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Database: UniProt
Entry: A0A068YGT4_BPCP7
LinkDB: A0A068YGT4_BPCP7
Original site: A0A068YGT4_BPCP7 
ID   A0A068YGT4_BPCP7        Unreviewed;       568 AA.
AC   A0A068YGT4;
DT   01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 41.
DE   RecName: Full=DNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00012417};
DE            EC=2.7.7.7 {ECO:0000256|ARBA:ARBA00012417};
OS   Streptococcus phage Cp-7 (Bacteriophage Cp-7).
OC   Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC   Salasmaviridae; Cepunavirus; Cepunavirus Cp7.
OX   NCBI_TaxID=10748 {ECO:0000313|EMBL:CDS43806.1, ECO:0000313|Proteomes:UP000027387};
OH   NCBI_TaxID=1313; Streptococcus pneumoniae.
RN   [1] {ECO:0000313|EMBL:CDS43806.1, ECO:0000313|Proteomes:UP000027387}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Garcia E.;
RL   Submitted (MAY-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:CDS43806.1, ECO:0000313|Proteomes:UP000027387}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Diez-Martinez R.;
RT   "Estudios estructurales y funcionales de la lisozima Cpl-7, del
RT   bacteriofago Cp-7 de neumococo.";
RL   Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases.
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:0000256|ARBA:ARBA00024632};
CC   -!- SIMILARITY: Belongs to the DNA polymerase type-B family.
CC       {ECO:0000256|ARBA:ARBA00005755}.
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DR   EMBL; LK392619; CDS43806.1; -; Genomic_DNA.
DR   OrthoDB; 4562at10239; -.
DR   Proteomes; UP000027387; 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 {ECO:0000256|ARBA:ARBA00022705};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW   DNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00022932};
KW   Exonuclease {ECO:0000256|ARBA:ARBA00022839};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Nuclease {ECO:0000256|ARBA:ARBA00022722};
KW   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695};
KW   Reference proteome {ECO:0000313|Proteomes:UP000027387};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Viral DNA replication {ECO:0000256|ARBA:ARBA00023109}.
FT   DOMAIN          148..478
FT                   /note="DNA-directed DNA polymerase family B
FT                   mitochondria/virus"
FT                   /evidence="ECO:0000259|Pfam:PF03175"
SQ   SEQUENCE   568 AA;  66149 MW;  4DEA127E0F655FDE CRC64;
     MTCYYAGDFE TTTNEEETEV WLSCFAKVID YDKLDTFKVN TSLEDFLKSL YLDLDKTYTE
     TGEDEFIIFF HNLKFDGSFL LSFFLNNDIE CTYFINDMGV WYSITLEFPD FTLTFRDSLK
     ILNFSIATMA GLFKMPIAKG TTPLLKHKPD EIKPEWIDYI HVDVAILARG IFAMYYEENF
     SKYTSASEAL TEFKRIFRKS KRKFRDFFPI LDEKVDDFCR KAYRGGWTFA NPKTQGRTLK
     QLIDIYDINS MYPATMLQNA LPIGIPKRYK GKPKEIKEDH YYIYHIKADF DLKRGYLPTI
     QIKKKLDALR IGVRTSDYVT TSKNEVIDLY LTNFDLDLFL KHYDATIMYV ETLEFQTESG
     LFDDYITTYR YKKENAQSPA EKQKAKIMLN SLYGKFGAKI ISVKKLAYLD DKGILRFKND
     DEEEVQPVYA PVALFVTSIA RHFIISNAQE NYDNFLYADT DSLHLFHSDS LVLDIDPSEF
     GKWAHEGRAV KAKYLRSKLY IEELIQEDGT THLDVKGAGM TPEIKEKITF ENFVIGATFE
     GKRASKQIKG GTLIYETTFK IRETDYLV
//
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