RDRP_ROTPG
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 29-SEP-2021, entry version 87.
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; Reoviridae; Sedoreovirinae; 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: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_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