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Conserved domains on  [gi|1941938483|ref|WP_197121667|]
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response regulator [Pseudoalteromonas sp. NZS100]

Protein Classification

response regulator( domain architecture ID 1002978)

response regulator receives the signal from a sensor partner in two-component systems through its receiver (REC) domain, similar to CitB family transcriptional regulators

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
dpiA super family cl32452
two-component response regulator DpiA; Provisional
 48-237 2.13e-44

two-component response regulator DpiA; Provisional


The actual alignment was detected with superfamily member PRK10046:

Pssm-ID: 182208 [Multi-domain]  Cd Length: 225  Bit Score: 148.63  E-value: 2.13e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941938483  48 IAGNLSTATALLHAIEPDLILLDIHLPDGNGLDLLTDLRRRTIKSEVMLLTAAKEVETLEKAMQLGACDFLVKPLMLNRL 127
Cdd:PRK10046   35 LAGNLAQARMMIERFKPGLILLDNYLPDGRGINLLHELVQAHYPGDVVFTTAASDMETVSEAVRCGVFDYLIKPIAYERL 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941938483 128 DQALARFESRQQCFSDASEVTQSMVDTLFGSKQQTNIFNRLPKGVDQLTLQKIHDAFVEhATTAFTAQQMGDLVGVSRST 207
Cdd:PRK10046  115 GQTLTRFRQRKHMLESIDSASQKQIDEMFNAYARGEPKDELPTGIDPLTLNAVRKLFKE-PGVQHTAETVAQALTISRTT 193

                         170       180       190
                  ....*....|....*....|....*....|
gi 1941938483 208 ARRYLEYLLESGKLTADQSYGSIGRPERCY 237
Cdd:PRK10046  194 ARRYLEYCASRHLIIAEIVHGKVGRPQRIY 223
 
Name Accession Description Interval E-value
dpiA PRK10046
two-component response regulator DpiA; Provisional
 48-237 2.13e-44

two-component response regulator DpiA; Provisional


Pssm-ID: 182208 [Multi-domain]  Cd Length: 225  Bit Score: 148.63  E-value: 2.13e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941938483  48 IAGNLSTATALLHAIEPDLILLDIHLPDGNGLDLLTDLRRRTIKSEVMLLTAAKEVETLEKAMQLGACDFLVKPLMLNRL 127
Cdd:PRK10046   35 LAGNLAQARMMIERFKPGLILLDNYLPDGRGINLLHELVQAHYPGDVVFTTAASDMETVSEAVRCGVFDYLIKPIAYERL 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941938483 128 DQALARFESRQQCFSDASEVTQSMVDTLFGSKQQTNIFNRLPKGVDQLTLQKIHDAFVEhATTAFTAQQMGDLVGVSRST 207
Cdd:PRK10046  115 GQTLTRFRQRKHMLESIDSASQKQIDEMFNAYARGEPKDELPTGIDPLTLNAVRKLFKE-PGVQHTAETVAQALTISRTT 193

                         170       180       190
                  ....*....|....*....|....*....|
gi 1941938483 208 ARRYLEYLLESGKLTADQSYGSIGRPERCY 237
Cdd:PRK10046  194 ARRYLEYCASRHLIIAEIVHGKVGRPQRIY 223
CitB COG4565
DNA-binding response regulator DpiB of citrate/malate metabolism [Transcription, Signal ...
 1-139 9.50e-33

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


Pssm-ID: 443622 [Multi-domain]  Cd Length: 138  Bit Score: 115.84  E-value: 9.50e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941938483   1 MTYSVVIIEDEVEVAQLLaqylllpngiagnqtpKQSLRQ-AQYQVVGIAGNLSTATALLHAIEPDLILLDIHLPDGNGL 79
Cdd:COG4565     2 KMIRVLIVEDDPMVAELL----------------RRYLERlPGFEVVGVASSGEEALALLAEHRPDLILLDIYLPDGDGL 65

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941938483  80 DLLTDLRRRTIKSEVMLLTAAKEVETLEKAMQLGACDFLVKPLMLNRLDQALARFESRQQ 139
Cdd:COG4565    66 ELLRELRARGPDVDVIVITAARDPETVREALRAGVVDYLIKPFTFERLREALERYLEYRR 125
REC_citrate_TCS cd19925
phosphoacceptor receiver (REC) domain of citrate family two-component system response ...
 42-135 4.14e-30

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


Pssm-ID: 381152 [Multi-domain]  Cd Length: 118  Bit Score: 108.49  E-value: 4.14e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941938483  42 QYQVVGIAGNLSTATALLHAIEPDLILLDIHLPDGNGLDLLTDLRRRTIKSEVMLLTAAKEVETLEKAMQLGACDFLVKP 121
Cdd:cd19925    25 GFTVIGTAGTGEEALKLLKERQPDLILLDIYLPDGNGLDLLRELRAAGHDVDVIVVTAANDVETVREALRLGVVDYLIKP 104

                          90
                  ....*....|....
gi 1941938483 122 LMLNRLDQALARFE 135
Cdd:cd19925   105 FTFERLRQRLERYR 118
Response_reg pfam00072
Response regulator receiver domain; This domain receives the signal from the sensor partner in ...
 35-132 6.06e-20

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: 81.81  E-value: 6.06e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941938483  35 KQSLRQAQYqVVGIAGNLSTATALLHAIEPDLILLDIHLPDGNGLDLLTDLRRRTIKSEVMLLTAAKEVETLEKAMQLGA 114
Cdd:pfam00072  15 RQLLEKEGY-VVAEADDGKEALELLKEERPDLILLDINMPGMDGLELLKRIRRRDPTTPVIILTAHGDEDDAVEALEAGA 93

                          90
                  ....*....|....*...
gi 1941938483 115 CDFLVKPLMLNRLDQALA 132
Cdd:pfam00072  94 DDFLSKPFDPDELLAAIR 111
spore_0_A TIGR02875
sporulation transcription factor Spo0A; Spo0A, the stage 0 sporulation protein A, is a ...
 40-127 2.67e-09

sporulation transcription factor Spo0A; Spo0A, the stage 0 sporulation protein A, is a transcription factor critical for the initiation of sporulation. It contains a response regulator receiver domain (pfam00072). In Bacillus subtilis, it works together with response regulator Spo0F and the phosphotransferase Spo0B, both of which are missing from at least some sporulating species and thus not part of the endospore forming bacteria minimal gene set. Spo0A, however, is universal among endospore-forming species. [Cellular processes, Sporulation and germination]


Pssm-ID: 131922 [Multi-domain]  Cd Length: 262  Bit Score: 55.95  E-value: 2.67e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941938483  40 QAQYQVVGIAGNLSTATALLHAIEPDLILLDIHLPDGNGLDLLTDLRR--RTIKSEVMLLTAAKEVETLEKAMQLGACDF 117
Cdd:TIGR02875  25 QPDMEVVGVAHNGVDALELIKEQQPDVVVLDIIMPHLDGIGVLEKLNEieLSARPRVIMLSAFGQEKITQRAVALGADYY 104

                          90
                  ....*....|
gi 1941938483 118 LVKPLMLNRL 127
Cdd:TIGR02875 105 VLKPFDLEIL 114
REC smart00448
cheY-homologous receiver domain; CheY regulates the clockwise rotation of E. coli flagellar ...
 35-74 8.12e-04

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: 36.39  E-value: 8.12e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 1941938483   35 KQSLRQAQYQVVgIAGNLSTATALLHAIEPDLILLDIHLP 74
Cdd:smart00448  17 KALLEKEGYEVD-EATDGEEALELLKEEKPDLILLDIMMP 55
 
Name Accession Description Interval E-value
dpiA PRK10046
two-component response regulator DpiA; Provisional
 48-237 2.13e-44

two-component response regulator DpiA; Provisional


Pssm-ID: 182208 [Multi-domain]  Cd Length: 225  Bit Score: 148.63  E-value: 2.13e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941938483  48 IAGNLSTATALLHAIEPDLILLDIHLPDGNGLDLLTDLRRRTIKSEVMLLTAAKEVETLEKAMQLGACDFLVKPLMLNRL 127
Cdd:PRK10046   35 LAGNLAQARMMIERFKPGLILLDNYLPDGRGINLLHELVQAHYPGDVVFTTAASDMETVSEAVRCGVFDYLIKPIAYERL 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941938483 128 DQALARFESRQQCFSDASEVTQSMVDTLFGSKQQTNIFNRLPKGVDQLTLQKIHDAFVEhATTAFTAQQMGDLVGVSRST 207
Cdd:PRK10046  115 GQTLTRFRQRKHMLESIDSASQKQIDEMFNAYARGEPKDELPTGIDPLTLNAVRKLFKE-PGVQHTAETVAQALTISRTT 193

                         170       180       190
                  ....*....|....*....|....*....|
gi 1941938483 208 ARRYLEYLLESGKLTADQSYGSIGRPERCY 237
Cdd:PRK10046  194 ARRYLEYCASRHLIIAEIVHGKVGRPQRIY 223
PRK10430 PRK10430
two-component system response regulator DcuR;
43-239 1.16e-33

two-component system response regulator DcuR;


Pssm-ID: 182454 [Multi-domain]  Cd Length: 239  Bit Score: 121.37  E-value: 1.16e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941938483  43 YQVVGIAGNLSTATALLHA--IEPDLILLDIHLPDGNGLDLLTDLRRRTIKSEVMLLTAAKEVETLEKAMQLGACDFLVK 120
Cdd:PRK10430   27 FQCCGTASTLEQAKEIIFNsdTPIDLILLDIYMQQENGLDLLPVLHEAGCKSDVIVISSAADAATIKDSLHYGVVDYLIK 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941938483 121 PLMLNRLDQALARFESRQQCFSDASEVTQSMVDTLF-GSKQQTNIFNRLPKGVDQLTLQKIHDAFVEHATTAFTAQQMGD 199
Cdd:PRK10430  107 PFQASRFEEALTGWRQKKMALEKHQYYDQAELDQLIhGSSSNEQDPRRLPKGLTPQTLRTLCQWIDAHQDYEFSTDELAN 186

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1941938483 200 LVGVSRSTARRYLEYLLESGKLTADQSYGSIGRPERCYKI 239
Cdd:PRK10430  187 AVNISRVSCRKYLIWLVNCHILFTSIHYGVTGRPVYRYRL 226
CitB COG4565
DNA-binding response regulator DpiB of citrate/malate metabolism [Transcription, Signal ...
 1-139 9.50e-33

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


Pssm-ID: 443622 [Multi-domain]  Cd Length: 138  Bit Score: 115.84  E-value: 9.50e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941938483   1 MTYSVVIIEDEVEVAQLLaqylllpngiagnqtpKQSLRQ-AQYQVVGIAGNLSTATALLHAIEPDLILLDIHLPDGNGL 79
Cdd:COG4565     2 KMIRVLIVEDDPMVAELL----------------RRYLERlPGFEVVGVASSGEEALALLAEHRPDLILLDIYLPDGDGL 65

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941938483  80 DLLTDLRRRTIKSEVMLLTAAKEVETLEKAMQLGACDFLVKPLMLNRLDQALARFESRQQ 139
Cdd:COG4565    66 ELLRELRARGPDVDVIVITAARDPETVREALRAGVVDYLIKPFTFERLREALERYLEYRR 125
REC_citrate_TCS cd19925
phosphoacceptor receiver (REC) domain of citrate family two-component system response ...
 42-135 4.14e-30

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


Pssm-ID: 381152 [Multi-domain]  Cd Length: 118  Bit Score: 108.49  E-value: 4.14e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941938483  42 QYQVVGIAGNLSTATALLHAIEPDLILLDIHLPDGNGLDLLTDLRRRTIKSEVMLLTAAKEVETLEKAMQLGACDFLVKP 121
Cdd:cd19925    25 GFTVIGTAGTGEEALKLLKERQPDLILLDIYLPDGNGLDLLRELRAAGHDVDVIVVTAANDVETVREALRLGVVDYLIKP 104

                          90
                  ....*....|....
gi 1941938483 122 LMLNRLDQALARFE 135
Cdd:cd19925   105 FTFERLRQRLERYR 118
AtoC COG2204
DNA-binding transcriptional response regulator, NtrC family, contains REC, AAA-type ATPase, ...
 1-150 7.90e-24

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: 98.50  E-value: 7.90e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941938483   1 MTYSVVIIEDEVEVAQLLaqylllpngiagnqtpKQSLRQAQYQVVgIAGNLSTATALLHAIEPDLILLDIHLPDGNGLD 80
Cdd:COG2204     1 SMARILVVDDDPDIRRLL----------------KELLERAGYEVE-TAASGEEALALLREEPPDLVLLDLRMPGMDGLE 63

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1941938483  81 LLTDLRRRTIKSEVMLLTAAKEVETLEKAMQLGACDFLVKPLMLNRL----DQALARFESRQQCFSDASEVTQS 150
Cdd:COG2204    64 LLRELRALDPDLPVILLTGYGDVETAVEAIKAGAFDYLTKPFDLEELlaavERALERRRLRRENAEDSGLIGRS 137
REC cd00156
phosphoacceptor receiver (REC) domain of response regulators (RRs) and pseudo response ...
 38-121 2.89e-21

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: 84.97  E-value: 2.89e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941938483  38 LRQAQYQVVgIAGNLSTATALLHAIEPDLILLDIHLPDGNGLDLLTDLRRRTIKSEVMLLTAAKEVETLEKAMQLGACDF 117
Cdd:cd00156    17 LEREGYEVD-TAADGEEALELLREERPDLVLLDLMMPGMDGLELLRKLRELPPDIPVIVLTAKADEEDAVRALELGADDY 95


                  ....
gi 1941938483 118 LVKP 121
Cdd:cd00156    96 LVKP 99
OmpR COG0745
DNA-binding response regulator, OmpR family, contains REC and winged-helix (wHTH) domain ...
 2-143 7.54e-21

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: 86.93  E-value: 7.54e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941938483   2 TYSVVIIEDEVEVAQLLaqylllpngiagnqtpKQSLRQAQYQVVgIAGNLSTATALLHAIEPDLILLDIHLPDGNGLDL 81
Cdd:COG0745     1 MPRILVVEDDPDIRELL----------------ADALEREGYEVD-TAADGEEALELLEEERPDLILLDLMLPGMDGLEV 63

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1941938483  82 LTDLRRRTIKSEVMLLTAAKEVETLEKAMQLGACDFLVKPL----MLNRLDQALARFESRQQCFSD 143
Cdd:COG0745    64 CRRLRARPSDIPIIMLTARDDEEDRVRGLEAGADDYLTKPFdpeeLLARIRALLRRRAAEVLRVGD 129
LytT COG3279
DNA-binding response regulator, LytR/AlgR family [Transcription, Signal transduction ...
 43-139 1.41e-20

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


Pssm-ID: 442510 [Multi-domain]  Cd Length: 235  Bit Score: 86.79  E-value: 1.41e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941938483  43 YQVVGIAGNLSTATALLHAIEPDLILLDIHLPDGNGLDLLTDLRRRTIKSEVMLLTAAKEVetLEKAMQLGACDFLVKPL 122
Cdd:COG3279    27 LEVVGEASNGEEALELLEEHKPDLVFLDIQMPGLDGFELARQLRELDPPPPIIFTTAYDEY--ALEAFEVNAVDYLLKPI 104

                          90
                  ....*....|....*..
gi 1941938483 123 MLNRLDQALARFESRQQ 139
Cdd:COG3279   105 DEERLAKALEKAKERLE 121
Response_reg pfam00072
Response regulator receiver domain; This domain receives the signal from the sensor partner in ...
 35-132 6.06e-20

