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Conserved domains on  [gi|15230202|ref|NP_191263|]
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response regulator 9 [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
1-234 4.76e-111

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: 317.75  E-value: 4.76e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230202    1 MGMAAESQFHVLAVDDSLFDRKLIERLLQKSSCQVTTVDSGSKALEFLGLRQSTDSNdPNAFSKAPVNHQVVEVNLIITD 80
Cdd:PLN03029   1 MGITTESQFHVLAVDDSLIDRKLIEKLLKTSSYQVTTVDSGSKALKFLGLHEDDRSN-PDTPSVSPNSHQEVEVNLIITD 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230202   81 YCMPGMTGYDLLKKVKESSAFRDIPVVIMSSENVPARISRCLEEGAEEFFLKPVRLADLNKLKPHMMKTKLKNQKLEEIE 160
Cdd:PLN03029  80 YCMPGMTGYDLLKKIKESSSLRNIPVVIMSSENVPSRITRCLEEGAEEFFLKPVQLSDLNRLKPHMMKTKSKNQKQENQE 159
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15230202  161 TTSKVENgvptavadPEIKDStniEIEILPLQQDLLLVQQEEQTLSINNKRKSVEEGISTDRARPRFDGIATAV 234
Cdd:PLN03029 160 KQEKLEE--------SEIQSE---KQEQPSQQPQSQPQPQQQPQQPNNNKRKAMEEGLSPDRTRPRYNGITTVV 222
 
Name Accession Description Interval E-value
PLN03029 PLN03029
type-a response regulator protein; Provisional
1-234 4.76e-111

type-a response regulator protein; Provisional


Pssm-ID: 215544 [Multi-domain]  Cd Length: 222  Bit Score: 317.75  E-value: 4.76e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230202    1 MGMAAESQFHVLAVDDSLFDRKLIERLLQKSSCQVTTVDSGSKALEFLGLRQSTDSNdPNAFSKAPVNHQVVEVNLIITD 80
Cdd:PLN03029   1 MGITTESQFHVLAVDDSLIDRKLIEKLLKTSSYQVTTVDSGSKALKFLGLHEDDRSN-PDTPSVSPNSHQEVEVNLIITD 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230202   81 YCMPGMTGYDLLKKVKESSAFRDIPVVIMSSENVPARISRCLEEGAEEFFLKPVRLADLNKLKPHMMKTKLKNQKLEEIE 160
Cdd:PLN03029  80 YCMPGMTGYDLLKKIKESSSLRNIPVVIMSSENVPSRITRCLEEGAEEFFLKPVQLSDLNRLKPHMMKTKSKNQKQENQE 159
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15230202  161 TTSKVENgvptavadPEIKDStniEIEILPLQQDLLLVQQEEQTLSINNKRKSVEEGISTDRARPRFDGIATAV 234
Cdd:PLN03029 160 KQEKLEE--------SEIQSE---KQEQPSQQPQSQPQPQQQPQQPNNNKRKAMEEGLSPDRTRPRYNGITTVV 222
REC_typeA_ARR cd17581
phosphoacceptor receiver (REC) domain of type A Arabidopsis response regulators (ARRs) and ...
11-142 6.79e-80

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: 235.34  E-value: 6.79e-80
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230202  11 VLAVDDSLFDRKLIERLLQKSSCQVTTVDSGSKALEFLGLRQSTDSndpnafskapVNHQVVEVNLIITDYCMPGMTGYD 90
Cdd:cd17581   1 VLAVDDSLVDRKVIERLLRISSCRVTAVDSGKRALEFLGLEDEEDS----------SNFNEPKVNMIITDYCMPGMTGYD 70
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 15230202  91 LLKKVKESSAFRDIPVVIMSSENVPARISRCLEEGAEEFFLKPVRLADLNKL 142
Cdd:cd17581  71 LLKKVKESSALKEIPVVIMSSENIPTRISRCLEEGAEDFLLKPVKLADVKRL 122
CheY COG0784
CheY-like REC (receiver) domain, includes chemotaxis protein CheY and sporulation regulator ...
10-139 1.45e-29

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: 107.24  E-value: 1.45e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230202  10 HVLAVDDSLFDRKLIERLLQKSSCQVTTVDSGSKALEFLglrqstdsndpnafskapvnhQVVEVNLIITDYCMPGMTGY 89
Cdd:COG0784   7 RILVVDDNPDNRELLRRLLERLGYEVTTAEDGAEALELL---------------------RAGPPDLILLDINMPGMDGL 65
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 15230202  90 DLLKKVKESSAFRDIPVVIMSSENVPARISRCLEEGAEEFFLKPVRLADL 139
Cdd:COG0784  66 ELLRRIRALPRLPDIPIIALTAYADEEDRERALEAGADDYLTKPVDPEEL 115
Response_reg pfam00072
Response regulator receiver domain; This domain receives the signal from the sensor partner in ...
11-139 1.41e-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: 77.96  E-value: 1.41e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230202    11 VLAVDDSLFDRKLIERLLQKSSCQVTTVDSGSKALEFLGLRQstdsndpnafskapvnhqvveVNLIITDYCMPGMTGYD 90
Cdd:pfam00072   1 VLIVDDDPLIRELLRQLLEKEGYVVAEADDGKEALELLKEER---------------------PDLILLDINMPGMDGLE 59
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 15230202    91 LLKKVKESSAfrDIPVVIMSSENVPARISRCLEEGAEEFFLKPVRLADL 139
Cdd:pfam00072  60 LLKRIRRRDP--TTPVIILTAHGDEDDAVEALEAGADDFLSKPFDPDEL 106
 
Name Accession Description Interval E-value
PLN03029 PLN03029
type-a response regulator protein; Provisional
1-234 4.76e-111

type-a response regulator protein; Provisional


Pssm-ID: 215544 [Multi-domain]  Cd Length: 222  Bit Score: 317.75  E-value: 4.76e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230202    1 MGMAAESQFHVLAVDDSLFDRKLIERLLQKSSCQVTTVDSGSKALEFLGLRQSTDSNdPNAFSKAPVNHQVVEVNLIITD 80
Cdd:PLN03029   1 MGITTESQFHVLAVDDSLIDRKLIEKLLKTSSYQVTTVDSGSKALKFLGLHEDDRSN-PDTPSVSPNSHQEVEVNLIITD 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230202   81 YCMPGMTGYDLLKKVKESSAFRDIPVVIMSSENVPARISRCLEEGAEEFFLKPVRLADLNKLKPHMMKTKLKNQKLEEIE 160
Cdd:PLN03029  80 YCMPGMTGYDLLKKIKESSSLRNIPVVIMSSENVPSRITRCLEEGAEEFFLKPVQLSDLNRLKPHMMKTKSKNQKQENQE 159
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15230202  161 TTSKVENgvptavadPEIKDStniEIEILPLQQDLLLVQQEEQTLSINNKRKSVEEGISTDRARPRFDGIATAV 234
Cdd:PLN03029 160 KQEKLEE--------SEIQSE---KQEQPSQQPQSQPQPQQQPQQPNNNKRKAMEEGLSPDRTRPRYNGITTVV 222
REC_typeA_ARR cd17581
phosphoacceptor receiver (REC) domain of type A Arabidopsis response regulators (ARRs) and ...
11-142 6.79e-80

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: 235.34  E-value: 6.79e-80
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230202  11 VLAVDDSLFDRKLIERLLQKSSCQVTTVDSGSKALEFLGLRQSTDSndpnafskapVNHQVVEVNLIITDYCMPGMTGYD 90
Cdd:cd17581   1 VLAVDDSLVDRKVIERLLRISSCRVTAVDSGKRALEFLGLEDEEDS----------SNFNEPKVNMIITDYCMPGMTGYD 70
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 15230202  91 LLKKVKESSAFRDIPVVIMSSENVPARISRCLEEGAEEFFLKPVRLADLNKL 142
Cdd:cd17581  71 LLKKVKESSALKEIPVVIMSSENIPTRISRCLEEGAEDFLLKPVKLADVKRL 122
CheY COG0784
CheY-like REC (receiver) domain, includes chemotaxis protein CheY and sporulation regulator ...
10-139 1.45e-29

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: 107.24  E-value: 1.45e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230202  10 HVLAVDDSLFDRKLIERLLQKSSCQVTTVDSGSKALEFLglrqstdsndpnafskapvnhQVVEVNLIITDYCMPGMTGY 89
Cdd:COG0784   7 RILVVDDNPDNRELLRRLLERLGYEVTTAEDGAEALELL---------------------RAGPPDLILLDINMPGMDGL 65
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 15230202  90 DLLKKVKESSAFRDIPVVIMSSENVPARISRCLEEGAEEFFLKPVRLADL 139
Cdd:COG0784  66 ELLRRIRALPRLPDIPIIALTAYADEEDRERALEAGADDYLTKPVDPEEL 115
PleD COG3706
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate ...
10-139 5.12e-27

