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 491527434 175 ILLVDDSSIARKQLCDALDSINIGYQICKNGLDALELMKSDA----AAHRPIDILVSDIEMPGLDGYELAFEVQNNSSLN 250
Cdd:cd19924    1 ILVVDDSPTARKQLRDLLKNLGFEIAEAVDGEEALNKLENLAkegnDLSKELDLIITDIEMPKMDGYELTFELRDDPRLA 80

                         90       100       110
                 ....*....|....*....|....*....|.
gi 491527434 251 HSYRILHTSLSSEICVDRAHQVGAHEALEKF 281
Cdd:cd19924   81 NIPVILNSSLSGEFSRARGKKVGADAYLAKF 111

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 491527434 175 ILLVDDSSIARKQLCDALDSINIGYQICKNGLDALELMKSDA----AAHRPIDILVSDIEMPGLDGYELAFEVQNNSSLN 250
Cdd:cd19924    1 ILVVDDSPTARKQLRDLLKNLGFEIAEAVDGEEALNKLENLAkegnDLSKELDLIITDIEMPKMDGYELTFELRDDPRLA 80

                         90       100       110
                 ....*....|....*....|....*....|.
gi 491527434 251 HSYRILHTSLSSEICVDRAHQVGAHEALEKF 281
Cdd:cd19924   81 NIPVILNSSLSGEFSRARGKKVGADAYLAKF 111

CheW-like domain; CheW proteins are part of the chemotaxis signaling mechanism in bacteria. CheW interacts with the methyl accepting chemotaxis proteins (MCPs) and relays signals to CheY, which affects flageller rotation. This family includes CheW and other related proteins that are involved in chemotaxis. The CheW-like regulatory domain in CheA binds to CheW, suggesting that these domains can interact with each other.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527434   14 MLMFKLTlQQSFAIGTLKVREIVPYMPTTKIPYSHHHVIGTVTIRNLTVPVIDMSAAVGFRPISEEEYKscYLIVTDCLR 93
Cdd:pfam01584   1 GLLFRLG-GETFAIPISKVREILRPPPITPIPGAPGYVLGVINLRGEVLPVIDLRRLLGLPPTEPRERT--RVVVVEVGG 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 491527434   94 TVVAFMVRSIEKIIECDWKAIETPPPSAGKNIFVTGITRYED-KTVQMLDVELL 146
Cdd:pfam01584  78 QVVGLLVDEVIGVLEIVIKQIEPPLGLGRVAGYISGATILGDgRVVLILDVEAL 131

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

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527434 169 RLKALSILLVDDSSIARKQLCDALDSINIGYQICKNGLDALELmksdaAAHRPIDILVSDIEMPGLDGYELAFEVQNNSS 248
Cdd:COG0784    2 PLGGKRILVVDDNPDNRELLRRLLERLGYEVTTAEDGAEALEL-----LRAGPPDLILLDINMPGMDGLELLRRIRALPR 76

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 491527434 249 LNHSYRILHTSLSSEICVDRAHQVGAHEALEK-FNAGELIEAMLR 292
Cdd:COG0784   77 LPDIPIIALTAYADEEDRERALEAGADDYLTKpVDPEELLEALRR 121

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 491527434  175 ILLVDDSSIARKQLCDALDSIniGYQICK--NGLDALELMKsdaaaHRPIDILVSDIEMPGLDGYELAFEVQNNSSlnHS 252
Cdd:pfam00072   1 VLIVDDDPLIRELLRQLLEKE--GYVVAEadDGKEALELLK-----EERPDLILLDINMPGMDGLELLKRIRRRDP--TT 71

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 491527434  253 YRILHTSLSSEICVDRAHQVGAHEALEK-FNAGELIEA 289
Cdd:pfam00072  72 PVIILTAHGDEDDAVEALEAGADDFLSKpFDPDELLAA 109

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 491527434   173 LSILLVDDSSIARKQLCDALDSINIGYQICKNGLDALELMKSDaaahrPIDILVSDIEMP 232
Cdd:smart00448   1 MRILVVDDDPLLRELLKALLEKEGYEVDEATDGEEALELLKEE-----KPDLILLDIMMP 55

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 491527434 175 ILLVDDSSIARKQLCDALDSINIGYQICKNGLDALELMKSDA----AAHRPIDILVSDIEMPGLDGYELAFEVQNNSSLN 250
Cdd:cd19924    1 ILVVDDSPTARKQLRDLLKNLGFEIAEAVDGEEALNKLENLAkegnDLSKELDLIITDIEMPKMDGYELTFELRDDPRLA 80

