RDRP_ROTBU
ID RDRP_ROTBU Reviewed; 1088 AA.
AC P21615;
DT 01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1991, sequence version 1.
DT 29-SEP-2021, entry version 88.
DE RecName: Full=RNA-directed RNA polymerase;
DE EC=2.7.7.48;
DE AltName: Full=Protein VP1;
OS Rotavirus A (strain RVA/Cow/United Kingdom/UK/1975/G6P7[5]) (RV-A).
OC Viruses; Riboviria; Orthornavirae; Duplornaviricota; Resentoviricetes;
OC Reovirales; Reoviridae; Sedoreovirinae; Rotavirus; Rotavirus A.
OX NCBI_TaxID=10934;
OH NCBI_TaxID=9913; Bos taurus (Bovine).
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2175888; DOI=10.1093/nar/18.23.7150;
RA Tarlow O., McCrae M.A.;
RT "Nucleotide sequence of gene 1 of the UK tissue culture adapted strain of
RT bovine rotavirus.";
RL Nucleic Acids Res. 18:7150-7150(1990).
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; X55444; CAA39085.1; -; mRNA.
DR SMR; P21615; -.
DR Proteomes; UP000008657; 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 2: Evidence at transcript level;
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_0000149526"
FT DOMAIN 501..687
FT /note="RdRp catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
SQ SEQUENCE 1088 AA; 125003 MW; 1A50AA359AE337FC CRC64;
MGKYNLILSE YLSFIYNSQS AVQIPIYYSS NSELEDRCIE FHSKCLENSK NGRSLKKLFT
EYSDVIENAT LLSILSYSYD KYNAVERKLV KYAKGKPLEA GLTVNELDYE NNKITSELFP
TAEEYTDSLM DPAILTSLSS NLNAVMFWLE KHENDVAEKL KIYKRRLDLF TIVASTVNKY
GVPRHNAKYR YEYEVMKDKP YYLVTWANSS IEMLMSVFSH EDYLIARELI VLSYSNRSTL
AKLVSSPMSI LVALVDINGT FITNEELELE FSNKYVRAIV PDQTFDELKQ MLDNMRKAGL
TDIPKMIQEW LVDCSIEKFP LMAKIYSWSF HVGFRKQKML DAALDQLKTE YTEDVDDEMY
REYTMLIRDE VVKMLEEPVK HDDHLLQDSE LAGLLSMSSA SNGESRQLKF GRKTIFSTKK
NMHVMDDMAN GRYTPGIIPP VNVDKPIPLG RRDVPGRRTR IIFILPYEYF IAQHAVVEKS
VIYAKHTREY AEFYSQSNQL LSYGDVTRFL SNNAMVLYTD VSQWDSSQHN TQPFRKGIIM
GLDMLANMTN DARVIQTLNL YKQTQINLMD SYVQIPDGNV IKKIQYGAVA SGEKQTKAAN
SIANLALIKT VLSRISNKYS FATKIIRVDG DDNYAVLQFN TEVTKQMVQD VSNDVRETYA
RMNAKVKALV STVGIEIAKR YIAGGKIFFR AGINLLNNEK RGQSTQWDQA AVLYSNYIVN
RLRGFETDRE FILTKIMQMT SVAITGSLRL FPSERVLTTN STFKVFDSED FIIEYGTTDD
EVYIQRAFMS LSSQKSGIAD EIAASSTFKN YVSKLSEQLL FSKNNIVSRG IALTEKAKLN
SYAPISLEKR RAQISALLTM LQKPVTFKSS KITINDILRD IKPFFTVSEA HLPIQYQKFM
PTLPDNVQYI IQCIGSRTYQ IEDDGSKSAI SRLISKYSVY KPSIEELYKV ISLHENEIQL
YLISLGIPKI DADTYVGSKI YSQDKYRILE SYVYNLLSIN YGCYQLFDFN SPDLEKLIRI
PFKGKIPAVT FILHLYAKLE VINYAIKNGS WISLFCNYPK SEMIKLWKKM WNITSLRSPY
TNANFFQD
