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Conserved domains on  [gi|880808944|ref|WP_048661104|]
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chemotaxis protein [Vibrio crassostreae]

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
REC super family cl19078
phosphoacceptor receiver (REC) domain of response regulators (RRs) and pseudo response ...
 175-281 3.42e-34

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: 120.56  E-value: 3.42e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808944 175 ILLVDDSLIARKQLSDALDSINIPYSICNNGLDAIDLMRRQAS----VDNAIDLLVSDIEMPGLDGYELAFEVQNDSALS 250
Cdd:cd19924    1 ILVVDDSPTARKQLRDLLKNLGFEIAEAVDGEEALNKLENLAKegndLSKELDLIITDIEMPKMDGYELTFELRDDPRLA 80

                         90       100       110
                 ....*....|....*....|....*....|.
gi 880808944 251 HAYCILHTSLSSEICVDRANQVGAHEALEKF 281
Cdd:cd19924   81 NIPVILNSSLSGEFSRARGKKVGADAYLAKF 111
CheW COG0835
Chemotaxis signal transduction protein CheW [Signal transduction mechanisms];
5-148 2.70e-31

Chemotaxis signal transduction protein CheW [Signal transduction mechanisms];


:

Pssm-ID: 440597  Cd Length: 151  Bit Score: 114.20  E-value: 2.70e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808944   5 ISKASQSQGMLMFKLSlTQSFAIGTLKVREIVPFQPMTQIPYSHHHVIGTVTIRDLTVPVIDMSAAIGFRPITPAEyqDC 84
Cdd:COG0835    1 LEAGANELQYLTFRLG-GERYAIPIEKVREILPLPPITPVPGAPPWVLGVINLRGRVVPVIDLRALLGLPPTEDTE--RT 77

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 880808944  85 VLIVTDCLRTVVAFLVRSIDKIIECDWKSIESPPTSV--GRNVFVTGITRFEDRIVQMLDVELLLS 148
Cdd:COG0835   78 RIIVLEVGGRVVGLLVDSVSGVVRIDPDDIEPPPELLsgGLAPFITGVAKLDDRLILLLDLEKLLA 143
 
Name Accession Description Interval E-value
REC_CheV-like cd19924
phosphoacceptor receiver (REC) domain of chemotaxis protein CheV and similar proteins; This ...
 175-281 3.42e-34

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: 120.56  E-value: 3.42e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808944 175 ILLVDDSLIARKQLSDALDSINIPYSICNNGLDAIDLMRRQAS----VDNAIDLLVSDIEMPGLDGYELAFEVQNDSALS 250
Cdd:cd19924    1 ILVVDDSPTARKQLRDLLKNLGFEIAEAVDGEEALNKLENLAKegndLSKELDLIITDIEMPKMDGYELTFELRDDPRLA 80

                         90       100       110
                 ....*....|....*....|....*....|.
gi 880808944 251 HAYCILHTSLSSEICVDRANQVGAHEALEKF 281
Cdd:cd19924   81 NIPVILNSSLSGEFSRARGKKVGADAYLAKF 111
CheW COG0835
Chemotaxis signal transduction protein CheW [Signal transduction mechanisms];
5-148 2.70e-31

Chemotaxis signal transduction protein CheW [Signal transduction mechanisms];


Pssm-ID: 440597  Cd Length: 151  Bit Score: 114.20  E-value: 2.70e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808944   5 ISKASQSQGMLMFKLSlTQSFAIGTLKVREIVPFQPMTQIPYSHHHVIGTVTIRDLTVPVIDMSAAIGFRPITPAEyqDC 84
Cdd:COG0835    1 LEAGANELQYLTFRLG-GERYAIPIEKVREILPLPPITPVPGAPPWVLGVINLRGRVVPVIDLRALLGLPPTEDTE--RT 77

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 880808944  85 VLIVTDCLRTVVAFLVRSIDKIIECDWKSIESPPTSV--GRNVFVTGITRFEDRIVQMLDVELLLS 148
Cdd:COG0835   78 RIIVLEVGGRVVGLLVDSVSGVVRIDPDDIEPPPELLsgGLAPFITGVAKLDDRLILLLDLEKLLA 143
CheW pfam01584
CheW-like domain; CheW proteins are part of the chemotaxis signaling mechanism in bacteria. ...
 14-146 2.39e-29

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: 108.44  E-value: 2.39e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808944   14 MLMFKLSlTQSFAIGTLKVREIVPFQPMTQIPYSHHHVIGTVTIRDLTVPVIDMSAAIGFRPITPAEYQdcVLIVTDCLR 93
Cdd:pfam01584   1 GLLFRLG-GETFAIPISKVREILRPPPITPIPGAPGYVLGVINLRGEVLPVIDLRRLLGLPPTEPRERT--RVVVVEVGG 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 880808944   94 TVVAFLVRSIDKIIECDWKSIESPPTSVGRNVFVTGITRFED-RIVQMLDVELL 146
Cdd:pfam01584  78 QVVGLLVDEVIGVLEIVIKQIEPPLGLGRVAGYISGATILGDgRVVLILDVEAL 131
CheY COG0784
CheY-like REC (receiver) domain, includes chemotaxis protein CheY and sporulation regulator ...
 169-292 6.02e-22

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: 89.14  E-value: 6.02e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808944 169 RLKALNILLVDDSLIARKQLSDALDSINIPYSICNNGLDAIDLMRRQAsvdnaIDLLVSDIEMPGLDGYELAFEVQNDSA 248
Cdd:COG0784    2 PLGGKRILVVDDNPDNRELLRRLLERLGYEVTTAEDGAEALELLRAGP-----PDLILLDINMPGMDGLELLRRIRALPR 76

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 880808944 249 LSHAYCILHTSLSSEICVDRANQVGAHEALEK-FNAGELIEAMLR 292
Cdd:COG0784   77 LPDIPIIALTAYADEEDRERALEAGADDYLTKpVDPEELLEALRR 121
CheW smart00260
Two component signalling adaptor domain;
14-147 3.95e-21

Two component signalling adaptor domain;


Pssm-ID: 214588 [Multi-domain]  Cd Length: 138  Bit Score: 86.91  E-value: 3.95e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808944    14 MLMFKLSLTQSFAIGTLKVREIVPFQPMTQIPYSHHHVIGTVTIRDLTVPVIDMSAAIGFRPITPAEYQdcVLIVTDCLR 93
Cdd:smart00260   5 PLTFAIGKDETYAIPIAAVREILRPPPITPIPGAPGYVLGVINLRGEVLPVVDLRRLLGLPPEPPTDET--RVIVVETGD 82

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 880808944    94 TVVAFLVRSIDKIIECDWKSIESPPTSVGRNV-FVTGITRFED-RIVQMLDVELLL 147
Cdd:smart00260  83 RKVGLVVDSVLGVREVVVKSIEPPPPVSLSNApGISGATILGDgRVVLILDVDKLL 138
CheW cd00732
CheW, a small regulator protein, unique to the chemotaxis signalling in prokaryotes and archea. ...
 23-150 8.25e-20

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: 83.77  E-value: 8.25e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808944  23 QSFAIGTLKVREIVPFQPMTQIPYSHHHVIGTVTIRDLTVPVIDMSAAIGfrpITPAEYQD-CVLIVTDCLRTVVAFLVR 101
Cdd:cd00732   12 EEYGIPIMQVREILKPTPITPIPNAPPYVLGVINLRGRIVPVIDLRKRLG---LPPAEDTKnTRIIVVEVGDQVVGLLVD 88

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 880808944 102 SIDKIIECDWKSIESPPTSVGR--NVFVTGITRFEDRIVQMLDVELLLSKI 150
Cdd:cd00732   89 SVSEVLRLSTDDIQPPPPVLSDinAKFIRGVVKLEGRLLILLDLDKILDER 139
PRK10841 PRK10841
two-component system sensor histidine kinase RcsC;
145-240 3.95e-11

two-component system sensor histidine kinase RcsC;


Pssm-ID: 182772 [Multi-domain]  Cd Length: 924  Bit Score: 63.84  E-value: 3.95e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808944 145 LLLSKIY----PDYENAHIPMLTDVERERLKALNILLVDDSLIARKQLSDALDSINIPYSICNNGLDAIDLMRRqasvdN 220
Cdd:PRK10841 770 ALLARIYrielESDDSANALPSTDKAVSDNDDMMILVVDDHPINRRLLADQLGSLGYQCKTANDGVDALNVLSK-----N 844

