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Conserved domains on  [gi|15227325|ref|NP_181663|]
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response regulator 3 [Arabidopsis thaliana]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PLN03029 super family cl33622
type-a response regulator protein; Provisional
 1-225 1.01e-100

type-a response regulator protein; Provisional


The actual alignment was detected with superfamily member PLN03029:

Pssm-ID: 215544 [Multi-domain]  Cd Length: 222  Bit Score: 291.17  E-value: 1.01e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227325    1 MVMETESKFHVLAVDDSLFDRKMIERLLQKSSCQVTTVDSGSKALEFLGLRVDD-NDPNALSTSPQIHQEVEINLIITDY 79
Cdd:PLN03029   1 MGITTESQFHVLAVDDSLIDRKLIEKLLKTSSYQVTTVDSGSKALKFLGLHEDDrSNPDTPSVSPNSHQEVEVNLIITDY 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227325   80 CMPGMTGYDLLKKVKESAAFRSIPVVIMSSENVPARISRCLEEGAEEFFLKPVKLADLTKLKPHMMKTKLKKESEKPVai 159
Cdd:PLN03029  81 CMPGMTGYDLLKKIKESSSLRNIPVVIMSSENVPSRITRCLEEGAEEFFLKPVQLSDLNRLKPHMMKTKSKNQKQENQ-- 158

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15227325  160 EEIVVSKPEIEEEEEESSVIEILPLHQEIESEQLEPmlSSNKRKAMEEVVSTDRSRPKYNDITTSV 225
Cdd:PLN03029 159 EKQEKLEESEIQSEKQEQPSQQPQSQPQPQQQPQQP--NNNKRKAMEEGLSPDRTRPRYNGITTVV 222
 
Name Accession Description Interval E-value
PLN03029 PLN03029
type-a response regulator protein; Provisional
 1-225 1.01e-100

type-a response regulator protein; Provisional


Pssm-ID: 215544 [Multi-domain]  Cd Length: 222  Bit Score: 291.17  E-value: 1.01e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227325    1 MVMETESKFHVLAVDDSLFDRKMIERLLQKSSCQVTTVDSGSKALEFLGLRVDD-NDPNALSTSPQIHQEVEINLIITDY 79
Cdd:PLN03029   1 MGITTESQFHVLAVDDSLIDRKLIEKLLKTSSYQVTTVDSGSKALKFLGLHEDDrSNPDTPSVSPNSHQEVEVNLIITDY 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227325   80 CMPGMTGYDLLKKVKESAAFRSIPVVIMSSENVPARISRCLEEGAEEFFLKPVKLADLTKLKPHMMKTKLKKESEKPVai 159
Cdd:PLN03029  81 CMPGMTGYDLLKKIKESSSLRNIPVVIMSSENVPSRITRCLEEGAEEFFLKPVQLSDLNRLKPHMMKTKSKNQKQENQ-- 158

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15227325  160 EEIVVSKPEIEEEEEESSVIEILPLHQEIESEQLEPmlSSNKRKAMEEVVSTDRSRPKYNDITTSV 225
Cdd:PLN03029 159 EKQEKLEESEIQSEKQEQPSQQPQSQPQPQQQPQQP--NNNKRKAMEEGLSPDRTRPRYNGITTVV 222
REC_typeA_ARR cd17581
phosphoacceptor receiver (REC) domain of type A Arabidopsis response regulators (ARRs) and ...
 11-140 2.51e-76

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.


Pssm-ID: 381119 [Multi-domain]  Cd Length: 122  Bit Score: 225.71  E-value: 2.51e-76
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227325  11 VLAVDDSLFDRKMIERLLQKSSCQVTTVDSGSKALEFLGLRVDDNDPNalstspqiHQEVEINLIITDYCMPGMTGYDLL 90
Cdd:cd17581   1 VLAVDDSLVDRKVIERLLRISSCRVTAVDSGKRALEFLGLEDEEDSSN--------FNEPKVNMIITDYCMPGMTGYDLL 72

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 15227325  91 KKVKESAAFRSIPVVIMSSENVPARISRCLEEGAEEFFLKPVKLADLTKL 140
Cdd:cd17581  73 KKVKESSALKEIPVVIMSSENIPTRISRCLEEGAEDFLLKPVKLADVKRL 122
CheY COG0784
CheY-like REC (receiver) domain, includes chemotaxis protein CheY and sporulation regulator ...
 10-137 5.28e-30

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


Pssm-ID: 440547 [Multi-domain]  Cd Length: 128  Bit Score: 108.01  E-value: 5.28e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227325  10 HVLAVDDSLFDRKMIERLLQKSSCQVTTVDSGSKALEFLglrvddndpnalstspqihQEVEINLIITDYCMPGMTGYDL 89
Cdd:COG0784   7 RILVVDDNPDNRELLRRLLERLGYEVTTAEDGAEALELL-------------------RAGPPDLILLDINMPGMDGLEL 67

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 15227325  90 LKKVKESAAFRSIPVVIMSSENVPARISRCLEEGAEEFFLKPVKLADL 137
Cdd:COG0784  68 LRRIRALPRLPDIPIIALTAYADEEDRERALEAGADDYLTKPVDPEEL 115
Response_reg pfam00072
Response regulator receiver domain; This domain receives the signal from the sensor partner in ...
 11-139 3.58e-18

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.


Pssm-ID: 395025 [Multi-domain]  Cd Length: 111  Bit Score: 76.81  E-value: 3.58e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227325    11 VLAVDDSLFDRKMIERLLQKSSCQVTTVDSGSKALEFLglrvddndpnalstspqihQEVEINLIITDYCMPGMTGYDLL 90
Cdd:pfam00072   1 VLIVDDDPLIRELLRQLLEKEGYVVAEADDGKEALELL-------------------KEERPDLILLDINMPGMDGLELL 61

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 15227325    91 KKVKESAAfrSIPVVIMSSENVPARISRCLEEGAEEFFLKPVKLADLTK 139
Cdd:pfam00072  62 KRIRRRDP--TTPVIILTAHGDEDDAVEALEAGADDFLSKPFDPDELLA 108
REC smart00448
cheY-homologous receiver domain; CheY regulates the clockwise rotation of E. coli flagellar ...
 10-82 8.34e-06

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.


Pssm-ID: 214668 [Multi-domain]  Cd Length: 55  Bit Score: 41.79  E-value: 8.34e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15227325     10 HVLAVDDSLFDRKMIERLLQKSSCQVTTVDSGSKALEFLglrvddndpnalstspqihQEVEINLIITDYCMP 82
Cdd:smart00448   2 RILVVDDDPLLRELLKALLEKEGYEVDEATDGEEALELL-------------------KEEKPDLILLDIMMP 55
 
Name Accession Description Interval E-value
PLN03029 PLN03029
type-a response regulator protein; Provisional
 1-225 1.01e-100

type-a response regulator protein; Provisional


Pssm-ID: 215544 [Multi-domain]  Cd Length: 222  Bit Score: 291.17  E-value: 1.01e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227325    1 MVMETESKFHVLAVDDSLFDRKMIERLLQKSSCQVTTVDSGSKALEFLGLRVDD-NDPNALSTSPQIHQEVEINLIITDY 79
Cdd:PLN03029   1 MGITTESQFHVLAVDDSLIDRKLIEKLLKTSSYQVTTVDSGSKALKFLGLHEDDrSNPDTPSVSPNSHQEVEVNLIITDY 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227325   80 CMPGMTGYDLLKKVKESAAFRSIPVVIMSSENVPARISRCLEEGAEEFFLKPVKLADLTKLKPHMMKTKLKKESEKPVai 159
Cdd:PLN03029  81 CMPGMTGYDLLKKIKESSSLRNIPVVIMSSENVPSRITRCLEEGAEEFFLKPVQLSDLNRLKPHMMKTKSKNQKQENQ-- 158

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15227325  160 EEIVVSKPEIEEEEEESSVIEILPLHQEIESEQLEPmlSSNKRKAMEEVVSTDRSRPKYNDITTSV 225
Cdd:PLN03029 159 EKQEKLEESEIQSEKQEQPSQQPQSQPQPQQQPQQP--NNNKRKAMEEGLSPDRTRPRYNGITTVV 222
REC_typeA_ARR cd17581
phosphoacceptor receiver (REC) domain of type A Arabidopsis response regulators (ARRs) and ...
 11-140 2.51e-76

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.


Pssm-ID: 381119 [Multi-domain]  Cd Length: 122  Bit Score: 225.71  E-value: 2.51e-76
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227325  11 VLAVDDSLFDRKMIERLLQKSSCQVTTVDSGSKALEFLGLRVDDNDPNalstspqiHQEVEINLIITDYCMPGMTGYDLL 90
Cdd:cd17581   1 VLAVDDSLVDRKVIERLLRISSCRVTAVDSGKRALEFLGLEDEEDSSN--------FNEPKVNMIITDYCMPGMTGYDLL 72

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 15227325  91 KKVKESAAFRSIPVVIMSSENVPARISRCLEEGAEEFFLKPVKLADLTKL 140
Cdd:cd17581  73 KKVKESSALKEIPVVIMSSENIPTRISRCLEEGAEDFLLKPVKLADVKRL 122
CheY COG0784
CheY-like REC (receiver) domain, includes chemotaxis protein CheY and sporulation regulator ...
 10-137 5.28e-30

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


Pssm-ID: 440547 [Multi-domain]  Cd Length: 128  Bit Score: 108.01  E-value: 5.28e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227325  10 HVLAVDDSLFDRKMIERLLQKSSCQVTTVDSGSKALEFLglrvddndpnalstspqihQEVEINLIITDYCMPGMTGYDL 89
Cdd:COG0784   7 RILVVDDNPDNRELLRRLLERLGYEVTTAEDGAEALELL-------------------RAGPPDLILLDINMPGMDGLEL 67

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 15227325  90 LKKVKESAAFRSIPVVIMSSENVPARISRCLEEGAEEFFLKPVKLADL 137
Cdd:COG0784  68 LRRIRALPRLPDIPIIALTAYADEEDRERALEAGADDYLTKPVDPEEL 115
PleD COG3706
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate ...
 8-137 6.70e-28

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


Pssm-ID: 442920 [Multi-domain]  Cd Length: 179  Bit Score: 104.22  E-value: 6.70e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227325   8 KFHVLAVDDSLFDRKMIERLLQKSSCQVTTVDSGSKALEFLglrvddndpnalstspqihQEVEINLIITDYCMPGMTGY 87
Cdd:COG3706   1 PARILVVDDDPTNRKLLRRLLEAAGYEVVEAADGEEALELL-------------------QEHRPDLILLDLEMPDMDGL 61

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 15227325  88 DLLKKVKESAAFRSIPVVIMSSENVPARISRCLEEGAEEFFLKPVKLADL 137
Cdd:COG3706  62 ELCRRLRADPRTADIPIIFLTALDDEEDRARALEAGADDYLTKPFDPEEL 111
RpfG COG3437
Response regulator c-di-GMP phosphodiesterase, RpfG family, contains REC and HD-GYP domains ...
 3-137 2.71e-26

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


Pssm-ID: 442663 [Multi-domain]  Cd Length: 224  Bit Score: 101.40  E-value: 2.71e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227325   3 METESKFHVLAVDDSLFDRKMIERLLQKSSCQVTTVDSGSKALEFLglrvddndpnalstspqihQEVEINLIITDYCMP 82
Cdd:COG3437   1 MRTGQAPTVLIVDDDPENLELLRQLLRTLGYDVVTAESGEEALELL-------------------LEAPPDLILLDVRMP 61

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 15227325  83 GMTGYDLLKKVKESAAFRSIPVVIMSSENVPARISRCLEEGAEEFFLKPVKLADL 137
Cdd:COG3437  62 GMDGFELLRLLRADPSTRDIPVIFLTALADPEDRERALEAGADDYLTKPFDPEEL 116
REC cd00156
phosphoacceptor receiver (REC) domain of response regulators (RRs) and pseudo response ...
 12-131 1.42e-24

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.


