phosphoacceptor receiver (REC) domain of hybrid sensor histidine kinase/response regulators similar to Pseudomonas savastanoi blue-light-activated histidine kinase; Typically, two-component regulatory systems (TCSs) consist of a sensor (histidine kinase) that responds to specific input(s) by modifying the output of a cognate response regulator (RR). TCSs allow organisms to sense and respond to changes in environmental conditions. Hybrid sensor histidine kinase (HK)/response regulators contain all the elements of a classical TCS in a single polypeptide chain. Pseudomonas savastanoi blue-light-activated histidine kinase is a photosensitive HK and RR that is involved in increased bacterial virulence upon exposure to light. RRs share the common phosphoacceptor REC domain and different effector/output domains such as DNA, RNA, ligand-binding, protein-binding, or enzymatic 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 740793425   8 ILVVEDDAIVRMLIVDVLEELEFKVLEAAGSEEALARLQdSALHIDLMMTDVGLPG-MDGKELAARARALRPELPVLFAS 86
Cdd:cd18161    1 VLVVEDDPDVRRLTAEVLEDLGYTVLEAASGDEALDLLE-SGPDIDLLVTDVIMPGgMNGSQLAEEARRRRPDLKVLLTS 79

                         90       100
                 ....*....|....*....|...
gi 740793425  87 GYAENIEVP----AGMAVIGKPF 105
Cdd:cd18161   80 GYAENAIEGgdlaPGVDVLSKPF 102

histidine kinase; Provisional

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740793425   3 PTDSTILVVEDDAIVRMLIVDVLEELEFKVLEAAGSEEALARLQDSAlHIDLMMTDVGLPG-MDGKELAARARALRPELP 81
Cdd:PRK13557 413 GGTETILIVDDRPDVAELARMILEDFGYRTLVASNGREALEILDSHP-EVDLLFTDLIMPGgMNGVMLAREARRRQPKIK 491

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 740793425  82 VLFASGYAE-NIEV----PAGMAVIGKPFSIDQLRDKVRAIL 118
Cdd:PRK13557 492 VLLTTGYAEaSIERtdagGSEFDILNKPYRRAELARRVRMVL 533

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 740793425   7 TILVVEDDAIVRMLIVDVLEELEFKVLEAAGSEEALARLQDSalHIDLMMTDVGLPGMDGKELAARARALRPELPVLFAS 86
Cdd:COG2204    4 RILVVDDDPDIRRLLKELLERAGYEVETAASGEEALALLREE--PPDLVLLDLRMPGMDGLELLRELRALDPDLPVILLT 81

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 740793425  87 GYAENIEVPAGM-----AVIGKPFSIDQLRDKVRAIL 118
Cdd:COG2204   82 GYGDVETAVEAIkagafDYLTKPFDLEELLAAVERAL 118

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 740793425   7 TILVVEDDAIVRMLIVDVLEELEFKVLEAAGSEEALARLQDSalHIDLMMTDVGLPGMDGKELAARARALRPELPVLFAS 86
Cdd:COG0745    3 RILVVEDDPDIRELLADALEREGYEVDTAADGEEALELLEEE--RPDLILLDLMLPGMDGLEVCRRLRARPSDIPIIMLT 80

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 740793425  87 GYAENIEVPAGMA-----VIGKPFSIDQLRDKVRAIL 118
Cdd:COG0745   81 ARDDEEDRVRGLEagaddYLTKPFDPEELLARIRALL 117

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 740793425    8 ILVVEDDAIVRMLIVDVLEELEFKVLEAAGSEEALARLQdsALHIDLMMTDVGLPGMDGKELAARARALRPELPVLFASG 87
Cdd:pfam00072   1 VLIVDDDPLIRELLRQLLEKEGYVVAEADDGKEALELLK--EERPDLILLDINMPGMDGLELLKRIRRRDPTTPVIILTA 78

                          90       100       110
                  ....*....|....*....|....*....|...
gi 740793425   88 YAENIEVPAGMAV-----IGKPFSIDQLRDKVR 115
Cdd:pfam00072  79 HGDEDDAVEALEAgaddfLSKPFDPDELLAAIR 111

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        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740793425   7 TILVVEDDAIVRMLIVDVLEELEFKVLEAAGSEEALARLQDSAlHIDLMMTDVGLPGMDGKELAARARALRPELPVLFAS 86
Cdd:cd18160    1 TILLADDEPSVRKFIVTTLKKAGYAVTEAESGAEALEKLQQGK-DIDIVVTDIVMPEMDGIELAREARKIDPDVKILFIS 79

