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Conserved domains on  [gi|445998103|ref|WP_000075958|]
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MULTISPECIES: chemotaxis protein [Bacillus]

Protein Classification

chemotaxis protein( domain architecture ID 10002869)

chemotaxis protein, similar to CheV, a response regulator with a receiver domain and a CheW domain which may function as a coupling protein in chemotaxis

CATH:  3.40.50.2300
Gene Ontology:  GO:0006935|GO:0000160|GO:0000156
PubMed:  20226724
SCOP:  4003632

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
CheW COG0835
Chemotaxis signal transduction protein CheW [Signal transduction mechanisms];
9-149 1.37e-39

Chemotaxis signal transduction protein CheW [Signal transduction mechanisms];


:

Pssm-ID: 440597  Cd Length: 151  Bit Score: 135.77  E-value: 1.37e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445998103   9 LESGTNELEIVTYTVGENLFSINVMKVREIINPFPVTTVPESHHAVEGVVQVRGEILPVINLATALNLKSTKPLDQTKFI 88
Cdd:COG0835    1 LEAGANELQYLTFRLGGERYAIPIEKVREILPLPPITPVPGAPPWVLGVINLRGRVVPVIDLRALLGLPPTEDTERTRII 80
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 445998103  89 ISELNQMKVIFRVDEVHRIQRISWEQIDE-PASLSMGLEETTSGIVKLDGQIILLLDYEKIV 149
Cdd:COG0835   81 VLEVGGRVVGLLVDSVSGVVRIDPDDIEPpPELLSGGLAPFITGVAKLDDRLILLLDLEKLL 142
REC super family cl19078
phosphoacceptor receiver (REC) domain of response regulators (RRs) and pseudo response ...
176-288 5.40e-29

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.


The actual alignment was detected with superfamily member cd19924:

Pssm-ID: 473134 [Multi-domain]  Cd Length: 111  Bit Score: 107.08  E-value: 5.40e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445998103 176 IYIAEDSAMLRQILEETLSSAGYtKMNFFSNGAEALAQIEKLAKEqGEKMFEHIHLLITDIEMPKMDGHHLTKVVKDSEV 255
Cdd:cd19924    1 ILVVDDSPTARKQLRDLLKNLGF-EIAEAVDGEEALNKLENLAKE-GNDLSKELDLIITDIEMPKMDGYELTFELRDDPR 78
                         90       100       110
                 ....*....|....*....|....*....|...
gi 445998103 256 MNRLPVIIFSSLITNELFHKGEAVGANAQVSKP 288
Cdd:cd19924   79 LANIPVILNSSLSGEFSRARGKKVGADAYLAKF 111
 
Name Accession Description Interval E-value
CheW COG0835
Chemotaxis signal transduction protein CheW [Signal transduction mechanisms];
9-149 1.37e-39

Chemotaxis signal transduction protein CheW [Signal transduction mechanisms];


Pssm-ID: 440597  Cd Length: 151  Bit Score: 135.77  E-value: 1.37e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445998103   9 LESGTNELEIVTYTVGENLFSINVMKVREIINPFPVTTVPESHHAVEGVVQVRGEILPVINLATALNLKSTKPLDQTKFI 88
Cdd:COG0835    1 LEAGANELQYLTFRLGGERYAIPIEKVREILPLPPITPVPGAPPWVLGVINLRGRVVPVIDLRALLGLPPTEDTERTRII 80
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 445998103  89 ISELNQMKVIFRVDEVHRIQRISWEQIDE-PASLSMGLEETTSGIVKLDGQIILLLDYEKIV 149
Cdd:COG0835   81 VLEVGGRVVGLLVDSVSGVVRIDPDDIEPpPELLSGGLAPFITGVAKLDDRLILLLDLEKLL 142
CheW cd00732
CheW, a small regulator protein, unique to the chemotaxis signalling in prokaryotes and archea. ...
15-148 1.65e-37

CheW, a small regulator protein, unique to the chemotaxis signalling in prokaryotes and archea. CheW interacts with the histidine kinase CheA, most likely with the related regulatory domain of CheA. CheW is proposed to form signalling arrays together with CheA and the methyl-accepting chemotaxis proteins (MCPs), which are involved in response modulation.


Pssm-ID: 238374  Cd Length: 140  Bit Score: 130.00  E-value: 1.65e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445998103  15 ELEIVTYTVGENLFSINVMKVREIINPFPVTTVPESHHAVEGVVQVRGEILPVINLATALNLKSTKPLDQTKFIISELNQ 94
Cdd:cd00732    1 ELEVVTFRLGDEEYGIPIMQVREILKPTPITPIPNAPPYVLGVINLRGRIVPVIDLRKRLGLPPAEDTKNTRIIVVEVGD 80
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 445998103  95 MKVIFRVDEVHRIQRISWEQIDE-PASLSMGLEETTSGIVKLDGQIILLLDYEKI 148
Cdd:cd00732   81 QVVGLLVDSVSEVLRLSTDDIQPpPPVLSDINAKFIRGVVKLEGRLLILLDLDKI 135
CheW pfam01584
CheW-like domain; CheW proteins are part of the chemotaxis signaling mechanism in bacteria. ...
18-148 8.27e-36

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


Pssm-ID: 460257 [Multi-domain]  Cd Length: 131  Bit Score: 125.39  E-value: 8.27e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445998103   18 IVTYTVGENLFSINVMKVREIINPFPVTTVPESHHAVEGVVQVRGEILPVINLATALNLKSTKPLDQTKFIISELNQMKV 97
Cdd:pfam01584   1 GLLFRLGGETFAIPISKVREILRPPPITPIPGAPGYVLGVINLRGEVLPVIDLRRLLGLPPTEPRERTRVVVVEVGGQVV 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 445998103   98 IFRVDEVHRIQRISWEQIdEPASLSMGLEETTSGIVKL-DGQIILLLDYEKI 148
Cdd:pfam01584  81 GLLVDEVIGVLEIVIKQI-EPPLGLGRVAGYISGATILgDGRVVLILDVEAL 131
CheW smart00260
Two component signalling adaptor domain;
14-149 3.35e-29

Two component signalling adaptor domain;


Pssm-ID: 214588 [Multi-domain]  Cd Length: 138  Bit Score: 108.48  E-value: 3.35e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445998103    14 NELEIVTYTVGEN-LFSINVMKVREIINPFPVTTVPESHHAVEGVVQVRGEILPVINLATALNLKSTKPLDQTKFIISEL 92
Cdd:smart00260   1 TIRLPLTFAIGKDeTYAIPIAAVREILRPPPITPIPGAPGYVLGVINLRGEVLPVVDLRRLLGLPPEPPTDETRVIVVET 80
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 445998103    93 NQMKVIFRVDEVHRIQRISWEQIDEPASLSMGLEETTSGIVKL-DGQIILLLDYEKIV 149
Cdd:smart00260  81 GDRKVGLVVDSVLGVREVVVKSIEPPPPVSLSNAPGISGATILgDGRVVLILDVDKLL 138
REC_CheV-like cd19924
phosphoacceptor receiver (REC) domain of chemotaxis protein CheV and similar proteins; This ...
176-288 5.40e-29

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: 107.08  E-value: 5.40e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445998103 176 IYIAEDSAMLRQILEETLSSAGYtKMNFFSNGAEALAQIEKLAKEqGEKMFEHIHLLITDIEMPKMDGHHLTKVVKDSEV 255
Cdd:cd19924    1 ILVVDDSPTARKQLRDLLKNLGF-EIAEAVDGEEALNKLENLAKE-GNDLSKELDLIITDIEMPKMDGYELTFELRDDPR 78
                         90       100       110
                 ....*....|....*....|....*....|...
gi 445998103 256 MNRLPVIIFSSLITNELFHKGEAVGANAQVSKP 288
Cdd:cd19924   79 LANIPVILNSSLSGEFSRARGKKVGADAYLAKF 111
CheY COG0784
CheY-like REC (receiver) domain, includes chemotaxis protein CheY and sporulation regulator ...
169-301 9.67e-25

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: 96.46  E-value: 9.67e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445998103 169 TDRAEKVIYIAEDSAMLRQILEETLSSAGYTkMNFFSNGAEALAQIEKlakeqgekmfEHIHLLITDIEMPKMDGHHLTK 248
Cdd:COG0784    1 PPLGGKRILVVDDNPDNRELLRRLLERLGYE-VTTAEDGAEALELLRA----------GPPDLILLDINMPGMDGLELLR 69
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 445998103 249 VVKDSEVMNRLPVIIFSSLITNELFHKGEAVGANAQVSKP-DIQELIGLVDKLV 301
Cdd:COG0784   70 RIRALPRLPDIPIIALTAYADEEDRERALEAGADDYLTKPvDPEELLEALRRLL 123
Response_reg pfam00072
Response regulator receiver domain; This domain receives the signal from the sensor partner in ...
176-298 2.73e-14

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: 67.56  E-value: 2.73e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445998103  176 IYIAEDSAMLRQILEETLSSAGYTKMnFFSNGAEALAQIEKlakeqgekmfEHIHLLITDIEMPKMDGHHLTKVVKDSEV 255
Cdd:pfam00072   1 VLIVDDDPLIRELLRQLLEKEGYVVA-EADDGKEALELLKE----------ERPDLILLDINMPGMDGLELLKRIRRRDP 69
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 445998103  256 mnRLPVIIFSSLITNELFHKGEAVGANAQVSKP-DIQELIGLVD 298
Cdd:pfam00072  70 --TTPVIILTAHGDEDDAVEALEAGADDFLSKPfDPDELLAAIR 111
PRK00742 PRK00742
chemotaxis-specific protein-glutamate methyltransferase CheB;
181-298 2.38e-08

chemotaxis-specific protein-glutamate methyltransferase CheB;


