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0  structures 214  species 0  interactions 329  sequences 8  architectures

Family: Herpes_UL52 (PF03121)

Summary: Herpesviridae UL52/UL70 DNA primase

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Herpesviridae UL52/UL70 DNA primase Provide feedback

Herpes simplex virus type 1 DNA replication in host cells is known to be mediated by seven viral-encoded proteins, three of which form a heterotrimeric DNA helicase-primase complex. This complex consists of UL5, UL8, and UL52 subunits. Heterodimers consisting of UL5 and UL52 have been shown to retain both helicase and primase activities. Nevertheless, UL8 is still essential for replication: though it lacks any DNA binding or catalytic activities, it is involved in the transport of UL5-UL52 and it also interacts with other replication proteins. The molecular mechanisms of the UL5-UL52 catalytic activities are not known. While UL5 is associated with DNA helicase activity and UL52 with DNA primase activity, the helicase activity requires the interaction of UL5 and UL52 [see 2,3]. It is not known if the primase activity can be maintained by UL52 alone. The region encompassed by residues 610-636 of HSV1 UL52 P10236 is thought to contain a divalent metal cation binding motif. Indeed, this region contains several aspartate and glutamate residues that might be involved in divalent cation binding. The biological significance of UL52-UL8 interaction is not known. Yeast two-hybrid analysis together with immunoprecipitation experiments have shown that the HSV1 UL52 region between residues 366-914 is essential for this interaction, while the first 349 N-terminal residues are dispensable [2]. This family also includes protein UL70 from cytomegalovirus (CMV, a subgroup of the Herpesviridae) strains (e.g. P17149), which, by analogy with UL52, is thought to have DNA primase activity. Indeed, CMV strains also possess a DNA helicase-primase complex, the other subunits being protein UL105 (with known similarity to HSV1 UL5) and protein UL102.

Literature references

  1. Boehmer PE, Lehman IR; , Annu Rev Biochem 1997;66:347-384.: Herpes simplex virus DNA replication. PUBMED:9242911 EPMC:9242911

  2. Constantin N, Dodson MS; , J Gen Virol 1999;80:2411-2415.: Two-hybrid analysis of the interaction between the UL52 and UL8 subunits of the herpes simplex virus type 1 helicase-primase. PUBMED:10501495 EPMC:10501495

  3. Biswas N, Weller SK; , J Biol Chem 2001;276:17610-17619.: The UL5 and UL52 subunits of the herpes simplex virus type 1 helicase-primase subcomplex exhibit a complex interdependence for DNA binding. PUBMED:11278618 EPMC:11278618

  4. Smith JA, Jairath S, Crute JJ, Pari GS; , Virology 1996;220:251-255.: Characterization of the human cytomegalovirus UL105 gene and identification of the putative helicase protein. PUBMED:8659123 EPMC:8659123


External database links

This tab holds annotation information from the InterPro database.

InterPro entry IPR004340

Human herpesvirus 1 (HHV-1) DNA replication in host cells is known to be mediated by seven viral-encoded proteins, three of which form a heterotrimeric DNA helicase-primase complex. This complex consists of UL5, UL8, and UL52 subunits. Heterodimers consisting of UL5 and UL52 have been shown to retain both helicase and primase activities. Nevertheless, UL8 is still essential for replication: though it lacks any DNA binding or catalytic activities, it is involved in the transport of UL5-UL52 and it also interacts with other replication proteins.

The molecular mechanisms of the UL5-UL52 catalytic activities are not known. While UL5 is associated with DNA helicase activity and UL52 with DNA primase activity, the helicase activity requires the interaction of UL5 and UL52 [PUBMED:10501495, PUBMED:11278618]. It is not known if the primase activity can be maintained by UL52 alone. The biological significance of UL52-UL8 interaction is not known. Yeast two-hybrid analysis together with immunoprecipitation experiments have shown that the HHV-1 UL52 region between residues 366-914 is essential for this interaction, while the first 349 N-terminal residues are dispensable [PUBMED:10501495].

This family also includes protein UL70 from cytomegalovirus (CMV, a subgroup of the Herpesviridae) strains which, by analogy with UL52, is thought to have DNA primase activity. Indeed, CMV strains also possess a DNA helicase-primase complex, the other subunits being protein UL105 (with known similarity to HHV-1 UL5) and protein UL102.

Gene Ontology

The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.

Domain organisation

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Pfam Clan

This family is a member of clan AEP (CL0243), which has the following description:

This clan includes the small subunit of 2 and eukaryotic DNA primase, and primase-helicase proteins from bacteriophages and plasmids. All known cellular life forms use primases to synthesis a short RNA primer which is extended during DNA replication by a polymerase. Bacterial DNA primase adopts a different fold to archaeal and eukaryotic primases and belongs to a different superfamily.

The clan contains the following 4 members:

DNA_primase_S Herpes_UL52 Replicase VirE_N

Alignments

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  Seed
(38)
Full
(329)
Representative proteomes NCBI
(310)
Meta
(49)
RP15
(37)
RP35
(49)
RP55
(70)
RP75
(89)
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Format an alignment

  Seed
(38)
Full
(329)
Representative proteomes NCBI
(310)
Meta
(49)
RP15
(37)
RP35
(49)
RP55
(70)
RP75
(89)
Alignment:
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Sequence:
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We make all of our alignments available in Stockholm format. You can download them here as raw, plain text files or as gzip-compressed files.

  Seed
(38)
Full
(329)
Representative proteomes NCBI
(310)
Meta
(49)
RP15
(37)
RP35
(49)
RP55
(70)
RP75
(89)
Raw Stockholm Download   Download   Download   Download   Download   Download   Download   Download  
Gzipped Download   Download   Download   Download   Download   Download   Download   Download  

You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.

External links

MyHits provides a collection of tools to handle multiple sequence alignments. For example, one can refine a seed alignment (sequence addition or removal, re-alignment or manual edition) and then search databases for remote homologs using HMMER3.

Pfam alignments:

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Trees

This page displays the phylogenetic tree for this family's seed alignment. We use FastTree to calculate neighbour join trees with a local bootstrap based on 100 resamples (shown next to the tree nodes). FastTree calculates approximately-maximum-likelihood phylogenetic trees from our seed alignment.

Note: You can also download the data file for the tree.

Curation and family details

This section shows the detailed information about the Pfam family. You can see the definitions of many of the terms in this section in the glossary and a fuller explanation of the scoring system that we use in the scores section of the help pages.

Curation View help on the curation process

Seed source: Pfam-B_203 (release 6.5)
Previous IDs: UL52_UL70;
Type: Family
Author: Mifsud W
Number in seed: 38
Number in full: 329
Average length of the domain: 69.60 aa
Average identity of full alignment: 23 %
Average coverage of the sequence by the domain: 8.88 %

HMM information View help on HMM parameters

HMM build commands:
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 20.8 20.8
Trusted cut-off 21.0 20.8
Noise cut-off 20.2 20.3
Model length: 69
Family (HMM) version: 10
Download: download the raw HMM for this family

Species distribution

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