ID   RDRP_ROTPC              Reviewed;        1082 AA.
AC   P26190;
DT   01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1992, sequence version 1.
DT   08-NOV-2023, entry version 90.
DE   RecName: Full=RNA-directed RNA polymerase;
DE            EC=2.7.7.48;
DE   AltName: Full=Protein VP1;
OS   Rotavirus C (strain RVC/Pig/United States/Cowden/1980) (RV-C).
OC   Viruses; Riboviria; Orthornavirae; Duplornaviricota; Resentoviricetes;
OC   Reovirales; Sedoreoviridae; Rotavirus; Rotavirus C.
OX   NCBI_TaxID=10916;
OH   NCBI_TaxID=9823; Sus scrofa (Pig).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1310192; DOI=10.1016/0042-6822(92)90035-n;
RA   Bremont M., Juste-Lesage P., Chabanne-Vautherot D., Charpilienne A.,
RA   Cohen J.;
RT   "Sequences of the four larger proteins of a porcine group C rotavirus and
RT   comparison with the equivalent group A rotavirus proteins.";
RL   Virology 186:684-692(1992).
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; M74216; AAB00801.1; -; Genomic_DNA.
DR   PIR; A40822; P1XRPC.
DR   SMR; P26190; -.
DR   Proteomes; UP000008175; 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; RNA-binding;
KW   RNA-directed RNA polymerase; Transferase; Viral RNA replication; Virion.
FT   CHAIN           1..1082
FT                   /note="RNA-directed RNA polymerase"
FT                   /id="PRO_0000149527"
FT   DOMAIN          498..670
FT                   /note="RdRp catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
SQ   SEQUENCE   1082 AA;  125082 MW;  4FE5D43379E89D96 CRC64;
     MDYDTLASKY LKFVYDFEDV TYQNNYFVTD EYKSDLEQYL KSIHDGEKIS QSKIDSMETA
     LLTKVPKEKR CLISKLVFAY GKHGNVENKL LKYGTKDALT HAIQKDVKPY ENNIITSEIF
     KDESEYTDTY MDPAINTSCQ SNCQAMMFTI SEMKLTDIKN ATRLEKLFTI VAATINKYGM
     PRHNIRYRYE WETMKDKPYH LAAWINSSIE MIACVVDHHT YMIARELIVK SFTNRTSLAK
     LVSSPMTVLT AMLPIRGTVI TTENLELEYS SKSVNYLISE EMAEDFMKAI EQLRDEGLEI
     YQDYYEKWFK SPDPLTFPNI ALIYSFSFHV GYRKQALSDA VYDQITVTYD DNVNMEMYKE
     YSERIENEIF TILKDKVVHE DKRLEEYELS ALLSMSSASN GVLREIDFGG QKVRSTKKNM
     HVIDDMYHKR YTTDIPPVDE RNPIPLGRRD VPGRRTRAIF ILPYQYFIAQ HSFAEMMLKY
     AKREREYSEF YSQANQVLSY GDVTRYLDSN SILCFTDVSQ WDASQHNTRV LRRSIIRAME
     RLKQLTHNTN IHKAIDIYIQ SQKNLENSYV LIDKKAIQYG ATASGEKQTK IMNSIANKAL
     IQTVLGKLMT DYTFDVKMIR VDGDDNYAIV RFPTAITEKL LSEFTSKLRS YYSEMNVKVK
     ALASLTGCEI AKRYIAGGML FFRAGVNILN HEKRNQDSAY DMAATLYANY IVNALRGLTM
     SRTFILVKIC QMTSIKITGT LRLFPMKSIL ALNSTFKVFD EVDYVINYPI SELFIQLQRK
     LSSIKAKSKI ADNIAKSPQF KSYVEFLNKS LTADENPIVS DGIKLTEKAK LNSYAPIALE
     KRRDQFNMMV SFLQNPTTFK SETVVTINDV LYFISGFIKI NSSVALPKEE NNTMPLLPVT
     IKRTLNYFGL RTHDYDIKGS SSTMSKIIKQ YSVYTPGIEE LYEVVNKSID SIRGYFASFN
     VPKADVDTYI STQMYKHDRF KILQAYIYNL LSVNYGMYQL VDLNSAKFFD HVIHTPMAKT
     PTAVFMIDLA LRLKVINHCI EKGEVITVSV HANKTDYLKL WRMLWNVKTM NSPYSKNSMF
     DE
//