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: 101.91  E-value: 5.12e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230202  10 HVLAVDDSLFDRKLIERLLQKSSCQVTTVDSGSKALEFLglrqstDSNDPNafskapvnhqvvevnLIITDYCMPGMTGY 89
Cdd:COG3706   3 RILVVDDDPTNRKLLRRLLEAAGYEVVEAADGEEALELL------QEHRPD---------------LILLDLEMPDMDGL 61
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 15230202  90 DLLKKVKESSAFRDIPVVIMSSENVPARISRCLEEGAEEFFLKPVRLADL 139
Cdd:COG3706  62 ELCRRLRADPRTADIPIIFLTALDDEEDRARALEAGADDYLTKPFDPEEL 111
RpfG COG3437
Response regulator c-di-GMP phosphodiesterase, RpfG family, contains REC and HD-GYP domains ...
3-139 3.82e-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: 101.01  E-value: 3.82e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230202   3 MAAESQFHVLAVDDSLFDRKLIERLLQKSSCQVTTVDSGSKALEFLGLRQstdsndpnafskapvnhqvveVNLIITDYC 82
Cdd:COG3437   1 MRTGQAPTVLIVDDDPENLELLRQLLRTLGYDVVTAESGEEALELLLEAP---------------------PDLILLDVR 59
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 15230202  83 MPGMTGYDLLKKVKESSAFRDIPVVIMSSENVPARISRCLEEGAEEFFLKPVRLADL 139
Cdd:COG3437  60 MPGMDGFELLRLLRADPSTRDIPVIFLTALADPEDRERALEAGADDYLTKPFDPEEL 116
REC cd00156
phosphoacceptor receiver (REC) domain of response regulators (RRs) and pseudo response ...
12-133 6.00e-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: 91.52  E-value: 6.00e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230202  12 LAVDDSLFDRKLIERLLQKSSCQVTTVDSGSKALEFLglrqstdsndpnafskapvnhQVVEVNLIITDYCMPGMTGYDL 91
Cdd:cd00156   1 LIVDDDPAIRELLKSLLEREGYEVDTAADGEEALELL---------------------REERPDLVLLDLMMPGMDGLEL 59
                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 15230202  92 LKKVKESsaFRDIPVVIMSSENVPARISRCLEEGAEEFFLKP 133
Cdd:cd00156  60 LRKLREL--PPDIPVIVLTAKADEEDAVRALELGADDYLVKP 99
REC_typeB_ARR-like cd17584
phosphoacceptor receiver (REC) domain of type B Arabidopsis response regulators (ARRs) and ...
11-139 1.36e-23

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: 91.15  E-value: 1.36e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230202  11 VLAVDDSLFDRKLIERLLQKSSCQVTTVDSGSKALEFLglrqstdSNDPNafskapvnhqvvEVNLIITDYCMPGMTGYD 90
Cdd:cd17584   1 VLVVDDDPTCLAILKRMLLRCGYQVTTCTDAEEALSML-------RENKD------------EFDLVITDVHMPDMDGFE 61
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 15230202  91 LLKKVKESsafRDIPVVIMSSENVPARISRCLEEGAEEFFLKPVRLADL 139
Cdd:cd17584  62 FLELIRLE---MDLPVIMMSADGSTSTVMKGLAHGACDYLLKPVSIEDL 107
REC_Rcp-like cd17557
phosphoacceptor receiver (REC) domain of cyanobacterial phytochrome response regulator Rcp and ...
10-142 1.21e-22

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: 89.01  E-value: 1.21e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230202  10 HVLAVDDSLFDRKLIERLLQKS--SCQVTTVDSGSKALEFLglrqstdsNDPNAFSKAPVnhqvveVNLIITDYCMPGMT 87
Cdd:cd17557   1 TILLVEDNPGDAELIQEAFKEAgvPNELHVVRDGEEALDFL--------RGEGEYADAPR------PDLILLDLNMPRMD 66
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 15230202  88 GYDLLKKVKESSAFRDIPVVIMSSENVPARISRCLEEGAEEFFLKPVRLADLNKL 142
Cdd:cd17557  67 GFEVLREIKADPDLRRIPVVVLTTSDAEEDIERAYELGANSYIVKPVDFEEFVEA 121
REC_hyHK_CKI1_RcsC-like cd17546
phosphoacceptor receiver (REC) domain of hybrid sensor histidine kinases/response regulators ...
11-139 3.23e-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: 3.23e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230202  11 VLAVDDSLFDRKLIERLLQKSSCQVTTVDSGSKALEflglrqstdsndpnAFSKAPvnhqvveVNLIITDYCMPGMTGYD 90
Cdd:cd17546   1 VLVVDDNPVNRKVLKKLLEKLGYEVDVAENGQEALE--------------LLKEEP-------FDLVLMDLQMPVMDGLE 59
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 15230202  91 LLKKVKES-SAFRDIPVVIMSSENVPARISRCLEEGAEEFFLKPVRLADL 139
Cdd:cd17546  60 ATRRIRELeGGGRRTPIIALTANALEEDREKCLEAGMDDYLSKPVKLDQL 109
AtoC COG2204
DNA-binding transcriptional response regulator, NtrC family, contains REC, AAA-type ATPase, ...
7-139 3.39e-21

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: 90.79  E-value: 3.39e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230202   7 SQFHVLAVDDSLFDRKLIERLLQKSSCQVTTVDSGSKALEFLGLRQstdsndpnafskapvnhqvveVNLIITDYCMPGM 86
Cdd:COG2204   1 SMARILVVDDDPDIRRLLKELLERAGYEVETAASGEEALALLREEP---------------------PDLVLLDLRMPGM 59
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 15230202  87 TGYDLLKKVKEssAFRDIPVVIMSSENVPARISRCLEEGAEEFFLKPVRLADL 139
Cdd:COG2204  60 DGLELLRELRA--LDPDLPVILLTGYGDVETAVEAIKAGAFDYLTKPFDLEEL 110
OmpR COG0745
DNA-binding response regulator, OmpR family, contains REC and winged-helix (wHTH) domain ...
10-139 1.62e-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: 83.08  E-value: 1.62e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230202  10 HVLAVDDSLFDRKLIERLLQKSSCQVTTVDSGSKALEFLglrqstDSNDPnafskapvnhqvvevNLIITDYCMPGMTGY 89
Cdd:COG0745   3 RILVVEDDPDIRELLADALEREGYEVDTAADGEEALELL------EEERP---------------DLILLDLMLPGMDGL 61
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 15230202  90 DLLKKVKESSafRDIPVVIMSSENVPARISRCLEEGAEEFFLKPVRLADL 139
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 1.41e-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: 77.96  E-value: 1.41e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230202    11 VLAVDDSLFDRKLIERLLQKSSCQVTTVDSGSKALEFLGLRQstdsndpnafskapvnhqvveVNLIITDYCMPGMTGYD 90
Cdd:pfam00072   1 VLIVDDDPLIRELLRQLLEKEGYVVAEADDGKEALELLKEER---------------------PDLILLDINMPGMDGLE 59
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 15230202    91 LLKKVKESSAfrDIPVVIMSSENVPARISRCLEEGAEEFFLKPVRLADL 139
Cdd:pfam00072  60 LLKRIRRRDP--TTPVIILTAHGDEDDAVEALEAGADDFLSKPFDPDEL 106
YesN COG4753
Two-component response regulator, YesN/AraC family, consists of REC and AraC-type DNA-binding ...
11-133 2.08e-18

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: 77.51  E-value: 2.08e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230202  11 VLAVDDSLFDRKLIERLLQKSS--CQVTTVDSGSKALEFLGLRQstdsndpnafskapvnhqvveVNLIITDYCMPGMTG 88
Cdd:COG4753   2 VLIVDDEPLIREGLKRILEWEAgfEVVGEAENGEEALELLEEHK---------------------PDLVITDINMPGMDG 60
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 15230202  89 YDLLKKVKESsaFRDIPVVIMSSENVPARISRCLEEGAEEFFLKP 133
Cdd:COG4753  61 LELLEAIREL--DPDTKIIILSGYSDFEYAQEAIKLGADDYLLKP 103
REC_RpfG-like cd17551
phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase response regulator ...
10-134 2.07e-16

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: 72.47  E-value: 2.07e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230202  10 HVLAVDDSLFDRKLIERLLQKSS-CQVTTVDSGSKALEFLglrqstDSNDPNafskapvnhqvvevnLIITDYCMPGMTG 88
Cdd:cd17551   2 RILIVDDNPTNLLLLEALLRSAGyLEVVSFTDPREALAWC------RENPPD---------------LILLDYMMPGMDG 60
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 15230202  89 YDLLKKVKESSAFRDIPVVIMSSENVPARISRCLEEGAEEFFLKPV 134
Cdd:cd17551  61 LEFIRRLRALPGLEDVPIVMITADTDREVRLRALEAGATDFLTKPF 106
CitB COG4565
DNA-binding response regulator DpiB of citrate/malate metabolism [Transcription, Signal ...
7-139 2.81e-16

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


Pssm-ID: 443622 [Multi-domain]  Cd Length: 138  Bit Score: 72.69  E-value: 2.81e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230202   7 SQFHVLAVDDSLFDRKLIERLLQKSS--CQVTTVDSGSKALEFLglrqstdsndpnafskapvnhQVVEVNLIITDYCMP 84
Cdd:COG4565   2 KMIRVLIVEDDPMVAELLRRYLERLPgfEVVGVASSGEEALALL---------------------AEHRPDLILLDIYLP 60
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 15230202  85 GMTGYDLLKKVKEssAFRDIPVVIMSSENVPARISRCLEEGAEEFFLKPVRLADL 139
Cdd:COG4565  61 DGDGLELLRELRA--RGPDVDVIVITAARDPETVREALRAGVVDYLIKPFTFERL 113
REC_D1_PleD-like cd17538
first (D1) phosphoacceptor receiver (REC) domain of response regulator PleD and similar ...
10-134 3.25e-16

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: 71.76  E-value: 3.25e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230202  10 HVLAVDDSLFDRKLIERLLQKSSCQVTTVDSGSKALEFLgLRQSTDsndpnafskapvnhqvvevnLIITDYCMPGMTGY 89
Cdd:cd17538   1 KILVVDDEPANRELLEALLSAEGYEVLTADSGQEALALA-EEELPD--------------------LILLDVMMPGMDGF 59
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 15230202  90 DLLKKVKESSAFRDIPVVIMSSENVPARISRCLEEGAEEFFLKPV 134
Cdd:cd17538  60 EVCRRLKEDPETRHIPVIMITALDDREDRIRGLEAGADDFLSKPI 104
REC_hyHK cd17598
phosphoacceptor receiver (REC) domain of uncharacterized hybrid sensor histidine kinase ...
11-133 4.05e-16

