phosphoacceptor receiver (REC) domain of YesN and related helix-turn-helix containing response regulators; This family is composed of uncharacterized response regulators that contain a REC domain and a AraC family helix-turn-helix (HTH) DNA-binding output domain, including Bacillus subtilis uncharacterized transcriptional regulatory protein YesN and Staphylococcus aureus uncharacterized response regulatory protein SAR0214. YesN is a member of the two-component regulatory system YesM/YesN and SAR0214 is a member of the probable two-component regulatory system SAR0215/SAR0214. Also included in this family is the AlgR-like group of LytTR/AlgR family response, which includes Pseudomonas aeruginosa positive alginate biosynthesis regulatory protein AlgR and Bacillus subtilis sensory transduction protein LytT, among others. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503147044  45 LEMLEKNRhFDIYLLDILMPELDGLSVGRVIRESDSSATIIYLS----FssDYAVESYRVRAQDYLLKPVTQEALFATLD 120
Cdd:cd17536   38 LELIEEHK-PDIVITDIRMPGMDGLELIEKIRELYPDIKIIILSgyddF--EYAQKAIRLGVVDYLLKPVDEEELEEALE 114

                 ....*..
gi 503147044 121 EAIKTID 127
Cdd:cd17536  115 KAKEELD 121

sigma-54-dependent response regulator transcription factor ZraR;

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503147044  45 LEMLEKNRH--FDIYLLDILMPELDGLSVGRVIRESDSSATI-IYLSFSS-DYAVESYRVRAQDYLLKPVTQEALFATLD 120
Cdd:PRK10365  39 RQALEQVREqvFDLVLCDVRMAEMDGIATLKEIKALNPAIPVlIMTAYSSvETAVEALKTGALDYLIKPLDFDNLQATLE 118

                 ...
gi 503147044 121 EAI 123
Cdd:PRK10365 119 KAL 121

sporulation transcription factor Spo0A; Spo0A, the stage 0 sporulation protein A, is a transcription factor critical for the initiation of sporulation. It contains a response regulator receiver domain (pfam00072). In Bacillus subtilis, it works together with response regulator Spo0F and the phosphotransferase Spo0B, both of which are missing from at least some sporulating species and thus not part of the endospore forming bacteria minimal gene set. Spo0A, however, is universal among endospore-forming species. [Cellular processes, Sporulation and germination]

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503147044    2 LQIAICDDEAEdlkrISHLAAAYAEAHPELNIACSQFlspcNLLEMLE--KNRHFDIYLLDILMPELDGLSVGRVIRESD 79
Cdd:TIGR02875   3 IRIVIADDNKE----FCNLLKEYLAAQPDMEVVGVAH----NGVDALEliKEQQPDVVVLDIIMPHLDGIGVLEKLNEIE 74

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 503147044   80 SSA--TIIYLsfsSDYAVESYRVRAQD-----YLLKPVTQEALFATLDE----AIKTIDA 128
Cdd:TIGR02875  75 LSArpRVIML---SAFGQEKITQRAVAlgadyYVLKPFDLEILAARIRQlawgTNADILA 131

phosphoacceptor receiver (REC) domain of YesN and related helix-turn-helix containing response regulators; This family is composed of uncharacterized response regulators that contain a REC domain and a AraC family helix-turn-helix (HTH) DNA-binding output domain, including Bacillus subtilis uncharacterized transcriptional regulatory protein YesN and Staphylococcus aureus uncharacterized response regulatory protein SAR0214. YesN is a member of the two-component regulatory system YesM/YesN and SAR0214 is a member of the probable two-component regulatory system SAR0215/SAR0214. Also included in this family is the AlgR-like group of LytTR/AlgR family response, which includes Pseudomonas aeruginosa positive alginate biosynthesis regulatory protein AlgR and Bacillus subtilis sensory transduction protein LytT, among others. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503147044  45 LEMLEKNRhFDIYLLDILMPELDGLSVGRVIRESDSSATIIYLS----FssDYAVESYRVRAQDYLLKPVTQEALFATLD 120
Cdd:cd17536   38 LELIEEHK-PDIVITDIRMPGMDGLELIEKIRELYPDIKIIILSgyddF--EYAQKAIRLGVVDYLLKPVDEEELEEALE 114