Pssm-ID: 234828 [Multi-domain]  Cd Length: 354  Bit Score: 54.39  E-value: 2.38e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445998103 181 DSAMLRQILEETLSS-AGYTKMNFFSNGAEALAQIEKLakeqgekmfeHIHLLITDIEMPKMDGhhLTKVVKdseVMNR- 258
Cdd:PRK00742  11 DSAFMRRLISEILNSdPDIEVVGTAPDGLEAREKIKKL----------NPDVITLDVEMPVMDG--LDALEK---IMRLr 75
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 445998103 259 -LPVIIFSSLItnelfHKGEAV-------GANAQVSKPDIQELIGLVD 298
Cdd:PRK00742  76 pTPVVMVSSLT-----ERGAEItlralelGAVDFVTKPFLGISLGMDE 118
PRK10612 PRK10612
chemotaxis protein CheW;
17-149 1.22e-07

chemotaxis protein CheW;


Pssm-ID: 182587  Cd Length: 167  Bit Score: 50.58  E-value: 1.22e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445998103  17 EIVTYTVGENLFSINVMKVREIINPFPVTTVPESHHAVEGVVQVRGEILPVINLATALNLKSTKPLDQTKFIISELNQMK 96
Cdd:PRK10612  18 EFLVFTLGDEEYGIDILKVQEIRGYDQVTRIANTPAFIKGVTNLRGVIVPIVDLRIKFSQVDVDYNDNTVVIVLNLGQRV 97
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 445998103  97 VIFRVDEVHRIQRISWEQIDEPASLSMGLE-ETTSGIVKLDGQIILLLDYEKIV 149
Cdd:PRK10612  98 VGIVVDGVSDVLSLTAEQIRPAPEFAVTLStEYLTGLGALGERMLILVNIEKLL 151
REC smart00448
cheY-homologous receiver domain; CheY regulates the clockwise rotation of E. coli flagellar ...
176-239 2.24e-06

cheY-homologous receiver domain; CheY regulates the clockwise rotation of E. coli flagellar motors. This domain contains a phosphoacceptor site that is phosphorylated by histidine kinase homologues.


Pssm-ID: 214668 [Multi-domain]  Cd Length: 55  Bit Score: 44.10  E-value: 2.24e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 445998103   176 IYIAEDSAMLRQILEETLSSAGYTkMNFFSNGAEALAQIEKlakeqgekmfEHIHLLITDIEMP 239
Cdd:smart00448   3 ILVVDDDPLLRELLKALLEKEGYE-VDEATDGEEALELLKE----------EKPDLILLDIMMP 55
 
Name Accession Description Interval E-value
CheW COG0835
Chemotaxis signal transduction protein CheW [Signal transduction mechanisms];
9-149 1.37e-39

Chemotaxis signal transduction protein CheW [Signal transduction mechanisms];


Pssm-ID: 440597  Cd Length: 151  Bit Score: 135.77  E-value: 1.37e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445998103   9 LESGTNELEIVTYTVGENLFSINVMKVREIINPFPVTTVPESHHAVEGVVQVRGEILPVINLATALNLKSTKPLDQTKFI 88
Cdd:COG0835    1 LEAGANELQYLTFRLGGERYAIPIEKVREILPLPPITPVPGAPPWVLGVINLRGRVVPVIDLRALLGLPPTEDTERTRII 80
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 445998103  89 ISELNQMKVIFRVDEVHRIQRISWEQIDE-PASLSMGLEETTSGIVKLDGQIILLLDYEKIV 149
Cdd:COG0835   81 VLEVGGRVVGLLVDSVSGVVRIDPDDIEPpPELLSGGLAPFITGVAKLDDRLILLLDLEKLL 142
CheW cd00732
CheW, a small regulator protein, unique to the chemotaxis signalling in prokaryotes and archea. ...
15-148 1.65e-37

CheW, a small regulator protein, unique to the chemotaxis signalling in prokaryotes and archea. CheW interacts with the histidine kinase CheA, most likely with the related regulatory domain of CheA. CheW is proposed to form signalling arrays together with CheA and the methyl-accepting chemotaxis proteins (MCPs), which are involved in response modulation.


Pssm-ID: 238374  Cd Length: 140  Bit Score: 130.00  E-value: 1.65e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445998103  15 ELEIVTYTVGENLFSINVMKVREIINPFPVTTVPESHHAVEGVVQVRGEILPVINLATALNLKSTKPLDQTKFIISELNQ 94
Cdd:cd00732    1 ELEVVTFRLGDEEYGIPIMQVREILKPTPITPIPNAPPYVLGVINLRGRIVPVIDLRKRLGLPPAEDTKNTRIIVVEVGD 80
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 445998103  95 MKVIFRVDEVHRIQRISWEQIDE-PASLSMGLEETTSGIVKLDGQIILLLDYEKI 148
Cdd:cd00732   81 QVVGLLVDSVSEVLRLSTDDIQPpPPVLSDINAKFIRGVVKLEGRLLILLDLDKI 135
CheW pfam01584
CheW-like domain; CheW proteins are part of the chemotaxis signaling mechanism in bacteria. ...
18-148 8.27e-36

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


Pssm-ID: 460257 [Multi-domain]  Cd Length: 131  Bit Score: 125.39  E-value: 8.27e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445998103   18 IVTYTVGENLFSINVMKVREIINPFPVTTVPESHHAVEGVVQVRGEILPVINLATALNLKSTKPLDQTKFIISELNQMKV 97
Cdd:pfam01584   1 GLLFRLGGETFAIPISKVREILRPPPITPIPGAPGYVLGVINLRGEVLPVIDLRRLLGLPPTEPRERTRVVVVEVGGQVV 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 445998103   98 IFRVDEVHRIQRISWEQIdEPASLSMGLEETTSGIVKL-DGQIILLLDYEKI 148
Cdd:pfam01584  81 GLLVDEVIGVLEIVIKQI-EPPLGLGRVAGYISGATILgDGRVVLILDVEAL 131
CheW smart00260
Two component signalling adaptor domain;
14-149 3.35e-29

Two component signalling adaptor domain;


Pssm-ID: 214588 [Multi-domain]  Cd Length: 138  Bit Score: 108.48  E-value: 3.35e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445998103    14 NELEIVTYTVGEN-LFSINVMKVREIINPFPVTTVPESHHAVEGVVQVRGEILPVINLATALNLKSTKPLDQTKFIISEL 92
Cdd:smart00260   1 TIRLPLTFAIGKDeTYAIPIAAVREILRPPPITPIPGAPGYVLGVINLRGEVLPVVDLRRLLGLPPEPPTDETRVIVVET 80
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 445998103    93 NQMKVIFRVDEVHRIQRISWEQIDEPASLSMGLEETTSGIVKL-DGQIILLLDYEKIV 149
Cdd:smart00260  81 GDRKVGLVVDSVLGVREVVVKSIEPPPPVSLSNAPGISGATILgDGRVVLILDVDKLL 138
REC_CheV-like cd19924
phosphoacceptor receiver (REC) domain of chemotaxis protein CheV and similar proteins; This ...
176-288 5.40e-29

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: 107.08  E-value: 5.40e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445998103 176 IYIAEDSAMLRQILEETLSSAGYtKMNFFSNGAEALAQIEKLAKEqGEKMFEHIHLLITDIEMPKMDGHHLTKVVKDSEV 255
Cdd:cd19924    1 ILVVDDSPTARKQLRDLLKNLGF-EIAEAVDGEEALNKLENLAKE-GNDLSKELDLIITDIEMPKMDGYELTFELRDDPR 78
                         90       100       110
                 ....*....|....*....|....*....|...
gi 445998103 256 MNRLPVIIFSSLITNELFHKGEAVGANAQVSKP 288
Cdd:cd19924   79 LANIPVILNSSLSGEFSRARGKKVGADAYLAKF 111
CheW_like cd00588
CheW-like domain. CheW proteins are part of the chemotaxis signalling mechanism in bacteria. ...
15-148 4.84e-27

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


Pssm-ID: 238331  Cd Length: 136  Bit Score: 102.74  E-value: 4.84e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445998103  15 ELEIVTYTVGENLFSINVMKVREIINPFPVTTVPESHHAVEGVVQVRGEILPVINLATALNLKSTKP-LDQTKFIISELN 93
Cdd:cd00588    1 ILQVLLFRVGDELYAIPIAVVEEILPLPPITRVPNAPDYVLGVINLRGEILPVIDLRRLFGLEAAEPdTDETRIVVVEVG 80
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 445998103  94 QMKVIFRVDEVHRIQRISWEQIDEPASLSMGLEETTSGIVKL-DGQIILLLDYEKI 148
Cdd:cd00588   81 DRKVGLVVDSVLGVLEVVIKDIEPPPDVGSSNAPGISGATILgDGRVVLILDVDKL 136
CheY COG0784
CheY-like REC (receiver) domain, includes chemotaxis protein CheY and sporulation regulator ...
169-301 9.67e-25

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: 96.46  E-value: 9.67e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445998103 169 TDRAEKVIYIAEDSAMLRQILEETLSSAGYTkMNFFSNGAEALAQIEKlakeqgekmfEHIHLLITDIEMPKMDGHHLTK 248
Cdd:COG0784    1 PPLGGKRILVVDDNPDNRELLRRLLERLGYE-VTTAEDGAEALELLRA----------GPPDLILLDINMPGMDGLELLR 69
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 445998103 249 VVKDSEVMNRLPVIIFSSLITNELFHKGEAVGANAQVSKP-DIQELIGLVDKLV 301
Cdd:COG0784   70 RIRALPRLPDIPIIALTAYADEEDRERALEAGADDYLTKPvDPEELLEALRRLL 123
PleD COG3706
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate ...
176-301 2.03e-21

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: 89.20  E-value: 2.03e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445998103 176 IYIAEDSAMLRQILEETLSSAGYtKMNFFSNGAEALAQIEKlakeqgekmfEHIHLLITDIEMPKMDGHHLTKVVKDSEV 255
Cdd:COG3706    4 ILVVDDDPTNRKLLRRLLEAAGY-EVVEAADGEEALELLQE----------HRPDLILLDLEMPDMDGLELCRRLRADPR 72
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 445998103 256 MNRLPVIIFSSLITNELFHKGEAVGANAQVSKP-DIQELIGLVDKLV 301
Cdd:COG3706   73 TADIPIIFLTALDDEEDRARALEAGADDYLTKPfDPEELLARVDLVA 119
REC_CheY4-like cd17562
phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY4 and similar CheY ...
174-301 2.12e-16