                         90       100
                 ....*....|....*....|
gi 880808944 221 AIDLLVSDIEMPGLDGYELA 240
Cdd:PRK10841 845 HIDIVLTDVNMPNMDGYRLT 864
Response_reg pfam00072
Response regulator receiver domain; This domain receives the signal from the sensor partner in ...
 175-289 8.26e-11

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: 58.32  E-value: 8.26e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808944  175 ILLVDDSLIARKQLSDALDSINIPYSICNNGLDAIDLMRRQAsvdnaIDLLVSDIEMPGLDGYELAFEVQNDSalSHAYC 254
Cdd:pfam00072   1 VLIVDDDPLIRELLRQLLEKEGYVVAEADDGKEALELLKEER-----PDLILLDINMPGMDGLELLKRIRRRD--PTTPV 73

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 880808944  255 ILHTSLSSEICVDRANQVGAHEALEK-FNAGELIEA 289
Cdd:pfam00072  74 IILTAHGDEDDAVEALEAGADDFLSKpFDPDELLAA 109
REC smart00448
cheY-homologous receiver domain; CheY regulates the clockwise rotation of E. coli flagellar ...
 173-232 7.70e-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: 42.56  E-value: 7.70e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808944   173 LNILLVDDSLIARKQLSDALDSINIPYSICNNGLDAIDLMRRqasvdNAIDLLVSDIEMP 232
Cdd:smart00448   1 MRILVVDDDPLLRELLKALLEKEGYEVDEATDGEEALELLKE-----EKPDLILLDIMMP 55
PRK10612 PRK10612
chemotaxis protein CheW;
5-148 2.09e-05

chemotaxis protein CheW;


Pssm-ID: 182587  Cd Length: 167  Bit Score: 44.03  E-value: 2.09e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808944   5 ISKASQSQGMLMFKLSlTQSFAIGTLKVREIVPFQPMTQIPYSHHHVIGTVTIRDLTVPVIDMSaaIGFRPITPAEYQDC 84
Cdd:PRK10612  10 LAGEPSGQEFLVFTLG-DEEYGIDILKVQEIRGYDQVTRIANTPAFIKGVTNLRGVIVPIVDLR--IKFSQVDVDYNDNT 86

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 880808944  85 VLIVTDCLRTVVAFLVRSIDKIIECDWKSIE-SPPTSVGRNV-FVTGITRFEDRIVQMLDVELLLS 148
Cdd:PRK10612  87 VVIVLNLGQRVVGIVVDGVSDVLSLTAEQIRpAPEFAVTLSTeYLTGLGALGERMLILVNIEKLLN 152
 
Name Accession Description Interval E-value
REC_CheV-like cd19924
phosphoacceptor receiver (REC) domain of chemotaxis protein CheV and similar proteins; This ...
 175-281 3.42e-34

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: 120.56  E-value: 3.42e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808944 175 ILLVDDSLIARKQLSDALDSINIPYSICNNGLDAIDLMRRQAS----VDNAIDLLVSDIEMPGLDGYELAFEVQNDSALS 250
Cdd:cd19924    1 ILVVDDSPTARKQLRDLLKNLGFEIAEAVDGEEALNKLENLAKegndLSKELDLIITDIEMPKMDGYELTFELRDDPRLA 80

                         90       100       110
                 ....*....|....*....|....*....|.
gi 880808944 251 HAYCILHTSLSSEICVDRANQVGAHEALEKF 281
Cdd:cd19924   81 NIPVILNSSLSGEFSRARGKKVGADAYLAKF 111
CheW COG0835
Chemotaxis signal transduction protein CheW [Signal transduction mechanisms];
5-148 2.70e-31

Chemotaxis signal transduction protein CheW [Signal transduction mechanisms];


Pssm-ID: 440597  Cd Length: 151  Bit Score: 114.20  E-value: 2.70e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808944   5 ISKASQSQGMLMFKLSlTQSFAIGTLKVREIVPFQPMTQIPYSHHHVIGTVTIRDLTVPVIDMSAAIGFRPITPAEyqDC 84
Cdd:COG0835    1 LEAGANELQYLTFRLG-GERYAIPIEKVREILPLPPITPVPGAPPWVLGVINLRGRVVPVIDLRALLGLPPTEDTE--RT 77

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 880808944  85 VLIVTDCLRTVVAFLVRSIDKIIECDWKSIESPPTSV--GRNVFVTGITRFEDRIVQMLDVELLLS 148
Cdd:COG0835   78 RIIVLEVGGRVVGLLVDSVSGVVRIDPDDIEPPPELLsgGLAPFITGVAKLDDRLILLLDLEKLLA 143
CheW pfam01584
CheW-like domain; CheW proteins are part of the chemotaxis signaling mechanism in bacteria. ...
 14-146 2.39e-29

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: 108.44  E-value: 2.39e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808944   14 MLMFKLSlTQSFAIGTLKVREIVPFQPMTQIPYSHHHVIGTVTIRDLTVPVIDMSAAIGFRPITPAEYQdcVLIVTDCLR 93
Cdd:pfam01584   1 GLLFRLG-GETFAIPISKVREILRPPPITPIPGAPGYVLGVINLRGEVLPVIDLRRLLGLPPTEPRERT--RVVVVEVGG 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 880808944   94 TVVAFLVRSIDKIIECDWKSIESPPTSVGRNVFVTGITRFED-RIVQMLDVELL 146
Cdd:pfam01584  78 QVVGLLVDEVIGVLEIVIKQIEPPLGLGRVAGYISGATILGDgRVVLILDVEAL 131
CheY COG0784
CheY-like REC (receiver) domain, includes chemotaxis protein CheY and sporulation regulator ...
 169-292 6.02e-22

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: 89.14  E-value: 6.02e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808944 169 RLKALNILLVDDSLIARKQLSDALDSINIPYSICNNGLDAIDLMRRQAsvdnaIDLLVSDIEMPGLDGYELAFEVQNDSA 248
Cdd:COG0784    2 PLGGKRILVVDDNPDNRELLRRLLERLGYEVTTAEDGAEALELLRAGP-----PDLILLDINMPGMDGLELLRRIRALPR 76

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 880808944 249 LSHAYCILHTSLSSEICVDRANQVGAHEALEK-FNAGELIEAMLR 292
Cdd:COG0784   77 LPDIPIIALTAYADEEDRERALEAGADDYLTKpVDPEELLEALRR 121
CheW smart00260
Two component signalling adaptor domain;
14-147 3.95e-21

Two component signalling adaptor domain;


Pssm-ID: 214588 [Multi-domain]  Cd Length: 138  Bit Score: 86.91  E-value: 3.95e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808944    14 MLMFKLSLTQSFAIGTLKVREIVPFQPMTQIPYSHHHVIGTVTIRDLTVPVIDMSAAIGFRPITPAEYQdcVLIVTDCLR 93
Cdd:smart00260   5 PLTFAIGKDETYAIPIAAVREILRPPPITPIPGAPGYVLGVINLRGEVLPVVDLRRLLGLPPEPPTDET--RVIVVETGD 82

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 880808944    94 TVVAFLVRSIDKIIECDWKSIESPPTSVGRNV-FVTGITRFED-RIVQMLDVELLL 147
Cdd:smart00260  83 RKVGLVVDSVLGVREVVVKSIEPPPPVSLSNApGISGATILGDgRVVLILDVDKLL 138
PleD COG3706
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate ...
 172-287 6.87e-20

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: 84.96  E-value: 6.87e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808944 172 ALNILLVDDSLIARKQLSDALDSINIPYSICNNGLDAIDLMRRQAsvdnaIDLLVSDIEMPGLDGYELAFEVQNDSALSH 251
Cdd:COG3706    1 PARILVVDDDPTNRKLLRRLLEAAGYEVVEAADGEEALELLQEHR-----PDLILLDLEMPDMDGLELCRRLRADPRTAD 75

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 880808944 252 AYCILHTSLSSEICVDRANQVGAHEALEK-FNAGELI 287
Cdd:COG3706   76 IPIIFLTALDDEEDRARALEAGADDYLTKpFDPEELL 112
CheW cd00732
CheW, a small regulator protein, unique to the chemotaxis signalling in prokaryotes and archea. ...
 23-150 8.25e-20

