RDRP_BPFR
ID RDRP_BPFR Reviewed; 545 AA.
AC P15965;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1991, sequence version 2.
DT 03-AUG-2022, entry version 82.
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 fr (Bacteriophage fr).
OC Viruses; Riboviria; Orthornavirae; Lenarviricota; Leviviricetes;
OC Levivirales; Leviviridae; Levivirus.
OX NCBI_TaxID=12017;
OH NCBI_TaxID=562; Escherichia coli.
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2207135; DOI=10.1016/0167-4781(90)90149-v;
RA Adhin M.R., Avots A.J., Berzin V.M., Overbeek G.P., van Duin J.;
RT "Complete nucleotide sequence of the group I RNA bacteriophage fr.";
RL Biochim. Biophys. Acta 1050:104-109(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-11.
RX PubMed=3628010; DOI=10.1093/nar/15.16.6741;
RA Berzin V.M., Avots A.J., Jansone I.V., Gintnere L., Tsimanis A.J.;
RT "Sequence of the genes coding for the A-protein and coat protein of
RT bacteriophage fr.";
RL Nucleic Acids Res. 15:6741-6741(1987).
RN [3]
RP NUCLEOTIDE SEQUENCE OF 1-11.
RA Berzin V.M., Gribanov V.A., Cielens I.E., Jansone I.V., Gren E.J.;
RT "Structure of regulator part of phage fr replicase gene.";
RL Bioorg. Khim. 7:306-308(1981).
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}.
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DR EMBL; X15031; CAA33138.1; -; mRNA.
DR EMBL; M31635; AAA32190.1; -; Genomic_RNA.
DR EMBL; M35063; AAA32191.1; -; Genomic_RNA.
DR EMBL; M38325; AAA32192.1; -; Genomic_RNA.
DR PIR; S08020; S08020.
DR SMR; P15965; -.
DR Proteomes; UP000002582; 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..545
FT /note="RNA-directed RNA polymerase beta chain"
FT /id="PRO_0000164851"
FT DOMAIN 243..373
FT /note="RdRp catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
SQ SEQUENCE 545 AA; 61340 MW; CF97EF7262C58BAC CRC64;
MSKSTKKFNS LCIDLSRDLS LEVYQSIASV ATGSSDPHSD DFTAIAYLRD ELLTKHPNLG
DGNDEATRRS LAIAKLLEAN DRCGQINRDG FLHDATASWD PDVLQTSIRS LIGNLLSGYS
SQLFRHCTFS NGASMGHKLQ DAAPYKKFAE QATVTPRALK AAVLVKDQCS PWIRHSHVFP
ESYTFRLVGG NGVFTVPKNN KIDRAACKEP DMNMYLQKGV GGFIRRRLKT VGIDLNDQTI
NQRLAQQGSR DGSLATIDLS SASDSISDRL VWSFLPPELY SYLDMIRSHY GYVNGKMIRW
ELFSTMGNGF TFELESMIFW AIVRATQIHF RNTGTIGIYG DDIICPTEIA PRVLEALSFY
GFKPNLRKTF TSGSFRESCG AHYFRGVDVK PFYIKKPITD LFSLMLILNR IRGWGVVNGI
ADPRLYEVWE KLSRLVPRYL FGGTDLQADY YVVSPPILKG IYSKMNGRRE YAEARTTGFK
LARIARWRKH FSDKHDSGRY IAWFHTGGEI TDSMKSAGVR VMRTSEWLQP VPVFPQECGP
ASSPQ