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: 73.87  E-value: 2.12e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445998103 174 KVIYIAEDSAMLRQILEETLSSAGYTKMnffsngaEALAQIEKLAKEQGEKmfehIHLLITDIEMPKMDGHHLTKVVKDS 253
Cdd:cd17562    1 KKILAVDDSASIRQMVSFTLRGAGYEVV-------EAADGRDALSKAQSKK----FDLIITDQNMPNMDGIELIKELRKL 69
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 445998103 254 EVMNRLPVIIFSSLITNELFHKGEAVGANAQVSKP-DIQELIGLVDKLV 301
Cdd:cd17562   70 PAYKFTPILMLTTESSDEKKQEGKAAGATGWLVKPfDPEQLLEVVKKVL 118
OmpR COG0745
DNA-binding response regulator, OmpR family, contains REC and winged-helix (wHTH) domain ...
176-301 3.83e-15

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: 72.68  E-value: 3.83e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445998103 176 IYIAEDSAMLRQILEETLSSAGYTkMNFFSNGAEALAQIEKlakeqgekmfEHIHLLITDIEMPKMDGHHLTKVVKDSEv 255
Cdd:COG0745    4 ILVVEDDPDIRELLADALEREGYE-VDTAADGEEALELLEE----------ERPDLILLDLMLPGMDGLEVCRRLRARP- 71
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 445998103 256 mNRLPVIIFSSLITNELFHKGEAVGANAQVSKP-DIQELIGLVDKLV 301
Cdd:COG0745   72 -SDIPIIMLTARDDEEDRVRGLEAGADDYLTKPfDPEELLARIRALL 117
YesN COG4753
Two-component response regulator, YesN/AraC family, consists of REC and AraC-type DNA-binding ...
176-288 9.99e-15

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: 68.65  E-value: 9.99e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445998103 176 IYIAEDSAMLRQILEETLSS-AGYTKMNFFSNGAEALAQIEKlakeqgekmfEHIHLLITDIEMPKMDGHHLTKVVKdsE 254
Cdd:COG4753    2 VLIVDDEPLIREGLKRILEWeAGFEVVGEAENGEEALELLEE----------HKPDLVITDINMPGMDGLELLEAIR--E 69
                         90       100       110
                 ....*....|....*....|....*....|....
gi 445998103 255 VMNRLPVIIFSSLITNELFHKGEAVGANAQVSKP 288
Cdd:COG4753   70 LDPDTKIIILSGYSDFEYAQEAIKLGADDYLLKP 103
Response_reg pfam00072
Response regulator receiver domain; This domain receives the signal from the sensor partner in ...
176-298 2.73e-14

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: 67.56  E-value: 2.73e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445998103  176 IYIAEDSAMLRQILEETLSSAGYTKMnFFSNGAEALAQIEKlakeqgekmfEHIHLLITDIEMPKMDGHHLTKVVKDSEV 255
Cdd:pfam00072   1 VLIVDDDPLIRELLRQLLEKEGYVVA-EADDGKEALELLKE----------ERPDLILLDINMPGMDGLELLKRIRRRDP 69
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 445998103  256 mnRLPVIIFSSLITNELFHKGEAVGANAQVSKP-DIQELIGLVD 298
Cdd:pfam00072  70 --TTPVIILTAHGDEDDAVEALEAGADDFLSKPfDPDELLAAIR 111
AtoC COG2204
DNA-binding transcriptional response regulator, NtrC family, contains REC, AAA-type ATPase, ...
176-301 4.68e-14

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: 71.92  E-value: 4.68e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445998103 176 IYIAEDSAMLRQILEETLSSAGYTkMNFFSNGAEALAQIEKlakeqgekmfEHIHLLITDIEMPKMDGHHLTKVVKdsEV 255
Cdd:COG2204    5 ILVVDDDPDIRRLLKELLERAGYE-VETAASGEEALALLRE----------EPPDLVLLDLRMPGMDGLELLRELR--AL 71
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 445998103 256 MNRLPVIIFSSLITNELFHKGEAVGANAQVSKP-DIQELIGLVDKLV 301
Cdd:COG2204   72 DPDLPVILLTGYGDVETAVEAIKAGAFDYLTKPfDLEELLAAVERAL 118
REC cd00156
phosphoacceptor receiver (REC) domain of response regulators (RRs) and pseudo response ...
178-288 5.31e-14

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: 66.48  E-value: 5.31e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445998103 178 IAEDSAMLRQILEETLSSAGYtKMNFFSNGAEALAQIEKlakeqgekmfEHIHLLITDIEMPKMDGHHLTKVVKDSEvmN 257
Cdd:cd00156    2 IVDDDPAIRELLKSLLEREGY-EVDTAADGEEALELLRE----------ERPDLVLLDLMMPGMDGLELLRKLRELP--P 68
                         90       100       110
                 ....*....|....*....|....*....|.
gi 445998103 258 RLPVIIFSSLITNELFHKGEAVGANAQVSKP 288
Cdd:cd00156   69 DIPVIVLTAKADEEDAVRALELGADDYLVKP 99
RpfG COG3437
Response regulator c-di-GMP phosphodiesterase, RpfG family, contains REC and HD-GYP domains ...
169-301 1.65e-13

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: 68.27  E-value: 1.65e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445998103 169 TDRAEKVIyIAEDSAMLRQILEETLSSAGYTKMnFFSNGAEALAQIEKlakeqgekmfEHIHLLITDIEMPKMDGHHLTK 248
Cdd:COG3437    3 TGQAPTVL-IVDDDPENLELLRQLLRTLGYDVV-TAESGEEALELLLE----------APPDLILLDVRMPGMDGFELLR 70
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 445998103 249 VVKDSEVMNRLPVIIFSSLITNELFHKGEAVGANAQVSKP-DIQELIGLVDKLV 301
Cdd:COG3437   71 LLRADPSTRDIPVIFLTALADPEDRERALEAGADDYLTKPfDPEELLARVRNAL 124
REC_Rcp-like cd17557
phosphoacceptor receiver (REC) domain of cyanobacterial phytochrome response regulator Rcp and ...
176-300 8.96e-12

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: 61.28  E-value: 8.96e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445998103 176 IYIAEDSAMLRQILEETLSSAGYT-KMNFFSNGAEALAQiekLAKEQGEKMFEHIHLLITDIEMPKMDGHHLTKVVKDSE 254
Cdd:cd17557    2 ILLVEDNPGDAELIQEAFKEAGVPnELHVVRDGEEALDF---LRGEGEYADAPRPDLILLDLNMPRMDGFEVLREIKADP 78
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 445998103 255 VMNRLPVIIFSSLITNELFHKGEAVGANAQVSKP-DIQELIGLVDKL 300
Cdd:cd17557   79 DLRRIPVVVLTTSDAEEDIERAYELGANSYIVKPvDFEEFVEAIRSL 125
REC_NtrC cd19919
phosphoacceptor receiver (REC) domain of DNA-binding transcriptional regulator NtrC; ...
174-299 1.30e-11

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: 60.36  E-value: 1.30e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445998103 174 KVIYIAEDSAMLRQILEETLSSAGYTkMNFFSNGAEALAQIEKlakeqgekmfEHIHLLITDIEMPKMDGHHLTKVVKds 253
Cdd:cd19919    1 KTVWIVDDDSSIRWVLERALAGAGLT-VTSFENAQEALAALAS----------SQPDVLISDIRMPGMDGLALLAQIK-- 67
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 445998103 254 EVMNRLPVII---FSSLITNELFHKGeavGANAQVSKP-DIQELIGLVDK 299
Cdd:cd19919   68 QRHPDLPVIImtaHSDLDSAVSAYQG---GAFEYLPKPfDIDEAVALVER 114
REC_hyHK_CKI1_RcsC-like cd17546
phosphoacceptor receiver (REC) domain of hybrid sensor histidine kinases/response regulators ...
178-294 1.52e-11

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: 60.18  E-value: 1.52e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445998103 178 IAEDSAMLRQILEETLSSAGYTkMNFFSNGAEALAQIEKlakeqgekmfEHIHLLITDIEMPKMDGHHLTKVVKDSEVMN 257
Cdd:cd17546    3 VVDDNPVNRKVLKKLLEKLGYE-VDVAENGQEALELLKE----------EPFDLVLMDLQMPVMDGLEATRRIRELEGGG 71
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 445998103 258 -RLPVIIFSSLITNELFHKGEAVGANAQVSKP-DIQELI 294
Cdd:cd17546   72 rRTPIIALTANALEEDREKCLEAGMDDYLSKPvKLDQLK 110
REC_CpdR_CckA-like cd18160
phosphoacceptor receiver (REC) domain of Brucella abortus CpdR and CckA, and similar domains; ...
176-288 4.93e-11

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: 58.67  E-value: 4.93e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445998103 176 IYIAEDSAMLRQILEETLSSAGYTkMNFFSNGAEALaqiEKLakEQGEKmfehIHLLITDIEMPKMDGHHLTKVVKdsEV 255
Cdd:cd18160    2 ILLADDEPSVRKFIVTTLKKAGYA-VTEAESGAEAL---EKL--QQGKD----IDIVVTDIVMPEMDGIELAREAR--KI 69
                         90       100       110
                 ....*....|....*....|....*....|...
gi 445998103 256 MNRLPVIIFSSLITNELFHKGEAVGANAQVSKP 288
Cdd:cd18160   70 DPDVKILFISGGAAAAPELLSDAVGDNATLKKP 102
REC_OmpR cd17574
phosphoacceptor receiver (REC) domain of OmpR family response regulators; OmpR-like proteins ...
178-288 2.51e-10

