ID   RDRP_ROTHP              Reviewed;        1088 AA.
AC   B1NKS9; Q9QAT9; Q9QRY2;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   29-APR-2008, sequence version 1.
DT   03-AUG-2022, entry version 42.
DE   RecName: Full=RNA-directed RNA polymerase;
DE            EC=2.7.7.48;
DE   AltName: Full=Protein VP1;
OS   Rotavirus A (strain RVA/Human/United States/P/1974/G3P1A[8]) (RV-A).
OC   Viruses; Riboviria; Orthornavirae; Duplornaviricota; Resentoviricetes;
OC   Reovirales; Reoviridae; Sedoreovirinae; Rotavirus; Rotavirus A.
OX   NCBI_TaxID=10957;
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 10-151.
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; EF583037; ABU87846.1; -; Genomic_RNA.
DR   EMBL; AF044368; AAF19595.1; -; Genomic_RNA.
DR   EMBL; AF106319; AAD47333.1; -; Genomic_RNA.
DR   SMR; B1NKS9; -.
DR   PRIDE; B1NKS9; -.
DR   Proteomes; UP000007047; 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   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_0000368046"
FT   DOMAIN          501..687
FT                   /note="RdRp catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT   CONFLICT        37
FT                   /note="R -> G (in Ref. 2; AAF19595 and 3; AAD47333)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1088 AA;  124811 MW;  27EFAB279B6CA9C1 CRC64;
     MGKYNLVLSE YLSFVYNSQS AVQIPIYYSS NSELEKRCIE FHAKCVDSSK KGLSLKPLFE
     EYKDVIDNAT LLSILSYSYD KYNAVERKLV NYAKGKPLEA DLTANELDYE NNKITSELFQ
     SAEEYTDSLM DPAILTSLSS NLNAVMFWLE RHSNDVADAN KIYKRRLDLF TIVASTVNKY
     GVPRHNEKYR YEYEVMKDKP YYLVTWANSS IEMLMSVFSH EDYLIAKELI ILSYSNRSTL
     AKLVSSPMSI LVALIDINGT FITNEELELE FSDKYVKAIV PDQIFDELQE MIDNMRKVGL
     VDIPKMIQEW LVDCSLEKFT LMSKIYSWSF HVGFRKQKMI DAALDQLKTE YTEDVDGEMY
     NEYTMLIRDE IVKMLEVPVK HDDHLLRDSE LAGLLSMSSA SNGESRQLKF GRKTIFSTKK
     NMHVMDDIAH GRYTPGVIPP VNVDRPIPLG RRDVPGRRTR IIFILPYEYF IAQHAVVEKM
     LLYAKHTREY AEFYSQSNQL LSYGDVTRFL SSNSMVLYTD VSQWDSSQHN TQPFRKGIIM
     GLDMLSNMTN DPKVAQTLNL YKQTQINLMD SYVQIPDGNV IKKIQYGAVA SGEKQTKAAN
     SIANLALIKM VLSRIANKYS FITKIIRVDG DDNYAVLQFN TDVTKQMVQD VSNDVRYIYS
     RMNAKVKALV STVGIEIAKR YIAGGKIFFR AGINLLNNEK RGQSTQWDQA AILYSNYIVN
     KLRGFETDRE FILTKIIQMT SVAITGSLRL FPSERVLTTN STFKVFDSED FIIEYGTTDD
     EVYIQRAFMS LSSQKSGIAD EIASSQTFKN YVNKLSDQLL VSKNVIVSKG IAVTEKAKLN
     SYAPVYLEKR RAQISALLTM LQKPVSFKSN KITINDILRD IKPFFVTSEA NLSIQYRKFM
     PTLPDNVQYV IQCIGSRTYQ IEDSGSKSSI SKLISKYSVY KPSIEELYKV ISLREQEIQL
     YLVSLGVPPV DAGTYVGSRI YSQDKYKILE SYVYNLLSIN YGCYQLFDFN SPDLEKLIRI
     PFKGKIPAVT FILHLYAKLE IINYAIKNGA WISLFCNYPK SEMIKLWKKM WNITALRSPY
     TSANFFQD