ID RDRP_TOMK1 Reviewed; 1616 AA.
AC Q9Q1T8; Q9Q1T7;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 2.
DT 27-MAR-2024, entry version 96.
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 Tomato mosaic virus (strain Kazakh K1) (ToMV) (TMV strain K1).
OC Viruses; Riboviria; Orthornavirae; Kitrinoviricota; Alsuviricetes;
OC Martellivirales; Virgaviridae; Tobamovirus; Tomato mosaic virus.
OX NCBI_TaxID=138311;
OH NCBI_TaxID=4151; Antirrhinum majus (Garden snapdragon).
OH NCBI_TaxID=4071; Capsicum (peppers).
OH NCBI_TaxID=46246; Delphinium.
OH NCBI_TaxID=4101; Petunia.
OH NCBI_TaxID=4081; Solanum lycopersicum (Tomato) (Lycopersicon esculentum).
OH NCBI_TaxID=13707; Tagetes (marigolds).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=10732356;
RA Belenovich E.V., Novikov V.K., Zavriev S.K.;
RT "Biological properties and genome structure of the Kazakh isolate K1 of
RT Tobacco Mosaic virus.";
RL Mol. Biol. (Mosk.) 34:172-176(2000).
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 Gln-1116 and Gln-
CC 1118, 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; AJ243571; CAB62911.1; -; Genomic_RNA.
DR EMBL; AJ243571; CAB62912.1; -; Genomic_RNA.
DR Proteomes; UP000008252; 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; IPR047310; Virgaviridae_RdRp.
DR Pfam; PF00978; RdRP_2; 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 3: Inferred from homology;
KW ATP-binding; Helicase; Host-virus interaction; Hydrolase;
KW Inhibition of host innate immune response by virus; Nucleotide-binding;
KW Nucleotidyltransferase; RNA suppression of termination;
KW RNA-directed RNA polymerase; Suppressor of RNA silencing; Transferase;
KW Viral immunoevasion; Viral RNA replication.
FT CHAIN 1..1616
FT /note="Replicase large subunit"
FT /id="PRO_0000041190"
FT CHAIN 1..1116
FT /note="Replicase small subunit"
FT /id="PRO_0000041191"
FT DOMAIN 72..281
FT /note="Alphavirus-like MT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01079"
FT DOMAIN 801..963
FT /note="(+)RNA virus helicase ATP-binding"
FT DOMAIN 964..1116
FT /note="(+)RNA virus helicase C-terminal"
FT DOMAIN 1380..1493
FT /note="RdRp catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT REGION 50..458
FT /note="Methyltransferase"
FT REGION 830..1085
FT /note="Helicase"
FT BINDING 833..840
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1616 AA; 183609 MW; 4BF9913CE791DE33 CRC64;
MAYTQTATSS ALLETVRGNN TLVNDLAKRR LYDTAVDEFN ARDRRPKVNF SKVVSEEQTL
IATKAYPEFQ ITFYNTQNAV HSLAGGLRSL ELEYLMMQIP YGSLTYDIGG NFASHLFKGR
AYVHCCMPNL DVRDIMRHEG QKDSIELYLS RLERGNKHVP NFQKEAFDRY AEMPNEVVCH
DTFQTCRHSQ ECYTGRVYAI ALHSIYDIPA DEFGAALLRK NVHVCYAAFH FSENLLLEDS
HVNLDEINAC FQRDGDRLTF SFASESTLNY SHSYSNILKY VCKTYFPASN REVYMKEFLV
TRVNTWFCKF SRIDTFLLYK GVAHKGVDNE QFYKAMEDAW HYKKTLAMCN SERILLEDSS
SVNYWFPKMR DMVIVPLFDI SLETSKRTRK EVLVSKDFVY TVLNHIRTYQ AKALTYSNVL
SFVESIRSRV IINGVTARSE WDVDKSLLQS LSMTFFLHTK LAVLKDDLLI SKFALGPKTV
SQHVWDEISL AFGNAFPSIK ERLINRKLIK ITENALEIRV PDLYVTFHDR LVSEYKMSVD
MPVLDIRKKM EETEEMYNAL SELSVLKTSD KFDVDVFSQM CQSLEVDPMT AAKVIVAVMS
NESGLTLTFE QPTEANVALA LQDSEKASDG ALVVTSRDVE EPSIRGSMAR GELQLAGLSG
DVPESSYTRS EEIESLEQFH MATASSLIHK QMCSIVYTGP LKVQQMKNFI DSLVASLSAA
VSNLVKILKD TAAIDLETRQ KFGVLDVASK RWLVKPSAKN HAWGVVETHA RKYHVALLEH
DEFGIITCDN WRRVAVSSES VVYSDMAKLR TLRRLLKDGE PHVSSAKVVL VDGVPGCGKT
KEILSRVNFE EDLILVPGRQ AAEMIRRRAN ASGIIVATKD NVRTVDSFLM NYGKGARCQF
KRLFIDEGLM LHTGCVNFLV EMSLCDIAYV YGDTQQIPYI NRVTGFPYPA HFAKLEVDEV
ETRRTTLRCP ADVTHFLNQR YEGHVMCTSS EKKSVSQEMV SGAASINPVS KPLKGKILTF
TQSDKEALLS RGYADVHTVH EVQGETYADV SLVRLTPTPV SIIARDSPHV LVSLSRHTKS
LKYYTVVMDP LVSIIRDLER VSSYLLDMYK VDAGTQXQLQ VDSVFKNFNL FVAAPKTGDI
SDMQFYYDKC LPGNSTLLNN YDAVTMKLTD ISLNVKDCIL DMSKSVAAPK DVKPTLIPMV
RTAAEMPRQT GLLENLVAMI KRNFNSPELS GVVDIENTAS LVVDKFFDSY LLKEKRKPNK
NFSLFSRESL NRWIAKQEQV TIGQLADFDF VDLPAVDQYR HMIKAQPKQK LDLSIQTEYP
ALQTIVYHSK KINAIFGPLF SELTRQLLDS IDSSRFLFFT RKTPAQIEDF FGDLDSHVPM
DVLELDVSKY DKSQNEFHCA VEYEIWRRLG LEDFLAEVWK QGHRKTTLKD YTAGIKTCLW
YQRKSGDVTT FIGNTVIIAS CLASMLPMEK LIKGAFCGDD SLLYFPKGCE YPDIQQAANL
MWNFEAKLFK KQYGYFCGRY VIHHDRGCIV YYDPLKLISK LGAKHIKDWD HLEEFRRSLC
DVAESLNNCA YYTQLDDAVG EVHKTAPPGS FVYKSLVKYL SDKVLFRSLF LDGSSC
//
