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   08-NOV-2023, entry version 71.
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; Sedoreoviridae; Rotavirus; Rotavirus C.
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   GeneID; 3773137; -.
DR   KEGG; vg:3773137; -.
DR   Proteomes; UP000007664; Genome.
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; 1.20.120.1400; -; 1.
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; 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
//