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: 71.59  E-value: 4.05e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230202  11 VLAVDDSLFDRKLIERLLQKSSCQVTTVDSGSKALEFLGLRQSTdsndpnafskapvnhqvvevnLIITDYCMPGMTGYD 90
Cdd:cd17598   1 ILIVEDSPTQAEQLKHILEEQGYKVQVARNGREALAMLAEHRPT---------------------LVISDIVMPEMDGYE 59
                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 15230202  91 LLKKVKESSAFRDIPVVIMSSENVPARISRCLEEGAEEFFLKP 133
Cdd:cd17598  60 LCRKIKSDPDLKDIPVILLTTLSDPRDVIRGLECGADNFITKP 102
psREC_PRR cd17582
pseudo receiver domain of pseudo-response regulators; In Arabidopsis, five pseudo-response ...
11-133 1.87e-15

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: 69.74  E-value: 1.87e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230202  11 VLAVDDSLFDRKLIERLLQKSSCQVTTVDSGSKALEFLGLRQStdsndpnafskapvnhqvvEVNLIITDYCMPGMTGYD 90
Cdd:cd17582   1 VLLVENDDSTRQIVTALLRKCSYEVTAASDGLQAWDVLEDEQN-------------------EIDLILTEVDLPVSSGFK 61
                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 15230202  91 LLKKVKESSAFRDIPVVIMSSENVPARISRCLEEGAEEFFLKP 133
Cdd:cd17582  62 LLSYIMRHKICKNIPVIMMSSQDSVGVVFKCLSKGAADYLVKP 104
REC_CheV-like cd19924
phosphoacceptor receiver (REC) domain of chemotaxis protein CheV and similar proteins; This ...
11-133 8.16e-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: 68.17  E-value: 8.16e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230202  11 VLAVDDSLFDRKLIERLLQKSSCQVTTVDSGSKALEFLGLRQSTDSNdpnafskapVNHqvvEVNLIITDYCMPGMTGYD 90
Cdd:cd19924   1 ILVVDDSPTARKQLRDLLKNLGFEIAEAVDGEEALNKLENLAKEGND---------LSK---ELDLIITDIEMPKMDGYE 68
                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 15230202  91 LLKKVKESSAFRDIPVVIMSSENVPARISRCLEEGAEEFFLKP 133
Cdd:cd19924  69 LTFELRDDPRLANIPVILNSSLSGEFSRARGKKVGADAYLAKF 111
PRK15347 PRK15347
two component system sensor kinase;
8-140 9.95e-14

two component system sensor kinase;


Pssm-ID: 237951 [Multi-domain]  Cd Length: 921  Bit Score: 70.06  E-value: 9.95e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230202    8 QFHVLAVDDSLFDRKLIERLLQKSSCQVTTVDSGSKALEfLGLRQSTDsndpnafskapvnhqvvevnLIITDYCMPGMT 87
Cdd:PRK15347 690 QLQILLVDDVETNRDIIGMMLVELGQQVTTAASGTEALE-LGRQHRFD--------------------LVLMDIRMPGLD 748
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 15230202   88 GYDLLKKVKESSAFRD--IPVVIMSSENVPARISRCLEEGAEEFFLKPVRLADLN 140
Cdd:PRK15347 749 GLETTQLWRDDPNNLDpdCMIVALTANAAPEEIHRCKKAGMNHYLTKPVTLAQLA 803
REC_2_GGDEF cd17544
second phosphoacceptor receiver (REC) domain of uncharacterized GGDEF domain proteins; This ...
10-133 1.24e-13

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: 65.23  E-value: 1.24e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230202  10 HVLAVDDSLFDRKLIERLLQKSSCQVTTVDSGSKALEFLGlrqstdsNDPnafskapvnhqvvEVNLIITDYCMPGMTGY 89
Cdd:cd17544   2 KVLVVDDSATSRNHLRALLRRHNFQVLEAANGQEALEVLE-------QHP-------------DIKLVITDYNMPEMDGF 61
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 15230202  90 DLLKKVKESSAFRDIPVVIMSSENVPARISRCLEEGAEEFFLKP 133
Cdd:cd17544  62 ELVREIRKKYSRDQLAIIGISASGDNALSARFIKAGANDFLTKP 105
REC_CheY_CheY3 cd19923
phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY3 and similar CheY ...
11-133 2.54e-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: 64.28  E-value: 2.54e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230202  11 VLAVDDSLFDRKLIERLLQKSSCQ-VTTVDSGSKALEFLglrqstDSNDpnafskapvnhqvveVNLIITDYCMPGMTGY 89
Cdd:cd19923   3 VLVVDDFSTMRRIIKNLLKELGFNnVEEAEDGVDALEKL------KAGG---------------FDFVITDWNMPNMDGL 61
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 15230202  90 DLLKKVKESSAFRDIPVVIMSSENVPARISRCLEEGAEEFFLKP 133
Cdd:cd19923  62 ELLKTIRADGALSHLPVLMVTAEAKKENVIAAAQAGVNNYIVKP 105
REC_ETR-like cd19933
phosphoacceptor receiver (REC) domain of plant ethylene receptors ETR1, ETR2, and EIN4, and ...
11-139 2.66e-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: 64.34  E-value: 2.66e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230202  11 VLAVDDSLFDRKLIERLLQKSSCQVTTVDSGSKALeflglrqstdsndpNAFSKAPVNHQVVevnliITDYCMPGMTGYD 90
Cdd:cd19933   3 VLLVDDNAVNRMVTKGLLEKLGCEVTTVSSGEECL--------------NLLASAEHSFQLV-----LLDLCMPEMDGFE 63
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 15230202  91 LLKKVKESSAFRDIP-VVIMSSENVPARISRCLEEGAEEFFLKPVRLADL 139
Cdd:cd19933  64 VALRIRKLFGRRERPlIVALTANTDDSTREKCLSLGMNGVITKPVSLHAL 113
REC_2_DhkD-like cd17580
second phosphoacceptor receiver (REC) domain of Dictyostelium discoideum hybrid signal ...
11-142 4.94e-12

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: 60.55  E-value: 4.94e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230202  11 VLAVDDSLFDRKLIERLLQKSSCQVTTVDSGSKALEFLglrqstDSNDPNafskapvnhqvvevnLIITDYCMPGMTGYD 90
Cdd:cd17580   1 ILVVDDNEDAAEMLALLLELEGAEVTTAHSGEEALEAA------QRFRPD---------------VILSDIGMPGMDGYE 59
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 15230202  91 LLKKVKESSAFRDIPVVIMSSENVPARISRCLEEGAEEFFLKPVRLADLNKL 142
Cdd:cd17580  60 LARRLRELPWLANTPAIALTGYGQPEDRERALEAGFDAHLVKPVDPDELIEL 111
REC_YesN-like cd17536
phosphoacceptor receiver (REC) domain of YesN and related helix-turn-helix containing response ...
11-142 5.61e-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: 60.81  E-value: 5.61e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230202  11 VLAVDDSLFDRKLIERLLQKSSCQVTTV---DSGSKALEFLglrqstdsndpnafskapvnhQVVEVNLIITDYCMPGMT 87
Cdd:cd17536   1 VLIVDDEPLIREGLKKLIDWEELGFEVVgeaENGEEALELI---------------------EEHKPDIVITDIRMPGMD 59
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 15230202  88 GYDLLKKVKESsaFRDIPVVIMSS----ENvpARisRCLEEGAEEFFLKPVRLADLNKL 142
Cdd:cd17536  60 GLELIEKIREL--YPDIKIIILSGyddfEY--AQ--KAIRLGVVDYLLKPVDEEELEEA 112
REC_PA4781-like cd19920
phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase PA4781 and similar ...
11-134 7.20e-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: 7.20e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230202  11 VLAVDDSLFDRKLIERLLQKSSCQVTTVDSGSKALEFLglrqstdsndpnafskapvnhQVVEVNLIITDYCMPGMTGYD 90
Cdd:cd19920   1 ILIVDDVPDNLRLLSELLRAAGYRVLVATDGQQALQRA---------------------QAEPPDLILLDVMMPGMDGFE 59
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 15230202  91 LLKKVKESSAFRDIPVVIMSSENVPARISRCLEEGAEEFFLKPV 134
Cdd:cd19920  60 VCRRLKADPATRHIPVIFLTALTDTEDKVKGFELGAVDYITKPF 103
REC_OmpR cd17574
phosphoacceptor receiver (REC) domain of OmpR family response regulators; OmpR-like proteins ...
12-133 9.08e-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: 59.73  E-value: 9.08e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230202  12 LAVDDSLFDRKLIERLLQKSSCQVTTVDSGSKALEFLglrqstDSNDPNafskapvnhqvvevnLIITDYCMPGMTGYDL 91
Cdd:cd17574   1 LVVEDDEEIAELLSDYLEKEGYEVDTAADGEEALELA------REEQPD---------------LIILDVMLPGMDGFEV 59
                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 15230202  92 LKKVKESSafRDIPVVIMSSENVPARISRCLEEGAEEFFLKP 133
Cdd:cd17574  60 CRRLREKG--SDIPIIMLTAKDEEEDKVLGLELGADDYITKP 99
REC_CheY4-like cd17562
phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY4 and similar CheY ...
10-133 2.04e-11

