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221  structures 7878  species 0  interactions 51560  sequences 443  architectures

Family: Acetyltransf_3 (PF13302)

Summary: Acetyltransferase (GNAT) domain

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

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 domain catalyses N-acetyltransferase reactions.

Internal 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.

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.

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Representative proteomes UniProt

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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.

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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: Jackhmmer:Q7P3G3
Previous IDs: none
Type: Domain
Sequence Ontology: SO:0000417
Author: Bateman A
Number in seed: 170
Number in full: 51560
Average length of the domain: 140.7 aa
Average identity of full alignment: 19 %
Average coverage of the sequence by the domain: 66.06 %

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 25.4 25.4
Trusted cut-off 25.4 25.4
Noise cut-off 25.3 25.3
Model length: 138
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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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...


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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_3 domain has been found. There are 221 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
A0A044UZA8 View 3D Structure Click here
A0A060D314 View 3D Structure Click here
A0A060D7E5 View 3D Structure Click here
A0A060D878 View 3D Structure Click here
A0A0D2E0R3 View 3D Structure Click here
A0A0D2GPZ0 View 3D Structure Click here
A0A0D2GQN5 View 3D Structure Click here
A0A0D2GWG7 View 3D Structure Click here
A0A0D2GWI6 View 3D Structure Click here
A0A0D2H9F8 View 3D Structure Click here
A0A0D2HEH6 View 3D Structure Click here
A0A0H3GMS2 View 3D Structure Click here
A0A0H3GPB1 View 3D Structure Click here
A0A0H3GPH6 View 3D Structure Click here
A0A0H3GPM1 View 3D Structure Click here
A0A0H3GSV6 View 3D Structure Click here
A0A0H3GTP7 View 3D Structure Click here
A0A0H3GWC9 View 3D Structure Click here
A0A0H3GX22 View 3D Structure Click here
A0A0H3GYR1 View 3D Structure Click here
A0A0K0DX11 View 3D Structure Click here
A0A0N4UF53 View 3D Structure Click here
A0A0N7KI73 View 3D Structure Click here
A0A0P0W438 View 3D Structure Click here
A0A0P0W473 View 3D Structure Click here
A0A0R0ECR9 View 3D Structure Click here
A0A175VPR6 View 3D Structure Click here
A0A175VYC4 View 3D Structure Click here
A0A175VYQ8 View 3D Structure Click here
A0A175W5V5 View 3D Structure Click here
A0A175W9U9 View 3D Structure Click here
A0A175WHD6 View 3D Structure Click here
A0A1C1CBR2 View 3D Structure Click here
A0A1C1CKJ0 View 3D Structure Click here
A0A1C1CS92 View 3D Structure Click here
A0A1C1CUV5 View 3D Structure Click here
A0A1C1D0U1 View 3D Structure Click here
A0A1D6ED41 View 3D Structure Click here
A0A1D6GFQ2 View 3D Structure Click here
A0A1D6GKR6 View 3D Structure Click here