ID   RDRP_ORSVS              Reviewed;        1612 AA.
AC   Q84133;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2000, sequence version 2.
DT   03-AUG-2022, entry version 98.
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   Odontoglossum ringspot virus (isolate Singapore 1) (ORSV).
OC   Viruses; Riboviria; Orthornavirae; Kitrinoviricota; Alsuviricetes;
OC   Martellivirales; Virgaviridae; Tobamovirus.
OX   NCBI_TaxID=138662;
OH   NCBI_TaxID=14366; Cymbidium.
OH   NCBI_TaxID=154697; Odontoglossum.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=8666266; DOI=10.1016/0378-1119(96)00046-7;
RA   Chng C.G., Wong S.M., Mahtani P.H., Loh C.S., Goh C.J., Kao M.C.C.,
RA   Chung M.C.M., Watanabe Y.;
RT   "The complete sequence of a Singapore isolate of odontoglossum ringspot
RT   virus and comparison with other tobamoviruses.";
RL   Gene 171:155-161(1996).
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 Leu-1112 and Gln-
CC       1114, 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; U34586; AAC55012.2; -; Genomic_RNA.
DR   PRIDE; Q84133; -.
DR   Proteomes; UP000008384; 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; Reference proteome; 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_0000041178"
FT   CHAIN           1..1112
FT                   /note="Replicase small subunit"
FT                   /id="PRO_0000041179"
FT   DOMAIN          72..280
FT                   /note="Alphavirus-like MT"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01079"
FT   DOMAIN          794..953
FT                   /note="(+)RNA virus helicase ATP-binding"
FT   DOMAIN          954..1112
FT                   /note="(+)RNA virus helicase C-terminal"
FT   DOMAIN          1374..1487
FT                   /note="RdRp catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT   REGION          50..452
FT                   /note="Methyltransferase"
FT   REGION          822..1080
FT                   /note="Helicase"
FT   BINDING         826..833
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   1612 AA;  183196 MW;  3B444670B0ACB189 CRC64;
     MAHFQQTMNN KVIEAGMGRN SLINDLAQRR VYDNAVEELN HRSRRPRVNF SKVISQEQII
     QATNAYPEFE ITFYNTQLAV HSMAGGLRAL ELEYLMMQIP FGSITYDIGG NFSAHLYKGR
     DYVHCCMPNL DIRDVARHIN QQDTVSTYLA RLERSKRGLP VFQQSAFNKY MNDPDAVCCD
     KRFQDCSYSA GLPGKTYAVG LHSIYDIPAD EFGAALLRKD VHICYAAFHF SENLLLETTS
     APLDEIGATF YKSGDRLSFF FQNESTLNYE HSYKNVIKYV CKTFFPASNR FVYHKEFMCT
     RVNTWFCKFT KVDTYFLFRG VYTRGEDSEQ FYTAMDEAWE YKKTLAMLNS ERTIFRDRAA
     VNFWFPKVKD MVIVPLFDGS VTSGKMKRSE VMVNKDFVYT VLNHIRTYQD KALTYKNVLS
     FVESIRSRVI INGVTARSEW DVDKSVLQAL SMTFLLQTKL AEAKDQVVLK KFQKFDDTVT
     NLFWKQISDA VGDLFPSIKE RLISGGFVKV AEQSLQIKTP DEYITPADKL VMEYQATEEL
     QHLDISKPLE RAEKYYNALS ELSVLKECDE FDITQFKNLC EEKDIAPDVV AKVIVPIMKN
     ELTLPFKNPT PEALSDALSP LPKDLDMRFC LLKLSTCAPF PSVKTLDSGL LPKQSYGDER
     QFESQSVVSV SDFHLKSVES VKMKSMSSAV YTGPLKVQQM KNYMDYLSAS ISATVSNLCK
     VLKDVYGADP ESAEKSGVYD VVKGKWLLKP KDKCHAWGVA ELNNGEKVIV LLEWADGFPI
     CGDWRRVAVS SDSPIYSDMG KLQTLLSCLK DGEPVLRMPK VTLVDGVPGC GKTKEILETV
     NFDEDLILVP GKEACKMIIK RANKSGHVRA TRDNVRTVDS FLMHLKPKTY NKLFIDEGLM
     LHTGCVNFLV ALSHCREAMV FGDAEQIPFI NRVANFPYPK HFRYTCLYHR EVRRLSLRCP
     ADVTHFMNSK YDGKVLCTND VIRSVDAEVV RGKGVFNPKS KPLKGKIITF TQSDKAELKE
     RGYEEVSTFG EINTVHEIQG ETFEDVSVVR LTPTPLELIS KSSPHVLVAL TRHTKSFKYY
     SVVLDPLVKV WSDLSKVSDF ILDMYKVDAG ILXQLQVGSI FKGENLFVPC PKSGYISDMQ
     TYYDTLVPGN STILNEYDAV TMNLRENNLN VKDCTIDFSK SVSVPRQQQE FFTPAHRTAA
     ERPRSAGLLE NLVAMIKRNF NSPDLTGILD IEDTAELVVN KFWDAYIIDE LSGGNVTPMT
     SDAFHRWMAK QEKSTIGQLA DFDFVDLPAI DQYKHMIKAQ PKQKLGLSPQ DEYAALQTIV
     YHSKQINAIF GPLFSELTRQ LLERIDSSKF LFYTRKTPEQ IEAFFSDLDS TVPMEVLELD
     ISKYDKSQNE FHCAVEYLIW EKLGLNGFLE EVWKQGHRKT SLKDYTAGIK TCLWYQRKSG
     DVTTFIGNTV IIAACLASMI PMDKVIKAAF CGDDSILYIP KGLDLPDIQS GANLMWNFEA
     KLYRKRYGYF CGRYIIHHDR GAIVYYDPLK LISKLGCKHI KSLDHLEEFR ISLCDVSSSL
     NNCAYFGQLN DAIAEVHKTA VNGSFAFCSI VKYLSDKNLF RTLFNNGSST KG