                 ....*..
gi 503147044 121 EAIKTID 127
Cdd:cd17536  115 KAKEELD 121

phosphoacceptor receiver (REC) domain of LytTR/AlgR family response regulators similar to AlgR; Members of the LytTR/AlgR family of response regulators contain a REC domain and a unique LytTR DNA-binding output domain that lacks the helix-turn-helix motif and consists mostly of beta-strands. Transcriptional regulators with the LytTR-type output domains are involved in biosynthesis of extracellular polysaccharides, fimbriation, expression of exoproteins, including toxins, and quorum sensing. Included in this AlgR-like group of LytTR/AlgR family response regulators are Streptococcus agalactiae sensory transduction protein LytR, Pseudomonas aeruginosa positive alginate biosynthesis regulatory protein AlgR, Bacillus subtilis sensory transduction protein LytT, and Escherichia coli transcriptional regulatory protein BtsR, which are members of two-component regulatory systems. LytR and LytT are components of regulatory systems that regulate genes involved in cell wall metabolism. AlgR positively regulates the algD gene, which codes for a GDP-mannose dehydrogenase, a key enzyme in the alginate biosynthesis pathway. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503147044   6 ICDDEAEDLKRISHLAaayaEAHPELNIaCSQFLSPCNLLEMLEKNRhFDIYLLDILMPELDGLSVGRVIRESDSSATII 85
Cdd:cd17532    3 IVDDEPLAREELRYLL----EEHPDIEI-VGEAENGEEALEAIEELK-PDVVFLDIQMPGLDGLELAKKLSKLAKPPLIV 76

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 503147044  86 YLSFSSDYAVESYRVRAQDYLLKPVTQEALFATLDEAIKT 125
Cdd:cd17532   77 FVTAYDEYAVEAFELNAVDYLLKPFSEERLAEALAKLRKR 116

CheY-like REC (receiver) domain, includes chemotaxis protein CheY and sporulation regulator Spo0F [Signal transduction mechanisms];

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503147044   1 MLQIAICDDEAEDLKRISHLAAayaeahpELNIACSQFLSPCNLLEMLEKNRhFDIYLLDILMPELDGLSVGRVIRESDS 80
Cdd:COG0784    5 GKRILVVDDNPDNRELLRRLLE-------RLGYEVTTAEDGAEALELLRAGP-PDLILLDINMPGMDGLELLRRIRALPR 76

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 503147044  81 SAT--IIYLSFSSDYAV--ESYRVRAQDYLLKPVTQEALFATLDEAIKTIDA 128
Cdd:COG0784   77 LPDipIIALTAYADEEDreRALEAGADDYLTKPVDPEELLEALRRLLARASA 128

DNA-binding response regulator DpiB of citrate/malate metabolism [Transcription, Signal transduction mechanisms];

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503147044   1 MLQIAICDDEAedlkRISHLAAAYAEAHPELNIaCSQFLSPCNLLEMLEKNRhFDIYLLDILMPELDGLSVGRVIRESDS 80
Cdd:COG4565    3 MIRVLIVEDDP----MVAELLRRYLERLPGFEV-VGVASSGEEALALLAEHR-PDLILLDIYLPDGDGLELLRELRARGP 76

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 503147044  81 SATIIYLSFSSDYAV--ESYRVRAQDYLLKPVTQEALFATLDEAIK 124
Cdd:COG4565   77 DVDVIVITAARDPETvrEALRAGVVDYLIKPFTFERLREALERYLE 122

Two-component response regulator, YesN/AraC family, consists of REC and AraC-type DNA-binding domains [Signal transduction mechanisms, Transcription];