Pssm-ID: 381085 [Multi-domain]  Cd Length: 99  Bit Score: 93.06  E-value: 1.42e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227325  12 LAVDDSLFDRKMIERLLQKSSCQVTTVDSGSKALEFLglrvddndpnalstspqihQEVEINLIITDYCMPGMTGYDLLK 91
Cdd:cd00156   1 LIVDDDPAIRELLKSLLEREGYEVDTAADGEEALELL-------------------REERPDLVLLDLMMPGMDGLELLR 61

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 15227325  92 KVKESaaFRSIPVVIMSSENVPARISRCLEEGAEEFFLKP 131
Cdd:cd00156  62 KLREL--PPDIPVIVLTAKADEEDAVRALELGADDYLVKP 99
REC_typeB_ARR-like cd17584
phosphoacceptor receiver (REC) domain of type B Arabidopsis response regulators (ARRs) and ...
 11-137 1.66e-22

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.


Pssm-ID: 381121 [Multi-domain]  Cd Length: 115  Bit Score: 88.07  E-value: 1.66e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227325  11 VLAVDDSLFDRKMIERLLQKSSCQVTTVDSGSKALEFLglrvdDNDPNalstspqihqevEINLIITDYCMPGMTGYDLL 90
Cdd:cd17584   1 VLVVDDDPTCLAILKRMLLRCGYQVTTCTDAEEALSML-----RENKD------------EFDLVITDVHMPDMDGFEFL 63

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 15227325  91 KKVKESaafRSIPVVIMSSENVPARISRCLEEGAEEFFLKPVKLADL 137
Cdd:cd17584  64 ELIRLE---MDLPVIMMSADGSTSTVMKGLAHGACDYLLKPVSIEDL 107
AtoC COG2204
DNA-binding transcriptional response regulator, NtrC family, contains REC, AAA-type ATPase, ...
 7-140 7.87e-22

DNA-binding transcriptional response regulator, NtrC family, contains REC, AAA-type ATPase, and a Fis-type DNA-binding domains [Signal transduction mechanisms];


Pssm-ID: 441806 [Multi-domain]  Cd Length: 418  Bit Score: 92.33  E-value: 7.87e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227325   7 SKFHVLAVDDSLFDRKMIERLLQKSSCQVTTVDSGSKALEFLglrvddndpnalstspqihQEVEINLIITDYCMPGMTG 86
Cdd:COG2204   1 SMARILVVDDDPDIRRLLKELLERAGYEVETAASGEEALALL-------------------REEPPDLVLLDLRMPGMDG 61

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 15227325  87 YDLLKKVKEsaAFRSIPVVIMSSENVPARISRCLEEGAEEFFLKPVKLADLTKL 140
Cdd:COG2204  62 LELLRELRA--LDPDLPVILLTGYGDVETAVEAIKAGAFDYLTKPFDLEELLAA 113
REC_hyHK_CKI1_RcsC-like cd17546
phosphoacceptor receiver (REC) domain of hybrid sensor histidine kinases/response regulators ...
 11-140 2.54e-21

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.


Pssm-ID: 381099 [Multi-domain]  Cd Length: 113  Bit Score: 84.83  E-value: 2.54e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227325  11 VLAVDDSLFDRKMIERLLQKSSCQVTTVDSGSKALEFLglrvddndpnalstspqihQEVEINLIITDYCMPGMTGYDLL 90
Cdd:cd17546   1 VLVVDDNPVNRKVLKKLLEKLGYEVDVAENGQEALELL-------------------KEEPFDLVLMDLQMPVMDGLEAT 61

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 15227325  91 KKVKES-AAFRSIPVVIMSSENVPARISRCLEEGAEEFFLKPVKLADLTKL 140
Cdd:cd17546  62 RRIRELeGGGRRTPIIALTANALEEDREKCLEAGMDDYLSKPVKLDQLKEV 112
REC_Rcp-like cd17557
phosphoacceptor receiver (REC) domain of cyanobacterial phytochrome response regulator Rcp and ...
 10-140 1.33e-20

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.


Pssm-ID: 381108 [Multi-domain]  Cd Length: 129  Bit Score: 83.62  E-value: 1.33e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227325  10 HVLAVDDSLFDRKMIERLLQKS--SCQVTTVDSGSKALEFLGLRvddnDPNALSTSPqihqeveiNLIITDYCMPGMTGY 87
Cdd:cd17557   1 TILLVEDNPGDAELIQEAFKEAgvPNELHVVRDGEEALDFLRGE----GEYADAPRP--------DLILLDLNMPRMDGF 68

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 15227325  88 DLLKKVKESAAFRSIPVVIMSSENVPARISRCLEEGAEEFFLKPVKLADLTKL 140
Cdd:cd17557  69 EVLREIKADPDLRRIPVVVLTTSDAEEDIERAYELGANSYIVKPVDFEEFVEA 121
YesN COG4753
Two-component response regulator, YesN/AraC family, consists of REC and AraC-type DNA-binding ...
 11-131 4.58e-19

Two-component response regulator, YesN/AraC family, consists of REC and AraC-type DNA-binding domains [Signal transduction mechanisms, Transcription];


Pssm-ID: 443786 [Multi-domain]  Cd Length: 103  Bit Score: 78.66  E-value: 4.58e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227325  11 VLAVDDSLFDRKMIERLLQKSS--CQVTTVDSGSKALEFLglrvddndpnalstspqihQEVEINLIITDYCMPGMTGYD 88
Cdd:COG4753   2 VLIVDDEPLIREGLKRILEWEAgfEVVGEAENGEEALELL-------------------EEHKPDLVITDINMPGMDGLE 62

                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 15227325  89 LLKKVKESaaFRSIPVVIMSSENVPARISRCLEEGAEEFFLKP 131
Cdd:COG4753  63 LLEAIREL--DPDTKIIILSGYSDFEYAQEAIKLGADDYLLKP 103
OmpR COG0745
DNA-binding response regulator, OmpR family, contains REC and winged-helix (wHTH) domain ...
 8-137 4.80e-19

DNA-binding response regulator, OmpR family, contains REC and winged-helix (wHTH) domain [Signal transduction mechanisms, Transcription];


Pssm-ID: 440508 [Multi-domain]  Cd Length: 204  Bit Score: 81.54  E-value: 4.80e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227325   8 KFHVLAVDDSLFDRKMIERLLQKSSCQVTTVDSGSKALEFLglrvddndpnalstspqihQEVEINLIITDYCMPGMTGY 87
Cdd:COG0745   1 MPRILVVEDDPDIRELLADALEREGYEVDTAADGEEALELL-------------------EEERPDLILLDLMLPGMDGL 61

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 15227325  88 DLLKKVKESAafRSIPVVIMSSENVPARISRCLEEGAEEFFLKPVKLADL 137
Cdd:COG0745  62 EVCRRLRARP--SDIPIIMLTARDDEEDRVRGLEAGADDYLTKPFDPEEL 109
Response_reg pfam00072
Response regulator receiver domain; This domain receives the signal from the sensor partner in ...
 11-139 3.58e-18

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.


Pssm-ID: 395025 [Multi-domain]  Cd Length: 111  Bit Score: 76.81  E-value: 3.58e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227325    11 VLAVDDSLFDRKMIERLLQKSSCQVTTVDSGSKALEFLglrvddndpnalstspqihQEVEINLIITDYCMPGMTGYDLL 90
Cdd:pfam00072   1 VLIVDDDPLIRELLRQLLEKEGYVVAEADDGKEALELL-------------------KEERPDLILLDINMPGMDGLELL 61

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 15227325    91 KKVKESAAfrSIPVVIMSSENVPARISRCLEEGAEEFFLKPVKLADLTK 139
Cdd:pfam00072  62 KRIRRRDP--TTPVIILTAHGDEDDAVEALEAGADDFLSKPFDPDELLA 108
CitB COG4565
DNA-binding response regulator DpiB of citrate/malate metabolism [Transcription, Signal ...
 7-137 1.41e-16

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


Pssm-ID: 443622 [Multi-domain]  Cd Length: 138  Bit Score: 73.47  E-value: 1.41e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227325   7 SKFHVLAVDDSLFDRKMIERLLQKSS--CQVTTVDSGSKALEFLglrvddndpnalstspqihQEVEINLIITDYCMPGM 84
Cdd:COG4565   2 KMIRVLIVEDDPMVAELLRRYLERLPgfEVVGVASSGEEALALL-------------------AEHRPDLILLDIYLPDG 62

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 15227325  85 TGYDLLKKVKEsaAFRSIPVVIMSSENVPARISRCLEEGAEEFFLKPVKLADL 137
Cdd:COG4565  63 DGLELLRELRA--RGPDVDVIVITAARDPETVREALRAGVVDYLIKPFTFERL 113
REC_RpfG-like cd17551
phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase response regulator ...
 10-132 1.88e-15

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.


Pssm-ID: 381103 [Multi-domain]  Cd Length: 118  Bit Score: 69.78  E-value: 1.88e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227325  10 HVLAVDDSLFDRKMIERLLQKSS-CQVTTVDSGSKALEFlglrvddndpnalstspqiHQEVEINLIITDYCMPGMTGYD 88
Cdd:cd17551   2 RILIVDDNPTNLLLLEALLRSAGyLEVVSFTDPREALAW-------------------CRENPPDLILLDYMMPGMDGLE 62

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 15227325  89 LLKKVKESAAFRSIPVVIMSSENVPARISRCLEEGAEEFFLKPV 132
Cdd:cd17551  63 FIRRLRALPGLEDVPIVMITADTDREVRLRALEAGATDFLTKPF 106
REC_D1_PleD-like cd17538
first (D1) phosphoacceptor receiver (REC) domain of response regulator PleD and similar ...
 10-132 2.51e-15

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.


Pssm-ID: 381093 [Multi-domain]  Cd Length: 104  Bit Score: 69.06  E-value: 2.51e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227325  10 HVLAVDDSLFDRKMIERLLQKSSCQVTTVDSGSKALEFLglrvddndpnalstspqihQEVEINLIITDYCMPGMTGYDL 89
Cdd:cd17538   1 KILVVDDEPANRELLEALLSAEGYEVLTADSGQEALALA-------------------EEELPDLILLDVMMPGMDGFEV 61

                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 15227325  90 LKKVKESAAFRSIPVVIMSSENVPARISRCLEEGAEEFFLKPV 132
Cdd:cd17538  62 CRRLKEDPETRHIPVIMITALDDREDRIRGLEAGADDFLSKPI 104
REC_CheV-like cd19924
phosphoacceptor receiver (REC) domain of chemotaxis protein CheV and similar proteins; This ...
 11-131 3.82e-15

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.


Pssm-ID: 381151 [Multi-domain]  Cd Length: 111  Bit Score: 68.94  E-value: 3.82e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227325  11 VLAVDDSLFDRKMIERLLQKSSCQVTTVDSGSKALEFL-GLRVDDNDPNAlstspqihqevEINLIITDYCMPGMTGYDL 89
Cdd:cd19924   1 ILVVDDSPTARKQLRDLLKNLGFEIAEAVDGEEALNKLeNLAKEGNDLSK-----------ELDLIITDIEMPKMDGYEL 69

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 15227325  90 LKKVKESAAFRSIPVVIMSSENVPARISRCLEEGAEEFFLKP 131
Cdd:cd19924  70 TFELRDDPRLANIPVILNSSLSGEFSRARGKKVGADAYLAKF 111
psREC_PRR cd17582
pseudo receiver domain of pseudo-response regulators; In Arabidopsis, five pseudo-response ...
 11-131 1.12e-14

pseudo receiver domain of pseudo-response regulators; In Arabidopsis, five pseudo-response regulators (PRRs), also called APRRs, comprise a core group of clock components that controls the pace of the central oscillator of the circadian clock, an endogenous time-keeping mechanism that enables organisms to adapt to external daily cycles. The coordinated sequential expression of PRR9 (APRR9), PRR7 (APRR7), PRR5 (APRR5), PRR3 (APRR3), and PRR1 (APRR1) results in circadian waves that may be at the basis of the endogenous circadian clock. PRRs contain an N-terminal pseudo receiver (psREC) domain that resembles the receiver domain of a two-component response regulator, but lacks an aspartate residue that accepts a phosphoryl group from the sensor kinase, and a CCT motif at the C-terminus that contains a putative nuclear localization signal. The psREC domain is involved in protein-protein interactions.


