phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY3 and similar CheY family proteins; CheY family chemotaxis response regulators (RRs) comprise about 17% of bacterial RRs and almost half of all RRs in archaea. This subfamily contains Vibrio cholerae CheY3, Escherichia coli CheY, and similar CheY family RRs. CheY proteins control bacterial motility and participate in signaling phosphorelays and in protein-protein interactions. CheY RRs contain only the REC domain with no 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 446686515   6 LKFLVVDDFSTMRRIVRNLLKELGFNNVEEAEDGVDALNKLQAGGFGFIISDWNMPNMDGLELLKTIRADSAMSALPVLM 85
Cdd:cd19923    1 MKVLVVDDFSTMRRIIKNLLKELGFNNVEEAEDGVDALEKLKAGGFDFVITDWNMPNMDGLELLKTIRADGALSHLPVLM 80

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 446686515  86 VTAEAKKENIIAAAQAGASGYVVKPFTAATLEEKLNKIF 124
Cdd:cd19923   81 VTAEAKKENVIAAAQAGVNNYIVKPFTAATLKEKLEKIF 119

Response regulator receiver domain; This domain receives the signal from the sensor partner in bacterial two-component systems. It is usually found N-terminal to a DNA binding effector domain.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446686515    9 LVVDDFSTMRRIVRNLLKELGFNnVEEAEDGVDALNKLQAGGFGFIISDWNMPNMDGLELLKTIRADSamSALPVLMVTA 88
Cdd:pfam00072   2 LIVDDDPLIRELLRQLLEKEGYV-VAEADDGKEALELLKEERPDLILLDINMPGMDGLELLKRIRRRD--PTTPVIILTA 78

                          90       100       110
                  ....*....|....*....|....*....|...
gi 446686515   89 EAKKENIIAAAQAGASGYVVKPFTAATLEEKLN 121
Cdd:pfam00072  79 HGDEDDAVEALEAGADDFLSKPFDPDELLAAIR 111

phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY3 and similar CheY family proteins; CheY family chemotaxis response regulators (RRs) comprise about 17% of bacterial RRs and almost half of all RRs in archaea. This subfamily contains Vibrio cholerae CheY3, Escherichia coli CheY, and similar CheY family RRs. CheY proteins control bacterial motility and participate in signaling phosphorelays and in protein-protein interactions. CheY RRs contain only the REC domain with no 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 446686515   6 LKFLVVDDFSTMRRIVRNLLKELGFNNVEEAEDGVDALNKLQAGGFGFIISDWNMPNMDGLELLKTIRADSAMSALPVLM 85
Cdd:cd19923    1 MKVLVVDDFSTMRRIIKNLLKELGFNNVEEAEDGVDALEKLKAGGFDFVITDWNMPNMDGLELLKTIRADGALSHLPVLM 80

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 446686515  86 VTAEAKKENIIAAAQAGASGYVVKPFTAATLEEKLNKIF 124
Cdd:cd19923   81 VTAEAKKENVIAAAQAGVNNYIVKPFTAATLKEKLEKIF 119

Two-component response regulator, PleD family, consists of two REC domains and a diguanylate cyclase (GGDEF) domain [Signal transduction mechanisms, Transcription];

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446686515   9 LVVDDFSTMRRIVRNLLKELGFNnVEEAEDGVDALNKLQAGGFGFIISDWNMPNMDGLELLKTIRADSAMSALPVLMVTA 88
Cdd:COG3706    5 LVVDDDPTNRKLLRRLLEAAGYE-VVEAADGEEALELLQEHRPDLILLDLEMPDMDGLELCRRLRADPRTADIPIIFLTA 83

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 446686515  89 EAKKENIIAAAQAGASGYVVKPFTAATLEEKLNKIF 124
Cdd:COG3706   84 LDDEEDRARALEAGADDYLTKPFDPEELLARVDLVA 119

DNA-binding response regulator, OmpR family, contains REC and winged-helix (wHTH) domain [Signal transduction mechanisms, Transcription];

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446686515   6 LKFLVVDDFSTMRRIVRNLLKELGFNnVEEAEDGVDALNKLQAGGFGFIISDWNMPNMDGLELLKTIRADSamSALPVLM 85
Cdd:COG0745    2 PRILVVEDDPDIRELLADALEREGYE-VDTAADGEEALELLEEERPDLILLDLMLPGMDGLEVCRRLRARP--SDIPIIM 78

