Summary: D-aminoacylase, C-terminal region
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D-aminoacylase, C-terminal region Provide feedback
D-aminoacylase (Q9AGH8 EC:3.5.1.81) hydrolyses a wide variety of N-acyl derivatives of neutral D-amino acids, in a zinc-dependent manner. The enzyme is composed of a small beta-barrel domain and a larger catalytic alpha/beta-barrel. The C-terminal region featured in this family forms part of the beta-barrel domain, together with a short N-terminal segment. The beta-strands of both barrels were found to superimpose well. The small beta-barrel domain does not seem to contribute to the substrate-binding site or to be involved in the catalytic process [1].
Literature references
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Liaw SH, Chen SJ, Ko TP, Hsu CS, Chen CJ, Wang AH, Tsai YC; , J Biol Chem 2003;278:4957-4962.: Crystal structure of D-aminoacylase from Alcaligenes faecalis DA1. A novel subset of amidohydrolases and insights into the enzyme mechanism. PUBMED:12454005 EPMC:12454005
External database links
| PANDIT: | PF07908 |
| Pseudofam: | PF07908 |
| SCOP: | 1m7j |
| SYSTERS: | D-aminoacyl_C |
This tab holds annotation information from the InterPro database.
InterPro entry IPR012855
D-aminoacylase (SWISSPROT, EC) hydrolyses a wide variety of N-acyl derivatives of neutral D-amino acids, in a zinc-dependent manner. The enzyme is composed of a small beta-barrel domain and a larger catalytic alpha/beta-barrel that contains a short alpha/beta insert. The overall structure shares significant similarity to the alpha/beta-barrel amidohydrolase superfamily, in which the beta-strands in both barrels superimpose well [PUBMED:12454005].
The C-terminal region featured in this entry forms part of the beta-barrel domain, together with a short N-terminal segment. This domain does not seem to contribute to the substrate-binding site or to be involved in the catalytic process.Gene Ontology
The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.
| Molecular function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides (GO:0016811) |
| zinc ion binding (GO:0008270) |
Domain organisation
Below is a listing of the unique domain organisations or architectures in which this domain is found. More...
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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...
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.
| Seed (150) |
Full (859) |
Representative proteomes | NCBI (878) |
Meta (733) |
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| RP15 (114) |
RP35 (222) |
RP55 (284) |
RP75 (324) |
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| PP/heatmap | 1 | |||||||
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1Cannot generate PP/Heatmap alignments for seeds; no PP data available
Key:
available,
not generated,
— not available.
Format an alignment
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.
| Seed (150) |
Full (859) |
Representative proteomes | NCBI (878) |
Meta (733) |
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|---|---|---|---|---|---|---|---|---|
| RP15 (114) |
RP35 (222) |
RP55 (284) |
RP75 (324) |
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| Raw Stockholm | ||||||||
| Gzipped | ||||||||
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
| Seed source: | Pfam-B_13711 (release 14.0) |
| Previous IDs: | none |
| Type: | Family |
| Author: | Fenech M |
| Number in seed: | 150 |
| Number in full: | 859 |
| Average length of the domain: | 47.40 aa |
| Average identity of full alignment: | 33 % |
| Average coverage of the sequence by the domain: | 9.08 % |
HMM information
| HMM build commands: |
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
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| Model details: |
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| Model length: | 48 | ||||||||||||
| Family (HMM) version: | 7 | ||||||||||||
| Download: | download the raw HMM for this family |
Species distribution
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Interactions
There is 1 interaction for this family. More...
Amidohydro_3Structures
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 D-aminoacyl_C domain has been found. There are 12 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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Archea
Eukaryota
Bacteria
Other sequences
Viruses
Unclassified
Viroids
Unclassified sequence