ID   DPOL_BPE32              Reviewed;         614 AA.
AC   B0FIL5;
DT   04-FEB-2015, integrated into UniProtKB/Swiss-Prot.
DT   26-FEB-2008, sequence version 1.
DT   29-SEP-2021, entry version 44.
DE   RecName: Full=DNA-directed DNA polymerase {ECO:0000303|PubMed:18294652};
DE            EC=2.7.7.7 {ECO:0000250|UniProtKB:P00581};
DE            EC=3.1.11.- {ECO:0000250|UniProtKB:P00581};
DE   AltName: Full=DNA polymerase gp53;
GN   OrderedLocusNames=53 {ECO:0000303|PubMed:18294652};
OS   Escherichia phage Phieco32 (Escherichia coli phage phi32).
OC   Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC   Caudovirales; Podoviridae; Kuravirus.
OX   NCBI_TaxID=490103 {ECO:0000312|Proteomes:UP000002006};
OH   NCBI_TaxID=562; Escherichia coli.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=18294652; DOI=10.1016/j.jmb.2007.12.077;
RA   Savalia D., Westblade L.F., Goel M., Florens L., Kemp P., Akulenko N.,
RA   Pavlova O., Padovan J.C., Chait B.T., Washburn M.P., Ackermann H.W.,
RA   Mushegian A., Gabisonia T., Molineux I., Severinov K.;
RT   "Genomic and proteomic analysis of phiEco32, a novel Escherichia coli
RT   bacteriophage.";
RL   J. Mol. Biol. 377:774-789(2008).
CC   -!- FUNCTION: Replicates viral genomic DNA. This polymerase possesses two
CC       enzymatic activities: DNA synthesis (polymerase) and an exonucleolytic
CC       activity that degrades single-stranded DNA in the 3'-5' direction.
CC       {ECO:0000250|UniProtKB:P00581}.
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         Evidence={ECO:0000250|UniProtKB:P00581};
CC   -!- SIMILARITY: Belongs to the DNA polymerase type-A family. {ECO:0000305}.
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DR   EMBL; EU330206; ABY52854.1; -; Genomic_DNA.
DR   RefSeq; YP_001671798.1; NC_010324.1.
DR   GeneID; 5896807; -.
DR   KEGG; vg:5896807; -.
DR   Proteomes; UP000002006; Genome.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0004527; F:exonuclease activity; IEA:UniProtKB-KW.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR   GO; GO:0039693; P:viral DNA genome replication; IEA:UniProtKB-KW.
DR   InterPro; IPR001098; DNA-dir_DNA_pol_A_palm_dom.
DR   InterPro; IPR043502; DNA/RNA_pol_sf.
DR   Pfam; PF00476; DNA_pol_A; 1.
DR   SMART; SM00482; POLAc; 1.
DR   SUPFAM; SSF56672; SSF56672; 1.
PE   3: Inferred from homology;
KW   DNA replication; DNA-binding; DNA-directed DNA polymerase; Exonuclease;
KW   Hydrolase; Nuclease; Nucleotidyltransferase; Reference proteome;
KW   Transferase; Viral DNA replication.
FT   CHAIN           1..614
FT                   /note="DNA-directed DNA polymerase"
FT                   /id="PRO_0000431824"
SQ   SEQUENCE   614 AA;  69212 MW;  F75BE5A457B2C408 CRC64;
     MSNPDALPFL TEMTVADIIS KQAKHGVSFN RRNARWYVHL LKEIIVNIDR ELIPLLPKMR
     LDGSTYMKPF KKSGALQKWP QAYCDRVGLK REDIGGAFTC VEYVDFDPSK DARVKEALMD
     EGFLPPEFNV SKKPWNTFEI KKDMRKYGTY QAWYTAWMRG NAKQKQTAEM VDADIKKFLE
     KHFRFKTKNY MKAYVFGLGL NPNRRNPVTF DEIKKALATS NKWPTAPTNL EETLEEGLGG
     ELGSVGSLLK RRVVAAHRLG LISGLIAKER EDGKLSAEAN SCATPTFRFK HRIVVNIPSR
     GLFGHECRSL FESDYNSDSD HSRPFVITNV VPDGCYIRKG TNVIYEKGKP GKKDKPVGAY
     KYYIPAGKEV FLGYDGSGLE LRMLAHYLIK ECRDMLAEAI EENNPAKKAL AERGLASAIM
     YRDILLEGDI HSHNQKLAGL PTRDNAKTFI YAFNYGAGDA KLGSIVGGGA DEGSVMRARF
     LAENPCIAIL IDRMTEKAAQ GYLIGVDGRK ITMRRDATGK VMVHKALNTL LQCAGAVVMK
     YAMMFLNKWI EKDKVRCAKV IDMHDEGQFS VNRNDVQKLK EHTELCVKKA GEYLNMECPL
     ASDCQIGLNW MHTH