AC   MF_04014;
DC   Protein; auto
TR   HAMAP; MF_04014; -; 1; level=0
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Names: HSV_TRM1
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ID   TRM1
DE   RecName: Full=Tripartite terminase subunit 1;
GN   Name=TRM1;
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CC   -!- FUNCTION: Component of the molecular motor that translocates viral
CC       genomic DNA in empty capsid during DNA packaging. Forms a tripartite
CC       terminase complex together with TRM2 and TRM3 in the host cytoplasm.
CC       Once the complex reaches the host nucleus, it interacts with the capsid
CC       portal vertex. This portal forms a ring in which genomic DNA is
CC       translocated into the capsid. TRM1 carries an endonuclease activity
CC       that plays an important role for the cleavage of concatemeric viral DNA
CC       into unit length genomes.
CC   -!- SUBUNIT: Associates with TRM2 and TRM3 to form the tripartite terminase
CC       complex. Interacts with portal protein.
CC   -!- SUBCELLULAR LOCATION: Host nucleus. Note=Found associated with the
CC       external surface of the viral capsid during assembly and DNA packaging,
CC       but seems absent in extracellular mature virions.
CC   -!- SIMILARITY: Belongs to the herpesviridae TRM1 protein family.
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DR   Pfam; PF01366; PRTP; 1; trigger=no
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KW   ATP-binding
KW   Host nucleus
KW   Late protein
KW   Metal-binding
KW   Nucleotide-binding
KW   Viral genome packaging
KW   Viral release from host cell
case <FTTag:Zinc>
KW   Zinc
KW   Zinc-finger
end case
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GO   GO:0042025; C:host cell nucleus
GO   GO:0016485; P:protein processing
GO   GO:0019069; P:viral capsid assembly
GO   GO:0019076; P:viral release from host cell
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FT   From: TRM1_HCMVM (F5HC79)
FT   ZN_FING         191..219
FT                   /note="C3H1-type"
FT   Tag: Zinc; Condition: C-x(2)-C-x(22)-C-x-H
FT   BINDING         709..716
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT   Condition: [YF]-x(3)-[WYF]-x(3)
FT   MOTIF           822..827
FT                   /note="Nuclear localization signal"
FT   Condition: R-K-R-P-R-R
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Size: 664-850;
Related: None;
Template: F5HC79; P10212;
Scope:
 Viruses; Herpesviridae
Fusion:
 Nter: None
 Cter: None
Duplicate: None
Plasmid: None
Comments: None
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# Revision 1.8 2022/11/19
//