AC MF_04100; DC Protein; auto TR HAMAP; MF_04100; -; 1; level=0 XX Names: DPOL_T4 XX ID DPOL DE RecName: Full=DNA-directed DNA polymerase; DE EC=2.7.7.7; DE EC=3.1.11.-; XX 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. 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 -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC -!- SUBUNIT: Part of the replicase complex that includes the DNA CC polymerase, the polymerase clamp, the clamp loader complex, the single- CC stranded DNA binding protein, and the primase/helicase. Interacts with CC the polymerase clamp; this interaction constitutes the polymerase CC holoenzyme. CC -!- DOMAIN: The N-terminus contains the 3'-5' exonuclease activity. The C- CC terminus contains the polymerase activity and is involved in binding to CC the polymerase clamp protein. A beta hairpin structure is necessary for CC the proofreading function of the polymerase. CC -!- SIMILARITY: Belongs to the DNA polymerase type-B family. XX DR PROSITE; PS00116; DNA_POLYMERASE_B; 1; trigger=no DR Pfam; PF00136; DNA_pol_B; 1; trigger=no DR Pfam; PF03104; DNA_pol_B_exo1; 1; trigger=no XX KW DNA replication KW DNA-binding KW DNA-directed DNA polymerase KW Exonuclease KW Hydrolase KW Magnesium KW Metal-binding KW Multifunctional enzyme KW Nuclease KW Nucleotidyltransferase KW Transferase KW Viral DNA replication XX GO GO:0008408; F:3'-5' exonuclease activity GO GO:0003677; F:DNA binding GO GO:0003887; F:DNA-directed DNA polymerase activity GO GO:0000166; F:nucleotide binding GO GO:0039686; P:bidirectional double-stranded viral DNA replication XX FT From: DPOL_BPT4 (P04415) FT REGION 101..337 FT /note="3'-5'exonuclease" FT REGION 245..261 FT /note="Beta hairpin" FT REGION 377..Cter FT /note="Polymerase" FT REGION 893..Cter FT /note="Interaction with the polymerase clamp" FT BINDING 112 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /ligand_note="catalytic; for 3'-5' exonuclease FT activity" FT Condition: D FT BINDING 114 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /ligand_note="catalytic; for 3'-5' exonuclease FT activity" FT Condition: E FT BINDING 219 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /ligand_note="catalytic; for 3'-5' exonuclease FT activity" FT Condition: D FT BINDING 324 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /ligand_note="catalytic; for 3'-5' exonuclease FT activity" FT Condition: D FT BINDING 324 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /ligand_note="catalytic; for 3'-5' exonuclease FT activity" FT Condition: D FT From: DPOL_BPR69 (Q38087) FT BINDING 414..416 FT /ligand="substrate" FT Condition: S-L-Y FT BINDING 482 FT /ligand="substrate" FT Condition: R FT BINDING 560 FT /ligand="substrate" FT Condition: K FT REGION 705..708 FT /note="Binding of DNA in B-conformation" FT Condition: K-K-R-Y FT BINDING 411 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="3" FT /ligand_note="catalytic; for polymerase activity" FT Condition: D FT BINDING 411 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="4" FT /ligand_note="catalytic; for polymerase activity" FT Condition: D FT BINDING 412 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="4" FT /ligand_note="catalytic; for polymerase activity" FT Condition: L FT BINDING 623 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="3" FT /ligand_note="catalytic; for polymerase activity" FT Condition: D FT BINDING 623 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="4" FT /ligand_note="catalytic; for polymerase activity" FT Condition: D FT SITE 621 FT /note="Optimization of metal coordination by the polymerase FT active site" FT Condition: D FT SITE 706 FT /note="Optimization of metal coordination by the polymerase FT active site" FT Condition: K FT SITE 714 FT /note="Essential for viral replication" FT Condition: D XX Size: 828-998; Related: None; Template: P04415; Q38087; Scope: Viruses; Caudoviricetes Fusion: Nter: None Cter: None Duplicate: None Plasmid: None Comments: None XX # Revision 1.9 2022/11/19 //