ID   RDRP_TVCV               Reviewed;        1601 AA.
AC   Q88920; Q88919;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 99.
DE   RecName: Full=Replicase large subunit;
DE            EC=2.1.1.-;
DE            EC=2.7.7.-;
DE            EC=2.7.7.48;
DE            EC=3.6.4.13;
DE   AltName: Full=183 kDa protein;
DE   AltName: Full=RNA-directed RNA polymerase;
DE   Contains:
DE     RecName: Full=Replicase small subunit;
DE              EC=2.1.1.-;
DE              EC=2.7.7.-;
DE              EC=3.6.4.13;
DE     AltName: Full=126 kDa protein;
DE     AltName: Full=Methyltransferase/RNA helicase;
DE              Short=MT/HEL;
OS   Turnip vein-clearing virus (TVCV).
OC   Viruses; Riboviria; Orthornavirae; Kitrinoviricota; Alsuviricetes;
OC   Martellivirales; Virgaviridae; Tobamovirus.
OX   NCBI_TaxID=29272;
OH   NCBI_TaxID=3700; Brassicaceae.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 1-1108.
RC   STRAIN=OSU;
RX   PubMed=7998835; DOI=10.1007/bf01379132;
RA   Lartey R.T., Lane L.C., Melcher U.;
RT   "Electron microscopic and molecular characterization of turnip vein-
RT   clearing virus.";
RL   Arch. Virol. 138:287-298(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 1109-1601.
RC   STRAIN=OSU;
RX   PubMed=8543186; DOI=10.1016/0378-1119(95)00674-5;
RA   Lartey R.T., Voss T.C., Melcher U.K.;
RT   "Completion of a cDNA sequence from a tobamovirus pathogenic to
RT   crucifers.";
RL   Gene 166:331-332(1995).
RN   [3]
RP   ERRATUM OF PUBMED:8543186.
RA   Lartey R.T., Voss T.C., Melcher U.K.;
RL   Gene 188:295-295(1997).
CC   -!- FUNCTION: [Replicase large subunit]: Is an RNA-dependent RNA polymerase
CC       active in viral RNA replication.
CC   -!- FUNCTION: [Replicase small subunit]: Is a methyltransferase active in
CC       RNA capping and an RNA helicase. Methyltransferase displays a
CC       cytoplasmic capping enzyme activity. This function is necessary since
CC       all viral RNAs are synthesized in the cytoplasm, and host capping
CC       enzymes are restricted to the nucleus. Helicase region probably
CC       exhibits NTPase and RNA unwinding activities (Potential). It also acts
CC       as a suppressor of RNA-mediated gene silencing, also known as post-
CC       transcriptional gene silencing (PTGS), a mechanism of plant viral
CC       defense that limits the accumulation of viral RNAs. May mediate
CC       silencing suppression through either inhibition of HEN1-mediated siRNA
CC       or siRNA demethylation (By similarity). {ECO:0000250, 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   -!- 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: This protein is translated as a fusion protein by
CC       episodic readthrough of a termination codon which is expressed as
CC       tyrosine. When readthrough of the terminator codon TGA occurs between
CC       the codons for Phe-1116 and Asp-1118, this results in the addition of
CC       the RdRp region to the replicase.
CC   -!- SIMILARITY: Belongs to the ssRNA positive-strand viruses RNA-directed
CC       RNA polymerase family. {ECO:0000305}.
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DR   EMBL; U03387; AAC02783.1; -; Genomic_RNA.
DR   EMBL; U03387; AAC02782.1; -; Genomic_RNA.
DR   RefSeq; NP_046151.1; NC_001873.1.
DR   RefSeq; NP_046152.1; NC_001873.1.
DR   SMR; Q88920; -.
DR   PRIDE; Q88920; -.
DR   GeneID; 1494923; -.
DR   GeneID; 1494926; -.
DR   KEGG; vg:1494923; -.
DR   KEGG; vg:1494926; -.
DR   Proteomes; UP000008264; 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   3: Inferred from homology;
KW   ATP-binding; Helicase; Hydrolase; Nucleotide-binding;
KW   Nucleotidyltransferase; RNA suppression of termination;
KW   RNA-directed RNA polymerase; Suppressor of RNA silencing; Transferase;
KW   Viral RNA replication.
