ID   RDRP_ROTSH              Reviewed;        1088 AA.
AC   A2T3S0;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   15-JAN-2008, sequence version 1.
DT   29-SEP-2021, entry version 45.
DE   RecName: Full=RNA-directed RNA polymerase;
DE            EC=2.7.7.48;
DE   AltName: Full=Protein VP1;
OS   Rotavirus A (isolate RVA/Monkey/South Africa/SA11-H96/1958/G3P5B[2]) (RV-A)
OS   (Simian Agent 11 (isolate SI/South Africa/H96/58)).
OC   Viruses; Riboviria; Orthornavirae; Duplornaviricota; Resentoviricetes;
OC   Reovirales; Reoviridae; Sedoreovirinae; Rotavirus; Rotavirus A.
OX   NCBI_TaxID=450149;
OH   NCBI_TaxID=60710; Chlorocebus pygerythrus (Vervet monkey) (Cercopithecus pygerythrus).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=17059839; DOI=10.1016/j.virol.2006.09.024;
RA   Small C., Barro M., Brown T.L., Patton J.T.;
RT   "Genome heterogeneity of SA11 rotavirus due to reassortment with 'O'
RT   agent.";
RL   Virology 359:415-424(2007).
RN   [2]
RP   INTERACTION WITH NSP2, INTERACTION WITH NSP5, AND SUBCELLULAR LOCATION.
RX   PubMed=17182692; DOI=10.1128/jvi.01494-06;
RA   Arnoldi F., Campagna M., Eichwald C., Desselberger U., Burrone O.R.;
RT   "Interaction of rotavirus polymerase VP1 with nonstructural protein NSP5 is
RT   stronger than that with NSP2.";
RL   J. Virol. 81:2128-2137(2007).
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.
CC       {ECO:0000269|PubMed:17182692, ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: Virion {ECO:0000305}. Note=Attached inside the
CC       inner capsid as a minor component (By similarity). Also found in
CC       spherical cytoplasmic structures, called virus factories, that appear
CC       early after infection and are the site of viral replication and
CC       packaging. {ECO:0000250, ECO:0000269|PubMed:17182692}.
CC   -!- SIMILARITY: Belongs to the reoviridae RNA-directed RNA polymerase
CC       family. {ECO:0000305}.
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DR   EMBL; DQ838640; ABG75819.1; -; Genomic_RNA.
DR   RefSeq; YP_002302227.1; NC_011507.2.
DR   SMR; A2T3S0; -.
DR   GeneID; 7011368; -.
DR   KEGG; vg:7011368; -.
DR   Proteomes; UP000001119; Genome.
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-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006351; P:transcription, DNA-templated; IEA:InterPro.
DR   GO; GO:0019079; P:viral genome replication; IEA:InterPro.
DR   Gene3D; 1.10.10.1990; -; 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; SSF56672; 1.
DR   PROSITE; PS50523; RDRP_DSRNA_REO; 1.
PE   1: Evidence at protein level;
KW   Magnesium; Nucleotide-binding; Nucleotidyltransferase; Reference proteome;
KW   RNA-binding; RNA-directed RNA polymerase; Transferase;
KW   Viral RNA replication; Virion.
FT   CHAIN           1..1088
FT                   /note="RNA-directed RNA polymerase"
FT                   /id="PRO_0000367811"
FT   DOMAIN          501..687
FT                   /note="RdRp catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
SQ   SEQUENCE   1088 AA;  125208 MW;  3C90CD5B59EF2D60 CRC64;
     MGKYNLILSE YLSFIYNSQS AVQIPIYYSS NSELENRCIE FHSKCLENSK NGLSLRKLFV
     EYNDVIENAT LLSILSYSYD KYNAVERKLV KYAKGKPLEA DLTVNELDYE NNKITSELFP
     TAEEYTDSLM DPAILTSLSS NLNAVMFWLE KHENDVAEKL KVYKRRLDLF TIVASTINKY
     GVPRHNAKYR YEYDVMKDKP YYLVTWANSS IEMLMSVFSH DDYLIAKELI VLSYSNRSTL
     AKLVSSPMSI LVALVDINGT FITNEELELE FSNKYVRAIV PDQTFDELNQ MLDNMRKAGL
     VDIPKMIQDW LVDRSIEKFP LMAKIYSWSF HVGFRKQKML DAALDQLKTE YTENVDDEMY
     REYTMLIRDE VVKMLEEPVK HDDHLLRDSE LAGLLSMSSA SNGESRQLKF GRKTIFSTKK
     NMHVMDDMAN ERYTPGIIPP VNVDKPIPLG RRDVPGRRTR IIFILPYEYF IAQHAVVEKM
     LIYAKHTREY AEFYSQSNQL LSYGDVTRFL SNNTMVLYTD VSQWDSSQHN TQPFRKGIIM
     GLDILANMTN DAKVLQTLNL YKQTQINLMD SYVQIPDGNV IKKIQYGAVA SGEKQTKAAN
     SIANLALIKT VLSRISNKHS FATKIIRVDG DDNYAVLQFN TEVTKQMIQD VSNDVRETYA
     RMNAKVKALV STVGIEIAKR YIAGGKIFFR AGINLLNNEK RGQSTQWDQA AILYSNYIVN
     RLRGFETDRE FILTKIMQMT SVAITGSLRL FPSERVLTTN STFKVFDSED FIIEYGTTDD
     EVYIQRAFMS LSSQKSGIAD EIAASSTFKN YVTRLSEQLL FSKNNIVSRG IALTEKAKLN
     SYAPISLEKR RAQISALLTM LQKPVTFKSS KITINDILRD IKPFFTVSDA HLPIQYQKFM
     PTLPDNVQYI IQCIGSRTYQ IEDDGSKSAI SRLISKYSVY KPSIEELYKV ISLHENEIQL
     YLISLGIPKI DADTYVGSKI YSQDKYRILE SYVYNLLSIN YGCYQLFDFN SPDLEKLIRI
     PFKGKIPAVT FILHLYAKLE VINYAIKNGS WISLFCNYPK SEMIKLWKKM WNITSLRSPY
     TNANFFQD