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: 59.24  E-value: 2.04e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230202  10 HVLAVDDSLFDRKLIERLLQKSSCQVTTVDSGSKALeflglrqstdsndpnafSKApvnhQVVEVNLIITDYCMPGMTGY 89
Cdd:cd17562   2 KILAVDDSASIRQMVSFTLRGAGYEVVEAADGRDAL-----------------SKA----QSKKFDLIITDQNMPNMDGI 60
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 15230202  90 DLLKKVKESSAFRDIPVVIMSSENVPARISRCLEEGAEEFFLKP 133
Cdd:cd17562  61 ELIKELRKLPAYKFTPILMLTTESSDEKKQEGKAAGATGWLVKP 104
REC_NarL-like cd17535
phosphoacceptor receiver (REC) domain of NarL (Nitrate/Nitrite response regulator L) family ...
11-139 6.85e-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: 57.52  E-value: 6.85e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230202  11 VLAVDDSLFDRKLIERLLQKSS--CQVTTVDSGSKALEFLGLRQstdsndpnafskapvnhqvveVNLIITDYCMPGMTG 88
Cdd:cd17535   1 VLIVDDHPLVREGLRRLLESEPdiEVVGEAADGEEALALLRELR---------------------PDVVLMDLSMPGMDG 59
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 15230202  89 YDLLKKVKesSAFRDIPVVIMSSENVPARISRCLEEGAEEFFLKPVRLADL 139
Cdd:cd17535  60 IEALRRLR--RRYPDLKVIVLTAHDDPEYVLRALKAGAAGYLLKDSSPEEL 108
REC_HupR-like cd17569
phosphoacceptor receiver (REC) domain of hydrogen uptake protein regulator (HupR) and similar ...
11-108 2.81e-10

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: 55.87  E-value: 2.81e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230202  11 VLAVDDSLFDRKLIERLLQKSSCQVTTVDSGSKALEFLglRQStdsndpnafskapvnhqvvEVNLIITDYCMPGMTGYD 90
Cdd:cd17569   3 ILLVDDEPNILKALKRLLRREGYEVLTATSGEEALEIL--KQE-------------------PVDVVISDQRMPGMDGAE 61
                        90       100
                ....*....|....*....|....*..
gi 15230202  91 LLKKVKES---------SAFRDIPVVI 108
Cdd:cd17569  62 LLKRVRERypdtvrillTGYADLDAAI 88
REC_OmpR_PhoB cd17618
phosphoacceptor receiver (REC) domain of PhoB response regulator from the OmpR family; The ...
10-139 3.49e-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: 55.72  E-value: 3.49e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230202  10 HVLAVDDSLFDRKLIERLLQKSSCQVTTVDSGSKALEFLglrqstdsNDPNAfskapvnhqvvevNLIITDYCMPGMTGY 89
Cdd:cd17618   2 TILIVEDEPAIREMIAFNLERAGFDVVEAEDAESAVNLI--------VEPRP-------------DLILLDWMLPGGSGI 60
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 15230202  90 DLLKKVKESSAFRDIPVVIMSSENVPARISRCLEEGAEEFFLKPVRLADL 139
Cdd:cd17618  61 QFIRRLKRDEMTRDIPIIMLTARGEEEDKVRGLEAGADDYITKPFSPREL 110
REC_CheB-like cd17541
phosphoacceptor receiver (REC) domain of chemotaxis response regulator protein-glutamate ...
11-140 1.87e-09

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: 53.93  E-value: 1.87e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230202  11 VLAVDDSLFDRKLIERLLQKSSCQ--VTTVDSGSKALEFLglrqstDSNDPNafskapvnhqvvevnLIITDYCMPGMTG 88
Cdd:cd17541   3 VLIVDDSAVMRKLLSRILESDPDIevVGTARDGEEALEKI------KELKPD---------------VITLDIEMPVMDG 61
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 15230202  89 YDLLKKVKESsafRDIPVVIMSS---ENVPARIsRCLEEGAEEFFLKPVRLADLN 140
Cdd:cd17541  62 LEALRRIMAE---RPTPVVMVSSlteEGAEITL-EALELGAVDFIAKPSGGISLD 112
REC_DctD-like cd17549
phosphoacceptor receiver (REC) domain of C4-dicarboxylic acid transport protein D (DctD) and ...
11-134 6.21e-09

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: 52.49  E-value: 6.21e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230202  11 VLAVDDSLFDRKLIERLLQKSSCQVTTVDSGSKALEFLglrqSTDSNDpnafskapvnhqvvevnLIITDYCMPGMTGYD 90
Cdd:cd17549   1 VLLVDDDADVREALQQTLELAGFRVRAFADAEEALAAL----SPDFPG-----------------VVISDIRMPGMDGLE 59
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 15230202  91 LLKKVKESSAfrDIPVVIMSSE-NVPARIsRCLEEGAEEFFLKPV 134
Cdd:cd17549  60 LLAQIRELDP--DLPVILITGHgDVPMAV-EAMRAGAYDFLEKPF 101
pleD PRK09581
response regulator PleD; Reviewed
11-143 6.28e-09

response regulator PleD; Reviewed


Pssm-ID: 236577 [Multi-domain]  Cd Length: 457  Bit Score: 55.29  E-value: 6.28e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230202   11 VLAVDDSLFDRKLIERLLQKSSCQVTTVDSGSKALEFLglrqstdsndpnafskapvnhQVVEVNLIITDYCMPGMTGYD 90
Cdd:PRK09581   5 ILVVDDIPANVKLLEAKLLAEYYTVLTASSGAEAIAIC---------------------EREQPDIILLDVMMPGMDGFE 63
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230202   91 LLKKVKESSAFRDIPVVIMSSENVPARISRCLEEGAEEFFLKPV-------RLADLNKLK 143
Cdd:PRK09581  64 VCRRLKSDPATTHIPVVMVTALDDPEDRVRGLEAGADDFLTKPIndvalfaRVKSLTRLK 123
AmiR COG3707
Two-component response regulator, AmiR/NasT family, consists of REC and RNA-binding ...
11-139 2.54e-08

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: 52.27  E-value: 2.54e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230202  11 VLAVDDSLFDRKLIERLLQKSSCQV-TTVDSGSKALEfLGLRQSTDsndpnafskapvnhqvvevnLIITDYCMPGMTGY 89
Cdd:COG3707   6 VLVVDDEPLRRADLREGLREAGYEVvAEAADGEDAVE-LVRELKPD--------------------LVIVDIDMPDRDGL 64
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 15230202  90 DLLKKVKESsafRDIPVVIMSSENVPARISRCLEEGAEEFFLKPVRLADL 139
Cdd:COG3707  65 EAARQISEE---RPAPVILLTAYSDPELIERALEAGVSAYLVKPLDPEDL 111
REC_TrrA-like cd17554
phosphoacceptor receiver (REC) domain of Thermotoga maritima response regulator TrrA and ...
10-111 2.65e-08

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: 50.68  E-value: 2.65e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230202  10 HVLAVDDSLFDRKLIERLLQKSSCQVTTVDSGSKALEFLglrqstDSNDPNafskapvnhqvvevnLIITDYCMPGMTGY 89
Cdd:cd17554   2 KILVVDDEENIRELYKEELEDEGYEVVTAGNGEEALEKL------ESEDPD---------------LVILDIKMPGMDGL 60
                        90       100
                ....*....|....*....|..
gi 15230202  90 DLLKKVKEssAFRDIPVVIMSS 111
Cdd:cd17554  61 ETLRKIRE--KKPDLPVIICTA 80
REC_NtrC cd19919
phosphoacceptor receiver (REC) domain of DNA-binding transcriptional regulator NtrC; ...
11-133 3.57e-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: 50.35  E-value: 3.57e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230202  11 VLAVDDSLFDRKLIERLLQKSSCQVTTVDSGSKALEFLGlrqstdsndpnafSKAPvnhqvvevNLIITDYCMPGMTGYD 90
Cdd:cd19919   3 VWIVDDDSSIRWVLERALAGAGLTVTSFENAQEALAALA-------------SSQP--------DVLISDIRMPGMDGLA 61
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 15230202  91 LLKKVKEssAFRDIPVVIMSS-ENVPARISrCLEEGAEEFFLKP 133
Cdd:cd19919  62 LLAQIKQ--RHPDLPVIIMTAhSDLDSAVS-AYQGGAFEYLPKP 102
FixJ COG4566
DNA-binding response regulator, FixJ family, consists of REC and HTH domains [Signal ...
14-139 3.59e-08

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: 51.64  E-value: 3.59e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230202  14 VDDslfD---RKLIERLLQKSSCQVTTVDSgskALEFLglrqstDSNDPNAFSkapvnhqvvevnLIITDYCMPGMTGYD 90
Cdd:COG4566   5 VDD---DeavRDSLAFLLESAGLRVETFAS---AEAFL------AALDPDRPG------------CLLLDVRMPGMSGLE 60
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 15230202  91 LLKKVKEssAFRDIPVVIMSSE-NVPArISRCLEEGAEEFFLKPVRLADL 139
Cdd:COG4566  61 LQEELAA--RGSPLPVIFLTGHgDVPM-AVRAMKAGAVDFLEKPFDDQAL 107
REC_Ycf29 cd19927
phosphoacceptor receiver (REC) domain of probable transcriptional regulator Ycf29; Ycf29 is a ...
11-110 4.87e-08

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: 49.68  E-value: 4.87e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230202  11 VLAVDDSLFDRKLIERLLQKSSCQVTTVDSGSKALEFLGLRQstdsndpnafskapvnhqvveVNLIITDYCMPGMTGYD 90
Cdd:cd19927   1 ILLVDDDPGIRLAVKDYLEDQGFTVIAASNGLEALDLLNQYI---------------------PDLIISDIIMPGVDGYS 59
                        90       100
                ....*....|....*....|
gi 15230202  91 LLKKVKESSAFRDIPVVIMS 110
Cdd:cd19927  60 LLGKLRKNADFDTIPVIFLT 79
REC_FixJ cd17537
phosphoacceptor receiver (REC) domain of FixJ family response regulators; FixJ family response ...
9-139 1.10e-07

