis is complete, the polymerase switches CC to the transcriptional mode, thus providing secondary transcription (By CC similarity). {ECO:0000255|PROSITE-ProRule:PRU00539}. CC -!- CATALYTIC ACTIVITY: CC Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + CC RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:14527, Rhea:RHEA- CC COMP:17342, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:140395; CC EC=2.7.7.48; Evidence={ECO:0000255|PROSITE-ProRule:PRU00539}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000305}; CC -!- SUBUNIT: Interacts with VP3 (Potential). Interacts with VP2; this CC interaction activates VP1. Interacts with NSP5; this interaction is CC probably necessary for the formation of functional virus factories. CC Interacts with NSP2; this interaction is weak (By similarity). CC {ECO:0000250, ECO:0000305}. CC -!- SUBCELLULAR LOCATION: Virion {ECO:0000305}. Note=Attached inside the CC inner capsid as a minor component. Also found in spherical cytoplasmic CC structures, called virus factories, that appear early after infection CC and are the site of viral replication and packaging (By similarity). CC {ECO:0000250}. CC -!- SIMILARITY: Belongs to the reoviridae RNA-directed RNA polymerase CC family. {ECO:0000305}. 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; EF583010; ABQ59572.1; -; Genomic_RNA. DR SMR; B3F2X5; -. DR GO; GO:0044423; C:virion component; IEA:UniProtKB-KW. DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW. DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW. DR GO; GO:0003968; F:RNA-dependent RNA polymerase activity; IEA:UniProtKB-KW. DR GO; GO:0006351; P:DNA-templated transcription; IEA:InterPro. DR GO; GO:0019079; P:viral genome replication; IEA:InterPro. DR Gene3D; 1.10.357.80; -; 2. DR Gene3D; 1.20.120.1390; -; 1. DR Gene3D; 3.30.230.140; -; 2. DR Gene3D; 3.30.70.2480; -; 1. DR Gene3D; 1.10.10.1990; Viral RNA-directed RNA polymerase, 4-helical domain; 1. DR InterPro; IPR043502; DNA/RNA_pol_sf. DR InterPro; IPR042032; RNA-dir_pol_4-hel_dom. DR InterPro; IPR001795; RNA-dir_pol_luteovirus. DR InterPro; IPR007097; RNA-dir_pol_reovirus. DR InterPro; IPR022071; Rotavirus_VP1_C. DR Pfam; PF02123; RdRP_4; 1. DR Pfam; PF12289; Rotavirus_VP1; 1. DR SUPFAM; SSF56672; DNA/RNA polymerases; 1. DR PROSITE; PS50523; RDRP_DSRNA_REO; 1. PE 3: Inferred from homology; KW Magnesium; Nucleotide-binding; Nucleotidyltransferase; RNA-binding; KW RNA-directed RNA polymerase; Transferase; Viral RNA replication; Virion. FT CHAIN 1..1088 FT /note="RNA-directed RNA polymerase" FT /id="PRO_0000368035" FT DOMAIN 501..687 FT /note="RdRp catalytic" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00539" SQ SEQUENCE 1088 AA; 124828 MW; 77C2821765BA15CC CRC64; MGKYNLILSE YLSFIYNSQS AVQIPIYYSS NSDLEKRCIE FHSKCLENSK KGLSLKNIFV EYKDVVENAT LLSILSYSYD KYNAVERKLV YYAKGKPLEA DLSANKLDYE NNKLTSDLFP TAEEYTDSLM DPAILTSLSS NLNAVMFWLE KHANDTAEKA KIYKRRLDLF TIVASTVNKY GVPRHNAKYR YEYEVMKDKP YYLVTWANSS IEMLMSVFSH EDYLIAKELI VLSYSNRSTL AKLVSSPMSI LVALVDINGT FITNEELELE FSNKYVKAIV PDQTFEELKE MLDNMKKAGL VDIPKMIQDW LVDCSIEKFP LMAKIYSWSF HVGFRKQKML DAALDQLKTE YTEDVDDEMY REYTMLIRDE VVKMLEEAVK HDDHLLQDSE LAGLLSMSSA SNGESRQLKF GRKTIFSTKK NMHVMDDMAN GRYTPGVIPP VNVDKPIPLG RRDVPGRRTR IIFILPYEYF IAQHAVVEKM LLYAKHTREY AEFYSQSNQL LSYGDVTRFL SNNAMVLYTD VSQWDSSQHN TQPFRKGIIM GLDILANMTN DAKVIQTLHL YKQTQINLMD SYVQIPDGNV IKKIQYGAVA SGEKQTKAAN SIANLALIKT VLSRIANKYS FVTKIIRVDG DDNYAVLQFN TEVTKQMVQD VSNDVRDTYA RMNAKVKALV STVGIEIAKR YIAGGKIFFR AGINLLNNEK RGQSTQWDQA AVLYSNYIVN RLRGFETDRE FILTKIMQMT SVAITGSLRL FPSERVLTTN STFKVFDSED FIIEYGTTDD EVYIQRAFMS LSSQKSGIAD EIAASQTFKN YVSKLSDQLL VSKNTIVSRG IALTEKAKLN SYAPISLEKR RAQISALLTM LQKPVTFKSN KITINDILHD IKPYFVTSEA NLPMQYQKFM PTLPNNVQYI IQCIGSRTYQ IEDDGSKSAI SKLISKYSVY RPSIEELYKV ISLHEQEIQL YLVSLGIPKI DADTYVGSKI YSQDKYRILE SYVYNLLSIN YGCYQLFDFN SPDLEKLIRI PFKGKIPAVT FILHLYAKLE IINYAIKNGS WISLFCNYPK SEMIKLWKKM WNITSLRSPY TNANFFQD //