FT   CHAIN           1..1601
FT                   /note="Replicase large subunit"
FT                   /id="PRO_0000041198"
FT   CHAIN           1..1107
FT                   /note="Replicase small subunit"
FT                   /id="PRO_0000041199"
FT   DOMAIN          72..280
FT                   /note="Alphavirus-like MT"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01079"
FT   DOMAIN          795..954
FT                   /note="(+)RNA virus helicase ATP-binding"
FT   DOMAIN          955..1107
FT                   /note="(+)RNA virus helicase C-terminal"
FT   DOMAIN          1369..1482
FT                   /note="RdRp catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT   REGION          50..436
FT                   /note="Methyltransferase"
FT   REGION          823..1076
FT                   /note="Helicase"
FT   BINDING         827..834
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   1601 AA;  181930 MW;  F9E0A041C15DB34D CRC64;
     MAQFQQTIDM QTLQAAAGRN SLVNDLASRR VYDNAVEELN ARSRRPKVHF SKAVSTEQTL
     IATNAYPEFE ISFTHTQSAV HSLAGGLRSL ELEYLMMQVP FGSLTYDIGG NFSAHLFKGR
     DYVHCCMPNL DVRDIARHEG HKEAIYSYVN RLKRQQRPVP EYQRAAFNNY AENPHFVHCD
     KPFQQCELTT AYGTDTYAVA LHSIYDIPVE EFGSALLRKN VKTCFAAFHF HENMLLDCDT
     VTLDEIGATF QKSGDNLSFF FHNESTLNYT HSFSNIIKYV CKTFFPASQR FVYHKEFLVT
     RVNTWYCKFT RVDTFTLFRG VYHNNVDCEE FYKAMDDAWH YKKTLAMLNA ERTIFKDNAA
     LNFWFPKVRD MVIVPLFDAS ITTGRMSRRE IMVNKDFVYT VLNHIKTYQA KALTYANVLS
     FVESIRSRVI INGVTARSEW DTDKAILGPL AMTFFLITKL GHVQDEIILK KFQKFDRTTN
     ELIWTSLCDA LMGVIPSVKE TLVRGGFVKV AEQALEIKVP ELYCTFADRL VLQYKKAEEF
     QSCDLSKPLE ESEKYYNALS ELSVLENLDS FDLEAFKTLC QQKNVDPDMA AKVVVAIMKS
     ELTLPFKKPT EEEISESLKP GEGSCAEHKE VLSLQNDAPF PCVKNLVEGS VPAYGMCPKG
     GGFDKLDVDI ADFHLKSVDA VKKGTMMSAV YTGSIKVQQM KNYIDYLSAS LAATVSNLCK
     VLRDVHGVDP ESQEKSGVWD VRRGRWLLKP NAKSHAWGVA EDANHKLVIV LLNWDDGKPV
     CDETWFRVAV SSDSLIYSDM GKLKTLTSCS PNGEPPEPNA KVILVDGVPG CGKTKEIIEK
     VNFSEDLILV PGKEASKMII RRANQAGVIR ADKDNVRTVD SFLMHPSRRV FKRLFIDEGL
     MLHTGCVNFL LLLSQCDVAY VYGDTKQIPF ICRVANFPYP AHFAKLVADE KEVRRVTLRC
     PADVTYFLNK KYDGAVMCTS AVERSVKAEV VRGKGALNPI TLPLEGKILT FTQADKFELL
     EKGYKDVNTV HEVQGETYEK TAIVRLTSTP LEIISSASPH VLVALTRHTT CCKYYTVVLD
     PMVNVISEME KLSNFLLDMY RVEAGVQYQL QIDAVFRDSN LFVQTPKSGD WRDMQFYYDA
     LLPGNSTILN EFDAVTMNLR DISLNVKDCR IDFSKSVQLP KEQPIFLKPK IRTAAEMPRT
     AGLLENLVAM IKRNMNAPDL TGTIDIEDTA SLVVEKFWDS YVDKEFSGTN EMTMTRESFS
     RWLSKQESST VGQLADFNFV DLPAVDEYKH MIKSQPKQKL DLSIQDEYPA LQTIVYHSKK
     INAIFGPMFS ELTRMLLERI DSSKFLFYTR KTPAQIEDFF SDLDSTQAME ILELDISKYD
     KSQNEFHCAV EYKIWEKLGI DEWLAEVWKQ GHRKTTLKDY TAGVKTCLWY QRKSGDVTTF
     IGNTIIIAAC LSSMIPMDKV IKAAFCGDDS LIYIPKGLDL PDIQAGANLM WNFEAKLFRK
     KYGYFCGRYV IHHDRGAIVY YDPLKLISKL GCKHIRDVVH LEELRESLCD VASNLNNCAY
     FSQLDEAVAE VHKTAVGGSF AFCSIIKYLS DKRLFRDLFF V