AC MF_04145; DC Protein; auto TR HAMAP; MF_04145; -; 1; level=0 XX Names: TERL_SPP1 XX ID TERL DE RecName: Full=Terminase, large subunit; DE AltName: Full=DNA-packaging protein; DE Includes: DE RecName: Full=Endonuclease; DE EC=3.1.-.-; DE Includes: DE RecName: Full=ATPase; DE EC=3.6.4.-; XX CC -!- FUNCTION: The terminase large subunit acts as an ATP driven molecular CC motor necessary for viral DNA translocation into empty capsids and as CC an endonuclease that cuts the viral genome to initiate and to end a CC packaging reaction. The terminase lies at a unique vertex of the CC procapsid and is composed of two subunits, a small terminase subunit CC involved in viral DNA recognition (packaging sequence), and a large CC terminase subunit possessing endonucleolytic and ATPase activities. CC Both terminase subunits heterooligomerize and are docked on the portal CC protein to form the packaging machine. The terminase large subunit CC exhibits endonuclease activity and cleaves the viral genome concatemer CC once the capsid is full (headful packaging). Once the capsid is CC packaged with the DNA, the terminase complex is substituted by the CC adapter and the stopper protein that form the connector. case CC -!- COFACTOR: CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Note=Binds 2 divalent metal cations per subunit. Mn(2+) is preferred CC over Mg(2+).; end case CC -!- SUBUNIT: Monomer. Interacts with the terminase small subunit; the CC active complex is probably heterooligomeric. Interacts with the portal CC protein. CC -!- DOMAIN: The N-terminus contains an ATPase domain and the C-terminus CC contains an endonuclease domain. XX DR Pfam; PF04466; Terminase_3; 1; trigger=no DR Pfam; PF17288; Terminase_3C; 1; trigger=no DR NCBIfam; TIGR01547; phage_term_2; 1; trigger=no XX KW ATP-binding KW Endonuclease KW Nucleotide-binding KW Hydrolase case KW Magnesium KW Manganese KW Metal-binding end case KW Nuclease KW Viral genome packaging KW Viral release from host cell XX GO GO:0098009; C:viral terminase, large subunit GO GO:0004519; F:endonuclease activity GO GO:0046872; F:metal ion binding GO GO:0004518; F:nuclease activity GO GO:0051276; P:chromosome organization GO GO:0019073; P:viral DNA genome packaging XX FT From: TERL_BPSPP (P54308) FT REGION 1..198 FT /note="ATPase activity" FT REGION 232..422 FT /note="Nuclease activity and binding to the portal protein" FT MOTIF 33..40 FT /note="Walker A motif" FT Condition: G-[GS]-[AR]-[AG]-S-[AGK]-[AGK]-S FT MOTIF 130..135 FT /note="Walker B motif" FT Condition: x-[CAGLM]-W-[IFY]-E-E FT ACT_SITE 135 FT /note="For ATPase activity" FT Condition: E FT BINDING 266 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="1" FT /ligand_note="catalytic; for nuclease activity" FT Group: 1; Condition: D FT BINDING 266 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT /ligand_note="catalytic; for nuclease activity" FT Group: 1; Condition: D FT BINDING 321 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="1" FT /ligand_note="catalytic; for nuclease activity" FT Group: 1; Condition: D FT BINDING 400 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT /ligand_note="catalytic; for nuclease activity" FT Group: 1; Condition: H FT BINDING 403 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT /ligand_note="catalytic; for nuclease activity" FT Group: 1; Condition: D XX Size: 370-540; Related: None; Template: P54308; Scope: Viruses; Caudoviricetes Fusion: Nter: None Cter: None Duplicate: None Plasmid: None Comments: None XX # Revision 1.9 2023/06/01 //