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 27-MAR-2024, entry version 102.
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 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-dependent RNA polymerase activity; IEA:UniProtKB-KW.
DR GO; GO:0006351; P:DNA-templated transcription; IEA:InterPro.
DR GO; GO:0006396; P:RNA processing; IEA:InterPro.
DR GO; GO:0039694; P:viral RNA genome replication; IEA:InterPro.
DR CDD; cd23251; Virgaviridae_RdRp; 1.
DR Gene3D; 3.30.450.420; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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; IPR001788; RNA-dep_RNA_pol_alsuvir.
DR InterPro; IPR007094; RNA-dir_pol_PSvirus.
DR InterPro; IPR049329; ToMV_Hel_N.
DR InterPro; IPR047310; Virgaviridae_RdRp.
DR Pfam; PF00978; RdRP_2; 1.
DR Pfam; PF20896; ToMV_Hel_N; 1.
DR Pfam; PF01443; Viral_helicase1; 1.
DR Pfam; PF01660; Vmethyltransf; 1.
DR SUPFAM; SSF56672; DNA/RNA polymerases; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 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; Host-virus interaction; Hydrolase;
KW Inhibition of host innate immune response by virus; Nucleotide-binding;
KW Nucleotidyltransferase; Reference proteome; RNA suppression of termination;
KW RNA-directed RNA polymerase; Suppressor of RNA silencing; Transferase;
KW Viral immunoevasion; 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
//
