ID   RDRP_YOMV               Reviewed;        1597 AA.
AC   Q66220;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2000, sequence version 2.
DT   03-AUG-2022, entry version 96.
DE   RecName: Full=Replicase large subunit;
DE            EC=2.7.7.48;
DE   AltName: Full=182 kDa protein;
DE   Contains:
DE     RecName: Full=Replicase small subunit;
DE              EC=3.6.4.13;
DE     AltName: Full=125 kDa protein;
DE     AltName: Full=Methyltransferase/RNA helicase;
DE              Short=MT/HEL;
OS   Youcai mosaic virus (YoMV).
OC   Viruses; Riboviria; Orthornavirae; Kitrinoviricota; Alsuviricetes;
OC   Martellivirales; Virgaviridae; Tobamovirus.
OX   NCBI_TaxID=228578;
OH   NCBI_TaxID=3708; Brassica napus (Rape).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=8616237; DOI=10.1007/bf00017814;
RA   Aguilar I., Sanchez F., Martin-Martin A., Martinez-Herrera D., Ponz F.;
RT   "Nucleotide sequence of Chinese rape mosaic virus (oilseed rape mosaic
RT   virus), a crucifer tobamovirus infectious on Arabidopsis thaliana.";
RL   Plant Mol. Biol. 30:191-197(1996).
CC   -!- FUNCTION: The replicase large subunit is an RNA-dependent RNA
CC       polymerase active in viral RNA replication. {ECO:0000250}.
CC   -!- FUNCTION: The replicase small subunit is a methyltransferase active in
CC       RNA capping and an RNA helicase. It also acts as a suppressor of RNA-
CC       mediated gene silencing, also known as post-transcriptional gene
CC       silencing (PTGS), a mechanism of plant viral defense that limits the
CC       accumulation of viral RNAs. May mediate silencing suppression through
CC       either inhibition of HEN1-mediated siRNA or siRNA demethylation (By
CC       similarity). {ECO:0000250}.
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   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13;
CC   -!- SUBUNIT: Heterodimer of a large and a small subunit. {ECO:0000250}.
CC   -!- MISCELLANEOUS: Readthrough of the terminator codon UAG occurs between
CC       codons for Gln-1103 and Gln-1105.
CC   -!- SIMILARITY: Belongs to the tobamovirus RNA-directed RNA polymerase
CC       family. {ECO:0000305}.
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DR   EMBL; U30944; AAB60599.2; -; mRNA.
DR   PIR; S65053; S65053.
DR   RefSeq; NP_740757.2; NC_004422.1.
DR   PRIDE; Q66220; -.
DR   GeneID; 955946; -.
DR   KEGG; vg:955946; -.
DR   Proteomes; UP000008609; Genome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR   GO; GO:0008174; F:mRNA methyltransferase activity; IEA:InterPro.
DR   GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR   GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR   GO; GO:0003968; F:RNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006396; P:RNA processing; IEA:InterPro.
DR   GO; GO:0006351; P:transcription, DNA-templated; IEA:InterPro.
DR   GO; GO:0039694; P:viral RNA genome replication; IEA:InterPro.
DR   Gene3D; 3.40.50.300; -; 2.
DR   InterPro; IPR027351; (+)RNA_virus_helicase_core_dom.
DR   InterPro; IPR002588; Alphavirus-like_MT_dom.
DR   InterPro; IPR043502; DNA/RNA_pol_sf.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR007094; RNA-dir_pol_PSvirus.
DR   InterPro; IPR001788; Tymovirus_RNA-dep_RNA_pol.
DR   Pfam; PF00978; RdRP_2; 1.
DR   Pfam; PF01443; Viral_helicase1; 1.
DR   Pfam; PF01660; Vmethyltransf; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   SUPFAM; SSF56672; SSF56672; 1.
DR   PROSITE; PS51743; ALPHAVIRUS_MT; 1.
DR   PROSITE; PS51657; PSRV_HELICASE; 1.
DR   PROSITE; PS50507; RDRP_SSRNA_POS; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Helicase; Hydrolase; Nucleotide-binding;
KW   Nucleotidyltransferase; Reference proteome; RNA suppression of termination;
KW   RNA-directed RNA polymerase; Suppressor of RNA silencing; Transferase;
KW   Viral RNA replication.
