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Conserved domains on  [gi|490280238|ref|WP_004176165|]
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MULTISPECIES: two-component system response regulator PgtA [Klebsiella]

Protein Classification

sigma-54-dependent transcriptional regulator( domain architecture ID 11454220)

sigma-54 factor interaction domain-containing protein with a domain similar to that found in the response regulator FleR from Pseudomonas aeruginosa

CATH:  3.40.50.2300
Gene Ontology:  GO:0006355|GO:0005524|GO:0000160|GO:0000156|GO:0003677
PubMed:  8830233|20226724|12618438|10966457
SCOP:  4003632

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
AtoC COG2204
DNA-binding transcriptional response regulator, NtrC family, contains REC, AAA-type ATPase, ...
 7-407 1.21e-98

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: 300.73  E-value: 1.21e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280238   7 SILLIDDDADVLDAYTQLLEQAGYHVSACNNPFDAREQVPKDWPGIVLSDVCMPGCSGIDLMTVFHQDDDLLPILLITGH 86
Cdd:COG2204    4 RILVVDDDPDIRRLLKELLERAGYEVETAASGEEALALLREEPPDLVLLDLRMPGMDGLELLRELRALDPDLPVILLTGY 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280238  87 GDVPMAVEAVKKGAWDFLQKPIDPGKLLTLVDAALRQRQSVIARRQycqqklQVELIGRSQWTVRYRQRLQQLAETDIAV 166
Cdd:COG2204   84 GDVETAVEAIKAGAFDYLTKPFDLEELLAAVERALERRRLRRENAE------DSGLIGRSPAMQEVRRLIEKVAPSDATV 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280238 167 WLYGEPGTGRMTGARYLHQLGRHAEGPFIA--CELTPAN----------------AHTLNE-LIAQAQGGTLVLSHPEHL 227
Cdd:COG2204  158 LITGESGTGKELVARAIHRLSPRADGPFVAvnCAAIPEElleselfghekgaftgAVARRIgKFELADGGTLFLDEIGEM 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280238 228 THEQQHQLVQ-LQSHEKRP----------FRLIGIGSASLVELAASSQIVAELYYCFAMTQIGCQPLSKRPDDIEPLFHH 296
Cdd:COG2204  238 PLALQAKLLRvLQEREFERvggnkpipvdVRVIAATNRDLEELVEEGRFREDLYYRLNVFPIELPPLRERREDIPLLARH 317

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280238 297 YLQKTCQRLNHPVPeVDAGLLKGMMRRVWPNNVRELANAAELFAVgvlpLAETvnplmHIGEPTPLDQRVEDVERQIITE 376
Cdd:COG2204  318 FLARFAAELGKPVK-LSPEALEALLAYDWPGNVRELENVIERAVI----LADG-----EVITAEDLPEALEEVERELIER 387

                        410       420       430
                 ....*....|....*....|....*....|.
gi 490280238 377 ALNIHQGRINEVAEYLLIPRKKLYLRMKKYG 407
Cdd:COG2204  388 ALEETGGNVSRAAELLGISRRTLYRKLKKYG 418
 
Name Accession Description Interval E-value
AtoC COG2204
DNA-binding transcriptional response regulator, NtrC family, contains REC, AAA-type ATPase, ...
 7-407 1.21e-98

