RDRP_RDVF
ID RDRP_RDVF Reviewed; 1444 AA.
AC Q98631;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 23-FEB-2022, entry version 74.
DE RecName: Full=RNA-directed RNA polymerase P1;
DE EC=2.7.7.48;
DE AltName: Full=Replicase;
GN Name=S1;
OS Rice dwarf virus (isolate Fujian) (RDV).
OC Viruses; Riboviria; Orthornavirae; Duplornaviricota; Resentoviricetes;
OC Reovirales; Reoviridae; Sedoreovirinae; Phytoreovirus.
OX NCBI_TaxID=142804;
OH NCBI_TaxID=114194; Alopecurus aequalis.
OH NCBI_TaxID=90397; Echinochloa crus-galli (Barnyard grass) (Panicum crus-galli).
OH NCBI_TaxID=94400; Nephotettix cincticeps (Green rice leafhopper) (Selenocephalus cincticeps).
OH NCBI_TaxID=4530; Oryza sativa (Rice).
OH NCBI_TaxID=147271; Paspalum.
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=12549398;
RA Xiao J., Li Y., Zhang J., Liu J., Chen Z.;
RT "Nucleotide and protein sequence analysis of rice dwarf virus replicase.";
RL Wei Sheng Wu Xue Bao 38:348-358(1998).
RN [2]
RP SUBCELLULAR LOCATION.
RX PubMed=16432031; DOI=10.1099/vir.0.81425-0;
RA Wei T., Shimizu T., Hagiwara K., Kikuchi A., Moriyasu Y., Suzuki N.,
RA Chen H., Omura T.;
RT "Pns12 protein of Rice dwarf virus is essential for formation of viroplasms
RT and nucleation of viral-assembly complexes.";
RL J. Gen. Virol. 87:429-438(2006).
RN [3]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=20190042; DOI=10.1093/jb/mvq017;
RA Miyazaki N., Wu B., Hagiwara K., Wang C.Y., Xing L., Hammar L.,
RA Higashiura A., Tsukihara T., Nakagawa A., Omura T., Cheng R.H.;
RT "The functional organization of the internal components of Rice dwarf
RT virus.";
RL J. Biochem. 147:843-850(2010).
CC -!- FUNCTION: RNA-directed RNA polymerase that is involved in both
CC transcription and genome replication. Together with the capping enzyme
CC P5 and protein P7, forms an enzyme complex positioned near the channels
CC situated at each of the five-fold vertices of the core.
CC {ECO:0000255|PROSITE-ProRule:PRU00539, ECO:0000269|PubMed:20190042}.
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 -!- SUBCELLULAR LOCATION: Virion {ECO:0000269|PubMed:20190042}. Host
CC cytoplasm {ECO:0000269|PubMed:16432031}. Note=Located inside the inner
CC capsid (PubMed:20190042). Found in the interior of spherical
CC cytoplasmic structures, called virus factories, that appear early after
CC infection and are the site of viral replication and packaging.
CC {ECO:0000269|PubMed:20190042, ECO:0000305}.
CC -!- SIMILARITY: Belongs to the reoviridae RNA-directed RNA polymerase
CC family. {ECO:0000305}.
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DR EMBL; U73201; AAB18743.1; -; Genomic_RNA.
DR RefSeq; NP_620544.1; NC_003773.1.
DR PRIDE; Q98631; -.
DR GeneID; 956505; -.
DR KEGG; vg:956505; -.
DR Proteomes; UP000002239; Genome.
DR GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0003968; F:RNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-KW.
DR GO; GO:0019079; P:viral genome replication; IEA:InterPro.
DR InterPro; IPR043502; DNA/RNA_pol_sf.
DR InterPro; IPR007097; RNA-dir_pol_reovirus.
DR InterPro; IPR014383; RNA-dir_poll_phytoreovirus.
DR PIRSF; PIRSF000822; RdRPol_RDV; 1.
DR SUPFAM; SSF56672; SSF56672; 1.
DR PROSITE; PS50523; RDRP_DSRNA_REO; 1.