Pssm-ID: 381120 [Multi-domain]  Cd Length: 104  Bit Score: 67.43  E-value: 1.12e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227325  11 VLAVDDSLFDRKMIERLLQKSSCQVTTVDSGSKALEFLglrvddndpNALSTspqihqevEINLIITDYCMPGMTGYDLL 90
Cdd:cd17582   1 VLLVENDDSTRQIVTALLRKCSYEVTAASDGLQAWDVL---------EDEQN--------EIDLILTEVDLPVSSGFKLL 63

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 15227325  91 KKVKESAAFRSIPVVIMSSENVPARISRCLEEGAEEFFLKP 131
Cdd:cd17582  64 SYIMRHKICKNIPVIMMSSQDSVGVVFKCLSKGAADYLVKP 104
REC_2_GGDEF cd17544
second phosphoacceptor receiver (REC) domain of uncharacterized GGDEF domain proteins; This ...
 10-131 1.67e-14

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.


Pssm-ID: 381098 [Multi-domain]  Cd Length: 122  Bit Score: 67.54  E-value: 1.67e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227325  10 HVLAVDDSLFDRKMIERLLQKSSCQVTTVDSGSKALEFLglrvdDNDPnalstspqihqevEINLIITDYCMPGMTGYDL 89
Cdd:cd17544   2 KVLVVDDSATSRNHLRALLRRHNFQVLEAANGQEALEVL-----EQHP-------------DIKLVITDYNMPEMDGFEL 63

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 15227325  90 LKKVKESAAFRSIPVVIMSSENVPARISRCLEEGAEEFFLKP 131
Cdd:cd17544  64 VREIRKKYSRDQLAIIGISASGDNALSARFIKAGANDFLTKP 105
REC_hyHK cd17598
phosphoacceptor receiver (REC) domain of uncharacterized hybrid sensor histidine kinase ...
 11-131 1.95e-14

phosphoacceptor receiver (REC) domain of uncharacterized hybrid sensor histidine kinase/response regulators; 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/response regulators contain all the elements of a classical TCS in a single polypeptide chain. 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.


Pssm-ID: 381128 [Multi-domain]  Cd Length: 118  Bit Score: 66.97  E-value: 1.95e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227325  11 VLAVDDSLFDRKMIERLLQKSSCQVTTVDSGSKALEFLglrvddndpnalstspqihQEVEINLIITDYCMPGMTGYDLL 90
Cdd:cd17598   1 ILIVEDSPTQAEQLKHILEEQGYKVQVARNGREALAML-------------------AEHRPTLVISDIVMPEMDGYELC 61

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 15227325  91 KKVKESAAFRSIPVVIMSSENVPARISRCLEEGAEEFFLKP 131
Cdd:cd17598  62 RKIKSDPDLKDIPVILLTTLSDPRDVIRGLECGADNFITKP 102
REC_2_DhkD-like cd17580
second phosphoacceptor receiver (REC) domain of Dictyostelium discoideum hybrid signal ...
 11-140 3.83e-14

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.


Pssm-ID: 381118 [Multi-domain]  Cd Length: 112  Bit Score: 65.94  E-value: 3.83e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227325  11 VLAVDDSLFDRKMIERLLQKSSCQVTTVDSGSKALEFLglrvDDNDPNalstspqihqeveinLIITDYCMPGMTGYDLL 90
Cdd:cd17580   1 ILVVDDNEDAAEMLALLLELEGAEVTTAHSGEEALEAA----QRFRPD---------------VILSDIGMPGMDGYELA 61

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 15227325  91 KKVKESAAFRSIPVVIMSSENVPARISRCLEEGAEEFFLKPVKLADLTKL 140
Cdd:cd17580  62 RRLRELPWLANTPAIALTGYGQPEDRERALEAGFDAHLVKPVDPDELIEL 111
REC_CheY_CheY3 cd19923
phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY3 and similar CheY ...
 11-151 3.11e-13

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.


Pssm-ID: 381150 [Multi-domain]  Cd Length: 119  Bit Score: 63.90  E-value: 3.11e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227325  11 VLAVDDSLFDRKMIERLLQKSSCQ-VTTVDSGSKALEFLglrvddndpnalstspqihQEVEINLIITDYCMPGMTGYDL 89
Cdd:cd19923   3 VLVVDDFSTMRRIIKNLLKELGFNnVEEAEDGVDALEKL-------------------KAGGFDFVITDWNMPNMDGLEL 63

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15227325  90 LKKVKESAAFRSIPVVIMSSENVPARISRCLEEGAEEFFLKPvkladltkLKPHMMKTKLKK 151
Cdd:cd19923  64 LKTIRADGALSHLPVLMVTAEAKKENVIAAAQAGVNNYIVKP--------FTAATLKEKLEK 117
REC_ETR-like cd19933
phosphoacceptor receiver (REC) domain of plant ethylene receptors ETR1, ETR2, and EIN4, and ...
 11-137 5.47e-13

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.


Pssm-ID: 381160 [Multi-domain]  Cd Length: 117  Bit Score: 63.19  E-value: 5.47e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227325  11 VLAVDDSLFDRKMIERLLQKSSCQVTTVDSGSKALeflglrvddndpNALSTSPQIHQeveinLIITDYCMPGMTGYDLL 90
Cdd:cd19933   3 VLLVDDNAVNRMVTKGLLEKLGCEVTTVSSGEECL------------NLLASAEHSFQ-----LVLLDLCMPEMDGFEVA 65

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 15227325  91 KKVKESAAFRSIP-VVIMSSENVPARISRCLEEGAEEFFLKPVKLADL 137
Cdd:cd19933  66 LRIRKLFGRRERPlIVALTANTDDSTREKCLSLGMNGVITKPVSLHAL 113
REC_YesN-like cd17536
phosphoacceptor receiver (REC) domain of YesN and related helix-turn-helix containing response ...
 11-140 1.65e-12

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.


Pssm-ID: 381091 [Multi-domain]  Cd Length: 121  Bit Score: 61.97  E-value: 1.65e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227325  11 VLAVDDSLFDRKMIERLLQKSSCQVTTV---DSGSKALEFLglrvddndpnalstspqihQEVEINLIITDYCMPGMTGY 87
Cdd:cd17536   1 VLIVDDEPLIREGLKKLIDWEELGFEVVgeaENGEEALELI-------------------EEHKPDIVITDIRMPGMDGL 61

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 15227325  88 DLLKKVKESaaFRSIPVVIMSS----ENvpARisRCLEEGAEEFFLKPVKLADLTKL 140
Cdd:cd17536  62 ELIEKIREL--YPDIKIIILSGyddfEY--AQ--KAIRLGVVDYLLKPVDEEELEEA 112
REC_CheY4-like cd17562
phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY4 and similar CheY ...
 10-131 1.93e-12

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.


Pssm-ID: 381110 [Multi-domain]  Cd Length: 118  Bit Score: 61.93  E-value: 1.93e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227325  10 HVLAVDDSLFDRKMIERLLQKSSCQVTTVDSGSKALEFLglrvddndpnalstspqihQEVEINLIITDYCMPGMTGYDL 89
Cdd:cd17562   2 KILAVDDSASIRQMVSFTLRGAGYEVVEAADGRDALSKA-------------------QSKKFDLIITDQNMPNMDGIEL 62

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 15227325  90 LKKVKESAAFRSIPVVIMSSENVPARISRCLEEGAEEFFLKP 131
Cdd:cd17562  63 IKELRKLPAYKFTPILMLTTESSDEKKQEGKAAGATGWLVKP 104
REC_OmpR cd17574
phosphoacceptor receiver (REC) domain of OmpR family response regulators; OmpR-like proteins ...
 12-131 5.05e-12

phosphoacceptor receiver (REC) domain of OmpR family response regulators; OmpR-like proteins are one of the most widespread transcriptional regulators. OmpR family members contain REC and winged helix-turn-helix (wHTH) DNA-binding output effector domain. They are involved in the control of environmental stress tolerance (such as the oxidative, osmotic and acid stress response), motility, virulence, outer membrane biogenesis and other processes. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381116 [Multi-domain]  Cd Length: 99  Bit Score: 60.11  E-value: 5.05e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227325  12 LAVDDSLFDRKMIERLLQKSSCQVTTVDSGSKALEflglrvddndpnalstspqIHQEVEINLIITDYCMPGMTGYDLLK 91
Cdd:cd17574   1 LVVEDDEEIAELLSDYLEKEGYEVDTAADGEEALE-------------------LAREEQPDLIILDVMLPGMDGFEVCR 61

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 15227325  92 KVKESaaFRSIPVVIMSSENVPARISRCLEEGAEEFFLKP 131
Cdd:cd17574  62 RLREK--GSDIPIIMLTAKDEEEDKVLGLELGADDYITKP 99
REC_PA4781-like cd19920
phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase PA4781 and similar ...
 11-132 7.59e-12

phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase PA4781 and similar domains; Pseudomonas aeruginosa cyclic di-GMP phosphodiesterase PA4781 contains an N-terminal REC domain and a C-terminal catalytic HD-GYP domain, characteristics of RpfG family response regulators. PA4781 is involved in cyclic di-3',5'-GMP (c-di-GMP) hydrolysis/degradation in a two-step reaction via the linear intermediate pGpG to produce GMP. Its unphosphorylated REC domain prevents accessibility of c-di-GMP to the active site. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381147 [Multi-domain]  Cd Length: 103  Bit Score: 59.83  E-value: 7.59e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227325  11 VLAVDDSLFDRKMIERLLQKSSCQVTTVDSGSKALEFLglrvddndpnalstspqihQEVEINLIITDYCMPGMTGYDLL 90
Cdd:cd19920   1 ILIVDDVPDNLRLLSELLRAAGYRVLVATDGQQALQRA-------------------QAEPPDLILLDVMMPGMDGFEVC 61

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 15227325  91 KKVKESAAFRSIPVVIMSSENVPARISRCLEEGAEEFFLKPV 132
Cdd:cd19920  62 RRLKADPATRHIPVIFLTALTDTEDKVKGFELGAVDYITKPF 103
REC_NarL-like cd17535
phosphoacceptor receiver (REC) domain of NarL (Nitrate/Nitrite response regulator L) family ...
 11-139 1.73e-11

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.


Pssm-ID: 381090 [Multi-domain]  Cd Length: 117  Bit Score: 59.06  E-value: 1.73e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227325  11 VLAVDDSLFDRKMIERLLQKSS--CQVTTVDSGSKALEFLglrvddndpnalstspqihQEVEINLIITDYCMPGMTGYD 88
Cdd:cd17535   1 VLIVDDHPLVREGLRRLLESEPdiEVVGEAADGEEALALL-------------------RELRPDVVLMDLSMPGMDGIE 61

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 15227325  89 LLKKVKEsaAFRSIPVVIMSSENVPARISRCLEEGAEEFFLKPVKLADLTK 139
Cdd:cd17535  62 ALRRLRR--RYPDLKVIVLTAHDDPEYVLRALKAGAAGYLLKDSSPEELIE 110
REC_HupR-like cd17569
phosphoacceptor receiver (REC) domain of hydrogen uptake protein regulator (HupR) and similar ...
 11-95 6.46e-11

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.