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 446686515  86 VTAEAKKENIIAAAQAGASGYVVKPFTAATLEEKLNKI 123
Cdd:COG0745   79 LTARDDEEDRVRGLEAGADDYLTKPFDPEELLARIRAL 116

DNA-binding transcriptional response regulator, NtrC family, contains REC, AAA-type ATPase, and a Fis-type DNA-binding domains [Signal transduction mechanisms];

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446686515   9 LVVDDFSTMRRIVRNLLKELGFNnVEEAEDGVDALNKLQAGGFGFIISDWNMPNMDGLELLKTIRADSamSALPVLMVTA 88
Cdd:COG2204    6 LVVDDDPDIRRLLKELLERAGYE-VETAASGEEALALLREEPPDLVLLDLRMPGMDGLELLRELRALD--PDLPVILLTG 82

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 446686515  89 EAKKENIIAAAQAGASGYVVKPFTAATLEEKLNKIFEK 126
Cdd:COG2204   83 YGDVETAVEAIKAGAFDYLTKPFDLEELLAAVERALER 120

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        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446686515   9 LVVDDFSTMRRIVRNLLKELGFNnVEEAEDGVDALNKLQAGGFGFIISDWNMPNMDGLELLKTIRADSamSALPVLMVTA 88
Cdd:cd00156    1 LIVDDDPAIRELLKSLLEREGYE-VDTAADGEEALELLREERPDLVLLDLMMPGMDGLELLRKLRELP--PDIPVIVLTA 77

                         90       100
                 ....*....|....*....|..
gi 446686515  89 EAKKENIIAAAQAGASGYVVKP 110
Cdd:cd00156   78 KADEEDAVRALELGADDYLVKP 99

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 446686515   8 FLVVDDFSTMRRIVRNLLKELGFNnVEEAEDGVDALNKLQAGGFGFIISDWNMPNMDGLELLKTIRAD-SAMSALPVLMV 86
Cdd:cd17546    1 VLVVDDNPVNRKVLKKLLEKLGYE-VDVAENGQEALELLKEEPFDLVLMDLQMPVMDGLEATRRIRELeGGGRRTPIIAL 79

                         90       100       110
                 ....*....|....*....|....*....|....
gi 446686515  87 TAEAKKENIIAAAQAGASGYVVKPFTAATLEEKL 120
Cdd:cd17546   80 TANALEEDREKCLEAGMDDYLSKPVKLDQLKEVL 113

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        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446686515   9 LVVDDFSTMRRIVRNLLKELGFNnVEEAEDGVDALNKLQAGGFGFIISDWNMPNMDGLELLKTIRADSamSALPVLMVTA 88
Cdd:cd17574    1 LVVEDDEEIAELLSDYLEKEGYE-VDTAADGEEALELAREEQPDLIILDVMLPGMDGFEVCRRLREKG--SDIPIIMLTA 77

                         90       100
                 ....*....|....*....|..
gi 446686515  89 EAKKENIIAAAQAGASGYVVKP 110
Cdd:cd17574   78 KDEEEDKVLGLELGADDYITKP 99

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 446686515   7 KFLVVDDFSTMRRIVRNLLKELGFNNVEEAEDGVDALNKLQAGGFGFIISDWNMPNMDGLELLKTIRADSAMSAlpVLMV 86
Cdd:cd17542    2 KVLIVDDAAFMRMMLKDILTKAGYEVVGEAANGEEAVEKYKELKPDLVTMDITMPEMDGIEALKEIKKIDPNAK--VIMC 79

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 446686515  87 TAEAKKENIIAAAQAGASGYVVKPFTAATLEEKLNKIF 124
Cdd:cd17542   80 SAMGQEEMVKEAIKAGAKDFIVKPFQPERVLEAVEKVL 117