FT   CHAIN           1..1597
FT                   /note="Replicase large subunit"
FT                   /id="PRO_0000041174"
FT   CHAIN           1..1103
FT                   /note="Replicase small subunit"
FT                   /id="PRO_0000041175"
FT   DOMAIN          72..280
FT                   /note="Alphavirus-like MT"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01079"
FT   DOMAIN          791..950
FT                   /note="(+)RNA virus helicase ATP-binding"
FT   DOMAIN          951..1103
FT                   /note="(+)RNA virus helicase C-terminal"
FT   DOMAIN          1365..1478
FT                   /note="RdRp catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT   BINDING         823..830
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
FT   VARIANT         919
FT                   /note="V -> G"
FT   VARIANT         1286
FT                   /note="H -> Y"
SQ   SEQUENCE   1597 AA;  181624 MW;  7256A908BD3308F2 CRC64;
     MAQFQQTVNM QTLQAAAGRN SLVNDLASRR VYDNAVEELN ARSRRPKVHF SKSVSTEQTL
     LASNAYPEFE ISFTHTQQAV HSLAGGLRTL ELEYLMMQVP FGSLTYDIGG NFAAHLFKGR
     DYVHCCMPNL DVRDIARHEG HKEAIFSYLS RLDRQRRPVP EYQRAAFHNY AENPHFVHCD
     RPFQQCELST VNRWDTYAIA LHSIYDIPAD EFGAALLRKN VKICYAAFHF HENMLLDCDS
     VTLEDIGATF QRAGDKLNFF FHNESTLNYT HSFSNIIKYV CKTFFPASQR YVYHKEFLVT
     RVNTWYCKFT RVDTFTLFRG VYKTSVDSEE FYKAMDDAWE YKKTLAMLNS ERTIFKDSAA
     INFWFPKVRD MVIIPLFDAS ITTGRMSRRE VLVNKDFVYT VLNHIKTYQA KALTYANVLS
     FVESIRSRVI INGVTARSEW DTDKAILGPL AMTFFLVTKL SHVQDEIVLK KFQKFDATAK
     ELIWSSLCDA LKGVIPSVKE TLARGGFVKL AEESLEIKIP ELYCTFTDRL VLEYKRTEEF
     QSCDLSKPLE ESEKYYNALS ELSVLENLGS FDLDAFKELC QKKNVDPDVA AKVVVAIMNS
     ELTLPFKKPT EEEVAEALSG EVVQDEGLRL SNKAPFPCVS NLKEGLVPAC GLCPNGANFD
     RVDMDISEFH LKSVDAVKKG AMMSAVYTGK IKVQQMKNYV DYLSASLSAT VSNLCKVLRD
     VHGVDPESQE KSGVWDVRRG RWLLKPNAKC HAWGVAEDAN HKLVIVLLNW DEGKPVCDET
     WFRLAVSSDS LVYSDMGKLK TLTSCCRDGE PPEPTAKLVL VDGVPGCGKT KEILEKVNFS
     EDLVLVPGKE ASKMIIRRAN QAGITRADKD NVRTVDSFLM HPPKRVFKRL FIDEGLMLHT
     GCVNFLMLLS HCDVAYVYVD TQQIPFICRV ANFPYPAHFA KLVVDEKEDR RVTLRCPADV
     TYFLNQKYDG SVLCTSSVER SVSAEVVRGK GALNPITLPL EGKILTFTQA DKFELLDKGY
     KDVNTVHEVQ GETYEKTAIV RLTATPLEII SRASPHVLVA LTRHTTRCKY YTVVLDPMVN
     VISELGKLSN FLLEMYKVES GTQXQLQIDT VFKGTNLFVP TPKSGDWRDM QFYYDTLLPG
     NSTILNEFDA VTMNLRDISL NVKDCRIDFS KSVQVPKERP VFMKPKLRTA AEMPRTAGLL
     ENLVAMIKRN MNAPDLTGTI DIEDTASLVV EKFWDAYVVK EFSGTDGMAM TRESFSRWLS
     KQESSTVGQL ADFNFVDLPA VDEYKHMIKS QPKQKLDLSI QDEYPALQTI VYHSKKINAI
     FGPMFSELTR MLLETIDTSK FLFYTRKTPT QIEEFFSDLD SSQAMEILEL DISKYDKSQN
     EFHCAVEYKI WEKLGIDDWL AEVWRQGHRK TTLKDYTAGI KTCLWYQRKS GDVTTFIGNT
     IIIAACLSSM IPMDKVIKAA FCGDDSLIYI PKGLDLPDIQ AGANLTWNFE AKLFRKKYGY
     FCGRYVIHHD RGAIVYYDPL KLISKLGCKH IRDEVHLEEL RRSLCDVTSN LNNCAYFSQL
     DEAVAEVHKT AVGGAFVYCS IIKYLSDKRL FKDLFFV