ID   RDRP_CVB                Reviewed;         260 AA.
AC   P37987;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1994, sequence version 1.
DT   23-FEB-2022, entry version 70.
DE   RecName: Full=RNA replication protein;
DE   AltName: Full=ORF 1 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;
DE   Flags: Fragment;
OS   Chrysanthemum virus B (CVB).
OC   Viruses; Riboviria; Orthornavirae; Kitrinoviricota; Alsuviricetes;
OC   Tymovirales; Betaflexiviridae; Quinvirinae; Carlavirus.
OX   NCBI_TaxID=12165;
OH   NCBI_TaxID=41568; Chrysanthemum morifolium (Florist's daisy) (Dendranthema grandiflorum).
OH   NCBI_TaxID=109564; Gynura.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=1919520; DOI=10.1099/0022-1317-72-10-2333;
RA   Levay K., Zavriev S.;
RT   "Nucleotide sequence and gene organization of the 3'-terminal region of
RT   chrysanthemum virus B genomic RNA.";
RL   J. Gen. Virol. 72:2333-2337(1991).
CC   -!- FUNCTION: RNA replication. The central part of this protein possibly
CC       functions as an ATP-binding helicase.
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 potexviruses/carlaviruses RNA replication
CC       protein family. {ECO:0000305}.
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DR   EMBL; S60150; AAB20076.2; -; Genomic_RNA.
DR   PIR; JQ1246; JQ1246.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
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:0006351; P:transcription, DNA-templated; IEA:InterPro.
DR   GO; GO:0039694; P:viral RNA genome replication; IEA:InterPro.
DR   InterPro; IPR043502; DNA/RNA_pol_sf.
DR   InterPro; IPR007094; RNA-dir_pol_PSvirus.
DR   InterPro; IPR001788; Tymovirus_RNA-dep_RNA_pol.
DR   Pfam; PF00978; RdRP_2; 1.
DR   SUPFAM; SSF56672; SSF56672; 1.
DR   PROSITE; PS50507; RDRP_SSRNA_POS; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Helicase; Hydrolase; Multifunctional enzyme;
KW   Nucleotide-binding; Nucleotidyltransferase; RNA-directed RNA polymerase;
KW   Transferase; Viral RNA replication.
FT   CHAIN           <1..260
FT                   /note="RNA replication protein"
FT                   /id="PRO_0000222560"
FT   DOMAIN          40..147
FT                   /note="RdRp catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT   NON_TER         1
SQ   SEQUENCE   260 AA;  30159 MW;  3AC15F37C8932B54 CRC64;
     PYMRYIEAKL HEVLPSRFYI HSGKGLEELN EWVIKGKFEG ICTESDYEAF DASQDQYIVA
     FELALMEYLG LPRDLIEDYA FIKCHLGSKL GNFAIMRFSG EASTFLFNTM ANMLFTFLRY
     NIKDSEHICF AGDDMCASER LCIKKEHEGF LNKLKLKAKV FFVDKPTFCG WHLCPDGIYK
     KPQLVLERMC IAKEKNNLAN CLDNYAIEVS YAYKLGERAV NRMDEEELEA AYNCVRIIIK
     NKKLLKSDIL GFYSNIEKQI