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11  structures 506  species 0  interactions 609  sequences 11  architectures

Clan: DNA_primase_lrg (CL0242)

Summary

DNA primase large subunit like Add an annotation

This clan contains the large subunit of archaeal and eukaryotic DNA primase, an enzyme which synthesises the oligoribonucleotide primers essential to DNA replication. The large subunit of DNA primase forms interactions with the small subunit and the structure implicates that it is not directly involved in catalysis, but plays a roles in correctly positioning the primase/DNA complex, and in the transfer of RNA to DNA polymerase [1]. The clan also contains the Lef-2 family, which is required for the expression of late genes. There is some evidence to suggest that LEF2 binds to both DNA and the DNA primase small subunit LEF-1 [3].

This clan contains 2 families and the total number of domains in the clan is 609. The clan was built by J Mistry.

Literature references

  1. Lao-Sirieix SH, Nookala RK, Roversi P, Bell SD, Pellegrini L; , Nat Struct Mol Biol. 2005;12:1137-1144.: Structure of the heterodimeric core primase. PUBMED:16273105 EPMC:16273105
  2. Ahrens CH, Rohrmann GF; , Virology 1995;212:650-662.: Replication of Orgyia pseudotsugata baculovirus DNA: lef-2 and ie-1 are essential and ie-2, p34, and Op-iap are stimulatory genes. PUBMED:7571435 EPMC:7571435
  3. Mikhailov VS, Rohrmann GF; , J Virol 2002;76:2287-2297.: Baculovirus replication factor LEF-1 is a DNA primase. PUBMED:11836407 EPMC:11836407

Members

This clan contains the following 2 member families:

Baculo_LEF-2 DNA_primase_lrg

Domain organisation

Below is a listing of the unique domain organisations or architectures from this clan. More...

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Alignments

The table below shows the number of occurrences of each domain throughout the sequence database. More...

Pfam family Num. domains Alignment
DNA_primase_lrg (PF04104) 540 (88.7%) View
Baculo_LEF-2 (PF03041) 69 (11.3%) View
Total: 2 Total: 609 Clan alignment
 

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Family relationships

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Species distribution

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Structures

For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the MSD group, to allow us to map Pfam domains onto UniProt three-dimensional structures. The table below shows the mapping between the Pfam families in this clan, the corresponding UniProt entries, and the region of the three-dimensional structures that are available for that sequence.

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