RDRP_PCV87
ID RDRP_PCV87 Reviewed; 1672 AA.
AC Q84687;
DT 31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 31-MAY-2011, sequence version 2.
DT 03-AUG-2022, entry version 89.
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=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=Methyltransferase/RNA helicase;
GN Name=rep; ORFNames=ORF1-1bis;
OS Peanut clump virus (isolate 87/TGTA2) (PCV).
OC Viruses; Riboviria; Orthornavirae; Kitrinoviricota; Alsuviricetes;
OC Martellivirales; Virgaviridae; Pecluvirus.
OX NCBI_TaxID=652837;
OH NCBI_TaxID=3818; Arachis hypogaea (Peanut).
OH NCBI_TaxID=4555; Setaria italica (Foxtail millet) (Panicum italicum).
OH NCBI_TaxID=91525; Sorghum arundinaceum.
OH NCBI_TaxID=4558; Sorghum bicolor (Sorghum) (Sorghum vulgare).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=7964624; DOI=10.1099/0022-1317-75-11-3147;
RA Herzog E., Guilley H., Manohar S.K., Dollet M., Richards K., Fritsch C.,
RA Jonard G.;
RT "Complete nucleotide sequence of peanut clump virus RNA 1 and relationships
RT with other fungus-transmitted rod-shaped viruses.";
RL J. Gen. Virol. 75:3147-3155(1994).
RN [2]
RP REVIEW.
RX PubMed=19862474; DOI=10.1007/s00705-009-0506-6;
RA Adams M.J., Antoniw J.F., Kreuze J.;
RT "Virgaviridae: a new family of rod-shaped plant viruses.";
RL Arch. Virol. 154:1967-1972(2009).
CC -!- FUNCTION: [Replicase large subunit]: Is an RNA-dependent RNA polymerase
CC active in viral RNA replication. {ECO:0000250}.
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).
CC {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: The replicase large subunit is translated as a fusion
CC protein by episodic readthrough of a termination codon. When
CC readthrough of the terminator codon TGA occurs between the codons for
CC 1145-Lys and 1147-Arg, this results in the addition of the RdRp region.
CC -!- SIMILARITY: Belongs to the ssRNA positive-strand viruses RNA-directed
CC RNA polymerase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA55335.1; Type=Erroneous translation; Note=Readthrough in 1146.; Evidence={ECO:0000305};
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DR EMBL; X78602; CAA55335.1; ALT_SEQ; Genomic_RNA.
DR PRIDE; Q84687; -.
DR Proteomes; UP000001668; 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:UniProtKB-KW.
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 InterPro; IPR013664; Virgavirus_MeTrfase_C.
DR Pfam; PF00978; RdRP_2; 1.
DR Pfam; PF01443; Viral_helicase1; 1.
DR Pfam; PF01660; Vmethyltransf; 1.
DR Pfam; PF08456; Vmethyltransf_C; 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; Coiled coil; Helicase; Hydrolase; Methyltransferase;
KW Nucleotide-binding; Nucleotidyltransferase; Reference proteome;
KW RNA-binding; RNA-directed RNA polymerase; Transferase;
KW Viral RNA replication.
