CCT motif; This short motif is found in a number of plant proteins. It is rich in basic amino acids and has been called a CCT motif after Co, Col and Toc1. The CCT motif is about 45 amino acids long and contains a putative nuclear localization signal within the second half of the CCT motif. Toc1 mutants have been identified in this region.

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 334188506  442 REAALMKFRLKRKERCFEKKVRYHSRKKLAEQRPHVKGQFIRK 484
Cdd:pfam06203   1 REEALLRYREKRKTRKFDKKIRYESRKALADKRPRVKGRFVKA 43

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 334188506  60 PVRSLKVLLVENDDSTRHIVTALLKNCSYEVTAVPDVLEAWRILEDEKscIDLVLTEVDMPVHSGTGLLSKIMSHKTLKN 139
Cdd:COG0784    2 PLGGKRILVVDDNPDNRELLRRLLERLGYEVTTAEDGAEALELLRAGP--PDLILLDINMPGMDGLELLRRIRALPRLPD 79

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 334188506 140 IPVIMMSSHDSMVLVFKCLSNGAVDFLVKPIRKNELKNL 178
Cdd:COG0784   80 IPIIALTAYADEEDRERALEAGADDYLTKPVDPEELLEA 118

CCT motif; This short motif is found in a number of plant proteins. It is rich in basic amino acids and has been called a CCT motif after Co, Col and Toc1. The CCT motif is about 45 amino acids long and contains a putative nuclear localization signal within the second half of the CCT motif. Toc1 mutants have been identified in this region.

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 334188506  442 REAALMKFRLKRKERCFEKKVRYHSRKKLAEQRPHVKGQFIRK 484
Cdd:pfam06203   1 REEALLRYREKRKTRKFDKKIRYESRKALADKRPRVKGRFVKA 43

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
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 334188506    64 LKVLLVENDDSTRHIVTALLKNCSYEVTAVPDVLEAWRILEDEKscIDLVLTEVDMP 120
Cdd:smart00448   1 MRILVVDDDPLLRELLKALLEKEGYEVDEATDGEEALELLKEEK--PDLILLDIMMP 55

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 334188506  66 VLLVENDDSTRHIVTALLKNCSYEVTAVPDVLEAWRILEDEKSCIDLVLTEVDMPVHSGTGLLSKIMShktLKNIPVIMM 145
Cdd:cd17584    1 VLVVDDDPTCLAILKRMLLRCGYQVTTCTDAEEALSMLRENKDEFDLVITDVHMPDMDGFEFLELIRL---EMDLPVIMM 77

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 334188506 146 SSHDSMVLVFKCLSNGAVDFLVKPIRKNELKNLWQHVW 183
Cdd:cd17584   78 SADGSTSTVMKGLAHGACDYLLKPVSIEDLKNIWQHVV 115

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

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334188506  63 SLKVLLVENDDSTRHIVTALLKNCSYEVTAVPDVLEAWRILEDEKscIDLVLTEVDMPVHSGTGLLSKIMSHKTLKNIPV 142
Cdd:COG3706    1 PARILVVDDDPTNRKLLRRLLEAAGYEVVEAADGEEALELLQEHR--PDLILLDLEMPDMDGLELCRRLRADPRTADIPI 78

                         90       100       110
                 ....*....|....*....|....*....|....
gi 334188506 143 IMMSSHDSMVLVFKCLSNGAVDFLVKPIRKNELK 176
Cdd:COG3706   79 IFLTALDDEEDRARALEAGADDYLTKPFDPEELL 112

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 334188506  62 RSLKVLLVENDDSTRHIVTALLKNCSYEVTAVPDVLEAWRILEDEKscIDLVLTEVDMPVHSGTGLLSKIMSHKTLKNIP 141
Cdd:COG3437    5 QAPTVLIVDDDPENLELLRQLLRTLGYDVVTAESGEEALELLLEAP--PDLILLDVRMPGMDGFELLRLLRADPSTRDIP 82