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: 81.81  E-value: 6.06e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941938483  35 KQSLRQAQYqVVGIAGNLSTATALLHAIEPDLILLDIHLPDGNGLDLLTDLRRRTIKSEVMLLTAAKEVETLEKAMQLGA 114
Cdd:pfam00072  15 RQLLEKEGY-VVAEADDGKEALELLKEERPDLILLDINMPGMDGLELLKRIRRRDPTTPVIILTAHGDEDDAVEALEAGA 93

                          90
                  ....*....|....*...
gi 1941938483 115 CDFLVKPLMLNRLDQALA 132
Cdd:pfam00072  94 DDFLSKPFDPDELLAAIR 111
PleD COG3706
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate ...
 38-134 1.87e-19

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: 82.26  E-value: 1.87e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941938483  38 LRQAQYQVVgIAGNLSTATALLHAIEPDLILLDIHLPDGNGLDLLTDLRRRTIKSE--VMLLTAAKEVETLEKAMQLGAC 115
Cdd:COG3706    21 LEAAGYEVV-EAADGEEALELLQEHRPDLILLDLEMPDMDGLELCRRLRADPRTADipIIFLTALDDEEDRARALEAGAD 99

                          90       100
                  ....*....|....*....|...
gi 1941938483 116 DFLVKPL----MLNRLDqALARF 134
Cdd:COG3706   100 DYLTKPFdpeeLLARVD-LVARY 121
CheY COG0784
CheY-like REC (receiver) domain, includes chemotaxis protein CheY and sporulation regulator ...
 35-139 3.79e-18

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: 77.58  E-value: 3.79e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941938483  35 KQSLRQAQYQVVgIAGNLSTATALLHAIEPDLILLDIHLPDGNGLDLLTDLRRRTIKSE--VMLLTAAKEVETLEKAMQL 112
Cdd:COG0784    22 RRLLERLGYEVT-TAEDGAEALELLRAGPPDLILLDINMPGMDGLELLRRIRALPRLPDipIIALTAYADEEDRERALEA 100

                          90       100
                  ....*....|....*....|....*..
gi 1941938483 113 GACDFLVKPLMLNRLDQALARFESRQQ 139
Cdd:COG0784   101 GADDYLTKPVDPEELLEALRRLLARAS 127
YesN COG4753
Two-component response regulator, YesN/AraC family, consists of REC and AraC-type DNA-binding ...
 39-121 5.00e-18

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


Pssm-ID: 443786 [Multi-domain]  Cd Length: 103  Bit Score: 76.35  E-value: 5.00e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941938483  39 RQAQYQVVGIAGNLSTATALLHAIEPDLILLDIHLPDGNGLDLLTDLRRRTIKSEVMLLTAAKEVETLEKAMQLGACDFL 118
Cdd:COG4753    21 WEAGFEVVGEAENGEEALELLEEHKPDLVITDINMPGMDGLELLEAIRELDPDTKIIILSGYSDFEYAQEAIKLGADDYL 100


                  ...
gi 1941938483 119 VKP 121
Cdd:COG4753   101 LKP 103
REC_OmpR_PmrA-like cd17624
phosphoacceptor receiver (REC) domain of PmrA-like OmpR family response regulators; This ...
 35-133 9.65e-18

phosphoacceptor receiver (REC) domain of PmrA-like OmpR family response regulators; This subfamily contains various OmpR family response regulators including PmrA, BasR, QseB, tctD, and RssB, which are components of two-component regulatory systems (TCSs). The PmrA/PmrB TCS controls transcription of genes that are involved in lipopolysaccharide modification in the outer membrane of bacteria, increasing bacterial resistance to host-derived antimicrobial peptides. The BasS/BasR TCS functions as an iron- and zinc-sensing transcription regulator. The QseB/QseC TCS activates the flagella regulon by activating transcription of FlhDC. The RssA/RssB TCS regulates swarming behavior in Serratia marcescens. OmpR family DNA-binding response regulators contain N-terminal receiver (REC) and C-terminal DNA-binding winged helix-turn-helix effector domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381139 [Multi-domain]  Cd Length: 115  Bit Score: 75.98  E-value: 9.65e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941938483  35 KQSLRQAQYQVvGIAGNLSTATALLHAIEPDLILLDIHLPDGNGLDLLTDLRRRTIKSEVMLLTAAKEVETLEKAMQLGA 114
Cdd:cd17624    15 KTGLRKAGYAV-DWVRTGAEAEAALASGPYDLVILDLGLPDGDGLDLLRRWRRQGQSLPVLILTARDGVDDRVAGLDAGA 93

                          90       100
                  ....*....|....*....|..
gi 1941938483 115 CDFLVKPLMLNRLD---QALAR 133
Cdd:cd17624    94 DDYLVKPFALEELLarlRALLR 115
COG4567 COG4567
DNA-binding response regulator, ActR/RegA family, consists of REC and Fis-type HTH domains ...
 35-139 1.72e-17

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


Pssm-ID: 443624 [Multi-domain]  Cd Length: 177  Bit Score: 77.26  E-value: 1.72e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941938483  35 KQSLRQAQYQVVgIAGNLSTATALLHAIEPDLILLDIHLPDGNGLDLLTDLRRRTIKSEVMLLTAAKEVETLEKAMQLGA 114
Cdd:COG4567    21 ARALERRGFEVT-TAASVEEALALLEQAPPDYAVLDLRLGDGSGLDLIEALRERDPDARIVVLTGYASIATAVEAIKLGA 99

                          90       100
                  ....*....|....*....|....*
gi 1941938483 115 CDFLVKPLMLNRLDQALARFESRQQ 139
Cdd:COG4567   100 DDYLAKPADADDLLAALERAEGDAP 124
RpfG COG3437
Response regulator c-di-GMP phosphodiesterase, RpfG family, contains REC and HD-GYP domains ...
 4-139 2.01e-17

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: 77.90  E-value: 2.01e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941938483   4 SVVIIEDEVEVAQLLaqylllpngiagnqtpKQSLRQAQYQVVgIAGNLSTATALLHAIEPDLILLDIHLPDGNGLDLLT 83
Cdd:COG3437     8 TVLIVDDDPENLELL----------------RQLLRTLGYDVV-TAESGEEALELLLEAPPDLILLDVRMPGMDGFELLR 70

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1941938483  84 DLRR--RTIKSEVMLLTAAKEVETLEKAMQLGACDFLVKPL----MLNRLDQALARFESRQQ 139
Cdd:COG3437    71 LLRAdpSTRDIPVIFLTALADPEDRERALEAGADDYLTKPFdpeeLLARVRNALELRRLQRE 132
REC_NtrC1-like cd17572
phosphoacceptor receiver (REC) domain of nitrogen regulatory protein C 1 (NtrC1) from Aquifex ...
 35-127 2.33e-17

phosphoacceptor receiver (REC) domain of nitrogen regulatory protein C 1 (NtrC1) from Aquifex aeolicus and similar NtrC family response regulators; NtrC family proteins are transcriptional regulators that have REC, AAA+ ATPase/sigma-54 interaction, and DNA-binding output domains. This subfamily of NtrC proteins include Aquifex aeolicus NtrC1 and Vibrio quorum-sensing signal integrator LuxO. The N-terminal REC domain of NtrC proteins regulate the activity of the protein and its phosphorylation controls the AAA+ domain oligomerization, while the central AAA+ domain participates in nucleotide binding, hydrolysis, oligomerization, and sigma54 interaction. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381114 [Multi-domain]  Cd Length: 121  Bit Score: 75.31  E-value: 2.33e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941938483  35 KQSLRQAQYQVVgIAGNLSTATALLHAIEPDLILLDIHLPDGNGLDLLTDLRRRTIKSEVMLLTAAKEVETLEKAMQLGA 114
Cdd:cd17572    15 QEYLSDEGYKVT-HVETGKEALAFLSDQPPDVVLLDLKLPDMSGMEILKWIQERSLPTSVIVITAHGSVDIAVEAMRLGA 93

                          90
                  ....*....|...
gi 1941938483 115 CDFLVKPLMLNRL 127
Cdd:cd17572    94 YDFLEKPFDADRL 106
AmiR COG3707
Two-component response regulator, AmiR/NasT family, consists of REC and RNA-binding ...
 1-139 5.67e-17

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: 76.15  E-value: 5.67e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941938483   1 MTYSVVIIEDEVEVAQLLaqylllpngiagnqtpKQSLRQAQYQVVGIAGNLSTATALLHAIEPDLILLDIHLPDGNGLD 80
Cdd:COG3707     2 RGLRVLVVDDEPLRRADL----------------REGLREAGYEVVAEAADGEDAVELVRELKPDLVIVDIDMPDRDGLE 65

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1941938483  81 LLTDLRRRTIKSeVMLLTAAKEVETLEKAMQLGACDFLVKPLMLNRL----DQALARFESRQQ 139
Cdd:COG3707    66 AARQISEERPAP-VILLTAYSDPELIERALEAGVSAYLVKPLDPEDLlpalELALARFRELRA 127
REC_YesN-like cd17536
phosphoacceptor receiver (REC) domain of YesN and related helix-turn-helix containing response ...
 5-133 2.15e-16

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: 72.76  E-value: 2.15e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941938483   5 VVIIEDEVEVAqllaqylllpNGIAgNQTPKQSLrqaQYQVVGIAGNLSTATALLHAIEPDLILLDIHLPDGNGLDLLTD 84
Cdd:cd17536     1 VLIVDDEPLIR----------EGLK-KLIDWEEL---GFEVVGEAENGEEALELIEEHKPDIVITDIRMPGMDGLELIEK 66

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1941938483  85 LRRRTIKSEVMLLTAAKEVETLEKAMQLGACDFLVKPLMLNRLDQALAR 133
Cdd:cd17536    67 IRELYPDIKIIILSGYDDFEYAQKAIRLGVVDYLLKPVDEEELEEALEK 115
REC_CheY cd17542
phosphoacceptor receiver (REC) domain of chemotaxis protein CheY; The chemotaxis response ...
 35-133 1.14e-15

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: 70.77  E-value: 1.14e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941938483  35 KQSLRQAQYQVVGIAGNLSTATALLHAIEPDLILLDIHLPDGNGLDLLTDLRRRTIKSEVMLLTAAKEVETLEKAMQLGA 114
Cdd:cd17542    17 KDILTKAGYEVVGEAANGEEAVEKYKELKPDLVTMDITMPEMDGIEALKEIKKIDPNAKVIMCSAMGQEEMVKEAIKAGA 96

                          90
                  ....*....|....*....
gi 1941938483 115 CDFLVKPLMLNRLDQALAR 133
Cdd:cd17542    97 KDFIVKPFQPERVLEAVEK 115
REC_OmpR cd17574
phosphoacceptor receiver (REC) domain of OmpR family response regulators; OmpR-like proteins ...
 38-121 2.59e-15

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: 68.97  E-value: 2.59e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941938483  38 LRQAQYQVVgIAGNLSTATALLHAIEPDLILLDIHLPDGNGLDLLTDLRRRTIKSEVMLLTAAKEVETLEKAMQLGACDF 117
Cdd:cd17574    17 LEKEGYEVD-TAADGEEALELAREEQPDLIILDVMLPGMDGFEVCRRLREKGSDIPIIMLTAKDEEEDKVLGLELGADDY 95


                  ....
gi 1941938483 118 LVKP 121
Cdd:cd17574    96 ITKP 99
REC_NarL-like cd17535
phosphoacceptor receiver (REC) domain of NarL (Nitrate/Nitrite response regulator L) family ...
 39-131 3.65e-15

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: 69.46  E-value: 3.65e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941938483  39 RQAQYQVVGIAGNLSTATALLHAIEPDLILLDIHLPDGNGLDLLTDLRRRTIKSEVMLLTAAKEVETLEKAMQLGACDFL 118
Cdd:cd17535    20 SEPDIEVVGEAADGEEALALLRELRPDVVLMDLSMPGMDGIEALRRLRRRYPDLKVIVLTAHDDPEYVLRALKAGAAGYL 99

                          90
                  ....*....|...
gi 1941938483 119 VKPLMLNRLDQAL 131
Cdd:cd17535   100 LKDSSPEELIEAI 112
REC_NtrX-like cd17550
phosphoacceptor receiver (REC) domain of nitrogen assimilation regulatory protein NtrX and ...
 43-133 6.96e-15

phosphoacceptor receiver (REC) domain of nitrogen assimilation regulatory protein NtrX and similar proteins; NtrX is part of the two-component regulatory system NtrY/NtrX that is involved in the activation of nitrogen assimilatory genes such as Gln. It is phosphorylated by the histidine kinase NtrY and interacts with sigma-54. NtrX is a member of the NtrC family, characterized by a domain architecture containing an N-terminal REC domain, followed by a central sigma-54 interaction/ATPase domain, and a C-terminal DNA binding domain. NtrC family response regulators are sigma54-dependent transcriptional activators. Also included in this subfamily is Aquifex aeolicus NtrC4. The ability of the central domain to hydrolyze ATP and thus to interact effectively with a complex of RNA polymerase, sigma54, and promoter, is controlled by the phosphorylation status of the REC domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381102 [Multi-domain]  Cd Length: 115  Bit Score: 68.68  E-value: 6.96e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941938483  43 YQVVgIAGNLSTATALLHAIEPDLILLDIHLPDGNGLDLLTDLRRRTIKSEVMLLTAAKEVETLEKAMQLGACDFLVKPL 122
Cdd:cd17550    23 YEVD-TAADGEEALKLIKERRPDLVLLDIWLPDMDGLELLKEIKEKYPDLPVIMISGHGTIETAVKATKLGAYDFIEKPL 101

                          90
                  ....*....|.
gi 1941938483 123 MLNRLDQALAR 133
Cdd:cd17550   102 SLDRLLLTIER 112
PRK10643 PRK10643
two-component system response regulator PmrA;
36-133 6.70e-14

two-component system response regulator PmrA;


Pssm-ID: 182612 [Multi-domain]  Cd Length: 222  Bit Score: 68.52  E-value: 6.70e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941938483  36 QSLRQAQYqVVGIAGNLSTATALLHAIEPDLILLDIHLPDGNGLDLLTDLRRRTIKSEVMLLTAAKEVETLEKAMQLGAC 115
Cdd:PRK10643   18 LALQTEGY-ACDCASTAREAEALLESGHYSLVVLDLGLPDEDGLHLLRRWRQKKYTLPVLILTARDTLEDRVAGLDVGAD 96

                          90
                  ....*....|....*...
gi 1941938483 116 DFLVKPLMLNRLdQALAR 133
Cdd:PRK10643   97 DYLVKPFALEEL-HARIR 113
FixJ COG4566
DNA-binding response regulator, FixJ family, consists of REC and HTH domains [Signal ...
 38-139 7.38e-14

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


Pssm-ID: 443623 [Multi-domain]  Cd Length: 196  Bit Score: 67.82  E-value: 7.38e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941938483  38 LRQAQYQVVGIAgnlsTATALLHAIEPDL---ILLDIHLPDGNGLDLLTDLRRRTIKSEVMLLTAAKEVETLEKAMQLGA 114
Cdd:COG4566    19 LESAGLRVETFA----SAEAFLAALDPDRpgcLLLDVRMPGMSGLELQEELAARGSPLPVIFLTGHGDVPMAVRAMKAGA 94

                          90       100
                  ....*....|....*....|....*....
gi 1941938483 115 CDFLVKPL----MLNRLDQALARFESRQQ 139
Cdd:COG4566    95 VDFLEKPFddqaLLDAVRRALARDRARRA 123
REC_OmpR_CusR-like cd19935
phosphoacceptor receiver (REC) domain of CusR-like OmpR family response regulators; ...
 35-121 8.29e-14

