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 18410485  22 VLAVDDNLIDRKLVERILKISSCKVTTAENGLRALEYLGLGDPQQtDSLTNVMKVNLIITDYCMPGMTGFELLKKVKESS 101
Cdd:cd17581   1 VLAVDDSLVDRKVIERLLRISSCRVTAVDSGKRALEFLGLEDEED-SSNFNEPKVNMIITDYCMPGMTGYDLLKKVKESS 79

                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 18410485 102 NLKEVPVVILSSENIPTRINKCLASGAQMFMQKPLKLSDVEKL 144
Cdd:cd17581  80 ALKEIPVVIMSSENIPTRISRCLEEGAEDFLLKPVKLADVKRL 122

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 18410485  22 VLAVDDNLIDRKLVERILKISSCKVTTAENGLRALEYLGLGDPQQtDSLTNVMKVNLIITDYCMPGMTGFELLKKVKESS 101
Cdd:cd17581   1 VLAVDDSLVDRKVIERLLRISSCRVTAVDSGKRALEFLGLEDEED-SSNFNEPKVNMIITDYCMPGMTGYDLLKKVKESS 79

                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 18410485 102 NLKEVPVVILSSENIPTRINKCLASGAQMFMQKPLKLSDVEKL 144
Cdd:cd17581  80 ALKEIPVVIMSSENIPTRISRCLEEGAEDFLLKPVKLADVKRL 122

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 18410485  20 LHVLAVDDNLIDRKLVERILKISSCKVTTAENGLRALEYLGLGDPqqtdsltnvmkvNLIITDYCMPGMTGFELLKKVKE 99
Cdd:COG0784   6 KRILVVDDNPDNRELLRRLLERLGYEVTTAEDGAEALELLRAGPP------------DLILLDINMPGMDGLELLRRIRA 73

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 18410485 100 SSNLKEVPVVILSSENIPTRINKCLASGAQMFMQKPLKLSD 140
Cdd:COG0784  74 LPRLPDIPIIALTAYADEEDRERALEAGADDYLTKPVDPEE 114

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 18410485     20 LHVLAVDDNLIDRKLVERILKISSCKVTTAENGLRALEYLglgdpqqtdsltNVMKVNLIITDYCMP 86
Cdd:smart00448   1 MRILVVDDDPLLRELLKALLEKEGYEVDEATDGEEALELL------------KEEKPDLILLDIMMP 55

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 18410485  22 VLAVDDNLIDRKLVERILKISSCKVTTAENGLRALEYLGLGDPQQtDSLTNVMKVNLIITDYCMPGMTGFELLKKVKESS 101
Cdd:cd17581   1 VLAVDDSLVDRKVIERLLRISSCRVTAVDSGKRALEFLGLEDEED-SSNFNEPKVNMIITDYCMPGMTGYDLLKKVKESS 79

                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 18410485 102 NLKEVPVVILSSENIPTRINKCLASGAQMFMQKPLKLSDVEKL 144
Cdd:cd17581  80 ALKEIPVVIMSSENIPTRISRCLEEGAEDFLLKPVKLADVKRL 122

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 18410485  20 LHVLAVDDNLIDRKLVERILKISSCKVTTAENGLRALEYLGLGDPqqtdsltnvmkvNLIITDYCMPGMTGFELLKKVKE 99
Cdd:COG0784   6 KRILVVDDNPDNRELLRRLLERLGYEVTTAEDGAEALELLRAGPP------------DLILLDINMPGMDGLELLRRIRA 73

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 18410485 100 SSNLKEVPVVILSSENIPTRINKCLASGAQMFMQKPLKLSD 140
Cdd:COG0784  74 LPRLPDIPIIALTAYADEEDRERALEAGADDYLTKPVDPEE 114

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 18410485  21 HVLAVDDNLIDRKLVERILKIS--SCKVTTAENGLRALEYLglgdpQQTDSLTNVMKVNLIITDYCMPGMTGFELLKKVK 98
Cdd:cd17557   1 TILLVEDNPGDAELIQEAFKEAgvPNELHVVRDGEEALDFL-----RGEGEYADAPRPDLILLDLNMPRMDGFEVLREIK 75

