ID   RDRP_ORSVC              Reviewed;        1612 AA.
AC   P89659; O39640;
DT   01-DEC-2000, 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   Odontoglossum ringspot virus (isolate Korean Cy) (ORSV-Cy).
OC   Viruses; Riboviria; Orthornavirae; Kitrinoviricota; Alsuviricetes;
OC   Martellivirales; Virgaviridae; Tobamovirus.
OX   NCBI_TaxID=138661;
OH   NCBI_TaxID=14366; Cymbidium.
OH   NCBI_TaxID=154697; Odontoglossum.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=8789059; DOI=10.1111/j.1348-0421.1995.tb03289.x;
RA   Ikegami M., Isomura Y., Matsumoto Y., Chatani M., Inouye N.;
RT   "The complete nucleotide sequence of odontoglossum ringspot virus (Cy-1
RT   strain) genomic RNA.";
RL   Microbiol. Immunol. 39:995-1001(1995).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAB49498.2; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; D13941; BAA21828.1; -; Genomic_RNA.
DR   EMBL; S83257; AAB49498.2; ALT_INIT; Genomic_RNA.
DR   Proteomes; UP000007788; 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_0000041176"
FT   CHAIN           1..1112
FT                   /note="Replicase small subunit"
FT                   /id="PRO_0000041177"
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;  183255 MW;  3F803A2B9611E0DF CRC64;
     MAHFQQTMNN KVIEAGMGRN SLINDLAQRR VYDNAVEELN HRSRRPKVNF SKVISQEQII
     QATNAYPEFE ITFYNTQLAV HSMAGGLRAL ELEYLMMQIP FGSITYDIGG NFSAHLYKGR
     DYVHCCMPNL DIRDVARHIN QQDTVSTYLA RLERSKRGLP VFQQSAFNKY MNDPDAVCCD
     KRFQDCSYSV DLPGKTYAVA LHSIYDIPAD EFGAALLRKD VHICYAAFHF SENLLLETTS
     APLDEIGATF YKSGDRLSFF FQNESTLNYE HSYKNVIKYV CKTFFPASNR FVYHKEFMCT
     RVNTWFCKFT KVDTYFLFRG VYTRGEDSEQ FYTAMDEAWE YKKTLAMLKC ERTIFRDRAA
     VNFWFPKVKD MVIVPLFDGS VTSGKMKRSE VMVNKDFVYT VLNHIRTYQD KALTYKNVLS
     FVESIRSRVI INGVSARSEW DVDKSVLQAL SMTFLLQTKL AEAKDQVVLK KFQKFDDTVT
     NLFWKQISDA VGDLFPSIKE TLISGGFVKV AEQSLQIKTP DEYITFADKL VMEYKATEEL
     QHLDISKPLE RAEKYYNALS ELSVLKECDE FDITQFKNLC EEKDIDPDVV AKVIVAIMKN
     ELTLPFKNPT PEALSDALSP LPKDLDMRFD LLKLSTCAPF PSVKTLDSGL LPKQSYGDER
     QFESQSVVSV SDFHLKSVES VKMKSMSSAV YTGPLKVQQM KNYMDYLSAS ISATVSNLCK
     VLKDVYGADP ESAEKSGVYD VVKGKWLLKP KGKCHAWGVA ELNNGEKVIV LLEWADGFPI
     CGDWRRVAVS SDSLIYSDMG KLQTLLSCLK DGEPVPSDAK VTLVDGVPGC GKTKEILETV
     NFDEDLILVP GKEACKMIIK RANKSGHVRA TKDNVRTVDS FLMHLKPKTY NKLFIDEGLM
     LHTGCVNFLI ALSHCREAMV FGDTEQIPFI NRVANFPYPK HFATLVYDHR EVRRLSLRCP
     ADVTHFMNSK YDGKVLCTND VIRSVDAEVV RGKGVFNPKS KPLKGKIITF TQSDKAELKE
     RGYEEVSTFG EINTVHEIQG ETFEDVSVVR LTPTPLELIS KSSPHVLVAL TRHTKSFKYY
     SVVLDPLVKV CSDLSKVSDF ILDMYKVDAG ILXQLQVGSI FKGENLFVPC PKSGYISDMQ
     FYYDTLLPGN STILNEYDAV TMNLRENNLN VKDCTIDFSK SVSVPRQQQE FFTPVIRTAA
     ERPRSRGLLE NLVAMIKRNF NSPDLTGILD IEDTAELVVN KFWDAYIIDE LSGGNVTPMT
     SDAFHRWMAK QEKSTIGQLA DFDFVDLPAI DQYKHMIKAQ PKQKLDLSPQ DEYAALQTIV
     YHSKQINAIF GPLFSELTRQ LLERIDSSKF LFYTRKTPEQ IEEFFSDLDS TVPMEVLELD
     ISKYDKSQNE FHCAVEYLIW EKLGLNGFLE EVWKQGHRKT SLKDYTAGIK TCLWYQRKSG
     DVTTFIGNTV IIAACLASMI PMDKVIKAAF CGDDSMLYIP KGLDLPDIQS GANLMWNFEA
     KLYRKRYGYF CGRYIIHHDR GAIVYYDPVK LISKLGCKHI KSLDHLEEFR ISLCDVSASL
     NNCAYYGQLN DAIAEVHKTA VNGSFAFCSI VKYLSDKNLF RTLFYNGSST KG