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: 65.15  E-value: 8.29e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941938483  35 KQSLRQAQYqVVGIAGNLSTATALLHAIEPDLILLDIHLPDGNGLDLLTDLRRRTIKSEVMLLTAAKEVETLEKAMQLGA 114
Cdd:cd19935    15 KKGLTEEGY-AVDVAYDGEDGLHLALTNEYDLIILDVMLPGLDGLEVLRRLRAAGKQTPVLMLTARDSVEDRVKGLDLGA 93


                  ....*..
gi 1941938483 115 CDFLVKP 121
Cdd:cd19935    94 DDYLVKP 100
REC_LytTR_AlgR-like cd17532
phosphoacceptor receiver (REC) domain of LytTR/AlgR family response regulators similar to AlgR; ...
 39-137 1.47e-13

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: 64.87  E-value: 1.47e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941938483  39 RQAQYQVVGIAGNLSTATALLHAIEPDLILLDIHLPDGNGLDLLTDLRRRTIKSEVMLLTAAKE--VetleKAMQLGACD 116
Cdd:cd17532    20 EHPDIEIVGEAENGEEALEAIEELKPDVVFLDIQMPGLDGLELAKKLSKLAKPPLIVFVTAYDEyaV----EAFELNAVD 95

                          90       100
                  ....*....|....*....|.
gi 1941938483 117 FLVKPLMLNRLDQALARFESR 137
Cdd:cd17532    96 YLLKPFSEERLAEALAKLRKR 116
REC_RpfG-like cd17551
phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase response regulator ...
 38-122 2.88e-13

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: 64.39  E-value: 2.88e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941938483  38 LRQAQYQVVGIAGNLSTATALLHAIEPDLILLDIHLPDGNGLDLLTDLRRRTIKSEV--MLLTAAKEVETLEKAMQLGAC 115
Cdd:cd17551    20 LRSAGYLEVVSFTDPREALAWCRENPPDLILLDYMMPGMDGLEFIRRLRALPGLEDVpiVMITADTDREVRLRALEAGAT 99


                  ....*..
gi 1941938483 116 DFLVKPL 122
Cdd:cd17551   100 DFLTKPF 106
REC_RegA-like cd17563
phosphoacceptor receiver (REC) domain of photosynthetic apparatus regulatory protein RegA; ...
 32-121 6.24e-13

phosphoacceptor receiver (REC) domain of photosynthetic apparatus regulatory protein RegA; Rhodobacter sphaeroides RegA, also called response regulator PrrA, is the DNA binding regulatory protein of a redox-responsive two-component regulatory system RegB/RegA that is involved in transactivating anaerobic expression of the photosynthetic apparatus. It contains a REC domain and a DNA-binding helix-turn-helix output domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381111 [Multi-domain]  Cd Length: 112  Bit Score: 63.23  E-value: 6.24e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941938483  32 QTPKQSLRQAQYQVVgIAGNLSTATALLHAIEPDLILLDIHLPDGNGLDLLTDLRRRTIKSEVMLLTA----AKEVEtle 107
Cdd:cd17563    14 ERLARALERRGFEVE-TAHSVEEALALAREEKPDYAVLDLRLGGDSGLDLIPPLRALQPDARIVVLTGyasiATAVE--- 89

                          90
                  ....*....|....
gi 1941938483 108 kAMQLGACDFLVKP 121
Cdd:cd17563    90 -AIKLGADDYLAKP 102
REC_typeB_ARR-like cd17584
phosphoacceptor receiver (REC) domain of type B Arabidopsis response regulators (ARRs) and ...
 35-127 1.16e-12

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: 62.65  E-value: 1.16e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941938483  35 KQSLRQAQYQVVgIAGNLSTATALL--HAIEPDLILLDIHLPDGNGLDLLTDLR-RRTIksEVMLLTAAKEVETLEKAMQ 111
Cdd:cd17584    15 KRMLLRCGYQVT-TCTDAEEALSMLreNKDEFDLVITDVHMPDMDGFEFLELIRlEMDL--PVIMMSADGSTSTVMKGLA 91

                          90
                  ....*....|....*.
gi 1941938483 112 LGACDFLVKPLMLNRL 127
Cdd:cd17584    92 HGACDYLLKPVSIEDL 107
PRK10651 PRK10651
transcriptional regulator NarL; Provisional
 35-176 3.49e-12

transcriptional regulator NarL; Provisional


Pssm-ID: 182619 [Multi-domain]  Cd Length: 216  Bit Score: 63.51  E-value: 3.49e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941938483  35 KQSLRQA-QYQVVGIAGNLSTATALLHAIEPDLILLDIHLPDGNGLDLLTDLRRRTIKSEVMLLTAAKEVETLEKAMQLG 113
Cdd:PRK10651   23 KQLISMApDITVVGEASNGEQGIELAESLDPDLILLDLNMPGMNGLETLDKLREKSLSGRIVVFSVSNHEEDVVTALKRG 102

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1941938483 114 ACDFLVKPLMLNRLDQALARFESRQQCFSDAseVTQSMVDTLFGSKQQTNifnrlpKGVDQLT 176
Cdd:PRK10651  103 ADGYLLKDMEPEDLLKALQQAAAGEMVLSEA--LTPVLAASLRANRATTE------RDVNQLT 157
REC_DC-like cd17534
phosphoacceptor receiver (REC) domain of modulated diguanylate cyclase and similar domains; ...
 4-121 4.53e-12

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: 60.88  E-value: 4.53e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941938483   4 SVVIIEDEVEVAQLLaqylllpngiagnqtpKQSLRQAQYQVVGIAGNLSTATALLHAIEPDLILLDIHLPDG-NGLDLL 82
Cdd:cd17534     2 KILIVEDEAIIALDL----------------KEILESLGYEVVGIADSGEEAIELAEENKPDLILMDINLKGDmDGIEAA 65

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1941938483  83 tdlrrRTIKSE----VMLLTAAKEVETLEKAMQLGACDFLVKP 121
Cdd:cd17534    66 -----REIREKfdipVIFLTAYSDEETLERAKETNPYGYLVKP 103
REC_DctD-like cd17549
phosphoacceptor receiver (REC) domain of C4-dicarboxylic acid transport protein D (DctD) and ...
 5-133 7.81e-12

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: 60.58  E-value: 7.81e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941938483   5 VVIIEDEVEVAQLLAqylllpngiagnqtpkQSLRQAQYQVVGIAGnlstATALLHAIEPD---LILLDIHLPDGNGLDL 81
Cdd:cd17549     1 VLLVDDDADVREALQ----------------QTLELAGFRVRAFAD----AEEALAALSPDfpgVVISDIRMPGMDGLEL 60

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1941938483  82 LTDLRRRTIKSEVMLLTAAKEVETLEKAMQLGACDFLVKPLMLNRLDQALAR 133
Cdd:cd17549    61 LAQIRELDPDLPVILITGHGDVPMAVEAMRAGAYDFLEKPFDPERLLDVVRR 112
REC_OmpR_PhoB cd17618
phosphoacceptor receiver (REC) domain of PhoB response regulator from the OmpR family; The ...
 5-121 7.87e-12

phosphoacceptor receiver (REC) domain of PhoB response regulator from the OmpR family; The transcription factor PhoB is a component of the PhoR/PhoB two-component system, a key regulatory protein network that facilitates response to inorganic phosphate (Pi) starvation conditions by turning on the phosphate (pho) regulon whose products are involved in phosphorus uptake and metabolism. PhoB is a member of the OmpR family of DNA-binding response regulators that contains REC and winged helix-turn-helix (wHTH) DNA-binding output effector domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381133 [Multi-domain]  Cd Length: 118  Bit Score: 60.34  E-value: 7.87e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941938483   5 VVIIEDEVEVAQLlaqylllpngIAGNqtpkqsLRQAQYQVVGiAGNLSTATALLHAIEPDLILLDIHLPDGNGLDLLTD 84
Cdd:cd17618     3 ILIVEDEPAIREM----------IAFN------LERAGFDVVE-AEDAESAVNLIVEPRPDLILLDWMLPGGSGIQFIRR 65

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1941938483  85 LRRRTIKSE--VMLLTAAKEVETLEKAMQLGACDFLVKP 121
Cdd:cd17618    66 LKRDEMTRDipIIMLTARGEEEDKVRGLEAGADDYITKP 104
REC_PA4781-like cd19920
phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase PA4781 and similar ...
 38-121 1.31e-11

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


Pssm-ID: 381147 [Multi-domain]  Cd Length: 103  Bit Score: 59.45  E-value: 1.31e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941938483  38 LRQAQYQVvGIAGNLSTATALLHAIEPDLILLDIHLPDGNGLDLLtdlrrRTIKSE-------VMLLTAAKEVETLEKAM 110
Cdd:cd19920    18 LRAAGYRV-LVATDGQQALQRAQAEPPDLILLDVMMPGMDGFEVC-----RRLKADpatrhipVIFLTALTDTEDKVKGF 91

                          90
                  ....*....|.
gi 1941938483 111 QLGACDFLVKP 121
Cdd:cd19920    92 ELGAVDYITKP 102
PRK11361 PRK11361
acetoacetate metabolism transcriptional regulator AtoC;
49-133 1.57e-11

acetoacetate metabolism transcriptional regulator AtoC;


Pssm-ID: 183099 [Multi-domain]  Cd Length: 457  Bit Score: 63.33  E-value: 1.57e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941938483  49 AGNLSTATALLHAIEPDLILLDIHLPDGNGLDLLTDLRRRTIKSEVMLLTAAKEVETLEKAMQLGACDFLVKPLMLNRLD 128
Cdd:PRK11361   34 ANNGRTALHLFADIHPDVVLMDIRMPEMDGIKALKEMRSHETRTPVILMTAYAEVETAVEALRCGAFDYVIKPFDLDELN 113


                  ....*
gi 1941938483 129 QALAR 133
Cdd:PRK11361  114 LIVQR 118
REC_OmpR_DrrD-like cd17625
phosphoacceptor receiver (REC) domain of DrrD-like OmpR family response regulators; DrrD is a ...
 31-136 1.88e-11

phosphoacceptor receiver (REC) domain of DrrD-like OmpR family response regulators; DrrD is a OmpR/PhoB homolog from Thermotoga maritima whose function is not yet known. This subfamily also includes Streptococcus agalactiae transcriptional regulatory protein DltR, part of the DltS/DltR two-component system (TCS), and Pseudomonas aeruginosa transcriptional activator protein PfeR, part of the PfeR/PfeS TCS, which activates expression of the ferric enterobactin receptor. The DltS/DltR TCS regulates the expression of the dlt operon, which comprises four genes (dltA, dltB, dltC, and dltD) that catalyze the incorporation of D-alanine residues into the lipoteichoic acids. Members of this subfamily belong to the OmpR/PhoB family, which comprises of two domains, an N-terminal receiver domain and a C-terminal DNA-binding winged helix-turn-helix effector domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381140 [Multi-domain]  Cd Length: 115  Bit Score: 59.16  E-value: 1.88e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941938483  31 NQTPKQSLRQAQYqVVGIAGNLSTATALLHAIEPDLILLDIHLPDGNGLDLLTDLRRRTIKSEVMLLTAAKEVETLEKAM 110
Cdd:cd17625    10 SEAITKHLKKEGY-TVDVCFDGEEGLEYALSGIYDLIILDIMLPGMDGLEVLKSLREEGIETPVLLLTALDAVEDRVKGL 88

                          90       100
                  ....*....|....*....|....*.
gi 1941938483 111 QLGACDFLVKPLMLNRLdqaLARFES 136
Cdd:cd17625    89 DLGADDYLPKPFSLAEL---LARIRA 111
REC_PdtaR-like cd19932
phosphoacceptor receiver (REC) domain of PdtaR and similar proteins; This subfamily includes ...
 35-133 3.21e-11

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: 58.96  E-value: 3.21e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941938483  35 KQSLRQAQYQVVGIAGNLSTATALLHAIEPDLILLDIHLPDGNGLDLLTDLRRRTIkSEVMLLTAAKEVETLEKAMQLGA 114
Cdd:cd19932    17 REMLEEAGYEVVGEASDGEEAVELAKKHKPDLVIMDVKMPRLDGIEAAKIITSENI-APIVLLTAYSQQDLVERAKEAGA 95

                          90       100
                  ....*....|....*....|...
gi 1941938483 115 CDFLVKPL----MLNRLDQALAR 133
Cdd:cd19932    96 MAYLVKPFsesdLIPAIEMAIAR 118
REC_Spo0A cd17561
phosphoacceptor receiver (REC) domain of Spo0A; Spo0A is a response regulator of the ...
 40-121 5.27e-11

phosphoacceptor receiver (REC) domain of Spo0A; Spo0A is a response regulator of the phosphorelay system in the early stage of spore formation. It may be an element of the effector pathway responsible for the activation of sporulation genes in response to nutritional stress and may act in the with sigma factor spo0H to control the expression of some genes that are critical to the sporulation process. Spo0A contains a regulatory N-terminal REC domain and a C-terminal DNA-binding transcription activation domain as its effector/output domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381109 [Multi-domain]  Cd Length: 108  Bit Score: 58.00  E-value: 5.27e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941938483  40 QAQYQVVGIAGNLSTATALLHAIEPDLILLDIHLPDGNGLDLLTDLRRRTIKSE--VMLLTAAKEVETLEKAMQLGACDF 117
Cdd:cd17561    24 QPDMEVVGVAHNGQEALELIEEKEPDVLLLDIIMPHLDGIGVLEKLRRMRLEKRpkIIMLTAFGQEDITQRAVELGASYY 103


                  ....
gi 1941938483 118 LVKP 121
Cdd:cd17561   104 ILKP 107
REC_Rcp-like cd17557
phosphoacceptor receiver (REC) domain of cyanobacterial phytochrome response regulator Rcp and ...
 64-136 5.68e-11

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: 58.20  E-value: 5.68e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1941938483  64 PDLILLDIHLPDGNGLDLLTDLRR----RTIksEVMLLTAAKEVETLEKAMQLGACDFLVKPLMLNRLDQALARFES 136
Cdd:cd17557    53 PDLILLDLNMPRMDGFEVLREIKAdpdlRRI--PVVVLTTSDAEEDIERAYELGANSYIVKPVDFEEFVEAIRSLGE 127
REC_RssB-like cd17555
phosphoacceptor receiver (REC) domain of Pseudomonas aeruginosa RssB and similar domains; ...
 43-133 7.41e-11

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


Pssm-ID: 381107 [Multi-domain]  Cd Length: 116  Bit Score: 57.60  E-value: 7.41e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941938483  43 YQVVGiAGNLSTATALLHAIEPDLILLDIHLPDGNGLDLLTDLRRRTIKSEVMLLTAAKEVETLEKAMQLGACDFLVKPL 122
Cdd:cd17555    25 FQVLQ-AADGRQGLELFRSEQPDLVLCDLRMPEMDGLEVLKQITKESPDTPVIVVSGAGVMSDAVEALRLGAWDYLTKPI 103

                          90
                  ....*....|..
gi 1941938483 123 M-LNRLDQALAR 133
Cdd:cd17555   104 EdLAVLEHAVRR 115
PRK10693 PRK10693
two-component system response regulator RssB;
49-137 8.52e-11

two-component system response regulator RssB;


Pssm-ID: 182652 [Multi-domain]  Cd Length: 303  Bit Score: 60.77  E-value: 8.52e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941938483  49 AGNLSTATALLHAIEPDLILLDIHLPDGNGLDLLTDLRRRTIKSEVMLLTAAKEVETLEKAMQLGACDFLVKPLM-LNRL 127
Cdd:PRK10693    3 AANGVDALELLGGFTPDLIICDLAMPRMNGIEFVEHLRNRGDQTPVLVISATENMADIAKALRLGVQDVLLKPVKdLNRL 82