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: 48.74  E-value: 1.10e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230202   9 FHVLAVDDSLFDRKLIERLLQKSSCQVTTVDSGSkalEFLglrqstDSNDPNAFSkapvnhqvvevnLIITDYCMPGMTG 88
Cdd:cd17537   1 ATVYVVDDDEAVRDSLAFLLRSVGLAVKTFTSAS---AFL------AAAPPDQPG------------CLVLDVRMPGMSG 59
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 15230202  89 YDLLKKVKESSAfrDIPVVIMSSE-NVPARIsRCLEEGAEEFFLKPVRLADL 139
Cdd:cd17537  60 LELQDELLARGS--NIPIIFITGHgDVPMAV-EAMKAGAVDFLEKPFRDQVL 108
PRK10610 PRK10610
chemotaxis protein CheY;
5-141 2.20e-07

chemotaxis protein CheY;


Pssm-ID: 170568 [Multi-domain]  Cd Length: 129  Bit Score: 48.43  E-value: 2.20e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230202    5 AESQFHVLAVDDSLFDRKLIERLLqksscqvttvdsgsKALEFLGLRQSTDSNDpnAFSKApvnhQVVEVNLIITDYCMP 84
Cdd:PRK10610   2 ADKELKFLVVDDFSTMRRIVRNLL--------------KELGFNNVEEAEDGVD--ALNKL----QAGGFGFVISDWNMP 61
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 15230202   85 GMTGYDLLKKVKESSAFRDIPVVIMSSENVPARISRCLEEGAEEFFLKPVRLADLNK 141
Cdd:PRK10610  62 NMDGLELLKTIRADGAMSALPVLMVTAEAKKENIIAAAQAGASGYVVKPFTAATLEE 118
REC_RssB-like cd17555
phosphoacceptor receiver (REC) domain of Pseudomonas aeruginosa RssB and similar domains; ...
11-142 3.15e-07

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: 47.58  E-value: 3.15e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230202  11 VLAVDDSLFDRKLIERLLQKSSCQVTTVDSGSKALEFLGLRQstdsndpnafskapvnhqvveVNLIITDYCMPGMTGYD 90
Cdd:cd17555   3 ILVIDDDEVVRESIAAYLEDSGFQVLQAADGRQGLELFRSEQ---------------------PDLVLCDLRMPEMDGLE 61
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 15230202  91 LLKKVKESSAfrDIPVVIMSSENVPARISRCLEEGAEEFFLKPvrLADLNKL 142
Cdd:cd17555  62 VLKQITKESP--DTPVIVVSGAGVMSDAVEALRLGAWDYLTKP--IEDLAVL 109
REC_CheC-like cd17593
phosphoacceptor receiver (REC) domain of uncharacterized response regulators containing a CheC ...
9-142 3.90e-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: 47.53  E-value: 3.90e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230202   9 FHVLAVDDSLFDRKLIERLLQKS-SCQVTTVDSGSKALEFLglrqstdsndpnafskapvNHQVVEVNLIitDYCMPGMT 87
Cdd:cd17593   1 MKVLICDDSSMARKQLARALPADwDVEITFAENGEEALEIL-------------------REGRIDVLFL--DLTMPVMD 59
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 15230202  88 GYDLLKKVKESSAfrDIPVVIMSSENVPARISRCLEEGAEEFFLKPVRLADLNKL 142
Cdd:cd17593  60 GYEVLEALPVEQL--ETKVIVVSGDVQPEAKERVLELGALAFLKKPFDPEKLAQL 112
orf27 CHL00148
Ycf27; Reviewed
3-133 4.29e-07

Ycf27; Reviewed


Pssm-ID: 214376 [Multi-domain]  Cd Length: 240  Bit Score: 49.33  E-value: 4.29e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230202    3 MAAESQFHVLAVDDSLFDRKLIERLLQKSSCQVTTVDSGSKALeflglrqstdsndpNAFSKapvnHQVvevNLIITDYC 82
Cdd:CHL00148   1 TMENSKEKILVVDDEAYIRKILETRLSIIGYEVITASDGEEAL--------------KLFRK----EQP---DLVILDVM 59
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 15230202   83 MPGMTGYDLLKKVKESSafrDIPVVIMSS-ENVPARISrCLEEGAEEFFLKP 133
Cdd:CHL00148  60 MPKLDGYGVCQEIRKES---DVPIIMLTAlGDVSDRIT-GLELGADDYVVKP 107
REC_RcNtrC-like cd19928
phosphoacceptor receiver (REC) domain of Rhodobacter capsulatus nitrogen regulatory protein C ...
73-133 5.50e-07

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: 46.73  E-value: 5.50e-07
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15230202  73 EVNLIITDYCMPGMTGYDLLKKVKESSAfrDIPVVIMSSENVPARISRCLEEGAEEFFLKP 133
Cdd:cd19928  42 EGDLVITDVVMPDENGLDLIPRIKKARP--DLPIIVMSAQNTLMTAVKAAERGAFEYLPKP 100
PRK10693 PRK10693
two-component system response regulator RssB;
76-143 6.10e-07

two-component system response regulator RssB;


Pssm-ID: 182652 [Multi-domain]  Cd Length: 303  Bit Score: 49.22  E-value: 6.10e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15230202   76 LIITDYCMPGMTGYDLLKKVKESSAfrDIPVVIMSSENVPARISRCLEEGAEEFFLKPVRlaDLNKLK 143
Cdd:PRK10693  20 LIICDLAMPRMNGIEFVEHLRNRGD--QTPVLVISATENMADIAKALRLGVQDVLLKPVK--DLNRLR 83
PRK10161 PRK10161
phosphate response regulator transcription factor PhoB;
75-168 8.01e-07

phosphate response regulator transcription factor PhoB;


Pssm-ID: 182277 [Multi-domain]  Cd Length: 229  Bit Score: 48.56  E-value: 8.01e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230202   75 NLIITDYCMPGMTGYDLLKKVKESSAFRDIPVVIMSSENVPARISRCLEEGAEEFFLKPVRLADL--------NKLKPHM 146
Cdd:PRK10161  48 DLILLDWMLPGGSGIQFIKHLKRESMTRDIPVVMLTARGEEEDRVRGLETGADDYITKPFSPKELvarikavmRRISPMA 127
                         90       100
                 ....*....|....*....|..
gi 15230202  147 MKTKLKNQKLEEIETTSKVENG 168
Cdd:PRK10161 128 VEEVIEMQGLSLDPTSHRVMAG 149
REC_DivK-like cd17548
phosphoacceptor receiver (REC) domain of DivK and similar proteins; Caulobacter crescentus ...
11-107 2.01e-06

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: 45.22  E-value: 2.01e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230202  11 VLAVDDSLFDRKLIERLLQKSSCQVTTVDSGSKALEFLglrqstDSNDPNafskapvnhqvvevnLIITDYCMPGMTGYD 90
Cdd:cd17548   2 ILIVEDNPLNMKLARDLLESAGYEVLEAADGEEALEIA------RKEKPD---------------LILMDIQLPGMDGLE 60
                        90
                ....*....|....*..
gi 15230202  91 LLKKVKESSAFRDIPVV 107
Cdd:cd17548  61 ATRLLKEDPATRDIPVI 77
REC_PatA-like cd17602
phosphoacceptor receiver (REC) domain of PatA and similar domains; Nostoc sp. (or Anabaena sp.) ...
11-133 3.29e-06

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: 44.28  E-value: 3.29e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230202  11 VLAVDDSLFDRKLIERLLQKSSCQVTTVDSGSKALEFLglrqstdsndpnafskapVNHQVvevNLIITDYCMPGMTGYD 90
Cdd:cd17602   1 VACVDDRPSIQKMIEYFLEKQGFRVVVIDDPLRALTTL------------------LNSKP---DLILIDIDMPDLDGYE 59
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 15230202  91 LLKKVKESSAFRDIPVVIMS-SENVPARIsRCLEEGAEEFFLKP 133
Cdd:cd17602  60 LCSLLRKSSALKDTPIIMLTgKDGLVDRI-RAKMAGASGYLTKP 102
REC_OmpR_BsPhoP-like cd19937
phosphoacceptor receiver (REC) domain of BsPhoP-like OmpR family response regulators; Bacillus ...
12-133 3.70e-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: 44.57  E-value: 3.70e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230202  12 LAVDDSLFDRKLIERLLQKSSCQVTTVDSGSKALEFLglrqstDSNDPNafskapvnhqvvevnLIITDYCMPGMTGYDL 91
Cdd:cd19937   1 LVVDDEEDIVELLKYNLEKEGYEVVTAYDGEEALKRA------KDEKPD---------------LIILDLMLPGIDGLEV 59
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 15230202  92 LKKVKESSAFRDIPVVIMSSENvpARISRC--LEEGAEEFFLKP 133
Cdd:cd19937  60 CRILRSDPKTSSIPIIMLTAKG--EEFDKVlgLELGADDYITKP 101
PRK10841 PRK10841
two-component system sensor histidine kinase RcsC;
10-139 3.82e-06

two-component system sensor histidine kinase RcsC;


Pssm-ID: 182772 [Multi-domain]  Cd Length: 924  Bit Score: 47.28  E-value: 3.82e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230202   10 HVLAVDDSLFDRKLIERLLQKSSCQVTTVDSGSKALEFLGlRQSTDsndpnafskapvnhqvvevnLIITDYCMPGMTGY 89
Cdd:PRK10841 803 MILVVDDHPINRRLLADQLGSLGYQCKTANDGVDALNVLS-KNHID--------------------IVLTDVNMPNMDGY 861
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 15230202   90 DLLKKVKESSafRDIPVVIMSSENVPARISRCLEEGAEEFFLKPVRLADL 139
Cdd:PRK10841 862 RLTQRLRQLG--LTLPVIGVTANALAEEKQRCLEAGMDSCLSKPVTLDVL 909
REC_RR468-like cd17552
phosphoacceptor receiver (REC) domain of Thermotoga maritima response regulator RR468 and ...
10-109 5.22e-06