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: 56.26  E-value: 2.51e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445998103 178 IAEDSAMLRQILEETLSSAGYTkMNFFSNGAEALAQIEKlakeqgekmfEHIHLLITDIEMPKMDGHHLTKVVKdsEVMN 257
Cdd:cd17574    2 VVEDDEEIAELLSDYLEKEGYE-VDTAADGEEALELARE----------EQPDLIILDVMLPGMDGFEVCRRLR--EKGS 68
                         90       100       110
                 ....*....|....*....|....*....|...
gi 445998103 258 RLPVIIFSSLitNELFHKGEA--VGANAQVSKP 288
Cdd:cd17574   69 DIPIIMLTAK--DEEEDKVLGleLGADDYITKP 99
REC_CheB-like cd17541
phosphoacceptor receiver (REC) domain of chemotaxis response regulator protein-glutamate ...
178-271 3.30e-10

phosphoacceptor receiver (REC) domain of chemotaxis response regulator protein-glutamate methylesterase CheB and similar chemotaxis proteins; Methylesterase CheB is a chemotaxis response regulator with an N-terminal REC domain and a C-terminal methylesterase domain. Chemotaxis is a behavior known in motile bacteria that directs their movement in response to chemical gradients. CheB is a phosphorylation-activated response regulator involved in the reversible modification of bacterial chemotaxis receptors. It catalyzes the demethylation of specific methylglutamate residues introduced into the chemoreceptors (methyl-accepting chemotaxis proteins) by CheR. The CheB REC domain packs against the active site of the C-terminal domain and inhibits methylesterase activity by directly restricting access to the active site. Also included in this family is chemotaxis response regulator CheY, which contains a stand-alone REC domain, and an uncharacterized subfamily composed of proteins containing an N-terminal REC domain and a C-terminal CheY-P phosphatase (CheC) domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381096 [Multi-domain]  Cd Length: 125  Bit Score: 56.63  E-value: 3.30e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445998103 178 IAEDSAMLRQILEETLSSAGYTK-MNFFSNGAEALAQIEKLakeqgekmfeHIHLLITDIEMPKMDGHHLTKvvkdsEVM 256
Cdd:cd17541    5 IVDDSAVMRKLLSRILESDPDIEvVGTARDGEEALEKIKEL----------KPDVITLDIEMPVMDGLEALR-----RIM 69
                         90
                 ....*....|....*..
gi 445998103 257 --NRLPVIIFSSLITNE 271
Cdd:cd17541   70 aeRPTPVVMVSSLTEEG 86
REC_CheY_CheY3 cd19923
phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY3 and similar CheY ...
176-288 3.58e-10

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: 56.58  E-value: 3.58e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445998103 176 IYIAEDSAMLRQILEETLSSAGYTKMNFFSNGAEALAQIEKlakeqgekmfEHIHLLITDIEMPKMDGHHLTKVVKDSEV 255
Cdd:cd19923    3 VLVVDDFSTMRRIIKNLLKELGFNNVEEAEDGVDALEKLKA----------GGFDFVITDWNMPNMDGLELLKTIRADGA 72
                         90       100       110
                 ....*....|....*....|....*....|...
gi 445998103 256 MNRLPVIIFSSLITNELFHKGEAVGANAQVSKP 288
Cdd:cd19923   73 LSHLPVLMVTAEAKKENVIAAAQAGVNNYIVKP 105
REC_hyHK cd17598
phosphoacceptor receiver (REC) domain of uncharacterized hybrid sensor histidine kinase ...
176-288 4.18e-10

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: 56.57  E-value: 4.18e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445998103 176 IYIAEDSAMLRQILEETLSSAGYtKMNFFSNGAEALAQIEKLAKEqgekmfehihLLITDIEMPKMDGHHLTKVVKDSEV 255
Cdd:cd17598    1 ILIVEDSPTQAEQLKHILEEQGY-KVQVARNGREALAMLAEHRPT----------LVISDIVMPEMDGYELCRKIKSDPD 69
                         90       100       110
                 ....*....|....*....|....*....|...
gi 445998103 256 MNRLPVIIFSSLITNELFHKGEAVGANAQVSKP 288
Cdd:cd17598   70 LKDIPVILLTTLSDPRDVIRGLECGADNFITKP 102
REC_PdtaR-like cd19932
phosphoacceptor receiver (REC) domain of PdtaR and similar proteins; This subfamily includes ...
176-288 1.12e-09

phosphoacceptor receiver (REC) domain of PdtaR and similar proteins; This subfamily includes Mycobacterium tuberculosis PdtaR, also called Rv1626, and similar proteins containing a REC domain and an ANTAR (AmiR and NasR transcription antitermination regulators) RNA-binding output domain. PdtaR is a response regulator that acts at the level of transcriptional antitermination and is a member of the PdtaR/PdtaS two-component regulatory system. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381159 [Multi-domain]  Cd Length: 118  Bit Score: 55.11  E-value: 1.12e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445998103 176 IYIAEDSAMLRQILEETLSSAGYTKMNFFSNGAEALAQIEKLAKEqgekmfehihLLITDIEMPKMDGHHLTKVVKDSEV 255
Cdd:cd19932    3 VLIAEDEALIRMDLREMLEEAGYEVVGEASDGEEAVELAKKHKPD----------LVIMDVKMPRLDGIEAAKIITSENI 72
                         90       100       110
                 ....*....|....*....|....*....|...
gi 445998103 256 MnrlPVIIFSSLITNELFHKGEAVGANAQVSKP 288
Cdd:cd19932   73 A---PIVLLTAYSQQDLVERAKEAGAMAYLVKP 102
REC_RpfG-like cd17551
phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase response regulator ...
176-294 2.69e-09

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: 53.99  E-value: 2.69e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445998103 176 IYIAEDSAMLRQILEETLSSAGYTKMNFFSNGAEALAQIEKlakeqgekmfEHIHLLITDIEMPKMDGHHLTKVVKDSEV 255
Cdd:cd17551    3 ILIVDDNPTNLLLLEALLRSAGYLEVVSFTDPREALAWCRE----------NPPDLILLDYMMPGMDGLEFIRRLRALPG 72
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 445998103 256 MNRLPVIIFSSLITNELFHKGEAVGANAQVSKP-DIQELI 294
Cdd:cd17551   73 LEDVPIVMITADTDREVRLRALEAGATDFLTKPfDPVELL 112
REC_D1_PleD-like cd17538
first (D1) phosphoacceptor receiver (REC) domain of response regulator PleD and similar ...
176-288 3.44e-09

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: 53.27  E-value: 3.44e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445998103 176 IYIAEDSAMLRQILEETLSSAGYTKMnFFSNGAEALAQIEKlakeqgekmfEHIHLLITDIEMPKMDGHHLTKVVKDSEV 255
Cdd:cd17538    2 ILVVDDEPANRELLEALLSAEGYEVL-TADSGQEALALAEE----------ELPDLILLDVMMPGMDGFEVCRRLKEDPE 70
                         90       100       110
                 ....*....|....*....|....*....|...
gi 445998103 256 MNRLPVIIFSSLITNELFHKGEAVGANAQVSKP 288
Cdd:cd17538   71 TRHIPVIMITALDDREDRIRGLEAGADDFLSKP 103
REC_TrrA-like cd17554
phosphoacceptor receiver (REC) domain of Thermotoga maritima response regulator TrrA and ...
174-266 9.98e-09

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: 52.22  E-value: 9.98e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445998103 174 KVIYIAEDSAMLRQILEETLSSAGYtKMNFFSNGAEALAQIEKlakeqgekmfEHIHLLITDIEMPKMDGHHLTKVVKds 253
Cdd:cd17554    1 KKILVVDDEENIRELYKEELEDEGY-EVVTAGNGEEALEKLES----------EDPDLVILDIKMPGMDGLETLRKIR-- 67
                         90
                 ....*....|...
gi 445998103 254 EVMNRLPVIIFSS 266
Cdd:cd17554   68 EKKPDLPVIICTA 80
REC_DivK-like cd17548
phosphoacceptor receiver (REC) domain of DivK and similar proteins; Caulobacter crescentus ...
175-299 1.51e-08

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: 51.77  E-value: 1.51e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445998103 175 VIYIAEDSAMLRQILEETLSSAGYTKMNFfSNGAEALAQIEKlakeqgekmfEHIHLLITDIEMPKMDGHHLTKVVKDSE 254
Cdd:cd17548    1 KILIVEDNPLNMKLARDLLESAGYEVLEA-ADGEEALEIARK----------EKPDLILMDIQLPGMDGLEATRLLKEDP 69
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 445998103 255 VMNRLPVIIFSSLITNELFHKGEAVGANAQVSKP-DIQELIGLVDK 299
Cdd:cd17548   70 ATRDIPVIALTAYAMKGDREKILEAGCDGYISKPiDTREFLETVAK 115
REC_YesN-like cd17536
phosphoacceptor receiver (REC) domain of YesN and related helix-turn-helix containing response ...
178-265 1.81e-08

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: 51.95  E-value: 1.81e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445998103 178 IAEDSAMLRQILEETL--SSAGYTKMNFFSNGAEALAQIEKlakeqgekmfEHIHLLITDIEMPKMDGHHLTKVVKdsEV 255
Cdd:cd17536    3 IVDDEPLIREGLKKLIdwEELGFEVVGEAENGEEALELIEE----------HKPDIVITDIRMPGMDGLELIEKIR--EL 70
                         90
                 ....*....|
gi 445998103 256 MNRLPVIIFS 265
Cdd:cd17536   71 YPDIKIIILS 80
REC_Ycf29 cd19927
phosphoacceptor receiver (REC) domain of probable transcriptional regulator Ycf29; Ycf29 is a ...
176-288 2.19e-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: 51.22  E-value: 2.19e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445998103 176 IYIAEDSAMLRQILEETLSSAGYTkMNFFSNGAEALAqieklakeqgEKMFEHIHLLITDIEMPKMDGHHLTKVVKDSEV 255
Cdd:cd19927    1 ILLVDDDPGIRLAVKDYLEDQGFT-VIAASNGLEALD----------LLNQYIPDLIISDIIMPGVDGYSLLGKLRKNAD 69
                         90       100       110
                 ....*....|....*....|....*....|...
gi 445998103 256 MNRLPVIIFSSLITNELFHKGEAVGANAQVSKP 288
Cdd:cd19927   70 FDTIPVIFLTAKGMTSDRIKGYNAGCDGYLSKP 102
PRK00742 PRK00742
chemotaxis-specific protein-glutamate methyltransferase CheB;
181-298 2.38e-08

chemotaxis-specific protein-glutamate methyltransferase CheB;