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: 83.77  E-value: 8.25e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808944  23 QSFAIGTLKVREIVPFQPMTQIPYSHHHVIGTVTIRDLTVPVIDMSAAIGfrpITPAEYQD-CVLIVTDCLRTVVAFLVR 101
Cdd:cd00732   12 EEYGIPIMQVREILKPTPITPIPNAPPYVLGVINLRGRIVPVIDLRKRLG---LPPAEDTKnTRIIVVEVGDQVVGLLVD 88

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 880808944 102 SIDKIIECDWKSIESPPTSVGR--NVFVTGITRFEDRIVQMLDVELLLSKI 150
Cdd:cd00732   89 SVSEVLRLSTDDIQPPPPVLSDinAKFIRGVVKLEGRLLILLDLDKILDER 139
CheW_like cd00588
CheW-like domain. CheW proteins are part of the chemotaxis signalling mechanism in bacteria. ...
 11-146 2.09e-19

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: 82.32  E-value: 2.09e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808944  11 SQGMLMFKLSlTQSFAIGTLKVREIVPFQPMTQIPYSHHHVIGTVTIRDLTVPVIDMSAAIGFRPITPAEYQDcVLIVTD 90
Cdd:cd00588    1 ILQVLLFRVG-DELYAIPIAVVEEILPLPPITRVPNAPDYVLGVINLRGEILPVIDLRRLFGLEAAEPDTDET-RIVVVE 78

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 880808944  91 CLRTVVAFLVRSIDKIIECDWKSIESPPTSVGRNV-FVTGITRFED-RIVQMLDVELL 146
Cdd:cd00588   79 VGDRKVGLVVDSVLGVLEVVIKDIEPPPDVGSSNApGISGATILGDgRVVLILDVDKL 136
RpfG COG3437
Response regulator c-di-GMP phosphodiesterase, RpfG family, contains REC and HD-GYP domains ...
 171-290 4.08e-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: 67.50  E-value: 4.08e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808944 171 KALNILLVDDSLIARKQLSDALDSINIPYSICNNGLDAIDLMRRQAsvdnaIDLLVSDIEMPGLDGYELAFEVQNDSALS 250
Cdd:COG3437    5 QAPTVLIVDDDPENLELLRQLLRTLGYDVVTAESGEEALELLLEAP-----PDLILLDVRMPGMDGFELLRLLRADPSTR 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 880808944 251 HAYCILHTSLSSEICVDRANQVGAHEALEK-FNAGELIEAM 290
Cdd:COG3437   80 DIPVIFLTALADPEDRERALEAGADDYLTKpFDPEELLARV 120
REC cd00156
phosphoacceptor receiver (REC) domain of response regulators (RRs) and pseudo response ...
 176-280 9.28e-13

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: 63.40  E-value: 9.28e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808944 176 LLVDDSLIARKQLSDALDSINIPYSICNNGLDAIDLMRrqasvDNAIDLLVSDIEMPGLDGYELAFEVQNDSalSHAYCI 255
Cdd:cd00156    1 LIVDDDPAIRELLKSLLEREGYEVDTAADGEEALELLR-----EERPDLVLLDLMMPGMDGLELLRKLRELP--PDIPVI 73

                         90       100
                 ....*....|....*....|....*
gi 880808944 256 LHTSLSSEICVDRANQVGAHEALEK 280
Cdd:cd00156   74 VLTAKADEEDAVRALELGADDYLVK 98
YesN COG4753
Two-component response regulator, YesN/AraC family, consists of REC and AraC-type DNA-binding ...
 174-280 3.86e-12

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: 61.71  E-value: 3.86e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808944 174 NILLVDDSLIARKQLSDALDSiNIPYSIC---NNGLDAIDLMRRQAsvdnaIDLLVSDIEMPGLDGYELAFEVQNDSalS 250
Cdd:COG4753    1 KVLIVDDEPLIREGLKRILEW-EAGFEVVgeaENGEEALELLEEHK-----PDLVITDINMPGMDGLELLEAIRELD--P 72

                         90       100       110
                 ....*....|....*....|....*....|
gi 880808944 251 HAYCILHTSLSSEICVDRANQVGAHEALEK 280
Cdd:COG4753   73 DTKIIILSGYSDFEYAQEAIKLGADDYLLK 102
OmpR COG0745
DNA-binding response regulator, OmpR family, contains REC and winged-helix (wHTH) domain ...
 175-292 7.47e-12

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: 63.44  E-value: 7.47e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808944 175 ILLVDDSLIARKQLSDALDSINIPYSICNNGLDAIDLMRRqasvdNAIDLLVSDIEMPGLDGYELAFEVQNDSalSHAYC 254
Cdd:COG0745    4 ILVVEDDPDIRELLADALEREGYEVDTAADGEEALELLEE-----ERPDLILLDLMLPGMDGLEVCRRLRARP--SDIPI 76

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 880808944 255 ILHTSLSSEICVDRANQVGAHEALEK-FNAGEL---IEAMLR 292
Cdd:COG0745   77 IMLTARDDEEDRVRGLEAGADDYLTKpFDPEELlarIRALLR 118
AtoC COG2204
DNA-binding transcriptional response regulator, NtrC family, contains REC, AAA-type ATPase, ...
 174-292 8.92e-12

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: 64.98  E-value: 8.92e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808944 174 NILLVDDSLIARKQLSDALDSINIPYSICNNGLDAIDLMRRQAsvdnaIDLLVSDIEMPGLDGYELAFEVQNDSalSHAY 253
Cdd:COG2204    4 RILVVDDDPDIRRLLKELLERAGYEVETAASGEEALALLREEP-----PDLVLLDLRMPGMDGLELLRELRALD--PDLP 76

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 880808944 254 CILHTSLSSEICVDRANQVGAHEALEK-FNAGELIEAMLR 292
Cdd:COG2204   77 VILLTGYGDVETAVEAIKAGAFDYLTKpFDLEELLAAVER 116
PRK10841 PRK10841
two-component system sensor histidine kinase RcsC;
145-240 3.95e-11

two-component system sensor histidine kinase RcsC;


Pssm-ID: 182772 [Multi-domain]  Cd Length: 924  Bit Score: 63.84  E-value: 3.95e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808944 145 LLLSKIY----PDYENAHIPMLTDVERERLKALNILLVDDSLIARKQLSDALDSINIPYSICNNGLDAIDLMRRqasvdN 220
Cdd:PRK10841 770 ALLARIYrielESDDSANALPSTDKAVSDNDDMMILVVDDHPINRRLLADQLGSLGYQCKTANDGVDALNVLSK-----N 844

                         90       100
                 ....*....|....*....|
gi 880808944 221 AIDLLVSDIEMPGLDGYELA 240
Cdd:PRK10841 845 HIDIVLTDVNMPNMDGYRLT 864
Response_reg pfam00072
Response regulator receiver domain; This domain receives the signal from the sensor partner in ...
 175-289 8.26e-11

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: 58.32  E-value: 8.26e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808944  175 ILLVDDSLIARKQLSDALDSINIPYSICNNGLDAIDLMRRQAsvdnaIDLLVSDIEMPGLDGYELAFEVQNDSalSHAYC 254
Cdd:pfam00072   1 VLIVDDDPLIRELLRQLLEKEGYVVAEADDGKEALELLKEER-----PDLILLDINMPGMDGLELLKRIRRRD--PTTPV 73

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 880808944  255 ILHTSLSSEICVDRANQVGAHEALEK-FNAGELIEA 289
Cdd:pfam00072  74 IILTAHGDEDDAVEALEAGADDFLSKpFDPDELLAA 109
REC_Ycf29 cd19927
phosphoacceptor receiver (REC) domain of probable transcriptional regulator Ycf29; Ycf29 is a ...
 175-258 2.55e-10

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: 56.62  E-value: 2.55e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808944 175 ILLVDDSLIARKQLSDALDSINIPYSICNNGLDAIDLMRRQAsvdnaIDLLVSDIEMPGLDGYELAFEVQNDSALSHAYC 254
Cdd:cd19927    1 ILLVDDDPGIRLAVKDYLEDQGFTVIAASNGLEALDLLNQYI-----PDLIISDIIMPGVDGYSLLGKLRKNADFDTIPV 75


                 ....
gi 880808944 255 ILHT 258
Cdd:cd19927   76 IFLT 79
REC_CheC-like cd17593
phosphoacceptor receiver (REC) domain of uncharacterized response regulators containing a CheC ...
 173-238 4.32e-10