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 18410485  99 ESSNLKEVPVVILSSENIPTRINKCLASGAQMFMQKPLKLSD 140
Cdd:cd17557  76 ADPDLRRIPVVVLTTSDAEEDIERAYELGANSYIVKPVDFEE 117

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 18410485  23 LAVDDNLIDRKLVERILKISSCKVTTAENGLRALEYLGLGDPqqtdsltnvmkvNLIITDYCMPGMTGFELLKKVKESSn 102
Cdd:cd00156   1 LIVDDDPAIRELLKSLLEREGYEVDTAADGEEALELLREERP------------DLVLLDLMMPGMDGLELLRKLRELP- 67

                        90       100       110
                ....*....|....*....|....*....|...
gi 18410485 103 lKEVPVVILSSENIPTRINKCLASGAQMFMQKP 135
Cdd:cd00156  68 -PDIPVIVLTAKADEEDAVRALELGADDYLVKP 99

phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase response regulator RpfG and similar proteins; Cyclic di-GMP phosphodiesterase response regulator RpfG, together with sensory/regulatory protein RpfC, constitute a two-component system implicated in sensing and responding to the diffusible signal factor (DSF) that is essential for cell-cell signaling. RpfC is a hybrid sensor/histidine kinase that phosphorylates and activates RpfG, which degrades cyclic di-GMP to GMP, leading to the activation of Clp, a global transcriptional regulator that regulates a large set of genes in the DSF pathway. RpfG contains a CheY-like receiver domain attached to a histidine-aspartic acid-glycine-tyrosine-proline (HD-GYP) cyclic di-GMP phosphodiesterase 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 18410485  21 HVLAVDDNLIDRKLVERIL-KISSCKVTTAENGLRALEYLGLGDPqqtDsltnvmkvnLIITDYCMPGMTGFELLKKVKE 99
Cdd:cd17551   2 RILIVDDNPTNLLLLEALLrSAGYLEVVSFTDPREALAWCRENPP---D---------LILLDYMMPGMDGLEFIRRLRA 69

                        90       100       110
                ....*....|....*....|....*....|....*...
gi 18410485 100 SSNLKEVPVVILSSENIP-TRInKCLASGAQMFMQKPL 136
Cdd:cd17551  70 LPGLEDVPIVMITADTDReVRL-RALEAGATDFLTKPF 106

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 18410485  22 VLAVDDNLIDRKLVERILKISS--CKVTTAENGLRALEYLglgdpQQTdsltnvmKVNLIITDYCMPGMTGFELLKKVKE 99
Cdd:COG4753   2 VLIVDDEPLIREGLKRILEWEAgfEVVGEAENGEEALELL-----EEH-------KPDLVITDINMPGMDGLELLEAIRE 69

                        90       100       110
                ....*....|....*....|....*....|....*.
gi 18410485 100 SSnlKEVPVVILSSENIPTRINKCLASGAQMFMQKP 135
Cdd:COG4753  70 LD--PDTKIIILSGYSDFEYAQEAIKLGADDYLLKP 103

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

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18410485  22 VLAVDDNLIDRKLVERILKISSCKVTTAENGLRALEYLglgdpqqtdsLTNVMKVNLIITDYCMPGMTGFELLKKVKESs 101
Cdd:cd17584   1 VLVVDDDPTCLAILKRMLLRCGYQVTTCTDAEEALSML----------RENKDEFDLVITDVHMPDMDGFEFLELIRLE- 69

                        90       100       110
                ....*....|....*....|....*....|....*....
gi 18410485 102 nlKEVPVVILSSENIPTRINKCLASGAQMFMQKPLKLSD 140
Cdd:cd17584  70 --MDLPVIMMSADGSTSTVMKGLAHGACDYLLKPVSIED 106

