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33  structures 3917  species 0  interactions 13825  sequences 107  architectures

Family: Acetyltransf_7 (PF13508)

Summary: Acetyltransferase (GNAT) domain

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

Acetyltransferase Edit Wikipedia article

Chemical structure of an acetyl group bound to the remainder R of a molecule.

Acetyltransferase (or transacetylase) is a type of transferase enzyme that transfers an acetyl group.

Examples include:

See also[edit]

External links[edit]

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

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 amino 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 2.3.1.48).
  • 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 2.3.1.4).
  • Escherichia coli rimI and rimJ, which acetylate the N-terminal alanine of ribosomal proteins S18 and S5, respectively (EC 2.3.1.128).
  • 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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Pfam Clan

This family is a member of clan Acetyltrans (CL0257), which has the following description:

This clan contains families related to N-acetyltransferases. N-acetyltransferases catalyse the transfer of acetyl groups from acetyl-CoA to arylamines.

The clan contains the following 31 members:

Acetyltransf_1 Acetyltransf_10 Acetyltransf_13 Acetyltransf_3 Acetyltransf_4 Acetyltransf_5 Acetyltransf_6 Acetyltransf_7 Acetyltransf_8 Acetyltransf_9 Acetyltransf_CG ATE_C ATE_N Autoind_synth DUF1248 DUF1999 DUF2156 DUF3749 DUF482 DUF619 FemAB FR47 Gly_acyl_tr_C GNAT_acetyltr_2 GNAT_acetyltran Leu_Phe_trans Mec-17 Mig-14 MOZ_SAS NMT NodA

Alignments

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 using the family HMM. We also generate alignments using four representative proteomes (RP) sets, the NCBI sequence database, and our metagenomics 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.

  Seed
(163)
Full
(13825)
Representative proteomes NCBI
(41376)
Meta
(6818)
RP15
(930)
RP35
(1796)
RP55
(2449)
RP75
(2973)
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1Cannot generate PP/Heatmap alignments for seeds; no PP data available

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

Format an alignment

  Seed
(163)
Full
(13825)
Representative proteomes NCBI
(41376)
Meta
(6818)
RP15
(930)
RP35
(1796)
RP55
(2449)
RP75
(2973)
Alignment:
Format:
Order:
Sequence:
Gaps:
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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.

  Seed
(163)
Full
(13825)
Representative proteomes NCBI
(41376)
Meta
(6818)
RP15
(930)
RP35
(1796)
RP55
(2449)
RP75
(2973)
Raw Stockholm Download   Download   Download   Download   Download   Download   Download   Download  
Gzipped Download   Download   Download   Download   Download   Download   Download   Download  

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

External links

MyHits provides a collection of tools to handle multiple sequence alignments. For example, one can refine a seed alignment (sequence addition or removal, re-alignment or manual edition) and then search databases for remote homologs using HMMER3.

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...

Trees

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:B5FCA0
Previous IDs: none
Type: Domain
Author: Bateman A
Number in seed: 163
Number in full: 13825
Average length of the domain: 86.50 aa
Average identity of full alignment: 18 %
Average coverage of the sequence by the domain: 43.91 %

HMM information View help on HMM parameters

HMM build commands:
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 27.0 27.0
Trusted cut-off 27.0 27.0
Noise cut-off 26.9 26.9
Model length: 79
Family (HMM) version: 1
Download: download the raw HMM for this family

Species distribution

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Structures

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_7 domain has been found. There are 33 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 seqence.

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