SMART: REC domain annotation

REC cheY-homologous receiver domain

SMART accession number:	SM00448
Description:	CheY regulates the clockwise rotation of E. coli flagellar motors. This domain contains a phosphoacceptor site that is phosphorylated by histidine kinase homologues.
Interpro abstract (IPR001789):	Two-component signal transduction systems enable bacteria to sense, respond, and adapt to a wide range of environments, stressors, and growth conditions [(PUBMED:16176121)]. Some bacteria can contain up to as many as 200 two-component systems that need tight regulation to prevent unwanted cross-talk [(PUBMED:18076326)]. These pathways have been adapted to response to a wide variety of stimuli, including nutrients, cellular redox state, changes in osmolarity, quorum signals, antibiotics, and more [(PUBMED:12372152)]. Two-component systems are comprised of a sensor histidine kinase (HK) and its cognate response regulator (RR) [(PUBMED:10966457)]. The HK catalyses its own auto-phosphorylation followed by the transfer of the phosphoryl group to the receiver domain on RR; phosphorylation of the RR usually activates an attached output domain, which can then effect changes in cellular physiology, often by regulating gene expression. Some HK are bifunctional, catalysing both the phosphorylation and dephosphorylation of their cognate RR. The input stimuli can regulate either the kinase or phosphatase activity of the bifunctional HK. A variant of the two-component system is the phospho-relay system. Here a hybrid HK auto-phosphorylates and then transfers the phosphoryl group to an internal receiver domain, rather than to a separate RR protein. The phosphoryl group is then shuttled to histidine phosphotransferase (HPT) and subsequently to a terminal RR, which can evoke the desired response [(PUBMED:11934609), (PUBMED:11489844)]. Bipartite response regulator proteins are involved in a two-component signal transduction system in bacteria, and certain eukaryotes like protozoa, that functions to detect and respond to environmental changes [(PUBMED:7699720)]. These systems have been detected during host invasion, drug resistance, motility, phosphate uptake, osmoregulation, and nitrogen fixation, amongst others [(PUBMED:12015152)]. The two-component system consists of a histidine protein kinase environmental sensor that phosphorylates the receiver domain of a response regulator protein; phosphorylation induces a conformational change in the response regulator, which activates the effector domain, triggering the cellular response [(PUBMED:10966457)]. The domains of the two-component proteins are highly modular, but the core structures and activities are maintained. The response regulators act as phosphorylation-activated switches to affect a cellular response, usually by transcriptional regulation. Most of these proteins consist of two domains, an N-terminal response regulator receiver domain, and a variable C-terminal effector domain with DNA-binding activity. This entry represents the response regulator receiver domain, which belongs to the CheY family, and receives the signal from the sensor partner in the two-component system.
GO process:	regulation of transcription, DNA-dependent (GO:0006355), two-component signal transduction system (phosphorelay) (GO:0000160)
GO function:	two-component response regulator activity (GO:0000156)
Family alignment:	View or

There are 64290 REC domains in 61868 proteins in SMART's nrdb database.

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Evolution (species in which this domain is found)
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Go to specific node: Arabidopsis thaliana, Homo sapiens, Mus musculus, Saccharomyces cerevisiae
Cellular role (predicted cellular role)
Cellular role: signalling
Literature (relevant references for this domain)
Primary literature is listed below; Automatically-derived, secondary literature is also avaliable.
- Pao GM, SaierMHJ r
- Response regulators of bacterial signal transduction systems: selective domain shuffling during evolution.