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 18410485  21 HVLAVDDNLIDRKLVERILKISSCKVTTAENGLRALEylglgdpqqtdsLTNVMKVNLIITDYCMPGMTGFELLKKVKES 100
Cdd:cd17538   1 KILVVDDEPANRELLEALLSAEGYEVLTADSGQEALA------------LAEEELPDLILLDVMMPGMDGFEVCRRLKED 68

                        90       100       110
                ....*....|....*....|....*....|....*
gi 18410485 101 SNLKEVPVVILSSENIPTRINKCLASGAQMFMQKP 135
Cdd:cd17538  69 PETRHIPVIMITALDDREDRIRGLEAGADDFLSKP 103

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 18410485  21 HVLAVDDNLIDRKLVERILKISSCKVTTAENGLRALeylglgdpqqtdSLTNVMKVNLIITDYCMPGMTGFELLKKVKES 100
Cdd:cd17562   2 KILAVDDSASIRQMVSFTLRGAGYEVVEAADGRDAL------------SKAQSKKFDLIITDQNMPNMDGIELIKELRKL 69

                        90       100       110
                ....*....|....*....|....*....|....*
gi 18410485 101 SNLKEVPVVILSSENIPTRINKCLASGAQMFMQKP 135
Cdd:cd17562  70 PAYKFTPILMLTTESSDEKKQEGKAAGATGWLVKP 104

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

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18410485  20 LHVLAVDDNLIDRKLVERIL-KISSCK-VTTAENGLRALEYLglgdpqqtdsltNVMKVNLIITDYCMPGMTGFELLKKV 97
Cdd:COG4565   4 IRVLIVEDDPMVAELLRRYLeRLPGFEvVGVASSGEEALALL------------AEHRPDLILLDIYLPDGDGLELLREL 71

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 18410485  98 KEssNLKEVPVVILSSENIPTRINKCLASGAQMFMQKPLKLSDVEKL 144
Cdd:COG4565  72 RA--RGPDVDVIVITAARDPETVREALRAGVVDYLIKPFTFERLREA 116

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 18410485  21 HVLAVDDNLIDRKLVERILKISSCKVTTAENGLRALEYLGlgdpQQTDsltnvmkVNLIITDYCMPGMTGFELLKKVKES 100
Cdd:cd17544   2 KVLVVDDSATSRNHLRALLRRHNFQVLEAANGQEALEVLE----QHPD-------IKLVITDYNMPEMDGFELVREIRKK 70

                        90       100       110
                ....*....|....*....|....*....|....*
gi 18410485 101 SNLKEVPVVILSSENIPTRINKCLASGAQMFMQKP 135
Cdd:cd17544  71 YSRDQLAIIGISASGDNALSARFIKAGANDFLTKP 105

phosphoacceptor receiver (REC) domain of DivK and similar proteins; Caulobacter crescentus DivK is an essential response regulator that is involved in the complex phosphorelay pathways controlling both cell division and motility. It localizes cell cycle regulators to specific poles of the cell during division. DivK contains a stand-alone 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 18410485  22 VLAVDDNLIDRKLVERILKISSCKVTTAENGLRALEYLGLGDPqqtdsltnvmkvNLIITDYCMPGMTGFELLKKVKESS 101
Cdd:cd17548   2 ILIVEDNPLNMKLARDLLESAGYEVLEAADGEEALEIARKEKP------------DLILMDIQLPGMDGLEATRLLKEDP 69

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 18410485 102 NLKEVPVVILSS-------ENIptrinkcLASGAQMFMQKPL 136
Cdd:cd17548  70 ATRDIPVIALTAyamkgdrEKI-------LEAGCDGYISKPI 104

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 18410485  22 VLAVDD---NLidrKLVERILKISSCKVTTAENGLRALEYLglgdpQQTdsltnvmKVNLIITDYCMPGMTGFELLKKVK 98
Cdd:cd17569   3 ILLVDDepnIL---KALKRLLRREGYEVLTATSGEEALEIL-----KQE-------PVDVVISDQRMPGMDGAELLKRVR 67

