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InterPro: IPR001610 PAC motif

Protein matches Help

UniProtKB

Matches:

16296 proteins

Overview:	sorted by AC,	sorted by name,	of known structure,	proteins with splice variants
Detailed:	sorted by AC,	sorted by name,	of known structure	proteins with splice variants
Table:	For all matching proteins,	of known structure
Architectures
Accession List
Matches in BioMart

Accession

IPR001610 PAC

Type

Repeat

Signatures Help

Database	ID	Name	Proteins
SMART	SM00086	PAC	16296
Signatures in BioMart

InterPro Relationships Help

Found in

IPR000700 PAS-associated, C-terminal
IPR001321 Hypoxia-inducible factor-1 alpha, PAS fold
IPR003949 Potassium channel, voltage-dependent, EAG
IPR003950 Potassium channel, voltage-dependent, ELK
IPR013655 PAS fold-3
IPR013767 PAS fold
IPR014285 Nitrogen fixation negative regulator NifL
IPR014409 Signal transduction histidine kinase, hybrid-type, aerobic respiration control ArcB
IPR015524 Period circadian protein 3
IPR017181 Signal transduction histidine kinase, CHASE2/PAS sensor domain-containing, predicted

GO Term annotation Help

Process

GO:0006355 regulation of transcription, DNA-dependent
GO:0007165 signal transduction

InterPro annotation

Entry Details in BioMart

Abstract

PAC motifs occur C-terminal to a subset of all known PAS motifs (see IPR000014). It is proposed to contribute to the PAS domain fold [1, 2, 3].

Structural links Help

PDB - click here

SCOP: d.110.3.2 , d.110.3.6 , d.110.3.7 , d.6.1.1

CATH: 1.10.790.10 , 3.30.450.20

Database links Help

Blocks: IPB001610

Interactions Help

This domain has been experimentally proven to be involved in Protein:Protein interactions.
Representative data is shown with the following example proteins:

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR001610

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

O48963 Phototropin-1

O54943 Period circadian protein homolog 2

P07663 Period circadian protein

P27540 Aryl hydrocarbon receptor nuclear translocator

P48158 60S ribosomal protein L23

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR017441	Protein kinase, ATP binding site
IPR000218	Ribosomal protein L14b/L23e
IPR017442	Serine/threonine-protein kinase-like domain
IPR001610	PAC motif
IPR000014	PAS
IPR001092	Helix-loop-helix DNA-binding domain
IPR019972	Ribosomal protein L14 conserved site
IPR011598	Helix-loop-helix DNA-binding
IPR013767	PAS fold
IPR011009	Protein kinase-like domain
IPR000700	PAS-associated, C-terminal
IPR008271	Serine/threonine-protein kinase, active site
IPR013655	PAS fold-3
IPR000719	Protein kinase, catalytic domain
IPR002290	Serine/threonine-protein kinase domain
IPR001067	Nuclear translocator
	PDB Chain
	ModBase
	CATH Domain
	SWISS-MODEL

Publications Open in usermanual
1.	Zhulin IB, Taylor BL, Dixon R. PAS domain S-boxes in Archaea, Bacteria and sensors for oxygen and redox. Trends Biochem. Sci. 22 331-3 1997 [PubMed: 9301332] http://dx.doi.org/10.1016/S0968-0004(97)01110-9
2.	Borgstahl GE, Williams DR, Getzoff ED. 1.4 A structure of photoactive yellow protein, a cytosolic photoreceptor: unusual fold, active site, and chromophore. Biochemistry 34 6278-87 1995 [PubMed: 7756254] http://dx.doi.org/10.1021/bi00019a004
3.	Ponting CP, Aravind L. PAS: a multifunctional domain family comes to light. Curr. Biol. 7 R674-7 1997 [PubMed: 9382818] http://dx.doi.org/10.1016/S0960-9822(06)00352-6

Additional Reading Open in usermanual
	Gilles-Gonzalez MA, Caceres AI, Sousa EH, Tomchick DR, Brautigam C, Gonzalez C, Machius M. A proximal arginine R206 participates in switching of the Bradyrhizobium japonicum FixL oxygen sensor. J. Mol. Biol. 360 2006 80-9 [PubMed: 16813836] http://dx.doi.org/10.1016/j.jmb.2006.04.054
	Key J, Moffat K. Crystal structures of deoxy and CO-bound bjFixLH reveal details of ligand recognition and signaling. Biochemistry 44 2005 4627-35 [PubMed: 15779889] http://dx.doi.org/10.1021/bi047942r
	Elferink CJ, Ge NL, Levine A. Maximal aryl hydrocarbon receptor activity depends on an interaction with the retinoblastoma protein. Mol. Pharmacol. 59 2001 664-73 [PubMed: 11259609] http://molpharm.aspetjournals.org/cgi/content/abstract/59/4/664
	Yildiz O, Doi M, Yujnovsky I, Cardone L, Berndt A, Hennig S, Schulze S, Urbanke C, Sassone-Corsi P, Wolf E. Crystal structure and interactions of the PAS repeat region of the Drosophila clock protein PERIOD. Mol. Cell 17 2005 69-82 [PubMed: 15629718] http://dx.doi.org/10.1016/j.molcel.2004.11.022
	Card PB, Erbel PJ, Gardner KH. Structural basis of ARNT PAS-B dimerization: use of a common beta-sheet interface for hetero- and homodimerization. J. Mol. Biol. 353 2005 664-77 [PubMed: 16181639] http://dx.doi.org/10.1016/j.jmb.2005.08.043
	Key J, Srajer V, Pahl R, Moffat K. Time-resolved crystallographic studies of the heme domain of the oxygen sensor FixL: structural dynamics of ligand rebinding and their relation to signal transduction. Biochemistry 46 2007 4706-15 [PubMed: 17385895] http://dx.doi.org/10.1021/bi700043c

InterPro 23.1