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: 44.46  E-value: 5.22e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230202  10 HVLAVDDSLFDRKLIERLLQKSS-CQVTTVDSGSKALEFLGLRQstdsndPNAfskapvnhqvvevnlIITDYCMPGMTG 88
Cdd:cd17552   3 RILVIDDEEDIREVVQACLEKLAgWEVLTASSGQEGLEKAATEQ------PDA---------------ILLDVMMPDMDG 61
                        90       100
                ....*....|....*....|.
gi 15230202  89 YDLLKKVKESSAFRDIPVVIM 109
Cdd:cd17552  62 LATLKKLQANPETQSIPVILL 82
REC_NtrX-like cd17550
phosphoacceptor receiver (REC) domain of nitrogen assimilation regulatory protein NtrX and ...
11-110 5.25e-06

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: 44.02  E-value: 5.25e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230202  11 VLAVDDSLFDRKLIERLLQKSSCQVTTVDSGSKALEFLGLRqstdsndpnafskapvnhqvvEVNLIITDYCMPGMTGYD 90
Cdd:cd17550   1 ILIVDDEEDIRESLSGILEDEGYEVDTAADGEEALKLIKER---------------------RPDLVLLDIWLPDMDGLE 59
                        90       100
                ....*....|....*....|
gi 15230202  91 LLKKVKEssAFRDIPVVIMS 110
Cdd:cd17550  60 LLKEIKE--KYPDLPVIMIS 77
REC_OmpR_PrrA-like cd17627
phosphoacceptor receiver (REC) domain of PrrA-like OmpR family response regulators; The ...
11-139 6.26e-06

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: 43.91  E-value: 6.26e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230202  11 VLAVDDSLFDRKLIERLLQKSSCQVTTVDSGSKALEflglrqSTDSNDPNafskapvnhqvvevnLIITDYCMPGMTGYD 90
Cdd:cd17627   1 ILVVDDDRAVRESLRRSLRFEGYEVETAVDGAEALR------VISGNRPD---------------AVVLDVMMPRLDGLE 59
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 15230202  91 LLKKVKEssAFRDIPVVIMSSEN-VPARISRcLEEGAEEFFLKPVRLADL 139
Cdd:cd17627  60 VCRRLRA--AGNDLPILVLTARDsVSDRVAG-LDAGADDYLVKPFALEEL 106
REC_CpdR_CckA-like cd18160
phosphoacceptor receiver (REC) domain of Brucella abortus CpdR and CckA, and similar domains; ...
11-110 6.91e-06

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: 43.64  E-value: 6.91e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230202  11 VLAVDDSLFDRKLIERLLQKSSCQVTTVDSGSKALEFLglrqstdsndpnafskapvnHQVVEVNLIITDYCMPGMTGYD 90
Cdd:cd18160   2 ILLADDEPSVRKFIVTTLKKAGYAVTEAESGAEALEKL--------------------QQGKDIDIVVTDIVMPEMDGIE 61
                        90       100
                ....*....|....*....|
gi 15230202  91 LLKKVKESSAfrDIPVVIMS 110
Cdd:cd18160  62 LAREARKIDP--DVKILFIS 79
REC_OmpR_DrrD-like cd17625
phosphoacceptor receiver (REC) domain of DrrD-like OmpR family response regulators; DrrD is a ...
12-139 7.89e-06

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: 43.75  E-value: 7.89e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230202  12 LAVDDSLFDRKLIERLLQKSSCQVTTVDSGSKALEFlglrqstdsndpnAFSkapvnhqvVEVNLIITDYCMPGMTGYDL 91
Cdd:cd17625   1 LVVEDEKDLSEAITKHLKKEGYTVDVCFDGEEGLEY-------------ALS--------GIYDLIILDIMLPGMDGLEV 59
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 15230202  92 LKKVKESSAfrDIPVVIMSSEN-VPARIsRCLEEGAEEFFLKPVRLADL 139
Cdd:cd17625  60 LKSLREEGI--ETPVLLLTALDaVEDRV-KGLDLGADDYLPKPFSLAEL 105
REC_OmpR_VirG cd17594
phosphoacceptor receiver (REC) domain of VirG-like OmpR family response regulators; VirG is ...
10-139 1.21e-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: 43.20  E-value: 1.21e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230202  10 HVLAVDDSLFDRKLIERLLQKSSCQVTTVDSGSKalEFLGLRQSTdsndpnafskapvnhqvveVNLIITDYCMPGMTGY 89
Cdd:cd17594   1 HVLVVDDDAAMRHLLILYLRERGFDVTAAADGAE--EARLMLHRR-------------------VDLVLLDLRLGQESGL 59
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 15230202  90 DLLKKVKESSafrDIPVVIMSSEN-VPARISRCLEEGAEEFFLKPVRLADL 139
Cdd:cd17594  60 DLLRTIRARS---DVPIIIISGDRrDEIDRVVGLELGADDYLAKPFGLREL 107
glnG PRK10923
nitrogen regulation protein NR(I); Provisional
11-133 1.98e-05

nitrogen regulation protein NR(I); Provisional


Pssm-ID: 182842 [Multi-domain]  Cd Length: 469  Bit Score: 44.86  E-value: 1.98e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230202   11 VLAVDDSLFDRKLIERLLQKSSCQVTTVDSGSKALEFLGlrqstdSNDPNafskapvnhqvvevnLIITDYCMPGMTGYD 90
Cdd:PRK10923   6 VWVVDDDSSIRWVLERALAGAGLTCTTFENGNEVLEALA------SKTPD---------------VLLSDIRMPGMDGLA 64
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 15230202   91 LLKKVKESSAFrdIPVVIMSSE-NVPARISrCLEEGAEEFFLKP 133
Cdd:PRK10923  65 LLKQIKQRHPM--LPVIIMTAHsDLDAAVS-AYQQGAFDYLPKP 105
fixJ PRK09390
response regulator FixJ; Provisional
10-133 3.44e-05

response regulator FixJ; Provisional


Pssm-ID: 181815 [Multi-domain]  Cd Length: 202  Bit Score: 43.45  E-value: 3.44e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230202   10 HVLAVDDSLFDRKLIERLLQKSSCQVTTVDSGSKALEFLGlrqstdsndpnafskapvnhqVVEVNLIITDYCMPGMTGY 89
Cdd:PRK09390   5 VVHVVDDDEAMRDSLAFLLDSAGFEVRLFESAQAFLDALP---------------------GLRFGCVVTDVRMPGIDGI 63
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 15230202   90 DLLKKVKESSAfrDIPVVIMSSE-NVPARIsRCLEEGAEEFFLKP 133
Cdd:PRK09390  64 ELLRRLKARGS--PLPVIVMTGHgDVPLAV-EAMKLGAVDFIEKP 105
PRK11107 PRK11107
hybrid sensory histidine kinase BarA; Provisional
11-107 3.79e-05

hybrid sensory histidine kinase BarA; Provisional


Pssm-ID: 236848 [Multi-domain]  Cd Length: 919  Bit Score: 44.07  E-value: 3.79e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230202   11 VLAVDDSLFDRKLIERLLQKSSCQVTTVDSGSKALEfLGLRQSTDsndpnafskapvnhqvvevnLIITDYCMPGMTGYD 90
Cdd:PRK11107 670 VMAVDDNPANLKLIGALLEEQVEHVVLCDSGHQAVE-QAKQRPFD--------------------LILMDIQMPGMDGIR 728
                         90
                 ....*....|....*..
gi 15230202   91 LLKKVKESSAFRDIPVV 107
Cdd:PRK11107 729 ACELIRQLPHNQNTPII 745
REC_hyHK_blue-like cd18161
phosphoacceptor receiver (REC) domain of hybrid sensor histidine kinase/response regulators ...
11-110 4.65e-05

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: 41.18  E-value: 4.65e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230202  11 VLAVDDSLFDRKLIERLLQKSSCQVTTVDSGSKALEFLglrqstdsndpnafskapvnHQVVEVNLIITDYCMPG-MTGY 89
Cdd:cd18161   1 VLVVEDDPDVRRLTAEVLEDLGYTVLEAASGDEALDLL--------------------ESGPDIDLLVTDVIMPGgMNGS 60
                        90       100
                ....*....|....*....|.
gi 15230202  90 DLLKKVKESsaFRDIPVVIMS 110
Cdd:cd18161  61 QLAEEARRR--RPDLKVLLTS 79
REC_OmpR_CpxR cd17623
phosphoacceptor receiver (REC) domain of CpxR-like OmpR family response regulators; CpxR is ...
11-133 6.94e-05

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: 41.14  E-value: 6.94e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230202  11 VLAVDDslfDRKLIE---RLLQKSSCQVTTVDSGSKALEFLgLRQSTDsndpnafskapvnhqvvevnLIITDYCMPGMT 87
Cdd:cd17623   1 ILLIDD---DRELTElltEYLEMEGFNVRAAHDGEQGLAAL-LEGSPD--------------------LVVLDVMLPKMN 56
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 15230202  88 GYDLLKKVKESSafrDIPVVIMSSENVParISRC--LEEGAEEFFLKP 133
Cdd:cd17623  57 GLDVLKELRKTS---QVPVLMLTARGDD--IDRIlgLELGADDYLPKP 99
PRK11361 PRK11361
acetoacetate metabolism transcriptional regulator AtoC;
11-142 9.23e-05

acetoacetate metabolism transcriptional regulator AtoC;