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 334188506 142 VIMMSSHDSMVLVFKCLSNGAVDFLVKPIRKNELK 176
Cdd:COG3437   83 VIFLTALADPEDRERALEAGADDYLTKPFDPEELL 117

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 334188506  62 RSLKVLLVENDDSTRHIVTALLKNCSYEVTAVPDVLEAWRILEDEKscIDLVLTEVDMPVHSGTGLLSKIMSHKtlKNIP 141
Cdd:COG2204    1 SMARILVVDDDPDIRRLLKELLERAGYEVETAASGEEALALLREEP--PDLVLLDLRMPGMDGLELLRELRALD--PDLP 76

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 334188506 142 VIMMSSHDSMVLVFKCLSNGAVDFLVKPIRKNELKNL 178
Cdd:COG2204   77 VILLTGYGDVETAVEAIKAGAFDYLTKPFDLEELLAA 113

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 334188506  66 VLLVenDDST--RHIVTALLKNCSYEVTAVPDVLEAWRIL--EDEKSC-------IDLVLTEVDMPVHSGTGLLSKIMSH 134
Cdd:cd17581    1 VLAV--DDSLvdRKVIERLLRISSCRVTAVDSGKRALEFLglEDEEDSsnfnepkVNMIITDYCMPGMTGYDLLKKVKES 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 334188506 135 KTLKNIPVIMMSSHDSMVLVFKCLSNGAVDFLVKPIRKNELKNL 178
Cdd:cd17581   79 SALKEIPVVIMSSENIPTRISRCLEEGAEDFLLKPVKLADVKRL 122

CCT motif; This short motif is found in a number of plant proteins. It is rich in basic amino acids and has been called a CCT motif after Co, Col and Toc1. The CCT motif is about 45 amino acids long and contains a putative nuclear localization signal within the second half of the CCT motif. Toc1 mutants have been identified in this region.

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 334188506  442 REAALMKFRLKRKERCFEKKVRYHSRKKLAEQRPHVKGQFIRK 484
Cdd:pfam06203   1 REEALLRYREKRKTRKFDKKIRYESRKALADKRPRVKGRFVKA 43

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 334188506  65 KVLLVENDDSTRHIVTALLKNCSYEVTAVPDVLEAWRILEDEKScIDLVLTEVDMPVHSGTGLLSKIMSHKTLKNIPVIM 144
Cdd:cd17544    2 KVLVVDDSATSRNHLRALLRRHNFQVLEAANGQEALEVLEQHPD-IKLVITDYNMPEMDGFELVREIRKKYSRDQLAIIG 80

                         90       100
                 ....*....|....*....|....*
gi 334188506 145 MSSHDSMVLVFKCLSNGAVDFLVKP 169
Cdd:cd17544   81 ISASGDNALSARFIKAGANDFLTKP 105

phosphoacceptor receiver (REC) domain of hybrid sensor histidine kinases/response regulators similar to Arabidopsis thaliana CKI1 and Escherichia coli RcsC; This family is composed of hybrid sensor histidine kinases/response regulators that are sensor histidine kinases (HKs) fused with a REC domain, similar to the sensor histidine kinase CKI1 from Arabidopsis thaliana, which is involved in multi-step phosphorelay (MSP) signaling that mediates responses to a variety of important stimuli in plants. MSP involves a signal being transferred from HKs via histidine phosphotransfer proteins (AHP1-AHP5) to nuclear response regulators. The CKI1 REC domain specifically interacts with the downstream signaling protein AHP2, AHP3 and AHP5. The plant MSP system has evolved from the prokaryotic two-component system (TCS), which allows organisms to sense and respond to changes in environmental conditions. This family also includes bacterial hybrid sensor HKs such as Escherichia coli RcsC, which is a component of the Rcs signalling pathway that controls a variety of physiological functions like capsule synthesis, cell division, and motility. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334188506  66 VLLVENDDSTRHIVTALLKNCSYEVTAVPDVLEAWRILEDEksCIDLVLTEVDMPVHSGTGLLSKI-MSHKTLKNIPVIM 144
Cdd:cd17546    1 VLVVDDNPVNRKVLKKLLEKLGYEVDVAENGQEALELLKEE--PFDLVLMDLQMPVMDGLEATRRIrELEGGGRRTPIIA 78