phosphoacceptor receiver (REC) domain of chemotaxis protein CheV and similar proteins; This subfamily includes the REC domains of Bacillus subtilis chemotaxis protein CheV, Myxococcus xanthus gliding motility regulatory protein FrzE, and similar proteins. CheV is a hybrid protein with an N-terminal CheW-like domain and a C-terminal CheY-like REC domain. The CheV pathway is one of three systems employed by B. subtilis for sensory adaptation that contribute to chemotaxis. It is involved in the transmission of sensory signals from chemoreceptors to flagellar motors. Together with CheW, it is involved in the coupling of methyl-accepting chemoreceptors to the central two-component histidine kinase CheA. FrzE is a hybrid sensor histidine kinase/response regulator that is part of the Frz pathway that controls cell reversal frequency to support directional motility during swarming and fruiting body formation. 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 446686515   9 LVVDDFSTMRRIVRNLLKELGFNnVEEAEDGVDALNKLQAGG---------FGFIISDWNMPNMDGLELLKTIRADSAMS 79
Cdd:cd19924    2 LVVDDSPTARKQLRDLLKNLGFE-IAEAVDGEEALNKLENLAkegndlskeLDLIITDIEMPKMDGYELTFELRDDPRLA 80

                         90       100       110
                 ....*....|....*....|....*....|.
gi 446686515  80 ALPVLMVTAEAKKENIIAAAQAGASGYVVKP 110
Cdd:cd19924   81 NIPVILNSSLSGEFSRARGKKVGADAYLAKF 111

phosphoacceptor receiver (REC) domain of PhoB response regulator from the OmpR family; The transcription factor PhoB is a component of the PhoR/PhoB two-component system, a key regulatory protein network that facilitates response to inorganic phosphate (Pi) starvation conditions by turning on the phosphate (pho) regulon whose products are involved in phosphorus uptake and metabolism. PhoB is a member of the OmpR family of DNA-binding response regulators that contains REC and winged helix-turn-helix (wHTH) DNA-binding output 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        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446686515   7 KFLVVDDFSTMRRIVRNLLKELGFNnVEEAEDGVDALNKLQAGGFGFIISDWNMPNMDGLELLKTIRADSAMSALPVLMV 86
Cdd:cd17618    2 TILIVEDEPAIREMIAFNLERAGFD-VVEAEDAESAVNLIVEPRPDLILLDWMLPGGSGIQFIRRLKRDEMTRDIPIIML 80

                         90       100       110
                 ....*....|....*....|....*....|
gi 446686515  87 TAEAKKENIIAAAQAGASGYVVKPFTAATL 116
Cdd:cd17618   81 TARGEEEDKVRGLEAGADDYITKPFSPREL 110

second phosphoacceptor receiver (REC) domain of uncharacterized GGDEF domain proteins; This family is composed of uncharacterized PleD-like response regulators that contain two N-terminal REC domains and a C-terminal diguanylate cyclase output domain with the characteristic GGDEF motif at the active site. Unlike PleD which contains a REC-like adaptor domain, the second REC domain of these uncharacterized GGDEF domain proteins, described in this model, contains characteristic metal-binding and active site residues. PleD response regulators are global regulators of cell metabolism in some important human pathogens. 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 446686515   7 KFLVVDDFSTMRRIVRNLLKELGFNnVEEAEDGVDALNKLQA-GGFGFIISDWNMPNMDGLELLKTIRADSAMSALPVLM 85
Cdd:cd17544    2 KVLVVDDSATSRNHLRALLRRHNFQ-VLEAANGQEALEVLEQhPDIKLVITDYNMPEMDGFELVREIRKKYSRDQLAIIG 80

                         90       100
                 ....*....|....*....|....*...
gi 446686515  86 VTAEAKkeNIIAAA--QAGASGYVVKPF 111
Cdd:cd17544   81 ISASGD--NALSARfiKAGANDFLTKPF 106

phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase PA4781 and similar domains; Pseudomonas aeruginosa cyclic di-GMP phosphodiesterase PA4781 contains an N-terminal REC domain and a C-terminal catalytic HD-GYP domain, characteristics of RpfG family response regulators. PA4781 is involved in cyclic di-3',5'-GMP (c-di-GMP) hydrolysis/degradation in a two-step reaction via the linear intermediate pGpG to produce GMP. Its unphosphorylated REC domain prevents accessibility of c-di-GMP to the active site. 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 446686515   9 LVVDDFSTMRRIVRNLLKELGFNnVEEAEDGVDALNKLQAGGFGFIISDWNMPNMDGLELLKTIRADSAMSALPVLMVTA 88
Cdd:cd19920    2 LIVDDVPDNLRLLSELLRAAGYR-VLVATDGQQALQRAQAEPPDLILLDVMMPGMDGFEVCRRLKADPATRHIPVIFLTA 80

