RDRP_TBRFV
ID RDRP_TBRFV Reviewed; 1615 AA.
AC A0A0S2T050; A0A0S2T034;
DT 11-DEC-2019, integrated into UniProtKB/Swiss-Prot.
DT 17-FEB-2016, sequence version 1.
DT 03-AUG-2022, entry version 37.
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 brown rugose fruit virus (isolate TOBRFV/Tomato/Jordan/Tom1-Jo/2015)
OS (ToBRFV).
OC Viruses; Riboviria; Orthornavirae; Kitrinoviricota; Alsuviricetes;
OC Martellivirales; Virgaviridae; Tobamovirus.
OX NCBI_TaxID=2654645;
OH NCBI_TaxID=4081; Solanum lycopersicum (Tomato) (Lycopersicon esculentum).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=26586328; DOI=10.1007/s00705-015-2677-7;
RA Salem N., Mansour A., Ciuffo M., Falk B.W., Turina M.;
RT "A new tobamovirus infecting tomato crops in Jordan.";
RL Arch. Virol. 161:503-506(2016).
CC -!- FUNCTION: [Replicase large subunit]: Is an RNA-dependent RNA polymerase
CC active in viral RNA replication. {ECO:0000250|UniProtKB:P03586}.
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. It also acts as a
CC 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. {ECO:0000250|UniProtKB:P03586}.
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 Evidence={ECO:0000250|UniProtKB:P03586};
CC -!- SUBUNIT: Heterodimer of a large and a small subunit.
CC {ECO:0000250|UniProtKB:P03586}.
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 {ECO:0000250|UniProtKB:P03586}.
CC -!- SIMILARITY: Belongs to the ssRNA positive-strand viruses RNA-directed
CC RNA polymerase family. {ECO:0000305}.
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DR EMBL; KT383474; ALP48477.1; -; Genomic_RNA.
DR EMBL; KT383474; ALP48476.1; -; Genomic_RNA.
DR RefSeq; YP_009182168.1; NC_028478.1.
DR RefSeq; YP_009182169.1; NC_028478.1.
DR GeneID; 26373865; -.
DR GeneID; 26373868; -.
DR KEGG; vg:26373865; -.
DR KEGG; vg:26373868; -.
DR Proteomes; UP000203541; 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-directed RNA polymerase;
KW Suppressor of RNA silencing; Transferase; Viral RNA replication.
FT CHAIN 1..1615
FT /note="Replicase large subunit"
FT /id="PRO_0000448837"
FT CHAIN 1..1116
FT /note="Replicase small subunit"
FT /evidence="ECO:0000250|UniProtKB:P03586"
FT /id="PRO_0000448838"
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 /evidence="ECO:0000255|PROSITE-ProRule:PRU00990"
FT DOMAIN 964..1116
FT /note="(+)RNA virus helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00990"
FT DOMAIN 1380..1493
FT /note="RdRp catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT BINDING 833..840
FT /ligand="a ribonucleoside 5'-triphosphate"
FT /ligand_id="ChEBI:CHEBI:61557"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00990"
SQ SEQUENCE 1615 AA; 183368 MW; 9C9D9869833B2428 CRC64;
MAYTQTATTS ALLDTVRGNN TLVNDLAKRR LYDTAVDEFN ARDRRPKVNF SKVISEEQTL
IATRAYPEFQ ITFYNTQNAV HSLAGGLRSL ELEYLMMQIP YGSLTYDIGG NFASHLFKGR
AYVHCCMPNL DVRDIMRHEG QKDSIELYLS RLERGNKVVP NFQKEAFDRY AETPDEVVCH
STFQTCTHQQ VENTGRVYAI ALHSIYDIPA DEFGAALLRK NVHVCYAAFH FSENLLLEDS
HVNLDEINAC FSRDGDKLTF SFASESTLNY CHSYSNILKY VCKTYFPASN REVYMKEFLV
TRVNTWFCKF SRIDTFLLYK GVAHKGVNSE QFYSAMEDAW HYKKTLAMCN SERILLEDSS
SVNYWFPKMR DMVIVPLFDI SLDTSKRTRK EVLVSKDFVF TVLNHIRTYQ AKALTYSNVL
SFVESIRSRV IINGVTARSE WDVDKSLLQS LSMTFFLHTK LAVLKDELLI SKFSLGPKSV
SQHVWDEISL AFGNAFPSIK ERLLNRKLIK VSGDALEIRV PDLYVTFHDR LVTEYKTSVD
MPVLDIRKRM EETEVMYNAL SELSVLKESD KFDVDVFSRM CQTLEVDPMT AAKVIVAVMS
NESGLTLTFE QPTEANVALA LKDSEKASEG ALVVTSRDVE EPSMKGSMAR GELQLAGLSG
DQPESSYTRN EEIESLEQFH MATASSLIRK QMSSIVYTGP IKVQQMKNFI DSLVASLSAA
VSNLVKILKD TAAIDLETRQ KFGVLDVATK RWLIKPLAKN HAWGVIETHA RKYHVALLEY
DEHGVVTCDS WRRVAVSSES MVYSDMAKLR TLRRLLRDGE PHVSSAKVVL VDGVPGCGKT
KEILSKVNFE EDLILVPGKQ AAEMIKRRAN ASGIIQATRD NVRTVDSFIM NYGKGTRCQF
KRLFIDEGLM LHTGCVNFLV SMSLCEIAYV YGDTQQIPYI NRVSGFPYPA HFAKIEVDEV
ETRRTTLRCP ADITHYLNRR YEGYVMCTSS VKKSVSQEMV SGAAMINPVS KPLNGKVLTF
TQSDKEALLS RGYTDVHTVH EVQGETYADV SLVRLTPTPV SIIAGDSPHV LVALSRHTQT
LKYYTVVMDP LVSIIRDLEK LSSYLLDMYK VDAGTQXQLQ VDSVFKGSNL FVAAPKTGDI
SDMQFYYDKC LPGNSTMLNN YDAVTMRLTD ISLNVKDCIL DFSKSVAAPK DPIKPLIPMV
RTAAEMPRQT GLLENLVAMI KRNFNSPELS GIIDIENTAS LVVDKFFDSY LLKEKRKPNK
NVSLFCRESL NRWLEKQEQV TIGQLADFDF VDLPAVDQYR HMIKAQPKQK LDTSIQSEYP
ALQTIVYHSK KINAIFGPLF SELTRQMLES IDSSKFLFFT RKTPAQIEDF FGDLDSHVPM
DILELDISKY DKSQNEFHCA VEYEIWRRLG LEDFLGEVWK QGHRKTTLKD YTAGIKTCLW
YQRKSGDVTT FIGNTVIIAA CLASMLPMEK IIKGAFCGDD SLLYFPKGCE FPDIQHTANL
MWNFEAKLFR KQYGYFCGRY VIHHDRGCIV YYDPLKLISK LGAKHIKDWD HLEEFRRSLC
DVANSLNNCA YYTQLDDAVS EVHKTAPPGS FVYKSLVKYL SDKVLFRSLF IDGSC
