AC   MF_04148;
DC   Protein; auto
TR   HAMAP; MF_04148; -; 1; level=0
XX
Names: TERL_BPP22
XX
ID   TERL
DE   RecName: Full=Terminase, large subunit;
DE   AltName: Full=DNA-packaging protein gp2;
DE   Includes:
DE     RecName: Full=Endonuclease;
DE              EC=3.1.21.-;
DE   Includes:
DE     RecName: Full=ATPase;
DE              EC=3.6.4.-;
XX
case <OC:Lederbergvirus>
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       tail.
else
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. Once the capsid is packaged with
CC       the DNA, the terminase cleaves the viral genome concatemer and is
CC       substituted by the tail.
end case
case <FTGroup:1>
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC       Note=Nuclease activity probably requires 2 Mg(2+) ions per subunit.
end case
CC   -!- SUBUNIT: Interacts with the terminase small subunit; the active complex
CC       is composed of a monomer of the terminase large subunit and a nonamer
CC       ring of terminase small subunits. Interacts with the portal protein;
CC       this interaction allows the packaging of viral DNA.
CC   -!- DOMAIN: The ATPase region is in the N-terminus, whereas the nuclease
CC       region is in the C-terminus.
CC   -!- SIMILARITY: Belongs to the Lederbergvirus large terminase family.
XX
DR   Pfam; PF03237; Terminase_6; 1; trigger=no
DR   Pfam; PF17289; Terminase_6C; 1; trigger=no
XX
KW   ATP-binding
KW   Endonuclease
KW   Hydrolase
KW   Late protein
KW   Nuclease
KW   Nucleotide-binding
KW   Viral genome packaging
KW   Viral release from host cell
case <FTGroup:1>
KW   Magnesium
KW   Metal-binding
end case
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_BPP22 (P26745)
case <OC:Lederbergvirus>
FT   REGION          1..58
FT                   /note="Interaction with the terminase small subunit"
FT   REGION          1..286
FT                   /note="ATPase activity"
FT   REGION          312..482
FT                   /note="Nuclease activity"
end case
FT   MOTIF           60..67
FT                   /note="Walker A motif"
FT   Condition: [ACT]-[AG]-N-[QR]-[CILV]-G-K-[ST]
FT   MOTIF           199..204
FT                   /note="Walker B motif"
FT   Condition: [FGILVWY]-[FIV]-[WH]-[FILM]-D-E
FT   ACT_SITE        204
FT                   /note="For ATPase activity"
FT   Condition: E
FT   BINDING         321
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_note="catalytic; for nuclease activity"
FT   Group: 1; Condition: D
FT   BINDING         459
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_note="catalytic; for nuclease activity"
FT   Group: 1; Condition: D
XX
Size: 400-530;
Related: None;
Template: P26745;
Scope:
 Viruses
Fusion:
 Nter: None
 Cter: None
Duplicate: None
Plasmid: None
Comments: None
XX
# Revision 1.5 2022/11/19
//