                          90
                  ....*....|....*.
gi 1941938483 128 DQAL------ARFESR 137
Cdd:PRK10693   83 REMVfaclypSMFNSR 98
PRK09836 PRK09836
DNA-binding transcriptional activator CusR; Provisional
 45-133 2.81e-10

DNA-binding transcriptional activator CusR; Provisional


Pssm-ID: 182102 [Multi-domain]  Cd Length: 227  Bit Score: 58.40  E-value: 2.81e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941938483  45 VVGIAGNLSTATALLHAIEPDLILLDIHLPDGNGLDLLTDLRRRTIKSEVMLLTAAKEVETLEKAMQLGACDFLVKPLML 124
Cdd:PRK09836   26 VVDLADNGLNGYHLAMTGDYDLIILDIMLPDVNGWDIVRMLRSANKGMPILLLTALGTIEHRVKGLELGADDYLVKPFAF 105


                  ....*....
gi 1941938483 125 NRLdqaLAR 133
Cdd:PRK09836  106 AEL---LAR 111
PRK10529 PRK10529
DNA-binding transcriptional activator KdpE; Provisional
 63-139 3.39e-10

DNA-binding transcriptional activator KdpE; Provisional


Pssm-ID: 182522 [Multi-domain]  Cd Length: 225  Bit Score: 58.28  E-value: 3.39e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941938483  63 EPDLILLDIHLPDGNGLDLLTDLRRRTiKSEVMLLTAAKEVETLEKAMQLGACDFLVKPL----MLNRLDQALARFESRQ 138
Cdd:PRK10529   45 KPDLIILDLGLPDGDGIEFIRDLRQWS-AIPVIVLSARSEESDKIAALDAGADDYLSKPFgigeLQARLRVALRRHSATP 123


                  .
gi 1941938483 139 Q 139
Cdd:PRK10529  124 A 124
REC_CheB-like cd17541
phosphoacceptor receiver (REC) domain of chemotaxis response regulator protein-glutamate ...
 44-128 4.03e-10

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


Pssm-ID: 381096 [Multi-domain]  Cd Length: 125  Bit Score: 55.86  E-value: 4.03e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941938483  44 QVVGIAGNLSTATALLHAIEPDLILLDIHLPDGNGLDLLtdlrrRTIKSE-----VML--LTaAKEVETLEKAMQLGACD 116
Cdd:cd17541    27 EVVGTARDGEEALEKIKELKPDVITLDIEMPVMDGLEAL-----RRIMAErptpvVMVssLT-EEGAEITLEALELGAVD 100

                          90
                  ....*....|..
gi 1941938483 117 FLVKPLMLNRLD 128
Cdd:cd17541   101 FIAKPSGGISLD 112
REC_FixJ cd17537
phosphoacceptor receiver (REC) domain of FixJ family response regulators; FixJ family response ...
 38-131 1.15e-09

phosphoacceptor receiver (REC) domain of FixJ family response regulators; FixJ family response regulators contain an N-terminal receiver domain (REC) and a C-terminal LuxR family helix-turn-helix (HTH) DNA-binding output domain. The Sinorhizobium meliloti two-component system FixL/FixJ regulates nitrogen fixation in response to oxygen during symbiosis. Under microaerobic conditions, the kinase FixL phosphorylates the response regulator FixJ resulting in the regulation of nitrogen fixation genes such as nifA and fixK. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381092 [Multi-domain]  Cd Length: 116  Bit Score: 54.52  E-value: 1.15e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941938483  38 LRQAQYQVVGiagnLSTATALLHAIEPDL---ILLDIHLPDGNGLDLLTDLRRRTIKSEVMLLTAAKEVETLEKAMQLGA 114
Cdd:cd17537    20 LRSVGLAVKT----FTSASAFLAAAPPDQpgcLVLDVRMPGMSGLELQDELLARGSNIPIIFITGHGDVPMAVEAMKAGA 95

                          90       100
                  ....*....|....*....|.
gi 1941938483 115 CDFLVKP----LMLNRLDQAL 131
Cdd:cd17537    96 VDFLEKPfrdqVLLDAIEQAL 116
REC_OmpR_PrrA-like cd17627
phosphoacceptor receiver (REC) domain of PrrA-like OmpR family response regulators; The ...
 35-133 1.51e-09

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: 54.31  E-value: 1.51e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941938483  35 KQSLRQAQYQVVGIAGNLStATALLHAIEPDLILLDIHLPDGNGLDLLTDLRRRTIKSEVMLLTAAKEVETLEKAMQLGA 114
Cdd:cd17627    15 RRSLRFEGYEVETAVDGAE-ALRVISGNRPDAVVLDVMMPRLDGLEVCRRLRAAGNDLPILVLTARDSVSDRVAGLDAGA 93

                          90
                  ....*....|....*....
gi 1941938483 115 CDFLVKPLMLNRLdqaLAR 133
Cdd:cd17627    94 DDYLVKPFALEEL---LAR 109
REC_OmpR_MtPhoP-like cd17615
phosphoacceptor receiver (REC) domain of MtPhoP-like OmpR family response regulators; ...
 37-127 1.84e-09

phosphoacceptor receiver (REC) domain of MtPhoP-like OmpR family response regulators; Mycobacterium tuberculosis PhoP (MtPhoP) is part of the PhoP/PhoR two-component system that is involved in phosphate control by stimulating expression of genes involved in scavenging, transport and mobilization of phosphate, and repressing the utilization of nitrogen sources. Also included in this subfamily is Mycobacterium tuberculosis transcriptional regulatory protein TcrX, part of the two-component regulatory system TcrY/TcrX that may be involved in virulence. 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: 381131 [Multi-domain]  Cd Length: 118  Bit Score: 53.90  E-value: 1.84e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941938483  37 SLRQAQYQVVgIAGNLSTATALLHAIEPDLILLDIHLPDGNGLDLLTDLRRRTIKSEVMLLTAAKEVETLEKAMQLGACD 116
Cdd:cd17615    18 ALRYEGWDVE-TAADGAEALAAAREFRPDAVVLDIMLPDMDGLEVLRRLRADGPDVPVLFLTAKDSVEDRIAGLTAGGDD 96

                          90
                  ....*....|.
gi 1941938483 117 FLVKPLMLNRL 127
Cdd:cd17615    97 YVTKPFSLEEV 107
spore_0_A TIGR02875
sporulation transcription factor Spo0A; Spo0A, the stage 0 sporulation protein A, is a ...
 40-127 2.67e-09

sporulation transcription factor Spo0A; Spo0A, the stage 0 sporulation protein A, is a transcription factor critical for the initiation of sporulation. It contains a response regulator receiver domain (pfam00072). In Bacillus subtilis, it works together with response regulator Spo0F and the phosphotransferase Spo0B, both of which are missing from at least some sporulating species and thus not part of the endospore forming bacteria minimal gene set. Spo0A, however, is universal among endospore-forming species. [Cellular processes, Sporulation and germination]


Pssm-ID: 131922 [Multi-domain]  Cd Length: 262  Bit Score: 55.95  E-value: 2.67e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941938483  40 QAQYQVVGIAGNLSTATALLHAIEPDLILLDIHLPDGNGLDLLTDLRR--RTIKSEVMLLTAAKEVETLEKAMQLGACDF 117
Cdd:TIGR02875  25 QPDMEVVGVAHNGVDALELIKEQQPDVVVLDIIMPHLDGIGVLEKLNEieLSARPRVIMLSAFGQEKITQRAVALGADYY 104

                          90
                  ....*....|
gi 1941938483 118 LVKPLMLNRL 127
Cdd:TIGR02875 105 VLKPFDLEIL 114
REC_hyHK_CKI1_RcsC-like cd17546
phosphoacceptor receiver (REC) domain of hybrid sensor histidine kinases/response regulators ...
 38-131 3.49e-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: 52.86  E-value: 3.49e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941938483  38 LRQAQYQVVgIAGNLSTATALLHAIEPDLILLDIHLPDGNGLDLLTDLRRR-TIKSEVML--LTAAKEVETLEKAMQLGA 114
Cdd:cd17546    18 LEKLGYEVD-VAENGQEALELLKEEPFDLVLMDLQMPVMDGLEATRRIRELeGGGRRTPIiaLTANALEEDREKCLEAGM 96

                          90
                  ....*....|....*..
gi 1941938483 115 CDFLVKPLMLNRLDQAL 131
Cdd:cd17546    97 DDYLSKPVKLDQLKEVL 113
REC_HP-RR-like cd17573
phosphoacceptor receiver (REC) domain of orphan response regulator HP-RR and similar proteins; ...
 5-133 3.89e-09

phosphoacceptor receiver (REC) domain of orphan response regulator HP-RR and similar proteins; Helicobacter pylori response regulator hp1043 (HP-RR) is an orphan response regulator which is phosphorylation-independent and is essential for growth. HP-RR functions as a cell growth-associated regulator in the absence of post-translational modification. Members of this subfamily contain REC and DNA-binding output domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381115 [Multi-domain]  Cd Length: 110  Bit Score: 52.82  E-value: 3.89e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941938483   5 VVIIEDEVEVaqllaqylllpngiagNQTPKQSLRQAQYQVvGIAGNLSTATALLHAIEPDLILLDIHLPDGNGLDLLTD 84
Cdd:cd17573     1 ILLIEDDSTL----------------GKEISKGLNEKGYQA-DVAESLKDGEYYIDIRNYDLVLVSDKLPDGNGLSIVSR 63

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1941938483  85 LRRRTIKSEVMLLTAAKEVETLEKAMQLGACDFLVKPLMLNRLdqaLAR 133
Cdd:cd17573    64 IKEKHPSIVVIVLSDNPKTEQEIEAFKEGADDYIAKPFDFKVL---VAR 109
REC_NarL cd19931
phosphoacceptor receiver (REC) domain of Nitrate/Nitrite response regulator L (NarL); Nitrate ...
 35-132 4.16e-09

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


Pssm-ID: 381158 [Multi-domain]  Cd Length: 117  Bit Score: 53.12  E-value: 4.16e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941938483  35 KQSLRQA-QYQVVGIAGNLSTATALLHAIEPDLILLDIHLPDGNGLDLLTDLRRRTIKSEVMLLTAAKEVETLEKAMQLG 113
Cdd:cd19931    15 KQLIELDpDFTVVGEASSGEEGIELAERLDPDLILLDLNMKGMSGLDTLKALREEGVSARIVILTVSDAEDDVVTALRAG 94

                          90       100
                  ....*....|....*....|...
gi 1941938483 114 ACDFLVK----PLMLNRLDQALA 132
Cdd:cd19931    95 ADGYLLKdmepEDLLEALKQAAS 117
PRK15479 PRK15479
transcriptional regulator TctD;
45-133 5.77e-09

transcriptional regulator TctD;


Pssm-ID: 185376 [Multi-domain]  Cd Length: 221  Bit Score: 54.73  E-value: 5.77e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941938483  45 VVGIAGNLSTATALLHAIEPDLILLDIHLPDGNGLDLLTDLRRRTIKSEVMLLTAAKEVETLEKAMQLGACDFLVKPLML 124
Cdd:PRK15479   26 AVDCVFDGLAADHLLQSEMYALAVLDINMPGMDGLEVLQRLRKRGQTLPVLLLTARSAVADRVKGLNVGADDYLPKPFEL 105

                          90
                  ....*....|..
gi 1941938483 125 NRLD---QALAR 133
Cdd:PRK15479  106 EELDarlRALLR 117
REC_RcNtrC-like cd19928
phosphoacceptor receiver (REC) domain of Rhodobacter capsulatus nitrogen regulatory protein C ...
 36-121 8.35e-09

phosphoacceptor receiver (REC) domain of Rhodobacter capsulatus nitrogen regulatory protein C (NtrC) and similar NtrC family response regulators; NtrC family proteins are transcriptional regulators that have REC, AAA+ ATPase/sigma-54 interaction, and DNA-binding output domains. This subfamily of NtrC proteins include NtrC, also called nitrogen regulator I (NRI), from Rhodobacter capsulatus, Azospirillum brasilense, and Azorhizobium caulinodans. NtrC is part of the NtrB/NtrC two-component system that controls the expression of the nitrogen-regulated (ntr) genes in response to nitrogen limitation. The N-terminal REC domain of NtrC proteins regulate the activity of the protein and its phosphorylation controls the AAA+ domain oligomerization, while the central AAA+ domain participates in nucleotide binding, hydrolysis, oligomerization, and sigma54 interaction. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381155 [Multi-domain]  Cd Length: 100  Bit Score: 51.74  E-value: 8.35e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941938483  36 QSLRQAQYQVVGiAGNLSTATALLHAIEPDLILLDIHLPDGNGLDLLTDLRRRTIKSEVMLLTAAKEVETLEKAMQLGAC 115
Cdd:cd19928    16 QALGRAGYEVRT-TGNAATLWRWVEEGEGDLVITDVVMPDENGLDLIPRIKKARPDLPIIVMSAQNTLMTAVKAAERGAF 94


                  ....*.
gi 1941938483 116 DFLVKP 121
Cdd:cd19928    95 EYLPKP 100
REC_PatA-like cd17602
phosphoacceptor receiver (REC) domain of PatA and similar domains; Nostoc sp. (or Anabaena sp.) ...
 32-121 9.99e-09

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: 51.60  E-value: 9.99e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941938483  32 QTPKQSLRQAQYQVVGIAGNLSTATALLHAiEPDLILLDIHLPDGNGLDLLTDLRRRTIKSE--VMLLTAAKEVETLEKA 109
Cdd:cd17602    12 KMIEYFLEKQGFRVVVIDDPLRALTTLLNS-KPDLILIDIDMPDLDGYELCSLLRKSSALKDtpIIMLTGKDGLVDRIRA 90

                          90
                  ....*....|..
gi 1941938483 110 MQLGACDFLVKP 121
Cdd:cd17602    91 KMAGASGYLTKP 102
REC_OmpR_KdpE-like cd17620
phosphoacceptor receiver (REC) domain of KdpE-like OmpR family response regulators; KdpE is a ...
 37-121 1.24e-08

phosphoacceptor receiver (REC) domain of KdpE-like OmpR family response regulators; KdpE is a component of the KdpD/KdpE two-component system (TCS) and is activated when histidine kinase KdpD senses a drop in external K+ concentration or upshift in ionic osmolarity, resulting in the expression of a heterooligomeric transporter KdpFABC. In addition, the KdpD/KdpE TCS is also an adaptive regulator involved in the virulence and intracellular survival of pathogenic bacteria. KdpE is a member of the OmpR family of DNA-binding response regulators that contain REC and winged helix-turn-helix (wHTH) DNA-binding output effector domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381135 [Multi-domain]  Cd Length: 99  Bit Score: 51.01  E-value: 1.24e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941938483  37 SLRQAQYQVVgIAGNLSTATALLHAIEPDLILLDIHLPDGNGLDLLTDLRRRTiKSEVMLLTAAKEVETLEKAMQLGACD 116
Cdd:cd17620    17 ALEAHGYRVF-EAETGQEGLLEAATRKPDLIILDLGLPDMDGLEVIRRLREWS-AVPVIVLSARDEESDKIAALDAGADD 94