Pssm-ID: 183099 [Multi-domain]  Cd Length: 457  Bit Score: 42.91  E-value: 9.23e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230202   11 VLAVDDSLFDRKLIERLLQKSSCQVTTVDSGSKALEFLGLrQSTDsndpnafskapvnhqvvevnLIITDYCMPGMTGYD 90
Cdd:PRK11361   7 ILIVDDEDNVRRMLSTAFALQGFETHCANNGRTALHLFAD-IHPD--------------------VVLMDIRMPEMDGIK 65
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 15230202   91 LLKKVKESSafRDIPVVIMSSENVPARISRCLEEGAEEFFLKPVRLADLNKL 142
Cdd:PRK11361  66 ALKEMRSHE--TRTPVILMTAYAEVETAVEALRCGAFDYVIKPFDLDELNLI 115
REC_DesR-like cd19930
phosphoacceptor receiver (REC) domain of DesR and similar proteins; This group is composed of ...
73-139 1.34e-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: 1.34e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15230202  73 EVNLIITDYCMPGMTGYDLLKKVKESSAfrDIPVVIMSSENVPARISRCLEEGAEEFFLKPVRLADL 139
Cdd:cd19930  44 SPDVAILDIEMPGRTGLEVAAELREELP--DTKVLIVTTFGRPGYFRRALAAGVDGYVLKDRPIEEL 108
REC_OmpR_PmrA-like cd17624
phosphoacceptor receiver (REC) domain of PmrA-like OmpR family response regulators; This ...
11-139 1.36e-04

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: 40.16  E-value: 1.36e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230202  11 VLAVDDSLFDRKLIERLLQKSSCQVTTVDSGSKALEFLGlRQSTDsndpnafskapvnhqvvevnLIITDYCMPGMTGYD 90
Cdd:cd17624   1 ILLVEDDALLGDGLKTGLRKAGYAVDWVRTGAEAEAALA-SGPYD--------------------LVILDLGLPDGDGLD 59
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 15230202  91 LLKKVKesSAFRDIPVVIMSS-ENVPARIsRCLEEGAEEFFLKPVRLADL 139
Cdd:cd17624  60 LLRRWR--RQGQSLPVLILTArDGVDDRV-AGLDAGADDYLVKPFALEEL 106
COG4567 COG4567
DNA-binding response regulator, ActR/RegA family, consists of REC and Fis-type HTH domains ...
10-139 1.59e-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: 41.06  E-value: 1.59e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230202  10 HVLAVDDSLFDRKLIERLLQKSSCQVTTVDSGSKALEFLglrqstDSNDPnafskapvnhqvvevNLIITDYCMPGMTGY 89
Cdd:COG4567   6 SLLLVDDDEAFARVLARALERRGFEVTTAASVEEALALL------EQAPP---------------DYAVLDLRLGDGSGL 64
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 15230202  90 DLLKKVKESSAfrDIPVVIMSSENVPARISRCLEEGAEEFFLKPVRLADL 139
Cdd:COG4567  65 DLIEALRERDP--DARIVVLTGYASIATAVEAIKLGADDYLAKPADADDL 112
REC_OmpR_MtrA-like cd17626
phosphoacceptor receiver (REC) domain of MtrA-like OmpR family response regulators; MtrA is ...
75-139 2.49e-04

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: 39.38  E-value: 2.49e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15230202  75 NLIITDYCMPGMTGYDLLKKVKESSafrDIPVVIMSSENVPARISRCLEEGAEEFFLKPVRLADL 139
Cdd:cd17626  46 DLVLLDLMLPGIDGIEVCRQIRAES---GVPIVMLTAKSDTVDVVLGLESGADDYVAKPFKPKEL 107
REC_Spo0F-like cd17553
phosphoacceptor receiver (REC) domain of Spo0F and similar domains; Spo0F, a stand-alone ...
11-139 3.99e-04

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: 39.07  E-value: 3.99e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230202  11 VLAVDDSLFDRKLIERLLQKSSCQVTTVDSGSKALEFLglrqstdsndpnafSKAPVNhqvvevnLIITDYCMPGMTGYD 90
Cdd:cd17553   3 ILIVDDQYGIRILLNEVFNKEGYQTFQAANGLQALDIV--------------TKERPD-------LVLLDMKIPGMDGIE 61
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 15230202  91 LLKKVKESSAfrDIPVVIMSSENVPARISRCLEEGAEEFFLKPVRLADL 139
Cdd:cd17553  62 ILKRMKVIDE--NIRVIIMTAYGELDMIQESKELGALTHFAKPFDIDEI 108
PRK10365 PRK10365
sigma-54-dependent response regulator transcription factor ZraR;
11-163 4.28e-04

sigma-54-dependent response regulator transcription factor ZraR;


Pssm-ID: 182412 [Multi-domain]  Cd Length: 441  Bit Score: 40.78  E-value: 4.28e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230202   11 VLAVDDSLFDRKLIERLLQKSSCQVTTVDSGSKALEflglrqstdsndpnafskaPVNHQVVEvnLIITDYCMPGMTGYD 90
Cdd:PRK10365   8 ILVVDDDISHCTILQALLRGWGYNVALANSGRQALE-------------------QVREQVFD--LVLCDVRMAEMDGIA 66
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15230202   91 LLKKVKESSAfrDIPVVIMSSENVPARISRCLEEGAEEFFLKPVrlaDLNKLKPHMMKTkLKNQKLEEIETTS 163
Cdd:PRK10365  67 TLKEIKALNP--AIPVLIMTAYSSVETAVEALKTGALDYLIKPL---DFDNLQATLEKA-LAHTHSIDAETPA 133
LytT COG3279
DNA-binding response regulator, LytR/AlgR family [Transcription, Signal transduction ...
10-141 6.06e-04

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


Pssm-ID: 442510 [Multi-domain]  Cd Length: 235  Bit Score: 39.80  E-value: 6.06e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230202  10 HVLAVDDSLFDRKLIERLLQK-SSCQ-VTTVDSGSKALEFLglrqstdsndpnafskapVNHQVvevNLIITDYCMPGMT 87
Cdd:COG3279   3 KILIVDDEPLARERLERLLEKyPDLEvVGEASNGEEALELL------------------EEHKP---DLVFLDIQMPGLD 61
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 15230202  88 GYDLLKKVKESSafRDIPVVIMSSEN---VPArisrcLEEGAEEFFLKPVRLADLNK 141
Cdd:COG3279  62 GFELARQLRELD--PPPPIIFTTAYDeyaLEA-----FEVNAVDYLLKPIDEERLAK 111
REC_OmpR_CusR-like cd19935
phosphoacceptor receiver (REC) domain of CusR-like OmpR family response regulators; ...
76-133 8.84e-04

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: 37.42  E-value: 8.84e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 15230202  76 LIITDYCMPGMTGYDLLKKVKESSafRDIPVVIMSS-ENVPARIsRCLEEGAEEFFLKP 133
Cdd:cd19935  45 LIILDVMLPGLDGLEVLRRLRAAG--KQTPVLMLTArDSVEDRV-KGLDLGADDYLVKP 100
PRK00742 PRK00742
chemotaxis-specific protein-glutamate methyltransferase CheB;
11-133 1.31e-03

chemotaxis-specific protein-glutamate methyltransferase CheB;


Pssm-ID: 234828 [Multi-domain]  Cd Length: 354  Bit Score: 39.36  E-value: 1.31e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230202   11 VLAVDDSLFDRKLIERLLQKSScQVTTVDS---GSKALEflglrqstdsndpnafskapvnhQVVEVN--LIITDYCMPG 85
Cdd:PRK00742   6 VLVVDDSAFMRRLISEILNSDP-DIEVVGTapdGLEARE-----------------------KIKKLNpdVITLDVEMPV 61
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 15230202   86 MTGYDLLKKVKESsafRDIPVVIMSS---ENvpARIS-RCLEEGAEEFFLKP 133
Cdd:PRK00742  62 MDGLDALEKIMRL---RPTPVVMVSSlteRG--AEITlRALELGAVDFVTKP 108
REC_HupR cd17596
phosphoacceptor receiver (REC) domain of hydrogen uptake protein regulator (HupR); Members of ...
11-133 1.34e-03

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: 37.73  E-value: 1.34e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230202  11 VLAVDDSLFDRKLIERLLQKSScQVTTVDSGSKALEFLglrqstdsndpnafskapvnhQVVEVNLIITDYCMPGMTGYD 90
Cdd:cd17596   3 ILVVDDEVRSLEALRRTLEEDF-DVLTAASAEEALAIL---------------------EEEWVQVILCDQRMPGTTGVE 60
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 15230202  91 LLKKVKESsaFRDIPVVIMS----SENVPARISrclEEGAEEFFLKP 133
Cdd:cd17596  61 FLKEVRER--WPEVVRIIISgytdSEDIIAGIN---EAGIYQYLTKP 102
PRK11517 PRK11517
DNA-binding response regulator HprR;
76-139 1.39e-03

DNA-binding response regulator HprR;


Pssm-ID: 183172 [Multi-domain]  Cd Length: 223  Bit Score: 38.73  E-value: 1.39e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15230202   76 LIITDYCMPGMTGYDLLKKVKESSAfrdIPVVIMSSENVPARISRCLEEGAEEFFLKPVRLADL 139
Cdd:PRK11517  47 LIILDIMLPGMDGWQILQTLRTAKQ---TPVICLTARDSVDDRVRGLDSGANDYLVKPFSFSEL 107
PRK09836 PRK09836
DNA-binding transcriptional activator CusR; Provisional
73-139 1.47e-03

DNA-binding transcriptional activator CusR; Provisional


Pssm-ID: 182102 [Multi-domain]  Cd Length: 227  Bit Score: 38.75  E-value: 1.47e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15230202   73 EVNLIITDYCMPGMTGYDLLKKVKesSAFRDIPVVIMSSENVPARISRCLEEGAEEFFLKPVRLADL 139
Cdd:PRK09836  44 DYDLIILDIMLPDVNGWDIVRMLR--SANKGMPILLLTALGTIEHRVKGLELGADDYLVKPFAFAEL 108
REC_NarL cd19931
phosphoacceptor receiver (REC) domain of Nitrate/Nitrite response regulator L (NarL); Nitrate ...
11-132 1.55e-03

