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51  structures 7247  species 0  interactions 26587  sequences 336  architectures

Family: Acetyltransf_10 (PF13673)

Summary: Acetyltransferase (GNAT) domain

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This is the Wikipedia entry entitled "Acetyltransferase". More...

Acetyltransferase Edit Wikipedia article

Acetyltransferase is a type of transferase enzyme which transfers an acetyl group.

Examples include:

External links

This page is based on a Wikipedia article. The text is available under the Creative Commons Attribution/Share-Alike License.

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.

Acetyltransferase (GNAT) domain Provide feedback

This family contains proteins with N-acetyltransferase functions such as Elp3-related proteins.

Literature references

  1. Neuwald AF, Landsman D; , Trends Biochem Sci 1997;22:154-155.: GCN5-related histone N-acetyltransferases belong to a diverse superfamily that includes the yeast SPT10 protein. PUBMED:9175471 EPMC:9175471

  2. Chinenov Y; , Trends Biochem Sci 2002;27:115-117.: A second catalytic domain in the Elp3 histone acetyltransferases: a candidate for histone demethylase activity?. PUBMED:11893502 EPMC:11893502

Internal database links

External database links

This tab holds annotation information from the InterPro database.

InterPro entry IPR000182

The N-acetyltransferases (NAT) (EC 2.3.1.-) are enzymes that use acetyl coenzyme A (CoA) to transfer an acetyl group to a substrate, a reaction implicated in various functions from bacterial antibiotic resistance to mammalian circadian rhythm and chromatin remodeling. The Gcn5-related N-acetyltransferases (GNAT) catalyze the transfer of the acetyl from the CoA donor to a primary amine of the acceptor. The GNAT proteins share a domain composed of four conserved sequence motifs A-D [ PUBMED:9175471 , PUBMED:10940244 ]. This GNAT domain is named after yeast GCN5 (from General Control Nonrepressed) and related histone acetyltransferases (HATs) like Hat1 and PCAF. HATs acetylate lysine residues of N-terminal histone tails, resulting in transcription activation. Another category of GNAT, the aminoglycoside N-acetyltransferases, confer antibiotic resistance by catalyzing the acetylation of amino groups in aminoglycoside antibiotics [ PUBMED:12592013 ]. GNAT proteins can also have anabolic and catabolic functions in both prokaryotes and eukaryotes [ PUBMED:9175471 , PUBMED:10940244 , PUBMED:12592013 , PUBMED:12527305 , PUBMED:15581578 ].

The acetyltransferase/GNAT domain forms a structurally conserved fold of 6 to 7 beta strands (B) and 4 helices (H) in the topology B1-H1-H2-B2-B3-B4-H3-B5-H4-B6, followed by a C-terminal strand which may be from the same monomer or contributed by another [ PUBMED:10940244 , PUBMED:15581578 ]. Motifs D (B2-B3), A (B4-H3) and B (B5-H4) are collectively called the HAT core [ PUBMED:10940244 , PUBMED:12527305 , PUBMED:15581578 ], while the N-terminal motif C (B1-H1) is less conserved.

Some proteins known to contain a GNAT domain:

  • Yeast GCN5 and Hat1, which are histone acetyltransferases (EC
  • Human PCAF, a histone acetyltransferase.
  • Mammalian serotonin N-acetyltransferase (SNAT) or arylalkylamine NAT (AANAT), which acetylates serotonin into a circadian neurohormone that may participate in light-dark rhythms, and human mood and behavior.
  • Mammalian glucosamine 6-phosphate N-acetyltransferase (GNA1) (EC
  • Escherichia coli rimI and rimJ, which acetylate the N-terminal alanine of ribosomal proteins S18 and S5, respectively (EC
  • Mycobacterium tuberculosis aminoglycoside 2'-N-acetyltransferase (aac), which acetylates the 2' hydroxyl or amino group of a broad spectrum of aminoglycoside antibiotics.
  • Bacillus subtilis bltD and paiA, which acetylate spermine and spermidine.

This entry represents the entire GNAT domain.

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...

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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.

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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.

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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.

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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: Jackhmmer:A9C0U2
Previous IDs: none
Type: Domain
Sequence Ontology: SO:0000417
Author: Coggill P
Number in seed: 50
Number in full: 26587
Average length of the domain: 118.8 aa
Average identity of full alignment: 15 %
Average coverage of the sequence by the domain: 60.99 %

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 23.6 23.6
Trusted cut-off 23.6 23.6
Noise cut-off 23.5 23.5
Model length: 128
Family (HMM) version: 10
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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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 Acetyltransf_10 domain has been found. There are 51 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
A0A044V976 View 3D Structure Click here
A0A077ZJM7 View 3D Structure Click here
A0A0D2FGL2 View 3D Structure Click here
A0A0D2H8S0 View 3D Structure Click here
A0A0H3GGR8 View 3D Structure Click here
A0A0H3GNQ9 View 3D Structure Click here
A0A0H3GPD4 View 3D Structure Click here
A0A0H3H0E6 View 3D Structure Click here
A0A0H3H101 View 3D Structure Click here
A0A0H3H4D0 View 3D Structure Click here
A0A0K0DZC4 View 3D Structure Click here
A0A0K0J474 View 3D Structure Click here
A0A0N4UBC6 View 3D Structure Click here
A0A0N4UK80 View 3D Structure Click here
A0A175VTN5 View 3D Structure Click here
A0A175VZ15 View 3D Structure Click here
A0A175W1M8 View 3D Structure Click here
A0A175W9Y8 View 3D Structure Click here
A0A175WHX0 View 3D Structure Click here
A0A1C1C8V7 View 3D Structure Click here
A0A1C1CA21 View 3D Structure Click here
A0A1C1CPG4 View 3D Structure Click here
A0A1C1CQQ0 View 3D Structure Click here
A0A1C1D137 View 3D Structure Click here
A0A1D8PFY0 View 3D Structure Click here
A0A5S6PD82 View 3D Structure Click here
C0NF01 View 3D Structure Click here
C0NJ58 View 3D Structure Click here
C0NT72 View 3D Structure Click here
C1GWM1 View 3D Structure Click here
C1GYS9 View 3D Structure Click here
C1H3J9 View 3D Structure Click here
C1HA78 View 3D Structure Click here
D6XCX1 View 3D Structure Click here
D7GG24 View 3D Structure Click here
K0ETA7 View 3D Structure Click here
K0EUU3 View 3D Structure Click here
K0EW69 View 3D Structure Click here
K0F001 View 3D Structure Click here
O14195 View 3D Structure Click here