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 503147044  45 LEMLEKNRhFDIYLLDILMPELDGLSVGRVIRESDSSATIIYLSFSSD--YAVESYRVRAQDYLLKP 109
Cdd:COG4753   38 LELLEEHK-PDLVITDINMPGMDGLELLEAIRELDPDTKIIILSGYSDfeYAQEAIKLGADDYLLKP 103

phosphoacceptor receiver (REC) domain of response regulators (RRs) and pseudo response regulators (PRRs); Two-component systems (TCSs) involving a sensor and a response regulator are used by bacteria to adapt to changing environments. Processes regulated by two-component systems in bacteria include sporulation, pathogenicity, virulence, chemotaxis, and membrane transport. Response regulators (RRs) share the common phosphoacceptor REC domain and different effector/output domains such as DNA, RNA, ligand-binding, protein-binding, or enzymatic domains. Response regulators regulate transcription, post-transcription or post-translation, or have functions such as methylesterases, adenylate or diguanylate cyclase, c-di-GMP-specific phosphodiesterases, histidine kinases, serine/threonine protein kinases, and protein phosphatases, depending on their output domains. The function of some output domains are still unknown. TCSs are found in all three domains of life - bacteria, archaea, and eukaryotes, however, the presence and abundance of particular RRs vary between the lineages. Archaea encode very few RRs with DNA-binding output domains; most are stand-alone REC domains. Among eukaryotes, TCSs are found primarily in protozoa, fungi, algae, and green plants. REC domains function as phosphorylation-mediated switches within RRs, but some also transfer phosphoryl groups in multistep phosphorelays.

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 503147044  48 LEKNRHFDIYLLDILMPELDGLSVGRVIRESDSSATIIYLS--FSSDYAVESYRVRAQDYLLKP 109
Cdd:cd00156   36 LLREERPDLVLLDLMMPGMDGLELLRKLRELPPDIPVIVLTakADEEDAVRALELGADDYLVKP 99

phosphoacceptor receiver (REC) domain of OmpR family response regulators; OmpR-like proteins are one of the most widespread transcriptional regulators. OmpR family members contain REC and winged helix-turn-helix (wHTH) DNA-binding output effector domain. They are involved in the control of environmental stress tolerance (such as the oxidative, osmotic and acid stress response), motility, virulence, outer membrane biogenesis and other processes. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503147044  45 LEMLEKNRhFDIYLLDILMPELDGLSVGRVIRESDSSATIIYLSFSSDyavESYRVR-----AQDYLLKP 109
Cdd:cd17574   34 LELAREEQ-PDLIILDVMLPGMDGFEVCRRLREKGSDIPIIMLTAKDE---EEDKVLglelgADDYITKP 99

Response regulator c-di-GMP phosphodiesterase, RpfG family, contains REC and HD-GYP domains [Signal transduction mechanisms];

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503147044   8 DDEAEDLKRISHLAAayaeahpELNIACSQFLSPCNLLEMLEKNRhFDIYLLDILMPELDGLSVGRVIRESDSSA--TII 85
Cdd:COG3437   13 DDDPENLELLRQLLR-------TLGYDVVTAESGEEALELLLEAP-PDLILLDVRMPGMDGFELLRLLRADPSTRdiPVI 84

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 503147044  86 YLS--FSSDYAVESYRVRAQDYLLKPVTQEALFATLDEAIKTIDAEDARR 133
Cdd:COG3437   85 FLTalADPEDRERALEAGADDYLTKPFDPEELLARVRNALELRRLQRELD 134

phosphoacceptor receiver (REC) domain of hybrid sensor histidine kinases/response regulators similar to Arabidopsis thaliana CKI1 and Escherichia coli RcsC; This family is composed of hybrid sensor histidine kinases/response regulators that are sensor histidine kinases (HKs) fused with a REC domain, similar to the sensor histidine kinase CKI1 from Arabidopsis thaliana, which is involved in multi-step phosphorelay (MSP) signaling that mediates responses to a variety of important stimuli in plants. MSP involves a signal being transferred from HKs via histidine phosphotransfer proteins (AHP1-AHP5) to nuclear response regulators. The CKI1 REC domain specifically interacts with the downstream signaling protein AHP2, AHP3 and AHP5. The plant MSP system has evolved from the prokaryotic two-component system (TCS), which allows organisms to sense and respond to changes in environmental conditions. This family also includes bacterial hybrid sensor HKs such as Escherichia coli RcsC, which is a component of the Rcs signalling pathway that controls a variety of physiological functions like capsule synthesis, cell division, and motility. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503147044  45 LEMLeKNRHFDIYLLDILMPELDGLSVGRVIRESDSSAT---IIYLsfsSDYAVESYRVRAQ-----DYLLKPVTQEALF 116
Cdd:cd17546   35 LELL-KEEPFDLVLMDLQMPVMDGLEATRRIRELEGGGRrtpIIAL---TANALEEDREKCLeagmdDYLSKPVKLDQLK 110

