UniProt functional annotation for Q9T1C3



	UniProt functional annotation for Q9T1C3

UniProt code: Q9T1C3.

Organism: Escherichia phage RB49 (Bacteriophage RB49).

Taxonomy: Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes; Caudovirales; Myoviridae; Tevenvirinae; Krischvirus.

Function: The terminase large subunit acts as an ATP driven molecular motor necessary for viral DNA translocation into empty capsids and as an endonuclease that cuts the viral genome to initiate and to end a packaging reaction. The terminase lies at a unique vertex of the procapsid and is composed of two subunits, a small terminase subunit involved in viral DNA recognition (packaging sequence), and a large terminase subunit possessing endonucleolytic and ATPase activities. Both terminase subunits heterooligomerize and are docked on the portal protein to form the packaging machine. The terminase large subunit exhibits endonuclease activity and cleaves the viral genome concatemer. Once the capsid is packaged with the DNA, the terminase complex is substituted by the tail. {ECO:0000256|HAMAP-Rule:MF_04146}.

Cofactor: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP-Rule:MF_04146}; Note=ATPase activity requires 1 Mg(2+) ion per subunit. Nuclease activity probably requires 2 Mg(2+) ions per subunit. {ECO:0000256|HAMAP-Rule:MF_04146};

Subunit: Interacts with the terminase small subunit; the active complex is probably heterooligomeric. Interacts with the portal protein. {ECO:0000256|HAMAP-Rule:MF_04146}.

Domain: The N-terminus contains an ATPase domain. The C-terminus contains an endonuclease domain. {ECO:0000256|HAMAP-Rule:MF_04146}.

Similarity: Belongs to the Tequatrovirus large terminase family. {ECO:0000256|HAMAP-Rule:MF_04146}.

Annotations taken from UniProtKB at the EBI.


Organism:		Escherichia phage RB49 (Bacteriophage RB49).
Taxonomy:		Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes; Caudovirales; Myoviridae; Tevenvirinae; Krischvirus.



Function:		The terminase large subunit acts as an ATP driven molecular motor necessary for viral DNA translocation into empty capsids and as an endonuclease that cuts the viral genome to initiate and to end a packaging reaction. The terminase lies at a unique vertex of the procapsid and is composed of two subunits, a small terminase subunit involved in viral DNA recognition (packaging sequence), and a large terminase subunit possessing endonucleolytic and ATPase activities. Both terminase subunits heterooligomerize and are docked on the portal protein to form the packaging machine. The terminase large subunit exhibits endonuclease activity and cleaves the viral genome concatemer. Once the capsid is packaged with the DNA, the terminase complex is substituted by the tail. {ECO:0000256\|HAMAP-Rule:MF_04146}.


Cofactor:		Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256\|HAMAP-Rule:MF_04146}; Note=ATPase activity requires 1 Mg(2+) ion per subunit. Nuclease activity probably requires 2 Mg(2+) ions per subunit. {ECO:0000256\|HAMAP-Rule:MF_04146};
Subunit:		Interacts with the terminase small subunit; the active complex is probably heterooligomeric. Interacts with the portal protein. {ECO:0000256\|HAMAP-Rule:MF_04146}.
Domain:		The N-terminus contains an ATPase domain. The C-terminus contains an endonuclease domain. {ECO:0000256\|HAMAP-Rule:MF_04146}.
Similarity:		Belongs to the Tequatrovirus large terminase family. {ECO:0000256\|HAMAP-Rule:MF_04146}.