                         90       100       110
                 ....*....|....*....|....*....|.
gi 491527434 251 HSYRILHTSLSSEICVDRAHQVGAHEALEKF 281
Cdd:cd19924   81 NIPVILNSSLSGEFSRARGKKVGADAYLAKF 111

CheW-like domain; CheW proteins are part of the chemotaxis signaling mechanism in bacteria. CheW interacts with the methyl accepting chemotaxis proteins (MCPs) and relays signals to CheY, which affects flageller rotation. This family includes CheW and other related proteins that are involved in chemotaxis. The CheW-like regulatory domain in CheA binds to CheW, suggesting that these domains can interact with each other.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527434   14 MLMFKLTlQQSFAIGTLKVREIVPYMPTTKIPYSHHHVIGTVTIRNLTVPVIDMSAAVGFRPISEEEYKscYLIVTDCLR 93
Cdd:pfam01584   1 GLLFRLG-GETFAIPISKVREILRPPPITPIPGAPGYVLGVINLRGEVLPVIDLRRLLGLPPTEPRERT--RVVVVEVGG 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 491527434   94 TVVAFMVRSIEKIIECDWKAIETPPPSAGKNIFVTGITRYED-KTVQMLDVELL 146
Cdd:pfam01584  78 QVVGLLVDEVIGVLEIVIKQIEPPLGLGRVAGYISGATILGDgRVVLILDVEAL 131

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

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527434 169 RLKALSILLVDDSSIARKQLCDALDSINIGYQICKNGLDALELmksdaAAHRPIDILVSDIEMPGLDGYELAFEVQNNSS 248
Cdd:COG0784    2 PLGGKRILVVDDNPDNRELLRRLLERLGYEVTTAEDGAEALEL-----LRAGPPDLILLDINMPGMDGLELLRRIRALPR 76

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 491527434 249 LNHSYRILHTSLSSEICVDRAHQVGAHEALEK-FNAGELIEAMLR 292
Cdd:COG0784   77 LPDIPIIALTAYADEEDRERALEAGADDYLTKpVDPEELLEALRR 121

CheW-like domain. CheW proteins are part of the chemotaxis signalling mechanism in bacteria. CheW interacts with the methyl accepting chemotaxis proteins (MCPs) and relays signals to CheY, which affects flageller rotation. This family includes CheW and other related proteins that are involved in chemotaxis. The CheW-like regulatory domain in the chemotaxis associated histidine kinase CheA binds to CheW, suggesting that these domains can interact with each other.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527434  11 SQGMLMFKLtLQQSFAIGTLKVREIVPYMPTTKIPYSHHHVIGTVTIRNLTVPVIDMSAAVGFRPISEEEYKScYLIVTD 90
Cdd:cd00588    1 ILQVLLFRV-GDELYAIPIAVVEEILPLPPITRVPNAPDYVLGVINLRGEILPVIDLRRLFGLEAAEPDTDET-RIVVVE 78

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 491527434  91 CLRTVVAFMVRSIEKIIECDWKAIETPPPSAGKNI-FVTGITRYED-KTVQMLDVELL 146
Cdd:cd00588   79 VGDRKVGLVVDSVLGVLEVVIKDIEPPPDVGSSNApGISGATILGDgRVVLILDVDKL 136

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

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527434 171 KALSILLVDDSSIARKQLCDALDsiNIGYQI--CKNGLDALELmksdaAAHRPIDILVSDIEMPGLDGYELAFEVQNNSS 248
Cdd:COG3437    5 QAPTVLIVDDDPENLELLRQLLR--TLGYDVvtAESGEEALEL-----LLEAPPDLILLDVRMPGMDGFELLRLLRADPS 77

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 491527434 249 LNHSYRILHTSLSSEICVDRAHQVGAHEALEK-FNAGELIEAM 290
Cdd:COG3437   78 TRDIPVIFLTALADPEDRERALEAGADDYLTKpFDPEELLARV 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 491527434 176 LLVDDSSIARKQLCDALDSINIGYQICKNGLDALELmksdaAAHRPIDILVSDIEMPGLDGYELAFEVQNNSSlnHSYRI 255
Cdd:cd00156    1 LIVDDDPAIRELLKSLLEREGYEVDTAADGEEALEL-----LREERPDLVLLDLMMPGMDGLELLRKLRELPP--DIPVI 73

                         90       100
                 ....*....|....*....|....*
gi 491527434 256 LHTSLSSEICVDRAHQVGAHEALEK 280
Cdd:cd00156   74 VLTAKADEEDAVRALELGADDYLVK 98

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 491527434 175 ILLVDDSSIARKQLCDALDSIniGYQI--CKNGLDALELmksdAAAHRPiDILVSDIEMPGLDGYELAFEVQNNSSLNHS 252
Cdd:cd17580    1 ILVVDDNEDAAEMLALLLELE--GAEVttAHSGEEALEA----AQRFRP-DVILSDIGMPGMDGYELARRLRELPWLANT 73