- J Mol Evol. 1995; 40: 136-54
- Display abstract
- Response regulators of bacterial sensory transduction systems generally consist of receiver module domains covalently linked to effector domains. The effector domains include DNA binding and/or catalytic units that are regulated by sensor kinase-catalyzed aspartyl phosphorylation within their receiver modules. Most receiver modules are associated with three distinct families of DNA binding domains, but some are associated with other types of DNA binding domains, with methylated chemotaxis protein (MCP) demethylases, or with sensor kinases. A few exist as independent entities which regulate their target systems by noncovalent interactions. In this study the molecular phylogenies of the receiver modules and effector domains of 49 fully sequenced response regulators and their homologues were determined. The three major, evolutionarily distinct, DNA binding domains found in response regulators were evaluated for their phylogenetic relatedness, and the phylogenetic trees obtained for these domains were compared with those for the receiver modules. Members of one family (family 1) of DNA binding domains are linked to large ATPase domains which usually function cooperatively in the activation of E. coli sigma 54-dependent promoters or their equivalents in other bacteria. Members of a second family (family 2) always function in conjunction with the E. coli sigma 70 or its equivalent in other bacteria. A third family of DNA binding domains (family 3) functions by an uncharacterized mechanism involving more than one sigma factor. These three domain families utilize distinct helix-turn-helix motifs for DNA binding. The phylogenetic tree of the receiver modules revealed three major and several minor clusters of these domains. The three major receiver module clusters (clusters 1, 2, and 3) generally function with the three major families of DNA binding domains (families 1, 2, and 3, respectively) to comprise three classes of response regulators (classes 1, 2, and 3), although several exceptions exist. The minor clusters of receiver modules were usually, but not always, associated with other types of effector domains. Finally, several receiver modules did not fit into a cluster. It was concluded that receiver modules usually diverged from common ancestral protein domains together with the corresponding effector domains, although domain shuffling, due to intragenic splicing and fusion, must have occurred during the evolution of some of these proteins. Multiple sequence alignments of the 49 receiver modules and their various types of effector domains, together with other homologous domains, allowed definition of regions of striking sequence similarity and degrees of conservation of specific residues. Sequence data were correlated with structure/function when such information was available.(ABSTRACT TRUNCATED AT 250 WORDS)
- Volz K
- Structural conservation in the CheY superfamily.
- Biochemistry. 1993; 32: 11741-53
- Stock JB, Stock AM, Mottonen JM
- Signal transduction in bacteria.
- Nature. 1990; 344: 395-400
- Display abstract
- Cells display a remarkable ability to respond to small fluctuations in their surroundings. In simple microbial systems, information from sensory receptors feeds into a circuitry of regulatory proteins that transfer high energy phosphoryl groups from histidine to aspartate side chains. This phosphotransfer network couples environmental signals to an array of response elements that control cell motility and regulate gene expression.
- Stock AM, Mottonen JM, Stock JB, Schutt CE
- Three-dimensional structure of CheY, the response regulator of bacterial chemotaxis.
- Nature. 1989; 337: 745-9
- Display abstract
- Homologies among bacterial signal transduction proteins suggest that a common mechanism mediates processes such as chemotaxis, osmoregulation, sporulation, virulence, and responses to nitrogen, phosphorous and oxygen deprivation. A common kinase-mediated phosphotransfer reaction has recently been identified in chemotaxis, nitrogen regulation, and osmoregulation. In chemotaxis, the CheA kinase passes a phosphoryl group to the cytoplasmic protein CheY, which functions as a phosphorylation-activated switch that interacts with flagellar components to regulate motility. We report here the X-ray crystal structure of the Salmonella typhimurium CheY protein. The determination of the structure was facilitated by the use of site-specific mutagenesis to engineer heavy-atom binding sites. CheY is a single-domain protein composed of a doubly wound five-stranded parallel beta-sheet. The phosphoacceptor site in CheY is probably a cluster of aspartic-acid side chains near the C-terminal edge of the beta-sheet. The pattern of sequence similarity of CheY with components of other regulatory systems can be interpreted in the light of the CheY structure and supports the view that this family of proteins have a common structural motif and active site.
- Drlica K, Rouviere-Yaniv J
- Histonelike proteins of bacteria.