Pssm-ID: 234828 [Multi-domain]  Cd Length: 354  Bit Score: 54.39  E-value: 2.38e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445998103 181 DSAMLRQILEETLSS-AGYTKMNFFSNGAEALAQIEKLakeqgekmfeHIHLLITDIEMPKMDGhhLTKVVKdseVMNR- 258
Cdd:PRK00742  11 DSAFMRRLISEILNSdPDIEVVGTAPDGLEAREKIKKL----------NPDVITLDVEMPVMDG--LDALEK---IMRLr 75
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 445998103 259 -LPVIIFSSLItnelfHKGEAV-------GANAQVSKPDIQELIGLVD 298
Cdd:PRK00742  76 pTPVVMVSSLT-----ERGAEItlralelGAVDFVTKPFLGISLGMDE 118
REC_typeB_ARR-like cd17584
phosphoacceptor receiver (REC) domain of type B Arabidopsis response regulators (ARRs) and ...
181-288 3.57e-08

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: 50.70  E-value: 3.57e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445998103 181 DSAMLRQILEETLSSAGYtKMNFFSNGAEALAQIEKLAKEqgekmfehIHLLITDIEMPKMDGHHLTKVVKdsEVMNrLP 260
Cdd:cd17584    6 DDPTCLAILKRMLLRCGY-QVTTCTDAEEALSMLRENKDE--------FDLVITDVHMPDMDGFEFLELIR--LEMD-LP 73
                         90       100
                 ....*....|....*....|....*...
gi 445998103 261 VIIFSSLITNELFHKGEAVGANAQVSKP 288
Cdd:cd17584   74 VIMMSADGSTSTVMKGLAHGACDYLLKP 101
orf27 CHL00148
Ycf27; Reviewed
168-288 5.66e-08

Ycf27; Reviewed


Pssm-ID: 214376 [Multi-domain]  Cd Length: 240  Bit Score: 52.41  E-value: 5.66e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445998103 168 KTDRAEKvIYIAEDSAMLRQILEETLSSAGYTKMNFfSNGAEALAQIEklakeqgekmFEHIHLLITDIEMPKMDGHHL- 246
Cdd:CHL00148   2 MENSKEK-ILVVDDEAYIRKILETRLSIIGYEVITA-SDGEEALKLFR----------KEQPDLVILDVMMPKLDGYGVc 69
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 445998103 247 TKVVKDSEVmnrlPVIIFSSL--ITNELfhKGEAVGANAQVSKP 288
Cdd:CHL00148  70 QEIRKESDV----PIIMLTALgdVSDRI--TGLELGADDYVVKP 107
CitB COG4565
DNA-binding response regulator DpiB of citrate/malate metabolism [Transcription, Signal ...
178-301 7.09e-08

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


Pssm-ID: 443622 [Multi-domain]  Cd Length: 138  Bit Score: 50.74  E-value: 7.09e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445998103 178 IAEDSAMLRQILEETLSS-AGYTKMNFFSNGAEALAQIEKlakeqgekmfEHIHLLITDIEMPKMDGhhlTKVVKD-SEV 255
Cdd:COG4565    8 IVEDDPMVAELLRRYLERlPGFEVVGVASSGEEALALLAE----------HRPDLILLDIYLPDGDG---LELLRElRAR 74
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 445998103 256 MNRLPVIIFSSLITNELFHKGEAVGANAQVSKP-DIQELIGLVDKLV 301
Cdd:COG4565   75 GPDVDVIVITAARDPETVREALRAGVVDYLIKPfTFERLREALERYL 121
PRK10612 PRK10612
chemotaxis protein CheW;
17-149 1.22e-07

chemotaxis protein CheW;


Pssm-ID: 182587  Cd Length: 167  Bit Score: 50.58  E-value: 1.22e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445998103  17 EIVTYTVGENLFSINVMKVREIINPFPVTTVPESHHAVEGVVQVRGEILPVINLATALNLKSTKPLDQTKFIISELNQMK 96
Cdd:PRK10612  18 EFLVFTLGDEEYGIDILKVQEIRGYDQVTRIANTPAFIKGVTNLRGVIVPIVDLRIKFSQVDVDYNDNTVVIVLNLGQRV 97
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 445998103  97 VIFRVDEVHRIQRISWEQIDEPASLSMGLE-ETTSGIVKLDGQIILLLDYEKIV 149
Cdd:PRK10612  98 VGIVVDGVSDVLSLTAEQIRPAPEFAVTLStEYLTGLGALGERMLILVNIEKLL 151
REC_OmpR_DrrD-like cd17625
phosphoacceptor receiver (REC) domain of DrrD-like OmpR family response regulators; DrrD is a ...
178-301 2.07e-07

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: 48.76  E-value: 2.07e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445998103 178 IAEDSAMLRQILEETLSSAGYTkMNFFSNGAEALAQIeklakeqgekmFEHIH-LLITDIEMPKMDGHHLTKVVKDSEVM 256
Cdd:cd17625    2 VVEDEKDLSEAITKHLKKEGYT-VDVCFDGEEGLEYA-----------LSGIYdLIILDIMLPGMDGLEVLKSLREEGIE 69
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 445998103 257 nrLPVIIFSSLITNELFHKGEAVGANAQVSKP-DIQELIGLVDKLV 301
Cdd:cd17625   70 --TPVLLLTALDAVEDRVKGLDLGADDYLPKPfSLAELLARIRALL 113
REC_2_GGDEF cd17544
second phosphoacceptor receiver (REC) domain of uncharacterized GGDEF domain proteins; This ...
176-292 2.26e-07

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: 48.67  E-value: 2.26e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445998103 176 IYIAEDSAMLRQILEETLSsagytKMNF----FSNGAEALAQIEklakeqgekmfEH--IHLLITDIEMPKMDGHHLTKV 249
Cdd:cd17544    3 VLVVDDSATSRNHLRALLR-----RHNFqvleAANGQEALEVLE-----------QHpdIKLVITDYNMPEMDGFELVRE 66
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 445998103 250 VKDSEVMNRLPVIIFSSLITNEL---FHKGeavGANAQVSKPDIQE 292
Cdd:cd17544   67 IRKKYSRDQLAIIGISASGDNALsarFIKA---GANDFLTKPFLPE 109
glnG PRK10923
nitrogen regulation protein NR(I); Provisional
175-301 3.22e-07

nitrogen regulation protein NR(I); Provisional


Pssm-ID: 182842 [Multi-domain]  Cd Length: 469  Bit Score: 51.41  E-value: 3.22e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445998103 175 VIYIAEDSAMLRQILEETLSSAGYTKMNFfSNGAEALaqiEKLAKEQGEkmfehihLLITDIEMPKMDGHHLTKVVKDSE 254
Cdd:PRK10923   5 IVWVVDDDSSIRWVLERALAGAGLTCTTF-ENGNEVL---EALASKTPD-------VLLSDIRMPGMDGLALLKQIKQRH 73
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 445998103 255 VMnrLPVIIFSSLITNELFHKGEAVGANAQVSKP-DIQELIGLVDKLV 301
Cdd:PRK10923  74 PM--LPVIIMTAHSDLDAAVSAYQQGAFDYLPKPfDIDEAVALVERAI 119
AmiR COG3707
Two-component response regulator, AmiR/NasT family, consists of REC and RNA-binding ...
176-288 3.45e-07

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: 49.57  E-value: 3.45e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445998103 176 IYIAEDSAMLRQILEETLSSAGYTKMNFFSNGAEALAQIEKLakeqgekmfeHIHLLITDIEMPKMDGhhlTKVVKDSEV 255
Cdd:COG3707    6 VLVVDDEPLRRADLREGLREAGYEVVAEAADGEDAVELVREL----------KPDLVIVDIDMPDRDG---LEAARQISE 72
                         90       100       110
                 ....*....|....*....|....*....|...
gi 445998103 256 MNRLPVIIFSSLITNELFHKGEAVGANAQVSKP 288
Cdd:COG3707   73 ERPAPVILLTAYSDPELIERALEAGVSAYLVKP 105
REC_NarL-like cd17535
phosphoacceptor receiver (REC) domain of NarL (Nitrate/Nitrite response regulator L) family ...
176-294 8.10e-07

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: 47.12  E-value: 8.10e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445998103 176 IYIAEDSAMLRQILEETLSSA-GYTKMNFFSNGAEALAQIEKLakeqgekmfeHIHLLITDIEMPKMDGHHLTKVVKdsE 254
Cdd:cd17535    1 VLIVDDHPLVREGLRRLLESEpDIEVVGEAADGEEALALLREL----------RPDVVLMDLSMPGMDGIEALRRLR--R 68
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 445998103 255 VMNRLPVIIFSSLITNELFHKGEAVGANAQVSKP-DIQELI 294
Cdd:cd17535   69 RYPDLKVIVLTAHDDPEYVLRALKAGAAGYLLKDsSPEELI 109
REC_typeA_ARR cd17581
phosphoacceptor receiver (REC) domain of type A Arabidopsis response regulators (ARRs) and ...
180-266 1.12e-06

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: 46.98  E-value: 1.12e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445998103 180 EDSAMLRQILEETLSSAGYtKMNFFSNGAEALaqiEKLAKEQGEKMFEH----IHLLITDIEMPKMDGHHLTKVVKDSEV 255
Cdd:cd17581    5 DDSLVDRKVIERLLRISSC-RVTAVDSGKRAL---EFLGLEDEEDSSNFnepkVNMIITDYCMPGMTGYDLLKKVKESSA 80
                         90
                 ....*....|.
gi 445998103 256 MNRLPVIIFSS 266
Cdd:cd17581   81 LKEIPVVIMSS 91
REC_DctD-like cd17549
phosphoacceptor receiver (REC) domain of C4-dicarboxylic acid transport protein D (DctD) and ...
175-269 1.39e-06

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: 46.71  E-value: 1.39e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445998103 175 VIYIaEDSAMLRQILEETLSSAGYtKMNFFSNGAEALAQIEKlakeqgekMFEHIhlLITDIEMPKMDGHHLTKVVK--D 252
Cdd:cd17549    1 VLLV-DDDADVREALQQTLELAGF-RVRAFADAEEALAALSP--------DFPGV--VISDIRMPGMDGLELLAQIRelD 68
                         90
                 ....*....|....*..
gi 445998103 253 SEvmnrLPVIifssLIT 269
Cdd:cd17549   69 PD----LPVI----LIT 77
REC_2_DhkD-like cd17580
second phosphoacceptor receiver (REC) domain of Dictyostelium discoideum hybrid signal ...
176-297 1.61e-06

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: 45.91  E-value: 1.61e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445998103 176 IYIAEDSAMLRQILEETLSSAGYTkMNFFSNGAEALAQIEKLAKEqgekmfehihLLITDIEMPKMDGHHLTKVVKDSEV 255
Cdd:cd17580    1 ILVVDDNEDAAEMLALLLELEGAE-VTTAHSGEEALEAAQRFRPD----------VILSDIGMPGMDGYELARRLRELPW 69
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 445998103 256 MNRLPVIIFSSLITNELFHKGEAVGANAQVSKP-DIQELIGLV 297
Cdd:cd17580   70 LANTPAIALTGYGQPEDRERALEAGFDAHLVKPvDPDELIELI 112
REC smart00448
cheY-homologous receiver domain; CheY regulates the clockwise rotation of E. coli flagellar ...
176-239 2.24e-06

cheY-homologous receiver domain; CheY regulates the clockwise rotation of E. coli flagellar motors. This domain contains a phosphoacceptor site that is phosphorylated by histidine kinase homologues.


