The domain within your query sequence starts at position 697 and ends at position 743; the E-value for the KA1 domain shown below is 2.5e-21.



PFAM accession number:PF02149
Interpro abstract (IPR001772):

Members of the KIN2/PAR-1/MARK kinase subfamily are conserved from yeast to human and share the same domain organisation: an N-terminal kinase domain ( IPR000719 ) and a C-terminal kinase associated domain 1 (KA1). Some members of the KIN1/PAR-1/MARK family also contain an UBA domain ( IPR015940 ). Members of this kinase subfamily are involved in various biological processes such as cell polarity, cell cycle control, intracellular signalling, microtubule stability and protein stability [ (PUBMED:15182702) ]. The function of the KA1 domain is not yet known but several studies strongly suggest that it is involved in protein localisation. In addition, it has been reported that this C-terminal region acts as an autoinhibitory domain for the N‐terminal kinase domain [ (PUBMED:17075132) ].

Some proteins known to contain a KA1 domain are listed below:
  • Mammalian MAP/microtubule affinity-regulating kinases (MARK 1,2,3). They regulate polarity in neuronal cell models and appear to function redundantly in phosphorylating MT-associated proteins and in regulating MT stability [ (PUBMED:12429843) ].
  • Mammalian maternal embryonic leucine zipper kinase (MELK). It phosphorylates ZNF622 and may contribute to its redirection to the nucleus. It may be involved in the inhibition of spliceosome assembly during mitosis.
  • Caenorhabditis elegans and drosophila PAR-1 protein. It is required for establishing polarity in embryos where it is asymmetrically distributed [ (PUBMED:7758115) ].
  • Fungal Kin1 and Kin2 protein kinases involved in regulation of exocytosis. They localise to the cytoplasmic face of the plasma membrane [ (PUBMED:15563607) ].

The KA1 domain comprises about 50 amino acid residues and end in the highly conserved Glu‐Leu‐Lys‐Leu motif, termed the ELKL motif which forms a concave surface surrounded by positively charged residues, being important for the KA1 domain function. This domain adopts a compact alpha+beta structure with a beta-alpha-beta-beta-beta-beta-alpha topology [ (PUBMED:17075132) ].

This is a PFAM domain. For full annotation and more information, please see the PFAM entry KA1