RDRP_WCMVO
ID RDRP_WCMVO Reviewed; 1294 AA.
AC P15402;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1990, sequence version 1.
DT 03-AUG-2022, entry version 110.
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 O) (WCMV).
OC Viruses; Riboviria; Orthornavirae; Kitrinoviricota; Alsuviricetes;
OC Tymovirales; Alphaflexiviridae; Potexvirus.
OX NCBI_TaxID=12190;
OH NCBI_TaxID=3898; Trifolium.
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=2353451; DOI=10.1016/0042-6822(90)90469-8;
RA Beck D.L., Forster R.L.S., Bevan M.W., Boxen K.A., Lowe S.C., Gardner R.C.;
RT "Infectious transcripts and nucleotide sequence of cloned cDNA of the
RT potexvirus white clover mosaic virus.";
RL Virology 177:152-158(1990).
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; X16636; CAA34628.1; -; Genomic_RNA.
DR PIR; A46350; A46350.
DR Proteomes; UP000007628; 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_0000222559"
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; 147571 MW; CE7342AA0D9992DF CRC64;
MAKVRAALDR ITDPSVKAVL NEEAYSHIRP VLRESLTNNP YAIAPDAADT LEKYGIATNP
FAVKVHSHGA VKSIENTLLE RVGFNLPKEP CTFLFLKRSK LRYLRRGPSN NDIFINLAIE
PRDLQRYEED TLVESWTRIT TRYAYISDTF HFFTRKMLAD LFFHNPALDV LYATLVLPPE
ALHKHPSIEP DLYTINYNFN GFQYIPGNHG GGSYSHEFKQ LEWLKVGHLK SPELCLTFQM
IESIGANHLF MITRGIKITP RVRTFTKDSY VLFPQIFHPR NLNPSKPFPK VKAMQLFTYV
KSVKNPTERD IYAKIRQLIK TSELSDYHPD EIVHIVNYFV FISKLDSINS YSDILSLPIW
SKALLPIKTK ITQLWEKLTG ARAFNQLLDA LQWKTFTYPL EVVDSPQPLQ TRDCFIEDER
LEIDTLEDEI PPNPNDNTSM SPQSIEEAVK NNPDLPWAPW LLILQAHNAD CTEKQYDPEN
NLILPIQEIN TLPKHQHPDI PTDLLTLLTK LHREPTTVSL DNHRARAYGS DVKNLRIGAL
LKKQSKDWLA SFALKTENIE REVLMSVIHG AGGSGKSHAI QTWMRSLNRR DRHVTIILPT
TDLRNDWTNK VPNLEQANFK TFEKALCQPC GKIIVFDDYS KLPQGYIEAF LAINQNVILA
ILTGDSKQSF HHESNEDAYT ATLEPSIITY QPFCRYYLNI THRNKPDLAN KLGVYSCSSG
TTSFTMSSQA LKGMPILSPS IMKKTALGEM GQKSMTYAGC QGLTTKAVQI LLDTNTPLCS
SNVIYTALSR AVDHIHFINT GPNSTDFWEK LDSTPYLKTF LDCVREEKMN EIIAAEEPPT
PVQAPTTHFP KVNPTTVIES YVHDLPEKHD REIFSETHGH SNAIQTDNPV VQLFPHQQAK
DETLYWATIE ARLQCTSSEE NLKEFHLKHD IGDILFLNYK QAMNLPQDPI PFNPDLWTLC
RQEIENTYLK KSAAALVNAA TRQSPDFDSH AIALFLKSQW VKKTEKIGCL KIKAGQTIAA
FMQQTVMIYG TMARYMRKFR NQYCPRKIFV NCETTPADFN SFILDEWNFN RTCFSNDFTA
FDQSQDGSIL QFEVIKAKFH NIPEDVIEGY IQIKTHAKIF LGTLSIMRLS GEGPTFDANT
EANIAYTHTK FNIPCDAAQV YAGDDMSIDY VASVKPSFNM IEHLMKLKGK PVFNTQTQGD
FAEFCGWTIS PKGIIKKPEK MNMSIELQKN INKFHEVKRS YALDHAFAYQ LGDELHELYN
ENEAEHHQLA TRSLILAGQA TALDILDYGL RDLK