ID   DPOL_BPSP2              Reviewed;         648 AA.
AC   P06225;
DT   01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1988, sequence version 1.
DT   03-AUG-2022, entry version 84.
DE   RecName: Full=DNA polymerase;
DE            EC=2.7.7.7;
DE            EC=3.1.11.- {ECO:0000269|PubMed:2790959};
GN   Name=L;
OS   Bacillus phage SP02 (Bacteriophage SP02).
OC   Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC   Caudovirales; Siphoviridae; Lambdavirus; unclassified Lambdavirus.
OX   NCBI_TaxID=10723;
OH   NCBI_TaxID=1423; Bacillus subtilis.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=6090713; DOI=10.1128/jvi.52.1.9-15.1984;
RA   Raden B., Rutberg L.;
RT   "Nucleotide sequence of the temperate Bacillus subtilis bacteriophage SPO2
RT   DNA polymerase gene L.";
RL   J. Virol. 52:9-15(1984).
RN   [2]
RP   FUNCTION.
RX   PubMed=2790959; DOI=10.1016/0092-8674(89)90883-0;
RA   Bernad A., Blanco L., Lazaro J.M., Martin G., Salas M.;
RT   "A conserved 3'->5' exonuclease active site in prokaryotic and eukaryotic
RT   DNA polymerases.";
RL   Cell 59:219-228(1989).
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'-5'
CC       direction. {ECO:0000269|PubMed:2790959}.
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   -!- SIMILARITY: Belongs to the DNA polymerase type-A family. {ECO:0000305}.
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DR   EMBL; X01458; CAA25691.1; -; Genomic_DNA.
DR   EMBL; K02752; AAA32600.1; -; Genomic_DNA.
DR   PIR; A21498; DJBPS2.
DR   SMR; P06225; -.
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:0006261; P:DNA-templated DNA replication; IEA:InterPro.
DR   GO; GO:0039693; P:viral DNA genome replication; IEA:UniProtKB-KW.
DR   InterPro; IPR019760; DNA-dir_DNA_pol_A_CS.
DR   InterPro; IPR001098; DNA-dir_DNA_pol_A_palm_dom.
DR   InterPro; IPR043502; DNA/RNA_pol_sf.
DR   InterPro; IPR002298; DNA_polymerase_A.
DR   PANTHER; PTHR10133; PTHR10133; 1.
DR   Pfam; PF00476; DNA_pol_A; 1.
DR   SMART; SM00482; POLAc; 1.
DR   SUPFAM; SSF56672; SSF56672; 1.
DR   PROSITE; PS00447; DNA_POLYMERASE_A; 1.
PE   3: Inferred from homology;
KW   DNA replication; DNA-binding; DNA-directed DNA polymerase; Exonuclease;
KW   Hydrolase; Nuclease; Nucleotidyltransferase; Transferase;
KW   Viral DNA replication.
FT   CHAIN           1..648
FT                   /note="DNA polymerase"
FT                   /id="PRO_0000101266"
SQ   SEQUENCE   648 AA;  72580 MW;  6E1F9F1D789B362D CRC64;
     MKTLSIDIET FSSVDLLKAG VYAYTEAPDF EILLFAYAFD DDPVKIIDLA QGDTLPHEVL
     VALTSSKVIK TAYNANFERT CIAKHFNLML LPAQWRCTAV HATTLGLPGN LDGVAKALKL
     SAQKDKAGKA LIRYFSVPCK PTKANGQRVR NLPEHDPEKW EKFKVYCIQD VEVERAIKNR
     ISKFEPLESE HKLWALDQEI NDRGVRIDVD LVKHAIACDE QYQAGLIAEA KKLTGLPNPN
     STAQLKKWLE EKGLTISSLA KDKIEELIEN TNDETVHRVL RLRQEMAKTS VKKYLAMEKA
     LCPDNRVRGL LQFYGASRTG RWAGRLVQVQ NLPQNKIEDL DTARNLLKGG HYEAIELLYG
     QVPFVLSQLV RTAFIPSEGN EFYVSDFSAI EARVIAWLAG EEWRLEVFNT HGKIYEASAA
     QMFKVPVESI TKGSPLRQKG KVAELALGYQ GGKGALIQMG ALNMGLAEGE LPELVKAWRT
     ANKKIVKFWY DVEAAAIKAV KERKPVKLQH GLTFLYESGI LFVQLPSGRR LAYAKPKLEL
     DERFGKEALT YEGKLESGKW GRLNTYGGKL VENIVQATAR DCLAITLMRL DNAGYKTVMH
     VHDEAVLDVP RGKNELDKVE AIMGEPISWA KGLPLTADGF VTDYYKKD