Pssm-ID: 381113 [Multi-domain]  Cd Length: 118  Bit Score: 57.80  E-value: 6.46e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227325  11 VLAVDDSLFDRKMIERLLQKSSCQVTTVDSGSKALEFLglrvddndpnalstspqihQEVEINLIITDYCMPGMTGYDLL 90
Cdd:cd17569   3 ILLVDDEPNILKALKRLLRREGYEVLTATSGEEALEIL-------------------KQEPVDVVISDQRMPGMDGAELL 63


                ....*
gi 15227325  91 KKVKE 95
Cdd:cd17569  64 KRVRE 68
PRK15347 PRK15347
two component system sensor kinase;
8-137 6.77e-11

two component system sensor kinase;


Pssm-ID: 237951 [Multi-domain]  Cd Length: 921  Bit Score: 61.20  E-value: 6.77e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227325    8 KFHVLAVDDSLFDRKMIERLLQKSSCQVTTVDSGSKALEfLGlrvddndpnalstspqiHQEVeINLIITDYCMPGMTGY 87
Cdd:PRK15347 690 QLQILLVDDVETNRDIIGMMLVELGQQVTTAASGTEALE-LG-----------------RQHR-FDLVLMDIRMPGLDGL 750

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 15227325   88 DLLKKVKESAAFRS--IPVVIMSSENVPARISRCLEEGAEEFFLKPVKLADL 137
Cdd:PRK15347 751 ETTQLWRDDPNNLDpdCMIVALTANAAPEEIHRCKKAGMNHYLTKPVTLAQL 802
REC_OmpR_PhoB cd17618
phosphoacceptor receiver (REC) domain of PhoB response regulator from the OmpR family; The ...
 10-137 2.10e-10

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.


Pssm-ID: 381133 [Multi-domain]  Cd Length: 118  Bit Score: 56.10  E-value: 2.10e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227325  10 HVLAVDDSLFDRKMIERLLQKSSCQVTTVDSGSKALEFLglrvddndpnalstspqihQEVEINLIITDYCMPGMTGYDL 89
Cdd:cd17618   2 TILIVEDEPAIREMIAFNLERAGFDVVEAEDAESAVNLI-------------------VEPRPDLILLDWMLPGGSGIQF 62

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 15227325  90 LKKVKESAAFRSIPVVIMSSENVPARISRCLEEGAEEFFLKPVKLADL 137
Cdd:cd17618  63 IRRLKRDEMTRDIPIIMLTARGEEEDKVRGLEAGADDYITKPFSPREL 110
pleD PRK09581
response regulator PleD; Reviewed
 11-141 5.40e-10

response regulator PleD; Reviewed


Pssm-ID: 236577 [Multi-domain]  Cd Length: 457  Bit Score: 58.37  E-value: 5.40e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227325   11 VLAVDDSLFDRKMIERLLQKSSCQVTTVDSGSKALEflglrvddndpnalstspqIHQEVEINLIITDYCMPGMTGYDLL 90
Cdd:PRK09581   5 ILVVDDIPANVKLLEAKLLAEYYTVLTASSGAEAIA-------------------ICEREQPDIILLDVMMPGMDGFEVC 65

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 15227325   91 KKVKESAAFRSIPVVIMSSENVPARISRCLEEGAEEFFLKPVK-------LADLTKLK 141
Cdd:PRK09581  66 RRLKSDPATTHIPVVMVTALDDPEDRVRGLEAGADDFLTKPINdvalfarVKSLTRLK 123
REC_CheB-like cd17541
phosphoacceptor receiver (REC) domain of chemotaxis response regulator protein-glutamate ...
 11-137 5.85e-10

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.


Pssm-ID: 381096 [Multi-domain]  Cd Length: 125  Bit Score: 55.09  E-value: 5.85e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227325  11 VLAVDDSLFDRKMIERLLQKSSCQ--VTTVDSGSKALEFLG-LRVDdndpnalstspqihqeveinLIITDYCMPGMTGY 87
Cdd:cd17541   3 VLIVDDSAVMRKLLSRILESDPDIevVGTARDGEEALEKIKeLKPD--------------------VITLDIEMPVMDGL 62

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 15227325  88 DLLKKVKESaafRSIPVVIMSS---ENVPARIsRCLEEGAEEFFLKPVKLADL 137
Cdd:cd17541  63 EALRRIMAE---RPTPVVMVSSlteEGAEITL-EALELGAVDFIAKPSGGISL 111
REC_Ycf29 cd19927
phosphoacceptor receiver (REC) domain of probable transcriptional regulator Ycf29; Ycf29 is a ...
 11-108 3.90e-09

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.


Pssm-ID: 381154 [Multi-domain]  Cd Length: 102  Bit Score: 52.38  E-value: 3.90e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227325  11 VLAVDDSLFDRKMIERLLQKSSCQVTTVDSGSKALEFLGLRVddndpnalstspqihqeveINLIITDYCMPGMTGYDLL 90
Cdd:cd19927   1 ILLVDDDPGIRLAVKDYLEDQGFTVIAASNGLEALDLLNQYI-------------------PDLIISDIIMPGVDGYSLL 61

                        90
                ....*....|....*...
gi 15227325  91 KKVKESAAFRSIPVVIMS 108
Cdd:cd19927  62 GKLRKNADFDTIPVIFLT 79
AmiR COG3707
Two-component response regulator, AmiR/NasT family, consists of REC and RNA-binding ...
 11-138 7.33e-09

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


Pssm-ID: 442921 [Multi-domain]  Cd Length: 194  Bit Score: 53.42  E-value: 7.33e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227325  11 VLAVDDSLFDRKMIERLLQKSSCQV-TTVDSGSKALEflglRVDDNDPNalstspqihqeveinLIITDYCMPGMTGYDL 89
Cdd:COG3707   6 VLVVDDEPLRRADLREGLREAGYEVvAEAADGEDAVE----LVRELKPD---------------LVIVDIDMPDRDGLEA 66

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 15227325  90 LKKVKESaafRSIPVVIMSSENVPARISRCLEEGAEEFFLKPVKLADLT 138
Cdd:COG3707  67 ARQISEE---RPAPVILLTAYSDPELIERALEAGVSAYLVKPLDPEDLL 112
REC_DctD-like cd17549
phosphoacceptor receiver (REC) domain of C4-dicarboxylic acid transport protein D (DctD) and ...
 11-132 3.09e-08

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.


Pssm-ID: 381101 [Multi-domain]  Cd Length: 130  Bit Score: 50.57  E-value: 3.09e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227325  11 VLAVDDSLFDRKMIERLLQKSSCQVTTVDSGSKALEFLglrvddnDPNAlstsPQIhqeveinlIITDYCMPGMTGYDLL 90
Cdd:cd17549   1 VLLVDDDADVREALQQTLELAGFRVRAFADAEEALAAL-------SPDF----PGV--------VISDIRMPGMDGLELL 61

                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 15227325  91 KKVKESAAfrSIPVVIMSSE-NVPARIsRCLEEGAEEFFLKPV 132
Cdd:cd17549  62 AQIRELDP--DLPVILITGHgDVPMAV-EAMRAGAYDFLEKPF 101
REC_NtrC cd19919
phosphoacceptor receiver (REC) domain of DNA-binding transcriptional regulator NtrC; ...
 11-140 4.04e-08

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.


Pssm-ID: 381146 [Multi-domain]  Cd Length: 116  Bit Score: 49.96  E-value: 4.04e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227325  11 VLAVDDSLFDRKMIERLLQKSSCQVTTVDSGSKALeflglrvddndpNALSTS-PQihqeveinLIITDYCMPGMTGYDL 89
Cdd:cd19919   3 VWIVDDDSSIRWVLERALAGAGLTVTSFENAQEAL------------AALASSqPD--------VLISDIRMPGMDGLAL 62

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 15227325  90 LKKVKEsaAFRSIPVVIMSS-ENVPARISrCLEEGAEEFFLKPVKLADLTKL 140
Cdd:cd19919  63 LAQIKQ--RHPDLPVIIMTAhSDLDSAVS-AYQGGAFEYLPKPFDIDEAVAL 111
PRK10693 PRK10693
two-component system response regulator RssB;
54-141 1.44e-07

two-component system response regulator RssB;


Pssm-ID: 182652 [Multi-domain]  Cd Length: 303  Bit Score: 50.76  E-value: 1.44e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227325   54 DNDPNALSTSPQIHQEveinLIITDYCMPGMTGYDLLKKVKESAAfrSIPVVIMSSENVPARISRCLEEGAEEFFLKPVK 133
Cdd:PRK10693   4 ANGVDALELLGGFTPD----LIICDLAMPRMNGIEFVEHLRNRGD--QTPVLVISATENMADIAKALRLGVQDVLLKPVK 77


                 ....*...
gi 15227325  134 laDLTKLK 141
Cdd:PRK10693  78 --DLNRLR 83
PRK10610 PRK10610
chemotaxis protein CheY;
12-137 1.70e-07

chemotaxis protein CheY;


Pssm-ID: 170568 [Multi-domain]  Cd Length: 129  Bit Score: 48.82  E-value: 1.70e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227325   12 LAVDDSLFDRKMIERLLQKSSCQ-VTTVDSGSKALeflglrvddndpNALSTSpqihqevEINLIITDYCMPGMTGYDLL 90
Cdd:PRK10610   9 LVVDDFSTMRRIVRNLLKELGFNnVEEAEDGVDAL------------NKLQAG-------GFGFVISDWNMPNMDGLELL 69

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 15227325   91 KKVKESAAFRSIPVVIMSSENVPARISRCLEEGAEEFFLKPVKLADL 137
Cdd:PRK10610  70 KTIRADGAMSALPVLMVTAEAKKENIIAAAQAGASGYVVKPFTAATL 116
REC_CheC-like cd17593
phosphoacceptor receiver (REC) domain of uncharacterized response regulators containing a CheC ...
 9-140 1.79e-07

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.


Pssm-ID: 381124 [Multi-domain]  Cd Length: 117  Bit Score: 48.30  E-value: 1.79e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227325   9 FHVLAVDDSLFDRKMIERLLQKS-SCQVTTVDSGSKALEFLglrvddndpnalstspqihQEVEINLIITDYCMPGMTGY 87
Cdd:cd17593   1 MKVLICDDSSMARKQLARALPADwDVEITFAENGEEALEIL-------------------REGRIDVLFLDLTMPVMDGY 61

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 15227325  88 DLLKKVKESAAfrSIPVVIMSSENVPARISRCLEEGAEEFFLKPVKLADLTKL 140
Cdd:cd17593  62 EVLEALPVEQL--ETKVIVVSGDVQPEAKERVLELGALAFLKKPFDPEKLAQL 112
FixJ COG4566
DNA-binding response regulator, FixJ family, consists of REC and HTH domains [Signal ...
 14-137 1.91e-07

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


Pssm-ID: 443623 [Multi-domain]  Cd Length: 196  Bit Score: 49.71  E-value: 1.91e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227325  14 VDDslfD---RKMIERLLQKSSCQVTTVDSgskALEFLGlRVDDNDPNALstspqihqeveinliITDYCMPGMTGYDLL 90
Cdd:COG4566   5 VDD---DeavRDSLAFLLESAGLRVETFAS---AEAFLA-ALDPDRPGCL---------------LLDVRMPGMSGLELQ 62

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 15227325  91 KKVKEsaAFRSIPVVIMSSE-NVPArISRCLEEGAEEFFLKPVKLADL 137
Cdd:COG4566  63 EELAA--RGSPLPVIFLTGHgDVPM-AVRAMKAGAVDFLEKPFDDQAL 107
REC_OmpR_PrrA-like cd17627
phosphoacceptor receiver (REC) domain of PrrA-like OmpR family response regulators; The ...
 11-137 1.94e-07

phosphoacceptor receiver (REC) domain of PrrA-like OmpR family response regulators; The Mycobacterium tuberculosis PrrA is part of the PrrA/PrrB two-component system (TCS) that has been implicated in early intracellular multiplication and is essential for viability. Also included in this subfamily is Mycobacterium tuberculosis MprA, part of the MprAB TCS that regulates EspR, a key regulator of the ESX-1 secretion system, and is required for establishment and maintenance of persistent infection in a tissue- and stage-specific fashion. PrrA and MprA 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.


