ID   RDRP_ROTHS              Reviewed;        1088 AA.
AC   A7J390; Q9QAU6; Q9QRZ8;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 1.
DT   29-SEP-2021, entry version 49.
DE   RecName: Full=RNA-directed RNA polymerase;
DE            EC=2.7.7.48;
DE   AltName: Full=Protein VP1;
OS   Rotavirus A (strain RVA/Human/Japan/S2/1980/G2P1B[4]) (RV-A).
OC   Viruses; Riboviria; Orthornavirae; Duplornaviricota; Resentoviricetes;
OC   Reovirales; Reoviridae; Sedoreovirinae; Rotavirus; Rotavirus A.
OX   NCBI_TaxID=10959;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=18216098; DOI=10.1128/jvi.02257-07;
RA   Matthijnssens J., Ciarlet M., Heiman E.M., Arijs I., Delbeke T.,
RA   McDonald S.M., Palombo E.A., Iturriza-Gomara M., Maes P., Patton J.T.,
RA   Rahman M., Van Ranst M.;
RT   "Full genome-based classification of rotaviruses reveals a common origin
RT   between human Wa-Like and porcine rotavirus strains and human DS-1-like and
RT   bovine rotavirus strains.";
RL   J. Virol. 82:3204-3219(2008).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 8-178.
RA   Lee C.N., Zao C.L.;
RL   Submitted (JAN-1998) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 10-150.
RX   PubMed=10374958; DOI=10.1099/0022-1317-80-6-1407;
RA   Zao C.L., Yu W.N., Kao C.L., Taniguchi K., Lee C.Y., Lee C.N.;
RT   "Sequence analysis of VP1 and VP7 genes suggests occurrence of a
RT   reassortant of G2 rotavirus responsible for an epidemic of
RT   gastroenteritis.";
RL   J. Gen. Virol. 80:1407-1415(1999).
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}.
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DR   EMBL; DQ870485; ABI60844.1; -; Genomic_RNA.
DR   EMBL; AF044361; AAF19588.1; -; Genomic_RNA.
DR   EMBL; AF106303; AAD47317.1; -; Genomic_RNA.
DR   SMR; A7J390; -.
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   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_0000368041"
FT   DOMAIN          501..687
FT                   /note="RdRp catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT   CONFLICT        146
FT                   /note="M -> W (in Ref. 3; AAD47317)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1088 AA;  125083 MW;  489F6E8F6D08A246 CRC64;
     MGKYNLILSE YLSFIYNSQS AVQIPIYYSS NSELENRCIE FHAKCLENSK NGLSLKKLFS
     EYSDVIQNAT LLSILSYSYD KYNAVERKLV KYARSKPLEA DLTVNELDYE NNKITSELFP
     TEEEYTDSLM DPAILTSLSS NLNAVMFWLE KHENDTAEKL KIYKRRLDLF IIVASTVNKY
     GVPRHNAKYR YEYDVMKDKP YYLVTWANSS IEMLMSVFSH EDYLIAKELI VLSYSNRSTL
     AKLVSSPMSI LVALVDINGT FITNEELELE FSNKYVRAIV PDQTFDELKQ MLDNMRKAGL
     VDIPKMIQDW LIDCSIEKFS LMAKIYSWSF HVGFRKQKML DAALDQLKTE YTEDVDDEMY
     REYTMLIRDE VVKMLEESVK HDDHLLQDSE LAGLLSMSSA SNGESRQLKF GRKTIFSTKK
     NMHVMDDMAN GRYTPGIIPP VNADKPIPLG RRDVPGRRTR IIFILPYEYF IAQHAVVEKM
     LIYAKHTREY AEFYSQSNQL LSYGDVTRFL SNNAMVLYTD VSQWDSSQHN TQPFRKGIIM
     GLDILANMTN DAKVVQTLNL YKQTQINLMD SYVQIPDGNV IKKIQYGAVA SGEKQTKAAN
     SIANLALIKT VLSRISNKYS FATKIIRVDG DDNYAVLQFN TEVTKQMVQD VSNDVRETYA
     RMNAKVKALV STVGIEIAKR YIAGGKIFFR AGINLLNNEK RGQSTQWDQA AVLYSNYIVN
     RLRGFETDRE FILTKIMQMT SVAITGSLRL FPSERVLTTN STFKVFDSED FIIEYGTTDD
     EVYIQRAFMS LSSQKSGIAD EISASSTFKN YVSKLSEQLL FSKNNIVSRG IALTEKAKLN
     SYAPISLEKR RAQISALLTM LQKPVTFKSN KITINDILKD IKPFFTLSEA HLPMQYQKFM
     PTLPENVQYI IQCIGSRTYQ IEDDGSKSAI SRLISKYSVY KPSIEELYKV ISLHENEIQL
     YLISLGIPKI DADTYVGSKI YSQDKYRILE SYVYNLLSIN YGCYQLFDFN SPDLEKLIRI
     PFKGKIPAVT FILHLYAKLE VINYAIKNGS WISLFCNYPK SEMIKLWKKM WNITSLRSPY
     TNANFFQD