InterPro domain: IPR038749

Sld5 is a component of GINS tetrameric protein complex, and within the complex Sld5 interacts with Psf1 via its N-terminal A-domain, and with Psf2 through a combination of the A and B domains [ 1 , 2 ]. Sld5 in Drosophila is required for normal cell cycle progression and the maintenance of genomic integrity [ 3 ]. GINS is a complex of four subunits (Sld5, Psf1, Psf2 and Psf3) that is involved in both initiation and elongation stages of eukaryotic chromosome replication [ 4 ]. Besides being essential for the maintenance of genomic integrity, GINS plays a central role in coordinating DNA replication with cell cycle checkpoints and is involved in cell growth. The eukaryotic GINS subunits are homologous and homologues are also found in the archaea; the complex is not found in bacteria. 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 [ 5 , 6 , 7 , 8 , 9 , 10 , 11 ].

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2. New insights into the GINS complex explain the controversy between existing structural models. Sci Rep 7, 40188
3. Drosophila Sld5 is essential for normal cell cycle progression and maintenance of genomic integrity. Biochem. Biophys. Res. Commun. 400, 145-50
4. GINS, a novel multiprotein complex required for chromosomal DNA replication in budding yeast. Genes Dev. 17, 1153-65
5. Crystal structure of the GINS complex and functional insights into its role in DNA replication. Proc. Natl. Acad. Sci. U.S.A. 104, 12685-90
6. Identification and characterization of mouse PSF1-binding protein, SLD5. Biochem. Biophys. Res. Commun. 339, 1204-7
7. Structure and function of the GINS complex, a key component of the eukaryotic replisome. Biochem. J. 425, 489-500
8. A key role for the GINS complex at DNA replication forks. Trends Cell Biol. 17, 271-8
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10. Crystal structure of the human GINS complex. Genes Dev. 21, 1316-21
11. The Cdc45·Mcm2-7·GINS protein complex in trypanosomes regulates DNA replication and interacts with two Orc1-like proteins in the origin recognition complex. J. Biol. Chem. 286, 32424-35