Pssm-ID: 381142 [Multi-domain]  Cd Length: 116  Bit Score: 48.15  E-value: 1.94e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227325  11 VLAVDDSLFDRKMIERLLQKSSCQVTTVDSGSKALEFLglrvDDNDPNalstspqihqeveinLIITDYCMPGMTGYDLL 90
Cdd:cd17627   1 ILVVDDDRAVRESLRRSLRFEGYEVETAVDGAEALRVI----SGNRPD---------------AVVLDVMMPRLDGLEVC 61

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 15227325  91 KKVKesAAFRSIPVVIMSSEN-VPARISRcLEEGAEEFFLKPVKLADL 137
Cdd:cd17627  62 RRLR--AAGNDLPILVLTARDsVSDRVAG-LDAGADDYLVKPFALEEL 106
REC_CheY cd17542
phosphoacceptor receiver (REC) domain of chemotaxis protein CheY; The chemotaxis response ...
 11-133 2.66e-07

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.


Pssm-ID: 381097 [Multi-domain]  Cd Length: 117  Bit Score: 47.66  E-value: 2.66e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227325  11 VLAVDDSLFDRKMIERLLQKSSCQVT-TVDSGSKALEflglrvddndpnalstspqIHQEVEINLIITDYCMPGMTGYDL 89
Cdd:cd17542   3 VLIVDDAAFMRMMLKDILTKAGYEVVgEAANGEEAVE-------------------KYKELKPDLVTMDITMPEMDGIEA 63

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 15227325  90 LKKVKESAAfrSIPVVIMSSENVPARISRCLEEGAEEFFLKPVK 133
Cdd:cd17542  64 LKEIKKIDP--NAKVIMCSAMGQEEMVKEAIKAGAKDFIVKPFQ 105
REC_PatA-like cd17602
phosphoacceptor receiver (REC) domain of PatA and similar domains; Nostoc sp. (or Anabaena sp.) ...
 11-131 3.03e-07

phosphoacceptor receiver (REC) domain of PatA and similar domains; Nostoc sp. (or Anabaena sp.) PatA is necessary for proper patterning of heterocysts along filaments. PatA contains phosphoacceptor REC domain at its C-terminus and an N-terminal PATAN (PatA N-terminus) domain, which was proposed in a bioinformatics study to mediate protein-protein interactions. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays. Some members of this group may have an inactive REC domain, lacking canonical metal-binding and active site residues.


Pssm-ID: 381129 [Multi-domain]  Cd Length: 102  Bit Score: 47.36  E-value: 3.03e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227325  11 VLAVDDSLFDRKMIERLLQKSSCQVTTVDSGSKALEFLglrvddndpnaLSTSPqihqeveiNLIITDYCMPGMTGYDLL 90
Cdd:cd17602   1 VACVDDRPSIQKMIEYFLEKQGFRVVVIDDPLRALTTL-----------LNSKP--------DLILIDIDMPDLDGYELC 61

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 15227325  91 KKVKESAAFRSIPVVIMS-SENVPARIsRCLEEGAEEFFLKP 131
Cdd:cd17602  62 SLLRKSSALKDTPIIMLTgKDGLVDRI-RAKMAGASGYLTKP 102
PRK10161 PRK10161
phosphate response regulator transcription factor PhoB;
73-163 3.35e-07

phosphate response regulator transcription factor PhoB;


Pssm-ID: 182277 [Multi-domain]  Cd Length: 229  Bit Score: 49.33  E-value: 3.35e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227325   73 NLIITDYCMPGMTGYDLLKKVKESAAFRSIPVVIMSSENVPARISRCLEEGAEEFFLKPVKLADLTKlkphMMKTKLKKE 152
Cdd:PRK10161  48 DLILLDWMLPGGSGIQFIKHLKRESMTRDIPVVMLTARGEEEDRVRGLETGADDYITKPFSPKELVA----RIKAVMRRI 123

                         90
                 ....*....|.
gi 15227325  153 SekPVAIEEIV 163
Cdd:PRK10161 124 S--PMAVEEVI 132
REC_CpdR_CckA-like cd18160
phosphoacceptor receiver (REC) domain of Brucella abortus CpdR and CckA, and similar domains; ...
 11-95 5.36e-07

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.


Pssm-ID: 381144 [Multi-domain]  Cd Length: 103  Bit Score: 46.73  E-value: 5.36e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227325  11 VLAVDDSLFDRKMIERLLQKSSCQVTTVDSGSKALEFLglrvddndpnalstspqiHQEVEINLIITDYCMPGMTGYDLL 90
Cdd:cd18160   2 ILLADDEPSVRKFIVTTLKKAGYAVTEAESGAEALEKL------------------QQGKDIDIVVTDIVMPEMDGIELA 63


                ....*
gi 15227325  91 KKVKE 95
Cdd:cd18160  64 REARK 68
orf27 CHL00148
Ycf27; Reviewed
 3-131 9.42e-07

Ycf27; Reviewed


Pssm-ID: 214376 [Multi-domain]  Cd Length: 240  Bit Score: 48.17  E-value: 9.42e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227325    3 METESKFHVLAVDDSLFDRKMIERLLQKSSCQVTTVDSGSKALEflglrvddndpnalstspQIHQEvEINLIITDYCMP 82
Cdd:CHL00148   1 TMENSKEKILVVDDEAYIRKILETRLSIIGYEVITASDGEEALK------------------LFRKE-QPDLVILDVMMP 61

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 15227325   83 GMTGYDLLKKVKESAafrSIPVVIMSS-ENVPARISrCLEEGAEEFFLKP 131
Cdd:CHL00148  62 KLDGYGVCQEIRKES---DVPIIMLTAlGDVSDRIT-GLELGADDYVVKP 107
REC_TrrA-like cd17554
phosphoacceptor receiver (REC) domain of Thermotoga maritima response regulator TrrA and ...
 10-109 1.30e-06

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.


Pssm-ID: 381106 [Multi-domain]  Cd Length: 113  Bit Score: 45.67  E-value: 1.30e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227325  10 HVLAVDDSLFDRKMIERLLQKSSCQVTTVDSGSKALEFLglrvDDNDPNalstspqihqeveinLIITDYCMPGMTGYDL 89
Cdd:cd17554   2 KILVVDDEENIRELYKEELEDEGYEVVTAGNGEEALEKL----ESEDPD---------------LVILDIKMPGMDGLET 62

                        90       100
                ....*....|....*....|
gi 15227325  90 LKKVKEsaAFRSIPVVIMSS 109
Cdd:cd17554  63 LRKIRE--KKPDLPVIICTA 80
REC_RcNtrC-like cd19928
phosphoacceptor receiver (REC) domain of Rhodobacter capsulatus nitrogen regulatory protein C ...
 11-131 1.47e-06

phosphoacceptor receiver (REC) domain of Rhodobacter capsulatus nitrogen regulatory protein C (NtrC) 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 NtrC, also called nitrogen regulator I (NRI), from Rhodobacter capsulatus, Azospirillum brasilense, and Azorhizobium caulinodans. NtrC is part of the NtrB/NtrC two-component system that controls the expression of the nitrogen-regulated (ntr) genes in response to nitrogen limitation. 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.


Pssm-ID: 381155 [Multi-domain]  Cd Length: 100  Bit Score: 45.19  E-value: 1.47e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227325  11 VLAVDDSLFDRKMIERLLQKSSCQVTTVdsgskaleflglrvddndPNAlSTSPQIHQEVEINLIITDYCMPGMTGYDLL 90
Cdd:cd19928   1 ILVADDDRAIRTVLTQALGRAGYEVRTT------------------GNA-ATLWRWVEEGEGDLVITDVVMPDENGLDLI 61

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 15227325  91 KKVKEsaAFRSIPVVIMSSENVPARISRCLEEGAEEFFLKP 131
Cdd:cd19928  62 PRIKK--ARPDLPIIVMSAQNTLMTAVKAAERGAFEYLPKP 100
fixJ PRK09390
response regulator FixJ; Provisional
 7-131 1.66e-06

response regulator FixJ; Provisional


Pssm-ID: 181815 [Multi-domain]  Cd Length: 202  Bit Score: 46.92  E-value: 1.66e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227325    7 SKFHVLAVDDSLFDRKMIERLLQKSSCQVTTVDSGSKALEFLGlrvddndpnalstspqihqEVEINLIITDYCMPGMTG 86
Cdd:PRK09390   2 DKGVVHVVDDDEAMRDSLAFLLDSAGFEVRLFESAQAFLDALP-------------------GLRFGCVVTDVRMPGIDG 62

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 15227325   87 YDLLKKVKESAAfrSIPVVIMSSE-NVPARIsRCLEEGAEEFFLKP 131
Cdd:PRK09390  63 IELLRRLKARGS--PLPVIVMTGHgDVPLAV-EAMKLGAVDFIEKP 105
REC_FixJ cd17537
phosphoacceptor receiver (REC) domain of FixJ family response regulators; FixJ family response ...
 9-137 1.93e-06

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.


Pssm-ID: 381092 [Multi-domain]  Cd Length: 116  Bit Score: 45.28  E-value: 1.93e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227325   9 FHVLAVDDSLFDRKMIERLLQKSSCQVTTVDSGSKALEFlglrVDDNDPNALstspqihqeveinliITDYCMPGMTGYD 88
Cdd:cd17537   1 ATVYVVDDDEAVRDSLAFLLRSVGLAVKTFTSASAFLAA----APPDQPGCL---------------VLDVRMPGMSGLE 61

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 15227325  89 LLKKVKESAAfrSIPVVIMSSE-NVPARIsRCLEEGAEEFFLKPVKLADL 137
Cdd:cd17537  62 LQDELLARGS--NIPIIFITGHgDVPMAV-EAMKAGAVDFLEKPFRDQVL 108
REC_OmpR_BsPhoP-like cd19937
phosphoacceptor receiver (REC) domain of BsPhoP-like OmpR family response regulators; Bacillus ...
 12-131 2.72e-06

phosphoacceptor receiver (REC) domain of BsPhoP-like OmpR family response regulators; Bacillus subtilis PhoP (BsPhoP) is part of the PhoPR two-component system that participates in a signal transduction network that controls adaptation of the bacteria to phosphate deficiency by regulating (activating or repressing) genes of the Pho regulon upon phosphorylation by PhoR. When activated, PhoPR directs expression of phosphate scavenging enzymes, lowers synthesis of the phosphate-rich wall teichoic acid (WTA) and initiates synthesis of teichuronic acid, a non-phosphate containing replacement anionic polymer. Members of this subfamily belong to the OmpR family of DNA-binding response regulators, which are characterized by a REC domain and a winged helix-turn-helix (wHTH) DNA-binding output effector domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381164 [Multi-domain]  Cd Length: 116  Bit Score: 44.96  E-value: 2.72e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227325  12 LAVDDSLFDRKMIERLLQKSSCQVTTVDSGSKALEflglRVDDNDPNalstspqihqeveinLIITDYCMPGMTGYDLLK 91
Cdd:cd19937   1 LVVDDEEDIVELLKYNLEKEGYEVVTAYDGEEALK----RAKDEKPD---------------LIILDLMLPGIDGLEVCR 61