FT CHAIN 1..1672
FT /note="Replicase large subunit"
FT /id="PRO_0000409146"
FT CHAIN 1..1145
FT /note="Replicase small subunit"
FT /id="PRO_0000409147"
FT DOMAIN 85..306
FT /note="Alphavirus-like MT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01079"
FT DOMAIN 823..982
FT /note="(+)RNA virus helicase ATP-binding"
FT DOMAIN 983..1145
FT /note="(+)RNA virus helicase C-terminal"
FT DOMAIN 1406..1519
FT /note="RdRp catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT REGION 64..801
FT /note="Methyltransferase"
FT /evidence="ECO:0000255"
FT REGION 853..1113
FT /note="Helicase"
FT /evidence="ECO:0000255"
FT COILED 547..575
FT /evidence="ECO:0000255"
FT BINDING 856..863
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1672 AA; 191375 MW; F6E0D9E37273DDB3 CRC64;
MAQSNIYSDM IDRYVNDETV VQNLFMTASS TTKSLLHDVI ADRAANHLKS LEKKQKQKEL
VDVRRVLSSE SLNALCALYP EFHVITSNCE RGSHTMAAVC RTLETLYIKS LLPVKHTVVW
DVGGNWLTHV KYASDQNVHC CCPLLDYRDA MRKQERLLSL ELFARNGKEK TEEFDECYKQ
IKAFELQRRA ALNAGTAASC NNKYCCDVFQ DCAYEPEEGK MRVAMGVHSV YDMTLQDLVN
GLERKGIEHF IGCFLFSPKL LLGQEEGELP FVNGRFKVKK GKIRFFFLDD TTHGYEHDLN
DYLDYIKKSF VVAKCGHVYM LELFSVRGDT IFFKLYDVTE YSLSRTRLLS SLLPTRDHVF
KAMPIPNTEE VIVPLYWIEN GEVVVERRYL PKSLVCRGME WLMRNKANAL QYETLLNYLV
STNVSAVFNG CQVREGLKTD PWILCKLAMT LLVREEFNRE KQKKILEMLR MSGSEQISLK
SIFRGVFVKF FGSVSLKARV LKTVARWCGV EFGSMKYDVE VLPLYVEIED SLCLWRKGRL
EGIESYDMKD EVLRYNEKKQ DVERLTRSLE QKVNDGSASD TSSKLKKVAA FAVLASNKDT
PLGRFIASRS LSSVSKRSSS SDASHSGSGL SASEKVVSSE EIASPQISVS ESCVEEVPPM
IIPYTVKKRW ADYSSDSSED VVAGEDFMSP VSTLVLRRRL PAPPAYPDDV QEAACLEYLW
YLKCKIICDF SAMYSVVCDF KDQLLHDGRC EFPKNAFFLK VGEETKWAMK RPTSQQVGHQ
YCVKFSENDD HMELVPVAWS KHDDEIRGIY PQGLGDGWYM FSDLTYLMNE WLIFNKLVLV
YPSLPKTQLK VRLIDGVPGC GKSTWILSNC DLDRQIVLAE GREATDDLRR RFTEKGFPKK
RCEERVRTVH SFMLKPLSRR FNSFHFDEAL MAHAGMIYIC GRMLNAREVI CQGDSKQIPF
INRVEQISLK YSSFNVVERE HVRKTYRCPL DIVYYLNKKK YYRGDDIVGY SKTTHSVDTK
SKSSGFTSLV KLPKEPVHYL TFLQAEKEEV SKHLAGVKGA TVSTVHEAQG KTFERVNLVR
LKMTDNELYP GGAKSEPYTI VGLTRHTRSL VYYSVVEDRL YEDISALKDV MEDQLLKCSF
SEQTKXRFGS KFESIVVADR KVMAPDVGDL VTIQDLYDRT FPGNSTLDSS FDGYTVASSD
LELEISNCKI APNKSIRGFQ EKICFSPKLR TAMPEKRQGS FAESILALRK RNMACPRLQE
SVNEHQIIED TIAKAFSCYF TDSFVDQSPL ITDESALRWW EKQSTTAKNQ MLADWRTLDQ
IDVCTYNFMI KNDVKPKLDL TPQSEYAALQ TVVYPEKIVN GLFGPVIKEI NERVLSALKP
NVFVNTRMTS EELSRTAEYL YPGDEFEVVE IDFSKYDKSK TSLHIRMVIK LYEQFGLNGY
MKYLWEKSQT QTVVKDRNYG VEAYILYQQK SGNCDTYGSN TYSSMFALLD CLPMEKAVYS
IFGGDDSLIL FPKGTIINDP CGRLASLWNF DCKSMKFRVP AFCGKFLIPV GGRYRFEPDP
MKLITKLGNK TIAIEGKTKA EVRKNGSKLL SEIYVSICDN YKNYDDARVL DALAYALVDR
YKPDICPKAA LYSLSKFLKS FESFTELFDI YFNGERLAFD FVPVKVRKDY EW
