ID   RDRP_TMOB               Reviewed;        1616 AA.
AC   P90211; Q83484;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   03-AUG-2022, entry version 104.
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   Tobamovirus Ob.
OC   Viruses; Riboviria; Orthornavirae; Kitrinoviricota; Alsuviricetes;
OC   Martellivirales; Virgaviridae; Tobamovirus.
OX   NCBI_TaxID=31749;
OH   NCBI_TaxID=4097; Nicotiana tabacum (Common tobacco).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=8376970; DOI=10.1099/0022-1317-74-9-1939;
RA   Ikeda R., Watanabe E., Watanabe Y., Okada Y.;
RT   "Nucleotide sequence of tobamovirus Ob which can spread systemically in N
RT   gene tobacco.";
RL   J. Gen. Virol. 74:1939-1944(1993).
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. When readthrough of the
CC       terminator codon TGA occurs between the codons for Ala-1115 and Gln-
CC       1117, this results in the addition of 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; D13438; BAA02700.1; -; Genomic_RNA.
DR   EMBL; D13438; BAA02701.1; -; Genomic_RNA.
DR   PIR; JQ2144; JQ2144.
DR   RefSeq; NP_620841.1; NC_003852.1.
DR   RefSeq; NP_620842.1; NC_003852.1.
DR   IntAct; P90211; 1.
DR   GeneID; 944437; -.
DR   GeneID; 944438; -.
DR   KEGG; vg:944437; -.
DR   KEGG; vg:944438; -.
DR   Proteomes; UP000008248; 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; Reference proteome; RNA suppression of termination;
KW   RNA-directed RNA polymerase; Suppressor of RNA silencing; Transferase;
KW   Viral RNA replication.
FT   CHAIN           1..1616
FT                   /note="Replicase large subunit"
FT                   /id="PRO_0000041188"
FT   CHAIN           1..1115
FT                   /note="Replicase small subunit"
FT                   /id="PRO_0000041189"
FT   DOMAIN          72..281
FT                   /note="Alphavirus-like MT"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01079"
FT   DOMAIN          800..962
FT                   /note="(+)RNA virus helicase ATP-binding"
FT   DOMAIN          963..1115
FT                   /note="(+)RNA virus helicase C-terminal"
FT   DOMAIN          1385..1498
FT                   /note="RdRp catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT   REGION          50..466
FT                   /note="Methyltransferase"
FT   REGION          828..1084
FT                   /note="Helicase"
FT   BINDING         832..839
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   1616 AA;  182999 MW;  14E6BD679AA46575 CRC64;
     MAHIQQSMQG ALLDTVRGQN SLVNDLAKRR LYDTAVEEFN AKDRRPKINF SKSINEEQTL
     IVSQAYPEFQ ITFYNTQLAV HSLAAGLRSL ELEYLMMQVP YGSLTYDIGG NFAAHLFKGR
     DYVHCCMPNL DLRDIMRHEN QKDSVATYLS RLKARNKVLP AFQQEAFQRY SERSDEVVCN
     NTFQCCESNR YSSGGRVYAI SLHSLYDIPA DELGAALLRK NVHTLYAAFH FAEELLLEVS
     TVELPTIGGI FSRDGDKINF CFSNESTLNY SHSYSNLLKY VCKTYFPASN RFVYMKEFLI
     TRVNTWFCKF TKLDTYTLYR GVYHRGCDQQ EFYSAMEDAW HYKKTLAMLN SERIVLEDHS
     SVNYWFPKMK DMVIVPLFDV SLETQKRTKK EVIVSKDFVY TVLNHIRTYQ AKALTYNNVL
     SFVESIRSRV IINGVTARSE WDVDKALLQS MAMTFFLITK LSMLKDELLV SKFTLSAKSV
     HEHVWDEIKR GCGNMFPSLK ESLLRKKLIS GSAEELEIEV PDMYVTFHDR FVAEYKASVE
     MPTIDISKDL SEAESYYSAL SELSVLENSK DFDLEKFSRM CAINCVNPDI AAKIVVAVLS
     NESGVTLPFK EPTEGNMAEA MKSGEKDEVL TLGSQTDNTD LTSKSMVISG SLPLCGIASE
     ISCDTFVRNE EINSLEEYHM LAAESVISNK MASIVYSGPL QVQQMQNYVD SLAASLSATV
     SNLKKLVKDS SVGFQDSLSK VGVFDVRKKM WLIKPTLKNH SWGVVQKFDG KCFLALLSYH
     NELPICDADW SKVAVSNESM VYSDMAKLRV LRKSIGEMPI SVSSAKVTLV DGVPGCGKTK
     EILRRVNFSE DLVLVPGKEA AAMIRKRANQ SGNIVANNDN VKTVDSFLMN LGKGPVCQFK
     RLFVDEGLML HPGCVYFLVK LSLCNEAFVF GDTQQIPYIN RVQNFPFPQH FSKLIVDETE
     KRRTTLRCPV DVTHFLNQCY DGAVTTTSKT QRSVGLEVVG GAAVMNPVTK PLKGKIVTFT
     QSDKLTMLSR GYQDVNTVHE IQGETYEEVS LVRLTPTPIH IISRESPHVL VGLTRHTRCF
     KYYTVVLDPL VKLVRDLECV SNFLLDVYMV DSVSAXQLQV SGVYLAENLF VQAPKSGDAQ
     DLQFYYDKCL PGNSTVLNEF DAVTMNCSDI SLNVKDCVLD FSKSVPLPRD NTKVPMTPVI
     RTAAERPRSQ GLLENLVAMI KRNFNSPELS GTVDMENTAS VVADRFFDSY FLKDKLSGCS
     LGDSGGKNII DRQALIRWME KQEKSTIGQL ADYDFVDLPA IDQYRHIIKS QPKQKLDLSI
     QSEYPSLQTI VYHSKKINAL FGPIFSELTR QMLSAIDTSR YLFFTRKTPE QIEEFFSDLD
     AHQPMEVLEL DVSKYDKSQN EFHCAVEYEI WKRLGIDEFL AEVWKQGHRK TTLKDYTAGI
     KTCLWYQRKS GDVTTFIGNT VIIAACMASM LPMEKVIKAA FCGDDSLVYL PKGCELPNIQ
     SCANLMWNFE AKLFKKTYGY FCGRYVIHHD RGAIVYVDPL KIISKLGAKH ITDKEHLEEF
     RISLADVSKS LNNCAYYAQL DEAVREVHKT APPGSFVYKC IVKFLSNRVL FESLFF