                 ...
gi 503147044 117 ATL 119
Cdd:cd17546  111 EVL 113

phosphoacceptor receiver (REC) domain of chemotaxis protein CheY; The chemotaxis response regulator CheY contains a stand-alone REC domain. Chemotaxis is a behavior known for motile bacteria that directs their movement in response to chemical gradients. CheY is involved in transmitting sensory signals from chemoreceptors to the flagellar motors. Phosphorylated CheY interacts with the flagella switch components FliM and FliY, which causes counterclockwise rotation of the flagella, resulting in smooth swimming. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503147044  43 NLLEMLEKNRHF--DIYLLDILMPELDGLSVGRVIRESDSSATIIYLSFSSDYA--VESYRVRAQDYLLKPVTQEALFAT 118
Cdd:cd17542   33 NGEEAVEKYKELkpDLVTMDITMPEMDGIEALKEIKKIDPNAKVIMCSAMGQEEmvKEAIKAGAKDFIVKPFQPERVLEA 112

                 ....
gi 503147044 119 LDEA 122
Cdd:cd17542  113 VEKV 116

sigma-54-dependent response regulator transcription factor ZraR;

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503147044  45 LEMLEKNRH--FDIYLLDILMPELDGLSVGRVIRESDSSATI-IYLSFSS-DYAVESYRVRAQDYLLKPVTQEALFATLD 120
Cdd:PRK10365  39 RQALEQVREqvFDLVLCDVRMAEMDGIATLKEIKALNPAIPVlIMTAYSSvETAVEALKTGALDYLIKPLDFDNLQATLE 118

                 ...
gi 503147044 121 EAI 123
Cdd:PRK10365 119 KAL 121

phosphoacceptor receiver (REC) domain of uncharacterized response regulators containing a CheC domain; This subfamily is composed of uncharacterized proteins containing an N-terminal REC domain and a C-terminal CheC domain that may function as the output/effector domain of a response regulator. CheC is a CheY-P phosphatase, affecting the level of phosphorylated CheY which controls the sense of flagella rotation and determine swimming behavior of chemotactic bacteria. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503147044   2 LQIAICDDEAedLKRISHLAAAYAEAHPELNIACsqflspcNLLEMLE--KNRHFDIYLLDILMPELDGLSVGRVIRESD 79
Cdd:cd17593    1 MKVLICDDSS--MARKQLARALPADWDVEITFAE-------NGEEALEilREGRIDVLFLDLTMPVMDGYEVLEALPVEQ 71

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 503147044  80 SSATIIYLsfSSDYAVESY-RVR---AQDYLLKPVTQEALFATLDE 121
Cdd:cd17593   72 LETKVIVV--SGDVQPEAKeRVLelgALAFLKKPFDPEKLAQLLEE 115

phosphoacceptor receiver (REC) domain of type B Arabidopsis response regulators (ARRs) and similar domains; Type-B ARRs (Arabidopsis response regulators) are a class of MYB-type transcription factors that act as major players in the transcriptional activation of cytokinin-responsive genes. They directly regulate the expression of type-A ARR genes and other downstream target genes. Cytokinin is a plant hormone implicated in many growth and development processes including shoot organogenesis, leaf senescence, sink/source relationships, vascular development, lateral bud release, and photomorphogenic development. Cytokinin signaling involves a phosphorelay cascade by histidine kinase receptors (AHKs), histidine phosphotransfer proteins (AHPs) and downstream ARRs. ARRs are divided into two groups, type-A and -B, according to their sequence and domain structure. Type-B ARRs contain a receiver (REC) domain and a large C-terminal extension that has characteristics of an effector or output domain, with a Myb-like DNA binding domain referred to as the GARP domain. The GARP domain is a motif specific to plant transcription factors. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503147044  31 LNIACSQFLSPCNLLEMLEKNRH-FDIYLLDILMPELDGLSVGRVIRESDSSATIIylsFSSDYAVESYRV----RAQDY 105
Cdd:cd17584   21 CGYQVTTCTDAEEALSMLRENKDeFDLVITDVHMPDMDGFEFLELIRLEMDLPVIM---MSADGSTSTVMKglahGACDY 97