                         90       100       110
                 ....*....|....*....|....*....|....
gi 334188506 145 MSSHDSMVLVFKCLSNGAVDFLVKPIRKNELKNL 178
Cdd:cd17546   79 LTANALEEDREKCLEAGMDDYLSKPVKLDQLKEV 112

Two-component response regulator, AmiR/NasT family, consists of REC and RNA-binding antiterminator (ANTAR) domains [Signal transduction mechanisms, Transcription];

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334188506  62 RSLKVLLVENDDSTRHIVTALLKNCSYEVTAVP-DVLEAWRILEDEKscIDLVLTEVDMPVHSGTGLLSKIMSHKTlknI 140
Cdd:COG3707    2 RGLRVLVVDDEPLRRADLREGLREAGYEVVAEAaDGEDAVELVRELK--PDLVIVDIDMPDRDGLEAARQISEERP---A 76

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 334188506 141 PVIMMSSHDSMVLVFKCLSNGAVDFLVKPIRKNELK 176
Cdd:COG3707   77 PVILLTAYSDPELIERALEAGVSAYLVKPLDPEDLL 112

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 334188506  65 KVLLVENDDSTRHIVTALLKNCSY-EVTAVPDVLEAWRILEDEKscIDLVLTEVDMPVHSGTGLLSKIMSHKTLKNIPVI 143
Cdd:cd17551    2 RILIVDDNPTNLLLLEALLRSAGYlEVVSFTDPREALAWCRENP--PDLILLDYMMPGMDGLEFIRRLRALPGLEDVPIV 79

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 334188506 144 MMSSHDSMVLVFKCLSNGAVDFLVKPIRKNEL----KNL 178
Cdd:cd17551   80 MITADTDREVRLRALEAGATDFLTKPFDPVELlarvRNL 118

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 334188506  66 VLLVENDDSTRHIVTALLKNCSYEVTAV---PDVLEAWRILEDEKscIDLVLTEVDMPVHSGTGLLSKImsHKTLKNIPV 142
Cdd:cd17536    1 VLIVDDEPLIREGLKKLIDWEELGFEVVgeaENGEEALELIEEHK--PDIVITDIRMPGMDGLELIEKI--RELYPDIKI 76

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 334188506 143 IMMSSHDSmvlvF----KCLSNGAVDFLVKPIRKNELKNL 178
Cdd:cd17536   77 IILSGYDD----FeyaqKAIRLGVVDYLLKPVDEEELEEA 112

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 334188506  65 KVLLVENDDSTRHIVTALLKNC--SYEVTAVPDVLEAWRILEDEKSCI-----DLVLTEVDMPVHSGTGLLSKIMSHKTL 137
Cdd:cd17557    1 TILLVEDNPGDAELIQEAFKEAgvPNELHVVRDGEEALDFLRGEGEYAdaprpDLILLDLNMPRMDGFEVLREIKADPDL 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 334188506 138 KNIPVIMMSSHDSMVLVFKCLSNGAVDFLVKPIRKNELKNLWQHVWR 184
Cdd:cd17557   81 RRIPVVVLTTSDAEEDIERAYELGANSYIVKPVDFEEFVEAIRSLGE 127

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

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334188506  64 LKVLLVENDDSTRHIVTALLKNCS-YEVTAV-PDVLEAWRILEDEKscIDLVLTEVDMPVHSGTGLLSKImsHKTLKNIP 141
Cdd:COG3279    2 MKILIVDDEPLARERLERLLEKYPdLEVVGEaSNGEEALELLEEHK--PDLVFLDIQMPGLDGFELARQL--RELDPPPP 77