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 15227325  92 KVKESAAFRSIPVVIMSSENvpARISRC--LEEGAEEFFLKP 131
Cdd:cd19937  62 ILRSDPKTSSIPIIMLTAKG--EEFDKVlgLELGADDYITKP 101
REC_RssB-like cd17555
phosphoacceptor receiver (REC) domain of Pseudomonas aeruginosa RssB and similar domains; ...
 11-137 2.78e-06

phosphoacceptor receiver (REC) domain of Pseudomonas aeruginosa RssB and similar domains; Pseudomonas aeruginosa RssB is an orphan atypical response regulator containing a REC domain and a PP2C-type protein phosphatase output domain. Its function is still unknown. Escherichia RssB, which is not included in this subfamily, is a ClpX adaptor protein which alters ClpX specificity by mediating a specific interaction between ClpX and the substrates such as RpoS, an RNA polymerase sigma factor. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381107 [Multi-domain]  Cd Length: 116  Bit Score: 44.88  E-value: 2.78e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227325  11 VLAVDDSLFDRKMIERLLQKSSCQVTTVDSGSKALEflglrvddndpnalstspqIHQEVEINLIITDYCMPGMTGYDLL 90
Cdd:cd17555   3 ILVIDDDEVVRESIAAYLEDSGFQVLQAADGRQGLE-------------------LFRSEQPDLVLCDLRMPEMDGLEVL 63

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 15227325  91 KKVKESAAfrSIPVVIMSSENVPARISRCLEEGAEEFFLKPVK-LADL 137
Cdd:cd17555  64 KQITKESP--DTPVIVVSGAGVMSDAVEALRLGAWDYLTKPIEdLAVL 109
PRK10841 PRK10841
two-component system sensor histidine kinase RcsC;
10-137 6.01e-06

two-component system sensor histidine kinase RcsC;


Pssm-ID: 182772 [Multi-domain]  Cd Length: 924  Bit Score: 46.51  E-value: 6.01e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227325   10 HVLAVDDSLFDRKMIERLLQKSSCQVTTVDSGSKALEFLglrvddndpnalstspqihQEVEINLIITDYCMPGMTGYDL 89
Cdd:PRK10841 803 MILVVDDHPINRRLLADQLGSLGYQCKTANDGVDALNVL-------------------SKNHIDIVLTDVNMPNMDGYRL 863

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 15227325   90 LKKVKESAafRSIPVVIMSSENVPARISRCLEEGAEEFFLKPVKLADL 137
Cdd:PRK10841 864 TQRLRQLG--LTLPVIGVTANALAEEKQRCLEAGMDSCLSKPVTLDVL 909
REC smart00448
cheY-homologous receiver domain; CheY regulates the clockwise rotation of E. coli flagellar ...
 10-82 8.34e-06

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.


Pssm-ID: 214668 [Multi-domain]  Cd Length: 55  Bit Score: 41.79  E-value: 8.34e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15227325     10 HVLAVDDSLFDRKMIERLLQKSSCQVTTVDSGSKALEFLglrvddndpnalstspqihQEVEINLIITDYCMP 82
Cdd:smart00448   2 RILVVDDDPLLRELLKALLEKEGYEVDEATDGEEALELL-------------------KEEKPDLILLDIMMP 55
REC_DivK-like cd17548
phosphoacceptor receiver (REC) domain of DivK and similar proteins; Caulobacter crescentus ...
 11-105 1.06e-05

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.


Pssm-ID: 381100 [Multi-domain]  Cd Length: 115  Bit Score: 43.30  E-value: 1.06e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227325  11 VLAVDDSLFDRKMIERLLQKSSCQVTTVDSGSKALEflglrvddndpnalstspqIHQEVEINLIITDYCMPGMTGYDLL 90
Cdd:cd17548   2 ILIVEDNPLNMKLARDLLESAGYEVLEAADGEEALE-------------------IARKEKPDLILMDIQLPGMDGLEAT 62

                        90
                ....*....|....*
gi 15227325  91 KKVKESAAFRSIPVV 105
Cdd:cd17548  63 RLLKEDPATRDIPVI 77
REC_RR468-like cd17552
phosphoacceptor receiver (REC) domain of Thermotoga maritima response regulator RR468 and ...
 10-107 1.51e-05

phosphoacceptor receiver (REC) domain of Thermotoga maritima response regulator RR468 and similar domains; Thermotoga maritima RR468 (encoded by gene TM0468) is the cognate response regulator (RR) of the class I histidine kinase HK853 (product of gene TM0853). HK853/RR468 comprise a two-component system (TCS) that couples environmental stimuli to adaptive responses. This subfamily also includes Fremyella diplosiphon complementary adaptation response regulator homolog RcaF, a small RR that is involved in four-step phosphorelays of the complementary chromatic adaptation (CCA) system that occurs in many cyanobacteria. Both RR468 and RcaF are stand-alone RRs 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.


Pssm-ID: 381104 [Multi-domain]  Cd Length: 121  Bit Score: 42.92  E-value: 1.51e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227325  10 HVLAVDDSLFDRKMIERLLQKSS-CQVTTVDSGSKALeflglrvddndpnalstspQIHQEVEINLIITDYCMPGMTGYD 88
Cdd:cd17552   3 RILVIDDEEDIREVVQACLEKLAgWEVLTASSGQEGL-------------------EKAATEQPDAILLDVMMPDMDGLA 63

                        90
                ....*....|....*....
gi 15227325  89 LLKKVKESAAFRSIPVVIM 107
Cdd:cd17552  64 TLKKLQANPETQSIPVILL 82
PRK11361 PRK11361
acetoacetate metabolism transcriptional regulator AtoC;
11-140 1.57e-05

acetoacetate metabolism transcriptional regulator AtoC;


Pssm-ID: 183099 [Multi-domain]  Cd Length: 457  Bit Score: 45.22  E-value: 1.57e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227325   11 VLAVDDSLFDRKMIERLLQKSSCQVTTVDSGSKALEFLGLRVDDndpnalstspqihqeveinLIITDYCMPGMTGYDLL 90
Cdd:PRK11361   7 ILIVDDEDNVRRMLSTAFALQGFETHCANNGRTALHLFADIHPD-------------------VVLMDIRMPEMDGIKAL 67

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 15227325   91 KKVKESAafRSIPVVIMSSENVPARISRCLEEGAEEFFLKPVKLADLTKL 140
Cdd:PRK11361  68 KEMRSHE--TRTPVILMTAYAEVETAVEALRCGAFDYVIKPFDLDELNLI 115
glnG PRK10923
nitrogen regulation protein NR(I); Provisional
 11-131 2.33e-05

nitrogen regulation protein NR(I); Provisional


Pssm-ID: 182842 [Multi-domain]  Cd Length: 469  Bit Score: 44.48  E-value: 2.33e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227325   11 VLAVDDSLFDRKMIERLLQKSSCQVTTVDSGSKALEFLGlrvdDNDPNALstspqihqeveinliITDYCMPGMTGYDLL 90
Cdd:PRK10923   6 VWVVDDDSSIRWVLERALAGAGLTCTTFENGNEVLEALA----SKTPDVL---------------LSDIRMPGMDGLALL 66

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 15227325   91 KKVKESAAFrsIPVVIMSSE-NVPARISrCLEEGAEEFFLKP 131
Cdd:PRK10923  67 KQIKQRHPM--LPVIIMTAHsDLDAAVS-AYQQGAFDYLPKP 105
REC_OmpR_DrrD-like cd17625
phosphoacceptor receiver (REC) domain of DrrD-like OmpR family response regulators; DrrD is a ...
 12-137 2.45e-05

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.


Pssm-ID: 381140 [Multi-domain]  Cd Length: 115  Bit Score: 42.21  E-value: 2.45e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227325  12 LAVDDSLFDRKMIERLLQKSSCQVTTVDSGSKALEFlglrvddndpnALSTspqihqevEINLIITDYCMPGMTGYDLLK 91
Cdd:cd17625   1 LVVEDEKDLSEAITKHLKKEGYTVDVCFDGEEGLEY-----------ALSG--------IYDLIILDIMLPGMDGLEVLK 61

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 15227325  92 KVKESAAfrSIPVVIMSSEN-VPARIsRCLEEGAEEFFLKPVKLADL 137
Cdd:cd17625  62 SLREEGI--ETPVLLLTALDaVEDRV-KGLDLGADDYLPKPFSLAEL 105
PRK10365 PRK10365
sigma-54-dependent response regulator transcription factor ZraR;
5-158 2.64e-05

sigma-54-dependent response regulator transcription factor ZraR;


Pssm-ID: 182412 [Multi-domain]  Cd Length: 441  Bit Score: 44.25  E-value: 2.64e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227325    5 TESKFHVLAVDDSLFDRKMIERLLQKSSCQVTTVDSGSKALEflglrvddndpnalstspQIHQEVeINLIITDYCMPGM 84
Cdd:PRK10365   2 THDNIDILVVDDDISHCTILQALLRGWGYNVALANSGRQALE------------------QVREQV-FDLVLCDVRMAEM 62

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15227325   85 TGYDLLKKVKesAAFRSIPVVIMSSENVPARISRCLEEGAEEFFLKPVKLADLTKLKPHMMKTKLKKESEKPVA 158
Cdd:PRK10365  63 DGIATLKEIK--ALNPAIPVLIMTAYSSVETAVEALKTGALDYLIKPLDFDNLQATLEKALAHTHSIDAETPAV 134
REC_NtrX-like cd17550
phosphoacceptor receiver (REC) domain of nitrogen assimilation regulatory protein NtrX and ...
 11-134 4.45e-05

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.


Pssm-ID: 381102 [Multi-domain]  Cd Length: 115  Bit Score: 41.33  E-value: 4.45e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227325  11 VLAVDDSLFDRKMIERLLQKSSCQVTTVDSGSKALEFLglrvddndpnalstspqihQEVEINLIITDYCMPGMTGYDLL 90
Cdd:cd17550   1 ILIVDDEEDIRESLSGILEDEGYEVDTAADGEEALKLI-------------------KERRPDLVLLDIWLPDMDGLELL 61

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 15227325  91 KKVKEsaAFRSIPVVIMSSEnvpARIS---RCLEEGAEEFFLKPVKL 134
Cdd:cd17550  62 KEIKE--KYPDLPVIMISGH---GTIEtavKATKLGAYDFIEKPLSL 103
REC_OmpR_MtrA-like cd17626
phosphoacceptor receiver (REC) domain of MtrA-like OmpR family response regulators; MtrA is ...
 34-137 5.10e-05

phosphoacceptor receiver (REC) domain of MtrA-like OmpR family response regulators; MtrA is part of MtrA/MtrB (or MtrAB), a highly conserved two-component system (TCS) implicated in the regulation of cell division in the actinobacteria. In unicellular Mycobacterium tuberculosis, MtrAB coordinates DNA replication with cell division and regulates the transcription of resuscitation-promoting factor B. In filamentous Streptomyces venezuelae, it links antibiotic production to sporulation. MtrA 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.


Pssm-ID: 381141 [Multi-domain]  Cd Length: 115  Bit Score: 41.30  E-value: 5.10e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227325  34 QVTTVDSGSKALEFLG--LRVDDNDPNALSTSPQI---HQEVEINLIITDYCMPGMTGYDLLKKVKESAafrSIPVVIMS 108
Cdd:cd17626   2 RILVVDDDAALAEMIGivLRGEGFDPAFCGDGTQAlaaFREVRPDLVLLDLMLPGIDGIEVCRQIRAES---GVPIVMLT 78

                        90       100
                ....*....|....*....|....*....
gi 15227325 109 SENVPARISRCLEEGAEEFFLKPVKLADL 137
Cdd:cd17626  79 AKSDTVDVVLGLESGADDYVAKPFKPKEL 107
REC_OmpR_VirG cd17594
phosphoacceptor receiver (REC) domain of VirG-like OmpR family response regulators; VirG is ...
 10-140 5.68e-05

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.


