SMART: Pfam domain PAS

PAS_8

PFAM accession number:	PF13188
Interpro abstract (IPR000014):	PAS domains are involved in many signalling proteins where they are used as a signal sensor domain [ (PUBMED:10357859) ]. PAS domains appear in archaea, bacteria and eukaryotes. Several PAS-domain proteins are known to detect their signal by way of an associated cofactor. Heme, 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 IPR001610 . 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) ].

PFAM accession number:

PF13188

Interpro abstract (IPR000014):

PAS domains are involved in many signalling proteins where they are used as a signal sensor domain [ (PUBMED:10357859) ]. PAS domains appear in archaea, bacteria and eukaryotes. Several PAS-domain proteins are known to detect their signal by way of an associated cofactor. Heme, 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 IPR001610 . 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) ].

This is a PFAM domain. For full annotation and more information, please see the PFAM entry PAS_8