The domain within your query sequence starts at position 844 and ends at position 908; the E-value for the POLO_box domain shown below is 1.6e-15.



PFAM accession number:PF00659
Interpro abstract (IPR000959):

A subgroup of serine/threonine protein kinases, Polo or Polo-like kinases play multiple roles during the cell cycle. Polo kinases are required at several key points through mitosis, starting from control of the G2/M transition through phosphorylation of Cdc25C and mitotic cyclins. They are also involved in meiosis I as regulators of kinetochore function [ (PUBMED:22018922) (PUBMED:25533956) ]. Polo kinases are characterised by an amino terminal catalytic domain, and a carboxy terminal non-catalytic domain consisting of three blocks of conserved sequences known as polo boxes which form one single functional domain [ (PUBMED:9914175) ]. The domain is named after its founding member encoded by the polo gene of Drosophila melanogaster [ (PUBMED:1660828) ]. This domain of around 70 amino acids has been found in species ranging from yeast to mammals. Polo boxes appear to mediate interaction with multiple proteins through protein:protein interactions; some but not all of these proteins are substrates for the kinase domain of the molecule [ (PUBMED:12615979) ].

The crystal structure of the polo domain of the murine protein, Sak, is dimeric, consisting of two alpha-helices and two six-stranded beta-sheets [ (PUBMED:12352953) ]. The topology of one polypeptide subunit of the dimer consists of, from its N- to C terminus, an extended strand segment, five beta-strands, one alpha-helix (A) and C-terminal beta-strand. Beta-strands from one subunit form a contiguous antiparallel beta-sheet with beta-strands from the second subunit. The two beta-sheets pack with crossing angle of 110 degrees, orienting the hydrophobic surfaces inward and the hydrophilic surfaces outward. Helix A, which is colinear with beta-strand 6 of the same polypeptide, buries a large portion of the non-overlapping hydrophobic beta-sheet surfaces.Interactions involving helices A comprise a majority of the hydrophobic core structure and also the dimer interface.

Point mutations in the Polo box of the budding yeast Cdc5 protein abolish the ability of overexpressed Cdc5 to interact with the spindle poles and to organise cytokinetic structures [ (PUBMED:10594031) ].

GO function:protein binding (GO:0005515)

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