Summary: POLO box duplicated region
POLO box duplicated region Provide feedback
No Pfam abstract.
Leung GC, Hudson JW, Kozarova A, Davidson A, Dennis JW, Sicheri F; , Nat Struct Biol. 2002;9:719-724.: The Sak polo-box comprises a structural domain sufficient for mitotic subcellular localization. PUBMED:12352953 EPMC:12352953
Internal database links
|Similarity to PfamA using HHSearch:||DUF4520 DUF4524|
External database links
This tab holds annotation information from the InterPro database.
InterPro entry 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. 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 a 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 a 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].
|Molecular function||protein binding (GO:0005515)|
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Curation and family details
|Author:||Bateman A, Mistry J, Sammut SJ|
|Number in seed:||246|
|Number in full:||1739|
|Average length of the domain:||66.80 aa|
|Average identity of full alignment:||25 %|
|Average coverage of the sequence by the domain:||17.60 %|
|HMM build commands:||
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 26740544 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||17|
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There are 3 interactions for this family. More...
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For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the POLO_box domain has been found. There are 136 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein seqence.
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