ID   DPOL_BPSP1              Reviewed;         924 AA.
AC   P30314;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1994, sequence version 2.
DT   03-AUG-2022, entry version 102.
DE   RecName: Full=DNA polymerase;
DE            EC=2.7.7.7;
DE            EC=3.1.11.- {ECO:0000250|UniProtKB:P00581};
GN   Name=31;
OS   Bacillus phage SP01 (Bacteriophage SP01).
OC   Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC   Caudovirales; Herelleviridae; Spounavirinae; Okubovirus.
OX   NCBI_TaxID=10685;
OH   NCBI_TaxID=1423; Bacillus subtilis.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1324872; DOI=10.1016/0378-1119(92)90256-o;
RA   Scarlato V., Gargano S.;
RT   "The DNA polymerase-encoding gene of Bacillus subtilis bacteriophage
RT   SPO1.";
RL   Gene 118:109-113(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 552-642.
RX   PubMed=2119891; DOI=10.1016/0092-8674(90)90174-d;
RA   Goodrich-Blair H., Scarlato V., Gott J.M., Xu M.Q., Shub D.A.;
RT   "A self-splicing group I intron in the DNA polymerase gene of Bacillus
RT   subtilis bacteriophage SPO1.";
RL   Cell 63:417-424(1990).
RN   [3]
RP   SEQUENCE REVISION TO 555-556.
RA   Shub D.A.;
RL   Submitted (JAN-1994) to the EMBL/GenBank/DDBJ databases.
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   -!- SIMILARITY: Belongs to the DNA polymerase type-A family. {ECO:0000305}.
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DR   EMBL; M84415; AAA03732.1; ALT_SEQ; Unassigned_DNA.
DR   EMBL; M37686; AAA64535.1; -; Genomic_DNA.
DR   PIR; JC1269; JC1269.
DR   SMR; P30314; -.
DR   PRIDE; P30314; -.
DR   GO; GO:0008408; F:3'-5' exonuclease activity; IEA:InterPro.
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:0006261; P:DNA-templated DNA replication; IEA:InterPro.
DR   GO; GO:0039693; P:viral DNA genome replication; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.420.10; -; 1.
DR   Gene3D; 3.40.470.10; -; 1.
DR   InterPro; IPR002562; 3'-5'_exonuclease_dom.
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   InterPro; IPR012337; RNaseH-like_sf.
DR   InterPro; IPR036397; RNaseH_sf.
DR   InterPro; IPR005122; Uracil-DNA_glycosylase-like.
DR   InterPro; IPR036895; Uracil-DNA_glycosylase-like_sf.
DR   PANTHER; PTHR10133; PTHR10133; 1.
DR   Pfam; PF00476; DNA_pol_A; 1.
DR   Pfam; PF01612; DNA_pol_A_exo1; 1.
DR   Pfam; PF03167; UDG; 1.
DR   PRINTS; PR00868; DNAPOLI.
DR   SMART; SM00474; 35EXOc; 1.
DR   SMART; SM00482; POLAc; 1.
DR   SUPFAM; SSF52141; SSF52141; 1.
DR   SUPFAM; SSF53098; SSF53098; 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..924
FT                   /note="DNA polymerase"
FT                   /id="PRO_0000101265"
FT   DOMAIN          235..386
FT                   /note="3'-5' exonuclease"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   924 AA;  106837 MW;  0F821B13B5A05EE6 CRC64;
     MGSALDTLKE FNPKPMKGQG SKKARIIIVQ ENPFDYEYRK KKYMTGKAGK LLKFGLAEVG
     IDPDEDVYYT SIVKYPTPEN RLPTPDEIKE SMDYMWAEIE VIDPDIIIPT GNLSLKFLTK
     MTAITKVRGK LYEIEGRKFF PMIHPNTVLK QPKYQDFFIK DLEILASLLE GKTPKNVLAF
     TKERRYCDTF EDAIDEIKRY LELPAGSRVV IDLETVKTNP FIEKVTMKKT TLEAYPMSQQ
     PKIVGIGLSD RSGYGCAIPL YHRENLMKGN QIGTIVKFLR KLLEREDLEF IAHNGKFDIR
     WLRASLDIYL DISIWDTMLI HIIDYRGERY SWSKRLAWLE TDMGGYDDAL DGEKPKGEDE
     GNYDLIPWDI LKVYLADDCD VTFRLSEKYI PLVEENEEKK WLWENIMVPG YYTLLDIEMD
     GIHVDREWLE VLRVSYEKEI SRLEDKMREF PEGVAMEREM RDKWKERVMI GNIKSANRTP
     EQQDKFKKYK KYDPSKGGDK INFGSTKQLG ELLFERMGLE TVIFTDKGAP STNDDSLKFM
     GSQSDFVKVL MEFRKANHLY NNFVSKLSLM IDPDNIVHPS YNIHGTVTGR LSSNEPNAQQ
     FPRKVNTPTL FQYNFEIKKM FNSRFGDGGV IVQFDYSQLE LRILVCYYSR PYTIDLYRSG
     ADLHKAVASD AFGVAIEEVS KDQRTASKKI QFGIVYQESA RGLSEDLRAE GITMSEDECE
     IFIKKYFKRF PKVSKWIRDT KKHVKDISTV KTLTGATRNL PDIDSIDQSK ANEAERQAVN
     TPIQGTGSDC TLMSLILINQ WLRESGLRSR ICITVHDSIV LDCPKDEVLE VAKKVKHIME
     NLGEYNEFYK FLGDVPILSE MEIGRNYGDA FEATIEDIEE HGVDGFIEMK EKEKLEKDMK
     EFTKIIEDGG SIPDYARIYW ENIS