ID   RDRP_WCMVM              Reviewed;        1294 AA.
AC   P09498;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1989, sequence version 1.
DT   03-AUG-2022, entry version 108.
DE   RecName: Full=RNA replication protein;
DE   AltName: Full=147 kDa protein;
DE   AltName: Full=ORF1 protein;
DE   Includes:
DE     RecName: Full=RNA-directed RNA polymerase;
DE              EC=2.7.7.48;
DE   Includes:
DE     RecName: Full=Helicase;
DE              EC=3.6.4.13;
OS   White clover mosaic virus (strain M) (WCMV).
OC   Viruses; Riboviria; Orthornavirae; Kitrinoviricota; Alsuviricetes;
OC   Tymovirales; Alphaflexiviridae; Potexvirus.
OX   NCBI_TaxID=12189;
OH   NCBI_TaxID=3898; Trifolium.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=3340527; DOI=10.1093/nar/16.1.291;
RA   Forster R.L.S., Bevan M.W., Harbison S.-A., Gardner R.C.;
RT   "The complete nucleotide sequence of the potexvirus white clover mosaic
RT   virus.";
RL   Nucleic Acids Res. 16:291-303(1988).
CC   -!- FUNCTION: RNA replication. The central part of this protein possibly
CC       functions as an ATP-binding helicase (Probable). {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   -!- SIMILARITY: Belongs to the potexvirus/carlavirus RNA replication
CC       protein family. {ECO:0000305}.
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DR   EMBL; X06728; CAA29904.1; -; Genomic_RNA.
DR   PIR; S01085; S01085.
DR   RefSeq; NP_620715.1; NC_003820.1.
DR   GeneID; 944395; -.
DR   KEGG; vg:944395; -.
DR   Proteomes; UP000007627; 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; -; 1.
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; 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; Helicase; Hydrolase; Multifunctional enzyme;
KW   Nucleotide-binding; Nucleotidyltransferase; Reference proteome;
KW   RNA-directed RNA polymerase; Transferase; Viral RNA replication.
FT   CHAIN           1..1294
FT                   /note="RNA replication protein"
FT                   /id="PRO_0000222558"
FT   DOMAIN          59..224
FT                   /note="Alphavirus-like MT"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01079"
FT   DOMAIN          541..698
FT                   /note="(+)RNA virus helicase ATP-binding"
FT   DOMAIN          699..832
FT                   /note="(+)RNA virus helicase C-terminal"
FT   DOMAIN          1071..1178
FT                   /note="RdRp catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT   BINDING         570..577
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   1294 AA;  147418 MW;  91A85986158BB10E CRC64;
     MAKVRAALDR ITDPSVKAVL NEEAYSHIRP VLRESLTNNP YAIAPDAADT LEKYGIATNP
     FAVKVHSHGA VKSIENTLLE RVGFNLPKEP CIFLFLKRSK LRYLRRGPSN KDIFINLAIE
     PRDLQRYEED TLVESWTRIT TRYAYISDTL HFFTRKMLAD LFFHNPALDV LYATLVLPPE
     ALHKHPSIEP DLYTINYNFN GFQYIPGNHG GGSYSHEFKQ LEWLKVGHLK SPELSLTFQM
     IESIGANHLF MITRGIKITP RVRTFTKDSY VLFPQIFHPR NLNPSKPFPK VKAMQLFTYV
     KSVKNPTERD IYAKIRQLIK TSELSDYHPD EIVHIVNYFV FISKLDSINS YSDILSLPIW
     SKALLPIKTK ITQLWEKLTG ARAFNQLLDA LQWKTFTYSL EVVDFSTAPS QRDCFMEDER
     LETDTLEDEV SQNANNNKPT SLQNIEEAVK NNPDLPWAPW LLILQAHNAD CTQKQYDPEN
     NLILPIQEIN TLPKHQHPDI PTDLLTLLTK LHREPTTVPL DNHRARAYGS DVKNLRIGAL
     LKKQSKDWLA SFALKTENIE RQVLMSVIHG AGGSGKSHAI QTWMRSLNRR DRHVTIILPT
     TDLRNDWTTK VPNLEQANFK TFEKALCQPC GKIIVFDDYS KLPQGYIEAF LAINQNVILA
     ILTGDSKQSF HHESNEDAYT ATLEPSINTY QPFCRYYLNI THRNKPDLAN KLGVYSCSSG
     TTSFTMSSQA LKGMPILSPS IMKKTALGEM GQKSMTYAGC QGLTTKAVQI LLDTNTPLCS
     SNVIYTALSR AVDHIHFINT GPNSTDFWEK LDSTPYLKTF LDCVREERMN EIVAVEEPPA
     PVPAPTTHFP KVNPTTVIES YVHDLPEKHG REIFSETHGH SNAIQTDNPV VQLFPHQQAK
     DETLYWATIE ARLQCTSSEE NLKEFHLKHD IGDILFLNYK QAMNLPQDPI PFNPDLWTLC
     KQEIENTYLK KSAAALVNAA TRQSPDFDSH AIALFLKSQW VKKTEKIGCL KIKAGQTIAA
     FMQQTVMIYG TMARYMRKFR NQYCPRKIFV NCETTPADFN SFILDEWNFN RTCFSNDFTA
     FDQSQDGSIL QFEVIKAKFH NIPEDIIEGY IQIKTHAKIF LGTLSIMRLS GEGPTFDANT
     EANIAYTHTK FNIPCDAAQV YAGDDMSIDY VASVKPSFNM IEHLMKLKGK PVFNTQTQGD
     FAEFCGWTIS PKGIIKKPEK MNMSIELQKN INKFHEVKRS YALDHAFAYQ LGDELHELYN
     ESEAEHHQLA TRSLILAGQA TALDILDYGL RDLK