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 491527434 253 YRILHTSLSSEICVDRAHQVGAHEALEK-FNAGELIEA 289
Cdd:cd17580   74 PAIALTGYGQPEDRERALEAGFDAHLVKpVDPDELIEL 111

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 491527434 175 ILLVDDSSIARKQLCDALDsiNIGYQI--CKNGLDALELmksdAAAHRPiDILVSDIEMPGLDGYELAFEVQNNSSlnhS 252
Cdd:COG0745    4 ILVVEDDPDIRELLADALE--REGYEVdtAADGEEALEL----LEEERP-DLILLDLMLPGMDGLEVCRRLRARPS---D 73

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 491527434 253 YRILH-TSLSSEICVDRAHQVGAHEALEK-FNAGEL---IEAMLR 292
Cdd:COG0745   74 IPIIMlTARDDEEDRVRGLEAGADDYLTKpFDPEELlarIRALLR 118

two-component system sensor histidine kinase RcsC;

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527434 137 TVQMLDVELLLSKIY----PQYENSKIPMLTDIERERLKALSILLVDDSSIARKQLCDALDSIniGYQiCK---NGLDAL 209
Cdd:PRK10841 762 TATPHELPALLARIYrielESDDSANALPSTDKAVSDNDDMMILVVDDHPINRRLLADQLGSL--GYQ-CKtanDGVDAL 838

                         90       100       110
                 ....*....|....*....|....*....|.
gi 491527434 210 ELMKSDaaahrPIDILVSDIEMPGLDGYELA 240
Cdd:PRK10841 839 NVLSKN-----HIDIVLTDVNMPNMDGYRLT 864

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

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491527434 173 LSILLVDDSSIARKQLCDAL-DSINIGYQICKNGLDALELMKSDaaahrPIDILVSDIEMPGLDGYE 238
Cdd:cd17593    1 MKVLICDDSSMARKQLARALpADWDVEITFAENGEEALEILREG-----RIDVLFLDLTMPVMDGYE 62

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
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491527434 175 ILLVDDSSIARKQLCDALDSIN----IGyqICKNGLDALELMKsdaaAHRPiDILVSDIEMPGLDGYE 238
Cdd:cd17541    3 VLIVDDSAVMRKLLSRILESDPdievVG--TARDGEEALEKIK----ELKP-DVITLDIEMPVMDGLE 63

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

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491527434 175 ILLVDDSSIARKQLCDALDSINIGYQICKNGLDALELMKSDAaahrPIDILVSDIEMPGLDGYELAFEV 243
Cdd:cd18160    2 ILLADDEPSVRKFIVTTLKKAGYAVTEAESGAEALEKLQQGK----DIDIVVTDIVMPEMDGIELAREA 66

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

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491527434 173 LSILLVDDSSIARKQLCDALDSINiGYQI---CKNGLDALELMKSdaaaHRPiDILVSDIEMPGLDGYELA 240
Cdd:COG3279    2 MKILIVDDEPLARERLERLLEKYP-DLEVvgeASNGEEALELLEE----HKP-DLVFLDIQMPGLDGFELA 66

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 491527434 173 LSILLVDDSSIARKQLCDALDsiNIGY---QICKNGLDALELMKsdaaaHRPIDILVSDIEMPGLDGYELAFEVQNNSSL 249
Cdd:cd19923    1 MKVLVVDDFSTMRRIIKNLLK--ELGFnnvEEAEDGVDALEKLK-----AGGFDFVITDWNMPNMDGLELLKTIRADGAL 73

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 491527434 250 NHSYRILHTSLSSEICVDRAHQVGAHEALEK-FNAGELIEAM 290
Cdd:cd19923   74 SHLPVLMVTAEAKKENVIAAAQAGVNNYIVKpFTAATLKEKL 115

phosphoacceptor receiver (REC) domain of probable transcriptional regulator Ycf29; Ycf29 is a probable response regulator of a two-component system (TCS), typically consisting a sensor and a response regulator, that functions in adaptation to changing environments. Processes regulated by TCSs in bacteria include sporulation, pathogenicity, virulence, chemotaxis, and membrane transport. Ycf29 contains an N-terminal REC domain and a LuxR-type helix-turn-helix DNA-binding output domain. 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
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491527434 175 ILLVDDSSIARKQLCDALDSINIGYQICKNGLDALELMKSdaaahRPIDILVSDIEMPGLDGYELAFEVQNNSSLNH 251
Cdd:cd19927    1 ILLVDDDPGIRLAVKDYLEDQGFTVIAASNGLEALDLLNQ-----YIPDLIISDIIMPGVDGYSLLGKLRKNADFDT 72

chemotaxis-specific protein-glutamate methyltransferase CheB;

