UniProt functional annotation for P07917

UniProt code: P07917.

Organism:		Human herpesvirus 1 (strain Angelotti) (HHV-1) (Human herpes simplex virus 1).
Taxonomy:		Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes; Herpesvirales; Herpesviridae; Alphaherpesvirinae; Simplexvirus.
Function:		Replicates viral genomic DNA. The replication complex is composed of six viral proteins: the DNA polymerase, processivity factor, primase, primase-associated factor, helicase, and ssDNA-binding protein. Additionally, the polymerase contains an intrinsic ribonuclease H (RNase H) activity that specifically degrades RNA/DNA heteroduplexes or duplex DNA substrates in the 5' to 3' direction. Therefore, it can catalyze the excision of the RNA primers that initiate the synthesis of Okazaki fragments at a replication fork during viral DNA replication (By similarity). {ECO:0000250}.
Catalytic activity:		Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:11130, Rhea:RHEA-COMP:11131, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560, ChEBI:CHEBI:83828; EC=2.7.7.7;
Catalytic activity:		Reaction=Endonucleolytic cleavage to 5'-phosphomonoester.; EC=3.1.26.4;
Subunit:		Forms a complex with the ssDNA-binding protein UL29, the DNA polymerase processivity factor, and the alkaline exonuclease. Interacts with the putative helicase-primase complex subunit UL8; this interaction may coordinate leading and lagging strand DNA synthesis at the replication fork (By similarity). {ECO:0000250}.
Subcellular location:		Host nucleus {ECO:0000305}. Note=The protein is present at discrete sites in nuclei, called replication compartments where viral DNA replication occurs. {ECO:0000250}.
Similarity:		Belongs to the DNA polymerase type-B family. {ECO:0000305}.

Annotations taken from UniProtKB at the EBI.