RDRP_ROTHC
ID RDRP_ROTHC Reviewed; 1090 AA.
AC Q91E95;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 29-SEP-2021, entry version 67.
DE RecName: Full=RNA-directed RNA polymerase;
DE EC=2.7.7.48;
DE AltName: Full=Protein VP1;
OS Rotavirus C (isolate RVC/Human/United Kingdom/Bristol/1989) (RV-C).
OC Viruses; Riboviria; Orthornavirae; Duplornaviricota; Resentoviricetes;
OC Reovirales; Reoviridae; Sedoreovirinae; Rotavirus.
OX NCBI_TaxID=31567;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=11864750; DOI=10.1016/s0168-1702(01)00442-7;
RA Chen Z., Lambden P.R., Lau J., Caul E.O., Clarke I.N.;
RT "Human group C rotavirus: completion of the genome sequence and gene coding
RT assignments of a non-cultivatable rotavirus.";
RL Virus Res. 83:179-187(2002).
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 dsDNA formation. To do so, the polymerase
CC specifically recognizes conserved 3' sequence(s) in plus-strand RNA
CC templates. Once dsRNA synthesis is complete, the polymerase switches to
CC 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; AJ304859; CAC44891.1; -; Genomic_RNA.
DR RefSeq; YP_392464.1; NC_007547.1.
DR SMR; Q91E95; -.
DR PRIDE; Q91E95; -.
DR GeneID; 3773137; -.
DR KEGG; vg:3773137; -.
DR Proteomes; UP000007664; 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; Reference proteome;
KW RNA-binding; RNA-directed RNA polymerase; Transferase;
KW Viral RNA replication; Virion.
FT CHAIN 1..1090
FT /note="RNA-directed RNA polymerase"
FT /id="PRO_0000369869"
FT DOMAIN 506..678
FT /note="RdRp catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
SQ SEQUENCE 1090 AA; 125802 MW; A8B60957412342F2 CRC64;
MAQSIVVDGD YDALASRYLK FVYDFENVTY QNNYFATDKF KKDIEQYLKS IHDGEKITQS
KIDEKEKILL DRVPAEERCL ISKLVFAYGK HGNVENKLVK YGVKDALSHA PQKDAKPYEN
NIITSEIFKE KSEYTDIYMD PSINTSCQSN CQAMMFTISE MKLNNIKNAA RLEKLFTIIA
ATINKYGMPR HNTRYRYEWE TMKNKPYHLA AWINSSIEMI ACVVDHHTYM IARELIVKSF
TNRTSLAKLV SSPMTVLTAM LPIRGTFITT ENLELEYSNK SINYLISKEM AEDFMQAIKQ
LRDEGLEYIP DYYEKWFKSP DPLTFPNIAL IYSFSFHVGY RKQALSDAVY DQITVTYSDN
VNMEMYKEYS ERIENEIFTI LKDKIIHEDK RLEEYELSAL LSMSSASNGI LREINFGGQK
VRSTKKNMHV IDDIYHKKYT TDIPPVDARN PIPLGRRDVP GRRTRAIFIL PYQYFIAQHS
FAEIMLNYAK REREYSEFYS QANQVLSYGD VTRYLDSNSI LCFTDVSQWD ASQHNTKVLR
RSIIRAMKRL KQLTHNINIH KAINIYIQSQ ENLENSYVLI DKKAIQYGAT ASGEKQTKIM
NSIANKALIQ TVLGKLMTDY TFDVKMIRVD GDDNYAIVRF PIAITEKLLS EFTSKLRSYY
SEMNVKVKAL ASLTGCEIAK RYVAGGMLFF RAGVNILHHE KRNQDSAYDM AATLYANYIV
NALRGLTMSR TFILTKICQM TSIKITGTLR LFPMKSILAL NSAFKVFDEV DYVINYPISN
LFIQLQRKLS SIKAKSKIAD NIAKSPQFKS YVELLNKSLT TDENPIVSDG IRLTEKAKLN
SYAPIALEKR RDQFSIMVSF LQNPTTFKSE TVVTINDVLY FISGFIKIDS STVLPKEENN
TMPLLPAIIK RTLSYFGLRT HDYDIKGSSS TVSKIIKQYS VYTPGIEELY EIVNKSVDTI
RGYFASFNVP KADVDTYIST QMYKHDRFKI LQAYIYNLLS VNYGMYQLVD LNSARFFDHV
IHTPMAKTPT AVFMIDLALR LKIINHCIEK GEIITVSVHA NKTDYLKLWR MLWNVKTMNS
PYSKNSMFDE
