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61  structures 1555  species 0  interactions 7072  sequences 139  architectures

Family: MOZ_SAS (PF01853)

Summary: MOZ/SAS family

Pfam includes annotations and additional family information from a range of different sources. These sources can be accessed via the tabs below.

The Pfam group coordinates the annotation of Pfam families in Wikipedia, but we have not yet assigned a Wikipedia article to this family. If you think that a particular Wikipedia article provides good annotation, please let us know.

This tab holds the annotation information that is stored in the Pfam database. As we move to using Wikipedia as our main source of annotation, the contents of this tab will be gradually replaced by the Wikipedia tab.

MOZ/SAS family Provide feedback

This region of these proteins has been suggested to be homologous to acetyltransferases [1].

Literature references

  1. Kamine J, Elangovan B, Subramanian T, Coleman D, Chinnadurai G; , Virology 1996;216:357-366.: Identification of a cellular protein that specifically interacts with the essential cysteine region of the HIV-1 Tat transactivator. PUBMED:8607265 EPMC:8607265

  2. Reifsnyder C, Lowell J, Clarke A, Pillus L; , Nat Genet 1996;14:42-49.: Yeast SAS silencing genes and human genes associated with AML and HIV-1 Tat interactions are homologous with acetyltransferases [see comments] [published erratum appears in Nat Genet 1997 May;16(1):109] PUBMED:8782818 EPMC:8782818

Internal database links

External database links

This tab holds annotation information from the InterPro database.

InterPro entry 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 ].

Gene Ontology

The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.

Domain organisation

Below is a listing of the unique domain organisations or architectures in which this domain is found. More...

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We store a range of different sequence alignments for families. As well as the seed alignment from which the family is built, we provide the full alignment, generated by searching the sequence database (reference proteomes) using the family HMM. We also generate alignments using four representative proteomes (RP) sets and the UniProtKB sequence database. More...

View options

We make a range of alignments for each Pfam-A family. You can see a description of each above. You can view these alignments in various ways but please note that some types of alignment are never generated while others may not be available for all families, most commonly because the alignments are too large to handle.

Representative proteomes UniProt
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PP/heatmap 1            

1Cannot generate PP/Heatmap alignments for seeds; no PP data available

Key: ✓ available, x not generated, not available.

Format an alignment

Representative proteomes UniProt

Download options

We make all of our alignments available in Stockholm format. You can download them here as raw, plain text files or as gzip-compressed files.

Representative proteomes UniProt
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You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.

HMM logo

HMM logos is one way of visualising profile HMMs. Logos provide a quick overview of the properties of an HMM in a graphical form. You can see a more detailed description of HMM logos and find out how you can interpret them here. More...


This page displays the phylogenetic tree for this family's seed alignment. We use FastTree to calculate neighbour join trees with a local bootstrap based on 100 resamples (shown next to the tree nodes). FastTree calculates approximately-maximum-likelihood phylogenetic trees from our seed alignment.

Note: You can also download the data file for the tree.

Curation and family details

This section shows the detailed information about the Pfam family. You can see the definitions of many of the terms in this section in the glossary and a fuller explanation of the scoring system that we use in the scores section of the help pages.

Curation View help on the curation process

Seed source: Pfam-B_3994 (Release 4.3)
Previous IDs: none
Type: Family
Sequence Ontology: SO:0100021
Author: Bateman A
Number in seed: 132
Number in full: 7072
Average length of the domain: 171.9 aa
Average identity of full alignment: 54 %
Average coverage of the sequence by the domain: 23.27 %

HMM information View help on HMM parameters

HMM build commands:
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 61295632 -E 1000 --cpu 4 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 32.2 25.6
Trusted cut-off 32.2 25.9
Noise cut-off 32.0 25.5
Model length: 180
Family (HMM) version: 21
Download: download the raw HMM for this family

Species distribution

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Colour assignments

Archea Archea Eukaryota Eukaryota
Bacteria Bacteria Other sequences Other sequences
Viruses Viruses Unclassified Unclassified
Viroids Viroids Unclassified sequence Unclassified sequence


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This visualisation provides a simple graphical representation of the distribution of this family across species. You can find the original interactive tree in the adjacent tab. More...

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The tree shows the occurrence of this domain across different species. More...


Please note: for large trees this can take some time. While the tree is loading, you can safely switch away from this tab but if you browse away from the family page entirely, the tree will not be loaded.


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 MOZ_SAS domain has been found. There are 61 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 sequence.

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AlphaFold Structure Predictions

The list of proteins below match this family and have AlphaFold predicted structures. Click on the protein accession to view the predicted structure.

Protein Predicted structure External Information
A0A044QZ81 View 3D Structure Click here
A0A044RD00 View 3D Structure Click here
A0A044SBR8 View 3D Structure Click here
A0A044T462 View 3D Structure Click here
A0A044T773 View 3D Structure Click here
A0A044VE59 View 3D Structure Click here
A0A077Z056 View 3D Structure Click here
A0A077Z0Y5 View 3D Structure Click here
A0A077Z5Q9 View 3D Structure Click here
A0A077ZAN9 View 3D Structure Click here
A0A077ZBZ3 View 3D Structure Click here
A0A077ZMK4 View 3D Structure Click here
A0A0A2V2K8 View 3D Structure Click here
A0A0D2GQL9 View 3D Structure Click here
A0A0D2GWX9 View 3D Structure Click here
A0A0D2GYJ9 View 3D Structure Click here
A0A0K0DWT3 View 3D Structure Click here
A0A0K0DWT7 View 3D Structure Click here
A0A0K0ECN4 View 3D Structure Click here
A0A0K0EEF3 View 3D Structure Click here
A0A0N4U716 View 3D Structure Click here
A0A0N4U772 View 3D Structure Click here
A0A0N4UDY1 View 3D Structure Click here
A0A0N4UK08 View 3D Structure Click here
A0A0N4UM69 View 3D Structure Click here
A0A0R0K7Z3 View 3D Structure Click here
A0A131MAV3 View 3D Structure Click here
A0A158Q3Y3 View 3D Structure Click here
A0A175VWE6 View 3D Structure Click here
A0A175VZD8 View 3D Structure Click here
A0A183XBV4 View 3D Structure Click here
A0A183XTT8 View 3D Structure Click here
A0A1C1C984 View 3D Structure Click here
A0A1C1CC87 View 3D Structure Click here
A0A1C1CG00 View 3D Structure Click here
A0A1D8PS09 View 3D Structure Click here
A0A1I9G338 View 3D Structure Click here
A0A2R8Q7K0 View 3D Structure Click here
A0A2R8RHP9 View 3D Structure Click here
A0A3P7DPE7 View 3D Structure Click here