                         90       100
                 ....*....|....*....|....
gi 740793425  87 GYAE-----NIEVPAGMAVIGKPF 105
Cdd:cd18160   80 GGAAaapelLSDAVGDNATLKKPF 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        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740793425   9 LVVEDDAIVRMLIVDVLEELEFKVLEAAGSEEALARLQDSalHIDLMMTDVGLPGMDGKELAARARALRPELPVLFASGY 88
Cdd:cd00156    1 LIVDDDPAIRELLKSLLEREGYEVDTAADGEEALELLREE--RPDLVLLDLMMPGMDGLELLRKLRELPPDIPVIVLTAK 78

                         90
                 ....*....|..
gi 740793425  89 AENIEVPAGMAV 100
Cdd:cd00156   79 ADEEDAVRALEL 90

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 740793425   6 STILVVEDDAIVRMLIVDVLEELEFKVLEAAGSEEALARLQDSalHIDLMMTDVGLPGMDGKELAARARALRPELPVLFA 85
Cdd:cd17554    1 KKILVVDDEENIRELYKEELEDEGYEVVTAGNGEEALEKLESE--DPDLVILDIKMPGMDGLETLRKIREKKPDLPVIIC 78

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 740793425  86 SGYAE---NIEVPAGMAVIGKPFSIDQLRDKVRAI 117
Cdd:cd17554   79 TAYSEyksDFSSWAADAYVVKSSDLTELKETIKRL 113

phosphoacceptor receiver (REC) domain of nitrogen assimilation regulatory protein NtrX and similar proteins; NtrX is part of the two-component regulatory system NtrY/NtrX that is involved in the activation of nitrogen assimilatory genes such as Gln. It is phosphorylated by the histidine kinase NtrY and interacts with sigma-54. NtrX 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. NtrC family response regulators are sigma54-dependent transcriptional activators. Also included in this subfamily is Aquifex aeolicus NtrC4. 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 740793425   8 ILVVEDDAIVRMLIVDVLEELEFKVLEAAGSEEALARLQDSAlhIDLMMTDVGLPGMDGKELAARARALRPELPVLFASG 87
Cdd:cd17550    1 ILIVDDEEDIRESLSGILEDEGYEVDTAADGEEALKLIKERR--PDLVLLDIWLPDMDGLELLKEIKEKYPDLPVIMISG 78

                         90       100       110
                 ....*....|....*....|....*....|...
gi 740793425  88 YAeNIEvpagMAV----------IGKPFSIDQL 110
Cdd:cd17550   79 HG-TIE----TAVkatklgaydfIEKPLSLDRL 106

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 740793425   9 LVVEDDAIVRMLIVDVLEELEFKVLEAAGSEEALARLQDsaLHIDLMMTDVGLPGMDGKELAARARALRPELPVLF 84
Cdd:cd17574    1 LVVEDDEEIAELLSDYLEKEGYEVDTAADGEEALELARE--EQPDLIILDVMLPGMDGFEVCRRLREKGSDIPIIM 74

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 740793425   8 ILVVEDDAIVRMLIVDVLEELEFKVLEAAGSEEALARLQDSAlhIDLMMTDVGLPGMDGKELAARARALRPELPVLFASG 87
Cdd:cd17549    1 VLLVDDDADVREALQQTLELAGFRVRAFADAEEALAALSPDF--PGVVISDIRMPGMDGLELLAQIRELDPDLPVILITG 78

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 740793425  88 YAeniEVPagMAV----------IGKPFSIDQLRDKVR 115
Cdd:cd17549   79 HG---DVP--MAVeamragaydfLEKPFDPERLLDVVR 111

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 740793425   8 ILVVEDDAIVRMLIVDVLEELEFKVLEAAGSEEALARLQDsalH--IDLMMTDVGLPGMDGKELAARARALRP--ELPVL 83
Cdd:cd17544    3 VLVVDDSATSRNHLRALLRRHNFQVLEAANGQEALEVLEQ---HpdIKLVITDYNMPEMDGFELVREIRKKYSrdQLAII 79

                 ....*...
gi 740793425  84 FASGYAEN 91
Cdd:cd17544   80 GISASGDN 87

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 740793425   8 ILVVEDDAIVRMLIVDVLE-ELEFKVL-EAAGSEEALARLQdsALHIDLMMTDVGLPGMDGKELAARARALRPELPVLFA 85
Cdd:cd17535    1 VLIVDDHPLVREGLRRLLEsEPDIEVVgEAADGEEALALLR--ELRPDVVLMDLSMPGMDGIEALRRLRRRYPDLKVIVL 78