                         90       100
                 ....*....|....*....|...
gi 446686515  89 EAKKENIIAAAQAGASGYVVKPF 111
Cdd:cd19920   81 LTDTEDKVKGFELGAVDYITKPF 103

second phosphoacceptor receiver (REC) domain of Dictyostelium discoideum hybrid signal transduction histidine kinase D and similar domains; Dictyostelium discoideum hybrid signal transduction histidine kinase D (DhkD) is a large protein that contains two histidine kinase (HK) and two REC domains on the intracellular side of a single pass transmembrane domain, and extracellular PAS and PAC domains that likely are involved in ligand binding. This model represents the second REC domain and similar domains. DhkD activates the cAMP phosphodiesterase RegA to ensure proper prestalk and prespore patterning, tip formation, and the vertical elongation of the mound into a finger, in Dictyostelium discoideum. 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 446686515   9 LVVDDFSTMRRIVRNLLKELGFNnVEEAEDGVDALNKLQAGGFGFIISDWNMPNMDGLELLKTIRADSAMSALPVLMVTA 88
Cdd:cd17580    2 LVVDDNEDAAEMLALLLELEGAE-VTTAHSGEEALEAAQRFRPDVILSDIGMPGMDGYELARRLRELPWLANTPAIALTG 80

                         90       100       110
                 ....*....|....*....|....*....|..
gi 446686515  89 EAKKENIIAAAQAGASGYVVKPFTAATLEEKL 120
Cdd:cd17580   81 YGQPEDRERALEAGFDAHLVKPVDPDELIELI 112

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 446686515   9 LVVDDFSTMRRIVRNLL--KELGFNNVEEAEDGVDALNKLQAGGFGFIISDWNMPNMDGLELLKTIRADSamSALPVLMV 86
Cdd:cd17536    2 LIVDDEPLIREGLKKLIdwEELGFEVVGEAENGEEALELIEEHKPDIVITDIRMPGMDGLELIEKIRELY--PDIKIIIL 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 446686515  87 TAEAKKENIIAAAQAGASGYVVKPFTAATLEEKLNKIFEKL 127
Cdd:cd17536   80 SGYDDFEYAQKAIRLGVVDYLLKPVDEEELEEALEKAKEEL 120

phosphoacceptor receiver (REC) domain of PmrA-like OmpR family response regulators; This subfamily contains various OmpR family response regulators including PmrA, BasR, QseB, tctD, and RssB, which are components of two-component regulatory systems (TCSs). The PmrA/PmrB TCS controls transcription of genes that are involved in lipopolysaccharide modification in the outer membrane of bacteria, increasing bacterial resistance to host-derived antimicrobial peptides. The BasS/BasR TCS functions as an iron- and zinc-sensing transcription regulator. The QseB/QseC TCS activates the flagella regulon by activating transcription of FlhDC. The RssA/RssB TCS regulates swarming behavior in Serratia marcescens. OmpR family DNA-binding response regulators 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        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446686515   8 FLVVDDFSTMRRIVRNLLKELGFNnVEEAEDGVDALNKLQAGGFGFIISDWNMPNMDGLELLKTIRADSamSALPVLMVT 87
Cdd:cd17624    1 ILLVEDDALLGDGLKTGLRKAGYA-VDWVRTGAEAEAALASGPYDLVILDLGLPDGDGLDLLRRWRRQG--QSLPVLILT 77

                         90       100
                 ....*....|....*....|....
gi 446686515  88 AEAKKENIIAAAQAGASGYVVKPF 111
Cdd:cd17624   78 ARDGVDDRVAGLDAGADDYLVKPF 101

Ycf27; Reviewed

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446686515   7 KFLVVDDFSTMRRIVRNLLKELGFNnVEEAEDGVDALNKLQAGGFGFIISDWNMPNMDGLELLKTIRADSAmsaLPVLMV 86
Cdd:CHL00148   8 KILVVDDEAYIRKILETRLSIIGYE-VITASDGEEALKLFRKEQPDLVILDVMMPKLDGYGVCQEIRKESD---VPIIML 83

