The domain within your query sequence starts at position 130 and ends at position 292; the E-value for the Cnd1 domain shown below is 2.1e-8.



PFAM accession number:PF12717
Interpro abstract (IPR032682):

Condensin is a multi-subunit protein complex that acts as an essential regulator of chromosome condensation [ (PUBMED:20442714) ]. It contains both SMC (structural maintenance of chromosomes) and non-SMC subunits. Condensin plays an important role during mitosis in the compaction and resolution of chromosomes to remove and prevent catenations that would otherwise inhibit segregation. This is thought to be acheived by the introducion of positive supercoils into relaxed DNA in the presence of type I topoisomerases and converts nicked DNA into positive knotted forms in the presence of type II topoisomerases. During interphase condensin promotes clustering of dispersed loci into subnuclear domains and inhibits associations between homologues. In meiosis, condensin has been shown to influence the number of crossover events by regulating programmed double-strand breaks. Roles in gene regulation and lymphocyte development have also been defined.

Condensin subunit 1 (known as Cnd1 in Schizosaccharomyces pombe (Fission yeast), and XCAP-D2 in Xenopus laevis laevis) represents one of the non-SMC subunits in the complex. This subunit is phosphorylated at several sites by Cdc2. This phosphorylation process increases the supercoiling activity of condensin [ (PUBMED:9774278) (PUBMED:10485849) ].

This entry represents the conserved C-terminal domain of Cnd1. It is also found in non-SMC subunit D3 of condensin II, a second condensin complex present in vertebrates [ (PUBMED:14532007) ]. This domain is also found in Sister chromatid cohesion protein PDS5 from Saccharomyces cerevisiae, which is required for the establishment and maintenance of sister chromatid cohesion and chromosomal condensation [ (PUBMED:11062262) ].

This is a PFAM domain. For full annotation and more information, please see the PFAM entry Cnd1