Pssm-ID: 381125 [Multi-domain]  Cd Length: 113  Bit Score: 41.28  E-value: 5.68e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227325  10 HVLAVDDSLFDRKMIERLLQKSSCQVTTVDSGSKalEFLGLRVDdndpnalstspqihqevEINLIITDYCMPGMTGYDL 89
Cdd:cd17594   1 HVLVVDDDAAMRHLLILYLRERGFDVTAAADGAE--EARLMLHR-----------------RVDLVLLDLRLGQESGLDL 61

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 15227325  90 LKKVKESAAfrsIPVVIMSSEN-VPARISRCLEEGAEEFFLKPVKLADLTKL 140
Cdd:cd17594  62 LRTIRARSD---VPIIIISGDRrDEIDRVVGLELGADDYLAKPFGLRELLAR 110
REC_OmpR_PmrA-like cd17624
phosphoacceptor receiver (REC) domain of PmrA-like OmpR family response regulators; This ...
 11-137 6.40e-05

phosphoacceptor receiver (REC) domain of PmrA-like OmpR family response regulators; This subfamily contains various OmpR family response regulators including PmrA, BasR, QseB, tctD, and RssB, which are components of two-component regulatory systems (TCSs). The PmrA/PmrB TCS controls transcription of genes that are involved in lipopolysaccharide modification in the outer membrane of bacteria, increasing bacterial resistance to host-derived antimicrobial peptides. The BasS/BasR TCS functions as an iron- and zinc-sensing transcription regulator. The QseB/QseC TCS activates the flagella regulon by activating transcription of FlhDC. The RssA/RssB TCS regulates swarming behavior in Serratia marcescens. OmpR family DNA-binding response regulators 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.


Pssm-ID: 381139 [Multi-domain]  Cd Length: 115  Bit Score: 40.93  E-value: 6.40e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227325  11 VLAVDDSLFDRKMIERLLQKSSCQVTTVDSGSKALEFLGlrvddndpnalSTSPQihqeveinLIITDYCMPGMTGYDLL 90
Cdd:cd17624   1 ILLVEDDALLGDGLKTGLRKAGYAVDWVRTGAEAEAALA-----------SGPYD--------LVILDLGLPDGDGLDLL 61

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 15227325  91 KKVKesAAFRSIPVVIMSS-ENVPARIsRCLEEGAEEFFLKPVKLADL 137
Cdd:cd17624  62 RRWR--RQGQSLPVLILTArDGVDDRV-AGLDAGADDYLVKPFALEEL 106
REC_DesR-like cd19930
phosphoacceptor receiver (REC) domain of DesR and similar proteins; This group is composed of ...
 68-137 1.32e-04

phosphoacceptor receiver (REC) domain of DesR and similar proteins; This group is composed of Bacillus subtilis DesR, Streptococcus pneumoniae response regulator spr1814, and similar proteins, all containing an N-terminal REC domain and a C-terminal LuxR family helix-turn-helix (HTH) DNA-binding output domain. DesR is a response regulator that, together with its cognate sensor kinase DesK, comprises a two-component regulatory system that controls membrane fluidity. Phosphorylation of the REC domain of DesR is allosterically coupled to two distinct exposed surfaces of the protein, controlling noncanonical dimerization/tetramerization, cooperative activation, and DesK binding. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381157 [Multi-domain]  Cd Length: 117  Bit Score: 40.33  E-value: 1.32e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227325  68 QEVEINLIITDYCMPGMTGYDLLKKVKESAAfrSIPVVIMSSENVPARISRCLEEGAEEFFLKPVKLADL 137
Cdd:cd19930  41 LKHSPDVAILDIEMPGRTGLEVAAELREELP--DTKVLIVTTFGRPGYFRRALAAGVDGYVLKDRPIEEL 108
REC_NarL cd19931
phosphoacceptor receiver (REC) domain of Nitrate/Nitrite response regulator L (NarL); Nitrate ...
 11-130 2.06e-04

phosphoacceptor receiver (REC) domain of Nitrate/Nitrite response regulator L (NarL); Nitrate/nitrite response regulator protein NarL contains an N-terminal REC domain and a C-terminal LuxR family helix-turn-helix (HTH) DNA-binding output domain. Escherichia coli NarL activates the expression of the nitrate reductase (narGHJI) and formate dehydrogenase-N (fdnGHI) operons, and represses the transcription of the fumarate reductase (frdABCD) operon in response to a nitrate/nitrite induction signal. Phosphorylation of the NarL REC domain releases the C-terminal HTH output domain that subsequently binds specific DNA promoter sites to repress or activate gene expression. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381158 [Multi-domain]  Cd Length: 117  Bit Score: 39.64  E-value: 2.06e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227325  11 VLAVDDSLFDRKMIERLLQKSS--CQVTTVDSGSKALEFlglrvddndpnALSTSPqihqeveiNLIITDYCMPGMTGYD 88
Cdd:cd19931   1 VLLIDDHPLLRKGIKQLIELDPdfTVVGEASSGEEGIEL-----------AERLDP--------DLILLDLNMKGMSGLD 61

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 15227325  89 LLKKVKESAAfrSIPVVIMSSENVPARISRCLEEGAEEFFLK 130
Cdd:cd19931  62 TLKALREEGV--SARIVILTVSDAEDDVVTALRAGADGYLLK 101
COG4567 COG4567
DNA-binding response regulator, ActR/RegA family, consists of REC and Fis-type HTH domains ...
 10-137 2.17e-04

DNA-binding response regulator, ActR/RegA family, consists of REC and Fis-type HTH domains [Signal transduction mechanisms, Transcription];


Pssm-ID: 443624 [Multi-domain]  Cd Length: 177  Bit Score: 40.67  E-value: 2.17e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227325  10 HVLAVDDSLFDRKMIERLLQKSSCQVTTVDSGSKALEflglRVDDNDPnalstspqihqeveiNLIITDYCMPGMTGYDL 89
Cdd:COG4567   6 SLLLVDDDEAFARVLARALERRGFEVTTAASVEEALA----LLEQAPP---------------DYAVLDLRLGDGSGLDL 66

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 15227325  90 LKKVKESAAfrSIPVVIMSSENVPARISRCLEEGAEEFFLKPVKLADL 137
Cdd:COG4567  67 IEALRERDP--DARIVVLTGYASIATAVEAIKLGADDYLAKPADADDL 112
PRK00742 PRK00742
chemotaxis-specific protein-glutamate methyltransferase CheB;
11-131 2.23e-04

chemotaxis-specific protein-glutamate methyltransferase CheB;


Pssm-ID: 234828 [Multi-domain]  Cd Length: 354  Bit Score: 41.29  E-value: 2.23e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227325   11 VLAVDDSLFDRKMIERLLQKSScQVTTVDS---GSKALEflglrvddndpNALSTSPQIhqeveinlIITDYCMPGMTGY 87
Cdd:PRK00742   6 VLVVDDSAFMRRLISEILNSDP-DIEVVGTapdGLEARE-----------KIKKLNPDV--------ITLDVEMPVMDGL 65

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 15227325   88 DLLKKVKESaafRSIPVVIMSS---ENvpARIS-RCLEEGAEEFFLKP 131
Cdd:PRK00742  66 DALEKIMRL---RPTPVVMVSSlteRG--AEITlRALELGAVDFVTKP 108
LytT COG3279
DNA-binding response regulator, LytR/AlgR family [Transcription, Signal transduction ...
 8-139 3.02e-04

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


Pssm-ID: 442510 [Multi-domain]  Cd Length: 235  Bit Score: 40.57  E-value: 3.02e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227325   8 KFHVLAVDDSLFDRKMIERLLQK-SSCQ-VTTVDSGSKALEFLglrvddndpnalstspqihQEVEINLIITDYCMPGMT 85
Cdd:COG3279   1 MMKILIVDDEPLARERLERLLEKyPDLEvVGEASNGEEALELL-------------------EEHKPDLVFLDIQMPGLD 61

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 15227325  86 GYDLLKKVKESAafRSIPVVIMSSEN---VPArisrcLEEGAEEFFLKPVKLADLTK 139
Cdd:COG3279  62 GFELARQLRELD--PPPPIIFTTAYDeyaLEA-----FEVNAVDYLLKPIDEERLAK 111
PRK09836 PRK09836
DNA-binding transcriptional activator CusR; Provisional
 42-137 3.18e-04

DNA-binding transcriptional activator CusR; Provisional


Pssm-ID: 182102 [Multi-domain]  Cd Length: 227  Bit Score: 40.68  E-value: 3.18e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227325   42 SKALEFLGLRVDDNDpNALsTSPQIHQEVEINLIITDYCMPGMTGYDLLKKVKesAAFRSIPVVIMSSENVPARISRCLE 121
Cdd:PRK09836  17 TKGLTEAGFVVDLAD-NGL-NGYHLAMTGDYDLIILDIMLPDVNGWDIVRMLR--SANKGMPILLLTALGTIEHRVKGLE 92

                         90
                 ....*....|....*.
gi 15227325  122 EGAEEFFLKPVKLADL 137
Cdd:PRK09836  93 LGADDYLVKPFAFAEL 108
REC_HupR cd17596
phosphoacceptor receiver (REC) domain of hydrogen uptake protein regulator (HupR); Members of ...
 11-131 5.07e-04

phosphoacceptor receiver (REC) domain of hydrogen uptake protein regulator (HupR); Members of this subfamily are response regulator components of two-component systems that regulates hydrogenase activity, including HupR and HoxA. HupR is part of the HupT/HupR system that controls the synthesis of the membrane-bound [NiFe]hydrogenase, HupSL, of the photosynthetic bacterium Rhodobacter capsulatus. It belongs to the nitrogen regulatory protein C (NtrC) family of response regulators, which activate transcription by RNA polymerase (RNAP) in response to a change in the environment. HupR is an unusual member of this family as it activates transcription when unphosphorylated, and transcription is inhibited by phosphorylation. Proteins in this subfamily contain an N-terminal REC domain, a central sigma-54 interaction domain that lacks ATPase activity, and a C-terminal DNA-binding domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381127 [Multi-domain]  Cd Length: 133  Bit Score: 38.89  E-value: 5.07e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227325  11 VLAVDDSLFDRKMIERLLQKSScQVTTVDSGSKALEFLglrvddndpnalstspqihQEVEINLIITDYCMPGMTGYDLL 90
Cdd:cd17596   3 ILVVDDEVRSLEALRRTLEEDF-DVLTAASAEEALAIL-------------------EEEWVQVILCDQRMPGTTGVEFL 62

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 15227325  91 KKVKESaaFRSIPVVIMSSENVPARISRCLEE-GAEEFFLKP 131
Cdd:cd17596  63 KEVRER--WPEVVRIIISGYTDSEDIIAGINEaGIYQYLTKP 102
REC_hyHK_blue-like cd18161
phosphoacceptor receiver (REC) domain of hybrid sensor histidine kinase/response regulators ...
 11-108 6.48e-04

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.


