RDRP_ROTB2
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 03-AUG-2022, entry version 45.
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; Reoviridae; Sedoreovirinae; Rotavirus; unclassified 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: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 2: Evidence at transcript level;
KW Nucleotide-binding; Nucleotidyltransferase; Reference proteome;
KW RNA-binding; RNA-directed RNA polymerase; Transferase;
KW 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