RDRP_PMTVS
ID RDRP_PMTVS Reviewed; 1812 AA.
AC Q9QBU0;
DT 31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 31-MAY-2011, sequence version 3.
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 Potato mop-top virus (isolate Potato/Sweden/Sw) (PMTV).
OC Viruses; Riboviria; Orthornavirae; Kitrinoviricota; Alsuviricetes;
OC Martellivirales; Virgaviridae; Pomovirus.
OX NCBI_TaxID=652839;
OH NCBI_TaxID=4112; Solanum nigrum (Black nightshade).
OH NCBI_TaxID=4113; Solanum tuberosum (Potato).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=10573175; DOI=10.1099/0022-1317-80-10-2779;
RA Savenkov E.I., Sandgren M., Valkonen J.P.;
RT "Complete sequence of RNA 1 and the presence of tRNA-like structures in all
RT RNAs of Potato mop-top virus, genus Pomovirus.";
RL J. Gen. Virol. 80:2779-2784(1999).
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 1303-Lys and 1305-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}.
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DR EMBL; AJ238607; CAB58364.1; -; Genomic_RNA.
DR Proteomes; UP000006715; 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; 2.
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..1812
FT /note="Replicase large subunit"
FT /id="PRO_0000409453"
FT CHAIN 1..1303
FT /note="Replicase small subunit"
FT /id="PRO_5000065197"
FT DOMAIN 79..306
FT /note="Alphavirus-like MT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01079"
FT DOMAIN 979..1140
FT /note="(+)RNA virus helicase ATP-binding"
FT DOMAIN 1141..1303
FT /note="(+)RNA virus helicase C-terminal"
FT DOMAIN 1565..1678
FT /note="RdRp catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT REGION 58..820
FT /note="Methyltransferase"
FT REGION 702..737
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 778..799
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1010..1272
FT /note="Helicase"
FT COILED 543..573
FT /evidence="ECO:0000255"
FT COMPBIAS 722..737
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 1014..1021
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1812 AA; 206364 MW; 97AF2F9BC94D0CFF CRC64;
MDQSILSKIT SDDYVNAILH TSATRVGSDL HNAMCNVIVD QIKDSTEKNK KKKKIDVKRN
LNEDQIQLLA ELFPERRVVT SSVHRGTHSM AAAMRKIETD VIFTSFPKNG VIYDIGGNWA
THAKRDDGGF VHCCCPILDF RDAQRKMTRL IDFNRFIDDA KVVSAEKAAV AAQIKKDCDL
ISENAKKDAY DANDLNGTWF CQNKFEDCVY DHSTLGDGKK EAYGMAIHSI YDIHLVDLVS
AMERKKVRVL KGTFLFSADI IIGKKRGELP SVNGFYIIDG ESIKYSFYDD PNCGYEHNLN
SLMLYVTKTF VKAAGGAVYY LELTEMRGDT MFFTITDASE ARVMGVLHDS STKCLPLNKR
DLVVFPLFDI DRATDELVFR EELLSREFVN RALEYAFQLK DNQVTAEGLI SYFASTNNAV
VIGGSARKTS EKVDPKLLPM ITTTLMVYQE LQKAKQKRVL GKLKSKVKEE LTLSGILESV
VHRVFGRQSL YQRGLGVFAK WMQYSYGQDL VGIHDVPLYL EINDRIKLGS ALKNVNGFSL
SFSELDEKVS LYEEYERERQ RISDEIVSEK IGLIGEGYVK VGESSLKPKQ KVASRDGMAQ
WVSGECHLYN TMKCEEKPVE KPRRFSKVVL EEWISEGNCF ALNNSFGDEV HWFDSLKEAC
GRAWRKQVSA VTFSDAEYFD NIENTENEEL EEEEVIKTTE QVEQDWPIGN LPDVDPDDSA
SAQVCLTESA STSSDEDCDP MEQLIVAACE RAFATKKFEE VTMDSQVVQS EEIEIVREGE
HAHANLSSGE SESSSQSQEL VAVGSVPLSK WAQMVEDSEV RARQCAVDHD LSWDEVKYAK
MPERPEEAEG DDFRTKAKRE FLWYLKCKLV ADKSTLVEIM RDFIYGQFHS GACETPKNAC
FLSYEKNVCG EWMFGKRYRH PSKGASSYAV RFTREDWKRA KLIKLQWKNA KAEENGEMSS
DNSDKPIVPQ GETGIYLFCD ITFLMNEIPI LNRLEISFKK RVQRRAPRIT LVDGVPGCGK
STYVVKEANL VNQYVVTIGR EAAEDLRERF KSERNATATQ LKRVRTVDSY LLNDTQSRAN
VLHFDEALMA HAGMVYFCAD DLSARSVICQ GDSQQIPFIN RVESITLRYS KLEIDNVVEK
RLTYRSPLDV ASYLTKKNFY GTSVVTSANP LVRSLKTVGP RDGMTSIYSI PKIPGTQYLT
FLQSEKEEMR QYLGRGNWNV NTVHESQGKT YDNVVLCRLK ATDNEIYPGG RNSSPYMVVG
VTRHRRSLVY YTKAEDKLYF DLAEMLSVQE GKLMKHLHEE GVKXRQASKY EEIMVSDNAV
TVPDVGNLVD LQEMYDIAFP GNSIVDTYFD GYEVATGGLQ IDMNASLTYY PNRQMKMWKE
CRGMYPMLRT AMPEKRQSGL AEGLLALNKR NMAAPKLQES VNEFEVIEST IEKAKKVFFD
ESRIDNSKLE TFEGAARWWV KQSCTAQKQM LADVRTLSEI DVTSYNFMIK GDVKPKLDLS
PQSEYSALQT VVYPDKIVNA LFGPIMKEIN ERIRVALKPH VIYNTRMTSD ELDPAVEFLD
VREDHESVEI DFSKFDKSKT SLHIRVVIEL YKLFGLDEMI AYLWEKSQCQ TTIKDRVNGI
IAQILYQQES GNCDTYGSNT WSAALSLLES LPLEKATFMI FGGDDSLIFF PKGMVIEDPC
RRLASMWNFD CKLFNFKNNS FCGKFLIKVG EKYKFAPDPY KLLTKLGRKD IKNSDLLSEI
FTSIGDNYKS YDDYRVLEAL NVAVMERYKL RCDVMFGLLA LKKYINSFDL FASLFSHKGR
YQRVEVGRNF EW
