phosphoacceptor receiver (REC) domain of cyanobacterial phytochrome response regulator Rcp and similar domains; This family is composed of response regulators (RRs) that are members of phytochrome-associated, light-sensing two-component signal transduction pathways such as Synechocystis sp. Rcp1, Tolypothrix sp. RcpA, and Agrobacterium tumefaciens bacteriophytochrome response regulator AtBRR. They are stand-alone RRs containing only a REC domain with no output/effector domain. The REC domain itself functions as an effector domain. Also included in this family us Methanosaeta harundinacea methanogenesis regulatory protein FilR2, also a stand-alone RR. 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 924872125   9 TILMADDDADDRLMAREALEEAGLNNVLKFVEDGEELLDYLRQSGAYADkysAPRPGLILLDLNMPRMDGREALREIKAD 88
Cdd:cd17557    1 TILLVEDNPGDAELIQEAFKEAGVPNELHVVRDGEEALDFLRGEGEYAD---APRPDLILLDLNMPRMDGFEVLREIKAD 77

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 924872125  89 PELRRIPVVVLTTSKAEEDILRTYDLGVNSFITKPVTFEGLVEVMKQLAHYW 140
Cdd:cd17557   78 PDLRRIPVVVLTTSDAEEDIERAYELGANSYIVKPVDFEEFVEAIRSLGEYW 129

phosphoacceptor receiver (REC) domain of cyanobacterial phytochrome response regulator Rcp and similar domains; This family is composed of response regulators (RRs) that are members of phytochrome-associated, light-sensing two-component signal transduction pathways such as Synechocystis sp. Rcp1, Tolypothrix sp. RcpA, and Agrobacterium tumefaciens bacteriophytochrome response regulator AtBRR. They are stand-alone RRs containing only a REC domain with no output/effector domain. The REC domain itself functions as an effector domain. Also included in this family us Methanosaeta harundinacea methanogenesis regulatory protein FilR2, also a stand-alone RR. 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 924872125   9 TILMADDDADDRLMAREALEEAGLNNVLKFVEDGEELLDYLRQSGAYADkysAPRPGLILLDLNMPRMDGREALREIKAD 88
Cdd:cd17557    1 TILLVEDNPGDAELIQEAFKEAGVPNELHVVRDGEEALDFLRGEGEYAD---APRPDLILLDLNMPRMDGFEVLREIKAD 77

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 924872125  89 PELRRIPVVVLTTSKAEEDILRTYDLGVNSFITKPVTFEGLVEVMKQLAHYW 140
Cdd:cd17557   78 PDLRRIPVVVLTTSDAEEDIERAYELGANSYIVKPVDFEEFVEAIRSLGEYW 129

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 924872125   10 ILMADDDADDRLMAREALEEAGLnnVLKFVEDGEELLDYLRQSgayadkysapRPGLILLDLNMPRMDGREALREIKADP 89
Cdd:pfam00072   1 VLIVDDDPLIRELLRQLLEKEGY--VVAEADDGKEALELLKEE----------RPDLILLDINMPGMDGLELLKRIRRRD 68

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 924872125   90 elRRIPVVVLTTSKAEEDILRTYDLGVNSFITKPVTFEGLVE 131
Cdd:pfam00072  69 --PTTPVIILTAHGDEDDAVEALEAGADDFLSKPFDPDELLA 108

cheY-homologous receiver domain; CheY regulates the clockwise rotation of E. coli flagellar motors. This domain contains a phosphoacceptor site that is phosphorylated by histidine kinase homologues.

                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 924872125     8 ITILMADDDADDRLMAREALEEAGLnnVLKFVEDGEELLDYLRQSgayadkysapRPGLILLDLNMP 74
Cdd:smart00448   1 MRILVVDDDPLLRELLKALLEKEGY--EVDEATDGEEALELLKEE----------KPDLILLDIMMP 55

phosphoacceptor receiver (REC) domain of cyanobacterial phytochrome response regulator Rcp and similar domains; This family is composed of response regulators (RRs) that are members of phytochrome-associated, light-sensing two-component signal transduction pathways such as Synechocystis sp. Rcp1, Tolypothrix sp. RcpA, and Agrobacterium tumefaciens bacteriophytochrome response regulator AtBRR. They are stand-alone RRs containing only a REC domain with no output/effector domain. The REC domain itself functions as an effector domain. Also included in this family us Methanosaeta harundinacea methanogenesis regulatory protein FilR2, also a stand-alone RR. 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 924872125   9 TILMADDDADDRLMAREALEEAGLNNVLKFVEDGEELLDYLRQSGAYADkysAPRPGLILLDLNMPRMDGREALREIKAD 88
Cdd:cd17557    1 TILLVEDNPGDAELIQEAFKEAGVPNELHVVRDGEEALDFLRGEGEYAD---APRPDLILLDLNMPRMDGFEVLREIKAD 77

