DPOL_BPPRD
ID DPOL_BPPRD Reviewed; 553 AA.
AC P10479; Q3T4P4;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 1.
DT 23-FEB-2022, entry version 123.
DE RecName: Full=DNA-directed DNA polymerase;
DE EC=2.7.7.7;
DE EC=3.1.11.- {ECO:0000250|UniProtKB:P04415};
DE AltName: Full=Protein P1;
GN Name=I;
OS Enterobacteria phage PRD1 (Bacteriophage PRD1).
OC Viruses; Varidnaviria; Bamfordvirae; Preplasmiviricota; Tectiliviricetes;
OC Kalamavirales; Tectiviridae; Alphatectivirus.
OX NCBI_TaxID=10658;
OH NCBI_TaxID=471; Acinetobacter calcoaceticus.
OH NCBI_TaxID=562; Escherichia coli.
OH NCBI_TaxID=584; Proteus mirabilis.
OH NCBI_TaxID=287; Pseudomonas aeruginosa.
OH NCBI_TaxID=294; Pseudomonas fluorescens.
OH NCBI_TaxID=303; Pseudomonas putida (Arthrobacter siderocapsulatus).
OH NCBI_TaxID=90371; Salmonella typhimurium.
OH NCBI_TaxID=666; Vibrio cholerae.
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3479792; DOI=10.1073/pnas.84.23.8287;
RA Jung G., Leavitt M.C., Hsieh J.-C., Ito J.;
RT "Bacteriophage PRD1 DNA polymerase: evolution of DNA polymerases.";
RL Proc. Natl. Acad. Sci. U.S.A. 84:8287-8291(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3322943; DOI=10.1016/0378-1119(87)90183-1;
RA Savilahti H., Bamford D.H.;
RT "The complete nucleotide sequence of the left very early region of
RT Escherichia coli bacteriophage PRD1 coding for the terminal protein and the
RT DNA polymerase.";
RL Gene 57:121-130(1987).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1853567; DOI=10.1016/0042-6822(91)90995-n;
RA Bamford J.K.H., Haenninen A.-L., Pakula T.M., Ojala P.M., Kalkkinen N.,
RA Frilander M., Bamford D.H.;
RT "Genome organization of membrane-containing bacteriophage PRD1.";
RL Virology 183:658-676(1991).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=15946683; DOI=10.1016/j.jmb.2005.04.059;
RA Saren A.M., Ravantti J.J., Benson S.D., Burnett R.M., Paulin L.,
RA Bamford D.H., Bamford J.K.H.;
RT "A snapshot of viral evolution from genome analysis of the tectiviridae
RT family.";
RL J. Mol. Biol. 350:427-440(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-9.
RX PubMed=3684578; DOI=10.1093/nar/15.21.8999;
RA Hsieh J.-C., Jung G., Leavitt M.C., Ito J.;
RT "Primary structure of the DNA terminal protein of bacteriophage PRD1.";
RL Nucleic Acids Res. 15:8999-9009(1987).
RN [6]
RP MUTAGENESIS.
RX PubMed=2202298; DOI=10.1016/0006-291x(90)90534-t;
RA Jung G., Leavitt M.C., Schultz M., Ito J.;
RT "Site-specific mutagenesis of PRD1 DNA polymerase: mutations in highly
RT conserved regions of the family B DNA polymerase.";
RL Biochem. Biophys. Res. Commun. 170:1294-1300(1990).
CC -!- FUNCTION: Replicates the viral genomic DNA. This polymerase possesses
CC two enzymatic activities: DNA synthesis (polymerase) and an
CC exonucleolytic activity that degrades single-stranded DNA in the 3'- to
CC 5'-direction for proofreading purpose. {ECO:0000250|UniProtKB:P04415}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) =
CC diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339,
CC Rhea:RHEA-COMP:17340, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560,
CC ChEBI:CHEBI:173112; EC=2.7.7.7;
CC -!- DOMAIN: The N-terminus contains the 3'-5' exonuclease activity and the
CC C-terminus contains the polymerase activity.
CC -!- MISCELLANEOUS: This DNA polymerase requires a protein as a primer.
CC -!- SIMILARITY: Belongs to the DNA polymerase type-B family. {ECO:0000305}.
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DR EMBL; J03018; AAA32452.1; -; Genomic_DNA.
DR EMBL; M22161; AAA32450.1; -; Genomic_DNA.
DR EMBL; AY848689; AAX45903.1; -; Genomic_DNA.
DR EMBL; X06321; CAA29637.1; -; Genomic_DNA.
DR PIR; B27328; DJBPD1.
DR RefSeq; NP_040682.1; NC_001421.2.
DR SMR; P10479; -.
DR Proteomes; UP000002143; Genome.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003887; F:DNA-directed DNA polymerase activity; IDA:CACAO.
DR GO; GO:0004527; F:exonuclease activity; IEA:UniProtKB-KW.
DR GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR GO; GO:0039693; P:viral DNA genome replication; IEA:UniProtKB-KW.
DR Gene3D; 3.30.420.10; -; 1.
DR Gene3D; 3.90.1600.10; -; 2.
DR InterPro; IPR006172; DNA-dir_DNA_pol_B.
DR InterPro; IPR004868; DNA-dir_DNA_pol_B_mt/vir.
DR InterPro; IPR043502; DNA/RNA_pol_sf.
DR InterPro; IPR023211; DNA_pol_palm_dom_sf.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR036397; RNaseH_sf.
DR Pfam; PF03175; DNA_pol_B_2; 1.
DR PRINTS; PR00106; DNAPOLB.
DR SMART; SM00486; POLBc; 1.
DR SUPFAM; SSF53098; SSF53098; 1.
DR SUPFAM; SSF56672; SSF56672; 1.
DR PROSITE; PS00116; DNA_POLYMERASE_B; 1.
PE 3: Inferred from homology;
KW DNA replication; DNA-binding; DNA-directed DNA polymerase; Exonuclease;
KW Hydrolase; Multifunctional enzyme; Nuclease; Nucleotidyltransferase;
KW Reference proteome; Transferase; Viral DNA replication.
FT CHAIN 1..553
FT /note="DNA-directed DNA polymerase"
FT /id="PRO_0000046545"
SQ SEQUENCE 553 AA; 63336 MW; 65E61D0599BDD51E CRC64;
MPRRSRKKVE YKIAAFDFET DPFKHDRIPK PFSWGFYNGE IYKDYWGDDC IEQFIYWLDT
IEEPHVIYAH NGGKFDFLFL MKYFRGKLKI VNGRILEVEH GIHKFRDSYA ILPVPLAASD
EKIEIDYGKM ERETREQHKA EILEYLKGDC VTLHKMVSLF IAEFGMRLTI GGTAMNELKQ
FHPYDPVRKG FDEAMRPFYF GGRCQAFEKG IIEDDIKVYD VNSMYPHAMR NFRHPFSDEF
YEANEITEET YFIEWEGENN GAVPVRTKTG LDFNQRSGIF HTSIHEWRAG IDTGTIKPNR
IIRTINFTET TTFGAFIDHF FSKRDAAKKA GDLFHNIFYK LILNSSYGKF AQNPENYKEW
CITEGGIYLE GYDGEGCEVQ EHLDYILWGR PAEMFNYFNV AVAASITGAA RSVLLRALAQ
AERPLYCDTD SIICRDLKNV PLDAYQLGAW DLEATGDKIA IAGKKLYALY AGDNCVKIAS
KGASLVPRDI GFLMPPDMEP KAAKKVAQQK AKNIGGEKIL KVANGGVYDF VNDAPSFKLN
GNVQFIKRTI KGT