PE 3: Inferred from homology;
KW Host cytoplasm; Nucleotide-binding; Nucleotidyltransferase;
KW Reference proteome; RNA-directed RNA polymerase; Transferase;
KW Viral RNA replication; Virion.
FT CHAIN 1..1444
FT /note="RNA-directed RNA polymerase P1"
FT /id="PRO_0000222778"
FT DOMAIN 690..897
FT /note="RdRp catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT REGION 156..182
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 156..170
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1444 AA; 164422 MW; A0CF28E1CB945D4C CRC64;
MDLARSDIIP HLLCLFQEII QANIQKVSEA YDLELKIMNI LTLWRNGSDN LISDNDDYMK
KGLFFSRSND PLALQARYAR MYDDLFKLNN YEVPDDVVRR HDNKILDIIL KESSVPFWYD
ISDDEAHESM LPEFRLQDIH EFRLNLKRVR VVPDESEEIQ MDESQSDKRR RKKRMEKSRP
VWLSGSESDR RIELNDSLKP SQKFETKLSS YLLNRLMNEM NPHYCGHPLP ALFVTLIMLK
AYSIKNKFFS YGIRYMELVC NEIAGPDLNT RTFPVLFGSD GSFVGTRVYS HYPIKLRMIL
NDLTYLLTYS DLHKFQEFEL DVNDEVLLHM LRTPNDGRQL KKAVTRLNHY YGLKFNPKTT
DCGVVNGMDF THKHPITKTA DFTSPVLPMT NSFNKAEICY GHNSKILNRA VFTDTVRGHI
REDLKNVADL DLPKLYEHVS KLVDMRVNYT IIYDLMFLRV MLNLGGYSRS NQITDFRKTI
DEITKMNEGF LSGADPEKNI DTLNAWMAPT MEDCGYRLTK SILFGKFRKA KYPSDLEAKS
NIDYYVTARS AGIGNLRISI ETDKRKYKVR TTSKSAFVNA MGSGILDVNP VSNEPMMLTD
YLLTQTPETR ANLEAAIDSG SKSDSELMRI LGQNSIGSRS TTAWRPVRPI YINVLQAHLA
QAFIIGPHIN ATVNQHEYQP TSLWFTGDDL GVGFATLYQS GTADIIVPAI EASSTGKALS
VLADCSSWDQ TYLTATMIPY YNGIKRALLE YQQADMRNFY MIDSGRTGVP GMKLSEIVDW
FNSFQTKRIF NASYLKERHS FVVKYMWSGR LDTFFMNSVQ NALITRRIAE EVSLRVSNTG
LSWFQVAGDD AIMVYDGSSI STTEQVTRIN EITVRNYEES NHIINPQKTV ISHISGEYAK
IYYYAGMHFR DPSIQLHESE KDSGASDVTE SLREFGQVIY EYNKRAIGTL RVNALYGRLI
AGLAYSVNCP QYDASKRTYA NMKYYPPPTS VIAPAAFKGG LGLSFTGLSL NEVLFIKLHL
HEAVSQGLHV ISMISFEANE VVSNSLSAYY LKDQKDLLRD MKLGKHLEKV KGISFKSSDL
AFSGSDFSQG LNLKRESIDK VKLEVSRKSI RDLRSSGISV PSTHAYENLP YASLHQSFKS
LKVDRDTSKF TNERLLVSLL EYKSDIPRVS VTSQYPVYDL INISKVDELN VRSGGPVRFI
SAPIEGKLLE ENIGTRQGVQ FKNRGYGGSQ EVLHFIRSNG LVITEQALID LIIKSGVLLM
INPQRGLIDL FQSLSGDTAS SMHLANFFMA EKPHWEDNAI SLTIAGSLLE NCDSRIENVK
NFVSVLATGM QKDLQRMFYY VGFVYYAQRL IWSGGHSSKI FVSIDEDKLA DFLRGSKPIT
RRRKAMAGTK REPINLSANF SYEISEPDRE ISEYDPLILC HPLSMPFFGN WQEKYSVMQS
DEQM