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 924872125  89 PELRRIPVVVLTTSKAEEDILRTYDLGVNSFITKPVTFEGLVEVMKQLAHYW 140
Cdd:cd17557   78 PDLRRIPVVVLTTSDAEEDIERAYELGANSYIVKPVDFEEFVEAIRSLGEYW 129

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 924872125   7 SITILMADDDADDRLMAREALEEAGLNnvLKFVEDGEELLDYLRQSgayadkysapRPGLILLDLNMPRMDGREALREIK 86
Cdd:COG3706    1 PARILVVDDDPTNRKLLRRLLEAAGYE--VVEAADGEEALELLQEH----------RPDLILLDLEMPDMDGLELCRRLR 68

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 924872125  87 ADPELRRIPVVVLTTSKAEEDILRTYDLGVNSFITKPVTFEGLVEVMKQLAHY 139
Cdd:COG3706   69 ADPRTADIPIIFLTALDDEEDRARALEAGADDYLTKPFDPEELLARVDLVARY 121

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 924872125   9 TILMADDDADDRLMAREALEEAGLNnvLKFVEDGEELLDYLRQSgayadkysapRPGLILLDLNMPRMDGREALREIKAD 88
Cdd:COG0745    3 RILVVEDDPDIRELLADALEREGYE--VDTAADGEEALELLEEE----------RPDLILLDLMLPGMDGLEVCRRLRAR 70

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 924872125  89 PelRRIPVVVLTTSKAEEDILRTYDLGVNSFITKPVTFEGLVEVMKQLA 137
Cdd:COG0745   71 P--SDIPIIMLTARDDEEDRVRGLEAGADDYLTKPFDPEELLARIRALL 117

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 924872125  10 ILMADDDADDRLMAREALEEAGLNNVLkfVEDGEELLDYLRQsgayadkysaPRPGLILLDLNMPRMDGREALREIKADP 89
Cdd:cd17546    1 VLVVDDNPVNRKVLKKLLEKLGYEVDV--AENGQEALELLKE----------EPFDLVLMDLQMPVMDGLEATRRIRELE 68

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 924872125  90 E-LRRIPVVVLTTSKAEEDILRTYDLGVNSFITKPVTFEGLVEVM 133
Cdd:cd17546   69 GgGRRTPIIALTANALEEDREKCLEAGMDDYLSKPVKLDQLKEVL 113

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 924872125   6 RSITILMADDDADDRLMAREALEEAGLNnvLKFVEDGEELLDYLRQSgayadkysapRPGLILLDLNMPRMDGREALREI 85
Cdd:COG2204    1 SMARILVVDDDPDIRRLLKELLERAGYE--VETAASGEEALALLREE----------PPDLVLLDLRMPGMDGLELLREL 68

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 924872125  86 KADPelRRIPVVVLTTSKAEEDILRTYDLGVNSFITKPVTFEGLVEVMKQLAHY 139
Cdd:COG2204   69 RALD--PDLPVILLTGYGDVETAVEAIKAGAFDYLTKPFDLEELLAAVERALER 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 924872125  11 LMADDDADDRLMAREALEEAGLNnvLKFVEDGEELLDYLRQsgayadkysaPRPGLILLDLNMPRMDGREALREIKADPe 90
Cdd:cd00156    1 LIVDDDPAIRELLKSLLEREGYE--VDTAADGEEALELLRE----------ERPDLVLLDLMMPGMDGLELLRKLRELP- 67

                         90       100       110
                 ....*....|....*....|....*....|...
gi 924872125  91 lRRIPVVVLTTSKAEEDILRTYDLGVNSFITKP 123
Cdd:cd00156   68 -PDIPVIVLTAKADEEDAVRALELGADDYLVKP 99

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 924872125   9 TILMADDDADDRLMAREALEEAGLNNVlkFVEDGEELLDYLRQSgayadkysapRPGLILLDLNMPRMDGREALREIKAD 88
Cdd:cd17538    1 KILVVDDEPANRELLEALLSAEGYEVL--TADSGQEALALAEEE----------LPDLILLDVMMPGMDGFEVCRRLKED 68