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 740793425  86 SGYAENIEVPAGM-----AVIGKPFSIDQLRDKVRAILG 119
Cdd:cd17535   79 TAHDDPEYVLRALkagaaGYLLKDSSPEELIEAIRAVAA 117

DNA-binding response regulator, FixJ family, consists of REC and HTH domains [Signal transduction mechanisms, Transcription];

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740793425   7 TILVVEDDAIVRMLIVDVLEELEFKVLEAAGSEEALARLQdsALHIDLMMTDVGLPGMDGKELAARARALRPELPVLFAS 86
Cdd:COG4566    1 TVYIVDDDEAVRDSLAFLLESAGLRVETFASAEAFLAALD--PDRPGCLLLDVRMPGMSGLELQEELAARGSPLPVIFLT 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 740793425  87 GYAeniEVPagMAV----------IGKPFSIDQLRDKVRAIL 118
Cdd:COG4566   79 GHG---DVP--MAVramkagavdfLEKPFDDQALLDAVRRAL 115

phosphoacceptor receiver (REC) domain of modulated diguanylate cyclase and similar domains; This groups includes a modulated diguanylate cyclase containing a PAS sensor domain from Desulfovibrio desulfuricans G20. Members of this group contain N-terminal REC domains and various output domains including the GGDEF, histidine kinase, and helix-turn-helix (HTH) DNA binding domains. Also included in this family is Mycobacterium tuberculosis PdtaR, a transcriptional antiterminator that contains a REC domain and an ANTAR RNA-binding output 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 740793425   7 TILVVEDDAIVRMLIVDVLEELEFKVLEAAGS-EEALARLQDsaLHIDLMMTDVGLPG-MDGKELAARARALRPeLPVLF 84
Cdd:cd17534    2 KILIVEDEAIIALDLKEILESLGYEVVGIADSgEEAIELAEE--NKPDLILMDINLKGdMDGIEAAREIREKFD-IPVIF 78

                         90       100       110
                 ....*....|....*....|....*....|....
gi 740793425  85 ASGYA--ENIE-----VPAGMavIGKPFSIDQLR 111
Cdd:cd17534   79 LTAYSdeETLEraketNPYGY--LVKPFNERELK 110

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 740793425   7 TILVVEDDAIVRMLIVDVLEELEFKVLEAAGSEEALARLQDSAlhIDLMMTDVGLPGMDGKELAARARALrPE---LPVL 83
Cdd:cd17562    2 KILAVDDSASIRQMVSFTLRGAGYEVVEAADGRDALSKAQSKK--FDLIITDQNMPNMDGIELIKELRKL-PAykfTPIL 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 740793425  84 FASGYAENIEVPAGMAV-----IGKPFSIDQLRDKVRAIL 118
Cdd:cd17562   79 MLTTESSDEKKQEGKAAgatgwLVKPFDPEQLLEVVKKVL 118

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 740793425   6 STILVVEDDAIVRMLIVDVLEELEFKVLEAAGSEEALARLQDSalHIDLMMTDVGLPGMDGKELAARAR--ALRPELPVL 83
Cdd:cd17618    1 RTILIVEDEPAIREMIAFNLERAGFDVVEAEDAESAVNLIVEP--RPDLILLDWMLPGGSGIQFIRRLKrdEMTRDIPII 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 740793425  84 FASGYAENIEVPAGMAV-----IGKPFSIDQLRDKVRAIL 118
Cdd:cd17618   79 MLTARGEEEDKVRGLEAgaddyITKPFSPRELVARIKAVL 118

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 740793425   8 ILVVEDDAIVRMLIVDVLEELEFKVLEAAGSEEALARLQDSAL-------HIDLMMTDVGLPGMDGKELAARARA--LRP 78
Cdd:cd19924    1 ILVVDDSPTARKQLRDLLKNLGFEIAEAVDGEEALNKLENLAKegndlskELDLIITDIEMPKMDGYELTFELRDdpRLA 80

                 ....*...
gi 740793425  79 ELPVLFAS 86
Cdd:cd19924   81 NIPVILNS 88

DNA-binding response regulator, LytR/AlgR family [Transcription, Signal transduction mechanisms];

