117  structures 1251  species 1  interaction 13139  sequences 1645  architectures

Family: PAS (PF00989)

Summary

PAS fold Add an annotation

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

  1. 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

  2. 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

  3. Ponting CP, Aravind L; , Curr Biol 1997;7:674-677.: PAS: a multifunctional domain family comes to light. PUBMED:9382818

  4. 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


InterPro entry IPR013767

PAS domains are involved in many signalling proteins where they are used as a signal sensor domain. PAS domains appear in archaea, bacteria and eukaryotes. Several PAS-domain proteins are known to detect their signal by way of an associated cofactor. Haeme, flavin, and a 4-hydroxycinnamyl chromophore are used in different proteins. The PAS domain was named after three proteins that it occurs in:

  • Per- period circadian protein
  • Arnt- Ah receptor nuclear translocator protein
  • Sim- single-minded protein.
  • PAS domains are often associated with PAC domains . It appears that these domains are directly linked, and that together they form the conserved 3D PAS fold. The division between the PAS and PAC domains is caused by major differences in sequences in the region connecting these two motifs PUBMED:15009198. In human PAS kinase, this region has been shown to be very flexible, and adopts different conformations depending on the bound ligand PUBMED:12377121. Probably the most surprising identification of a PAS domain was that in EAG-like K+-channels PUBMED:9301332.

    Clan

    This family is a member of clan PAS (CL0183), which contains the following 7 members:

    MEKHLA PAS PAS_2 PAS_3 PAS_4 PAS_5 PAS_6

    Gene Ontology

    External database links

    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

    There are various ways to view or download the sequence alignments that we store. You can use a sequence viewer to look at either the seed or full alignment for the family, or you can look at a plain text version of the sequence in a variety of different formats. More...

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    Very large alignments can often cause problems for the formatting tool above. If you find that downloading or viewing a large alignment is problematic, you can also download a gzip-compressed, Stockholm-format file containing the seed or full alignment for this family.

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

    The main seed and full alignments are generated using sequences from the UniProt sequence database. However, we also generate alignments using sequences from the NCBI sequence database and the "metaseq" metagenomics dataset.

    You can view alignments from these two additional datasets using the form above, or you can download alignments of NCBI or metagenomics sequences, as gzip-compressed files.

    Pfam alignments:
    Full length sequences

    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 HMMER2.

    Pfam alignments:

    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. 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 or full alignments.

    Note: You can also download the data files for the seed, full, NCBI or metagenomics trees.

    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: Sequences from SMART alignment
    Previous IDs: none
    Type: Domain
    Author: Bateman A
    Number in seed: 49
    Number in full: 13139
    Average length of the domain: 106.30 aa
    Average identity of full alignment: 15 %
    Average coverage of the sequence by the domain: 14.26 %

    HMM information View help on HMM parameters

    HMM build commands:
    build method: hmmbuild -o /dev/null HMM SEED
    search method: hmmsearch -Z 9421015 -E 1000 HMM pfamseq
    Model details:
    Parameter Sequence Domain
    Gathering cut-off 22.6 22.6
    Trusted cut-off 22.6 22.6
    Noise cut-off 22.5 22.5
    Model length: 113
    Family (HMM) version: 17
    Download: download the raw HMM for this family

    Species distribution

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    The tree shows the occurrence of this domain across different species. More...

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    Interactions

    There is 1 interaction for this family. More...

    PAS

    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 PAS domain has been found.

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