Summary: PAS fold
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 "PAS domain". More...
PAS domain Edit Wikipedia article
| PAS fold | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Crystallographic structure of the PAS domain of the bacterial oxygen sensor protein fixL.[1] The protein is depicted as a rainbow colored cartoon (N-terminus = blue, C-terminus = red while the heme ligand is shown as sticks (carbon = white, nitrogen = blue, oxygen = red, iron = orange). | |||||||||
| Identifiers | |||||||||
| Symbol | PAS | ||||||||
| Pfam | PF00989 | ||||||||
| InterPro | IPR013767 | ||||||||
| SMART | PAS | ||||||||
| PROSITE | PDOC50112 | ||||||||
| SCOP | 2phy | ||||||||
| SUPERFAMILY | 2phy | ||||||||
|
|||||||||
The PAS domain is a protein domain contained in many signaling proteins where it functions as a signal sensor.[2][3] PAS domains are found in a large number of organisms from bacteria to humans. The PAS domain was named after the three proteins in which it occurs:
- Per â period circadian protein
- Arnt â aryl hydrocarbon receptor nuclear translocator protein
- Sim â single-minded protein
Many PAS-domain proteins detect their signal by way of an associated cofactor such as heme.[4] Proteins that contain a PAS domain include Hypoxia-inducible factors.
[edit] References
- ^ PDB 1y28; Dunham CM, Dioum EM, Tuckerman JR, Gonzalez G, Scott WG, Gilles-Gonzalez MA (July 2003). "A distal arginine in oxygen-sensing heme-PAS domains is essential to ligand binding, signal transduction, and structure". Biochemistry 42 (25): 7701â8. doi:10.1021/bi0343370. PMID 12820879.
- ^ Ponting CP, Aravind L (November 1997). "PAS: a multi-functional domain family comes to light". Curr. Biol. 7 (11): R674â7. doi:10.1016/S0960-9822(06)00352-6. PMID 9382818.
- ^ Hefti MH, Françoijs KJ, de Vries SC, Dixon R, Vervoort J (March 2004). "The PAS fold. A redefinition of the PAS domain based upon structural prediction". Eur. J. Biochem. 271 (6): 1198â208. doi:10.1111/j.1432-1033.2004.04023.x. PMID 15009198.
- ^ Gilles-Gonzalez MA, Gonzalez G (February 2004). "Signal transduction by heme-containing PAS-domain proteins". J. Appl. Physiol. 96 (2): 774â83. doi:10.1152/japplphysiol.00941.2003. PMID 14715687.
|
|
|||||
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.
PAS fold Provide feedback
The PAS fold corresponds to the structural domain that has previously been defined as PAS and PAC motifs [4]. The PAS fold appears in archaea, eubacteria and eukarya.
Literature references
-
Zhulin IB, Taylor BL, Dixon R; , Trends Biochem Sci 1997;22:331-333.: PAS domain S-boxes in archaea, bacteria and sensors for oxygen and redox. PUBMED:9301332 EPMC:9301332
-
Borgstahl GE, Williams DR, Getzoff ED; , Biochemistry 1995;34:6278-6287.: 1.4 A structure of photoactive yellow protein, a cytosolic photoreceptor: unusual fold, active site, and chromophore. PUBMED:7756254 EPMC:7756254
-
Ponting CP, Aravind L; , Curr Biol 1997;7:674-677.: PAS: a multifunctional domain family comes to light. PUBMED:9382818 EPMC:9382818
-
Hefti MH, Francoijs KJ, de Vries SC, Dixon R, Vervoort J; , Eur J Biochem 2004;271:1198-1208.: The PAS fold: a redefination of the PAS domain based upon structural prediction. PUBMED:15009198 EPMC:15009198
External database links
| HOMSTRAD: | PAS |
| PANDIT: | PF12860 |
| Pseudofam: | PF12860 |
| SCOP: | 2phy |
| SMART: | PAS |
| SYSTERS: | PAS_7 |
This tab holds annotation information from the InterPro database.
No InterPro data for this Pfam family.
Domain organisation
Below is a listing of the unique domain organisations or architectures in which this domain is found. More...
Loading domain graphics...
Pfam Clan
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 (164) |
Full (2444) |
Representative proteomes | NCBI (2460) |
Meta (395) |
||||
|---|---|---|---|---|---|---|---|---|
| RP15 (225) |
RP35 (493) |
RP55 (644) |
RP75 (913) |
|||||
| 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 (164) |
Full (2444) |
Representative proteomes | NCBI (2460) |
Meta (395) |
||||
|---|---|---|---|---|---|---|---|---|
| RP15 (225) |
RP35 (493) |
RP55 (644) |
RP75 (913) |
|||||
| 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_21375 (release 24.0) |
| Previous IDs: | none |
| Type: | Domain |
| Author: | Mistry J |
| Number in seed: | 164 |
| Number in full: | 2444 |
| Average length of the domain: | 113.00 aa |
| Average identity of full alignment: | 23 % |
| Average coverage of the sequence by the domain: | 15.73 % |
HMM information
| HMM build commands: |
build method: hmmbuild --amino -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
|
||||||||||||
| Model details: |
|
||||||||||||
| Model length: | 115 | ||||||||||||
| Family (HMM) version: | 2 | ||||||||||||
| 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.

Archea
Eukaryota
Bacteria
Other sequences
Viruses
Unclassified
Viroids
Unclassified sequence