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: 56.39  E-value: 4.32e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 880808944 173 LNILLVDDSLIARKQLSDAL-DSINIPYSICNNGLDAIDLMRRQasvdnAIDLLVSDIEMPGLDGYE 238
Cdd:cd17593    1 MKVLICDDSSMARKQLARALpADWDVEITFAENGEEALEILREG-----RIDVLFLDLTMPVMDGYE 62
REC_YesN-like cd17536
phosphoacceptor receiver (REC) domain of YesN and related helix-turn-helix containing response ...
 175-244 8.88e-10

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: 55.42  E-value: 8.88e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 880808944 175 ILLVDDSLIARKQLSDALDSINIPYSIC---NNGLDAIDLMRRQAsvdnaIDLLVSDIEMPGLDGYELAFEVQ 244
Cdd:cd17536    1 VLIVDDEPLIREGLKKLIDWEELGFEVVgeaENGEEALELIEEHK-----PDIVITDIRMPGMDGLELIEKIR 68
REC_hyHK_CKI1_RcsC-like cd17546
phosphoacceptor receiver (REC) domain of hybrid sensor histidine kinases/response regulators ...
 175-240 1.74e-09

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: 54.40  E-value: 1.74e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 880808944 175 ILLVDDSLIARKQLSDALDSINIPYSICNNGLDAIDLMRRQasvdnAIDLLVSDIEMPGLDGYELA 240
Cdd:cd17546    1 VLVVDDNPVNRKVLKKLLEKLGYEVDVAENGQEALELLKEE-----PFDLVLMDLQMPVMDGLEAT 61
LytT COG3279
DNA-binding response regulator, LytR/AlgR family [Transcription, Signal transduction ...
 173-240 2.22e-09

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


Pssm-ID: 442510 [Multi-domain]  Cd Length: 235  Bit Score: 56.75  E-value: 2.22e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 880808944 173 LNILLVDDSLIARKQLSDAL---DSINIPYSiCNNGLDAIDLMRRqasvdNAIDLLVSDIEMPGLDGYELA 240
Cdd:COG3279    2 MKILIVDDEPLARERLERLLekyPDLEVVGE-ASNGEEALELLEE-----HKPDLVFLDIQMPGLDGFELA 66
REC_hyHK cd17598
phosphoacceptor receiver (REC) domain of uncharacterized hybrid sensor histidine kinase ...
 175-274 4.97e-09

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: 53.48  E-value: 4.97e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808944 175 ILLVDDSLIARKQLSDALDSINIPYSICNNGLDAIDLMRRqasvdNAIDLLVSDIEMPGLDGYELAFEVQNDSALSHAYC 254
Cdd:cd17598    1 ILIVEDSPTQAEQLKHILEEQGYKVQVARNGREALAMLAE-----HRPTLVISDIVMPEMDGYELCRKIKSDPDLKDIPV 75

                         90       100
                 ....*....|....*....|
gi 880808944 255 ILHTSLSSEICVDRANQVGA 274
Cdd:cd17598   76 ILLTTLSDPRDVIRGLECGA 95
REC_2_DhkD-like cd17580
second phosphoacceptor receiver (REC) domain of Dictyostelium discoideum hybrid signal ...
 175-289 1.32e-08

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: 52.08  E-value: 1.32e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808944 175 ILLVDDSLIARKQLSDALDSINIPYSICNNGLDAIDLMRRQASvdnaiDLLVSDIEMPGLDGYELAFEVQNDSALSHAYC 254
Cdd:cd17580    1 ILVVDDNEDAAEMLALLLELEGAEVTTAHSGEEALEAAQRFRP-----DVILSDIGMPGMDGYELARRLRELPWLANTPA 75

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 880808944 255 ILHTSLSSEICVDRANQVGAHEALEK-FNAGELIEA 289
Cdd:cd17580   76 IALTGYGQPEDRERALEAGFDAHLVKpVDPDELIEL 111
REC_Rcp-like cd17557
phosphoacceptor receiver (REC) domain of cyanobacterial phytochrome response regulator Rcp and ...
 174-251 2.09e-08

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: 52.03  E-value: 2.09e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808944 174 NILLVDDSLIARKQLSDALDSINIPY--SICNNGLDAIDLMRRQASVDNAI--DLLVSDIEMPGLDGYELAFEVQNDSAL 249
Cdd:cd17557    1 TILLVEDNPGDAELIQEAFKEAGVPNelHVVRDGEEALDFLRGEGEYADAPrpDLILLDLNMPRMDGFEVLREIKADPDL 80


                 ..
gi 880808944 250 SH 251
Cdd:cd17557   81 RR 82
REC_CheB-like cd17541
phosphoacceptor receiver (REC) domain of chemotaxis response regulator protein-glutamate ...
 174-238 2.95e-08

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: 51.24  E-value: 2.95e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 880808944 174 NILLVDDSLIARKQLSDALDSinIPY----SICNNGLDAIDLMRRQasvdnAIDLLVSDIEMPGLDGYE 238
Cdd:cd17541    2 RVLIVDDSAVMRKLLSRILES--DPDievvGTARDGEEALEKIKEL-----KPDVITLDIEMPVMDGLE 63
REC_CheY_CheY3 cd19923
phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY3 and similar CheY ...
 173-290 5.94e-08

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: 50.41  E-value: 5.94e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808944 173 LNILLVDDSLIARKQLSDALDSINIPYSI-CNNGLDAIDLMRRqasvdNAIDLLVSDIEMPGLDGYELAFEVQNDSALSH 251
Cdd:cd19923    1 MKVLVVDDFSTMRRIIKNLLKELGFNNVEeAEDGVDALEKLKA-----GGFDFVITDWNMPNMDGLELLKTIRADGALSH 75

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 880808944 252 AYCILHTSLSSEICVDRANQVGAHEALEK-FNAGELIEAM 290
Cdd:cd19923   76 LPVLMVTAEAKKENVIAAAQAGVNNYIVKpFTAATLKEKL 115
REC_D1_PleD-like cd17538
first (D1) phosphoacceptor receiver (REC) domain of response regulator PleD and similar ...
 175-280 8.42e-08

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: 49.42  E-value: 8.42e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808944 175 ILLVDDSLIARKQLSDALDSINIPYSICNNGLDAIDLMRRQAsvdnaIDLLVSDIEMPGLDGYELAFEVQNDSALSHAYC 254
Cdd:cd17538    2 ILVVDDEPANRELLEALLSAEGYEVLTADSGQEALALAEEEL-----PDLILLDVMMPGMDGFEVCRRLKEDPETRHIPV 76

                         90       100
                 ....*....|....*....|....*.
gi 880808944 255 ILHTSLSSEICVDRANQVGAHEALEK 280
Cdd:cd17538   77 IMITALDDREDRIRGLEAGADDFLSK 102
REC_2_GGDEF cd17544
second phosphoacceptor receiver (REC) domain of uncharacterized GGDEF domain proteins; This ...
 175-239 1.44e-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: 49.44  E-value: 1.44e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 880808944 175 ILLVDDSLIARKQLSDALDSINIPYSICNNGLDAIDLMRRqasvDNAIDLLVSDIEMPGLDGYEL 239
Cdd:cd17544    3 VLVVDDSATSRNHLRALLRRHNFQVLEAANGQEALEVLEQ----HPDIKLVITDYNMPEMDGFEL 63
REC_CheY cd17542
phosphoacceptor receiver (REC) domain of chemotaxis protein CheY; The chemotaxis response ...
 174-290 3.61e-07

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


Pssm-ID: 381097 [Multi-domain]  Cd Length: 117  Bit Score: 48.04  E-value: 3.61e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808944 174 NILLVDDSLIARKQLSDALDSINipYSI---CNNGLDAIDLMRrqasvDNAIDLLVSDIEMPGLDGYELAFEVQNDSalS 250
Cdd:cd17542    2 KVLIVDDAAFMRMMLKDILTKAG--YEVvgeAANGEEAVEKYK-----ELKPDLVTMDITMPEMDGIEALKEIKKID--P 72