                         90
                 ....*....|
gi 503147044 106 LLKPVTQEAL 115
Cdd:cd17584   98 LLKPVSIEDL 107

phosphoacceptor receiver (REC) domain of PdtaR and similar proteins; This subfamily includes Mycobacterium tuberculosis PdtaR, also called Rv1626, and similar proteins containing a REC domain and an ANTAR (AmiR and NasR transcription antitermination regulators) RNA-binding output domain. PdtaR is a response regulator that acts at the level of transcriptional antitermination and is a member of the PdtaR/PdtaS two-component regulatory system. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503147044  55 DIYLLDILMPELDGLSVGRVIRESDSSATIIYLSFSSDYAVESYR-VRAQDYLLKPVTQEALFATLDEAI 123
Cdd:cd19932   47 DLVIMDVKMPRLDGIEAAKIITSENIAPIVLLTAYSQQDLVERAKeAGAMAYLVKPFSESDLIPAIEMAI 116

phosphoacceptor receiver (REC) domain of Thermotoga maritima response regulator TrrA and similar domains; Thermotoga maritima contains a two-component signal transduction system (TCS) composed of the ThkA sensory histidine kinase (HK) and its cognate response regulator (RR) TrrA; the specific function of the system is unknown. TCSs couple environmental stimuli to adaptive responses. TrrA is a stand-alone RR containing only a REC domain with no output/effector domain. The REC domain itself functions as an effector domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 503147044  45 LEMLEKNRhFDIYLLDILMPELDGLSVGRVIRESDSSATII----YLSFSSDYAVESyrvrAQDYLLK 108
Cdd:cd17554   37 LEKLESED-PDLVILDIKMPGMDGLETLRKIREKKPDLPVIictaYSEYKSDFSSWA----ADAYVVK 99

phosphoacceptor receiver (REC) domain of DrrD-like OmpR family response regulators; DrrD is a OmpR/PhoB homolog from Thermotoga maritima whose function is not yet known. This subfamily also includes Streptococcus agalactiae transcriptional regulatory protein DltR, part of the DltS/DltR two-component system (TCS), and Pseudomonas aeruginosa transcriptional activator protein PfeR, part of the PfeR/PfeS TCS, which activates expression of the ferric enterobactin receptor. The DltS/DltR TCS regulates the expression of the dlt operon, which comprises four genes (dltA, dltB, dltC, and dltD) that catalyze the incorporation of D-alanine residues into the lipoteichoic acids. Members of this subfamily belong to the OmpR/PhoB family, which comprises of two domains, an N-terminal receiver domain and a C-terminal DNA-binding winged helix-turn-helix effector domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503147044  45 LEMLEKNRhFDIYLLDILMPELDGLSVGRVIRESDSSATIIYLSFSSDyavESYRVR-----AQDYLLKPvtqealFAtL 119
Cdd:cd17625   34 LEYALSGI-YDLIILDIMLPGMDGLEVLKSLREEGIETPVLLLTALDA---VEDRVKgldlgADDYLPKP------FS-L 102

                 ....*....
gi 503147044 120 DEAIKTIDA 128
Cdd:cd17625  103 AELLARIRA 111

phosphoacceptor receiver (REC) domain of citrate family two-component system response regulators; This family includes Lactobacillus paracasei MaeR, Escherichia coli DcuR and DpiA, Klebsiella pneumoniae CitB, as well as Bacillus DctR, MalR, and CitT. These are all response regulators of two-component systems (TCSs) from the citrate family, and are involved in the transcriptional regulation of genes associated with L-malate catabolism (MaeRK), citrate-specific fermentation (DpiAB, CitAB), plasmid inheritance (DpiAB), anaerobic fumarate respiratory system (DcuRS), and malate transport/utilization (MalKR). REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503147044   2 LQIAICDDEAedlkRISHLAAAYAEAHPELNIAcsqfLSPCNLLEMLE--KNRHFDIYLLDILMPELDGLSVGRVIRESD 79
Cdd:cd19925    1 INVLIVEDDP----MVAEIHRAYVEQVPGFTVI----GTAGTGEEALKllKERQPDLILLDIYLPDGNGLDLLRELRAAG 72

