ID   RDRP_ROTB2              Reviewed;        1167 AA.
AC   A9Q1K7;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 1.
DT   27-MAR-2024, entry version 50.
DE   RecName: Full=RNA-directed RNA polymerase;
DE            EC=2.7.7.48;
DE   AltName: Full=Protein VP1;
OS   Rotavirus X (isolate RVX/Human/Bangladesh/NADRV-B219/2002/GXP[X]) (RV
OS   ADRV-N) (Rotavirus (isolate novel adult diarrhea rotavirus-B219)).
OC   Viruses; Riboviria; Orthornavirae; Duplornaviricota; Resentoviricetes;
OC   Reovirales; Sedoreoviridae; Rotavirus.
OX   NCBI_TaxID=348136;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=18814255; DOI=10.1002/jmv.21286;
RA   Nagashima S., Kobayashi N., Ishino M., Alam M.M., Ahmed M.U., Paul S.K.,
RA   Ganesh B., Chawla-Sarkar M., Krishnan T., Naik T.N., Wang Y.-H.;
RT   "Whole genomic characterization of a human rotavirus strain B219 belonging
RT   to a novel group of the genus Rotavirus.";
RL   J. Med. Virol. 80:2023-2033(2008).
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; EF453355; ABR32122.1; -; mRNA.
DR   SMR; A9Q1K7; -.
DR   Proteomes; UP000174021; 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; -; 1.
DR   Gene3D; 3.30.70.2480; -; 1.
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; DNA/RNA polymerases; 1.
DR   PROSITE; PS50523; RDRP_DSRNA_REO; 1.
PE   2: Evidence at transcript level;
KW   Nucleotide-binding; Nucleotidyltransferase; RNA-binding;
KW   RNA-directed RNA polymerase; Transferase; Viral RNA replication; Virion.
FT   CHAIN           1..1167
FT                   /note="RNA-directed RNA polymerase"
FT                   /id="PRO_0000369830"
FT   DOMAIN          553..735
FT                   /note="RdRp catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
SQ   SEQUENCE   1167 AA;  132901 MW;  C612426A9D1FE310 CRC64;
     MEPENYLAWL ARDIVRNLSY TSLVYNNPKV AIVELLDNKE AFFTYEKEQK TPEALINYID
     SIVKSSISVE DKIEALLKIR YISVYVDDKS DKRDIVLQLL NRTIKKIESK TKISNELNDA
     INAITIESRN WKIQNSESFK PYHYNQLVSD FLKYNEFEIL EGTDPLKWKS DTLQGLSPNY
     NHRTHTLISS IIYATSVRFD NYNDEQLQVL LYLFSIIKTN YVNGYLEILP NRKWSHSLAD
     LRENKSIMMY SAKIIHASCA MISILHAVPI DYFFLAQIIA SFSEIPAHAA KQLSSPMTLY
     IGIAQLRSNI VVSTKIAAES VATESPNISR LEESQLREWE QEMNEYPFQS SRMVRMMKKN
     IFDVSVDVFY AIFNCFSATF HVGHRIDNPQ DAIEAQVKVE YTSDVDKEMY DQYYFLLKRM
     LTDQLAEYAE EMYFKYNSDV TAESLAAMAN SSNGYSRSVT FIDREIKTTK KMLHLDDDLS
     KNLNFTNIGE QIKKGIPMGT RNVPARQTRG IFILSWQVAA IQHTIAEFLY KKAKKGGFGA
     TFAEAYVSKA ATLTYGILAE ATSKADQLIL YTDVSQWDAS QHNTEPYRSA WINAIKEART
     KYKINYNQEP VVLGMNVLDK MIEIQEALLN SNLIVESQGS KRQPLRIKYH GVASGEKTTK
     IGNSFANVAL ITTVFNNLTN TMPSIRVNHM RVDGDDNVVT MYTANRIDEV QENIKEKYKR
     MNAKVKALAS YTGLEMAKRF IICGKIFERG AISIFTAERP YGTDLSVQST TGSLIYSAAV
     NAYRGFGDDY LNFMTDVLVP PSASVKITGR LRSLLSPVTL YSTGPLSFEI TPYGLGGRMR
     LFSLSKENME LYKILTSSLA ISIQPDEIKK YSSTPQFKAR VDRMISSVQI AMKSEAKIIT
     SILRDKEEQK TLGVPNVATA KNRQQIDKAR KTLSLPKEIL PKVTKYYPEE IFHLILRNST
     LTIPKLNTMT KVYMNNSVNI TKLQQQIGVR VSSGIQVHKP INTLLKLVEK HSPIKISPSD
     LILYSKKYDL TNLNGKKQFL MDLGISGNEL RFYLNSKLLF HDLLLSKYDK LYEAPGFGAT
     QLNALPLDLT AAEKVFSIKL NLPNTYYELL MLVLLYEYVN FVMFTGNTFR AVCIPESQTI
     NAKLVKTIMT MIDNIQLDTV MFSDNIF
//