The domain within your query sequence starts at position 430 and ends at position 760; the E-value for the Hist_deacetyl domain shown below is 9e-92.

KHQCSCGDNSKHPEHAGRIQSIWSRLQERGLRSQCECLRGRKASLEELQSVHSERHVLLY
GTNPLSRLKLDNGKLTGLLAQRTFVMLPCGGVGVDTDTIWNELHSSNAARWAAGSVTDLA
FKVASRELKNGFAVVRPPGHHADHSTAMGFCFFNSVAIACRQLQQHGKASKILIVDWDVH
HGNGTQQTFYQDPSVLYISLHRHDDGNFFPGSGAVDEVGTGSGEGFNVNVAWAGGLDPPM
GDPEYLAAFRIVVMPIAREFAPDLVLVSAGFDAAEGHPAPLGGYHVSAKCFGYMTQQLMN
LAGGAVVLALEGGHDLTAICDASEACVAALL

Hist_deacetyl

Hist_deacetyl
PFAM accession number:PF00850
Interpro abstract (IPR023801):

Regulation of transcription is, in part, modulated by reversible histone acetylation on several lysine. Histone deacetylases (HDA) catalyse the removal of the acetyl group. Histone deacetylases, acetoin utilization proteins and acetylpolyamine amidohydrolases are all members of this ancient protein superfamily [(PUBMED:9278492)].

HDAs function in multi-subunit complexes, reversing the acetylation of histones by histone acetyltransferases [(PUBMED:10322454), (PUBMED:10072350)], and are also believed to deacetylate general transcription factors such as TFIIF and sequence-specific transcription factors such as p53 [(PUBMED:10322454)]. Thus, HDAs contribute to the regulation of transcription, in particular transcriptional repression [(PUBMED:10072350)]. At N-terminal tails of histones, removal of the acetyl group from the epsilon-amino group of a lysine side chain will restore its positivecharge, which may stabilise the histone-DNA interaction and prevent activating transcription factors binding to promoter elements [(PUBMED:9278492)]. HDAs play important roles in the cell cycle and differentiation, and their deregulation can contribute to the development of cancer [(PUBMED:10072350), (PUBMED:10322142)].

This entry represents the structural domain found in histone deacetylases. It consists of a 3-layer(alpha-beta-alpha) sandwich.

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