                  ....*
gi 1941938483 117 FLVKP 121
Cdd:cd17620    95 YLTKP 99
REC_OmpR_CtrA cd17616
phosphoacceptor receiver (REC) domain of CtrA-like OmpR family response regulators; CtrA is ...
 65-121 1.29e-08

phosphoacceptor receiver (REC) domain of CtrA-like OmpR family response regulators; CtrA is part of the CckA-ChpT-CtrA phosphorelay that is conserved in alphaproteobacteria and is important in orchestrating the cell cycle, polar development, and flagellar biogenesis. CtrA is the master regulator of flagella synthesis genes and also regulates genes involved in the cell cycle, exopolysaccharide synthesis, and cyclic-di-GMP signaling. CtrA is active as a transcription factor when phosphorylated. It is a member of the OmpR family of DNA-binding response regulators, characterized by a REC domain and a winged helix-turn-helix (wHTH) DNA-binding output effector domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381132 [Multi-domain]  Cd Length: 114  Bit Score: 51.64  E-value: 1.29e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1941938483  65 DLILLDIHLPDGNGLDLLTDLRRRTIKSEVMLLTAAKEVETLEKAMQLGACDFLVKP 121
Cdd:cd17616    44 DIILLDLNLPDMSGYEVLRTLRLAKVKTPILILSGLADIEDKVKGLGFGADDYMTKP 100
REC_PilR cd19926
phosphoacceptor receiver (REC) domain of type 4 fimbriae expression regulatory protein PilR ...
 49-121 1.38e-08

phosphoacceptor receiver (REC) domain of type 4 fimbriae expression regulatory protein PilR and similar proteins; Pseudomonas aeruginosa PilR is the response regulator of the PilS/PilR two-component regulatory system (PilSR TCS) that acts in conjunction with sigma-54 to regulate the expression of type 4 pilus (T4P) major subunit PilA. In addition, the PilSR TCS regulates flagellum-dependent swimming motility and pilus-dependent twitching motility. PilR contains an N-terminal REC domain, a central sigma-54 interaction domain, and a C-terminal Fis-type helix-turn-helix DNA-binding domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381153 [Multi-domain]  Cd Length: 100  Bit Score: 51.00  E-value: 1.38e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1941938483  49 AGNLSTATALLHAIEPDLILLDIHLPDGNGLDLLTDLRRRTIKSEVMLLTAAKEVETLEKAMQLGACDFLVKP 121
Cdd:cd19926    28 ARNVKEARELLASEPYDLCLTDMRLPDGSGLELVQHIQQRLPQTPVAVITAYGSLDTAIEALKAGAFDFLTKP 100
REC_DesR-like cd19930
phosphoacceptor receiver (REC) domain of DesR and similar proteins; This group is composed of ...
 44-120 1.52e-08

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: 51.50  E-value: 1.52e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1941938483  44 QVVGIAGNLSTATALLHAIEPDLILLDIHLPDGNGLDLLTDLRRRTIKSEVMLLTAAKEVETLEKAMQLGACDFLVK 120
Cdd:cd19930    25 EVVAQASNGQEALRLVLKHSPDVAILDIEMPGRTGLEVAAELREELPDTKVLIVTTFGRPGYFRRALAAGVDGYVLK 101
REC_OmpR_CpxR cd17623
phosphoacceptor receiver (REC) domain of CpxR-like OmpR family response regulators; CpxR is ...
 55-121 1.66e-08

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: 51.15  E-value: 1.66e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1941938483  55 ATALLHAIEPDLILLDIHLPDGNGLDLLTDLRRRTiKSEVMLLTAAKEVETLEKAMQLGACDFLVKP 121
Cdd:cd17623    34 GLAALLEGSPDLVVLDVMLPKMNGLDVLKELRKTS-QVPVLMLTARGDDIDRILGLELGADDYLPKP 99
REC_OmpR_BaeR-like cd19938
phosphoacceptor receiver (REC) domain of BaeR-like OmpR family response regulators; BaeR is ...
 38-121 1.87e-08

phosphoacceptor receiver (REC) domain of BaeR-like OmpR family response regulators; BaeR is part of the BaeSR two-component system that is involved in regulating genes that confer multidrug and metal resistance. In Salmonella, BaeSR induces AcrD and MdtABC drug efflux systems, increasing multidrug and metal resistance. In Escherichia coli, BaeR stimulates multidrug resistance via mdtABC (multidrug transporter ABC, formerly known as yegMNO) genes, which encode a resistance-nodulation-cell division (RND) drug efflux system. 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: 381165 [Multi-domain]  Cd Length: 114  Bit Score: 51.22  E-value: 1.87e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941938483  38 LRQAQYQVVGIAGNLSTATALLHAiEPDLILLDIHLPDGNGLDLLTDLRRrtiKSEVMLLTAAKEVETLEK--AMQLGAC 115
Cdd:cd19938    19 LRAAGYAPTLLAHGDQVLPYVRHT-PPDLILLDLMLPGTDGLTLCREIRR---FSDVPIIMVTARVEEIDRllGLELGAD 94


                  ....*.
gi 1941938483 116 DFLVKP 121
Cdd:cd19938    95 DYICKP 100
REC_OmpR_BsPhoP-like cd19937
phosphoacceptor receiver (REC) domain of BsPhoP-like OmpR family response regulators; Bacillus ...
 38-121 3.56e-08

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


Pssm-ID: 381164 [Multi-domain]  Cd Length: 116  Bit Score: 50.35  E-value: 3.56e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941938483  38 LRQAQYQVVgIAGNLSTATALLHAIEPDLILLDIHLPDGNGLDLLTDLRRRTIKSE--VMLLTAAKE----VETLEkamq 111
Cdd:cd19937    17 LEKEGYEVV-TAYDGEEALKRAKDEKPDLIILDLMLPGIDGLEVCRILRSDPKTSSipIIMLTAKGEefdkVLGLE---- 91

                          90
                  ....*....|
gi 1941938483 112 LGACDFLVKP 121
Cdd:cd19937    92 LGADDYITKP 101
REC_D1_PleD-like cd17538
first (D1) phosphoacceptor receiver (REC) domain of response regulator PleD and similar ...
 43-121 4.99e-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: 4.99e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941938483  43 YQVVgIAGNLSTATALLHAIEPDLILLDIHLPDGNGLDLLtdlrrRTIKSE-------VMLLTAAKEVETLEKAMQLGAC 115
Cdd:cd17538    24 YEVL-TADSGQEALALAEEELPDLILLDVMMPGMDGFEVC-----RRLKEDpetrhipVIMITALDDREDRIRGLEAGAD 97


                  ....*.
gi 1941938483 116 DFLVKP 121
Cdd:cd17538    98 DFLSKP 103
PRK10403 PRK10403
nitrate/nitrite response regulator protein NarP;
35-120 5.08e-08

nitrate/nitrite response regulator protein NarP;


Pssm-ID: 182431 [Multi-domain]  Cd Length: 215  Bit Score: 51.78  E-value: 5.08e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941938483  35 KQSLRQ-----AQYQVVGIAGNLSTATALLHAIEPDLILLDIHLPDGNGLDLLTDLRRRTIKSEVMLLTAAKEVETLEKA 109
Cdd:PRK10403   19 RRGVRQlleldPGFEVVAEAGDGASAIDLANRLDPDVILLDLNMKGMSGLDTLNALRRDGVTAQIIILTVSDASSDVFAL 98

                          90
                  ....*....|.
gi 1941938483 110 MQLGACDFLVK 120
Cdd:PRK10403   99 IDAGADGYLLK 109
PRK13435 PRK13435
response regulator; Provisional
 37-138 6.45e-08

response regulator; Provisional


Pssm-ID: 184052 [Multi-domain]  Cd Length: 145  Bit Score: 50.44  E-value: 6.45e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941938483  37 SLRQAQYQVVGIAGNLSTATALLHAIEPDLILLDIHLPDG-NGldllTDLRRRTIKS---EVMLLTA-AKEVETLEKamq 111
Cdd:PRK13435   24 LVEEAGHEVVGIAMSSEQAIALGRRRQPDVALVDVHLADGpTG----VEVARRLSADggvEVVFMTGnPERVPHDFA--- 96

                          90       100
                  ....*....|....*....|....*..
gi 1941938483 112 lGACDFLVKPLMLNRLDQALARFESRQ 138
Cdd:PRK13435   97 -GALGVIAKPYSPRGVARALSYLSARR 122
PRK00742 PRK00742
chemotaxis-specific protein-glutamate methyltransferase CheB;
39-121 6.89e-08

chemotaxis-specific protein-glutamate methyltransferase CheB;


Pssm-ID: 234828 [Multi-domain]  Cd Length: 354  Bit Score: 52.07  E-value: 6.89e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941938483  39 RQAQYQVVGIAGNLSTATALLHAIEPDLILLDIHLPDGNGLDLLTDL--RRRTIKseVML--LTAAKEVETLEkAMQLGA 114
Cdd:PRK00742   25 SDPDIEVVGTAPDGLEAREKIKKLNPDVITLDVEMPVMDGLDALEKImrLRPTPV--VMVssLTERGAEITLR-ALELGA 101


                  ....*..
gi 1941938483 115 CDFLVKP 121
Cdd:PRK00742  102 VDFVTKP 108
REC_NtrC cd19919
phosphoacceptor receiver (REC) domain of DNA-binding transcriptional regulator NtrC; ...
 38-132 8.50e-08

phosphoacceptor receiver (REC) domain of DNA-binding transcriptional regulator NtrC; DNA-binding transcriptional regulator NtrC is also called nitrogen regulation protein NR(I) or nitrogen regulator I (NRI). It contains an N-terminal receiver (REC) domain, followed by a sigma-54 interaction domain, and a C-terminal helix-turn-helix DNA-binding domain. It is part of the two-component regulatory system NtrB/NtrC, which controls expression of the nitrogen-regulated (ntr) genes in response to nitrogen limitation. DNA-binding response regulator NtrC is phosphorylated by NtrB; phosphorylation of the N-terminal REC domain activates the central sigma-54 interaction domain and leads to the transcriptional activation from promoters that require sigma(54)-containing RNA polymerase. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381146 [Multi-domain]  Cd Length: 116  Bit Score: 49.19  E-value: 8.50e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941938483  38 LRQAQYQVVGIAGNLSTATALLHAiEPDLILLDIHLPDGNGLDLLTDLRRRTIKSEVMLLTAAKEVETLEKAMQLGACDF 117
Cdd:cd19919    20 LAGAGLTVTSFENAQEALAALASS-QPDVLISDIRMPGMDGLALLAQIKQRHPDLPVIIMTAHSDLDSAVSAYQGGAFEY 98

                          90
                  ....*....|....*
gi 1941938483 118 LVKPLmlnRLDQALA 132
Cdd:cd19919    99 LPKPF---DIDEAVA 110
PRK10365 PRK10365
sigma-54-dependent response regulator transcription factor ZraR;
65-150 1.08e-07

sigma-54-dependent response regulator transcription factor ZraR;


Pssm-ID: 182412 [Multi-domain]  Cd Length: 441  Bit Score: 51.96  E-value: 1.08e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941938483  65 DLILLDIHLPDGNGLDLLTDLRRRTIKSEVMLLTAAKEVETLEKAMQLGACDFLVKPLMLNRLDQALAR-FESRQQCFSD 143
Cdd:PRK10365   51 DLVLCDVRMAEMDGIATLKEIKALNPAIPVLIMTAYSSVETAVEALKTGALDYLIKPLDFDNLQATLEKaLAHTHSIDAE 130


                  ....*..
gi 1941938483 144 ASEVTQS 150
Cdd:PRK10365  131 TPAVTAS 137
PRK11091 PRK11091
aerobic respiration control sensor protein ArcB; Provisional
 65-154 1.09e-07

aerobic respiration control sensor protein ArcB; Provisional


Pssm-ID: 236842 [Multi-domain]  Cd Length: 779  Bit Score: 51.87  E-value: 1.09e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941938483  65 DLILLDIHLPDGNGLDLLTDLRRRTIKSE---VMLLTA---AKEVETLEKAMQlgacDFLVKPLMLNRLDQALARFESRQ 138
Cdd:PRK11091  571 DLVLLDIQLPDMTGLDIARELRERYPREDlppLVALTAnvlKDKKEYLDAGMD----DVLSKPLSVPALTAMIKKFWDTQ 646

                          90
                  ....*....|....*.
gi 1941938483 139 QcfsDASEVTQSMVDT 154
Cdd:PRK11091  647 D---DEESTVTTEESS 659
REC_OmpR_NsrR-like cd18159
phosphoacceptor receiver (REC) domain of Streptococcus agalactiae NsrR-like OmpR family ...
 35-121 1.22e-07

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


Pssm-ID: 381143 [Multi-domain]  Cd Length: 113  Bit Score: 48.82  E-value: 1.22e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941938483  35 KQSLRQAQYQVVGIAgNLSTATALLHAIEPDLILLDIHLPDGNGLDLLTDLRRRTiKSEVMLLTAAKEVETLEKAMQLGA 114
Cdd:cd18159    15 KKHLEKWGYEVVLIE-DFEDVLEEFLQFKPDLVLLDINLPYFDGFYWCREIRQIS-NVPIIFISSRDDNMDQVMAINMGG 92


                  ....*..
gi 1941938483 115 CDFLVKP 121
Cdd:cd18159    93 DDYITKP 99
CitB COG2197
DNA-binding response regulator, NarL/FixJ family, contains REC and HTH domains [Signal ...
 39-85 1.46e-07

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: 49.12  E-value: 1.46e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1941938483  39 RQAQYQVVGIAGNLSTATALLHAIEPDLILLDIHLPDGNGLDLLTDL 85
Cdd:COG2197    23 AEPDIEVVGEAADGEEALELLEELRPDVVLLDIRMPGMDGLEALRRL 69
PRK10161 PRK10161
phosphate response regulator transcription factor PhoB;
38-122 1.49e-07

phosphate response regulator transcription factor PhoB;


Pssm-ID: 182277 [Multi-domain]  Cd Length: 229  Bit Score: 50.49  E-value: 1.49e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941938483  38 LRQAQYQVVGiAGNLSTATALLHAIEPDLILLDIHLPDGNGLDLLTDLRRRTIKSE--VMLLTAAKEVETLEKAMQLGAC 115
Cdd:PRK10161   22 LEQNGFQPVE-AEDYDSAVNQLNEPWPDLILLDWMLPGGSGIQFIKHLKRESMTRDipVVMLTARGEEEDRVRGLETGAD 100


                  ....*..
gi 1941938483 116 DFLVKPL 122
Cdd:PRK10161  101 DYITKPF 107
REC_OmpR_EcPhoP-like cd19934
phosphoacceptor receiver (REC) domain of EcPhoP-like OmpR family response regulators; ...
 35-133 1.71e-07

phosphoacceptor receiver (REC) domain of EcPhoP-like OmpR family response regulators; Escherichia coli PhoP (EcPhoP) is part of the PhoQ/PhoP two-component system (TCS) that regulates virulence genes and plays an essential role in the response of the bacteria to the environment of their mammalian hosts, sensing several stimuli such as extracellular magnesium limitation, low pH, the presence of cationic antimicrobial peptides, and osmotic upshift. This subfamily also includes Brucella suis FeuP, part of the FeuPQ TCS that is involved in the regulation of iron uptake, and Microchaete diplosiphon RcaC, which is required for chromatic adaptation. Members of this subfamily belong to the OmpR family of DNA-binding response regulators, which contain N-terminal receiver (REC) and C-terminal DNA-binding winged helix-turn-helix effector domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381161 [Multi-domain]  Cd Length: 117  Bit Score: 48.43  E-value: 1.71e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941938483  35 KQSLRQAQYqVVGIAGNLSTATALLHAIEPDLILLDIHLPDGNGLDLLTDLRRRTIKSEVMLLTA-AKEVETLEkAMQLG 113
Cdd:cd19934    15 KEQLSDAGY-VVDVAEDGEEALFQGEEEPYDLVVLDLGLPGMDGLSVLRRWRSEGRATPVLILTArDSWQDKVE-GLDAG 92

                          90       100
                  ....*....|....*....|....
gi 1941938483 114 ACDFLVKPL----MLNRLdQALAR 133
Cdd:cd19934    93 ADDYLTKPFhieeLLARL-RALIR 115
REC_OmpR_ArcA_TorR-like cd17619
phosphoacceptor receiver (REC) domain of ArcA- and TorR-like OmpR family response regulators; ...
 3-127 2.06e-07

