ID   RDRP_BPGA               Reviewed;         532 AA.
AC   P07393;
DT   01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1988, sequence version 1.
DT   03-AUG-2022, entry version 83.
DE   RecName: Full=RNA-directed RNA polymerase beta chain;
DE            EC=2.7.7.48 {ECO:0000250|UniProtKB:P00585};
DE   AltName: Full=RNA replicase beta chain;
OS   Enterobacteria phage GA (Bacteriophage GA).
OC   Viruses; Riboviria; Orthornavirae; Lenarviricota; Leviviricetes;
OC   Norzivirales; Fiersviridae; Emesvirus; Emesvirus japonicum.
OX   NCBI_TaxID=12018;
OH   NCBI_TaxID=562; Escherichia coli.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=3711059; DOI=10.1093/oxfordjournals.jbchem.a135580;
RA   Inokuchi Y., Takahashi R., Hirose T., Inayama S., Jacobson A.B.,
RA   Hirashima A.;
RT   "The complete nucleotide sequence of the group II RNA coliphage GA.";
RL   J. Biochem. 99:1169-1180(1986).
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. {ECO:0000250|UniProtKB:P00585}.
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:P00585,
CC         ECO:0000255|PROSITE-ProRule:PRU00539};
CC   -!- SUBUNIT: Part of the viral RNA-dependent RNA polymerase complex, the
CC       other subunits are probably the host ribosomal protein S1, EF-Tu and
CC       EF-Ts. {ECO:0000250|UniProtKB:P00585}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; X03869; CAA27499.1; -; mRNA.
DR   PIR; JS0008; RRBPBG.
DR   SMR; P07393; -.
DR   PRIDE; P07393; -.
DR   Proteomes; UP000002126; Genome.
DR   GO; GO:0000166; F:nucleotide 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   2: Evidence at transcript level;
KW   Nucleotide-binding; Nucleotidyltransferase; Reference proteome;
KW   RNA-directed RNA polymerase; Transferase; Viral RNA replication.
FT   CHAIN           1..532
FT                   /note="RNA-directed RNA polymerase beta chain"
FT                   /id="PRO_0000164852"
FT   DOMAIN          245..375
FT                   /note="RdRp catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
SQ   SEQUENCE   532 AA;  59929 MW;  EF416B83D504CEE3 CRC64;
     MFRFREIEKT LCMDRTRDCA VRFHVYLQSL DLGSSDPLSP DFDGLAYLRD ECLTKHPSLG
     DSNSDARRKE LAYAKLMDSD QRCKIQNSNG YDYSHIESGV LSGILKTAQA LVANLLTGFE
     SHFLNDCSFS NGASQGFKLR DAAPFKKIAG QATVTAPAYD IAVAAVKTCA PWYAYMQETY
     GDETKWFRRV YGNGLFSVPK NNKIDRAACK EPDMNMYLQK GAGSFIRKRL RSVGIDLNDQ
     TRNQELARLG SIDGSLATID LSSASDSISD RLVWDLLPPH VYSYLARIRT SFTMIDGRLH
     KWGLFSTMGN GFTFELESMI FWALSKSIML SMGVTGSLGI YGDDIIVPVE CRPTLLKVLS
     AVNFLPNEEK TFTTGYFRES CGAHFFKDAD MKPFYCKRPM ETLPDVMLLC NRIRGWQTVG
     GMSDPRLFPI WKEFADMIPP KFKGGCNLDR DTYLVSPDKP GVSLVRIAKV RSGFNHAFPY
     GHENGRYVHW LHMGSGEVLE TISSARYRCK PNSEWRTQIP LFPQELEACV LS