Pssm-ID: 214668 [Multi-domain]  Cd Length: 55  Bit Score: 44.10  E-value: 2.24e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 445998103   176 IYIAEDSAMLRQILEETLSSAGYTkMNFFSNGAEALAQIEKlakeqgekmfEHIHLLITDIEMP 239
Cdd:smart00448   3 ILVVDDDPLLRELLKALLEKEGYE-VDEATDGEEALELLKE----------EKPDLILLDIMMP 55
REC_PA4781-like cd19920
phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase PA4781 and similar ...
176-288 2.30e-06

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: 45.19  E-value: 2.30e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445998103 176 IYIAEDSAMLRQILEETLSSAGYtKMNFFSNGAEALAQIEklakeqgekmFEHIHLLITDIEMPKMDGHHLTKVVKDSEV 255
Cdd:cd19920    1 ILIVDDVPDNLRLLSELLRAAGY-RVLVATDGQQALQRAQ----------AEPPDLILLDVMMPGMDGFEVCRRLKADPA 69
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 445998103 256 MNRLPVIIFSSLitNELFHK--GEAVGANAQVSKP 288
Cdd:cd19920   70 TRHIPVIFLTAL--TDTEDKvkGFELGAVDYITKP 102
PRK12555 PRK12555
chemotaxis-specific protein-glutamate methyltransferase CheB;
176-290 3.31e-06

chemotaxis-specific protein-glutamate methyltransferase CheB;


Pssm-ID: 237135 [Multi-domain]  Cd Length: 337  Bit Score: 47.95  E-value: 3.31e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445998103 176 IYIAEDSAMLRQILEETLSS-AGYTKMNFFSNGAEALAQIEKLAKEqgekmfehihLLITDIEMPKMDGHHLTKvvkdsE 254
Cdd:PRK12555   3 IGIVNDSPLAVEALRRALARdPDHEVVWVATDGAQAVERCAAQPPD----------VILMDLEMPRMDGVEATR-----R 67
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 445998103 255 VMNR--LPVIIFSSLI---TNELFhkgEAVGANA--QVSKPDI 290
Cdd:PRK12555  68 IMAErpCPILIVTSLTernASRVF---EAMGAGAldAVDTPTL 107
REC_OmpR_BsPhoP-like cd19937
phosphoacceptor receiver (REC) domain of BsPhoP-like OmpR family response regulators; Bacillus ...
177-302 4.78e-06

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


Pssm-ID: 381164 [Multi-domain]  Cd Length: 116  Bit Score: 44.96  E-value: 4.78e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445998103 177 YIAEDSAMLRQILEETLSSAGYtKMNFFSNGAEALAQIEKlakeqgekmfEHIHLLITDIEMPKMDGHHLTKVVKDSEVM 256
Cdd:cd19937    1 LVVDDEEDIVELLKYNLEKEGY-EVVTAYDGEEALKRAKD----------EKPDLIILDLMLPGIDGLEVCRILRSDPKT 69
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 445998103 257 NRLPVIIFSSliTNELFHK--GEAVGANAQVSKP-DIQELIGLVdKLVL 302
Cdd:cd19937   70 SSIPIIMLTA--KGEEFDKvlGLELGADDYITKPfSPRELLARV-KAVL 115
REC_OmpR_PmrA-like cd17624
phosphoacceptor receiver (REC) domain of PmrA-like OmpR family response regulators; This ...
176-294 6.68e-06

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: 44.40  E-value: 6.68e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445998103 176 IYIAEDSAMLRQILEETLSSAGYTkMNFFSNGAEALAQIEKlakeqgekmfEHIHLLITDIEMPKMDGHHLTKVVKDSEv 255
Cdd:cd17624    1 ILLVEDDALLGDGLKTGLRKAGYA-VDWVRTGAEAEAALAS----------GPYDLVILDLGLPDGDGLDLLRRWRRQG- 68
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 445998103 256 mNRLPVIIFSSLITNELFHKGEAVGANAQVSKP-DIQELI 294
Cdd:cd17624   69 -QSLPVLILTARDGVDDRVAGLDAGADDYLVKPfALEELL 107
CitB COG2197
DNA-binding response regulator, NarL/FixJ family, contains REC and HTH domains [Signal ...
176-248 7.09e-06

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


Pssm-ID: 441799 [Multi-domain]  Cd Length: 131  Bit Score: 44.50  E-value: 7.09e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 445998103 176 IYIAEDSAMLRQILEETLSSA-GYTKMNFFSNGAEALAQIEKLakeqgekmfeHIHLLITDIEMPKMDGHHLTK 248
Cdd:COG2197    4 VLIVDDHPLVREGLRALLEAEpDIEVVGEAADGEEALELLEEL----------RPDVVLLDIRMPGMDGLEALR 67
REC_CheC-like cd17593
phosphoacceptor receiver (REC) domain of uncharacterized response regulators containing a CheC ...
176-288 7.53e-06

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: 44.45  E-value: 7.53e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445998103 176 IYIAEDSAMLRQILEETLSSAGYTKMNFFSNGAEALAQIEKlakeqgekmfEHIHLLITDIEMPKMDGHHLTKVVKDSEV 255
Cdd:cd17593    3 VLICDDSSMARKQLARALPADWDVEITFAENGEEALEILRE----------GRIDVLFLDLTMPVMDGYEVLEALPVEQL 72
                         90       100       110
                 ....*....|....*....|....*....|...
gi 445998103 256 mnRLPVIIFSSLITNELFHKGEAVGANAQVSKP 288
Cdd:cd17593   73 --ETKVIVVSGDVQPEAKERVLELGALAFLKKP 103
PRK10610 PRK10610
chemotaxis protein CheY;
178-288 8.41e-06

chemotaxis protein CheY;


Pssm-ID: 170568 [Multi-domain]  Cd Length: 129  Bit Score: 44.58  E-value: 8.41e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445998103 178 IAEDSAMLRQILEETLSSAGYTKMNFFSNGAEALAQIEKLAkeqgekmfehIHLLITDIEMPKMDGHHLTKVVKDSEVMN 257
Cdd:PRK10610  10 VVDDFSTMRRIVRNLLKELGFNNVEEAEDGVDALNKLQAGG----------FGFVISDWNMPNMDGLELLKTIRADGAMS 79
                         90       100       110
                 ....*....|....*....|....*....|.
gi 445998103 258 RLPVIIFSSLITNELFHKGEAVGANAQVSKP 288
Cdd:PRK10610  80 ALPVLMVTAEAKKENIIAAAQAGASGYVVKP 110
REC_DesR-like cd19930
phosphoacceptor receiver (REC) domain of DesR and similar proteins; This group is composed of ...
176-253 2.00e-05

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: 43.03  E-value: 2.00e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445998103 176 IYIAEDSAMLRQIL------EETLSSAGYTkmnffSNGAEALAQIEKLAKEqgekmfehihLLITDIEMPKMDGHHLTKV 249
Cdd:cd19930    1 VLIAEDQEMVRGALaallelEDDLEVVAQA-----SNGQEALRLVLKHSPD----------VAILDIEMPGRTGLEVAAE 65

                 ....
gi 445998103 250 VKDS 253
Cdd:cd19930   66 LREE 69
REC_CheY cd17542
phosphoacceptor receiver (REC) domain of chemotaxis protein CheY; The chemotaxis response ...
176-288 6.94e-05

phosphoacceptor receiver (REC) domain of chemotaxis protein CheY; The chemotaxis response regulator CheY contains a stand-alone REC domain. Chemotaxis is a behavior known for motile bacteria that directs their movement in response to chemical gradients. CheY is involved in transmitting sensory signals from chemoreceptors to the flagellar motors. Phosphorylated CheY interacts with the flagella switch components FliM and FliY, which causes counterclockwise rotation of the flagella, resulting in smooth swimming. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381097 [Multi-domain]  Cd Length: 117  Bit Score: 41.50  E-value: 6.94e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445998103 176 IYIAEDSAMLRQILEETLSSAGYTKMNFFSNGAEALaqieKLAKEqgekmfEHIHLLITDIEMPKMDGHHLTKVVK--DS 253
Cdd:cd17542    3 VLIVDDAAFMRMMLKDILTKAGYEVVGEAANGEEAV----EKYKE------LKPDLVTMDITMPEMDGIEALKEIKkiDP 72
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 445998103 254 EVMnrlpVIIFSSLITNELFHKGEAVGANAQVSKP 288
Cdd:cd17542   73 NAK----VIMCSAMGQEEMVKEAIKAGAKDFIVKP 103
PLN03029 PLN03029
type-a response regulator protein; Provisional
180-266 9.54e-05

type-a response regulator protein; Provisional


Pssm-ID: 215544 [Multi-domain]  Cd Length: 222  Bit Score: 42.71  E-value: 9.54e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445998103 180 EDSAMLRQILEETLSSAGYtKMNFFSNGAEALA------------QIEKLAKEQGEKMfeHIHLLITDIEMPKMDGHHLT 247
Cdd:PLN03029  15 DDSLIDRKLIEKLLKTSSY-QVTTVDSGSKALKflglheddrsnpDTPSVSPNSHQEV--EVNLIITDYCMPGMTGYDLL 91
                         90
                 ....*....|....*....
gi 445998103 248 KVVKDSEVMNRLPVIIFSS 266
Cdd:PLN03029  92 KKIKESSSLRNIPVVIMSS 110
LytT COG3279
DNA-binding response regulator, LytR/AlgR family [Transcription, Signal transduction ...
176-264 9.94e-05

