The domain within your query sequence starts at position 287 and ends at position 505; the E-value for the UNC45-central domain shown below is 3.5e-44.

PARELKVLINSLLELLTEVGVSGQGRDNALTLLIKMVPRKSPKDPNNSLTLWVIDQGLKK
ILEVGGSLQDAAGELTVTANSRMSASILLSKLFDDLKCDAERENFHRLCENYIRNWFEGH
GLAGKLRAIQTVSCLLQGPCDAGNRALELSGVMESVIALCASEREEEQLVAVEALIHAAG
KAKRASFITANGVSLLKDLYKGSERDSIRIRALVGLCKL

UNC45-central

UNC45-central
PFAM accession number:PF11701
Interpro abstract (IPR024660):

The UNC-45 protein contain an NH2-terminal domain with three tetratricopeptide repeat motifs, a unique central domain, and a COOH-terminal domain homologous to CRO1 and She4 [ (PUBMED:9832550) ]. This entry represents the central domain of the UNC-45 protein.

The UNC-45 or small muscle protein 1 of Caenorhabditis elegans is expressed in two forms from different genomic positions in mammals: as a general tissue protein (UNC-45a) and as a specific form (UNC-45b) expressed only in striated and skeletal muscle. Myofibril formation requires both UNC-45 forms, consistent with the fact that the cytoskeleton is necessary for the development and maintenance of organised myofibrils [ (PUBMED:12356907) ]. Rng3 (Ring assembly protein 3), the homologue in Schizosaccharomyces pombe, is crucial for cell shape, normal actin cytoskeleton, and contractile ring assembly, and is essential for assembly of the myosin II-containing progenitors of the contractile ring. Widespread defects in the cytoskeleton are found in null mutants of all three fungal proteins [ (PUBMED:18523008) ]. Mammalian Unc45 is found to act as a specific chaperone during the folding of myosin and the assembly of striated muscle by forming a stable complex with the general chaperone Hsp90 [ (PUBMED:18478096) ].

This is a PFAM domain. For full annotation and more information, please see the PFAM entry UNC45-central