- Microbiol Rev. 1987; 51: 301-19
Metabolism (metabolic pathways involving proteins which contain this domain)

Structure (3D structures containing this domain)

3D Structures of REC domains in PDB

PDB code	Main view	Title
1a04		The structure of the nitrate/nitrite response regulator protein narl in the monoclinic c2 crystal form
1a0o		Chey-binding domain of chea in complex with chey
1a2o		Structural basis for methylesterase cheb regulation by a phosphorylation-activated domain
1ab5		Structure of chey mutant f14n, v21t
1ab6		Structure of chey mutant f14n, v86t
1b00		Phob receiver domain from escherichia coli
1bdj		Complex structure of hpt domain and chey
1c4w		1.9 a structure of a-thiophosphonate modified chey d57c
1cey		Assignments, secondary structure, global fold, and dynamics of chemotaxis y protein using three-and four-dimensional heteronuclear (13c,15n) nmr spectroscopy
1chn		Magnesium binding to the bacterial chemotaxis protein chey results in large conformational changes involving its functional surface
1cye		Three dimensional structure of chemotactic che y protein in aqueous solution by nuclear magnetic resonance methods
1d4z		Crystal structure of chey-95iv, a hyperactive chey mutant
1d5w		Phosphorylated fixj receiver domain
1dbw		Crystal structure of fixj-n
1dc7		Structure of a transiently phosphorylated "switch" in bacterial signal transduction
1dc8		Structure of a transiently phosphorylated "switch" in bacterial signal transduction
1dcf		Crystal structure of the receiver domain of the ethylene receptor of arabidopsis thaliana
1dck		Structure of unphosphorylated fixj-n complexed with mn2+
1dcm		Structure of unphosphorylated fixj-n with an atypical conformer (monomer a)
1djm		Solution structure of bef3-activated chey from escherichia coli
1dz3		Domain-swapping in the sporulation response regulator spo0a
1e6k		Two-component signal transduction system d12a mutant of chey
1e6l		Two-component signal transduction system d13a mutant of chey
1e6m		Two-component signal transduction system d57a mutant of chey
1eay		Chey-binding (p2) domain of chea in complex with chey from escherichia coli
1ehc		Structure of signal transduction protein chey
1f4v		Crystal structure of activated chey bound to the n-terminus of flim
1f51		A transient interaction between two phosphorelay proteins trapped in a crystal lattice reveals the mechanism of molecular recognition and phosphotransfer in singal transduction
1ffg		Chey-binding domain of chea in complex with chey at 2.1 a resolution
1ffs		Chey-binding domain of chea in complex with chey from crystals soaked in acetyl phosphate
1ffw		Chey-binding domain of chea in complex with chey with a bound imido diphosphate
1fqw		Crystal structure of activated chey
1fsp		Nmr solution structure of bacillus subtilis spo0f protein, structures
1hey		Investigating the structural determinants of the p21-like triphosphate and mg2+ binding site
1i3c		Response regulator for cyanobacterial phytochrome, rcp1
1j56		Minimized average structure of beryllofluoride-activated ntrc receiver domain: model structure incorporating active site contacts
1jbe		1.08 a structure of apo-chey reveals meta-active conformation
1jlk		Crystal structure of the mn(2+)-bound form of response regulator rcp1
1k66		Crystal structure of the cyanobacterial phytochrome response regulator, rcpb
1k68		Crystal structure of the phosphorylated cyanobacterial phytochrome response regulator rcpa
1kgs		Crystal structure at 1.50 a of an ompr/phob homolog from thermotoga maritima
1kmi		Crystal structure of an e.coli chemotaxis protein, chez
1krw		Solution structure and backbone dynamics of beryllofluoride- activated ntrc receiver domain
1krx		Solution structure of beryllofluoride-activated ntrc receiver domain: model structures incorporating active site contacts
1l5y		Crystal structure of mg2+ / bef3-bound receiver domain of sinorhizobium meliloti dctd
1l5z		Crystal structure of the e121k substitution of the receiver domain of sinorhizobium meliloti dctd
1m5t		Crystal structure of the response regulator divk
1m5u		Crystal structure of the response regulator divk. structure at ph 8.0 in the apo-form
1mav		Crystal structure of the response regulator divk at ph 6.0 in complex with mn2+
1mb0		Crystal structure of the response regulator divk at ph 8.0 in complex with mn2+
1mb3		Crystal structure of the response regulator divk at ph 8.5 in complex with mg2+
1mih		A role for chey glu 89 in chez-mediated dephosphorylation of the e. coli chemotaxis response regulator chey
1mvo		Crystal structure of the phop receiver domain from bacillus subtilis
1nat		Crystal structure of spoof from bacillus subtilis
1ntr		Solution structure of the n-terminal receiver domain of ntrc
1nxo		Micarec ph7.0
1nxp		Micarec ph4.5
1nxs		Micarec ph4.9
1nxt		Micarec ph 4.0
1nxv		Micarec ph 4.2
1nxw		Micarec ph 5.1
1nxx		Micarec ph 5.5
1ny5		Crystal structure of sigm54 activator (aaa+ atpase) in the inactive state
1oxb		Complex between ypd1 and sln1 response regulator domain in space group p2(1)2(1)2(1)
1oxk		Complex between ypd1 and sln1 response regulator domain in space group p3(2)
1p2f		Crystal structure analysis of response regulator drrb, a thermotoga maritima ompr/phob homolog
1p6q		Nmr structure of the response regulator chey2 from sinorhizobium meliloti, complexed with mg++
1p6u		Nmr structure of the bef3-activated structure of the response regulator chey2-mg2+ from sinorhizobium meliloti