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 446686515  87 TAEAKKENIIAAAQAGASGYVVKPFTAATLEEKLNKIFEK 126
Cdd:CHL00148  84 TALGDVSDRITGLELGADDYVVKPFSPKELEARIRSVLRR 123

first (D1) phosphoacceptor receiver (REC) domain of response regulator PleD and similar domains; PleD contains a REC domain (D1) with the phosphorylatable aspartate, a REC-like adaptor domain (D2), and the enzymatic diguanylate cyclase (DGC) domain, also called the GGDEF domain according to a conserved sequence motif, as its output domain. The GGDEF-containing PleD response regulators are global regulators of cell metabolism in some important human pathogens. This model describes D1 of PleD and similar 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        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446686515   7 KFLVVDDFSTMRRIVRNLLKELGFNnVEEAEDGVDALNKLQAGGFGFIISDWNMPNMDGLELLKTIRADSAMSALPVLMV 86
Cdd:cd17538    1 KILVVDDEPANRELLEALLSAEGYE-VLTADSGQEALALAEEELPDLILLDVMMPGMDGFEVCRRLKEDPETRHIPVIMI 79

                         90       100
                 ....*....|....*....|....*
gi 446686515  87 TAEAKKENIIAAAQAGASGYVVKPF 111
Cdd:cd17538   80 TALDDREDRIRGLEAGADDFLSKPI 104

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 446686515   9 LVVDDFSTMRRIVR-NLLKElGFNnVEEAEDGVDALNKLQAGGFGFIISDWNMPNMDGLELLKTIRADSAMSALPVLMVT 87
Cdd:cd19937    1 LVVDDEEDIVELLKyNLEKE-GYE-VVTAYDGEEALKRAKDEKPDLIILDLMLPGIDGLEVCRILRSDPKTSSIPIIMLT 78

                         90       100
                 ....*....|....*....|....*
gi 446686515  88 AEAKKENIIAAAQAGASGYVVKPFT 112
Cdd:cd19937   79 AKGEEFDKVLGLELGADDYITKPFS 103

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        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446686515   7 KFLVVDDFSTMRRIVRNLLKELGFNnVEEAEDGVDALNKLQAGGFGFIISDWNMPNMDGLELLKTIRADSamSALPVLMV 86
Cdd:cd17554    2 KILVVDDEENIRELYKEELEDEGYE-VVTAGNGEEALEKLESEDPDLVILDIKMPGMDGLETLRKIREKK--PDLPVIIC 78

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 446686515  87 TA--EAKKENIIAAAQAgasgYVVKPFTAATLEEKLNKI 123
Cdd:cd17554   79 TAysEYKSDFSSWAADA----YVVKSSDLTELKETIKRL 113

phosphoacceptor receiver (REC) domain of chemotaxis response regulator protein-glutamate methylesterase CheB and similar chemotaxis proteins; Methylesterase CheB is a chemotaxis response regulator with an N-terminal REC domain and a C-terminal methylesterase domain. Chemotaxis is a behavior known in motile bacteria that directs their movement in response to chemical gradients. CheB is a phosphorylation-activated response regulator involved in the reversible modification of bacterial chemotaxis receptors. It catalyzes the demethylation of specific methylglutamate residues introduced into the chemoreceptors (methyl-accepting chemotaxis proteins) by CheR. The CheB REC domain packs against the active site of the C-terminal domain and inhibits methylesterase activity by directly restricting access to the active site. Also included in this family is chemotaxis response regulator CheY, which contains a stand-alone REC domain, and an uncharacterized subfamily composed of proteins containing an N-terminal REC domain and a C-terminal CheY-P phosphatase (CheC) 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 446686515   9 LVVDDFSTMRRIVRNLLKEL-GFNNVEEAEDGVDALNKLQAGGFGFIISDWNMPNMDGLELLKTIRADSAMsalPVLMVT 87
Cdd:cd17541    4 LIVDDSAVMRKLLSRILESDpDIEVVGTARDGEEALEKIKELKPDVITLDIEMPVMDGLEALRRIMAERPT---PVVMVS 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 446686515  88 AEAKK--ENIIAAAQAGASGYVVKPftAATLEEKLNKIFEKL 127
Cdd:cd17541   81 SLTEEgaEITLEALELGAVDFIAKP--SGGISLDLEEIAEEL 120

sigma-54-dependent response regulator transcription factor ZraR;

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446686515   1 MADKELKFLVVDDFSTMRRIVRNLLKELGFNnVEEAEDGVDALNKLQAGGFGFIISDWNMPNMDGLELLKTIRADSAmsA 80
Cdd:PRK10365   1 MTHDNIDILVVDDDISHCTILQALLRGWGYN-VALANSGRQALEQVREQVFDLVLCDVRMAEMDGIATLKEIKALNP--A 77

