ID   RPOL_BPT3               Reviewed;         884 AA.
AC   P07659;
DT   01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1988, sequence version 1.
DT   03-AUG-2022, entry version 106.
DE   RecName: Full=DNA-directed RNA polymerase;
DE            EC=2.7.7.6;
GN   Name=1;
OS   Enterobacteria phage T3 (Bacteriophage T3).
OC   Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC   Caudovirales; Autographiviridae; Studiervirinae; Teetrevirus;
OC   Escherichia virus T3.
OX   NCBI_TaxID=10759;
OH   NCBI_TaxID=562; Escherichia coli.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Hausmann;
RX   PubMed=3903658; DOI=10.1093/nar/13.18.6753;
RA   McGraw N.J., Bailey J.N., Cleaves G.R., Dembinski D.R., Gocke C.R.,
RA   Joliffe L.K., Macwright R.S., McAllister W.T.;
RT   "Sequence and analysis of the gene for bacteriophage T3 RNA polymerase.";
RL   Nucleic Acids Res. 13:6753-6766(1985).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 855-884.
RC   STRAIN=Luria;
RX   PubMed=3586029; DOI=10.1016/0022-2836(87)90261-0;
RA   Schmitt M.P., Beck P.J., Kearney C.A., Spence J.L., Digiovanni D.,
RA   Condreay J.P., Molineux I.J.;
RT   "Sequence of a conditionally essential region of bacteriophage T3,
RT   including the primary origin of DNA replication.";
RL   J. Mol. Biol. 193:479-495(1987).
CC   -!- FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of
CC       DNA into RNA using the four ribonucleoside triphosphates as substrates.
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=2.7.7.6; Evidence={ECO:0000255|PROSITE-ProRule:PRU10031,
CC         ECO:0000255|PROSITE-ProRule:PRU10032};
CC   -!- SIMILARITY: Belongs to the phage and mitochondrial RNA polymerase
CC       family. {ECO:0000305}.
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DR   EMBL; X05031; CAA28696.1; -; Genomic_DNA.
DR   EMBL; X17255; CAA35121.1; -; Genomic_DNA.
DR   EMBL; X02981; CAA26719.1; -; Genomic_DNA.
DR   PIR; A29060; RNBPT3.
DR   RefSeq; NP_523301.1; NC_003298.1.
DR   SMR; P07659; -.
DR   ChEMBL; CHEMBL4854; -.
DR   GeneID; 927437; -.
DR   KEGG; vg:927437; -.
DR   PRO; PR:P07659; -.
DR   GO; GO:0000428; C:DNA-directed RNA polymerase complex; IEA:UniProtKB-KW.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0003899; F:DNA-directed 5'-3' RNA polymerase activity; IDA:CACAO.
DR   GO; GO:0039695; P:DNA-templated viral transcription; IDA:UniProtKB.
DR   GO; GO:0006351; P:transcription, DNA-templated; IEA:InterPro.
DR   Gene3D; 1.10.1320.10; -; 1.
DR   Gene3D; 1.10.287.260; -; 1.
DR   InterPro; IPR024075; DNA-dir_RNA_pol_helix_hairp_sf.
DR   InterPro; IPR002092; DNA-dir_Rpol_phage-type.
DR   InterPro; IPR043502; DNA/RNA_pol_sf.
DR   InterPro; IPR037159; RNA_POL_N_sf.
DR   InterPro; IPR029262; RPOL_N.
DR   PANTHER; PTHR10102; PTHR10102; 1.
DR   Pfam; PF00940; RNA_pol; 1.
DR   Pfam; PF14700; RPOL_N; 1.
DR   SMART; SM01311; RPOL_N; 1.
DR   SUPFAM; SSF56672; SSF56672; 1.
DR   PROSITE; PS00900; RNA_POL_PHAGE_1; 1.
DR   PROSITE; PS00489; RNA_POL_PHAGE_2; 1.
PE   3: Inferred from homology;
KW   DNA-directed RNA polymerase; Nucleotidyltransferase; Transcription;
KW   Transferase; Viral transcription.
FT   CHAIN           1..884
FT                   /note="DNA-directed RNA polymerase"
FT                   /id="PRO_0000087748"
FT   ACT_SITE        538
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        632
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        813
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   884 AA;  98790 MW;  D589E02D879ADA45 CRC64;
     MNIIENIEKN DFSEIELAAI PFNTLADHYG SALAKEQLAL EHESYELGER RFLKMLERQA
     KAGEIADNAA AKPLLATLLP KLTTRIVEWL EEYASKKGRK PSAYAPLQLL KPEASAFITL
     KVILASLTST NMTTIQAAAG MLGKAIEDEA RFGRIRDLEA KHFKKHVEEQ LNKRHGQVYK
     KAFMQVVEAD MIGRGLLGGE AWSSWDKETT MHVGIRLIEM LIESTGLVEL QRHNAGNAGS
     DHEALQLAQE YVDVLAKRAG ALAGISPMFQ PCVVPPKPWV AITGGGYWAN GRRPLALVRT
     HSKKGLMRYE DVYMPEVYKA VNLAQNTAWK INKKVLAVVN EIVNWKNCPV ADIPSLERQE
     LPPKPDDIDT NEAALKEWKK AAAGIYRLDK ARVSRRISLE FMLEQANKFA SKKAIWFPYN
     MDWRGRVYAV PMFNPQGNDM TKGLLTLAKG KPIGEEGFYW LKIHGANCAG VDKVPFPERI
     AFIEKHVDDI LACAKDPINN TWWAEQDSPF CFLAFCFEYA GVTHHGLSYN CSLPLAFDGS
     CSGIQHFSAM LRDEVGGRAV NLLPSETVQD IYGIVAQKVN EILKQDAING TPNEMITVTD
     KDTGEISEKL KLGTSTLAQQ WLAYGVTRSV TKRSVMTLAY GSKEFGFRQQ VLDDTIQPAI
     DSGKGLMFTQ PNQAAGYMAK LIWDAVSVTV VAAVEAMNWL KSAAKLLAAE VKDKKTKEIL
     RHRCAVHWTT PDGFPVWQEY RKPLQKRLDM IFLGQFRLQP TINTLKDSGI DAHKQESGIA
     PNFVHSQDGS HLRMTVVYAH EKYGIESFAL IHDSFGTIPA DAGKLFKAVR ETMVITYENN
     DVLADFYSQF ADQLHETQLD KMPPLPKKGN LNLQDILKSD FAFA