RDRP_ROTPY
ID RDRP_ROTPY Reviewed; 1088 AA.
AC Q85036;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 29-SEP-2021, entry version 63.
DE RecName: Full=RNA-directed RNA polymerase;
DE EC=2.7.7.48;
DE AltName: Full=Protein VP1;
OS Rotavirus A (strain RVA/Pig/Mexico/YM/1983/G11P9[7]) (RV-A).
OC Viruses; Riboviria; Orthornavirae; Duplornaviricota; Resentoviricetes;
OC Reovirales; Reoviridae; Sedoreovirinae; Rotavirus; Rotavirus A.
OX NCBI_TaxID=10919;
OH NCBI_TaxID=9823; Sus scrofa (Pig).
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=7839009; DOI=10.1016/s0923-2516(07)80036-7;
RA Almanza L., Arias C.F., Lopez S.;
RT "Amino acid sequence of the porcine rotavirus YM VP1 protein.";
RL Res. Virol. 145:313-317(1994).
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; X76486; CAA54024.1; -; mRNA.
DR PIR; S39261; S39261.
DR SMR; Q85036; -.
DR PRIDE; Q85036; -.
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_0000368048"
FT DOMAIN 501..687
FT /note="RdRp catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
SQ SEQUENCE 1088 AA; 124793 MW; 73C5723B9EA74357 CRC64;
MGKYNLILSE YLSFVYNSQS AVQIPIYYSS NSELEKRCID FHAKCVDNSK KGLSLSSLFE
EYKDVIDNAT LLSILSYSYD KYNAVERKLI NYAKGKPLEA DLTANELDYE NNKITSELFK
SAEEYTDSLM DPAILTSISS NLNAVMFWLE RHSNDVGDAN KVYRRRLDLF IIVASTINKY
GVPRHNEKYR YEYEVMKDKP YYLVTWANSA IEMLMSVFSH EDYLIAKELI ILSYSNRSTL
AKLVSSPMSI LVALIDINGT FITNEELELE FSDKYVKAIV PDQTFNELQE MIDNMKKAGL
VDIPRMIQEW LVDCSLEKFT LMSKIYSWSF HVGFRKQKMI DAALDQLKTE YTEDVDNEMY
NEYTMLIRDE IVKMLEVPVK HDDHLLRDSE LAGLLSMSSA SNGESRQLKF GRKTIFSTKK
NMHVMDDIAH GRYTPGVIPP VNVDRPIPLG RRDVPGRRTR IIFILPYEYN SAQHAVVEKM
LSYAKHTREY AEFYSQSNQL LSYGDVTRFL SSNSMVLYTD VSQWDSSQHN TQPFRKGIIM
GLDMLANMTN DPKVVQTLNL YKQTQINLMD SYVQIPDGNV IKKIQYGAVA SGEKQTKAAN
SIANLALIKT VLSRIANKYS FITKIIRVDG DDNYAVLQFN TDVTKQMVQE VSNDVRYIYS
RMNAKVKALV STVGIEIAKR YIAGGKIFFR AGINLLNNEK RGQSTQWDQA AILYSNYIVN
KLRGFDTDRE FILTKIIQMT SVAITGSLRL FPSERVLTTN STFKVFDSED FIIEYGTTDD
EVYIQRAFMS LSSQKSGIAD EIASSQTFKN YVSKLSDQLL VSKNAIVSKG IAVTEKAKLN
SYAPVYLEKR RAQISALLTM LQKPVSFKSN KITINDILRD IKPFFVTTEA KLPIQYRKFM
PTLPDNVQYV IQCIGSRTYQ IEDSGSKSSI SKLISKYSVY KPSIEELYKV ISLREQEIQL
YLVSLGVPPV DAGTYVGSRI YSQDKYKILE SYVYNLLSIN YGCYQLFDFN SPDLEKLIRI
PFKGKIPAVT FILHLYAKLE IINYAIKNKS WISLFCNYPK SEMIKLWKKM WNITALRSPY
TSANFFQD
