ID   RDRP_PVSP               Reviewed;         353 AA.
AC   P22657;
DT   01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1991, sequence version 1.
DT   23-FEB-2022, entry version 71.
DE   RecName: Full=RNA replication protein;
DE   AltName: Full=152 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;
DE   Flags: Fragment;
OS   Potato virus S (strain Peruvian).
OC   Viruses; Riboviria; Orthornavirae; Kitrinoviricota; Alsuviricetes;
OC   Tymovirales; Betaflexiviridae; Quinvirinae; Carlavirus.
OX   NCBI_TaxID=12170;
OH   NCBI_TaxID=4113; Solanum tuberosum (Potato).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=2732711; DOI=10.1099/0022-1317-70-5-1053;
RA   Mackenzie D.J., Tremaine J.H., Stace-Smith R.;
RT   "Organization and interviral homologies of the 3'-terminal portion of
RT   potato virus S RNA.";
RL   J. Gen. Virol. 70:1053-1063(1989).
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; D00461; BAA00350.1; -; Genomic_RNA.
DR   PIR; JA0123; JA0123.
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..353
FT                   /note="RNA replication protein"
FT                   /id="PRO_0000222562"
FT   DOMAIN          137..244
FT                   /note="RdRp catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT   NON_TER         1
SQ   SEQUENCE   353 AA;  41063 MW;  3DEF0B11BB0D16F6 CRC64;
     MYGPFLLKEF LNDVPLKPMH NTRMMAEAKF DFEEKKTQKS AATIENHSNR SCRDWLADMG
     MVFSKSQLCT KFDNRFRDAK AAQTIVCFQH SVLCRFAPYM RYIEKKLNEV LPATFYIHSG
     KGLEELNKWV IESKFEGVCT ESDYEAFDAS QDQYIVAFEL ALMRYLGLPN DLIEDYKYIK
     THLGSKLGNF AIMRFSGEAS TFLFNTMANM LFTFLRYKLK GDERICFAGD DMCANRALFI
     KDTHEGFLKK LKLKAKVDRT NRPSFCGWSL SSDGIYKKPQ LVFERLCIAK ETANLANCID
     NYAIEVSYAY KLGERIKERM SEEELEAFYN CVRVIIKHKH LLKSEIRSVY EEV