                .
gi 18410485  99 E 99
Cdd:cd17569  68 E 68

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 18410485  22 VLAVDDNLIDRKLVERILKISSCKVT---TAENGLRALEYLglgdpQQtdsltnvMKVNLIITDYCMPGMTGFELLKKVK 98
Cdd:cd17536   1 VLIVDDEPLIREGLKKLIDWEELGFEvvgEAENGEEALELI-----EE-------HKPDIVITDIRMPGMDGLELIEKIR 68

                        90
                ....*....|....
gi 18410485  99 EssNLKEVPVVILS 112
Cdd:cd17536  69 E--LYPDIKIIILS 80

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 18410485  22 VLAVDDNLIDRKLVERILKISS--CKVTTAENGLRALEYLGLGDPQqtdsltnvmkvnLIITDYCMPGMTGFELLKKVKE 99
Cdd:cd17535   1 VLIVDDHPLVREGLRRLLESEPdiEVVGEAADGEEALALLRELRPD------------VVLMDLSMPGMDGIEALRRLRR 68

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 18410485 100 SsnLKEVPVVILSSENIPTRINKCLASGAQMFMqkpLKLSDVEKL 144
Cdd:cd17535  69 R--YPDLKVIVLTAHDDPEYVLRALKAGAAGYL---LKDSSPEEL 108

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 18410485  21 HVLAVDDNLIDRKLVERILKISSCKVTTAENGLRALEYLGLGDPqqtdsltnvmkvNLIITDYCMPGMTGFELLKKVKES 100
Cdd:cd17554   2 KILVVDDEENIRELYKEELEDEGYEVVTAGNGEEALEKLESEDP------------DLVILDIKMPGMDGLETLRKIREK 69

                        90
                ....*....|...
gi 18410485 101 SnlKEVPVVILSS 113
Cdd:cd17554  70 K--PDLPVIICTA 80

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 18410485  22 VLAVDDNLIDRKLVERILKISSCKVTTAENGLRALEYLglgDPQQTDsltnvmkvnLIITDYCMPGMTGFELLKKVKESS 101
Cdd:cd17549   1 VLLVDDDADVREALQQTLELAGFRVRAFADAEEALAAL---SPDFPG---------VVISDIRMPGMDGLELLAQIRELD 68

                        90       100       110
                ....*....|....*....|....*....|....*
gi 18410485 102 nlKEVPVVILSSE-NIPTRInKCLASGAQMFMQKP 135
Cdd:cd17549  69 --PDLPVILITGHgDVPMAV-EAMRAGAYDFLEKP 100

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 18410485  20 LHVLAVDDNLIDRKLVERILKISSCKVTTAENGLRALEYLGLGDpqqtdsltnvMKVNLIITDYCMPGMTGFELLKKVKE 99
Cdd:cd19933   1 LKVLLVDDNAVNRMVTKGLLEKLGCEVTTVSSGEECLNLLASAE----------HSFQLVLLDLCMPEMDGFEVALRIRK 70

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 18410485 100 SSNLKEVP-VVILSSENIPTRINKCLASGAQMFMQKPLKLSDVEK 143
Cdd:cd19933  71 LFGRRERPlIVALTANTDDSTREKCLSLGMNGVITKPVSLHALGD 115

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 18410485  21 HVLAVDDNLIDRKLVERILKISSCKVTTAENGLRALEYLGLGDPqqtdsltnvmkvNLIITDYCMPGMTGFELLKKVKES 100
Cdd:cd17618   2 TILIVEDEPAIREMIAFNLERAGFDVVEAEDAESAVNLIVEPRP------------DLILLDWMLPGGSGIQFIRRLKRD 69

                        90       100       110
                ....*....|....*....|....*....|....*
gi 18410485 101 SNLKEVPVVILSSENIPTRINKCLASGAQMFMQKP 135
Cdd:cd17618  70 EMTRDIPIIMLTARGEEEDKVRGLEAGADDYITKP 104