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740793425   7 TILVVEDDAIVRMLIVDVLEEL-EFKVLEAAGS-EEALARLQDsaLHIDLMMTDVGLPGMDGKELAARARALRPELPVLF 84
Cdd:COG3279    3 KILIVDDEPLARERLERLLEKYpDLEVVGEASNgEEALELLEE--HKPDLVFLDIQMPGLDGFELARQLRELDPPPPIIF 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 740793425  85 ASGYAEN----IEVPAgmavIG---KPFSIDQLR---DKVRAIL 118
Cdd:COG3279   81 TTAYDEYaleaFEVNA----VDyllKPIDEERLAkalEKAKERL 120

phosphoacceptor receiver (REC) domain of hydrogen uptake protein regulator (HupR) and similar domains; This family is composed of mostly uncharacterized response regulators with similarity to the REC domains of response regulator components of two-component systems that regulates hydrogenase activity, including HupR and HoxA. HupR is part of the HupT/HupR system that controls the synthesis of the membrane-bound [NiFe]hydrogenase, HupSL, of the photosynthetic bacterium Rhodobacter capsulatus. It contains an N-terminal REC domain, a central sigma-54 interaction domain that lacks ATPase activity, and a C-terminal DNA-binding domain. Members of this family contain a REC domain and various output domains including the cyclase homology domain (CHD) and the c-di-GMP phosphodiesterase domains, HD-GYP and EAL. 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 740793425   7 TILVVEDDAIVRMLIVDVLEELEFKVLEAAGSEEALARLQDSalHIDLMMTDVGLPGMDGKELAARARALRPELPVLFAS 86
Cdd:cd17569    2 TILLVDDEPNILKALKRLLRREGYEVLTATSGEEALEILKQE--PVDVVISDQRMPGMDGAELLKRVRERYPDTVRILLT 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 740793425  87 GYAeniEVPAGMAVIG---------KPFSIDQLRDKVRAIL 118
Cdd:cd17569   80 GYA---DLDAAIEAINegeiyrfltKPWDDEELKETIRQAL 117

phosphoacceptor receiver (REC) domain of Spo0F and similar domains; Spo0F, a stand-alone response regulator containing only a REC domain with no output/effector domain, controls sporulation in Bacillus subtilis through the exchange of a phosphoryl group. Bacillus subtilis forms spores when conditions for growth become unfavorable. The initiation of sporulation is controlled by a phosphorelay (an expanded version of the two-component system) that consists of four main components: a histidine kinase (KinA), a secondary messenger (Spo0F), a phosphotransferase (Spo0B), and a transcription factor (Spo0A). 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 740793425   8 ILVVEDDAIVRMLIVDVLEELEFKVLEAAGSEEALARLQDSAlhIDLMMTDVGLPGMDGKELAARARALRPELPVLFASG 87
Cdd:cd17553    3 ILIVDDQYGIRILLNEVFNKEGYQTFQAANGLQALDIVTKER--PDLVLLDMKIPGMDGIEILKRMKVIDENIRVIIMTA 80

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 740793425  88 YAENIEVPAGMAV-----IGKPFSIDQLRDKVRAILG 119
Cdd:cd17553   81 YGELDMIQESKELgalthFAKPFDIDEIRDAVKKYLP 117

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 740793425   9 LVVEDDAIVRMLIVDVLEELEFKVLEAAGSEEALARLQDsaLHIDLMMTDVGLPGMDGKELAARAR--ALRPELPVLFAS 86
Cdd:cd19937    1 LVVDDEEDIVELLKYNLEKEGYEVVTAYDGEEALKRAKD--EKPDLIILDLMLPGIDGLEVCRILRsdPKTSSIPIIMLT 78

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 740793425  87 GYAENIEVPAGMAV-----IGKPFSIDQLRDKVRAIL 118
Cdd:cd19937   79 AKGEEFDKVLGLELgaddyITKPFSPRELLARVKAVL 115

