ID DPOL_BPCP1 Reviewed; 568 AA.
AC Q37989;
DT 31-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 27-MAR-2024, entry version 109.
DE RecName: Full=DNA polymerase;
DE EC=2.7.7.7;
DE EC=3.1.11.- {ECO:0000250|UniProtKB:P03680};
GN Name=5;
OS Streptococcus phage Cp-1 (Bacteriophage Cp-1).
OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC Salasmaviridae; Cepunavirus; Cepunavirus Cp1.
OX NCBI_TaxID=10747;
OH NCBI_TaxID=1313; Streptococcus pneumoniae.
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7645213; DOI=10.1006/viro.1995.1375;
RA Martin A.C., Lopez R., Garcia P.;
RT "Nucleotide sequence and transcription of the left early region of
RT Streptococcus pneumoniae bacteriophage Cp-1 coding for the terminal protein
RT and the DNA polymerase.";
RL Virology 211:21-32(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=8648702; DOI=10.1128/jvi.70.6.3678-3687.1996;
RA Martin A.C., Lopez R., Garcia P.;
RT "Analysis of the complete nucleotide sequence and functional organization
RT of the genome of Streptococcus pneumoniae bacteriophage Cp-1.";
RL J. Virol. 70:3678-3687(1996).
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:P03680}.
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 -!- 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; Z47794; CAA87725.1; -; Genomic_DNA.
DR PIR; S51275; S51275.
DR RefSeq; NP_044817.1; NC_001825.1.
DR SMR; Q37989; -.
DR IntAct; Q37989; 1.
DR GeneID; 1261225; -.
DR KEGG; vg:1261225; -.
DR OrthoDB; 4562at10239; -.
DR Proteomes; UP000009089; 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:0001882; F:nucleoside binding; IEA:InterPro.
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; 1.10.287.690; Helix hairpin bin; 1.
DR Gene3D; 3.90.1600.10; Palm domain of DNA polymerase; 1.
DR Gene3D; 3.30.420.10; Ribonuclease H-like superfamily/Ribonuclease H; 1.
DR Gene3D; 3.30.1770.10; TPR 1 domain of DNA polymerase; 1.
DR InterPro; IPR006172; DNA-dir_DNA_pol_B.
DR InterPro; IPR017964; DNA-dir_DNA_pol_B_CS.
DR InterPro; IPR004868; DNA-dir_DNA_pol_B_mt/vir.
DR InterPro; IPR014416; DNA-dir_DNA_polB_phi29_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 PANTHER; PTHR33568; DNA POLYMERASE; 1.
DR PANTHER; PTHR33568:SF3; DNA-DIRECTED DNA POLYMERASE; 1.
DR Pfam; PF03175; DNA_pol_B_2; 1.
DR PIRSF; PIRSF004178; Dpol_Bac_phage; 1.
DR PRINTS; PR00106; DNAPOLB.
DR SUPFAM; SSF56672; DNA/RNA polymerases; 1.
DR SUPFAM; SSF53098; Ribonuclease H-like; 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; Nuclease; Nucleotidyltransferase; Reference proteome;
KW Transferase; Viral DNA replication.
FT CHAIN 1..568
FT /note="DNA polymerase"
FT /id="PRO_0000046541"
SQ SEQUENCE 568 AA; 66149 MW; 515F5EAEF1897896 CRC64;
MTCYYAGDFE TTTNEEETEV WLSCFAKVID YDKLDTFKVN TSLEDFLKSL YLDLDKTYTE
TGEDEFIIFF HNLKFDGSFL LSFFLNNDIE CTYFINDMGV WYSITLEFPD FTLTFRDSLK
ILNFSIATMA GLFKMPIAKG TTPLLKHKPE VIKPEWIDYI HVDVAILARG IFAMYYEENF
TKYTSASEAL TEFKRIFRKS KRKFRDFFPI LDEKVDDFCR KHIVGAGRLP TLKHRGRTLN
QLIDIYDINS MYPATMLQNA LPIGIPKRYK GKPKEIKEDH YYIYHIKADF DLKRGYLPTI
QIKKKLDALR IGVRTSDYVT TSKNEVIDLY LTNFDLDLFL KHYDATIMYV ETLEFQTESD
LFDDYITTYR YKKENAQSPA EKQKAKIMLN SLYGKFGAKI ISVKKLAYLD DKGILRFKND
DEEEVQPVYA PVALFVTSIA RHFIISNAQE NYDNFLYADT DSLHLFHSDS LVLDIDPSEF
GKWAHEGRAV KAKYLRSKLY IEELIQEDGT THLDVKGAGM TPEIKEKITF ENFVIGATFE
GKRASKQIKG GTLIYETTFK IRETDYLV
//
