AC   MF_04147;
DC   Protein; auto
TR   HAMAP; MF_04147; -; 1; level=0
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Names: TERL_T7
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ID   TERL
DE   RecName: Full=Terminase, large subunit;
DE   AltName: Full=DNA-packaging protein;
DE   Includes:
DE     RecName: Full=ATPase;
DE              EC=3.6.4.-;
DE   Includes:
DE     RecName: Full=Endonuclease;
DE              EC=3.1.21.-;
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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 at a unique and precise
CC       dsDNA sequence to initiate and to end a packaging reaction. The
CC       terminase lies at a unique vertex of the procapsid and is composed of
CC       two subunits, a small terminase subunit involved in viral DNA
CC       recognition (packaging sequence), and a large terminase subunit
CC       possessing endonucleolytic and ATPase activities. Both terminase
CC       subunits heterooligomerize and are docked on the portal protein to form
CC       the packaging machine. The terminase large subunit exhibits
CC       endonuclease activity and cleaves the viral genome concatemer. Once the
CC       DNA is packaged, the terminase detaches from the portal and gets
CC       replaced by the tail to finish maturation of the virion.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC   -!- SUBUNIT: Homopentamer. Interacts with the terminase small subunit; the
CC       active complex is probably heterooligomeric. Interacts with the portal
CC       protein.
CC   -!- DOMAIN: The ATPase region is in the N-terminus, whereas the nuclease
CC       region is in the central part. The C-terminus is involved in prohead
CC       binding.
CC   -!- SIMILARITY: Belongs to the Teseptimavirus large terminase family.
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KW   ATP-binding
KW   Endonuclease
KW   Hydrolase
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
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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
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FT   From: TERL_BPT7 (P03694)
FT   REGION          1..229
FT                   /note="ATPase activity"
FT   REGION          344..429
FT                   /note="Nuclease activity"
FT   REGION          571..586
FT                   /note="Involved in prohead binding"
FT   MOTIF           58..65
FT                   /note="Walker A motif"
FT   Condition: [AG]-F-R-G-[AIV]-[AG]-K-[ST]
FT   MOTIF           156..161
FT                   /note="Walker B motif"
FT   Condition: [ILV]-[ILM]-[ILV]-[AF]-D-D
FT   BINDING         364
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic; for nuclease activity"
FT   Group: 1; Condition: D
FT   BINDING         364
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /ligand_note="catalytic; for nuclease activity"
FT   Group: 1; Condition: D
FT   BINDING         420
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /ligand_note="catalytic; for nuclease activity"
FT   Group: 1; Condition: E
FT   BINDING         518
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic; for nuclease activity"
FT   Group: 1; Condition: D
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Size: 500-680;
Related: None;
Template: P03694; P10310;
Scope:
 Viruses; Caudoviricetes
Fusion:
 Nter: None
 Cter: None
Duplicate: None
Plasmid: None
Comments: None
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# Revision 1.6 2022/11/19
//