phosphoacceptor receiver (REC) domain of plant ethylene receptors ETR1, ETR2, and EIN4, and similar proteins; Plant ethylene receptors contain N-terminal transmembrane domains that contain an ethylene binding site and also serve in localization of the receptor to the endoplasmic reticulum or the Golgi apparatus and a C-terminal histidine kinase (HK)-like domain. There are five ethylene receptors (ETR1, ERS1, ETR2, ERS2, and EIN4) in Arabidopsis thaliana. ETR1, ETR2, and EIN4 also contain REC domains C-terminal to the HK domain. ETR1 and ERS1 belong to subfamily 1, and have functional HK domains while ETR2, ERS2, and EIN4 belong to subfamily 2, and lack the necessary residues for HK activity and may function as serine/threonine kinases. The plant hormone ethylene plays an important role in plant growth and development. It regulates seed germination, seedling growth, leaf and petal abscission, fruit ripening, organ senescence, and pathogen responses. 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 740793425   8 ILVVEDDAIVRMLIVDVLEELEFKVLEAAGSEEALARLQDSALHIDLMMTDVGLPGMDGKELAARARALRP--ELPVLFA 85
Cdd:cd19933    3 VLLVDDNAVNRMVTKGLLEKLGCEVTTVSSGEECLNLLASAEHSFQLVLLDLCMPEMDGFEVALRIRKLFGrrERPLIVA 82

                         90       100       110
                 ....*....|....*....|....*....|...
gi 740793425  86 SGYAENIEV-----PAGM-AVIGKPFSIDQLRD 112
Cdd:cd19933   83 LTANTDDSTrekclSLGMnGVITKPVSLHALGD 115

phosphoacceptor receiver (REC) domain of hydrogen uptake protein regulator (HupR); Members of this subfamily are response regulator components of two-component systems that regulates hydrogenase activity, including HupR and HoxA. HupR is part of the HupT/HupR system that controls the synthesis of the membrane-bound [NiFe]hydrogenase, HupSL, of the photosynthetic bacterium Rhodobacter capsulatus. It belongs to the nitrogen regulatory protein C (NtrC) family of response regulators, which activate transcription by RNA polymerase (RNAP) in response to a change in the environment. HupR is an unusual member of this family as it activates transcription when unphosphorylated, and transcription is inhibited by phosphorylation. Proteins in this subfamily contain an N-terminal REC domain, a central sigma-54 interaction domain that lacks ATPase activity, and a C-terminal DNA-binding 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 740793425   7 TILVVEDDAIVRMLIVDVLEElEFKVLEAAGSEEALARLQDSALHIdlMMTDVGLPGMDGKELAARARALRPELPVLFAS 86
Cdd:cd17596    2 TILVVDDEVRSLEALRRTLEE-DFDVLTAASAEEALAILEEEWVQV--ILCDQRMPGTTGVEFLKEVRERWPEVVRIIIS 78

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 740793425  87 GYAENIEVPAGM------AVIGKPFSIDQLRDKVR 115
Cdd:cd17596   79 GYTDSEDIIAGIneagiyQYLTKPWHPDQLLLTVR 113

phosphoacceptor receiver (REC) domain of BaeR-like OmpR family response regulators; BaeR is part of the BaeSR two-component system that is involved in regulating genes that confer multidrug and metal resistance. In Salmonella, BaeSR induces AcrD and MdtABC drug efflux systems, increasing multidrug and metal resistance. In Escherichia coli, BaeR stimulates multidrug resistance via mdtABC (multidrug transporter ABC, formerly known as yegMNO) genes, which encode a resistance-nodulation-cell division (RND) drug efflux system. 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 740793425   7 TILVVEDDAIVRMLIVDVLEELEFKVLEAAGSEEALARLQDSAlhIDLMMTDVGLPGMDGKELAARARALrPELPVLFAS 86
Cdd:cd19938    1 RILIVEDEPKLAQLLIDYLRAAGYAPTLLAHGDQVLPYVRHTP--PDLILLDLMLPGTDGLTLCREIRRF-SDVPIIMVT 77

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 740793425  87 GYAENIEVPAGMAV-----IGKPFSIDQLRDKVRAIL 118
Cdd:cd19938   78 ARVEEIDRLLGLELgaddyICKPYSPREVVARVKAIL 114

chemotaxis protein CheY;

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740793425   1 MSPTDSTILVVEDDAIVRMLIVDVLEELEF-KVLEAAGSEEALARLQDSALhiDLMMTDVGLPGMDGKEL--AARARALR 77
Cdd:PRK10610   1 MADKELKFLVVDDFSTMRRIVRNLLKELGFnNVEEAEDGVDALNKLQAGGF--GFVISDWNMPNMDGLELlkTIRADGAM 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 740793425  78 PELPVLFASGYA--ENIEVPAGMAVIG---KPFSIDQLRDKVRAIL 118
Cdd:PRK10610  79 SALPVLMVTAEAkkENIIAAAQAGASGyvvKPFTAATLEEKLNKIF 124