RDRP_TMGMV
ID RDRP_TMGMV Reviewed; 1609 AA.
AC P18339; Q88596;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 2.
DT 03-AUG-2022, entry version 101.
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 Tobacco mild green mosaic virus (TMGMV) (TMV strain U2).
OC Viruses; Riboviria; Orthornavirae; Kitrinoviricota; Alsuviricetes;
OC Martellivirales; Virgaviridae; Tobamovirus.
OX NCBI_TaxID=12241;
OH NCBI_TaxID=4072; Capsicum annuum (Capsicum pepper).
OH NCBI_TaxID=43071; Eryngium planum.
OH NCBI_TaxID=4090; Nicotiana glauca (Glaucous tobacco) (Tree tobacco).
OH NCBI_TaxID=4097; Nicotiana tabacum (Common tobacco).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=2371769; DOI=10.1016/0042-6822(90)90520-2;
RA Solis I., Garcia-Arenal F.;
RT "The complete nucleotide sequence of the genomic RNA of the tobamovirus
RT tobacco mild green mosaic virus.";
RL Virology 177:553-558(1990).
RN [2]
RP INTERACTION WITH HOST PROTEIN TM-1, AND ACTIVITY REGULATION.
RX PubMed=19423673; DOI=10.1073/pnas.0809105106;
RA Ishibashi K., Naito S., Meshi T., Ishikawa M.;
RT "An inhibitory interaction between viral and cellular proteins underlies
RT the resistance of tomato to nonadapted tobamoviruses.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:8778-8783(2009).
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 -!- ACTIVITY REGULATION: In resistant plants, is bound by host protein Tm-1
CC (e.g tomato Tm-1 AC A7M6E7), thereby inhibiting replication complex
CC activity. {ECO:0000269|PubMed:19423673}.
CC -!- SUBUNIT: Heterodimer of a large and a small subunit (By similarity).
CC Both large and small subunits interact, via an ATP bridge, with host
CC protein Tm-1 (e.g. tomato Tm-1 AC A7M6E7 and AC A7M6E8)
CC (PubMed:19423673). {ECO:0000250, ECO:0000269|PubMed:19423673}.
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 Arg-1111 and Gln-
CC 1113, 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; M34077; AAA47934.2; -; Genomic_RNA.
DR EMBL; M34077; AAA47935.1; -; Genomic_RNA.
DR PIR; A35520; WMTMGM.
DR RefSeq; NP_062913.2; NC_001556.1.
DR RefSeq; NP_062914.1; NC_001556.1.
DR GeneID; 1494074; -.
DR GeneID; 1494075; -.
DR KEGG; vg:1494074; -.
DR KEGG; vg:1494075; -.
DR Proteomes; UP000000281; 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; SSF56672; SSF56672; 1.
DR PROSITE; PS51743; ALPHAVIRUS_MT; 1.
DR PROSITE; PS51657; PSRV_HELICASE; 1.
DR PROSITE; PS50507; RDRP_SSRNA_POS; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Helicase; Host-virus interaction; Hydrolase;
KW Nucleotide-binding; Nucleotidyltransferase; RNA suppression of termination;
KW RNA-directed RNA polymerase; Suppressor of RNA silencing; Transferase;
KW Viral RNA replication.