1pey		Crystal structure of the response regulator spo0f complexed with mn2+
1pux		Nmr solution structure of bef3-activated spo0f, 20 conformers
1qkk		Crystal structure of the receiver domain and linker region of dctd from sinorhizobium meliloti
1qmp		Phosphorylated aspartate in the crystal structure of the sporulation response regulator, spo0a
1rnl		The nitrate/nitrite response regulator protein narl from narl
1s8n		Crystal structure of rv1626 from mycobacterium tuberculosis
1sd5		Crystal structure of rv1626
1srr		Crystal structure of a phosphatase resistant mutant of sporulation response regulator spo0f from bacillus subtilis
1tmy		Chey from thermotoga maritima (apo-i)
1u0s		Chemotaxis kinase chea p2 domain in complex with response regulator chey from the thermophile thermotoga maritima
1u8t		Crystal structure of chey d13k y106w alone and in complex with a flim peptide
1udr		Chey mutant with lys 91 replaced by asp, lys 92 replaced by ala, ile 96 replaced by lys and ala 98 replaced by leu (stabilizing mutations in helix 4)
1vlz		Uncoupled phosphorylation and activation in bacterial chemotaxis: the 2.1 angstrom structure of a threonine to isoleucine mutant at position 87 of chey
1w25		Response regulator pled in complex with c-digmp
1xhe		Crystal structure of the receiver domain of redox response regulator arca
1xhf		Crystal structure of the bef3-activated receiver domain of redox response regulator arca
1yio		Crystallographic structure of response regulator styr from pseudomonas fluorescens
1ymu		Signal transduction protein chey mutant with met 17 replaced by gly (m17g)
1ymv		Signal transduction protein chey mutant with phe 14 replaced by gly, ser 15 replaced by gly, and met 17 replaced by gly
1ys6		Crystal structure of the response regulatory protein prra from mycobacterium tuberculosis
1ys7		Crystal structure of the response regulator protein prra comlexed with mg2+
1zdm		Crystal structure of activated chey bound to xe
1zes		Bef3- activated phob receiver domain
1zgz		Crystal structure of the receiver domain of tmao respiratory system response regulator torr
1zh2		Crystal structure of the calcium-bound receiver domain of kdp potassium transport system response regulator kdpe
1zh4		Crystal structure of the mg+2/bef3-bound receiver domain of kdp potassium transport system response regulator kdpe
1zit		Structure of the receiver domain of ntrc4 from aquifex aeolicus
1zn2		Low resolution structure of response regulator styr
1zy2		Crystal structure of the phosphorylated receiver domain of the transcription regulator ntrc1 from aquifex aeolicus
2a9o		Crystal structures of an activated yycf homologue, the essential response regulator from s.pneumoniae in complex with bef3 and the effect of ph on bef3 binding, possible phosphate in the active site
2a9p		Medium resolution bef3 bound rr02-rec
2a9q		Low resolution structure rr02-rec on bef3 bound
2a9r		Rr02-rec phosphate in the active site
2ayx		Solution structure of the e.coli rcsc c-terminus (residues 700-949) containing linker region and phosphoreceiver domain
2ayz		Solution structure of the e.coli rcsc c-terminus (residues 817-949) containing phosphoreceiver domain
2b1j		Crystal structure of unphosphorylated chey bound to the n- terminus of flim
2b4a		Crystal structure of bh3024 protein (10175646) from bacillus halodurans at 2.42 a resolution
2che		Structure of the mg2+-bound form of chey and mechanism of phosphoryl transfer in bacterial chemotaxis
2chf		Structure of the mg2+-bound form of chey and the mechanism of phosphoryl transfer in bacterial chemotaxis
2chy		Three-dimensional structure of chey, the response regulator of bacterial chemotaxis
2fka		Crystal structure of mg(2+) and bef(3)(-)-bound chey in complex with chez(200-214) solved from a f432 crystal grown in caps (ph 10.5)
2flk		Crystal structure of chey in complex with chez(200-214) solved from a f432 crystal grown in caps (ph 10.5)
2flw		Crystal structure of mg2+ and bef3- ound chey in complex with chez 200-214 solved from a f432 crystal grown in hepes (ph 7.5)
2fmf		Crystal structure of chey in complex with chez 200-214 solved from a f432 crystal grown in hepes (ph 7.5)
2fmh		Crystal structure of mg2+ and bef3- bound chey in complex with chez 200-214 solved from a f432 crystal grown in tris (ph 8.4)
2fmi		Crystal structure of chey in complex with chez 200-214 solved from a f432 crystal grown in tris (ph 8.4)
2fmk		Crystal structure of mg2+ and bef3- bound chey in complex with chez 200-214 solved from a p2(1)2(1)2 crystal grown in mes (ph 6.0)
2fsp		Nmr solution structure of bacillus subtilis spo0f protein, minimized average structure
2ftk		Berylloflouride spo0f complex with spo0b
2gkg		Receiver domain from myxococcus xanthus social motility protein frzs
2gwr		Crystal structure of the response regulator protein mtra from mycobacterium tuberculosis
2hqo		Structure of a atypical orphan response regulator protein revealed a new phosphorylation-independent regulatory mechanism
2hqr		Structure of a atypical orphan response regulator protein revealed a new phosphorylation-independent regulatory mechanism
2i6f		Receiver domain from myxococcus xanthus social motility protein frzs
2id7		1.75 a structure of t87i phosphono-chey
2id9		1.85 a structure of t87i/y106w phosphono-chey
2idm		2.00 a structure of t87i/y106w phosphono-chey
2iyn		The co-factor-induced pre-active conformation in phob
2j48		Nmr structure of the pseudo-receiver domain of the cika protein.
