ID   RDRP_OCSVU              Reviewed;         752 AA.
AC   Q83927; Q83926;
DT   05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   29-SEP-2021, entry version 77.
DE   RecName: Full=RNA-directed RNA polymerase;
DE            EC=2.7.7.48;
DE   AltName: Full=Protein p84;
DE   Contains:
DE     RecName: Full=Protein p23;
GN   ORFNames=ORF1;
OS   Oat chlorotic stunt virus (isolate United Kingdom) (OCSV).
OC   Viruses; Riboviria; Orthornavirae; Kitrinoviricota; Tolucaviricetes;
OC   Tolivirales; Tombusviridae; Procedovirinae; Avenavirus.
OX   NCBI_TaxID=652110;
OH   NCBI_TaxID=4498; Avena sativa (Oat).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=7636483; DOI=10.1099/0022-1317-76-8-2025;
RA   Boonham N., Henry C.M., Wood K.R.;
RT   "The nucleotide sequence and proposed genome organization of oat chlorotic
RT   stunt virus, a new soil-borne virus of cereals.";
RL   J. Gen. Virol. 76:2025-2034(1995).
CC   -!- FUNCTION: RNA-dependent RNA polymerase that plays an essential role in
CC       the virus replication. {ECO:0000305}.
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   -!- MISCELLANEOUS: Readthrough of the terminator UAG occurs at position
CC       213.
CC   -!- SIMILARITY: Belongs to the tombusviridae RNA polymerase family.
CC       {ECO:0000305}.
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DR   EMBL; X83964; CAA58796.1; -; Genomic_RNA.
DR   EMBL; X83964; CAA58797.1; -; Genomic_RNA.
DR   RefSeq; NP_619751.1; NC_003633.1.
DR   RefSeq; NP_619752.1; NC_003633.1.
DR   GeneID; 1732851; -.
DR   GeneID; 940248; -.
DR   KEGG; vg:1732851; -.
DR   KEGG; vg:940248; -.
DR   Proteomes; UP000000573; Genome.
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:0039694; P:viral RNA genome replication; IEA:InterPro.
DR   Gene3D; 3.30.70.270; -; 1.
DR   InterPro; IPR043502; DNA/RNA_pol_sf.
DR   InterPro; IPR043128; Rev_trsase/Diguanyl_cyclase.
DR   InterPro; IPR007094; RNA-dir_pol_PSvirus.
DR   InterPro; IPR002166; RNA_pol_HCV.
DR   Pfam; PF00998; RdRP_3; 1.
DR   SUPFAM; SSF56672; SSF56672; 1.
DR   PROSITE; PS50507; RDRP_SSRNA_POS; 1.
PE   3: Inferred from homology;
KW   Nucleotide-binding; Nucleotidyltransferase; Reference proteome;
KW   RNA suppression of termination; RNA-directed RNA polymerase; Transferase;
KW   Viral RNA replication.
FT   CHAIN           1..752
FT                   /note="RNA-directed RNA polymerase"
FT                   /id="PRO_0000399490"
FT   CHAIN           1..212
FT                   /note="Protein p23"
FT                   /id="PRO_0000399491"
FT   DOMAIN          442..561
FT                   /note="RdRp catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
SQ   SEQUENCE   752 AA;  84449 MW;  798BB83729EC00C2 CRC64;
     MSWPSLSGVP NGSSSVSTWL SVTHPRRSLP KELLTAFDTC NVAPEALLVL RSTSLMILEE
     TCVVVGAAEM PTAEDNSGRE LFIGSNGDPM ERKTRTAHHA IKKTVRIKKG HRTTFAMTVA
     NGAYVKFGAR PLTEANVLVV RKWIVKLIAD EYKDLRVCDQ ALVIDRATFL SFIPTMAWNN
     YKFIFHGKNA VTDRVAGENL FSRIAQWANP GKXGCPVVVT GQGCVISRAP DCAQLRVKRL
     LGVTKNRTCM RVSGVSPNIQ IIPFNNDITT LERAIKERVF FVKNLDKGSP TKFVSPPRPA
     PGVFAQRLSN TLGLLVPFLP STAPMSHQQF VDSTPSRKRK VYQQALEDIS CHGLNLETDS
     KVKVFVKYEK TDHTSKADPV PRVISPRDPK YNLALGRYLR PMEERIFKAL GKLFGHRTVM
     KGMDTDVTAR VIQEKWNMFN KPVAIGLDAS RFDQHVSLEA LEFEHSVYLK CVRRMVDKRK
     LGNILRHQLL NKCYGNTPDG AVSYTIEGTR MSGDMNTSLG NCVLMCMMIH AYGLHKSVNI
     QLANNGDDCV VFLEQSDLAT FSEGLFEWFL EMGFNMAIEE PSYELEHIEF CQCRPVFDGV
     KYTMCRNPRT AIAKDSVYLK HVDQFVTYSS WLNAVGTGGL ALAGGLPIFD AFYTCYKRNS
     NSHWFSGRKG RLKTLSSVDD SLPWFMRELG LKGKRSSAEP LPASRASFYL AWGVTPCEQL
     ELEKYYKSFK LDTSTLLEEH LWQPRGVFPD ED