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 446686515  81 LPVLMVTAEAKKENIIAAAQAGASGYVVKPFTAATLEEKLNK 122
Cdd:PRK10365  78 IPVLIMTAYSSVETAVEALKTGALDYLIKPLDFDNLQATLEK 119

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 446686515   9 LVVDDFSTMRRIVRNLLKELGFNnVEEAEDGVDALNKL--QAGGFGFIISDWNMPNMDGLELLKTIRadSAMSaLPVLMV 86
Cdd:cd17584    2 LVVDDDPTCLAILKRMLLRCGYQ-VTTCTDAEEALSMLreNKDEFDLVITDVHMPDMDGFEFLELIR--LEMD-LPVIMM 77

                         90       100       110
                 ....*....|....*....|....*....|
gi 446686515  87 TAEAKKENIIAAAQAGASGYVVKPFTAATL 116
Cdd:cd17584   78 SADGSTSTVMKGLAHGACDYLLKPVSIEDL 107

phosphoacceptor receiver (REC) domain of Pseudomonas aeruginosa RssB and similar domains; Pseudomonas aeruginosa RssB is an orphan atypical response regulator containing a REC domain and a PP2C-type protein phosphatase output domain. Its function is still unknown. Escherichia RssB, which is not included in this subfamily, is a ClpX adaptor protein which alters ClpX specificity by mediating a specific interaction between ClpX and the substrates such as RpoS, an RNA polymerase sigma factor. 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 446686515   7 KFLVVDDFSTMRRIVRNLLKELGFNnVEEAEDGVDALNKLQAGGFGFIISDWNMPNMDGLELLKTIRADSamSALPVLMV 86
Cdd:cd17555    2 TILVIDDDEVVRESIAAYLEDSGFQ-VLQAADGRQGLELFRSEQPDLVLCDLRMPEMDGLEVLKQITKES--PDTPVIVV 78

                         90       100
                 ....*....|....*....|....
gi 446686515  87 TAEAKKENIIAAAQAGASGYVVKP 110
Cdd:cd17555   79 SGAGVMSDAVEALRLGAWDYLTKP 102

phosphoacceptor receiver (REC) domain of EcPhoP-like OmpR family response regulators; Escherichia coli PhoP (EcPhoP) is part of the PhoQ/PhoP two-component system (TCS) that regulates virulence genes and plays an essential role in the response of the bacteria to the environment of their mammalian hosts, sensing several stimuli such as extracellular magnesium limitation, low pH, the presence of cationic antimicrobial peptides, and osmotic upshift. This subfamily also includes Brucella suis FeuP, part of the FeuPQ TCS that is involved in the regulation of iron uptake, and Microchaete diplosiphon RcaC, which is required for chromatic adaptation. 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        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446686515   9 LVVDDFSTMRRIVRNLLKELGFNnVEEAEDGVDALNKLQAGGFGFIISDWNMPNMDGLELLKTIRADSAmsALPVLMVTA 88
Cdd:cd19934    2 LLVEDDALLAAQLKEQLSDAGYV-VDVAEDGEEALFQGEEEPYDLVVLDLGLPGMDGLSVLRRWRSEGR--ATPVLILTA 78

                         90       100       110
                 ....*....|....*....|....*....|...
gi 446686515  89 EAKKENIIAAAQAGASGYVVKPFTAATLEEKLN 121
Cdd:cd19934   79 RDSWQDKVEGLDAGADDYLTKPFHIEELLARLR 111

acid-sensing system histidine kinase EvgS;

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446686515    4 KELKFLVVDDFSTMRRIVRNLLKELGFNnVEEAEDGVDALNKLQAGGFGFIISDWNMPNMDGLELLKTIRADSamSALPV 83
Cdd:PRK09959  957 EKLSILIADDHPTNRLLLKRQLNLLGYD-VDEATDGVQALHKVSMQHYDLLITDVNMPNMDGFELTRKLREQN--SSLPI 1033

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 446686515   84 LMVTAEAKKENIIAAAQAGASGYVVKPFTAATLEEKLNKIFE 125
Cdd:PRK09959 1034 WGLTANAQANEREKGLSCGMNLCLFKPLTLDVLKTHLSQLHQ 1075