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 924872125  89 PELRRIPVVVLTTSKAEEDILRTYDLGVNSFITKPV 124
Cdd:cd17538   69 PETRHIPVIMITALDDREDRIRGLEAGADDFLSKPI 104

phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY4 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 CheY4 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 924872125   9 TILMADDDADDRLMAREALEEAGLNNVLkfVEDGEELLDylrqsgayadKYSAPRPGLILLDLNMPRMDGREALREIKAD 88
Cdd:cd17562    2 KILAVDDSASIRQMVSFTLRGAGYEVVE--AADGRDALS----------KAQSKKFDLIITDQNMPNMDGIELIKELRKL 69

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 924872125  89 PELRRIPVVVLTTSKAEEDILRTYDLGVNSFITKPVTFEGLVEVMKQL 136
Cdd:cd17562   70 PAYKFTPILMLTTESSDEKKQEGKAAGATGWLVKPFDPEQLLEVVKKV 117

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 924872125  11 LMADDDADDRLMAREALEEAGLNnvLKFVEDGEELLDYLRQsgayadkysaPRPGLILLDLNMPRMDGREALREIKADPe 90
Cdd:cd17574    1 LVVEDDEEIAELLSDYLEKEGYE--VDTAADGEEALELARE----------EQPDLIILDVMLPGMDGFEVCRRLREKG- 67

                         90       100       110
                 ....*....|....*....|....*....|...
gi 924872125  91 lRRIPVVVLTTSKAEEDILRTYDLGVNSFITKP 123
Cdd:cd17574   68 -SDIPIIMLTAKDEEEDKVLGLELGADDYITKP 99

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        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924872125   9 TILMADDDADDRLMAREALEEAGLNNVLKFVEDGEELLDYLRQSgayadkysapRPGLILLDLNMPRMDGREALREIKAd 88
Cdd:COG4753    1 KVLIVDDEPLIREGLKRILEWEAGFEVVGEAENGEEALELLEEH----------KPDLVITDINMPGMDGLELLEAIRE- 69

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 924872125  89 pELRRIPVVVLTTSKAEEDILRTYDLGVNSFITKP 123
Cdd:COG4753   70 -LDPDTKIIILSGYSDFEYAQEAIKLGADDYLLKP 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 924872125  10 ILMADDDADDRLMAREALEEAGlnNVLKFVEDGEELLDYLRQSgayadkysapRPGLILLDLNMPRMDGREALREIKADP 89
Cdd:cd17580    1 ILVVDDNEDAAEMLALLLELEG--AEVTTAHSGEEALEAAQRF----------RPDVILSDIGMPGMDGYELARRLRELP 68

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 924872125  90 ELRRIPVVVLTTSKAEEDILRTYDLGVNSFITKPVTFEGLVEV 132
Cdd:cd17580   69 WLANTPAIALTGYGQPEDRERALEAGFDAHLVKPVDPDELIEL 111

phosphoacceptor receiver (REC) domain of NarL (Nitrate/Nitrite response regulator L) family response regulators; The NarL family is one of the more abundant families of DNA-binding response regulators (RRs). Members of the NarL family contain a REC domain and a helix-turn-helix (HTH) DNA-binding output domain, with a majority of members containing a LuxR-type HTH domain. They function as transcriptional regulators. 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 924872125  17 ADDRLMAREALE-----EAGLNNVLKfVEDGEELLDYLRQsgayadkysaPRPGLILLDLNMPRMDGREALREIKAdpEL 91
Cdd:cd17535    4 VDDHPLVREGLRrllesEPDIEVVGE-AADGEEALALLRE----------LRPDVVLMDLSMPGMDGIEALRRLRR--RY 70

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 924872125  92 RRIPVVVLTTSKAEEDILRTYDLGVNSFITKPVTFEGLVEVMKQLA 137
Cdd:cd17535   71 PDLKVIVLTAHDDPEYVLRALKAGAAGYLLKDSSPEELIEAIRAVA 116

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 924872125  10 ILMADDDADDRLMAREALEEAGLNnvLKFVEDGEELLDYLRQSGAYADKYSAPRPgLILLDLNMPRMDGREALREIKADP 89
Cdd:cd19924    1 ILVVDDSPTARKQLRDLLKNLGFE--IAEAVDGEEALNKLENLAKEGNDLSKELD-LIITDIEMPKMDGYELTFELRDDP 77

                         90       100       110
                 ....*....|....*....|....*....|....
gi 924872125  90 ELRRIPVVVLTTSKAEEDILRTYDLGVNSFITKP 123
Cdd:cd19924   78 RLANIPVILNSSLSGEFSRARGKKVGADAYLAKF 111