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 503147044  80 SSATIIYLSFSSDYAV--ESYRVRAQDYLLKPVTQEALFATLD 120
Cdd:cd19925   73 HDVDVIVVTAANDVETvrEALRLGVVDYLIKPFTFERLRQRLE 115

phosphoacceptor receiver (REC) domain of CusR-like OmpR family response regulators; Escherichia coli CusR is part of the CusS/CusR two-component system (TCS) that is involved in response to copper and silver. Other members of this subfamily include Escherichia coli PcoR, Pseudomonas syringae CopR, and Streptomyces coelicolor CutR, which are all transcriptional regulatory proteins and components of TCSs that regulate genes involved in copper resistance and/or metabolism. member of the subfamily is Escherichia coli HprR (hydrogen peroxide response regulator), previously called YdeW, which is part of the HprSR (or YedVW) TCS involved in stress response to hydrogen peroxide, as well as Cupriavidus metallidurans CzcR, which is part of the CzcS/CzcR TCS involved in the control of cobalt, zinc, and cadmium homeostasis. Members of this subfamily belong to the OmpR family of DNA-binding response regulators, which contain N-terminal receiver (REC) and C-terminal DNA-binding winged helix-turn-helix effector domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503147044  45 LEMLEKNRhFDIYLLDILMPELDGLSVGRVIRESDSSATIIYLSfSSDyAVEsYRVR-----AQDYLLKP 109
Cdd:cd19935   35 LHLALTNE-YDLIILDVMLPGLDGLEVLRRLRAAGKQTPVLMLT-ARD-SVE-DRVKgldlgADDYLVKP 100

phosphoacceptor receiver (REC) domain of Brucella abortus CpdR and CckA, and similar domains; Two-component systems (TCSs), consisting of a sensor and a response regulator, are used by bacteria to adapt to changing environments. Processes regulated by TCSs in bacteria include sporulation, pathogenicity, virulence, chemotaxis and membrane transport. Response regulators share the common phosphoacceptor REC domain and differ output domains such as DNA, RNA, ligand, and protein-binding, or enzymatic domain. CpdR is a stand-alone REC protein. CckA is a sensor histidine kinase containing N-terminal PAS domains and a C-terminal REC domain. CpdR and CckA are components of a regulatory phosphorelay system (composed of CckA, ChpT, CtrA and CpdR) that controls Brucella abortus cell growth, division, and intracellular survival inside mammalian host cells. CckA autophosphorylates in the presence of ATP and transfers a phosphoryl group to the conserved aspartic acid residue on its C-terminal REC domain, which is relayed to the ChpT phosphotransferase. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 503147044  45 LEMLEKNRHFDIYLLDILMPELDGLSVGRVIRESDSSATIIYLS-FSSD-YAVESYRVRAQDYLLKP 109
Cdd:cd18160   36 LEKLQQGKDIDIVVTDIVMPEMDGIELAREARKIDPDVKILFISgGAAAaPELLSDAVGDNATLKKP 102

Two-component response regulator, AmiR/NasT family, consists of REC and RNA-binding antiterminator (ANTAR) domains [Signal transduction mechanisms, Transcription];

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503147044   1 MLQIAICDDEAEDLKRIS-HLAAA----YAEAHpelniacsqflSPCNLLEMLEKnRHFDIYLLDILMPELDGLSVGRVI 75
Cdd:COG3707    3 GLRVLVVDDEPLRRADLReGLREAgyevVAEAA-----------DGEDAVELVRE-LKPDLVIVDIDMPDRDGLEAARQI 70

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 503147044  76 RESDSSATIIYLSFSSDYAVE-SYRVRAQDYLLKPVTQEALFATLDEAI 123
Cdd:COG3707   71 SEERPAPVILLTAYSDPELIErALEAGVSAYLVKPLDPEDLLPALELAL 119