2jb9		Phob response regulator receiver domain constitutively- active double mutant d10a and d53e.
2jba		Phob response regulator receiver domain constitutively- active double mutant d53a and y102c.
2jk1		Crystal structure of the wild-type hupr receiver domain
2jrl		Solution structure of the beryllofluoride-activated ntrc4 receiver domain dimer
2jvi		Nmr solution structure of the hyper-sporulation response regulator spo0f mutant h101a from bacillus subtilis
2jvj		Nmr solution structure of the hyper-sporulation response regulator spo0f mutant i90a from bacillus subtilis
2jvk		Nmr solution structure of the hyper-sporulation response regulator spo0f mutant l66a from bacillus subtilis
2nt3		Receiver domain from myxococcus xanthus social motility protein frzs (y102a mutant)
2nt4		Receiver domain from myxococcus xanthus social motility protein frzs (h92f mutant)
2oqr		The structure of the response regulator regx3 from mycobacterium tuberculosis
2pkx		E.coli response regulator phop receiver domain
2pl1		Berrylium fluoride activated receiver domain of e.coli phop
2pl9		Crystal structure of chey-mg(2+)-bef(3)(-) in complex with chez(c19) peptide solved from a p2(1)2(1)2 crystal
2pln		Crystal structure analysis of hp1043, an orphan resonse regulator of h. pylori
2pmc		Crystal structure of chey-mg(2+) in complex with chez(c15) peptide solved from a p1 crystal
2qr3		Crystal structure of the n-terminal signal receiver domain of two-component system response regulator from bacteroides fragilis
2qsj		Crystal structure of a luxr family dna-binding response regulator from silicibacter pomeroyi
2qv0		Crystal structure of the response regulatory domain of protein mrke from klebsiella pneumoniae
2qvg		The crystal structure of a two-component response regulator from legionella pneumophila
2qxy		Crystal structure of a response regulator from thermotoga maritima
2qzj		Crystal structure of a two-component response regulator from clostridium difficile
2r25		Complex of ypd1 and sln1-r1 with bound mg2+ and bef3-
2rdm		Crystal structure of response regulator receiver protein from sinorhizobium medicae wsm419
2rjn		Crystal structure of an uncharacterized protein q2bku2 from neptuniibacter caesariensis
2tmy		Chey from thermotoga maritima (apo-ii)
2v0n		Activated response regulator pled in complex with c-digmp and gtp-alpha-s
2vuh		Crystal structure of the d55e mutant of the hupr receiver domain
2vui		Crystal structure of the hupr receiver domain in inhibitory phospho-state
2zay		Crystal structure of response regulator from desulfuromonas acetoxidans
2zwm		Crystal structure of yycf receiver domain from bacillus subtilis
3a0r		Crystal structure of histidine kinase thka (tm1359) in complex with response regulator protein trra (tm1360)
3a0u		Crystal structure of response regulator protein trra (tm1360) from thermotoga maritima in complex with mg(2+)- bef (wild type)
3a10		Crystal structure of response regulator protein trra (tm1360) from thermotoga maritima in complex with mg(2+)- bef (semet, l89m)
3b2n		Crystal structure of dna-binding response regulator, luxr family, from staphylococcus aureus
3bre		Crystal structure of p.aeruginosa pa3702
3c3m		Crystal structure of the n-terminal domain of response regulator receiver protein from methanoculleus marisnigri jr1
3c3w		Crystal structure of the mycobacterium tuberculosis hypoxic response regulator dosr
3c97		Crystal structure of the response regulator receiver domain of a signal transduction histidine kinase from aspergillus oryzae
3cfy		Crystal structure of signal receiver domain of putative luxo repressor protein from vibrio parahaemolyticus
3cg0		Crystal structure of signal receiver domain of modulated diguanylate cyclase from desulfovibrio desulfuricans g20, an example of alternate folding