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: 300.73  E-value: 1.21e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280238   7 SILLIDDDADVLDAYTQLLEQAGYHVSACNNPFDAREQVPKDWPGIVLSDVCMPGCSGIDLMTVFHQDDDLLPILLITGH 86
Cdd:COG2204    4 RILVVDDDPDIRRLLKELLERAGYEVETAASGEEALALLREEPPDLVLLDLRMPGMDGLELLRELRALDPDLPVILLTGY 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280238  87 GDVPMAVEAVKKGAWDFLQKPIDPGKLLTLVDAALRQRQSVIARRQycqqklQVELIGRSQWTVRYRQRLQQLAETDIAV 166
Cdd:COG2204   84 GDVETAVEAIKAGAFDYLTKPFDLEELLAAVERALERRRLRRENAE------DSGLIGRSPAMQEVRRLIEKVAPSDATV 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280238 167 WLYGEPGTGRMTGARYLHQLGRHAEGPFIA--CELTPAN----------------AHTLNE-LIAQAQGGTLVLSHPEHL 227
Cdd:COG2204  158 LITGESGTGKELVARAIHRLSPRADGPFVAvnCAAIPEElleselfghekgaftgAVARRIgKFELADGGTLFLDEIGEM 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280238 228 THEQQHQLVQ-LQSHEKRP----------FRLIGIGSASLVELAASSQIVAELYYCFAMTQIGCQPLSKRPDDIEPLFHH 296
Cdd:COG2204  238 PLALQAKLLRvLQEREFERvggnkpipvdVRVIAATNRDLEELVEEGRFREDLYYRLNVFPIELPPLRERREDIPLLARH 317

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280238 297 YLQKTCQRLNHPVPeVDAGLLKGMMRRVWPNNVRELANAAELFAVgvlpLAETvnplmHIGEPTPLDQRVEDVERQIITE 376
Cdd:COG2204  318 FLARFAAELGKPVK-LSPEALEALLAYDWPGNVRELENVIERAVI----LADG-----EVITAEDLPEALEEVERELIER 387

                        410       420       430
                 ....*....|....*....|....*....|.
gi 490280238 377 ALNIHQGRINEVAEYLLIPRKKLYLRMKKYG 407
Cdd:COG2204  388 ALEETGGNVSRAAELLGISRRTLYRKLKKYG 418
REC_DctD-like cd17549
phosphoacceptor receiver (REC) domain of C4-dicarboxylic acid transport protein D (DctD) and ...
 8-136 3.49e-64

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: 201.95  E-value: 3.49e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280238   8 ILLIDDDADVLDAYTQLLEQAGYHVSACNNPFDAREQVPKDWPGIVLSDVCMPGCSGIDLMTVFHQDDDLLPILLITGHG 87
Cdd:cd17549    1 VLLVDDDADVREALQQTLELAGFRVRAFADAEEALAALSPDFPGVVISDIRMPGMDGLELLAQIRELDPDLPVILITGHG 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 490280238  88 DVPMAVEAVKKGAWDFLQKPIDPGKLLTLVDAALRQRQSVIARRQYCQQ 136
Cdd:cd17549   81 DVPMAVEAMRAGAYDFLEKPFDPERLLDVVRRALEKRRLVLENRRLRQQ 129
PRK11361 PRK11361
acetoacetate metabolism transcriptional regulator AtoC;
8-409 3.65e-42

acetoacetate metabolism transcriptional regulator AtoC;


Pssm-ID: 183099 [Multi-domain]  Cd Length: 457  Bit Score: 154.24  E-value: 3.65e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280238   8 ILLIDDDADVLDAYTQLLEQAGYHVSACNNPFDAREQVPKDWPGIVLSDVCMPGCSGIDLMTVFHQDDDLLPILLITGHG 87
Cdd:PRK11361   7 ILIVDDEDNVRRMLSTAFALQGFETHCANNGRTALHLFADIHPDVVLMDIRMPEMDGIKALKEMRSHETRTPVILMTAYA 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280238  88 DVPMAVEAVKKGAWDFLQKPIDPGKLLTLVDAALR---QRQSVIARRQYCQQKLQVELI-GRSQWTVRYRQRLQQLAETD 163
Cdd:PRK11361  87 EVETAVEALRCGAFDYVIKPFDLDELNLIVQRALQlqsMKKEIRHLHQALSTSWQWGHIlTNSPAMMDICKDTAKIALSQ 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280238 164 IAVWLYGEPGTGRMTGARYLHQLGRHAEGPFIA--CELTP----------------ANAHTLNE-LIAQAQGGTLVLSHP 224
Cdd:PRK11361 167 ASVLISGESGTGKELIARAIHYNSRRAKGPFIKvnCAALPeslleselfghekgafTGAQTLRQgLFERANEGTLLLDEI 246