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


Pssm-ID: 442510 [Multi-domain]  Cd Length: 235  Bit Score: 42.88  E-value: 9.94e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445998103 176 IYIAEDSAMLRQILEETLSS-AGYTKMNFFSNGAEALAQIEKLakeqgekmfeHIHLLITDIEMPKMDGhhlTKVVKDSE 254
Cdd:COG3279    4 ILIVDDEPLARERLERLLEKyPDLEVVGEASNGEEALELLEEH----------KPDLVFLDIQMPGLDG---FELARQLR 70
                         90
                 ....*....|
gi 445998103 255 VMNRLPVIIF 264
Cdd:COG3279   71 ELDPPPPIIF 80
REC_hyHK_blue-like cd18161
phosphoacceptor receiver (REC) domain of hybrid sensor histidine kinase/response regulators ...
176-288 1.02e-04

phosphoacceptor receiver (REC) domain of hybrid sensor histidine kinase/response regulators similar to Pseudomonas savastanoi blue-light-activated histidine kinase; Typically, two-component regulatory systems (TCSs) consist of a sensor (histidine kinase) that responds to specific input(s) by modifying the output of a cognate response regulator (RR). TCSs allow organisms to sense and respond to changes in environmental conditions. Hybrid sensor histidine kinase (HK)/response regulators contain all the elements of a classical TCS in a single polypeptide chain. Pseudomonas savastanoi blue-light-activated histidine kinase is a photosensitive HK and RR that is involved in increased bacterial virulence upon exposure to light. RRs share the common phosphoacceptor REC domain and different effector/output domains such as DNA, RNA, ligand-binding, protein-binding, or enzymatic domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381145 [Multi-domain]  Cd Length: 102  Bit Score: 40.79  E-value: 1.02e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445998103 176 IYIAEDSAMLRQILEETLSSAGYTKMNfFSNGAEALAQIEKLAKeqgekmfehIHLLITDIEMP-KMDGHHLTKVVKdsE 254
Cdd:cd18161    1 VLVVEDDPDVRRLTAEVLEDLGYTVLE-AASGDEALDLLESGPD---------IDLLVTDVIMPgGMNGSQLAEEAR--R 68
                         90       100       110
                 ....*....|....*....|....*....|....
gi 445998103 255 VMNRLPVIIFSSLITNELFHKGEAVGANAqVSKP 288
Cdd:cd18161   69 RRPDLKVLLTSGYAENAIEGGDLAPGVDV-LSKP 101
PRK09959 PRK09959
acid-sensing system histidine kinase EvgS;
163-288 1.51e-04

acid-sensing system histidine kinase EvgS;


Pssm-ID: 182169 [Multi-domain]  Cd Length: 1197  Bit Score: 43.18  E-value: 1.51e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445998103  163 AGLEQKTDRAEKV-IYIAEDSAMLRQILEETLSSAGYtKMNFFSNGAEALAQIEklakeqgekmFEHIHLLITDIEMPKM 241
Cdd:PRK09959  947 AKAEQPITLPEKLsILIADDHPTNRLLLKRQLNLLGY-DVDEATDGVQALHKVS----------MQHYDLLITDVNMPNM 1015
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 445998103  242 DGHHLTKVVKDSEvmNRLPVIIFSSLITNELFHKGEAVGANAQVSKP 288
Cdd:PRK09959 1016 DGFELTRKLREQN--SSLPIWGLTANAQANEREKGLSCGMNLCLFKP 1060
REC_HupR-like cd17569
phosphoacceptor receiver (REC) domain of hydrogen uptake protein regulator (HupR) and similar ...
189-252 1.54e-04

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: 40.46  E-value: 1.54e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 445998103 189 LEETLSSAGYtKMNFFSNGAEALAQIEKlakeqgekmfEHIHLLITDIEMPKMDGHHLTKVVKD 252
Cdd:cd17569   16 LKRLLRREGY-EVLTATSGEEALEILKQ----------EPVDVVISDQRMPGMDGAELLKRVRE 68
REC_DC-like cd17534
phosphoacceptor receiver (REC) domain of modulated diguanylate cyclase and similar domains; ...
176-293 6.22e-04

phosphoacceptor receiver (REC) domain of modulated diguanylate cyclase and similar domains; This groups includes a modulated diguanylate cyclase containing a PAS sensor domain from Desulfovibrio desulfuricans G20. Members of this group contain N-terminal REC domains and various output domains including the GGDEF, histidine kinase, and helix-turn-helix (HTH) DNA binding domains. Also included in this family is Mycobacterium tuberculosis PdtaR, a transcriptional antiterminator that contains a REC domain and an ANTAR RNA-binding output domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381089 [Multi-domain]  Cd Length: 117  Bit Score: 38.93  E-value: 6.22e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445998103 176 IYIAEDSAMLRQILEETLSSAGYTKMNFFSNGAEALAQIEKlakeqgekmfEHIHLLITDIEMP-KMDGHHLTKVVKDse 254
Cdd:cd17534    3 ILIVEDEAIIALDLKEILESLGYEVVGIADSGEEAIELAEE----------NKPDLILMDINLKgDMDGIEAAREIRE-- 70
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 445998103 255 vMNRLPVIIFSSLITNELFHKGEAVGANAQVSKP-DIQEL 293
Cdd:cd17534   71 -KFDIPVIFLTAYSDEETLERAKETNPYGYLVKPfNEREL 109
REC_OmpR_PrrA-like cd17627
phosphoacceptor receiver (REC) domain of PrrA-like OmpR family response regulators; The ...
176-266 8.02e-04

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: 38.52  E-value: 8.02e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445998103 176 IYIAEDSAMLRQILEETLSSAGYTkMNFFSNGAEALAQIEKLAKEqgekmfehihLLITDIEMPKMDGHHLTKVVKdsEV 255
Cdd:cd17627    1 ILVVDDDRAVRESLRRSLRFEGYE-VETAVDGAEALRVISGNRPD----------AVVLDVMMPRLDGLEVCRRLR--AA 67
                         90
                 ....*....|.
gi 445998103 256 MNRLPVIIFSS 266
Cdd:cd17627   68 GNDLPILVLTA 78
CheA COG0643
Chemotaxis protein histidine kinase CheA [Signal transduction mechanisms];
23-105 1.04e-03

Chemotaxis protein histidine kinase CheA [Signal transduction mechanisms];


Pssm-ID: 440408 [Multi-domain]  Cd Length: 563  Bit Score: 40.55  E-value: 1.04e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445998103  23 VGENLFSINVMKVREIINPFPvttvpESHHAVEG--VVQVRGEILPVINLATALNLKSTKPLDQTKF-IISELNQMKVIF 99
Cdd:COG0643  430 VGGETYAIPLSSVEEVLRLDP-----DDIETVEGreVIRLRGELLPLVRLGELLGLPGAEPEGERGPvVVVRSGGRRVAL 504

                 ....*.
gi 445998103 100 RVDEVH 105
Cdd:COG0643  505 VVDELL 510
REC_RssB-like cd17555
phosphoacceptor receiver (REC) domain of Pseudomonas aeruginosa RssB and similar domains; ...
176-265 1.08e-03

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: 37.95  E-value: 1.08e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445998103 176 IYIAEDSAMLRQILEETLSSAGYTKMNFfSNGAEALAQIEKlakeqgekmfEHIHLLITDIEMPKMDGHHLTKVVKDSEv 255
Cdd:cd17555    3 ILVIDDDEVVRESIAAYLEDSGFQVLQA-ADGRQGLELFRS----------EQPDLVLCDLRMPEMDGLEVLKQITKES- 70
                         90
                 ....*....|
gi 445998103 256 mNRLPVIIFS 265
Cdd:cd17555   71 -PDTPVIVVS 79
PRK10643 PRK10643
two-component system response regulator PmrA;
176-288 1.09e-03

two-component system response regulator PmrA;


Pssm-ID: 182612 [Multi-domain]  Cd Length: 222  Bit Score: 39.63  E-value: 1.09e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445998103 176 IYIAEDSAMLRQILEETLSSAGYTkMNFFSNGAEALAQIEKlakeqgekmfEHIHLLITDIEMPKMDGHHLTKVVKDSEV 255
Cdd:PRK10643   3 ILIVEDDTLLLQGLILALQTEGYA-CDCASTAREAEALLES----------GHYSLVVLDLGLPDEDGLHLLRRWRQKKY 71
                         90       100       110
                 ....*....|....*....|....*....|...
gi 445998103 256 MnrLPVIIFSSLITNELFHKGEAVGANAQVSKP 288
Cdd:PRK10643  72 T--LPVLILTARDTLEDRVAGLDVGADDYLVKP 102
REC_OmpR_KdpE-like cd17620
phosphoacceptor receiver (REC) domain of KdpE-like OmpR family response regulators; KdpE is a ...
176-288 1.20e-03

phosphoacceptor receiver (REC) domain of KdpE-like OmpR family response regulators; KdpE is a component of the KdpD/KdpE two-component system (TCS) and is activated when histidine kinase KdpD senses a drop in external K+ concentration or upshift in ionic osmolarity, resulting in the expression of a heterooligomeric transporter KdpFABC. In addition, the KdpD/KdpE TCS is also an adaptive regulator involved in the virulence and intracellular survival of pathogenic bacteria. KdpE is a member of the OmpR family of DNA-binding response regulators that contain 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: 381135 [Multi-domain]  Cd Length: 99  Bit Score: 37.53  E-value: 1.20e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445998103 176 IYIAEDSAMLRQILEETLSSAGYTkmnFFS--NGAEALAQIeklakeqgekMFEHIHLLITDIEMPKMDGHHLTKVVKD- 252
Cdd:cd17620    1 ILVIEDEPQIRRFLRTALEAHGYR---VFEaeTGQEGLLEA----------ATRKPDLIILDLGLPDMDGLEVIRRLREw 67
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 445998103 253 SEVmnrlPVIIFSSLITNElfHKGEAV--GANAQVSKP 288
Cdd:cd17620   68 SAV----PVIVLSARDEES--DKIAALdaGADDYLTKP 99
PRK11517 PRK11517
DNA-binding response regulator HprR;
176-288 1.46e-03

