The domain within your query sequence starts at position 561 and ends at position 748; the E-value for the MOZ_SAS domain shown below is 5.9e-92.

WFHPPANEIYRKNNISVFEVDGNVSTIYCQNLCLLAKLFLDHKTLYYDVEPFLFYVLTQN
DVKGCHLVGYFSKEKHCQQKYNVSCIMILPQYQRKGYGRFLIDFSYLLSKREGQAGSPEK
PLSDLGRLSYMAYWKSVILECLYHQNDKQISIKKLSKLTGVCPQDITSTLHHLRMLDFRS
DQFVIIRR

MOZ_SAS

MOZ_SAS
PFAM accession number:PF01853
Interpro abstract (IPR002717):

Histone acetyltransferases (HATs) fall into at least four different families based on sequence conservation within the HAT domain [(PUBMED:18722564)]. The MYST family is the largest family of HATs and is named after the founding members: MOZ, Ybf2/ Sas3, Sas2 and Tip60. MYST proteins mediate many biological functions including gene regulation, DNA repair, cell-cycle regulation and development [(PUBMED:21132344)] and have been shown to acetylate several non-histone substrates [(PUBMED:19303850)]. MYST proteins are autoregulated by posttranslational modifications [(PUBMED:22020126)].

The MYST-type HAT domain contains three regions: a central region associated with acetyl-CoA cofactor binding and catalysis in addition to flanking N- and C-terminal regions harboring respectively a C2HC-type zinc finger and a helix- turn-helix DNA-binding motif. The N- and C-terminal segments directly flanking the catalytic core are likely to play an important role in histone substrate binding [(PUBMED:11106757), (PUBMED:17925393)]. The catalytic mechanism for the MYST-type HAT domain is still unresolved but seems to involve a conserved glutamate that functions to abstract a proton from lysine to promote the nucleophilic attack on the acetyl carbonyl carbon of acetyl-CoA [(PUBMED:11106757), (PUBMED:22918831), (PUBMED:22020126), (PUBMED:18245364)].

GO process:regulation of transcription, DNA-templated (GO:0006355), histone acetylation (GO:0016573)
GO function:histone acetyltransferase activity (GO:0004402)

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