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 924872125   6 RSITILMADDDADDRLMAREALEEAGLNnVLKFVEDGEELLDYLRqsgayadkysAPRPGLILLDLNMPRMDGREALREI 85
Cdd:COG3707    2 RGLRVLVVDDEPLRRADLREGLREAGYE-VVAEAADGEDAVELVR----------ELKPDLVIVDIDMPDRDGLEAARQI 70

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 924872125  86 KADpelRRIPVVVLTTSKAEEDILRTYDLGVNSFITKPVTFEGLVEVMKQLAHYWFELVQVAR 148
Cdd:COG3707   71 SEE---RPAPVILLTAYSDPELIERALEAGVSAYLVKPLDPEDLLPALELALARFRELRALRR 130

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 924872125   8 ITILMADDDADDRLMAREALEEAGLNNVLKFVEDGEELLDYLRQSgayadkysapRPGLILLDLNMPRMDGREALREIKA 87
Cdd:cd17541    1 IRVLIVDDSAVMRKLLSRILESDPDIEVVGTARDGEEALEKIKEL----------KPDVITLDIEMPVMDGLEALRRIMA 70

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 924872125  88 dpeLRRIPVVVLT--TSKAEEDILRTYDLGVNSFITKPV--TFEGLVEVMKQL 136
Cdd:cd17541   71 ---ERPTPVVMVSslTEEGAEITLEALELGAVDFIAKPSggISLDLEEIAEEL 120

Stage 0 sporulation initiation response regulator Spo0F [Cell cycle control, cell division, chromosome partitioning, Signal transduction mechanisms];

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924872125   9 TILMADDDADDRLMAREALEEAGLNNVLkfVEDGEELLDYLRQSgayadkysapRPGLILLDLNMPRMDGREALREIKA- 87
Cdd:COG5803    4 KILIVDDQAGIRMLLKEVLKKEGYEVFQ--AANGKEALEKVKEL----------KPDLVLLDMKMPGMDGIEILKEIKEi 71

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 924872125  88 DPELRripvVVLTTSKAEEDILRTYD-LGVNSFITKPVTFEGLVEVMKQL 136
Cdd:COG5803   72 DPDIP----VIMMTAYGELDMVEEAKeLGAKGYFTKPFDIDELREAVNKL 117

phosphoacceptor receiver (REC) domain of KdpE-like OmpR family response regulators; KdpE is a component of the KdpD/KdpE two-component system (TCS) and is activated when histidine kinase KdpD senses a drop in external K+ concentration or upshift in ionic osmolarity, resulting in the expression of a heterooligomeric transporter KdpFABC. In addition, the KdpD/KdpE TCS is also an adaptive regulator involved in the virulence and intracellular survival of pathogenic bacteria. KdpE is a member of the OmpR family of DNA-binding response regulators that contain 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 924872125  10 ILMADDDADDRLMAREALEEAGLnnVLKFVEDGEELLDylrqsgayadKYSAPRPGLILLDLNMPRMDGREALREIKadp 89
Cdd:cd17620    1 ILVIEDEPQIRRFLRTALEAHGY--RVFEAETGQEGLL----------EAATRKPDLIILDLGLPDMDGLEVIRRLR--- 65

                         90       100       110
                 ....*....|....*....|....*....|....
gi 924872125  90 ELRRIPVVVLTTSKAEEDILRTYDLGVNSFITKP 123
Cdd:cd17620   66 EWSAVPVIVLSARDEESDKIAALDAGADDYLTKP 99

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 924872125  11 LMADDDADDRLMAREALEEAGlNNVLKFvEDGEELLDYLRQSgayadkysapRPGLILLDLNMPRMDGREALREIKADPE 90
Cdd:cd19937    1 LVVDDEEDIVELLKYNLEKEG-YEVVTA-YDGEEALKRAKDE----------KPDLIILDLMLPGIDGLEVCRILRSDPK 68

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 924872125  91 LRRIPVVVLTTSKAEEDILRTYDLGVNSFITKPVTFEGLVEVMKQL 136
Cdd:cd19937   69 TSSIPIIMLTAKGEEFDKVLGLELGADDYITKPFSPRELLARVKAV 114

