ID   RDRP_BPMX1              Reviewed;         586 AA.
AC   O64308;
DT   30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   03-AUG-2022, entry version 61.
DE   RecName: Full=RNA-directed RNA polymerase subunit beta;
DE            EC=2.7.7.48 {ECO:0000250|UniProtKB:P14647};
DE   AltName: Full=RNA replicase beta chain;
OS   Escherichia phage Qbeta.
OC   Viruses; Riboviria; Orthornavirae; Lenarviricota; Leviviricetes;
OC   Norzivirales; Fiersviridae; Qubevirus; Qubevirus durum.
OX   NCBI_TaxID=2789016;
OH   NCBI_TaxID=562; Escherichia coli.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=7723040; DOI=10.1006/jmbi.1995.0189;
RA   Beekwilder M.J., Nieuwenhuizen R., van Duin J.;
RT   "Secondary structure model for the last two domains of single-stranded RNA
RT   phage Q beta.";
RL   J. Mol. Biol. 247:903-917(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=8609616; DOI=10.1006/jmbi.1996.0064;
RA   Beekwilder J., Nieuwenhuizen R., Poot R., van Duin J.;
RT   "Secondary structure model for the first three domains of Q beta RNA.
RT   Control of A-protein synthesis.";
RL   J. Mol. Biol. 256:8-19(1996).
CC   -!- FUNCTION: This is the catalytic subunit of the viral RNA-dependent RNA
CC       polymerase complex. This complex is involved in viral RNA replication
CC       that produces (+)-stranded genomes via a complementary, (-)-stranded
CC       intermediate. Binds RNA cooperatively with the host ribosomal protein
CC       S1. {ECO:0000250|UniProtKB:P14647}.
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:0000250|UniProtKB:P14647,
CC         ECO:0000255|PROSITE-ProRule:PRU00539};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:P14647};
CC       Note=Binds 2 Mg(2+) per subunit, Ca(2+) is used in crystallization to
CC       prevent RNA polymerase activity. {ECO:0000250|UniProtKB:P14647};
CC   -!- SUBUNIT: Homodimer; the replicase complex can dimerize. Part of the
CC       viral RNA-dependent RNA polymerase complex, the other subunits are the
CC       host ribosomal protein S1, EF-Tu and EF-Ts. S1 is needed for the
CC       initiation of genomic RNA (+)-strand replication.
CC       {ECO:0000250|UniProtKB:P14647}.
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DR   EMBL; AF059242; AAC14701.1; -; Genomic_RNA.
DR   RefSeq; NP_046752.1; NC_001890.1.
DR   SMR; O64308; -.
DR   GeneID; 1261500; -.
DR   KEGG; vg:1261500; -.
DR   Proteomes; UP000001832; Genome.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003968; F:RNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0039694; P:viral RNA genome replication; IEA:InterPro.
DR   InterPro; IPR043502; DNA/RNA_pol_sf.
DR   InterPro; IPR007096; RNA-dir_Rpol_phage_catalytic.
DR   InterPro; IPR005093; RNArep_beta.
DR   Pfam; PF03431; RNA_replicase_B; 1.
DR   SUPFAM; SSF56672; SSF56672; 1.
DR   PROSITE; PS50522; RDRP_PHAGE; 1.
PE   3: Inferred from homology;
KW   Magnesium; Metal-binding; Nucleotide-binding; Nucleotidyltransferase;
KW   Reference proteome; RNA-binding; RNA-directed RNA polymerase; Transferase;
KW   Viral RNA replication.
FT   CHAIN           1..586
FT                   /note="RNA-directed RNA polymerase subunit beta"
FT                   /id="PRO_0000402539"
FT   DOMAIN          259..391
FT                   /note="RdRp catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT   BINDING         274
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P14647"
FT   BINDING         274
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P14647"
FT   BINDING         359
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P14647"
FT   BINDING         359
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P14647"
FT   BINDING         360
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P14647"
FT   BINDING         360
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P14647"
SQ   SEQUENCE   586 AA;  65953 MW;  879B877A1990C83C CRC64;
     MSKTLQSRKS LSGKLRRAAN TRIVVEGNLA LSIANDLLSA LDVEPFNSEE DCISRSPKFG
     ISPDQFRNSY LRAEIMSKYD SFSLGINTEA VAWEKFLAAE AECAKTNLRL YRPNYNEDFN
     FSLGETCIHM ARRKIVKLLG DSVPFEAVLR HCRFSGGATT TNSRLYGHPS FKFALAQECT
     PRAVPYVQAL KACTNMDLGI TKVSPFNKAV TVPKNSKTDR CIAIEPGWNM FFQLGIGGVI
     REKLHLWNID LNDQTINQVR AYSGSCSNEL ATVDLSSASD TISLALVELL LPPAWFKVLT
     DLRSRRGMLP DGRIITYEKI SSMGNGFTFE LESLIFAALA RSLCELLNLQ PSSVTVYGDD
     IILPSDACSS LIEVFSYVGF RTNEKKTFFD GPFRESCGKH YFMGVDVTPF YIRHRIVSPS
     DLILVLNQMY RWATIDGVWD PRVYPVYTKY RRLLPDILRR NVVPDGYGDG ALVGSVLTSP
     FAENRGWVRR VPMIIDKKKD RVRDERGSYL YELWSLQQLE CDSEFPFNGS LVVGTNDGVC
     TYRHRERVST AISDSVGAYD IVWIPCSSRV LAPYGDFRRH EGSILK