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 880808944 251 HAYCILHTSLSSEICVDRANQVGAHEALEK-FNAGELIEAM 290
Cdd:cd17542   73 NAKVIMCSAMGQEEMVKEAIKAGAKDFIVKpFQPERVLEAV 113
AmiR COG3707
Two-component response regulator, AmiR/NasT family, consists of REC and RNA-binding ...
 171-290 3.77e-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: 3.77e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808944 171 KALNILLVDDSLIARKQLSDALDSINI-PYSICNNGLDAIDLMRRQAsvdnaIDLLVSDIEMPGLDGYELAFEVQNDSAL 249
Cdd:COG3707    2 RGLRVLVVDDEPLRRADLREGLREAGYeVVAEAADGEDAVELVRELK-----PDLVIVDIDMPDRDGLEAARQISEERPA 76

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 880808944 250 ShayCILHTSLSSEICVDRANQVGAHEALEK-FNAGELIEAM 290
Cdd:COG3707   77 P---VILLTAYSDPELIERALEAGVSAYLVKpLDPEDLLPAL 115
REC_LytTR_AlgR-like cd17532
phosphoacceptor receiver (REC) domain of LytTR/AlgR family response regulators similar to AlgR; ...
 175-240 6.06e-07

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: 47.53  E-value: 6.06e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 880808944 175 ILLVDDSLIARKQLSDALDSINipySI-----CNNGLDAIDLMRRqasvdNAIDLLVSDIEMPGLDGYELA 240
Cdd:cd17532    1 ALIVDDEPLAREELRYLLEEHP---DIeivgeAENGEEALEAIEE-----LKPDVVFLDIQMPGLDGLELA 63
REC_CpdR_CckA-like cd18160
phosphoacceptor receiver (REC) domain of Brucella abortus CpdR and CckA, and similar domains; ...
 175-243 1.17e-06

phosphoacceptor receiver (REC) domain of Brucella abortus CpdR and CckA, and similar domains; Two-component systems (TCSs), consisting of a sensor and a response regulator, are used by bacteria to adapt to changing environments. Processes regulated by TCSs in bacteria include sporulation, pathogenicity, virulence, chemotaxis and membrane transport. Response regulators share the common phosphoacceptor REC domain and differ output domains such as DNA, RNA, ligand, and protein-binding, or enzymatic domain. CpdR is a stand-alone REC protein. CckA is a sensor histidine kinase containing N-terminal PAS domains and a C-terminal REC domain. CpdR and CckA are components of a regulatory phosphorelay system (composed of CckA, ChpT, CtrA and CpdR) that controls Brucella abortus cell growth, division, and intracellular survival inside mammalian host cells. CckA autophosphorylates in the presence of ATP and transfers a phosphoryl group to the conserved aspartic acid residue on its C-terminal REC domain, which is relayed to the ChpT phosphotransferase. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381144 [Multi-domain]  Cd Length: 103  Bit Score: 46.34  E-value: 1.17e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 880808944 175 ILLVDDSLIARKQLSDALDSINIPYSICNNGLDAIDLMRRQAsvdnAIDLLVSDIEMPGLDGYELAFEV 243
Cdd:cd18160    2 ILLADDEPSVRKFIVTTLKKAGYAVTEAESGAEALEKLQQGK----DIDIVVTDIVMPEMDGIELAREA 66
REC_RpfG-like cd17551
phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase response regulator ...
 174-251 3.13e-06

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: 45.51  E-value: 3.13e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 880808944 174 NILLVDDSLIARKQLSDALDSI-NIPYSICNNGLDAIDLMRRqasvdNAIDLLVSDIEMPGLDGYELAFEVQNDSALSH 251
Cdd:cd17551    2 RILIVDDNPTNLLLLEALLRSAgYLEVVSFTDPREALAWCRE-----NPPDLILLDYMMPGMDGLEFIRRLRALPGLED 75
REC_NtrC cd19919
phosphoacceptor receiver (REC) domain of DNA-binding transcriptional regulator NtrC; ...
 175-288 3.18e-06

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: 45.34  E-value: 3.18e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808944 175 ILLVDDSLIARKQLSDALDSINIPYSICNNGLDAID-LMRRQASVdnaidlLVSDIEMPGLDGYELAFEVQNDsaLSHAY 253
Cdd:cd19919    3 VWIVDDDSSIRWVLERALAGAGLTVTSFENAQEALAaLASSQPDV------LISDIRMPGMDGLALLAQIKQR--HPDLP 74

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 880808944 254 CIL---HTSLSSEIcvdRANQVGAHEALEK-FNAGELIE 288
Cdd:cd19919   75 VIImtaHSDLDSAV---SAYQGGAFEYLPKpFDIDEAVA 110
REC_PdtaR-like cd19932
phosphoacceptor receiver (REC) domain of PdtaR and similar proteins; This subfamily includes ...
 173-290 3.57e-06

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: 45.10  E-value: 3.57e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808944 173 LNILLVDDSLIARKQLSDALDSINipYSI---CNNGLDAIDLMRRQASvdnaiDLLVSDIEMPGLDGYELAFEVQNDSAl 249
Cdd:cd19932    1 VRVLIAEDEALIRMDLREMLEEAG--YEVvgeASDGEEAVELAKKHKP-----DLVIMDVKMPRLDGIEAAKIITSENI- 72

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 880808944 250 shAYCILHTSLSSEICVDRANQVGAHEALEK-FNAGELIEAM 290
Cdd:cd19932   73 --APIVLLTAYSQQDLVERAKEAGAMAYLVKpFSESDLIPAI 112
orf27 CHL00148
Ycf27; Reviewed
 175-247 4.04e-06

Ycf27; Reviewed


Pssm-ID: 214376 [Multi-domain]  Cd Length: 240  Bit Score: 47.02  E-value: 4.04e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 880808944 175 ILLVDDSLIARKQLSDALDSINIPYSICNNGLDAIDLMRRQAsvdnaIDLLVSDIEMPGLDGYELAFEVQNDS 247
Cdd:CHL00148   9 ILVVDDEAYIRKILETRLSIIGYEVITASDGEEALKLFRKEQ-----PDLVILDVMMPKLDGYGVCQEIRKES 76
REC_CheY4-like cd17562
phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY4 and similar CheY ...
 175-297 4.09e-06

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: 44.98  E-value: 4.09e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808944 175 ILLVDDSLIARKQLSDALDSINIPYSICNNGLDAIDLmrrqASVDNaIDLLVSDIEMPGLDGYELAFEVQNDSALSHAYC 254
Cdd:cd17562    3 ILAVDDSASIRQMVSFTLRGAGYEVVEAADGRDALSK----AQSKK-FDLIITDQNMPNMDGIELIKELRKLPAYKFTPI 77

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 880808944 255 ILHTSLSSEICVDRANQVGAHEALEK-FNAGELIEAMlrgAKVL 297
Cdd:cd17562   78 LMLTTESSDEKKQEGKAAGATGWLVKpFDPEQLLEVV---KKVL 118
REC_typeA_ARR cd17581
phosphoacceptor receiver (REC) domain of type A Arabidopsis response regulators (ARRs) and ...
 175-280 4.36e-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: 45.05  E-value: 4.36e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808944 175 ILLVDDSLIARKQLSDALDSINIPYSICNNGLDAIDLM------RRQASVDNAIDLLVSDIEMPGLDGYELAFEVQNDSA 248
Cdd:cd17581    1 VLAVDDSLVDRKVIERLLRISSCRVTAVDSGKRALEFLgledeeDSSNFNEPKVNMIITDYCMPGMTGYDLLKKVKESSA 80

                         90       100       110
                 ....*....|....*....|....*....|..
gi 880808944 249 LSHAYCILHTSLSSEICVDRANQVGAHEALEK 280
Cdd:cd17581   81 LKEIPVVIMSSENIPTRISRCLEEGAEDFLLK 112
CitB COG4565
DNA-binding response regulator DpiB of citrate/malate metabolism [Transcription, Signal ...
 170-292 5.47e-06

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


Pssm-ID: 443622 [Multi-domain]  Cd Length: 138  Bit Score: 45.35  E-value: 5.47e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808944 170 LKALNILLVDDSLIARKQLSDALDSINIPYSI--CNNGLDAIDLMRRqasvdNAIDLLVSDIEMPGLDGYELAFEVQNDS 247
Cdd:COG4565    1 MKMIRVLIVEDDPMVAELLRRYLERLPGFEVVgvASSGEEALALLAE-----HRPDLILLDIYLPDGDGLELLRELRARG 75