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: 48.15  E-value: 2.06e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941938483   3 YSVVIIEDEVevaqllaqylllpngiAGNQTPKQSLRQAQYQVVgIAGNLSTATALLHAIEPDLILLDIHLPDGNGLDLL 82
Cdd:cd17619     1 PHILIVEDEP----------------VTRATLKSYFEQEGYDVS-EAGDGEEMRQILARQDIDLVLLDINLPGKDGLSLT 63

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1941938483  83 TDLRRRtikSEVMLLTAAKEVETLEK--AMQLGACDFLVKPLMLNRL 127
Cdd:cd17619    64 RELREQ---SEVGIILVTGRDDEVDRivGLEIGADDYVTKPFNPREL 107
fixJ PRK09390
response regulator FixJ; Provisional
 55-149 2.88e-07

response regulator FixJ; Provisional


Pssm-ID: 181815 [Multi-domain]  Cd Length: 202  Bit Score: 49.23  E-value: 2.88e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941938483  55 ATALLHA---IEPDLILLDIHLPDGNGLDLLTDLRRRTIKSEVMLLTAAKEVETLEKAMQLGACDFLVKPL----MLNRL 127
Cdd:PRK09390   36 AQAFLDAlpgLRFGCVVTDVRMPGIDGIELLRRLKARGSPLPVIVMTGHGDVPLAVEAMKLGAVDFIEKPFederLIGAI 115

                          90       100
                  ....*....|....*....|..
gi 1941938483 128 DQALARFESRQQCFSDASEVTQ 149
Cdd:PRK09390  116 ERALAQAPEAAKSEAVAADIRA 137
REC_DivK-like cd17548
phosphoacceptor receiver (REC) domain of DivK and similar proteins; Caulobacter crescentus ...
 38-133 2.96e-07

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: 47.92  E-value: 2.96e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941938483  38 LRQAQYQVVgIAGNLSTATALLHAIEPDLILLDIHLPDGNGLDLLTDLRR----RTIKseVMLLTAAKEVETLEKAMQLG 113
Cdd:cd17548    19 LESAGYEVL-EAADGEEALEIARKEKPDLILMDIQLPGMDGLEATRLLKEdpatRDIP--VIALTAYAMKGDREKILEAG 95

                          90       100
                  ....*....|....*....|
gi 1941938483 114 ACDFLVKPLMLNRLDQALAR 133
Cdd:cd17548    96 CDGYISKPIDTREFLETVAK 115
PRK15369 PRK15369
two component system response regulator;
1-120 3.51e-07

two component system response regulator;


Pssm-ID: 185267 [Multi-domain]  Cd Length: 211  Bit Score: 49.31  E-value: 3.51e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941938483   1 MTYSVVIIEDEVEVAqllaqylllpNGIAGNQTPkqslrQAQYQVVGIAGNLSTATALLHAIEPDLILLDIHLPDGNGLD 80
Cdd:PRK15369    2 KNYKILLVDDHELII----------NGIKNMLAP-----YPRYKIVGQVDNGLEVYNACRQLEPDIVILDLGLPGMNGLD 66

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1941938483  81 LLTDLRRRTIKSEVMLLTAAKEVETLEKAMQLGACDFLVK 120
Cdd:PRK15369   67 VIPQLHQRWPAMNILVLTARQEEHMASRTLAAGALGYVLK 106
REC_hyHK cd17598
phosphoacceptor receiver (REC) domain of uncharacterized hybrid sensor histidine kinase ...
 38-131 3.65e-07

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: 47.71  E-value: 3.65e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941938483  38 LRQAQYQVvGIAGNLSTATALLHAIEPDLILLDIHLPDGNGLDLLtdlrrRTIKSE-------VMLLTAAKEVETLEKAM 110
Cdd:cd17598    18 LEEQGYKV-QVARNGREALAMLAEHRPTLVISDIVMPEMDGYELC-----RKIKSDpdlkdipVILLTTLSDPRDVIRGL 91

                          90       100
                  ....*....|....*....|....*
gi 1941938483 111 QLGACDFLVKP----LMLNRLDQAL 131
Cdd:cd17598    92 ECGADNFITKPydekYLLSRIKYIL 116
REC_OmpR_YycF-like cd17614
phosphoacceptor receiver (REC) domain of YrcF-like OmpR family response regulators; YycF ...
 35-136 5.38e-07

phosphoacceptor receiver (REC) domain of YrcF-like OmpR family response regulators; YycF appears to play an important role in cell wall integrity in a wide range of gram-positive bacteria, and may also modulate cell membrane integrity. It functions as part of a phosphotransfer system that ultimately controls the levels of competence within the bacteria. YycF belongs to the OmpR family of response regulators, which are characterized by a REC domain and a winged helix-turn-helix effector domain involved in DNA binding. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381130 [Multi-domain]  Cd Length: 115  Bit Score: 47.03  E-value: 5.38e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941938483  35 KQSLRQAQYQVVgIAGNLSTATALLHAIEPDLILLDIHLPDGNGLDLLTDLRRRTIKSEVMLltAAKEVEtLEK--AMQL 112
Cdd:cd17614    15 KFNLTKEGYEVV-TAYDGREALEKVEEEQPDLILLDLMLPEKDGLEVCREVRKTSNVPIIML--TAKDSE-VDKvlGLEL 90

                          90       100
                  ....*....|....*....|....
gi 1941938483 113 GACDFLVKPLMLNRLdqaLARFES 136
Cdd:cd17614    91 GADDYVTKPFSNREL---LARVKA 111
glnG PRK10923
nitrogen regulation protein NR(I); Provisional
 55-139 5.94e-07

nitrogen regulation protein NR(I); Provisional


Pssm-ID: 182842 [Multi-domain]  Cd Length: 469  Bit Score: 49.48  E-value: 5.94e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941938483  55 ATALLHAIE---PDLILLDIHLPDGNGLDLLTDLRRRTIKSEVMLLTAAKEVETLEKAMQLGACDFLVKPLMLNR----L 127
Cdd:PRK10923   36 GNEVLEALAsktPDVLLSDIRMPGMDGLALLKQIKQRHPMLPVIIMTAHSDLDAAVSAYQQGAFDYLPKPFDIDEavalV 115

                          90
                  ....*....|..
gi 1941938483 128 DQALARFESRQQ 139
Cdd:PRK10923  116 ERAISHYQEQQQ 127
PRK10701 PRK10701
DNA-binding transcriptional regulator RstA; Provisional
 54-158 6.26e-07

DNA-binding transcriptional regulator RstA; Provisional


Pssm-ID: 236738 [Multi-domain]  Cd Length: 240  Bit Score: 48.86  E-value: 6.26e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941938483  54 TATALLHAIEPDLILLDIHLPDGNGLDLLTDLRRRtIKSEVMLLTaakeveTLEKAM------QLGACDFLVK----PLM 123
Cdd:PRK10701   36 RAEATILREQPDLVLLDIMLPGKDGMTICRDLRPK-WQGPIVLLT------SLDSDMnhilalEMGACDYILKttppAVL 108

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1941938483 124 LNRLDQALARFESRQQCFSDASEVTQSMVDTLFGS 158
Cdd:PRK10701  109 LARLRLHLRQNEQATQTKGLQETSLTPYKALHFGT 143
PRK11083 PRK11083
DNA-binding response regulator CreB; Provisional
 55-121 6.72e-07

DNA-binding response regulator CreB; Provisional


Pssm-ID: 236838 [Multi-domain]  Cd Length: 228  Bit Score: 48.80  E-value: 6.72e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1941938483  55 ATALLHAIEPDLILLDIHLPDGNGLDLLTDLRRRTIKSEVMLLTA-AKEVETLeKAMQLGACDFLVKP 121
Cdd:PRK11083   39 ALDKLRQQPPDLVILDVGLPDISGFELCRQLLAFHPALPVIFLTArSDEVDRL-VGLEIGADDYVAKP 105
REC_TrrA-like cd17554
phosphoacceptor receiver (REC) domain of Thermotoga maritima response regulator TrrA and ...
 35-120 6.97e-07

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: 46.83  E-value: 6.97e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941938483  35 KQSLRQAQYQVVgIAGNLSTATALLHAIEPDLILLDIHLPDGNGLDLLTDLRRRTIKSEVMLLTAAKEVETleKAMQLGA 114
Cdd:cd17554    17 KEELEDEGYEVV-TAGNGEEALEKLESEDPDLVILDIKMPGMDGLETLRKIREKKPDLPVIICTAYSEYKS--DFSSWAA 93


                  ....*.
gi 1941938483 115 CDFLVK 120
Cdd:cd17554    94 DAYVVK 99
REC_OmpR_kpRstA-like cd17622
phosphoacceptor receiver (REC) domain of kpRstA-like OmpR family response regulators; ...
 35-133 8.25e-07

phosphoacceptor receiver (REC) domain of kpRstA-like OmpR family response regulators; Klebsiella pneumoniae RstA (kpRstA) is part of the RstA/RstB two-component regulatory system that may play a regulatory role in virulence. 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: 381137 [Multi-domain]  Cd Length: 116  Bit Score: 46.60  E-value: 8.25e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941938483  35 KQSLRQAQYQVVgIAGNLSTATALLHAIEPDLILLDIHLPDGNGLDLLTDLRRRTiKSEVMLLTAAKEVETLEKAMQLGA 114
Cdd:cd17622    17 ADFLESHGFNVV-VEHRGDRALEVIAREKPDAVLLDIMLPGIDGLTLCRDLRPKY-QGPILLLTALDSDIDHILGLELGA 94

                          90       100
                  ....*....|....*....|...
gi 1941938483 115 CDFLVKP----LMLNRLdQALAR 133
Cdd:cd17622    95 DDYVVKPvepaVLLARL-RALLR 116
REC_Spo0F-like cd17553
phosphoacceptor receiver (REC) domain of Spo0F and similar domains; Spo0F, a stand-alone ...
 64-134 1.50e-06

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


Pssm-ID: 381105 [Multi-domain]  Cd Length: 117  Bit Score: 46.01  E-value: 1.50e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1941938483  64 PDLILLDIHLPDGNGLDLLTDLRRRTIKSEVMLLTAAKEVETLEKAMQLGACDFLVKPLMLNRLDQALARF 134
Cdd:cd17553    45 PDLVLLDMKIPGMDGIEILKRMKVIDENIRVIIMTAYGELDMIQESKELGALTHFAKPFDIDEIRDAVKKY 115
REC_RR468-like cd17552
phosphoacceptor receiver (REC) domain of Thermotoga maritima response regulator RR468 and ...
 41-121 1.67e-06

phosphoacceptor receiver (REC) domain of Thermotoga maritima response regulator RR468 and similar domains; Thermotoga maritima RR468 (encoded by gene TM0468) is the cognate response regulator (RR) of the class I histidine kinase HK853 (product of gene TM0853). HK853/RR468 comprise a two-component system (TCS) that couples environmental stimuli to adaptive responses. This subfamily also includes Fremyella diplosiphon complementary adaptation response regulator homolog RcaF, a small RR that is involved in four-step phosphorelays of the complementary chromatic adaptation (CCA) system that occurs in many cyanobacteria. Both RR468 and RcaF are stand-alone RRs containing only a REC domain with no output/effector domain. The REC domain itself functions as an effector domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381104 [Multi-domain]  Cd Length: 121  Bit Score: 45.62  E-value: 1.67e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941938483  41 AQYQVVgIAGNLSTATALLHAIEPDLILLDIHLPDGNGLDLLTDLRR--RTIKSEVMLLTAAKEVETLEKAMQLGACDFL 118
Cdd:cd17552    25 AGWEVL-TASSGQEGLEKAATEQPDAILLDVMMPDMDGLATLKKLQAnpETQSIPVILLTAKAQPSDRQRFASLGVAGVI 103


                  ...
gi 1941938483 119 VKP 121
Cdd:cd17552   104 AKP 106
PRK12555 PRK12555
chemotaxis-specific protein-glutamate methyltransferase CheB;
39-138 1.79e-06

chemotaxis-specific protein-glutamate methyltransferase CheB;


Pssm-ID: 237135 [Multi-domain]  Cd Length: 337  Bit Score: 47.95  E-value: 1.79e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941938483  39 RQAQYQVVGIAGNLSTATALLHAIEPDLILLDIHLPDGNGLDLLTDLRRRTIKSEVML--LTAAKEVETLEkAMQLGACD 116
Cdd:PRK12555   22 RDPDHEVVWVATDGAQAVERCAAQPPDVILMDLEMPRMDGVEATRRIMAERPCPILIVtsLTERNASRVFE-AMGAGALD 100

                          90       100
                  ....*....|....*....|..
gi 1941938483 117 FLVKPlmlnRLDQALARFESRQ 138
Cdd:PRK12555  101 AVDTP----TLGIGAGLEEYAA 118
psREC_PRR cd17582
pseudo receiver domain of pseudo-response regulators; In Arabidopsis, five pseudo-response ...
 38-121 1.90e-06

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


Pssm-ID: 381120 [Multi-domain]  Cd Length: 104  Bit Score: 45.08  E-value: 1.90e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941938483  38 LRQAQYQVVGIAGNLSTATAL-LHAIEPDLILLDIHLPDGNGLDLLTDLRRRTIKSE--VMLLTAAKEVETLEKAMQLGA 114
Cdd:cd17582    18 LRKCSYEVTAASDGLQAWDVLeDEQNEIDLILTEVDLPVSSGFKLLSYIMRHKICKNipVIMMSSQDSVGVVFKCLSKGA 97


                  ....*..
gi 1941938483 115 CDFLVKP 121
Cdd:cd17582    98 ADYLVKP 104
PRK10766 PRK10766
two-component system response regulator TorR;
1-127 1.96e-06

two-component system response regulator TorR;


Pssm-ID: 182711 [Multi-domain]  Cd Length: 221  Bit Score: 47.34  E-value: 1.96e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941938483   1 MTYSVVIIEDEVEVAQLLaqylllpngiagnqtpKQSLRQAQYQVVgIAGNLSTATALLHAIEPDLILLDIHLPDGNGLD 80
Cdd:PRK10766    1 MSYHILVVEDEPVTRARL----------------QGYFEQEGYTVS-EAASGAGMREIMQNQHVDLILLDINLPGEDGLM 63

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1941938483  81 LLTDLRRRtikSEVMLLTAAKEVETLEK--AMQLGACDFLVKPLMLNRL 127
Cdd:PRK10766   64 LTRELRSR---STVGIILVTGRTDSIDRivGLEMGADDYVTKPLELREL 109
REC_OmpR_MtrA-like cd17626
phosphoacceptor receiver (REC) domain of MtrA-like OmpR family response regulators; MtrA is ...
 48-137 2.39e-06

phosphoacceptor receiver (REC) domain of MtrA-like OmpR family response regulators; MtrA is part of MtrA/MtrB (or MtrAB), a highly conserved two-component system (TCS) implicated in the regulation of cell division in the actinobacteria. In unicellular Mycobacterium tuberculosis, MtrAB coordinates DNA replication with cell division and regulates the transcription of resuscitation-promoting factor B. In filamentous Streptomyces venezuelae, it links antibiotic production to sporulation. MtrA belongs to the OmpR family of DNA-binding response regulators that contain N-terminal receiver (REC) and C-terminal DNA-binding winged helix-turn-helix effector domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381141 [Multi-domain]  Cd Length: 115  Bit Score: 45.15  E-value: 2.39e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941938483  48 IAGNLSTATALLHAIEPDLILLDIHLPDGNGLDLLTDLRRRTIKSEVMlLTAAKEVETLEKAMQLGACDFLVKPLMLNRL 127
Cdd:cd17626    29 FCGDGTQALAAFREVRPDLVLLDLMLPGIDGIEVCRQIRAESGVPIVM-LTAKSDTVDVVLGLESGADDYVAKPFKPKEL 107