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

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18410485  20 LHVLAVDDNLIDRKLVERIL-KISSCKVTTAENGLRALEYLGLGDPQqtdsltnvmkvnLIITDYCMPGMTGFELLKKVK 98
Cdd:cd17593   1 MKVLICDDSSMARKQLARALpADWDVEITFAENGEEALEILREGRID------------VLFLDLTMPVMDGYEVLEALP 68

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 18410485  99 ESSnlKEVPVVILSSENIPTRINKCLASGAQMFMQKPLKLSDVEKL 144
Cdd:cd17593  69 VEQ--LETKVIVVSGDVQPEAKERVLELGALAFLKKPFDPEKLAQL 112

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 18410485  22 VLAVDDNLIDRKLVERILKISSCKVTTAENGLRALEYLGLGDPqqtdsltnvmkvNLIITDYCMPGMTGFELLKKVKEss 101
Cdd:cd17550   1 ILIVDDEEDIRESLSGILEDEGYEVDTAADGEEALKLIKERRP------------DLVLLDIWLPDMDGLELLKEIKE-- 66

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 18410485 102 NLKEVPVVILSSE-NIPTRInKCLASGAQMFMQKPLKLsdvEKL 144
Cdd:cd17550  67 KYPDLPVIMISGHgTIETAV-KATKLGAYDFIEKPLSL---DRL 106

phosphoacceptor receiver (REC) domain of MtPhoP-like OmpR family response regulators; Mycobacterium tuberculosis PhoP (MtPhoP) is part of the PhoP/PhoR two-component system that is involved in phosphate control by stimulating expression of genes involved in scavenging, transport and mobilization of phosphate, and repressing the utilization of nitrogen sources. Also included in this subfamily is Mycobacterium tuberculosis transcriptional regulatory protein TcrX, part of the two-component regulatory system TcrY/TcrX that may be involved in virulence. 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 18410485  22 VLAVDDNLIDRKLVERILKISSCKVTTAENGLRALEylgLGDPQQTDsltnvmkvnLIITDYCMPGMTGFELLKKVKESS 101
Cdd:cd17615   2 VLVVDDEPNITELLSMALRYEGWDVETAADGAEALA---AAREFRPD---------AVVLDIMLPDMDGLEVLRRLRADG 69

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 18410485 102 NlkEVPVVILSSEN-IPTRINKcLASGAQMFMQKPLKLSDV 141
Cdd:cd17615  70 P--DVPVLFLTAKDsVEDRIAG-LTAGGDDYVTKPFSLEEV 107

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 18410485  23 LAVDDNLIDRKLVERILKISSCKVTTAENGLRALEYLGLGDPQqtdsltnvmkvnLIITDYCMPGMTGFELLKKVKESSN 102
Cdd:cd17625   1 LVVEDEKDLSEAITKHLKKEGYTVDVCFDGEEGLEYALSGIYD------------LIILDIMLPGMDGLEVLKSLREEGI 68

                        90       100       110
                ....*....|....*....|....*....|....
gi 18410485 103 lkEVPVVILSSEN-IPTRInKCLASGAQMFMQKP 135
Cdd:cd17625  69 --ETPVLLLTALDaVEDRV-KGLDLGADDYLPKP 99

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

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18410485  20 LHVLAVDDNLIDRKLVERIL-KISSCK-VTTAENGLRALEYLglgdpQQTdsltnvmKVNLIITDYCMPGMTGFELLKKV 97
Cdd:COG3279   2 MKILIVDDEPLARERLERLLeKYPDLEvVGEASNGEEALELL-----EEH-------KPDLVFLDIQMPGLDGFELARQL 69

                        90
                ....*....|....
gi 18410485  98 KEssnLKEVPVVIL 111
Cdd:COG3279  70 RE---LDPPPPIIF 80

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
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18410485  22 VLAVDDNLIDRKLVERILKISSCKVTTAENGLRALEYLGLGDPqqtdsltnvmkVNLIITDYCMPGMTGFELLKKVKE 99
Cdd:cd18160   2 ILLADDEPSVRKFIVTTLKKAGYAVTEAESGAEALEKLQQGKD-----------IDIVVTDIVMPEMDGIELAREARK 68