phosphoacceptor receiver (REC) domain of BsPhoP-like OmpR family response regulators; Bacillus subtilis PhoP (BsPhoP) is part of the PhoPR two-component system that participates in a signal transduction network that controls adaptation of the bacteria to phosphate deficiency by regulating (activating or repressing) genes of the Pho regulon upon phosphorylation by PhoR. When activated, PhoPR directs expression of phosphate scavenging enzymes, lowers synthesis of the phosphate-rich wall teichoic acid (WTA) and initiates synthesis of teichuronic acid, a non-phosphate containing replacement anionic polymer. Members of this subfamily belong to the OmpR family of DNA-binding response regulators, which are characterized by a REC domain and a winged helix-turn-helix (wHTH) DNA-binding output effector domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503147044  45 LEMLEKNRhFDIYLLDILMPELDGLSVGRVIRESD--SSATIIYLSFSSDyavESYRV-----RAQDYLLKPVTQEALFA 117
Cdd:cd19937   34 LKRAKDEK-PDLIILDLMLPGIDGLEVCRILRSDPktSSIPIIMLTAKGE---EFDKVlglelGADDYITKPFSPRELLA 109

phosphoacceptor receiver (REC) domain of DNA-binding transcriptional regulator NtrC; DNA-binding transcriptional regulator NtrC is also called nitrogen regulation protein NR(I) or nitrogen regulator I (NRI). It contains an N-terminal receiver (REC) domain, followed by a sigma-54 interaction domain, and a C-terminal helix-turn-helix DNA-binding domain. It is part of the two-component regulatory system NtrB/NtrC, which controls expression of the nitrogen-regulated (ntr) genes in response to nitrogen limitation. DNA-binding response regulator NtrC is phosphorylated by NtrB; phosphorylation of the N-terminal REC domain activates the central sigma-54 interaction domain and leads to the transcriptional activation from promoters that require sigma(54)-containing RNA polymerase. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503147044  20 LAAAYAEAHpelnIACSQFLSPCNLLEMLEKNRHfDIYLLDILMPELDGLSVGRVIRESDSSATIIYLSFSSDY--AVES 97
Cdd:cd19919   16 LERALAGAG----LTVTSFENAQEALAALASSQP-DVLISDIRMPGMDGLALLAQIKQRHPDLPVIIMTAHSDLdsAVSA 90

                         90       100       110
                 ....*....|....*....|....*....|
gi 503147044  98 YRVRAQDYLLKPVtqealfaTLDEAIKTID 127
Cdd:cd19919   91 YQGGAFEYLPKPF-------DIDEAVALVE 113

nitrogen regulation protein NR(I); Provisional

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503147044  35 CSQFLSPCNLLEMLEKNRHfDIYLLDILMPELDGLSVGRVIRESDSSATIIYLSFSSDY--AVESYRVRAQDYLLKPVTQ 112
Cdd:PRK10923  30 CTTFENGNEVLEALASKTP-DVLLSDIRMPGMDGLALLKQIKQRHPMLPVIIMTAHSDLdaAVSAYQQGAFDYLPKPFDI 108

                         90
                 ....*....|.
gi 503147044 113 EALFATLDEAI 123
Cdd:PRK10923 109 DEAVALVERAI 119

two-component system response regulator RssB;

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503147044  45 LEMLEKNRHfDIYLLDILMPELDGLSVGRVIRESDSSATIIYLSFSSDYA--VESYRVRAQDYLLKPVT-----QEALFA 117
Cdd:PRK10693  10 LELLGGFTP-DLIICDLAMPRMNGIEFVEHLRNRGDQTPVLVISATENMAdiAKALRLGVQDVLLKPVKdlnrlREMVFA 88

                         90
                 ....*....|....*..
gi 503147044 118 TLDEAIKTIDAEDARRL 134
Cdd:PRK10693  89 CLYPSMFNSRVEEEERL 105

phosphoacceptor receiver (REC) domain of YrcF-like OmpR family response regulators; YycF appears to play an important role in cell wall integrity in a wide range of gram-positive bacteria, and may also modulate cell membrane integrity. It functions as part of a phosphotransfer system that ultimately controls the levels of competence within the bacteria. YycF belongs to the OmpR family of response regulators, which are characterized by a REC domain and a winged helix-turn-helix effector domain involved in DNA binding. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 503147044  46 EMLEKNRHF--DIYLLDILMPELDGLSVGRVIRESdSSATIIYLSfSSDYAVES---YRVRAQDYLLKPVTQEALFA 117
Cdd:cd17614   33 EALEKVEEEqpDLILLDLMLPEKDGLEVCREVRKT-SNVPIIMLT-AKDSEVDKvlgLELGADDYVTKPFSNRELLA 107