ID   RDRP_ROTGI              Reviewed;        1159 AA.
AC   P35942;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 1.
DT   23-FEB-2022, entry version 70.
DE   RecName: Full=RNA-directed RNA polymerase;
DE            EC=2.7.7.48;
DE   AltName: Full=Protein VP1;
OS   Rotavirus B (isolate RVB/Rat/United States/IDIR/1984/G1P[X]) (RV-B)
OS   (Rotavirus B (isolate infectious diarrhea of infant rats)).
OC   Viruses; Riboviria; Orthornavirae; Duplornaviricota; Resentoviricetes;
OC   Reovirales; Reoviridae; Sedoreovirinae; Rotavirus.
OX   NCBI_TaxID=28877;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
OH   NCBI_TaxID=10116; Rattus norvegicus (Rat).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=8390749; DOI=10.1006/viro.1993.1017;
RA   Eiden J.J., Hirshon C.;
RT   "Sequence analysis of group B rotavirus gene 1 and definition of a
RT   rotavirus-specific sequence motif within the RNA polymerase gene.";
RL   Virology 192:154-160(1993).
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   -!- SUBUNIT: Interacts with VP3 (Potential). Interacts with VP2
CC       (Potential). Interacts with NSP5; this interaction is probably
CC       necessary for the formation of functional virus factories (By
CC       similarity). {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; M97203; -; NOT_ANNOTATED_CDS; Genomic_RNA.
DR   PIR; A44280; A44280.
DR   SMR; P35942; -.
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   InterPro; IPR043502; DNA/RNA_pol_sf.
DR   InterPro; IPR001795; RNA-dir_pol_luteovirus.
DR   InterPro; IPR007097; RNA-dir_pol_reovirus.
DR   Pfam; PF02123; RdRP_4; 1.
DR   SUPFAM; SSF56672; SSF56672; 1.
DR   PROSITE; PS50523; RDRP_DSRNA_REO; 1.
PE   3: Inferred from homology;
KW   Nucleotide-binding; Nucleotidyltransferase; RNA-binding;
KW   RNA-directed RNA polymerase; Transferase; Viral RNA replication; Virion.
FT   CHAIN           1..1159
FT                   /note="RNA-directed RNA polymerase"
FT                   /id="PRO_0000149530"
FT   DOMAIN          545..727
FT                   /note="RdRp catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
SQ   SEQUENCE   1159 AA;  131650 MW;  E355F9BF79E225A8 CRC64;
     MDSFQFFEWL LRDIERNLLY TSLVYTNPKI AIVRYEPSEN AKLWRSKELN TDSPNELLLT
     LKKTLDECST LDEKIETLLR IRYFTVYVGD KSDKRNIIRS WLSTTINRLN VEEYASIQEI
     ELQAKQWRAE NAKSLRPYHY NIPINEYLRD NEIEVLDTGD NRWKSDTLQG LLPNFYHRTH
     TLIGAILFAV TSRLEIYSYE QKKALRYLLR TIEKCYNEGY LEMSRDRKWS HTLPELRTLT
     FRLYNSKVIH AACAMISLVH ANPIDYEFLC QVVAVYQIIP ANAAKLLSTP MTLYVGVATF
     SSNQVASTGN ASECAPLQIE NNIYVSEAQK KEWAESFKSD PLNKSRMLKL MNENLNTTLD
     KFSLIFNCFS STFHVGHRID NAQDAITDQV TATYTSNVNR EMYDSYYYKL KQMLKEEIVQ
     YVEDHVAKQY KDVTAESLSA LANSSNGFSK EVKFIDRNIK TTKKILHLDN DLITNDYSDL
     SKALSHGIPM GTRNVPARQT RGIFILPWQV AAVQHTIAES LYKRAKKGAY QGSFAEAYTA
     KTASLTYGVL AEDTSKATKI ILYTDVSQWD ASQHNTEPYR SAWINAIREA RAELKWRYDD
     EPKVLEMNVL DSMIKIQEYL LNSNLVVASP GSQRPTKIIR YHGVASGEKT TKIGNSFANV
     ALIETVLDFA KTDIPDLEIS HLRVDGDDNV VSINTSCTID RLQRIIKEKY SSLNARVKAL
     ASYTGLEMAK RFIICGKIFE RGAIPIFTAE RPYGTDVSIQ SMCGSSIYSS AVNAYRGFGD
     AYFSFMQDVL VPPSASTRIT GRLRVLMSPV TLYATGPLSF EITPQGLGGR CRFFTQSAKL
     FTLFKMLTQT AAVSITPDEI KKYAETVQFK KRTEVMIASM QRKLLVPAKA LARIIVDKEQ
     QKTLGVPNVQ SQKNRSQVSK AIEILGVPER NDIVAKGYYP EELYSLIISH SVVVYTSHST
     PISIYRVNCE PVELLRSQLG IRIADSKPIA KPTNHLYDIV SGLSPIKISP SDLLTQAKKY
     DLSTYKGKRD YLSDLGLVGN TLKTYLASKM LFRDLLMSKY DDLYSTPGFG ATQLTTIPLD
     VTSAEKVFSI RLGLPPHLYE VVMLLLLYEY IHYVFSCKRT FTAQMHAISQ EQSAVITKNI
     ILMLDNIQLD QVSFSDDAW