phosphoacceptor receiver (REC) domain of C4-dicarboxylic acid transport protein D (DctD) and similar proteins; C4-dicarboxylic acid transport protein D (DctD) is part of the two-component regulatory system DctB/DctD, which regulates C4-dicarboxylate transport via regulation of expression of the dctPQM operon and dctA. It is an activator of sigma(54)-RNA polymerase holoenzyme that uses the energy released from ATP hydrolysis to stimulate the isomerization of a closed promoter complex to an open complex capable of initiating transcription. DctD is a member of the NtrC family, characterized by a domain architecture containing an N-terminal REC domain, followed by a central sigma-54 interaction/ATPase domain, and a C-terminal DNA binding domain. The ability of the central domain to hydrolyze ATP and thus to interact effectively with a complex of RNA polymerase, sigma54, and promoter, is controlled by the phosphorylation status of the REC 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 924872125  10 ILMADDDADDRLMAREALEEAGLNnVLKFvEDGEELLDYLrqsgayadkySAPRPGLILLDLNMPRMDGREALREIKA-D 88
Cdd:cd17549    1 VLLVDDDADVREALQQTLELAGFR-VRAF-ADAEEALAAL----------SPDFPGVVISDIRMPGMDGLELLAQIRElD 68

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 924872125  89 PELrriPVVVLTtskAEEDI------LRtydLGVNSFITKPVTFEGLVEVMKQ 135
Cdd:cd17549   69 PDL---PVILIT---GHGDVpmaveaMR---AGAYDFLEKPFDPERLLDVVRR 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 924872125  10 ILMADDDAddrlMAREAL------EEAGLNNVLKFvEDGEELLDYLRQSgayadkysapRPGLILLDLNMPRMDGREALR 83
Cdd:cd17536    1 VLIVDDEP----LIREGLkklidwEELGFEVVGEA-ENGEEALELIEEH----------KPDIVITDIRMPGMDGLELIE 65

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 924872125  84 EIKAdpELRRIPVVVLTtskaeedilrTYD----------LGVNSFITKPVTFEGLVEVMKQLAHYW 140
Cdd:cd17536   66 KIRE--LYPDIKIIILS----------GYDdfeyaqkairLGVVDYLLKPVDEEELEEALEKAKEEL 120

phosphate response regulator transcription factor PhoB;

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924872125  10 ILMADDDADDRLMAREALEEAGLNNVlkfvedgeELLDYlrqsGAYADKYSAPRPGLILLDLNMPRMDGREALREIKADP 89
Cdd:PRK10161   5 ILVVEDEAPIREMVCFVLEQNGFQPV--------EAEDY----DSAVNQLNEPWPDLILLDWMLPGGSGIQFIKHLKRES 72

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 924872125  90 ELRRIPVVVLTTSKAEEDILRTYDLGVNSFITKPVTFEGLVEVMK 134
Cdd:PRK10161  73 MTRDIPVVMLTARGEEEDRVRGLETGADDYITKPFSPKELVARIK 117

DNA-binding response regulator HprR;

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924872125  10 ILMADDDADDRLMAREALEEAGLnnVLKFVEDGEELLdYLrqsgAYADKYSaprpgLILLDLNMPRMDGREALREIKAdp 89
Cdd:PRK11517   3 ILLIEDNQRTQEWVTQGLSEAGY--VIDAVSDGRDGL-YL----ALKDDYA-----LIILDIMLPGMDGWQILQTLRT-- 68

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 924872125  90 eLRRIPVVVLTTSKAEEDILRTYDLGVNSFITKPVTF-EGLVEVMKQL 136
Cdd:PRK11517  69 -AKQTPVICLTARDSVDDRVRGLDSGANDYLVKPFSFsELLARVRAQL 115

phosphoacceptor receiver (REC) domain of type A Arabidopsis response regulators (ARRs) and similar proteins; Type-A response regulators of Arabidopsis (ARRs) are involved in cytokinin signaling, which involves a phosphorelay cascade by histidine kinase receptors (AHKs), histidine phosphotransfer proteins (AHPs) and downstream ARRs. 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. Type-A ARRs function downstream of and are regulated by type-B ARRs, which are a class of MYB-type transcription factors. As primary cytokinin response genes, type-A ARRs act as redundant negative feedback regulators of cytokinin signaling by inactivating the phosphorelay. ARRs are divided into two groups, type-A and -B, according to their sequence and domain structure. Type-A ARRs are similar in domain structure to CheY, in that they lack a typical output domain and only contain a stand-alone receiver (REC) 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 924872125  39 VEDGEELLDYL-RQSGAYADKYSAPRPGLILLDLNMPRMDGREALREIKADPELRRIPVVVLTTSKAEEDILRTYDLGVN 117
Cdd:cd17581   28 VDSGKRALEFLgLEDEEDSSNFNEPKVNMIITDYCMPGMTGYDLLKKVKESSALKEIPVVIMSSENIPTRISRCLEEGAE 107

                 ....*..
gi 924872125 118 SFITKPV 124
Cdd:cd17581  108 DFLLKPV 114