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 334188506 142 VIMMSSHDSMVL-VFKclsNGAVDFLVKPIRKNELKNLWQHVWRRCHSSSGSGSESGIHDKKSVK 205
Cdd:COG3279   78 IIFTTAYDEYALeAFE---VNAVDYLLKPIDEERLAKALEKAKERLEAKAAAEASPEEKDRIFVK 139

phosphoacceptor receiver (REC) domain of VirG-like OmpR family response regulators; VirG is part of the VirA/VirG two-component system that regulates the expression of virulence (vir) genes. The histidine kinase VirA senses a phenolic wound response signal, undergoes autophosphorylation, and phosphorelays to the VirG response regulator, which induces transcription of the vir regulon. VirG belongs to the OmpR family of DNA-binding response regulators that contain N-terminal receiver (REC) and C-terminal DNA-binding winged helix-turn-helix effector domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334188506  65 KVLLVENDDSTRHIVTALLKNCSYEVTAVPDVLEAWRILEDEKscIDLVLTEVDMPVHSGTGLLSKImshKTLKNIPVIM 144
Cdd:cd17594    1 HVLVVDDDAAMRHLLILYLRERGFDVTAAADGAEEARLMLHRR--VDLVLLDLRLGQESGLDLLRTI---RARSDVPIII 75

                         90       100       110
                 ....*....|....*....|....*....|..
gi 334188506 145 MSSH-DSMVLVFKCLSNGAVDFLVKPIRKNEL 175
Cdd:cd17594   76 ISGDrRDEIDRVVGLELGADDYLAKPFGLREL 107

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 334188506  65 KVLLVENDDSTRHIVTALLKNCSYEVTAVPDVLEAWRILEDEKSciDLVLTEVDMPVHSGTGLLSKIMSHKTLKNIPVIM 144
Cdd:cd17618    2 TILIVEDEPAIREMIAFNLERAGFDVVEAEDAESAVNLIVEPRP--DLILLDWMLPGGSGIQFIRRLKRDEMTRDIPIIM 79

                         90       100       110
                 ....*....|....*....|....*....|.
gi 334188506 145 MSSHDSMVLVFKCLSNGAVDFLVKPIRKNEL 175
Cdd:cd17618   80 LTARGEEEDKVRGLEAGADDYITKPFSPREL 110

phosphoacceptor receiver (REC) domain of FixJ family response regulators; FixJ family response regulators contain an N-terminal receiver domain (REC) and a C-terminal LuxR family helix-turn-helix (HTH) DNA-binding output domain. The Sinorhizobium meliloti two-component system FixL/FixJ regulates nitrogen fixation in response to oxygen during symbiosis. Under microaerobic conditions, the kinase FixL phosphorylates the response regulator FixJ resulting in the regulation of nitrogen fixation genes such as nifA and fixK. 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 334188506  66 VLLVENDDSTRHIVTALLKNCSYEVTAVP---DVLEAWRIleDEKSCidlVLTEVDMPVHSGTGLLSKIMSHKTlkNIPV 142
Cdd:cd17537    3 VYVVDDDEAVRDSLAFLLRSVGLAVKTFTsasAFLAAAPP--DQPGC---LVLDVRMPGMSGLELQDELLARGS--NIPI 75

                         90       100       110
                 ....*....|....*....|....*....|...
gi 334188506 143 IMMSSHDSMVLVFKCLSNGAVDFLVKPIRKNEL 175
Cdd:cd17537   76 IFITGHGDVPMAVEAMKAGAVDFLEKPFRDQVL 108

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 334188506  65 KVLLVenDDS--TRHIVTALLKNCSYEV--TAVpDVLEAWRILEDEKscIDLVLTEVDMPVHSGTGLLSKIMshKTLKNI 140
Cdd:cd17542    2 KVLIV--DDAafMRMMLKDILTKAGYEVvgEAA-NGEEAVEKYKELK--PDLVTMDITMPEMDGIEALKEIK--KIDPNA 74