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 880808944 248 AlsHAYCILHTSLSSEICVDRANQVGAHEALEK-FNAGELIEAMLR 292
Cdd:COG4565   76 P--DVDVIVITAARDPETVREALRAGVVDYLIKpFTFERLREALER 119
REC smart00448
cheY-homologous receiver domain; CheY regulates the clockwise rotation of E. coli flagellar ...
 173-232 7.70e-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: 42.56  E-value: 7.70e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808944   173 LNILLVDDSLIARKQLSDALDSINIPYSICNNGLDAIDLMRRqasvdNAIDLLVSDIEMP 232
Cdd:smart00448   1 MRILVVDDDPLLRELLKALLEKEGYEVDEATDGEEALELLKE-----EKPDLILLDIMMP 55
REC_HupR-like cd17569
phosphoacceptor receiver (REC) domain of hydrogen uptake protein regulator (HupR) and similar ...
 174-239 8.75e-06

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: 43.93  E-value: 8.75e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 880808944 174 NILLVDDSLIARKQLSDALdsINIPYSI--CNNGLDAIDLMRRqasvdNAIDLLVSDIEMPGLDGYEL 239
Cdd:cd17569    2 TILLVDDEPNILKALKRLL--RREGYEVltATSGEEALEILKQ-----EPVDVVISDQRMPGMDGAEL 62
REC_OmpR cd17574
phosphoacceptor receiver (REC) domain of OmpR family response regulators; OmpR-like proteins ...
 176-239 1.36e-05

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: 43.17  E-value: 1.36e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 880808944 176 LLVDDSLIARKQLSDALDSINIPYSICNNGLDAIDLMRRQAsvdnaIDLLVSDIEMPGLDGYEL 239
Cdd:cd17574    1 LVVEDDEEIAELLSDYLEKEGYEVDTAADGEEALELAREEQ-----PDLIILDVMLPGMDGFEV 59
PRK10612 PRK10612
chemotaxis protein CheW;
5-148 2.09e-05

chemotaxis protein CheW;


Pssm-ID: 182587  Cd Length: 167  Bit Score: 44.03  E-value: 2.09e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808944   5 ISKASQSQGMLMFKLSlTQSFAIGTLKVREIVPFQPMTQIPYSHHHVIGTVTIRDLTVPVIDMSaaIGFRPITPAEYQDC 84
Cdd:PRK10612  10 LAGEPSGQEFLVFTLG-DEEYGIDILKVQEIRGYDQVTRIANTPAFIKGVTNLRGVIVPIVDLR--IKFSQVDVDYNDNT 86

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 880808944  85 VLIVTDCLRTVVAFLVRSIDKIIECDWKSIE-SPPTSVGRNV-FVTGITRFEDRIVQMLDVELLLS 148
Cdd:PRK10612  87 VVIVLNLGQRVVGIVVDGVSDVLSLTAEQIRpAPEFAVTLSTeYLTGLGALGERMLILVNIEKLLN 152
REC_NarL-like cd17535
phosphoacceptor receiver (REC) domain of NarL (Nitrate/Nitrite response regulator L) family ...
 175-289 2.63e-05

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: 42.88  E-value: 2.63e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808944 175 ILLVDDSLIARKQLSDALDSINiPYSI---CNNGLDAIDLMRRqasvdNAIDLLVSDIEMPGLDGYELAFEVQndSALSH 251
Cdd:cd17535    1 VLIVDDHPLVREGLRRLLESEP-DIEVvgeAADGEEALALLRE-----LRPDVVLMDLSMPGMDGIEALRRLR--RRYPD 72

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 880808944 252 AYCILHTSLSSEICVDRANQVGAHEALEK-FNAGELIEA 289
Cdd:cd17535   73 LKVIVLTAHDDPEYVLRALKAGAAGYLLKdSSPEELIEA 111
REC_typeB_ARR-like cd17584
phosphoacceptor receiver (REC) domain of type B Arabidopsis response regulators (ARRs) and ...
 175-239 4.51e-05

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: 41.84  E-value: 4.51e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 880808944 175 ILLVDDSLIARKQLSDALDSINIPYSICNNGLDAIDLMRRQasvDNAIDLLVSDIEMPGLDGYEL 239
Cdd:cd17584    1 VLVVDDDPTCLAILKRMLLRCGYQVTTCTDAEEALSMLREN---KDEFDLVITDVHMPDMDGFEF 62
PRK10610 PRK10610
chemotaxis protein CheY;
171-290 4.51e-05

chemotaxis protein CheY;


Pssm-ID: 170568 [Multi-domain]  Cd Length: 129  Bit Score: 42.27  E-value: 4.51e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808944 171 KALNILLVDDSLIARKQLSDALDSI---NIPYSicNNGLDAIDLMRrqasvDNAIDLLVSDIEMPGLDGYELAFEVQNDS 247
Cdd:PRK10610   4 KELKFLVVDDFSTMRRIVRNLLKELgfnNVEEA--EDGVDALNKLQ-----AGGFGFVISDWNMPNMDGLELLKTIRADG 76

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 880808944 248 ALSHAYCILHTSLSSEICVDRANQVGAHEALEK-FNAGELIEAM 290
Cdd:PRK10610  77 AMSALPVLMVTAEAKKENIIAAAQAGASGYVVKpFTAATLEEKL 120
CitB COG2197
DNA-binding response regulator, NarL/FixJ family, contains REC and HTH domains [Signal ...
 173-240 5.48e-05

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: 42.19  E-value: 5.48e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 880808944 173 LNILLVDDSLIARKQLSDALDS---INIpYSICNNGLDAIDLMRRQAsvdnaIDLLVSDIEMPGLDGYELA 240
Cdd:COG2197    2 IRVLIVDDHPLVREGLRALLEAepdIEV-VGEAADGEEALELLEELR-----PDVVLLDIRMPGMDGLEAL 66
PRK15347 PRK15347
two component system sensor kinase;
173-280 5.63e-05

two component system sensor kinase;


Pssm-ID: 237951 [Multi-domain]  Cd Length: 921  Bit Score: 44.63  E-value: 5.63e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808944 173 LNILLVDDSLIARKQLSDALDSINIPYSICNNGLDAIDLMRRQAsvdnaIDLLVSDIEMPGLDGYELAFEVQNDSALSHA 252
Cdd:PRK15347 691 LQILLVDDVETNRDIIGMMLVELGQQVTTAASGTEALELGRQHR-----FDLVLMDIRMPGLDGLETTQLWRDDPNNLDP 765

                         90       100       110
                 ....*....|....*....|....*....|...
gi 880808944 253 YCILhTSLS-----SEIcvDRANQVGAHEALEK 280
Cdd:PRK15347 766 DCMI-VALTanaapEEI--HRCKKAGMNHYLTK 795
PRK00742 PRK00742
chemotaxis-specific protein-glutamate methyltransferase CheB;
171-236 5.83e-05

chemotaxis-specific protein-glutamate methyltransferase CheB;


Pssm-ID: 234828 [Multi-domain]  Cd Length: 354  Bit Score: 43.99  E-value: 5.83e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 880808944 171 KALNILLVDDSLIARKQLSDALDS---INIpYSICNNGLDAIDLMRRQAsvdnaIDLLVSDIEMPGLDG 236
Cdd:PRK00742   2 MKIRVLVVDDSAFMRRLISEILNSdpdIEV-VGTAPDGLEAREKIKKLN-----PDVITLDVEMPVMDG 64
REC_DivK-like cd17548
phosphoacceptor receiver (REC) domain of DivK and similar proteins; Caulobacter crescentus ...
 174-251 6.86e-05

phosphoacceptor receiver (REC) domain of DivK and similar proteins; Caulobacter crescentus DivK is an essential response regulator that is involved in the complex phosphorelay pathways controlling both cell division and motility. It localizes cell cycle regulators to specific poles of the cell during division. DivK contains a stand-alone REC domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381100 [Multi-domain]  Cd Length: 115  Bit Score: 41.37  E-value: 6.86e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808944 174 NILLVDDSLIARKQLSDALDSINipYSICN--NGLDAIDLMRRQASvdnaiDLLVSDIEMPGLDGYELAFEVQNDSALSH 251
Cdd:cd17548    1 KILIVEDNPLNMKLARDLLESAG--YEVLEaaDGEEALEIARKEKP-----DLILMDIQLPGMDGLEATRLLKEDPATRD 73
REC_PA4781-like cd19920
phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase PA4781 and similar ...
 175-262 1.22e-04