3cg4		Crystal structure of response regulator receiver domain protein (chey-like) from methanospirillum hungatei jf-1
3chy		Crystal structure of escherichia coli chey refined at 1.7- angstrom resolution
3cnb		Crystal structure of signal receiver domain of dna binding response regulator protein (merr) from colwellia psychrerythraea 34h
3crn		Crystal structure of response regulator receiver domain protein (chey-like) from methanospirillum hungatei jf-1
3cu5		Crystal structure of a two component transcriptional regulator arac from clostridium phytofermentans isdg
3cwo		A beta/alpha-barrel built by the combination of fragments from different folds
3cz5		Crystal structure of two-component response regulator, luxr family, from aurantimonas sp. si85-9a1
3dge		Structure of a histidine kinase-response regulator complex reveals insights into two-component signaling and a novel cis-autophosphorylation mechanism
3dgf		Structure of a histidine kinase-response regulator complex reveals insights into two-component signaling and a novel cis-autophosphorylation mechanism
3dzd		Crystal structure of sigma54 activator ntrc4 in the inactive state
3eod		Crystal structure of n-terminal domain of e. coli rssb
3eq2		Structure of hexagonal crystal form of pseudomonas aeruginosa rssb
3eqz		Crystal structure of a response regulator from colwellia psychrerythraea
3eul		Structure of the signal receiver domain of the putative response regulator narl from mycobacterium tuberculosis
3f6c		Crystal structure of n-terminal domain of positive transcription regulator evga from escherichia coli
3f7a		Structure of orthorhombic crystal form of pseudomonas aeruginosa rssb
3f7n		Crystal structure of chey triple mutant f14e, n59m, e89l complexed with bef3- and mn2+
3fft		Crystal structure of chey double mutant f14e, e89r complexed with bef3- and mn2+
3ffw		Crystal structure of chey triple mutant f14q, n59k, e89y complexed with bef3- and mn2+
3ffx		Crystal structure of chey triple mutant f14e, n59r, e89h complexed with bef3- and mn2+
3fgz		Crystal structure of chey triple mutant f14e, n59m, e89r complexed with bef3- and mn2+
3gl9		The structure of a histidine kinase-response regulator complex sheds light into two-component signaling and reveals a novel cis autophosphorylation mechanism
3grc		Crystal structure of a sensor protein from polaromonas sp. js666
3gt7		Crystal structure of signal receiver domain of signal transduction histidine kinase from syntrophus aciditrophicus
3h5i		Crystal structure of the n-terminal domain of a response regulator/sensory box/ggdef 3-domain protein from carboxydothermus hydrogenoformans
3hdg		Crystal structure of the n-terminal domain of an uncharacterized protein (ws1339) from wolinella succinogenes
3hdv		Crystal structure of response regulator receiver protein from pseudomonas putida
3heb		Crystal structure of response regulator receiver domain from rhodospirillum rubrum
3hv2		Crystal structure of signal receiver domain of hd domain- containing protein from pseudomonas fluorescens pf-5
3i42		Structure of response regulator receiver domain (chey-like) from methylobacillus flagellatus
3i5a		Crystal structure of full-length wpsr from pseudomonas syringae
3ilh		Crystal structure of two component response regulator from cytophaga hutchinsonii
3jte		Crystal structure of response regulator receiver domain protein from clostridium thermocellum
3kcn		The crystal structure of adenylate cyclase from rhodopirellula baltica
3kht		Crystal structure of response regulator from hahella chejuensis
3tmy		Chey from thermotoga maritima (mn-iii)
4tmy		Chey from thermotoga maritima (mg-iv)
5chy		Structure of chemotaxis protein chey
6chy		Structure of chemotaxis protein chey

Links (links to other resources describing this domain)
PFAM response_reg
INTERPRO IPR001789

PFAM	response_reg
INTERPRO	IPR001789