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 334188506 141 PVIMMSSHDSMVLVFKCLSNGAVDFLVKPIRKNEL 175
Cdd:cd17542   75 KVIMCSAMGQEEMVKEAIKAGAKDFIVKPFQPERV 109

phosphoacceptor receiver (REC) domain of nitrogen regulatory protein C 1 (NtrC1) from Aquifex aeolicus and similar NtrC family response regulators; NtrC family proteins are transcriptional regulators that have REC, AAA+ ATPase/sigma-54 interaction, and DNA-binding output domains. This subfamily of NtrC proteins include Aquifex aeolicus NtrC1 and Vibrio quorum-sensing signal integrator LuxO. The N-terminal REC domain of NtrC proteins regulate the activity of the protein and its phosphorylation controls the AAA+ domain oligomerization, while the central AAA+ domain participates in nucleotide binding, hydrolysis, oligomerization, and sigma54 interaction. 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 334188506  66 VLLVENDDSTRHIVTALLKNCSYEVTAVPDVLEAWRILEDekSCIDLVLTEVDMPVHSGTGLLSKImsHKTLKNIPVIMM 145
Cdd:cd17572    1 VLLVEDSPSLAALYQEYLSDEGYKVTHVETGKEALAFLSD--QPPDVVLLDLKLPDMSGMEILKWI--QERSLPTSVIVI 76

                         90       100       110
                 ....*....|....*....|....*....|.
gi 334188506 146 SSHDSMVLVFKCLSNGAVDFLVKPIRKNELK 176
Cdd:cd17572   77 TAHGSVDIAVEAMRLGAYDFLEKPFDADRLR 107

chemotaxis-specific protein-glutamate methyltransferase CheB;

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334188506  64 LKVLLVenDDST--RHIVTALL-KNCSYEVTAV-PDVLEAWRILEDEKscIDLVLTEVDMPVHSGTGLLSKIMShktLKN 139
Cdd:PRK00742   4 IRVLVV--DDSAfmRRLISEILnSDPDIEVVGTaPDGLEAREKIKKLN--PDVITLDVEMPVMDGLDALEKIMR---LRP 76

                         90       100       110
                 ....*....|....*....|....*....|..
gi 334188506 140 IPVIMMSS--HDSMVLVFKCLSNGAVDFLVKP 169
Cdd:PRK00742  77 TPVVMVSSltERGAEITLRALELGAVDFVTKP 108

phosphoacceptor receiver (REC) domain of RegX3-like OmpR family response regulators; RegX3 is a member of the SenX3-RegX3 two-component system that is involved in phosphate-sensing signal transduction. Phosphorylated RegX3 functions as a transcriptional activator of phoA. It induces transcription in phosphate limiting environment and also controls expression of several critical metabolic enzymes in aerobic condition. RegX3 belongs to the OmpR family of DNA-binding response regulators that contain N-terminal receiver and C-terminal DNA-binding winged helix-turn-helix effector domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334188506  66 VLLVENDDSTRHIVTALLKNCSYEVTAVPDVLEAwrILEDEKSCIDLVLTEVDMPVHSGTGLLSKImshKTLKNIPVIMM 145
Cdd:cd17621    1 VLVVEDEESFSDPLAYLLRKEGFEVTVATDGPAA--LAEFDRAGADIVLLDLMLPGLSGTEVCRQL---RARSNVPVIMV 75

                         90       100
                 ....*....|....*....|....
gi 334188506 146 SSHDSMVLVFKCLSNGAVDFLVKP 169
Cdd:cd17621   76 TAKDSEIDKVVGLELGADDYVTKP 99

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 334188506  66 VLLVENDDSTRHIVTALLKNCSYEVTAVPDVLEAWRILEDEKSCIdlVLTEVDMPVHSGTGLLSKImsHKTLKNIPVIMM 145
Cdd:cd17549    1 VLLVDDDADVREALQQTLELAGFRVRAFADAEEALAALSPDFPGV--VISDIRMPGMDGLELLAQI--RELDPDLPVILI 76

                         90       100
                 ....*....|....*....|....
gi 334188506 146 SSHDSMVLVFKCLSNGAVDFLVKP 169
Cdd:cd17549   77 TGHGDVPMAVEAMRAGAYDFLEKP 100