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: 40.57  E-value: 1.22e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808944 175 ILLVDDSLIARKQLSDALDSINIPYSICNNGLDAIDLMRRQAsvdnaIDLLVSDIEMPGLDGYELAFEVQNDSALSHAYC 254
Cdd:cd19920    1 ILIVDDVPDNLRLLSELLRAAGYRVLVATDGQQALQRAQAEP-----PDLILLDVMMPGMDGFEVCRRLKADPATRHIPV 75


                 ....*...
gi 880808944 255 ILHTSLSS 262
Cdd:cd19920   76 IFLTALTD 83
PLN03029 PLN03029
type-a response regulator protein; Provisional
 173-276 2.81e-04

type-a response regulator protein; Provisional


Pssm-ID: 215544 [Multi-domain]  Cd Length: 222  Bit Score: 41.56  E-value: 2.81e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808944 173 LNILLVDDSLIARKQLSDALDSINIPYSICNNGLDAIDLMRRQASVDNA---------------IDLLVSDIEMPGLDGY 237
Cdd:PLN03029   9 FHVLAVDDSLIDRKLIEKLLKTSSYQVTTVDSGSKALKFLGLHEDDRSNpdtpsvspnshqeveVNLIITDYCMPGMTGY 88

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 880808944 238 ELAFEVQNDSALSHAYCILHTSLSSEICVDRANQVGAHE 276
Cdd:PLN03029  89 DLLKKIKESSSLRNIPVVIMSSENVPSRITRCLEEGAEE 127
REC_OmpR_ArcA_TorR-like cd17619
phosphoacceptor receiver (REC) domain of ArcA- and TorR-like OmpR family response regulators; ...
 174-287 3.10e-04

phosphoacceptor receiver (REC) domain of ArcA- and TorR-like OmpR family response regulators; This subfamily includes Escherichia coli TorR and ArcA, both OmpR family response regulators that mediate adaptation to changes in various respiratory growth conditions. The TorS-TorR two-component system (TCS) is responsible for the tight regulation of the torCAD operon, which encodes the trimethylamine N-oxide (TMAO) reductase respiratory system in response to anaerobic conditions and the presence of TMAO. The ArcA-ArcB TCS is involved in cell growth during anaerobiosis. ArcA is a global regulator that controls more than 30 operons involved in redox regulation (the Arc modulon). OmpR family DNA-binding response regulators are characterized by a REC domain and a winged helix-turn-helix (wHTH) DNA-binding output effector domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381134 [Multi-domain]  Cd Length: 113  Bit Score: 39.68  E-value: 3.10e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808944 174 NILLVDDSLIARKQLSDALDSINIPYSICNNGLDAIDLMRRQAsvdnaIDLLVSDIEMPGLDGYELAFEVQndsALSHAY 253
Cdd:cd17619    2 HILIVEDEPVTRATLKSYFEQEGYDVSEAGDGEEMRQILARQD-----IDLVLLDINLPGKDGLSLTRELR---EQSEVG 73

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 880808944 254 CILHTSLSSEIcvDR--ANQVGAHEALEK-FNAGELI 287
Cdd:cd17619   74 IILVTGRDDEV--DRivGLEIGADDYVTKpFNPRELL 108
PRK11107 PRK11107
hybrid sensory histidine kinase BarA; Provisional
 146-236 3.17e-04

hybrid sensory histidine kinase BarA; Provisional


Pssm-ID: 236848 [Multi-domain]  Cd Length: 919  Bit Score: 42.14  E-value: 3.17e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808944 146 LLSKIYPDYENAHIPMLTDVERERLkALNILLVDDSLiARKQLSDAL-----DSInipySICNNGLDAIDLMRRQAsvdn 220
Cdd:PRK11107 642 LLPALLEPCHHKQPPLLPPTDESRL-PLTVMAVDDNP-ANLKLIGALleeqvEHV----VLCDSGHQAVEQAKQRP---- 711

                         90
                 ....*....|....*.
gi 880808944 221 aIDLLVSDIEMPGLDG 236
Cdd:PRK11107 712 -FDLILMDIQMPGMDG 726
REC_OmpR_CpxR cd17623
phosphoacceptor receiver (REC) domain of CpxR-like OmpR family response regulators; CpxR is ...
 175-292 6.33e-04

phosphoacceptor receiver (REC) domain of CpxR-like OmpR family response regulators; CpxR is part of the CpxA/CpxR two-component regulatory system that mediates envelope stress responses that is key for virulence and antibiotic resistance in several Gram negative pathogens. CpxR is a transcription factor/response regulator that controls the expression of numerous genes, including those of the classical porins OmpF and OmpC. It belongs to the OmpR family of DNA-binding response regulators that contain N-terminal receiver (REC) and C-terminal DNA-binding winged helix-turn-helix effector domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381138 [Multi-domain]  Cd Length: 115  Bit Score: 38.83  E-value: 6.33e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808944 175 ILLVDDSLIARKQLSDALDSINIPYSICNNGLDAIDLMRRQAsvdnaIDLLVSDIEMPGLDGYELAFEVQNDSALShayC 254
Cdd:cd17623    1 ILLIDDDRELTELLTEYLEMEGFNVRAAHDGEQGLAALLEGS-----PDLVVLDVMLPKMNGLDVLKELRKTSQVP---V 72

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 880808944 255 ILHTSLSSEIcvDR--ANQVGAHEALEK-FNAGEL---IEAMLR 292
Cdd:cd17623   73 LMLTARGDDI--DRilGLELGADDYLPKpFNPRELvarIRAILR 114
REC_DctD-like cd17549
phosphoacceptor receiver (REC) domain of C4-dicarboxylic acid transport protein D (DctD) and ...
 175-239 1.01e-03

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: 38.62  E-value: 1.01e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 880808944 175 ILLVDDSLIARKQLSDALDSINIPYSICNNGLDAIDLMRRqasvdNAIDLLVSDIEMPGLDGYEL 239
Cdd:cd17549    1 VLLVDDDADVREALQQTLELAGFRVRAFADAEEALAALSP-----DFPGVVISDIRMPGMDGLEL 60
REC_DesR-like cd19930
phosphoacceptor receiver (REC) domain of DesR and similar proteins; This group is composed of ...
 204-244 1.19e-03

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: 38.02  E-value: 1.19e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 880808944 204 NGLDAIDLMRRQASvdnaiDLLVSDIEMPGLDGYELAFEVQ 244
Cdd:cd19930   32 NGQEALRLVLKHSP-----DVAILDIEMPGRTGLEVAAELR 67
pleD PRK09581
response regulator PleD; Reviewed
 175-262 1.27e-03

response regulator PleD; Reviewed


Pssm-ID: 236577 [Multi-domain]  Cd Length: 457  Bit Score: 40.27  E-value: 1.27e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808944 175 ILLVDDSLIARKQLSDALDSINIPYSICNNGLDAIDLMRRQAsvdnaIDLLVSDIEMPGLDGYELAFEVQNDSALSHAYC 254
Cdd:PRK09581   5 ILVVDDIPANVKLLEAKLLAEYYTVLTASSGAEAIAICEREQ-----PDIILLDVMMPGMDGFEVCRRLKSDPATTHIPV 79


                 ....*...
gi 880808944 255 ILHTSLSS 262
Cdd:PRK09581  80 VMVTALDD 87
PRK11697 PRK11697
two-component system response regulator BtsR;
173-239 1.40e-03

two-component system response regulator BtsR;


Pssm-ID: 236956 [Multi-domain]  Cd Length: 238  Bit Score: 39.44  E-value: 1.40e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808944 173 LNILLVDDSLIARKQLSDALDS---INIPYSiCNNGLDAIDLMRRQASvdnaiDLLVSDIEMPGLDGYEL 239
Cdd:PRK11697   2 IKVLIVDDEPLAREELRELLQEegdIEIVGE-CSNAIEAIGAIHRLKP-----DVVFLDIQMPRISGLEL 65
REC_OmpR_PrrA-like cd17627
phosphoacceptor receiver (REC) domain of PrrA-like OmpR family response regulators; The ...
 175-240 1.53e-03

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: 37.75  E-value: 1.53e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 880808944 175 ILLVDDSLIARKQLSDALDSINIPYSICNNGLDAIDLMrrqasVDNAIDLLVSDIEMPGLDGYELA 240
Cdd:cd17627    1 ILVVDDDRAVRESLRRSLRFEGYEVETAVDGAEALRVI-----SGNRPDAVVLDVMMPRLDGLEVC 61
REC_DC-like cd17534
phosphoacceptor receiver (REC) domain of modulated diguanylate cyclase and similar domains; ...
 174-290 1.57e-03