FT CHAIN 1..1609
FT /note="Replicase large subunit"
FT /id="PRO_0000041186"
FT CHAIN 1..1111
FT /note="Replicase small subunit"
FT /id="PRO_0000041187"
FT DOMAIN 72..281
FT /note="Alphavirus-like MT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01079"
FT DOMAIN 799..958
FT /note="(+)RNA virus helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00990"
FT DOMAIN 959..1111
FT /note="(+)RNA virus helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00990"
FT DOMAIN 1374..1487
FT /note="RdRp catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT REGION 50..453
FT /note="Methyltransferase"
FT REGION 828..1080
FT /note="Helicase"
FT BINDING 834..839
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P03587,
FT ECO:0000255|PROSITE-ProRule:PRU00990"
FT BINDING 866
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P03587"
FT BINDING 962..963
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P03587"
FT BINDING 1071
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P03587"
FT BINDING 1092..1095
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P03587"
SQ SEQUENCE 1609 AA; 182802 MW; B48F5695BAC0E3D2 CRC64;
MAHIQSIISN ALLESVSGKN TLVNDLARRR MYDTAVEEFN ARDRRPKVNF SKTISEEQTL
LVSNAYPEFQ ITFYNTQNAV HSLAGGLRAL ELEYLMLQVP YGSPTYDIGG NFAAHLFKGR
DYVHCCMPNL DIRDIMRHEG QKDSIEMYLS RLSRSNKVIP EFQREAFNRY AEAPNEVCCS
KTFQDCRIHP PENSGRRYAV ALHSLYDIPV HEFGAALISK NIHVCYAASI LAEALLLDQT
EVTLNEIGAT FKREGDDVSF FFADESTLNY SHKYKNILHY VVKSYFPASS RIVYFKEFLV
TRVNTWFCKF TKVDTYILYK SVRQVGCDSD QFYEAMEDAF AYKKTLAMFN TERAIFRDTA
SVNFWFPKMK DMVIVPLFEG SITSKKMTRS EVIVNRDFVY TVLNHIRTYQ AKALTYQNVL
SFVESIRSRV IINGVTARSE WDVDKAILQP LSMTFFLQTK LAALQDDIVM GKFRCLDKTT
SELIWDEVGK FFGNVFPTIK ERLVSRKILD VSENALKIKI PDLYVTWKDR FVAEYTKSEE
LPHLDIKKDL EEAEQMYDAL SELSILKGAD NFDIAKFKDM CKALDVSPDV AARVIVAVAE
NRSGLTLTFD KPTEENVAKA LKSTASEAVV CLEPTSEEVN VNKFSIAEKG RLPVCAESHG
LTNANLEHQE LESLNDFHKA CVDSVITKQM ASVVYTGSLK VQQMKNYVDS LAASLSATVS
NLCKSLKDEV GYDSDSREKV GVWDVTLKKW LLKPAAKGHS WGVVLDYKGK MFTALLSYEG
DRMVTESDWR RVAVSSDTMV YSDIAKLQNL RKTMRDGEPH EPTAKMVLVD GVPGCGKYKG
DFERFDLDED LILVPGKQAA AMIRRRANSS GLIRATMDNV RTVDSLLMHP KPRSHKRLFI
DEGLMLHTGC VNFLVLISGC DIAYIYGDTQ QIPFINRVQN FPYPKHFEKL QVDEVEMRRT
TLRCPGDVNF FLQSKYEGAV TTTSTVQRSV SSEMIGGKGV LNSVSKPLKG KIVTFTQADK
FELEEKGYKN VNTVHEIQGE TFEDVSLVRL TATPLTLISK SSPHVLVALT RHTKSFKYYT
VVLDPLVQII SDLSSLSSFL LEMYMVEAGS RXQLQMDAVF KGHNLFVATP KSGDFPDLQF
YYDVCLPGNS TILNKYDAVT MRLRDNSLNV KDCVLDFSKS IPMPKEVKPC LEPVLRTAAE
PPRAAGLLEN LVAMIKRNFN APDLTGTIDI ESTASVVVDK FFDSYFIKKE KYTKNIAGVM
TKDSMMRWLE NRKEVLLDDL ANYNFTDLPA IDQYKHMIKA QPKQKLDLSI QNEYPALQTI
VYHSKQINGI LAGFSELTRL LLEAFDSKKF LFFTRKTPEQ IQEFFSDLDS HVPMDVLELD
ISKYDKSQNE FHCAVEYEIW KRLGLNEFLA EVWKQGHRKT TLKDYIAGIK TCLWYQRKSG
DVTTFIGNTV IIAACLGSML PMEKVIKGAF CGDDSVLYFP KGLDFPDIQS CANLMWNFEA
KLYRKRYGYF CGRYIIHHDK GAIVYYDPLK LISKLGAKHI KDYDHLEELR VSLCDVACSL
GNWCLGFPQL NAAIKEVHKT AIDGSFAFNC VNKFLCDKFL FRTLFLNGC
