Summary: Catalase-related immune-responsive
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 "Catalase-related immune-responsive domain". More...
Catalase-related immune-responsive domain Edit Wikipedia article
| helicobacter pylori catalase compound i | |||||||||
| Identifiers | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Symbol | Catalase-rel | ||||||||
| Pfam | PF06628 | ||||||||
| InterPro | IPR010582 | ||||||||
| SCOP | 1ggh | ||||||||
| SUPERFAMILY | 1ggh | ||||||||
|
|||||||||
In molecular biology, the catalase-related immune-responsive domain is a protein domain found in catalases. This domain carries the immune-responsive amphipathic octa-peptide that is recognised by T cells.[1]
[edit] References
- ^ Guy B, Krell T, Sanchez V, Kennel A, Manin C, Sodoyer R (January 2005). "Do Th1 or Th2 sequence motifs exist in proteins? Identification of amphipatic immunomodulatory domains in Helicobacter pylori catalase". Immunol. Lett. 96 (2): 26175. doi:10.1016/j.imlet.2004.09.011. PMID 15585332.
This article incorporates text from the public domain Pfam and InterPro IPR010582
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.
Catalase-related immune-responsive Provide feedback
This family represents a small conserved region within catalase enzymes ( EC:1.11.1.6). All members also contain the Catalase family, PF00199 domain. Catalase decomposes hydrogen peroxide into water and oxygen, serving to protect cells from its toxic effects [1]. This domain carries the immune-responsive amphipathic octa-peptide that is recognised by T cells [2].
Literature references
-
Bai J, Cederbaum AI; , Biol Signals Recept 2001;10:189-199.: Mitochondrial catalase and oxidative injury. PUBMED:11351128 EPMC:11351128
-
Guy B, Krell T, Sanchez V, Kennel A, Manin C, Sodoyer R; , Immunol Lett. 2005;96:261-275.: Do Th1 or Th2 sequence motifs exist in proteins? Identification of amphipatic immunomodulatory domains in Helicobacter pylori catalase. PUBMED:15585332 EPMC:15585332
External database links
| PANDIT: | PF06628 |
| Pseudofam: | PF06628 |
| SCOP: | 1ggh |
| SYSTERS: | Catalase-rel |
This tab holds annotation information from the InterPro database.
InterPro entry IPR010582
Catalases (EC) are antioxidant enzymes that catalyse the conversion of hydrogen peroxide to water and molecular oxygen, serving to protect cells from its toxic effects [PUBMED:11351128]. Hydrogen peroxide is produced as a consequence of oxidative cellular metabolism and can be converted to the highly reactive hydroxyl radical via transition metals, this radical being able to damage a wide variety of molecules within a cell, leading to oxidative stress and cell death. Catalases act to neutralise hydrogen peroxide toxicity, and are produced by all aerobic organisms ranging from bacteria to man. Most catalases are mono-functional, haem-containing enzymes, although there are also bifunctional haem-containing peroxidase/catalases (INTERPRO) that are closely related to plant peroxidases, and non-haem, manganese-containing catalases (INTERPRO) that are found in bacteria [PUBMED:14745498].
This entry represents a small conserved region within catalase enzymes that carries the immune-responsive amphipathic octa-peptide that is recognised by T cells [PUBMED:15585332].
Domain organisation
Below is a listing of the unique domain organisations or architectures in which this domain is found. More...
Loading domain graphics...
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 (343) |
Full (4316) |
Representative proteomes | NCBI (3539) |
Meta (63) |
||||
|---|---|---|---|---|---|---|---|---|
| RP15 (326) |
RP35 (674) |
RP55 (986) |
RP75 (1207) |
|||||
| Jalview | ||||||||
| HTML | ||||||||
| PP/heatmap | 1 | |||||||
| Pfam viewer | ||||||||
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 (343) |
Full (4316) |
Representative proteomes | NCBI (3539) |
Meta (63) |
||||
|---|---|---|---|---|---|---|---|---|
| RP15 (326) |
RP35 (674) |
RP55 (986) |
RP75 (1207) |
|||||
| 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_16304 (release 10.0) |
| Previous IDs: | none |
| Type: | Family |
| Author: | Vella Briffa B, Coggill P |
| Number in seed: | 343 |
| Number in full: | 4316 |
| Average length of the domain: | 67.50 aa |
| Average identity of full alignment: | 25 % |
| Average coverage of the sequence by the domain: | 12.26 % |
HMM information
| HMM build commands: |
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
|
||||||||||||
| Model details: |
|
||||||||||||
| Model length: | 68 | ||||||||||||
| Family (HMM) version: | 7 | ||||||||||||
| Download: | download the raw HMM for this family |
Species distribution
Sunburst controls
ShowThis 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...
Tree controls
HideThe tree shows the occurrence of this domain across different species. More...
Loading...
Please note: for large trees this can take some time. While the tree is loading, you can safely switch away from this tab but if you browse away from the family page entirely, the tree will not be loaded.
Interactions
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 Catalase-rel domain has been found. There are 287 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.
Loading structure mapping...

Archea
Eukaryota
Bacteria
Other sequences
Viruses
Unclassified
Viroids
Unclassified sequence