ID   RDRP_ROTPG              Reviewed;        1088 AA.
AC   P17699;
DT   01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1990, sequence version 1.
DT   22-FEB-2023, entry version 90.
DE   RecName: Full=RNA-directed RNA polymerase;
DE            EC=2.7.7.48;
DE   AltName: Full=Protein VP1;
OS   Rotavirus A (strain RVA/Pig/United States/Gottfried/1983/G4P2B[6]) (RV-A).
OC   Viruses; Riboviria; Orthornavirae; Duplornaviricota; Resentoviricetes;
OC   Reovirales; Sedoreoviridae; Rotavirus; Rotavirus A.
OX   NCBI_TaxID=10917;
OH   NCBI_TaxID=9823; Sus scrofa (Pig).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=2556853; DOI=10.1016/0042-6822(89)90590-4;
RA   Fukuhara N., Nishikawa K., Gorziglia M., Kapikian A.Z.;
RT   "Nucleotide sequence of gene segment 1 of a porcine rotavirus strain.";
RL   Virology 173:743-749(1989).
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; M32805; AAA43833.1; -; Genomic_RNA.
DR   PIR; A33749; P1XRPR.
DR   SMR; P17699; -.
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_0000149528"
FT   DOMAIN          501..687
FT                   /note="RdRp catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
SQ   SEQUENCE   1088 AA;  124955 MW;  7B21BB4E55B0C52E CRC64;
     MGKYNLILSE YLSFVYNSQS AVQIPIYYSS NPELEKRCID FHAKCVDNSK KGLSLKPLFE
     EYKDVIDNAT LLSILSYSYD KYNAVERKLV NYAKGKPLEA DLTANELDYE NNKITSELFQ
     SAKEYTYSLM DPAILTSLSS NLNAVMFWLE RHSNDVADAN KIYKRRLDLF TIVASTINKY
     GVPRHNEKYR YEYEVMKDKP YYLVTWANSA IEMLMSVFSH EDYLIAKELM VLSCSNRSTL
     AKLVSSPMSI LVALIDINGT FITNEEFDLE FSDKYVRAIV PDQTFDELQE MIDNMKKAGL
     VDIPRMIQEW LVDCSLEKFT LMSKIYSWSF HVGFRKQKMI DAALDQLKTE YTEDVDNEMY
     NEYTMLIRDE IVKMLEVPVK HDDHLLRNSE LAGLLSMSSA SNGASRQLKF GRKTIFSTKK
     NMHVMDDIAR GRYTPGVIPP VNVDRPIPLG RRDVPGRRTR IIFILPYEYF IAQHAVVEKM
     LSYAKHTREY AEFYSQSNQL LSYGDVTRFL SSNSMVLYTD VSQWDSSQHN TQPFRKGIIM
     GLDMLANMTN DPKVVQTLNL YKQTQINLMD SYVQIPDGDV IKKIQYGAVA SGEKQTKAAN
     SIANLALIKT VLSRIANKYS FITKIIRVDG DDNYAVLQFN TDVTKQMVQE VSNDVRYIYS
     RMNAKVKALV STVGIEIAKR YIAGGKIFFR AGINLLNNEK RGQSTQWDQA AILYSNYIVN
     KLRGFETDRE FILTKIIQMT SVAITGSLRL FPSERVLTTN STFKVFDSED FIIEYGTTDD
     EVYIQRAFMS LSSQKSGIAD EIASSQTFKN YVSKLSDQLL VSKNAIVSKG IAVTEKAKLN
     SYAPVYLEKR RAQISALLTM LQKPVSFKSN KITINDILRD IKPFFVTTEA SLPIQYRKFM
     PTLPDNVQYV IQCIGSRTYQ IEDSGSKSSI SKLISKYSVY KPSIEELYRV ISLREQEIQL
     YLVSLGVPPV DASTYVGSRI YSQDKYKILE SYVYNLLSIN YGCYQLFDFN SPDLEKLIRI
     PFKGKIPAVT FILHLYAKLE IINYAIKNKS WISLFCNYPK SEMIKLWKKM WNITAFRSPY
     TSANFFED
//