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: 37.33  E-value: 1.55e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230202  11 VLAVDDSLFDRKLIERLLQKSS--CQVTTVDSGSKALEfLGLRQSTDsndpnafskapvnhqvvevnLIITDYCMPGMTG 88
Cdd:cd19931   1 VLLIDDHPLLRKGIKQLIELDPdfTVVGEASSGEEGIE-LAERLDPD--------------------LILLDLNMKGMSG 59
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 15230202  89 YDLLKKVKESSAfrDIPVVIMSSENVPARISRCLEEGAEEFFLK 132
Cdd:cd19931  60 LDTLKALREEGV--SARIVILTVSDAEDDVVTALRAGADGYLLK 101
REC_WspR-like cd17575
phosphoacceptor receiver (REC) domain of WspR response regulator and similar proteins; The ...
77-132 1.94e-03

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: 37.39  E-value: 1.94e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 15230202  77 IITDYCMPGMTGYDLLKKVKESSAFRDIPVVIMSSENVPARISRCLEEGAEEFFLK 132
Cdd:cd17575  49 ILQDLVMPGVDGLTLVRFFRANPATRDIPIIVLSTKEEPEVKSEAFALGANDYLVK 104
REC_OmpR_ChvI-like cd19936
phosphoacceptor receiver (REC) domain of ChvI-like OmpR family response regulators; ...
40-133 2.69e-03

phosphoacceptor receiver (REC) domain of ChvI-like OmpR family response regulators; Sinorhizobium meliloti ChvI is part of the ExoS/ChvI two-component regulatory system (TCS) that is required for nitrogen-fixing symbiosis and exopolysaccharide synthesis. ExoS/ChvI also play important roles in regulating biofilm formation, motility, nutrient utilization, and the viability of free-living bacteria. ChvI 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: 381163 [Multi-domain]  Cd Length: 99  Bit Score: 36.27  E-value: 2.69e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230202  40 SGSKALEFLGLRQSTDSNDPNA---FSKAPVNhqvvevnLIITDYCMPGMTGYDLLKKVKESSafrDIPVVIMSSENVPA 116
Cdd:cd19936  13 SVSMALEAEGFSVETYTDGASAldgLNARPPD-------LAILDIKMPRMDGMELLQRLRQKS---TLPVIFLTSKDDEI 82
                        90
                ....*....|....*..
gi 15230202 117 RISRCLEEGAEEFFLKP 133
Cdd:cd19936  83 DEVFGLRMGADDYITKP 99
REC_TrxB cd17595
phosphoacceptor receiver (REC) domain a fused response regulator with a thioredoxin reductase ...
11-97 2.70e-03

phosphoacceptor receiver (REC) domain a fused response regulator with a thioredoxin reductase output domain; This family is composed of uncharacterized fusion proteins containing a REC domain and a thioredoxin reductase domain. Thioredoxin reductase catalyzes the reduction of thioredoxin and is thus a central component in the thioredoxin system. Fusion proteins containing REC and thioredoxin reductase domains could play an important role in the environmental regulation of the cellular dithiol-disulfide ratio. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381126 [Multi-domain]  Cd Length: 135  Bit Score: 36.93  E-value: 2.70e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230202  11 VLAVDDSLFDRKLIERLLQ---KSSCQVTTVDSGSKALEflGLRQSTDSNDPNAfskapvnhqvvevnLIITDYCMPGMT 87
Cdd:cd17595   3 ILTVDDDPQVLRAVARDLRrqyGKDYRVLRADSGAEALD--ALKELKLRGEAVA--------------LFLVDQRMPEMD 66
                        90
                ....*....|
gi 15230202  88 GYDLLKKVKE 97
Cdd:cd17595  67 GVEFLEKAME 76
PRK10336 PRK10336
two-component system response regulator QseB;
77-139 3.59e-03

two-component system response regulator QseB;


Pssm-ID: 182387 [Multi-domain]  Cd Length: 219  Bit Score: 37.57  E-value: 3.59e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15230202   77 IITDYCMPGMTGYDLLKKVKESSafRDIPVVIMSSENVPARISRCLEEGAEEFFLKPVRLADL 139
Cdd:PRK10336  48 VILDLTLPGMDGRDILREWREKG--QREPVLILTARDALAERVEGLRLGADDYLCKPFALIEV 108
PRK10840 PRK10840
transcriptional regulator RcsB; Provisional
72-150 4.78e-03

transcriptional regulator RcsB; Provisional


Pssm-ID: 182771 [Multi-domain]  Cd Length: 216  Bit Score: 37.12  E-value: 4.78e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230202   72 VEVNLIITDYCMPGMT---GYDLLKKVKESsaFRDIPVVIMSSENVPARISRCLEEGAEEFFLKPVRLADLNKLKPHMMK 148
Cdd:PRK10840  48 LDAHVLITDLSMPGDKygdGITLIKYIKRH--FPSLSIIVLTMNNNPAILSAVLDLDIEGIVLKQGAPTDLPKALAALQK 125

                 ..
gi 15230202  149 TK 150
Cdd:PRK10840 126 GK 127
REC_OmpR_CtrA cd17616
phosphoacceptor receiver (REC) domain of CtrA-like OmpR family response regulators; CtrA is ...
11-133 5.37e-03

phosphoacceptor receiver (REC) domain of CtrA-like OmpR family response regulators; CtrA is part of the CckA-ChpT-CtrA phosphorelay that is conserved in alphaproteobacteria and is important in orchestrating the cell cycle, polar development, and flagellar biogenesis. CtrA is the master regulator of flagella synthesis genes and also regulates genes involved in the cell cycle, exopolysaccharide synthesis, and cyclic-di-GMP signaling. CtrA is active as a transcription factor when phosphorylated. It is a member of the OmpR family of DNA-binding response regulators, 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: 381132 [Multi-domain]  Cd Length: 114  Bit Score: 35.85  E-value: 5.37e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230202  11 VLAVDDSLFDRKLIERLLQKSSCQVTTVDSGSKALEfLGLRQSTDsndpnafskapvnhqvvevnLIITDYCMPGMTGYD 90
Cdd:cd17616   1 VLLIEDDSATAQSIELMLKSEGFNVYTTDLGEEGLD-LGKLYDYD--------------------IILLDLNLPDMSGYE 59
                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 15230202  91 LLKKVKESSAfrDIPVVIMSSENVPARISRCLEEGAEEFFLKP 133
Cdd:cd17616  60 VLRTLRLAKV--KTPILILSGLADIEDKVKGLGFGADDYMTKP 100
PRK11091 PRK11091
aerobic respiration control sensor protein ArcB; Provisional
10-177 5.72e-03

aerobic respiration control sensor protein ArcB; Provisional


Pssm-ID: 236842 [Multi-domain]  Cd Length: 779  Bit Score: 37.61  E-value: 5.72e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230202   10 HVLAVDDslfdrklIE-------RLLQKSSCQVTTVDSGSKALEFLglrqstdsnDPNAFskapvnhqvvevNLIITDYC 82
Cdd:PRK11091 527 NILLVED-------IElnvivarSVLEKLGNSVDVAMTGKEALEMF---------DPDEY------------DLVLLDIQ 578
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230202   83 MPGMTGYDLLKKVKESSAFRDIPVVIMSSENVPARISRCLEEGAEEFFLKPVRLADLNKlkphMMKTKLKNQKLEEIETT 162
Cdd:PRK11091 579 LPDMTGLDIARELRERYPREDLPPLVALTANVLKDKKEYLDAGMDDVLSKPLSVPALTA----MIKKFWDTQDDEESTVT 654
                        170
                 ....*....|....*
gi 15230202  163 SKVENGVPTAVADPE 177
Cdd:PRK11091 655 TEESSKANEALLDIP 669
REC_OmpR_RegX3-like cd17621
phosphoacceptor receiver (REC) domain of RegX3-like OmpR family response regulators; RegX3 is ...
11-133 7.23e-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: 34.87  E-value: 7.23e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230202  11 VLAVDDSLFDRKLIERLLQKSSCQVTTVDSGSKAL-EFlglrqstdsnDPNAfskapvnhqvveVNLIITDYCMPGMTGY 89
Cdd:cd17621   1 VLVVEDEESFSDPLAYLLRKEGFEVTVATDGPAALaEF----------DRAG------------ADIVLLDLMLPGLSGT 58
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 15230202  90 DLLKKVKESSafrDIPVVIMSSENVPARISRCLEEGAEEFFLKP 133
Cdd:cd17621  59 EVCRQLRARS---NVPVIMVTAKDSEIDKVVGLELGADDYVTKP 99
PRK10529 PRK10529
DNA-binding transcriptional activator KdpE; Provisional
75-139 8.21e-03

DNA-binding transcriptional activator KdpE; Provisional


Pssm-ID: 182522 [Multi-domain]  Cd Length: 225  Bit Score: 36.32  E-value: 8.21e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15230202   75 NLIITDYCMPGMTGYDLLKKVKESSAfrdIPVVIMSSENVPARISRCLEEGAEEFFLKPVRLADL 139
Cdd:PRK10529  47 DLIILDLGLPDGDGIEFIRDLRQWSA---IPVIVLSARSEESDKIAALDAGADDYLSKPFGIGEL 108
REC_citrate_TCS cd19925
phosphoacceptor receiver (REC) domain of citrate family two-component system response ...
10-139 8.24e-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: 8.24e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230202  10 HVLAVDD----SLFDRKLIERLLQKSscQVTTVDSGSKALEFLGLRQstdsndpnafskapvnhqvveVNLIITDYCMPG 85
Cdd:cd19925   2 NVLIVEDdpmvAEIHRAYVEQVPGFT--VIGTAGTGEEALKLLKERQ---------------------PDLILLDIYLPD 58
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 15230202  86 MTGYDLLKKVKEssAFRDIPVVIMSSENVPARISRCLEEGAEEFFLKPVRLADL 139
Cdd:cd19925  59 GNGLDLLRELRA--AGHDVDVIVVTAANDVETVREALRLGVVDYLIKPFTFERL 110
 
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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