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
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 334188506    64 LKVLLVENDDSTRHIVTALLKNCSYEVTAVPDVLEAWRILEDEKscIDLVLTEVDMP 120
Cdd:smart00448   1 MRILVVDDDPLLRELLKALLEKEGYEVDEATDGEEALELLKEEK--PDLILLDIMMP 55

phosphoacceptor receiver (REC) domain of DNA-binding transcriptional regulator NtrC; DNA-binding transcriptional regulator NtrC is also called nitrogen regulation protein NR(I) or nitrogen regulator I (NRI). It contains an N-terminal receiver (REC) domain, followed by a sigma-54 interaction domain, and a C-terminal helix-turn-helix DNA-binding domain. It is part of the two-component regulatory system NtrB/NtrC, which controls expression of the nitrogen-regulated (ntr) genes in response to nitrogen limitation. DNA-binding response regulator NtrC is phosphorylated by NtrB; phosphorylation of the N-terminal REC domain activates the central sigma-54 interaction domain and leads to the transcriptional activation from promoters that require sigma(54)-containing RNA polymerase. 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 334188506  65 KVLLVENDDSTRHIVTALLKNCSYEVTAVPDVLEAWRILEDEKSciDLVLTEVDMPVHSGTGLLSKImsHKTLKNIPVIM 144
Cdd:cd19919    2 TVWIVDDDSSIRWVLERALAGAGLTVTSFENAQEALAALASSQP--DVLISDIRMPGMDGLALLAQI--KQRHPDLPVII 77

                         90       100       110
                 ....*....|....*....|....*....|...
gi 334188506 145 MSSH---DSMVLVFKclsNGAVDFLVKPIRKNE 174
Cdd:cd19919   78 MTAHsdlDSAVSAYQ---GGAFEYLPKPFDIDE 107

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 334188506  66 VLLVENDDSTRH-IVTALLKNCSYEVTA-VPDVLEAWRILEDEKscIDLVLTEVDMPVHSGTGLLSKIMSHktLKNIPVI 143
Cdd:cd17535    1 VLIVDDHPLVREgLRRLLESEPDIEVVGeAADGEEALALLRELR--PDVVLMDLSMPGMDGIEALRRLRRR--YPDLKVI 76

                         90       100       110
                 ....*....|....*....|....*....|..
gi 334188506 144 MMSSHDSMVLVFKCLSNGAVDFLVKPIRKNEL 175
Cdd:cd17535   77 VLTAHDDPEYVLRALKAGAAGYLLKDSSPEEL 108

phosphoacceptor receiver (REC) domain of Streptococcus agalactiae NsrR-like OmpR family response regulators; Streptococcus agalactiae NsrR is a lantibiotic resistance-associated response regulator and is part of the nisin resistance operon. It is a member of the NsrRK two-component system (TCS) that is involved in the regulation of lantibiotic resistance genes such as a membrane-associated lipoprotein of LanI, and the nsr gene cluster which encodes for the resistance protein NSR and the ABC transporter NsrFP, both conferring resistance against nisin. This subfamily also includes Staphylococcus epidermidis GraR, part of the GraR/GraS TCS involved in resistance against cationic antimicrobial peptides, and Bacillus subtilis BceR, part of the BceS/BceR TCS involved in the regulation of bacitracin resistance. Members of this subfamily belong to the OmpR family of DNA-binding response regulators, which contain N-terminal receiver (REC) and C-terminal DNA-binding winged helix-turn-helix effector domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334188506  66 VLLVENDDSTRHIVTALLKNCSYEVTAVPD---VLEawrilEDEKSCIDLVLTEVDMPVHSGTGLLSKImshKTLKNIPV 142
Cdd:cd18159    1 ILIVEDDETIASLLKKHLEKWGYEVVLIEDfedVLE-----EFLQFKPDLVLLDINLPYFDGFYWCREI---RQISNVPI 72