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527434 171 KALSILLVDDSSIARKQLCDALDS---IN-IGyqICKNGLDALELMKsdaaAHRPiDILVSDIEMPGLDG 236
Cdd:PRK00742   2 MKIRVLVVDDSAFMRRLISEILNSdpdIEvVG--TAPDGLEAREKIK----KLNP-DVITLDVEMPVMDG 64

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 491527434 175 ILLVDDSSIARKQLCDALDSIniGYQI--CKNGLDALELmksdAAAHRPiDILVSDIEMPGLDGYELAFEVQNNSSLNHS 252
Cdd:cd17538    2 ILVVDDEPANRELLEALLSAE--GYEVltADSGQEALAL----AEEELP-DLILLDVMMPGMDGFEVCRRLKEDPETRHI 74

                         90       100
                 ....*....|....*....|....*...
gi 491527434 253 YRILHTSLSSEICVDRAHQVGAHEALEK 280
Cdd:cd17538   75 PVIMITALDDREDRIRGLEAGADDFLSK 102

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
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491527434 175 ILLVDDSSIARKQLCDALDSIniGYQICK--NGLDALELMKSDAAahrpIDILVSDIEMPG-LDGYELAFEV 243
Cdd:cd18161    1 VLVVEDDPDVRRLTAEVLEDL--GYTVLEaaSGDEALDLLESGPD----IDLLVTDVIMPGgMNGSQLAEEA 66

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 491527434 175 ILLVDDSSIAR---KQLCDALDSINIGYQiCKNGLDALELmksdAAAHRPiDILVSDIEMPGLDGYELAFEVQnnsSLNH 251
Cdd:cd17535    1 VLIVDDHPLVReglRRLLESEPDIEVVGE-AADGEEALAL----LRELRP-DVVLMDLSMPGMDGIEALRRLR---RRYP 71

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 491527434 252 SYRIL-HTSLSSEICVDRAHQVGAHEALEK-FNAGELIEA 289
Cdd:cd17535   72 DLKVIvLTAHDDPEYVLRALKAGAAGYLLKdSSPEELIEA 111

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 491527434 175 ILLVDDSSIARKQLCDALDSinIGYQI---CKNGLDALELMKsdaaAHRPiDILVSDIEMPGLDGYELAFEVQnnsSLNH 251
Cdd:cd17542    3 VLIVDDAAFMRMMLKDILTK--AGYEVvgeAANGEEAVEKYK----ELKP-DLVTMDITMPEMDGIEALKEIK---KIDP 72

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 491527434 252 SYRILH-TSLSSEICVDRAHQVGAHEALEK-FNAGELIEAM 290
Cdd:cd17542   73 NAKVIMcSAMGQEEMVKEAIKAGAKDFIVKpFQPERVLEAV 113

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
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491527434 175 ILLVDDSSIARKQLCDALDSINIGYQICKNGLDALELMKSDAAahrpiDILVSDIEMPGLDGYEL 239
Cdd:cd17549    1 VLLVDDDADVREALQQTLELAGFRVRAFADAEEALAALSPDFP-----GVVISDIRMPGMDGLEL 60

DNA-binding response regulator, NarL/FixJ family, contains REC and HTH domains [Signal transduction mechanisms, Transcription];

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491527434 175 ILLVDDSSIARKQLCDALDSiNIGYQI---CKNGLDALELmksdAAAHRPiDILVSDIEMPGLDGYELA 240
Cdd:COG2197    4 VLIVDDHPLVREGLRALLEA-EPDIEVvgeAADGEEALEL----LEELRP-DVVLLDIRMPGMDGLEAL 66

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 491527434 174 SILLVDDSSIARKQLCDALDSINIGYQI--CKNGLDALE-LMKSD--AAAHRPiDILVSDIEMPGLDGYELAFEVQNNSS 248
Cdd:cd17557    1 TILLVEDNPGDAELIQEAFKEAGVPNELhvVRDGEEALDfLRGEGeyADAPRP-DLILLDLNMPRMDGFEVLREIKADPD 79

                 ...
gi 491527434 249 LNH 251
Cdd:cd17557   80 LRR 82

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

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527434 176 LLVDDSSIARKQLCDALDSINIGYQICKNGLDALElmksdAAAHRPIDILVSDIEMPGLDGYELAFEVQNNSslNHSYRI 255
Cdd:cd17625    1 LVVEDEKDLSEAITKHLKKEGYTVDVCFDGEEGLE-----YALSGIYDLIILDIMLPGMDGLEVLKSLREEG--IETPVL 73