Summary: Acetyltransferase (GNAT) domain
This is the Wikipedia entry entitled "Acetyltransferase". More...
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Acetyltransferase Edit Wikipedia article
- Histone acetyltransferases including CBP histone acetyltransferase
- Choline acetyltransferase
- Chloramphenicol acetyltransferase
- Serotonin N-acetyltransferase
- NatA Acetyltransferase
- NatB acetyltransferase
|This enzyme-related article is a stub. You can help Wikipedia by expanding it.|
Acetyltransferase (GNAT) domain Provide feedback
This domain catalyses N-acetyltransferase reactions.
Internal database links
|SCOOP:||Acetyltransf_10 GNAT_acetyltr_2 Acetyltransf_13 Acetyltransf_CG Acetyltransf_15|
|Similarity to PfamA using HHSearch:||Acetyltransf_1 NMT NodA FR47 GNAT_acetyltran Acetyltransf_3 Acetyltransf_4 Acetyltransf_7 Acetyltransf_10 Acetyltransf_CG Acetyltransf_15|
This tab holds annotation information from the InterPro database.
No InterPro data for this Pfam family.
- the number of sequences which exhibit this architecture
a textual description of the architecture, e.g. Gla, EGF x 2, Trypsin.
This example describes an architecture with one
Gladomain, followed by two consecutive
EGFdomains, and finally a single
- the UniProt description of the protein sequence
- the number of residues in the sequence
- the Pfam graphic itself.
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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 35 members:Acetyltransf_1 Acetyltransf_10 Acetyltransf_13 Acetyltransf_15 Acetyltransf_16 Acetyltransf_3 Acetyltransf_4 Acetyltransf_5 Acetyltransf_6 Acetyltransf_7 Acetyltransf_8 Acetyltransf_9 Acetyltransf_CG AstA ATE_C ATE_N Autoind_synth DUF1122 DUF1248 DUF1999 DUF2156 DUF3749 FemAB FemAB_like FR47 Gly_acyl_tr_C GNAT_acetyltr_2 GNAT_acetyltran Leu_Phe_trans Mig-14 MOZ_SAS NAT NMT NodA ODC_AZ
We make a range of alignments for each Pfam-A family:
- the curated alignment from which the HMM for the family is built
- the alignment generated by searching the sequence database using the HMM
- Representative Proteomes (RPs) at 15%, 35%, 55% and 75% co-membership thresholds
- alignment generated by searching the UniProtKB sequence database using the family HMM
- alignment generated by searching the NCBI sequence database using the family HMM
- alignment generated by searching the metagenomics sequence database using the family HMM
You can see the alignments as HTML or in three different sequence viewers:
1Cannot generate PP/Heatmap alignments for seeds; no PP data available
Key: available, not generated, — not available.
Format an alignment
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Note: You can also download the data file for the tree.
Curation and family details
|Number in seed:||75|
|Number in full:||1196|
|Average length of the domain:||125.40 aa|
|Average identity of full alignment:||18 %|
|Average coverage of the sequence by the domain:||40.09 %|
|HMM build commands:||
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 11927849 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||4|
|Download:||download the raw HMM for this family|
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selected sequences to HMM
a FASTA-format file
- 0 sequences
- 0 species
How the sunburst is generated
Colouring and labels
Anomalies in the taxonomy tree
Missing taxonomic levels
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The tree shows the occurrence of this domain across different species. More...
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There are 3 interactions for this family. More...
We determine these interactions using iPfam, which considers the interactions between residues in three-dimensional protein structures and maps those interactions back to Pfam families. You can find more information about the iPfam algorithm in the journal article that accompanies the website.
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_9 domain has been found. There are 62 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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