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: 37.77  E-value: 1.57e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808944 174 NILLVDDSLIARKQLSDALDSINipYSIC---NNGLDAIDLMRRqasvdNAIDLLVSDIEMPG-LDGYELAFEVQNDSAL 249
Cdd:cd17534    2 KILIVEDEAIIALDLKEILESLG--YEVVgiaDSGEEAIELAEE-----NKPDLILMDINLKGdMDGIEAAREIREKFDI 74

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 880808944 250 SHAYCilhTSLSSEICVDRANQVGAHEALEK-FNAGELIEAM 290
Cdd:cd17534   75 PVIFL---TAYSDEETLERAKETNPYGYLVKpFNERELKAAI 113
PRK10955 PRK10955
envelope stress response regulator transcription factor CpxR;
175-292 1.95e-03

envelope stress response regulator transcription factor CpxR;


Pssm-ID: 182864 [Multi-domain]  Cd Length: 232  Bit Score: 39.02  E-value: 1.95e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808944 175 ILLVDDSLIARKQLSDALDSINIPYSICNNGLDAIDLMrrqasvDNAIDLLVSDIEMPGLDGYELAFEVQNDSALShayC 254
Cdd:PRK10955   4 ILLVDDDRELTSLLKELLEMEGFNVIVAHDGEQALDLL------DDSIDLLLLDVMMPKKNGIDTLKELRQTHQTP---V 74

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 880808944 255 ILHTSLSSEIcvDR--ANQVGAHEALEK-FNAGEL---IEAMLR 292
Cdd:PRK10955  75 IMLTARGSEL--DRvlGLELGADDYLPKpFNDRELvarIRAILR 116
REC_PatA-like cd17602
phosphoacceptor receiver (REC) domain of PatA and similar domains; Nostoc sp. (or Anabaena sp.) ...
 175-280 2.10e-03

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


Pssm-ID: 381129 [Multi-domain]  Cd Length: 102  Bit Score: 36.96  E-value: 2.10e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808944 175 ILLVDDSLIARKQLSDALDSINIPYSICNNGLDAI-DLMRRQAsvdnaiDLLVSDIEMPGLDGYELAFEVQNDSALSHAY 253
Cdd:cd17602    1 VACVDDRPSIQKMIEYFLEKQGFRVVVIDDPLRALtTLLNSKP------DLILIDIDMPDLDGYELCSLLRKSSALKDTP 74

                         90       100
                 ....*....|....*....|....*..
gi 880808944 254 CILHTSLSSEICVDRANQVGAHEALEK 280
Cdd:cd17602   75 IIMLTGKDGLVDRIRAKMAGASGYLTK 101
PRK15115 PRK15115
response regulator GlrR; Provisional
 171-244 2.40e-03

response regulator GlrR; Provisional


Pssm-ID: 185070 [Multi-domain]  Cd Length: 444  Bit Score: 39.44  E-value: 2.40e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 880808944 171 KALNILLVDDSLIARKQLSDALDSINIPYSICNNGLDAIDLMRRQAsvdnaIDLLVSDIEMPGLDGYELAFEVQ 244
Cdd:PRK15115   4 KPAHLLLVDDDPGLLKLLGMRLTSEGYSVVTAESGQEALRVLNREK-----VDLVISDLRMDEMDGMQLFAEIQ 72
PRK12555 PRK12555
chemotaxis-specific protein-glutamate methyltransferase CheB;
174-238 3.00e-03

chemotaxis-specific protein-glutamate methyltransferase CheB;


Pssm-ID: 237135 [Multi-domain]  Cd Length: 337  Bit Score: 38.71  E-value: 3.00e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 880808944 174 NILLVDDSLIARKQLSDALDS---INIPYsICNNGLDAIDLMRRQASvdnaiDLLVSDIEMPGLDGYE 238
Cdd:PRK12555   2 RIGIVNDSPLAVEALRRALARdpdHEVVW-VATDGAQAVERCAAQPP-----DVILMDLEMPRMDGVE 63
REC_OmpR_CusR-like cd19935
phosphoacceptor receiver (REC) domain of CusR-like OmpR family response regulators; ...
 175-239 3.93e-03

phosphoacceptor receiver (REC) domain of CusR-like OmpR family response regulators; Escherichia coli CusR is part of the CusS/CusR two-component system (TCS) that is involved in response to copper and silver. Other members of this subfamily include Escherichia coli PcoR, Pseudomonas syringae CopR, and Streptomyces coelicolor CutR, which are all transcriptional regulatory proteins and components of TCSs that regulate genes involved in copper resistance and/or metabolism. member of the subfamily is Escherichia coli HprR (hydrogen peroxide response regulator), previously called YdeW, which is part of the HprSR (or YedVW) TCS involved in stress response to hydrogen peroxide, as well as Cupriavidus metallidurans CzcR, which is part of the CzcS/CzcR TCS involved in the control of cobalt, zinc, and cadmium homeostasis. Members of this subfamily belong to the OmpR family of DNA-binding response regulators, which contain N-terminal receiver (REC) and C-terminal DNA-binding winged helix-turn-helix effector domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381162 [Multi-domain]  Cd Length: 100  Bit Score: 36.26  E-value: 3.93e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 880808944 175 ILLV-DDSLIA---RKQLSDALDSINIpysiCNNGLDAIDLMRRqasvdNAIDLLVSDIEMPGLDGYEL 239
Cdd:cd19935    1 ILVVeDEKKLAeylKKGLTEEGYAVDV----AYDGEDGLHLALT-----NEYDLIILDVMLPGLDGLEV 60
REC_hyHK_blue-like cd18161
phosphoacceptor receiver (REC) domain of hybrid sensor histidine kinase/response regulators ...
 175-243 3.93e-03

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: 36.17  E-value: 3.93e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808944 175 ILLVDDSLIARKQLSDALDSINIPYSICNNGLDAIDLMRRqasvDNAIDLLVSDIEMPG-LDGYELAFEV 243
Cdd:cd18161    1 VLVVEDDPDVRRLTAEVLEDLGYTVLEAASGDEALDLLES----GPDIDLLVTDVIMPGgMNGSQLAEEA 66
REC_OmpR_BfmR-like cd19939
phosphoacceptor receiver (REC) domain of BfmR-like OmpR family response regulators; ...
 175-292 4.73e-03

phosphoacceptor receiver (REC) domain of BfmR-like OmpR family response regulators; Acinetobacter baumannii BfmR is part of the BfmR/S two-component system that functions as the master regulator of biofilm initiation. BfmR confers resistance to complement-mediated bactericidal activity, independent of capsular polysaccharide, and also increases resistance to the clinically important antimicrobials meropenem and colistin, making it a potential antimicrobial target. Its inhibition would have the dual benefit of significantly decreasing in vivo survival and increasing sensitivity to selected antimicrobials. 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: 381166 [Multi-domain]  Cd Length: 116  Bit Score: 36.20  E-value: 4.73e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808944 175 ILLVDDSLIARKQLSDALDSINIPYSICNNGLDAIDLMRRQASvdnaiDLLVSDIEMPGLDGYELAFEVQNDsalSHAYC 254
Cdd:cd19939    2 ILIVEDELELARLTRDYLIKAGLEVSVFTDGQRAVRRIIDEQP-----SLVVLDIMLPGMDGLTVCREVREH---SHVPI 73

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 880808944 255 ILHTSLSSEIcvDR--ANQVGAHEALEK-FNAGEL---IEAMLR 292
Cdd:cd19939   74 LMLTARTEEM--DRvlGLEMGADDYLCKpFSPRELlarVRALLR 115
REC_TrrA-like cd17554
phosphoacceptor receiver (REC) domain of Thermotoga maritima response regulator TrrA and ...
 174-243 8.50e-03

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: 35.66  E-value: 8.50e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808944 174 NILLVDDSLIARKQLSDALDSINIPYSICNNGLDAIDLMRRQAsvdnaIDLLVSDIEMPGLDGYELAFEV 243
Cdd:cd17554    2 KILVVDDEENIRELYKEELEDEGYEVVTAGNGEEALEKLESED-----PDLVILDIKMPGMDGLETLRKI 66
 
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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