DNA-binding response regulator HprR;


Pssm-ID: 183172 [Multi-domain]  Cd Length: 223  Bit Score: 39.11  E-value: 1.46e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445998103 176 IYIAEDSAMLRQILEETLSSAGYTkMNFFSNGAEALaqieKLAKEqgekmfEHIHLLITDIEMPKMDGHHLTKVVKDSev 255
Cdd:PRK11517   3 ILLIEDNQRTQEWVTQGLSEAGYV-IDAVSDGRDGL----YLALK------DDYALIILDIMLPGMDGWQILQTLRTA-- 69
                         90       100       110
                 ....*....|....*....|....*....|...
gi 445998103 256 mNRLPVIIFSSLITNELFHKGEAVGANAQVSKP 288
Cdd:PRK11517  70 -KQTPVICLTARDSVDDRVRGLDSGANDYLVKP 101
PRK11361 PRK11361
acetoacetate metabolism transcriptional regulator AtoC;
171-299 1.61e-03

acetoacetate metabolism transcriptional regulator AtoC;


Pssm-ID: 183099 [Multi-domain]  Cd Length: 457  Bit Score: 39.83  E-value: 1.61e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445998103 171 RAEKVIYIAEDSAMLRQILEETLSSAGYTKMNFfSNGAEALaQIEKLAkeqgekmfeHIHLLITDIEMPKMDGHHLTKVV 250
Cdd:PRK11361   2 TAINRILIVDDEDNVRRMLSTAFALQGFETHCA-NNGRTAL-HLFADI---------HPDVVLMDIRMPEMDGIKALKEM 70
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 445998103 251 KDSEvmNRLPVIIFSSLITNELFHKGEAVGANAQVSKP-DIQELIGLVDK 299
Cdd:PRK11361  71 RSHE--TRTPVILMTAYAEVETAVEALRCGAFDYVIKPfDLDELNLIVQR 118
REC_OmpR_ChvI-like cd19936
phosphoacceptor receiver (REC) domain of ChvI-like OmpR family response regulators; ...
176-288 1.71e-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: 37.04  E-value: 1.71e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445998103 176 IYIAEDSAMLRQILEETLSSAGYtKMNFFSNGAEALAQIEKLAKEqgekmfehihLLITDIEMPKMDGHHLTKVVKDsev 255
Cdd:cd19936    1 IALVDDDRNILTSVSMALEAEGF-SVETYTDGASALDGLNARPPD----------LAILDIKMPRMDGMELLQRLRQ--- 66
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 445998103 256 MNRLPVIIFSSLIT--NELFhkGEAVGANAQVSKP 288
Cdd:cd19936   67 KSTLPVIFLTSKDDeiDEVF--GLRMGADDYITKP 99
REC_OmpR_EcPhoP-like cd19934
phosphoacceptor receiver (REC) domain of EcPhoP-like OmpR family response regulators; ...
176-301 2.15e-03

phosphoacceptor receiver (REC) domain of EcPhoP-like OmpR family response regulators; Escherichia coli PhoP (EcPhoP) is part of the PhoQ/PhoP two-component system (TCS) that regulates virulence genes and plays an essential role in the response of the bacteria to the environment of their mammalian hosts, sensing several stimuli such as extracellular magnesium limitation, low pH, the presence of cationic antimicrobial peptides, and osmotic upshift. This subfamily also includes Brucella suis FeuP, part of the FeuPQ TCS that is involved in the regulation of iron uptake, and Microchaete diplosiphon RcaC, which is required for chromatic adaptation. 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: 381161 [Multi-domain]  Cd Length: 117  Bit Score: 37.26  E-value: 2.15e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445998103 176 IYIAEDSAMLRQILEETLSSAGYTkMNFFSNGAEALAQIEKlakeqgekmfEHIHLLITDIEMPKMDGHHLTKVVKDSEV 255
Cdd:cd19934    1 LLLVEDDALLAAQLKEQLSDAGYV-VDVAEDGEEALFQGEE----------EPYDLVVLDLGLPGMDGLSVLRRWRSEGR 69
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 445998103 256 mnRLPVIIfssLITNELFHK---GEAVGANAQVSKP-DIQELIGLVDKLV 301
Cdd:cd19934   70 --ATPVLI---LTARDSWQDkveGLDAGADDYLTKPfHIEELLARLRALI 114
PRK10841 PRK10841
two-component system sensor histidine kinase RcsC;
176-262 2.53e-03

two-component system sensor histidine kinase RcsC;


Pssm-ID: 182772 [Multi-domain]  Cd Length: 924  Bit Score: 39.57  E-value: 2.53e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445998103 176 IYIAEDSAMLRQILEETLSSAGY-TKMNffSNGAEALAQIEKlakeqgekmfEHIHLLITDIEMPKMDGHHLTKVVKdsE 254
Cdd:PRK10841 804 ILVVDDHPINRRLLADQLGSLGYqCKTA--NDGVDALNVLSK----------NHIDIVLTDVNMPNMDGYRLTQRLR--Q 869

                 ....*...
gi 445998103 255 VMNRLPVI 262
Cdd:PRK10841 870 LGLTLPVI 877
REC_LytTR_AlgR-like cd17532
phosphoacceptor receiver (REC) domain of LytTR/AlgR family response regulators similar to AlgR; ...
178-264 2.90e-03

phosphoacceptor receiver (REC) domain of LytTR/AlgR family response regulators similar to AlgR; Members of the LytTR/AlgR family of response regulators contain a REC domain and a unique LytTR DNA-binding output domain that lacks the helix-turn-helix motif and consists mostly of beta-strands. Transcriptional regulators with the LytTR-type output domains are involved in biosynthesis of extracellular polysaccharides, fimbriation, expression of exoproteins, including toxins, and quorum sensing. Included in this AlgR-like group of LytTR/AlgR family response regulators are Streptococcus agalactiae sensory transduction protein LytR, Pseudomonas aeruginosa positive alginate biosynthesis regulatory protein AlgR, Bacillus subtilis sensory transduction protein LytT, and Escherichia coli transcriptional regulatory protein BtsR, which are members of two-component regulatory systems. LytR and LytT are components of regulatory systems that regulate genes involved in cell wall metabolism. AlgR positively regulates the algD gene, which codes for a GDP-mannose dehydrogenase, a key enzyme in the alginate biosynthesis pathway. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381087 [Multi-domain]  Cd Length: 118  Bit Score: 36.75  E-value: 2.90e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445998103 178 IAEDSAMLRQILEETLS-SAGYTKMNFFSNGAEALAQIEKLAkeqgekmfehIHLLITDIEMPKMDGHHLTKVVKDsevM 256
Cdd:cd17532    3 IVDDEPLAREELRYLLEeHPDIEIVGEAENGEEALEAIEELK----------PDVVFLDIQMPGLDGLELAKKLSK---L 69

                 ....*...
gi 445998103 257 NRLPVIIF 264
Cdd:cd17532   70 AKPPLIVF 77
PRK15479 PRK15479
transcriptional regulator TctD;
178-293 3.19e-03

transcriptional regulator TctD;


Pssm-ID: 185376 [Multi-domain]  Cd Length: 221  Bit Score: 38.16  E-value: 3.19e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445998103 178 IAEDSAMLRQILEETLSSAGYTkMNFFSNG--AEALAQIEKLAkeqgekmfehihLLITDIEMPKMDGhhLTKVVKDSEV 255
Cdd:PRK15479   5 LAEDNRELAHWLEKALVQNGFA-VDCVFDGlaADHLLQSEMYA------------LAVLDINMPGMDG--LEVLQRLRKR 69
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 445998103 256 MNRLPVIIFSSLITNELFHKGEAVGANAQVSKP-DIQEL 293
Cdd:PRK15479  70 GQTLPVLLLTARSAVADRVKGLNVGADDYLPKPfELEEL 108
fixJ PRK09390
response regulator FixJ; Provisional
173-263 3.28e-03

response regulator FixJ; Provisional


Pssm-ID: 181815 [Multi-domain]  Cd Length: 202  Bit Score: 38.06  E-value: 3.28e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445998103 173 EKVIYIAEDSAMLRQILEETLSSAGYTKMNFFSngaeALAQIEKLA-KEQGekmfehihLLITDIEMPKMDGHHLTKVVK 251
Cdd:PRK09390   3 KGVVHVVDDDEAMRDSLAFLLDSAGFEVRLFES----AQAFLDALPgLRFG--------CVVTDVRMPGIDGIELLRRLK 70
                         90
                 ....*....|..
gi 445998103 252 DSEVmnRLPVII 263
Cdd:PRK09390  71 ARGS--PLPVIV 80
psREC_PRR cd17582
pseudo receiver domain of pseudo-response regulators; In Arabidopsis, five pseudo-response ...
186-266 3.41e-03

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: 36.61  E-value: 3.41e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445998103 186 RQILEETLSSAGYtKMNFFSNGAEAlaqIEKLAKEQGekmfeHIHLLITDIEMPKMDGHHLTKVVKDSEVMNRLPVIIFS 265
Cdd:cd17582   11 RQIVTALLRKCSY-EVTAASDGLQA---WDVLEDEQN-----EIDLILTEVDLPVSSGFKLLSYIMRHKICKNIPVIMMS 81

                 .
gi 445998103 266 S 266
Cdd:cd17582   82 S 82
 
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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