The domain within your query sequence starts at position 66 and ends at position 173; the E-value for the Sld5 domain shown below is 1.3e-10.



PFAM accession number:PF05916
Interpro abstract (IPR021151):

The GINS complex is essential for initiation of DNA replication in Xenopus egg extracts [ (PUBMED:12730133) ]. This 100kDa stable complex includes Sld5, Psf1, Psf2, and Psf3. Homologues of these components are found also in other eukaryotes [ (PUBMED:12730134) ]. The archaeal GINS complex contains two subunits (SSO0772/gins23 and SO1049/gins15 in Sulfolobus) that are poorly conserved homologues of the eukaryotic GINS subunits [ (PUBMED:16485022) ]. Only Gins23 is included in this entry.

The eukaryotic GINS subunits are homologous. The four subunits of the complex consist of two domains each, termed the alpha-helical (A) and beta-strand (B) domains. The A and B domains of Sld5/Psf1 are permuted with respect to Psf1/Psf3 [ (PUBMED:17417653) ].

DNA replication in eukaryotes results from a highly coordinated interaction between proteins, often as part of protein complexes, and the DNA template. One of the key early steps leading to DNA replication is formation of the pre-replication complex, or pre-RC. The pre-RC is formed by the sequential binding of the origin recognition complex (ORC), Cdc6 and Cdt1 proteins, and the MCM complex. Activation of the pre-RC into the initiation complex (IC) is achieved via the action of S-phase kinases, eventually leading to the loading of the replication machinery.

Recently, a novel replication complex, GINS (for Go, Ichi, Nii, and San; five, one, two, and three in Japanese), has been identified [ (PUBMED:12730133) (PUBMED:12730134) ]. The precise function of GINS is not known. However, genetic and two-hybrid interactions indicate that it mediates the loading of the enzymatic replication machinery at a step after the action of the S-phase kinases [ (PUBMED:12730134) ]. Furthermore, GINS may be a part of the replication machinery itself, since it is found associated with replicating DNA [ (PUBMED:12730133) (PUBMED:12730134) ]. Electron microscopy of GINS shows that it forms a ring-like structure [ (PUBMED:12730133) ], reminiscent of the structure of PCNA [ (PUBMED:8001157) ], the DNA polymerase delta replication clamp.This observation, coupled with the observed interactions for GINS, indicates that the complex may represent the replication clamp for DNA polymerase epsilon [ (PUBMED:12730133) ].

This is a PFAM domain. For full annotation and more information, please see the PFAM entry Sld5