                          90
                  ....*....|
gi 1941938483 128 dqaLARFESR 137
Cdd:cd17626   108 ---VARIRAR 114
REC_PhyR cd17540
phosphoacceptor receiver (REC) domain of response regulator PhyR and similar proteins; PhyR is ...
 4-99 3.71e-06

phosphoacceptor receiver (REC) domain of response regulator PhyR and similar proteins; PhyR is a hybrid stress regulator that contains an N-terminal sigma-like (SL) domain and a C-terminal REC domain. Phosphorylation of the REC domain is known to promote binding of the SL domain to an anti-sigma factor. PhyR thus functions as an anti-anti-sigma factor in its phosphorylated state. It is involved in the general stress response. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381095 [Multi-domain]  Cd Length: 117  Bit Score: 44.55  E-value: 3.71e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941938483   4 SVVIIEDEvevaqllaqylllPNgIAGNQtpKQSLRQAQYQVVGIAGNLSTATALLHAIEPDLILLDIHLPDG-NGLDLL 82
Cdd:cd17540     2 RVLIIEDE-------------PL-IAMDL--EQIVEDLGHQVVGIARTRDEAVALARRERPDLILADIQLADGsSGIDAV 65

                          90
                  ....*....|....*..
gi 1941938483  83 TDLrRRTIKSEVMLLTA 99
Cdd:cd17540    66 NEI-LTTHDVPVIFVTA 81
orf27 CHL00148
Ycf27; Reviewed
 38-121 4.59e-06

Ycf27; Reviewed


Pssm-ID: 214376 [Multi-domain]  Cd Length: 240  Bit Score: 46.25  E-value: 4.59e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941938483  38 LRQAQYQVVgIAGNLSTATALLHAIEPDLILLDIHLPDGNGLDLLTDLRRrtiKSEV--MLLTAAKEVETLEKAMQLGAC 115
Cdd:CHL00148   26 LSIIGYEVI-TASDGEEALKLFRKEQPDLVILDVMMPKLDGYGVCQEIRK---ESDVpiIMLTALGDVSDRITGLELGAD 101


                  ....*.
gi 1941938483 116 DFLVKP 121
Cdd:CHL00148  102 DYVVKP 107
REC_CheY_CheY3 cd19923
phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY3 and similar CheY ...
 35-121 6.66e-06

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: 44.25  E-value: 6.66e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941938483  35 KQSLRQAQYQVVGIAGNLSTATALLHAIEPDLILLDIHLPDGNGLDLLTDLRRRTIKSE--VMLLTAAKEVETLEKAMQL 112
Cdd:cd19923    17 KNLLKELGFNNVEEAEDGVDALEKLKAGGFDFVITDWNMPNMDGLELLKTIRADGALSHlpVLMVTAEAKKENVIAAAQA 96


                  ....*....
gi 1941938483 113 GACDFLVKP 121
Cdd:cd19923    97 GVNNYIVKP 105
REC_OmpR_VirG cd17594
phosphoacceptor receiver (REC) domain of VirG-like OmpR family response regulators; VirG is ...
 38-133 8.18e-06

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


Pssm-ID: 381125 [Multi-domain]  Cd Length: 113  Bit Score: 43.59  E-value: 8.18e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941938483  38 LRQAQYQVVGIAGNLSTATALLHAiEPDLILLDIHLPDGNGLDLLTDLRRRTIKSEVMLLTAAKEVETLEKAMQLGACDF 117
Cdd:cd17594    19 LRERGFDVTAAADGAEEARLMLHR-RVDLVLLDLRLGQESGLDLLRTIRARSDVPIIIISGDRRDEIDRVVGLELGADDY 97

                          90
                  ....*....|....*.
gi 1941938483 118 LVKPLMLNRLdqaLAR 133
Cdd:cd17594    98 LAKPFGLREL---LAR 110
PRK10336 PRK10336
two-component system response regulator QseB;
54-138 8.34e-06

two-component system response regulator QseB;


Pssm-ID: 182387 [Multi-domain]  Cd Length: 219  Bit Score: 45.27  E-value: 8.34e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941938483  54 TATALLHAIEPDLILLDIHLPDGNGLDLLTDLRRRTIKSEVMLLTAAKEVETLEKAMQLGACDFLVKPLML----NRLdQ 129
Cdd:PRK10336   35 QGKEALYSAPYDAVILDLTLPGMDGRDILREWREKGQREPVLILTARDALAERVEGLRLGADDYLCKPFALievaARL-E 113


                  ....*....
gi 1941938483 130 ALARFESRQ 138
Cdd:PRK10336  114 ALMRRTNGQ 122
PRK09958 PRK09958
acid-sensing system DNA-binding response regulator EvgA;
53-177 8.64e-06

acid-sensing system DNA-binding response regulator EvgA;


Pssm-ID: 182168 [Multi-domain]  Cd Length: 204  Bit Score: 45.27  E-value: 8.64e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941938483  53 STATALLHAIEPDLILLDIHLPDGNGLDLLTDLRRRTIKSEVMLLTAAKEVETLEKAMQLGACDFLVKPLMLNRLDQAL- 131
Cdd:PRK09958   35 GSAVQRVETLKPDIVIIDVDIPGVNGIQVLETLRKRQYSGIIIIVSAKNDHFYGKHCADAGANGFVSKKEGMNNIIAAIe 114

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1941938483 132 ------ARFESRQQCFSDASEVTQSMVDTLfgSKQQTNIFNRLPKGVDQLTL 177
Cdd:PRK09958  115 aakngyCYFPFSLNRFVGSLTSDQQKLDSL--SKQEISVMRYILDGKDNNDI 164
PRK11517 PRK11517
DNA-binding response regulator HprR;
35-133 1.02e-05

DNA-binding response regulator HprR;


Pssm-ID: 183172 [Multi-domain]  Cd Length: 223  Bit Score: 45.27  E-value: 1.02e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941938483  35 KQSLRQAQYQVVGIAGNlstATALLHAIEPD--LILLDIHLPDGNGLDLLTDLRRRTiKSEVMLLTAAKEVETLEKAMQL 112
Cdd:PRK11517   17 TQGLSEAGYVIDAVSDG---RDGLYLALKDDyaLIILDIMLPGMDGWQILQTLRTAK-QTPVICLTARDSVDDRVRGLDS 92

                          90       100
                  ....*....|....*....|.
gi 1941938483 113 GACDFLVKPLMLNRLdqaLAR 133
Cdd:PRK11517   93 GANDYLVKPFSFSEL---LAR 110
PRK10955 PRK10955
envelope stress response regulator transcription factor CpxR;
35-148 1.19e-05

envelope stress response regulator transcription factor CpxR;


Pssm-ID: 182864 [Multi-domain]  Cd Length: 232  Bit Score: 45.18  E-value: 1.19e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941938483  35 KQSLRQAQYQVVgIAGNLSTATALLHAiEPDLILLDIHLPDGNGLDLLTDLRRRTIKSEVMLLTAAKEVETLeKAMQLGA 114
Cdd:PRK10955   18 KELLEMEGFNVI-VAHDGEQALDLLDD-SIDLLLLDVMMPKKNGIDTLKELRQTHQTPVIMLTARGSELDRV-LGLELGA 94

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1941938483 115 CDFLVKPL----MLNRLDQALARFE-SRQQCFSDASEVT 148
Cdd:PRK10955   95 DDYLPKPFndreLVARIRAILRRSHwSEQQQNNDNGSPT 133
PRK09191 PRK09191
two-component response regulator; Provisional
 44-88 1.21e-05

two-component response regulator; Provisional


Pssm-ID: 236402 [Multi-domain]  Cd Length: 261  Bit Score: 45.22  E-value: 1.21e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1941938483  44 QVVGIAGNLSTATALLHAIEPDLILLDIHLPDG-NGLDLLTDLRRR 88
Cdd:PRK09191  163 RVTGIARTRAEAVALAKKTRPGLILADIQLADGsSGIDAVNDILKT 208
REC_CheC-like cd17593
phosphoacceptor receiver (REC) domain of uncharacterized response regulators containing a CheC ...
 64-134 1.22e-05

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: 43.29  E-value: 1.22e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1941938483  64 PDLILLDIHLPDGNGLDLLTDLRRRTIKSEVMLLTAAKEVETLEKAMQLGACDFLVKPLMLNRLDQALARF 134
Cdd:cd17593    46 IDVLFLDLTMPVMDGYEVLEALPVEQLETKVIVVSGDVQPEAKERVLELGALAFLKKPFDPEKLAQLLEEL 116
PEP_resp_reg TIGR02915
PEP-CTERM-box response regulator transcription factor; Members of this protein family share ...
 41-133 1.59e-05

PEP-CTERM-box response regulator transcription factor; Members of this protein family share full-length homology with (but do not include) the acetoacetate metabolism regulatory protein AtoC (see SP|Q06065). These proteins have a Fis family DNA binding sequence (pfam02954), a response regulator receiver domain (pfam00072), and sigma-54 interaction domain (pfam00158). [Regulatory functions, DNA interactions]


Pssm-ID: 274348 [Multi-domain]  Cd Length: 445  Bit Score: 45.12  E-value: 1.59e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941938483  41 AQYQVVgIAGNLSTATALLHAIEPDLILLDIHLP---DG--NGLDLLTDLRRRTIKSEVMLLTAAKEVETLEKAMQLGAC 115
Cdd:TIGR02915  19 ADYELA-VAADRESAIALVRRHEPAVVTLDLGLPpdaDGasEGLAALQQILAIAPDTKVIVITGNDDRENAVKAIGLGAY 97

                          90
                  ....*....|....*...
gi 1941938483 116 DFLVKPLMLNRLDQALAR 133
Cdd:TIGR02915  98 DFYQKPIDPDVLKLIVDR 115
REC_OmpR_ChvI-like cd19936
phosphoacceptor receiver (REC) domain of ChvI-like OmpR family response regulators; ...
 35-121 2.19e-05

phosphoacceptor receiver (REC) domain of ChvI-like OmpR family response regulators; Sinorhizobium meliloti ChvI is part of the ExoS/ChvI two-component regulatory system (TCS) that is required for nitrogen-fixing symbiosis and exopolysaccharide synthesis. ExoS/ChvI also play important roles in regulating biofilm formation, motility, nutrient utilization, and the viability of free-living bacteria. ChvI belongs to the OmpR family of DNA-binding response regulators that contain N-terminal receiver (REC) and C-terminal DNA-binding winged helix-turn-helix effector domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381163 [Multi-domain]  Cd Length: 99  Bit Score: 42.05  E-value: 2.19e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941938483  35 KQSLRQAQYQVVGIAGNLSTATALLHAIePDLILLDIHLPDGNGLDLLTDLRRRTIKSEVMLLTAAKEVETLeKAMQLGA 114
Cdd:cd19936    15 SMALEAEGFSVETYTDGASALDGLNARP-PDLAILDIKMPRMDGMELLQRLRQKSTLPVIFLTSKDDEIDEV-FGLRMGA 92


                  ....*..
gi 1941938483 115 CDFLVKP 121
Cdd:cd19936    93 DDYITKP 99
PRK10816 PRK10816
two-component system response regulator PhoP;
38-133 3.35e-05

two-component system response regulator PhoP;


Pssm-ID: 182755 [Multi-domain]  Cd Length: 223  Bit Score: 43.57  E-value: 3.35e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941938483  38 LRQAQYQVvGIAGNLSTATALLHAIEPDLILLDIHLPDGNGLDLLTDLRRRTIKSEVMLLTAAKEVETLEKAMQLGACDF 117
Cdd:PRK10816   20 LQDAGHQV-DAAEDAKEADYYLNEHLPDIAIVDLGLPDEDGLSLIRRWRSNDVSLPILVLTARESWQDKVEVLSAGADDY 98

                          90
                  ....*....|....*....
gi 1941938483 118 LVKPLMLNRLD---QALAR 133
Cdd:PRK10816   99 VTKPFHIEEVMarmQALMR 117
REC_2_DhkD-like cd17580
second phosphoacceptor receiver (REC) domain of Dictyostelium discoideum hybrid signal ...
 38-131 5.31e-05

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: 41.29  E-value: 5.31e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941938483  38 LRQAQYQVVgIAGNLSTATALLHAIEPDLILLDIHLPDGNGLDLLTDLRRRTIKSEVML--LTAAKEVETLEKAMQLGAC 115
Cdd:cd17580    18 LELEGAEVT-TAHSGEEALEAAQRFRPDVILSDIGMPGMDGYELARRLRELPWLANTPAiaLTGYGQPEDRERALEAGFD 96

                          90
                  ....*....|....*.
gi 1941938483 116 DFLVKPLMLNRLDQAL 131
Cdd:cd17580    97 AHLVKPVDPDELIELI 112
REC_2_GGDEF cd17544
second phosphoacceptor receiver (REC) domain of uncharacterized GGDEF domain proteins; This ...
 38-121 6.78e-05

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: 41.35  E-value: 6.78e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941938483  38 LRQAQYQVVGiAGNLSTATALLHAiEPD--LILLDIHLPDGNGLDLLTDLRRRTIKSEV----------MLLTAakevet 105
Cdd:cd17544    20 LRRHNFQVLE-AANGQEALEVLEQ-HPDikLVITDYNMPEMDGFELVREIRKKYSRDQLaiigisasgdNALSA------ 91

                          90
                  ....*....|....*.
gi 1941938483 106 leKAMQLGACDFLVKP 121
Cdd:cd17544    92 --RFIKAGANDFLTKP 105
PRK10710 PRK10710
DNA-binding transcriptional regulator BaeR; Provisional
 64-153 1.17e-04

DNA-binding transcriptional regulator BaeR; Provisional


Pssm-ID: 182665 [Multi-domain]  Cd Length: 240  Bit Score: 41.98  E-value: 1.17e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941938483  64 PDLILLDIHLPDGNGLDLLTDLRRRTIKSEVMLLTAAKEVETLeKAMQLGACDFLVKPL----MLNRLDQALARFeSRQQ 139
Cdd:PRK10710   55 PDLILLDLMLPGTDGLTLCREIRRFSDIPIVMVTAKIEEIDRL-LGLEIGADDYICKPYspreVVARVKTILRRC-KPQR 132

                          90
                  ....*....|....
gi 1941938483 140 CFSDASEVTQSMVD 153
Cdd:PRK10710  133 ELQQQDAESPLIID 146
pleD PRK09581
response regulator PleD; Reviewed
 41-121 1.26e-04

response regulator PleD; Reviewed


Pssm-ID: 236577 [Multi-domain]  Cd Length: 457  Bit Score: 42.58  E-value: 1.26e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941938483  41 AQYQVVGIAGNLSTATALLHAIEPDLILLDIHLPDGNGLDLLtdlrrRTIKSE-------VMLLTAAKEVETLEKAMQLG 113
Cdd:PRK09581   24 AEYYTVLTASSGAEAIAICEREQPDIILLDVMMPGMDGFEVC-----RRLKSDpatthipVVMVTALDDPEDRVRGLEAG 98


                  ....*...
gi 1941938483 114 ACDFLVKP 121
Cdd:PRK09581   99 ADDFLTKP 106
PRK10610 PRK10610
chemotaxis protein CheY;
38-135 1.29e-04

chemotaxis protein CheY;