Pssm-ID: 381145 [Multi-domain]  Cd Length: 102  Bit Score: 38.10  E-value: 6.48e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227325  11 VLAVDDSLFDRKMIERLLQKSSCQVTTVDSGSKALEFLglrvddndpnalstspqiHQEVEINLIITDYCMPG-MTGYDL 89
Cdd:cd18161   1 VLVVEDDPDVRRLTAEVLEDLGYTVLEAASGDEALDLL------------------ESGPDIDLLVTDVIMPGgMNGSQL 62

                        90
                ....*....|....*....
gi 15227325  90 LKKVKesAAFRSIPVVIMS 108
Cdd:cd18161  63 AEEAR--RRRPDLKVLLTS 79
PRK11107 PRK11107
hybrid sensory histidine kinase BarA; Provisional
 11-105 9.35e-04

hybrid sensory histidine kinase BarA; Provisional


Pssm-ID: 236848 [Multi-domain]  Cd Length: 919  Bit Score: 39.83  E-value: 9.35e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227325   11 VLAVDDSLFDRKMIERLLQKSSCQVTTVDSGSKALEflglrvddndpnalstspqIHQEVEINLIITDYCMPGMTGYDLL 90
Cdd:PRK11107 670 VMAVDDNPANLKLIGALLEEQVEHVVLCDSGHQAVE-------------------QAKQRPFDLILMDIQMPGMDGIRAC 730

                         90
                 ....*....|....*
gi 15227325   91 KKVKESAAFRSIPVV 105
Cdd:PRK11107 731 ELIRQLPHNQNTPII 745
REC_WspR-like cd17575
phosphoacceptor receiver (REC) domain of WspR response regulator and similar proteins; The ...
 65-143 9.47e-04

phosphoacceptor receiver (REC) domain of WspR response regulator and similar proteins; The GGDEF response regulator WspR is part of the Wsp system that is homologous to chemotaxis systems and also includes the membrane-bound receptor protein WspA. In response to growth on surfaces, WspR is phosphorylated by the Wsp signal transduction complex and is activated, functioning as a diguanylate cyclase (DGC) that catalyzes c-di-GMP synthesis. WspR is a hybrid response regulator-diguanylate cyclase, containing an N-terminal REC domain and a C-terminal GGDEF domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381117 [Multi-domain]  Cd Length: 128  Bit Score: 38.16  E-value: 9.47e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227325  65 QIHQEVEINLIITDYCMPGMTGYDLLKKVKESAAFRSIPVVIMSSENVPARISRCLEEGAEEFFLK-PVKLADLTKLKPH 143
Cdd:cd17575  39 EVASQIKPTVILQDLVMPGVDGLTLVRFFRANPATRDIPIIVLSTKEEPEVKSEAFALGANDYLVKlPDKIELVARIRYH 118
PRK11517 PRK11517
DNA-binding response regulator HprR;
74-137 9.77e-04

DNA-binding response regulator HprR;


Pssm-ID: 183172 [Multi-domain]  Cd Length: 223  Bit Score: 39.11  E-value: 9.77e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15227325   74 LIITDYCMPGMTGYDLLKKVKESaafRSIPVVIMSSENVPARISRCLEEGAEEFFLKPVKLADL 137
Cdd:PRK11517  47 LIILDIMLPGMDGWQILQTLRTA---KQTPVICLTARDSVDDRVRGLDSGANDYLVKPFSFSEL 107
PRK10336 PRK10336
two-component system response regulator QseB;
75-137 9.79e-04

two-component system response regulator QseB;


Pssm-ID: 182387 [Multi-domain]  Cd Length: 219  Bit Score: 39.11  E-value: 9.79e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15227325   75 IITDYCMPGMTGYDLLKKVKESAafRSIPVVIMSSENVPARISRCLEEGAEEFFLKPVKLADL 137
Cdd:PRK10336  48 VILDLTLPGMDGRDILREWREKG--QREPVLILTARDALAERVEGLRLGADDYLCKPFALIEV 108
REC_OmpR_CusR-like cd19935
phosphoacceptor receiver (REC) domain of CusR-like OmpR family response regulators; ...
 74-131 1.76e-03

phosphoacceptor receiver (REC) domain of CusR-like OmpR family response regulators; Escherichia coli CusR is part of the CusS/CusR two-component system (TCS) that is involved in response to copper and silver. Other members of this subfamily include Escherichia coli PcoR, Pseudomonas syringae CopR, and Streptomyces coelicolor CutR, which are all transcriptional regulatory proteins and components of TCSs that regulate genes involved in copper resistance and/or metabolism. member of the subfamily is Escherichia coli HprR (hydrogen peroxide response regulator), previously called YdeW, which is part of the HprSR (or YedVW) TCS involved in stress response to hydrogen peroxide, as well as Cupriavidus metallidurans CzcR, which is part of the CzcS/CzcR TCS involved in the control of cobalt, zinc, and cadmium homeostasis. 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.


Pssm-ID: 381162 [Multi-domain]  Cd Length: 100  Bit Score: 36.65  E-value: 1.76e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 15227325  74 LIITDYCMPGMTGYDLLKKVKESAafRSIPVVIMSS-ENVPARIsRCLEEGAEEFFLKP 131
Cdd:cd19935  45 LIILDVMLPGLDGLEVLRRLRAAG--KQTPVLMLTArDSVEDRV-KGLDLGADDYLVKP 100
REC_Spo0F-like cd17553
phosphoacceptor receiver (REC) domain of Spo0F and similar domains; Spo0F, a stand-alone ...
 11-137 2.07e-03

phosphoacceptor receiver (REC) domain of Spo0F and similar domains; Spo0F, a stand-alone response regulator containing only a REC domain with no output/effector domain, controls sporulation in Bacillus subtilis through the exchange of a phosphoryl group. Bacillus subtilis forms spores when conditions for growth become unfavorable. The initiation of sporulation is controlled by a phosphorelay (an expanded version of the two-component system) that consists of four main components: a histidine kinase (KinA), a secondary messenger (Spo0F), a phosphotransferase (Spo0B), and a transcription factor (Spo0A). REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381105 [Multi-domain]  Cd Length: 117  Bit Score: 36.76  E-value: 2.07e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227325  11 VLAVDDSLFDRKMIERLLQKSSCQVTTVDSGSKALEFLGLRVDDndpnalstspqihqeveinLIITDYCMPGMTGYDLL 90
Cdd:cd17553   3 ILIVDDQYGIRILLNEVFNKEGYQTFQAANGLQALDIVTKERPD-------------------LVLLDMKIPGMDGIEIL 63

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 15227325  91 KKVKESAAfrSIPVVIMSSENVPARISRCLEEGAEEFFLKPVKLADL 137
Cdd:cd17553  64 KRMKVIDE--NIRVIIMTAYGELDMIQESKELGALTHFAKPFDIDEI 108
REC_OmpR_ArcA_TorR-like cd17619
phosphoacceptor receiver (REC) domain of ArcA- and TorR-like OmpR family response regulators; ...
 10-138 3.47e-03

phosphoacceptor receiver (REC) domain of ArcA- and TorR-like OmpR family response regulators; This subfamily includes Escherichia coli TorR and ArcA, both OmpR family response regulators that mediate adaptation to changes in various respiratory growth conditions. The TorS-TorR two-component system (TCS) is responsible for the tight regulation of the torCAD operon, which encodes the trimethylamine N-oxide (TMAO) reductase respiratory system in response to anaerobic conditions and the presence of TMAO. The ArcA-ArcB TCS is involved in cell growth during anaerobiosis. ArcA is a global regulator that controls more than 30 operons involved in redox regulation (the Arc modulon). OmpR family DNA-binding response regulators 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.


Pssm-ID: 381134 [Multi-domain]  Cd Length: 113  Bit Score: 36.21  E-value: 3.47e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227325  10 HVLAVDDSLFDRKMIERLLQKSSCQVTTVDSGSKALeflglrvddndpnalstspQIHQEVEINLIITDYCMPGMTGYDL 89
Cdd:cd17619   2 HILIVEDEPVTRATLKSYFEQEGYDVSEAGDGEEMR-------------------QILARQDIDLVLLDINLPGKDGLSL 62

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 15227325  90 LKKVKESAafrSIPVVIMSSENvpARISRC--LEEGAEEFFLKPVKLADLT 138
Cdd:cd17619  63 TRELREQS---EVGIILVTGRD--DEVDRIvgLEIGADDYVTKPFNPRELL 108
CitB COG2197
DNA-binding response regulator, NarL/FixJ family, contains REC and HTH domains [Signal ...
 10-93 4.69e-03

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


Pssm-ID: 441799 [Multi-domain]  Cd Length: 131  Bit Score: 36.02  E-value: 4.69e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227325  10 HVLAVDDSLFDRKMIERLLQKSS--CQVTTVDSGSKALEFLglrvddndpnalstspqihQEVEINLIITDYCMPGMTGY 87
Cdd:COG2197   3 RVLIVDDHPLVREGLRALLEAEPdiEVVGEAADGEEALELL-------------------EELRPDVVLLDIRMPGMDGL 63


                ....*.
gi 15227325  88 DLLKKV 93
Cdd:COG2197  64 EALRRL 69
REC_citrate_TCS cd19925
phosphoacceptor receiver (REC) domain of citrate family two-component system response ...
 68-137 6.49e-03

phosphoacceptor receiver (REC) domain of citrate family two-component system response regulators; This family includes Lactobacillus paracasei MaeR, Escherichia coli DcuR and DpiA, Klebsiella pneumoniae CitB, as well as Bacillus DctR, MalR, and CitT. These are all response regulators of two-component systems (TCSs) from the citrate family, and are involved in the transcriptional regulation of genes associated with L-malate catabolism (MaeRK), citrate-specific fermentation (DpiAB, CitAB), plasmid inheritance (DpiAB), anaerobic fumarate respiratory system (DcuRS), and malate transport/utilization (MalKR). REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381152 [Multi-domain]  Cd Length: 118  Bit Score: 35.30  E-value: 6.49e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227325  68 QEVEINLIITDYCMPGMTGYDLLKKVKesAAFRSIPVVIMSSENVPARISRCLEEGAEEFFLKPVKLADL 137
Cdd:cd19925  43 KERQPDLILLDIYLPDGNGLDLLRELR--AAGHDVDVIVVTAANDVETVREALRLGVVDYLIKPFTFERL 110
REC_OmpR_CpxR cd17623
phosphoacceptor receiver (REC) domain of CpxR-like OmpR family response regulators; CpxR is ...
 69-131 7.00e-03

phosphoacceptor receiver (REC) domain of CpxR-like OmpR family response regulators; CpxR is part of the CpxA/CpxR two-component regulatory system that mediates envelope stress responses that is key for virulence and antibiotic resistance in several Gram negative pathogens. CpxR is a transcription factor/response regulator that controls the expression of numerous genes, including those of the classical porins OmpF and OmpC. It 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.


Pssm-ID: 381138 [Multi-domain]  Cd Length: 115  Bit Score: 35.36  E-value: 7.00e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15227325  69 EVEINLIITDYCMPGMTGYDLLKKVKESAafrSIPVVIMSSENVParISRC--LEEGAEEFFLKP 131
Cdd:cd17623  40 EGSPDLVVLDVMLPKMNGLDVLKELRKTS---QVPVLMLTARGDD--IDRIlgLELGADDYLPKP 99
PRK10840 PRK10840
transcriptional regulator RcsB; Provisional
 70-148 8.27e-03

transcriptional regulator RcsB; Provisional


Pssm-ID: 182771 [Multi-domain]  Cd Length: 216  Bit Score: 36.35  E-value: 8.27e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227325   70 VEINLIITDYCMPGMT---GYDLLKKVKESAAFRSIPVVIMSseNVPARISRCLEEGAEEFFLKPVKLADLTKLKPHMMK 146
Cdd:PRK10840  48 LDAHVLITDLSMPGDKygdGITLIKYIKRHFPSLSIIVLTMN--NNPAILSAVLDLDIEGIVLKQGAPTDLPKALAALQK 125


                 ..
gi 15227325  147 TK 148
Cdd:PRK10840 126 GK 127
REC_OmpR_RegX3-like cd17621
phosphoacceptor receiver (REC) domain of RegX3-like OmpR family response regulators; RegX3 is ...
 39-131 9.95e-03

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.


Pssm-ID: 381136 [Multi-domain]  Cd Length: 99  Bit Score: 34.48  E-value: 9.95e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227325  39 DSGSKALEFLgLRVDDNDPNALSTSPQIHQEVEIN---LIITDYCMPGMTGYDLLKKVKESAafrSIPVVIMSSENVPAR 115
Cdd:cd17621   8 ESFSDPLAYL-LRKEGFEVTVATDGPAALAEFDRAgadIVLLDLMLPGLSGTEVCRQLRARS---NVPVIMVTAKDSEID 83

                        90
                ....*....|....*.
gi 15227325 116 ISRCLEEGAEEFFLKP 131
Cdd:cd17621  84 KVVGLELGADDYVTKP 99
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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