RDRP_PMMVS
ID RDRP_PMMVS Reviewed; 1612 AA.
AC P29098; Q84924;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 2.
DT 03-AUG-2022, entry version 100.
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 Pepper mild mottle virus (strain Spain) (PMMV-S).
OC Viruses; Riboviria; Orthornavirae; Kitrinoviricota; Alsuviricetes;
OC Martellivirales; Virgaviridae; Tobamovirus.
OX NCBI_TaxID=31745;
OH NCBI_TaxID=4072; Capsicum annuum (Capsicum pepper).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=1765765; DOI=10.1099/0022-1317-72-12-2875;
RA Alonso E., Garcia-Luque I., de la Cruz A., Wicke B., Avila-Rincon M.J.,
RA Serra M.T., Castresana C., Diaz-Ruiz J.R.;
RT "Nucleotide sequence of the genomic RNA of pepper mild mottle virus, a
RT resistance-breaking tobamovirus in pepper.";
RL J. Gen. Virol. 72:2875-2884(1991).
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-1117 and Gln-
CC 1119, 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; M81413; AAB02334.1; -; Genomic_RNA.
DR EMBL; M81413; AAB02335.1; -; Genomic_RNA.
DR PIR; JQ1312; WMTMPV.
DR RefSeq; NP_619740.1; NC_003630.1.
DR RefSeq; NP_619741.1; NC_003630.1.
DR GeneID; 1724827; -.
DR GeneID; 1724829; -.
DR KEGG; vg:1724827; -.
DR KEGG; vg:1724829; -.
DR Proteomes; UP000000476; 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..1612
FT /note="Replicase large subunit"
FT /id="PRO_0000041182"
FT CHAIN 1..1117
FT /note="Replicase small subunit"
FT /id="PRO_0000041183"
FT DOMAIN 72..280
FT /note="Alphavirus-like MT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01079"
FT DOMAIN 803..964
FT /note="(+)RNA virus helicase ATP-binding"
FT DOMAIN 965..1117
FT /note="(+)RNA virus helicase C-terminal"
FT DOMAIN 1380..1493
FT /note="RdRp catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT REGION 52..466
FT /note="Methyltransferase"
FT REGION 831..1086
FT /note="Helicase"
FT BINDING 835..842
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1612 AA; 183268 MW; 465677F4924802BF CRC64;
MAYTQQATNA ALASTLRGNN PLVNDLANRR LYESAVEQCN AHDRRPKVNF LRSISEEQTL
IATKAYPEFQ ITFYNTQNAV HSLAGGLRSL ELEYLMMQIP YGSTTYDIGG NFAAHMFKGR
DYVHCCMPNM DLRDVMRHNA QKDSIELYLS KLAQKKKVIP PYQKPCFDKY TDDPQSVVCS
KPFQHCEGVS HCTDKVYAVA LHSLYDIPAD EFGAALLRRN VHVCYAAFHF SENLLLEDSY
VSLDDIGAFF SREGDMLNFS FVAESTLNYT HSYSNVLKYV CKTYFPASSR EVYMKEFLVT
RVNTWFCKFS RLDTFVLYRG VYHRGVDKEQ FYSAMEDAWH YKKTLAMMNS ERILLEDSSS
VNYWFPKMKD MVIVPLFDVS LQNEGKRLAR KEVMVSKDFV YTVLNHIRTY QSKALTYANV
LSFVESIRSR VIINGVTARS EWDVDKALLQ SLSMTFFLQT KLAMLKDDLV VQKFQVHSKS
LTEYVWDEIT AAFHNCFPTI KERLINKKLI TVSEKALEIK VPDLYVTFHD RLVKEYKSSV
EMPVLDVKKS LEEAEVMYNA LSEISILKDS DKFDVDVFSR MCNTLGVDPL VAAKVMVAVV
SNESGLTLTF ERPTEANVAL ALQPTITSKE EGSLKIVSSD VGESSIKEVV RKSEISMLGL
TGNTVSDEFQ RSTEIESLQQ FHMVSTETII RKQMHAMVYT GPLKVQQCKN YLDSLVASLS
AAVSNLKKII KDTAAIDLET KEKFGVYDVC LKKWLVKPLS KGHAWGVVMD SDYKCFVALL
TYDGENIVCG ETWRRVAVSS ESLVYSDMGK IRAIRSVLKD GEPHISSAKV TLVDGVPGCG
KTKEILSRVN FDEDLVLVPG KQAAEMIRRR ANSSGLIVAT KENVRTVDSF LMNYGRGPCQ
YKRLFLDEGL MLHPGCVNFL VGMSLCSEAF VYGDTQQIPY INRVATFPYP KHLSQLEVDA
VETRRTTLRC PADITFFLNQ KYEGQVMCTS SVTRSVSHEV IQGAAVMNPV SKPLKGKVIT
FTQSDKSLLL SRGYEDVHTV HEVQGETFED VSLVRLTPTP VGIISKQSPH LLVSLSRHTR
SIKYYTVVLD AVVSVLRDLE CVSSYLLDMY KVDVSTQXQL QIESVYKGVN LFVAAPKTGD
VSDMQYYYDK CLPGNSTILN EYDAVTMQIR ENSLNVKDCV LDMSKSVPLP RESETTLKPV
IRTAAEKPRK PGLLENLVAM IKRNFNSPEL VGVVDIEDTA SLVVDKFFDA YLIKEKKKPK
NIPLLSRASL ERWIEKQEKS TIGQLADFDF IDLPAVDQYR HMIKQQPKQR LDLSIQTEYP
ALQTIVYHSK KINALFGPVF SELTRQLLET IDSSRFMFYT RKTPTQIEEF FSDLDSNVPM
DILELDISKY DKSQNEFHCA VEYEIWKRLG LDDFLAEVWK HGHRKTTLKD YTAGIKTCLW
YQRKSGDVTT FIGNTIIIAA CLSSMLPMER LIKGAFCGDD SILYFPKGTD FPDIQQGANL
LWNFEAKLFR KRYGYFCGRY IIHHDRGCIV YYDPLKLISK LGAKHIKNRE HLEEFRTSLC
DVAGSLNNCA YYTHLNDAVG EVIKTAPLGS FVYRALVKYL CDKRLFQTLF LE