Pssm-ID: 170568 [Multi-domain]  Cd Length: 129  Bit Score: 40.73  E-value: 1.29e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941938483  38 LRQAQYQVVGIAGNLSTATALLHAIEPDLILLDIHLPDGNGLDLLTDLRR--RTIKSEVMLLTAAKEVETLEKAMQLGAC 115
Cdd:PRK10610   25 LKELGFNNVEEAEDGVDALNKLQAGGFGFVISDWNMPNMDGLELLKTIRAdgAMSALPVLMVTAEAKKENIIAAAQAGAS 104

                          90       100
                  ....*....|....*....|.
gi 1941938483 116 DFLVKPLMLNRLDQALAR-FE 135
Cdd:PRK10610  105 GYVVKPFTAATLEEKLNKiFE 125
PRK14084 PRK14084
DNA-binding response regulator;
43-181 1.39e-04

DNA-binding response regulator;


Pssm-ID: 184495 [Multi-domain]  Cd Length: 246  Bit Score: 42.05  E-value: 1.39e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941938483  43 YQVVGIAGNLS-TATALLHAiEPDLILLDIHLPDGNGLDLLTDLRRRTIKSEVMLLTAAKEVETleKAMQLGACDFLVKP 121
Cdd:PRK14084   26 FEEINEAENVKeTLEALLIN-QYDIIFLDINLMDESGIELAAKIQKMKEPPAIIFATAHDQFAV--KAFELNATDYILKP 102

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941938483 122 LMLNRLDQALARFESRQQCFSDASEVTQsmvdtlfgSKQQTNIFNRLPKGVDqltlQKIH 181
Cdd:PRK14084  103 FEQKRIEQAVNKVRATKAKDDNNASAIA--------NDMSANFDQSLPIEID----DKIH 150
PRK11697 PRK11697
two-component system response regulator BtsR;
44-133 1.48e-04

two-component system response regulator BtsR;


Pssm-ID: 236956 [Multi-domain]  Cd Length: 238  Bit Score: 41.76  E-value: 1.48e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941938483  44 QVVGIAGNLSTATALLHAIEPDLILLDIHLPDGNGLDLLTDLRRRTIkSEVMLLTAAKEVETleKAMQLGACDFLVKPLM 123
Cdd:PRK11697   28 EIVGECSNAIEAIGAIHRLKPDVVFLDIQMPRISGLELVGMLDPEHM-PYIVFVTAFDEYAI--KAFEEHAFDYLLKPID 104

                          90
                  ....*....|
gi 1941938483 124 LNRLDQALAR 133
Cdd:PRK11697  105 PARLAKTLAR 114
COG2345 COG2345
Predicted transcriptional regulator, ArsR family [Transcription];
193-240 1.85e-04

Predicted transcriptional regulator, ArsR family [Transcription];


Pssm-ID: 441914 [Multi-domain]  Cd Length: 217  Bit Score: 41.45  E-value: 1.85e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1941938483 193 TAQQMGDLVGVSRSTARRYLEYLLESGKLTADQSYGSIGRPERCYKIA 240
Cdd:COG2345    29 TAAELAEALGLTPNAVRRHLDALEEEGLVERETERRGRGRPAKLYRLT 76
REC_OmpR_BfmR-like cd19939
phosphoacceptor receiver (REC) domain of BfmR-like OmpR family response regulators; ...
 46-133 2.35e-04

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: 39.66  E-value: 2.35e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941938483  46 VGIAGNLSTATALLHAIEPDLILLDIHLPDGNGLDLLTDLRRRTIKSEVMLLTAAKEVETLeKAMQLGACDFLVKP---- 121
Cdd:cd19939    26 VSVFTDGQRAVRRIIDEQPSLVVLDIMLPGMDGLTVCREVREHSHVPILMLTARTEEMDRV-LGLEMGADDYLCKPfspr 104

                          90
                  ....*....|..
gi 1941938483 122 LMLNRLDQALAR 133
Cdd:cd19939   105 ELLARVRALLRR 116
REC_CheY4-like cd17562
phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY4 and similar CheY ...
 37-134 2.41e-04

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: 39.59  E-value: 2.41e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941938483  37 SLRQAQYQVVgIAGNLSTATALLHAIEPDLILLDIHLPDGNGLDLLTDLR-----RRTiksEVMLLTAAKEVETLEKAMQ 111
Cdd:cd17562    19 TLRGAGYEVV-EAADGRDALSKAQSKKFDLIITDQNMPNMDGIELIKELRklpayKFT---PILMLTTESSDEKKQEGKA 94

                          90       100
                  ....*....|....*....|...
gi 1941938483 112 LGACDFLVKPLMLNRLDQALARF 134
Cdd:cd17562    95 AGATGWLVKPFDPEQLLEVVKKV 117
REC_GlnL-like cd17565
phosphoacceptor receiver (REC) domain of transcriptional regulatory protein GlnL and similar ...
 45-122 5.24e-04

phosphoacceptor receiver (REC) domain of transcriptional regulatory protein GlnL and similar proteins; Bacillus subtilis GlnL is part of the GlnK-GlnL (formerly YcbA-YcbB) two-component system that positively regulates the expression of the glsA-glnT (formerly ybgJ-ybgH) operon in response to glutamine. It contains a REC domain and a DNA-binding output domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381112 [Multi-domain]  Cd Length: 103  Bit Score: 38.41  E-value: 5.24e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1941938483  45 VVGIAGNLSTATALLHAIEPDLILLDIHLPDGNGLDLLTDLRRRTIKSEVMLLTAAKEVETLEKAMQLGACDFLVKPL 122
Cdd:cd17565    26 VVGEADNGAQAYDEILFLQPDIVLIDLLMPGMDGIQLVRKLKDTGSNGKFIMISQVSDKEMIGKAYQAGIEFFINKPI 103
REC_HupR-like cd17569
phosphoacceptor receiver (REC) domain of hydrogen uptake protein regulator (HupR) and similar ...
 35-121 7.92e-04

phosphoacceptor receiver (REC) domain of hydrogen uptake protein regulator (HupR) and similar domains; This family is composed of mostly uncharacterized response regulators with similarity to the REC domains of response regulator components of two-component systems that regulates hydrogenase activity, including HupR and HoxA. HupR is part of the HupT/HupR system that controls the synthesis of the membrane-bound [NiFe]hydrogenase, HupSL, of the photosynthetic bacterium Rhodobacter capsulatus. It contains an N-terminal REC domain, a central sigma-54 interaction domain that lacks ATPase activity, and a C-terminal DNA-binding domain. Members of this family contain a REC domain and various output domains including the cyclase homology domain (CHD) and the c-di-GMP phosphodiesterase domains, HD-GYP and EAL. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381113 [Multi-domain]  Cd Length: 118  Bit Score: 38.15  E-value: 7.92e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941938483  35 KQSLRQAQYQVVgIAGNLSTATALLHAIEPDLILLDIHLPDGNGLDLLTDLRRR---TIKsevMLLTAAKEVETLEKAMQ 111
Cdd:cd17569    17 KRLLRREGYEVL-TATSGEEALEILKQEPVDVVISDQRMPGMDGAELLKRVRERypdTVR---ILLTGYADLDAAIEAIN 92

                          90
                  ....*....|.
gi 1941938483 112 LGACD-FLVKP 121
Cdd:cd17569    93 EGEIYrFLTKP 103
REC smart00448
cheY-homologous receiver domain; CheY regulates the clockwise rotation of E. coli flagellar ...
 35-74 8.12e-04

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: 36.39  E-value: 8.12e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 1941938483   35 KQSLRQAQYQVVgIAGNLSTATALLHAIEPDLILLDIHLP 74
Cdd:smart00448  17 KALLEKEGYEVD-EATDGEEALELLKEEKPDLILLDIMMP 55
PRK09483 PRK09483
response regulator; Provisional
 44-168 1.31e-03

response regulator; Provisional


Pssm-ID: 236538 [Multi-domain]  Cd Length: 217  Bit Score: 38.93  E-value: 1.31e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941938483  44 QVVGIAGNLSTATALLHAIEPDLILLDIHLPDGNGLDLLTDLRRRTIKSEVMLLTAAKEVETLEKAMQLGACDFLVKPLM 123
Cdd:PRK09483   28 KVVGEACCGEDAVKWCRTNAVDVVLMDMNMPGIGGLEATRKILRYTPDVKIIMLTVHTENPLPAKVMQAGAAGYLSKGAA 107

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1941938483 124 LNRLDQALARFESRQQCFsdASEVTQSMVDTLFgSKQQTNIFNRL 168
Cdd:PRK09483  108 PQEVVSAIRSVHSGQRYI--ASDIAQQMALSQI-EPATENPFASL 149
REC_OmpR_RegX3-like cd17621
phosphoacceptor receiver (REC) domain of RegX3-like OmpR family response regulators; RegX3 is ...
 38-121 1.54e-03

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


Pssm-ID: 381136 [Multi-domain]  Cd Length: 99  Bit Score: 36.79  E-value: 1.54e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941938483  38 LRQAQYQVVgIAGNLSTATALLHAIEPDLILLDIHLPDGNGLDLLTDLRRRTIKSEVMLLTAAKEVETLeKAMQLGACDF 117
Cdd:cd17621    18 LRKEGFEVT-VATDGPAALAEFDRAGADIVLLDLMLPGLSGTEVCRQLRARSNVPVIMVTAKDSEIDKV-VGLELGADDY 95


                  ....
gi 1941938483 118 LVKP 121
Cdd:cd17621    96 VTKP 99
REC_WspR-like cd17575
phosphoacceptor receiver (REC) domain of WspR response regulator and similar proteins; The ...
 55-120 2.26e-03

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


Pssm-ID: 381117 [Multi-domain]  Cd Length: 128  Bit Score: 37.00  E-value: 2.26e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1941938483  55 ATALLHAIEPDLILLDIHLPDGNGLDLLTDLRRR--TIKSEVMLLTAAKEVETLEKAMQLGACDFLVK 120
Cdd:cd17575    37 AIEVASQIKPTVILQDLVMPGVDGLTLVRFFRANpaTRDIPIIVLSTKEEPEVKSEAFALGANDYLVK 104
REC_ETR-like cd19933
phosphoacceptor receiver (REC) domain of plant ethylene receptors ETR1, ETR2, and EIN4, and ...
 66-131 3.60e-03

phosphoacceptor receiver (REC) domain of plant ethylene receptors ETR1, ETR2, and EIN4, and similar proteins; Plant ethylene receptors contain N-terminal transmembrane domains that contain an ethylene binding site and also serve in localization of the receptor to the endoplasmic reticulum or the Golgi apparatus and a C-terminal histidine kinase (HK)-like domain. There are five ethylene receptors (ETR1, ERS1, ETR2, ERS2, and EIN4) in Arabidopsis thaliana. ETR1, ETR2, and EIN4 also contain REC domains C-terminal to the HK domain. ETR1 and ERS1 belong to subfamily 1, and have functional HK domains while ETR2, ERS2, and EIN4 belong to subfamily 2, and lack the necessary residues for HK activity and may function as serine/threonine kinases. The plant hormone ethylene plays an important role in plant growth and development. It regulates seed germination, seedling growth, leaf and petal abscission, fruit ripening, organ senescence, and pathogen responses. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381160 [Multi-domain]  Cd Length: 117  Bit Score: 36.22  E-value: 3.60e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1941938483  66 LILLDIHLPDGNGLDLLTDLRRRTIKSEVML---LTAAKEVETLEKAMQLGACDFLVKPLMLNRLDQAL 131
Cdd:cd19933    49 LVLLDLCMPEMDGFEVALRIRKLFGRRERPLivaLTANTDDSTREKCLSLGMNGVITKPVSLHALGDEL 117
PRK09959 PRK09959
acid-sensing system histidine kinase EvgS;
65-134 3.87e-03

acid-sensing system histidine kinase EvgS;


Pssm-ID: 182169 [Multi-domain]  Cd Length: 1197  Bit Score: 38.18  E-value: 3.87e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941938483   65 DLILLDIHLPDGNGLDLLTDLRRRTIKSEVMLLTAAKEVETLEKAMQLGACDFLVKPLMLNRLDQALARF 134
Cdd:PRK09959  1004 DLLITDVNMPNMDGFELTRKLREQNSSLPIWGLTANAQANEREKGLSCGMNLCLFKPLTLDVLKTHLSQL 1073
PRK15115 PRK15115
response regulator GlrR; Provisional
 38-132 4.68e-03

response regulator GlrR; Provisional


Pssm-ID: 185070 [Multi-domain]  Cd Length: 444  Bit Score: 37.89  E-value: 4.68e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941938483  38 LRQAQYQVVgIAGNLSTATALLHAIEPDLILLDIHLPDGNGLDLLTDLRRRTIKSEVMLLTAAKEVETLEKAMQLGACDF 117
Cdd:PRK15115   25 LTSEGYSVV-TAESGQEALRVLNREKVDLVISDLRMDEMDGMQLFAEIQKVQPGMPVIILTAHGSIPDAVAATQQGVFSF 103

                          90
                  ....*....|....*....
gi 1941938483 118 LVKPL----MLNRLDQALA 132
Cdd:PRK15115  104 LTKPVdrdaLYKAIDDALE 122
PRK10360 PRK10360
transcriptional regulator UhpA;
40-120 4.88e-03

transcriptional regulator UhpA;


Pssm-ID: 182408 [Multi-domain]  Cd Length: 196  Bit Score: 36.88  E-value: 4.88e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941938483  40 QAQYQVVGIAGNLSTATALLHAIEPDLILLDIHLPDGNGLDLLTDLRRRTiksEVMLLTAAKEVETLEKAMQLGACDFLV 119
Cdd:PRK10360   24 EPDLQVVAEFGSGREALAGLPGRGVQVCICDISMPDISGLELLSQLPKGM---ATIMLSVHDSPALVEQALNAGARGFLS 100


                  .
gi 1941938483 120 K 120
Cdd:PRK10360  101 K 101
REC_CheV-like cd19924
phosphoacceptor receiver (REC) domain of chemotaxis protein CheV and similar proteins; This ...
 65-121 7.94e-03

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: 35.05  E-value: 7.94e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1941938483  65 DLILLDIHLPDGNGLDLLTDLRR--RTIKSEVMLLTAAKEVETLEKAMQLGACDFLVKP 121
Cdd:cd19924    53 DLIITDIEMPKMDGYELTFELRDdpRLANIPVILNSSLSGEFSRARGKKVGADAYLAKF 111
CitT pfam12431
Transcriptional regulator; This domain family is found in bacteria, and is approximately 30 ...
 147-175 8.07e-03

Transcriptional regulator; This domain family is found in bacteria, and is approximately 30 amino acids in length. The family is found in association with pfam00072. There is a single completely conserved residue G that may be functionally important. CitT is a transcriptional regulator which allows transcription of the citM gene which codes for the secondary transporter in the Mg-citrate transport complex.


Pssm-ID: 432549  Cd Length: 30  Bit Score: 33.22  E-value: 8.07e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1941938483 147 VTQSMVDTLFG--SKQQTNIfNRLPKGVDQL 175
Cdd:pfam12431   1 VDQSDVDRLFQlqAKGAPPS-GDLPKGIDKL 30
ompR PRK09468
osmolarity response regulator; Provisional
 38-121 9.58e-03

osmolarity response regulator; Provisional


Pssm-ID: 181883 [Multi-domain]  Cd Length: 239  Bit Score: 36.49  E-value: 9.58e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1941938483  38 LRQAQYQVVgIAGNLSTATALLHAIEPDLILLDIHLPDGNGLDLLTDLRRRTIKSEVMLLTA-AKEVETLeKAMQLGACD 116
Cdd:PRK09468   25 LTEQGFQVR-SAANAEQMDRLLTRESFHLMVLDLMLPGEDGLSICRRLRSQNNPTPIIMLTAkGEEVDRI-VGLEIGADD 102


                  ....*
gi 1941938483 117 FLVKP 121
Cdd:PRK09468  103 YLPKP 107
 
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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