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280238 225 EHLTHEQQHQLVQ-LQSHE----------KRPFRLIGIGSASLVELAASSQIVAELYYCFAMTQIGCQPLSKRPDDIEPL 293
Cdd:PRK11361 247 GEMPLVLQAKLLRiLQEREferigghqtiKVDIRIIAATNRDLQAMVKEGTFREDLFYRLNVIHLILPPLRDRREDISLL 326

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280238 294 FHHYLQKTCQRLNHPVPEVDAGLLKGMMRRVWPNNVRELANAAE---LFAVGVLPLAETVNPLMHIG-------EPTP-- 361
Cdd:PRK11361 327 ANHFLQKFSSENQRDIIDIDPMAMSLLTAWSWPGNIRELSNVIEravVMNSGPIIFSEDLPPQIRQPvcnagevKTAPvg 406

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|.
gi 490280238 362 ---LDQRVEDVERQIITEALNIHQGRINEVAEYLLIPRKKLYLRMKKYGLN 409
Cdd:PRK11361 407 ernLKEEIKRVEKRIIMEVLEQQEGNRTRTALMLGISRRALMYKLQEYGID 457
Response_reg pfam00072
Response regulator receiver domain; This domain receives the signal from the sensor partner in ...
 8-118 5.68e-35

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: 125.34  E-value: 5.68e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280238    8 ILLIDDDADVLDAYTQLLEQAGYHVSACNNPFDAREQVPKDWPGIVLSDVCMPGCSGIDLMTVFHQDDDLLPILLITGHG 87
Cdd:pfam00072   1 VLIVDDDPLIRELLRQLLEKEGYVVAEADDGKEALELLKEERPDLILLDINMPGMDGLELLKRIRRRDPTTPVIILTAHG 80

                          90       100       110
                  ....*....|....*....|....*....|.
gi 490280238   88 DVPMAVEAVKKGAWDFLQKPIDPGKLLTLVD 118
Cdd:pfam00072  81 DEDDAVEALEAGADDFLSKPFDPDELLAAIR 111
PEP_resp_reg TIGR02915
PEP-CTERM-box response regulator transcription factor; Members of this protein family share ...
 8-408 2.49e-34

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: 132.56  E-value: 2.49e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280238    8 ILLIDDDadvLDAYTQL-LEQAGYHVSACNNPFDAREQVPKDWPGIVLSDVCMP--GCSGIDLMTVFHQDDDLLP---IL 81
Cdd:TIGR02915   1 LLIVEDD---LGLQKQLkWSFADYELAVAADRESAIALVRRHEPAVVTLDLGLPpdADGASEGLAALQQILAIAPdtkVI 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280238   82 LITGHGDVPMAVEAVKKGAWDFLQKPIDPGKLLTLVDAALR----QRQSVIARRQYCQQKLQvELIGRSQWTVRYRQRLQ 157
Cdd:TIGR02915  78 VITGNDDRENAVKAIGLGAYDFYQKPIDPDVLKLIVDRAFHlytlETENRRLQSALGGTALR-GLITSSPGMQKICRTIE 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280238  158 QLAETDIAVWLYGEPGTGRMTGARYLHQLGRHAEGPFIA--CELTPAN----------------AH--TLNElIAQAQGG 217
Cdd:TIGR02915 157 KIAPSDITVLLLGESGTGKEVLARALHQLSDRKDKRFVAinCAAIPENlleselfgyekgaftgAVkqTLGK-IEYAHGG 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280238  218 TLVLSHPEHLTHEQQHQLVQ-LQS--------HEKRPF--RLIGIGSASLVELAASSQIVAELYYCFAMTQIGCQPLSKR 286
Cdd:TIGR02915 236 TLFLDEIGDLPLNLQAKLLRfLQErvierlggREEIPVdvRIVCATNQDLKRMIAEGTFREDLFYRIAEISITIPPLRSR 315

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280238  287 PDDIEPLFHHYLQKTCQRLNHPVPEVDAGLLKGMMRRVWPNNVRELANA---AELFAVGVLPLAETVNPLMHIGEPTP-- 361
Cdd:TIGR02915 316 DGDAVLLANAFLERFARELKRKTKGFTDDALRALEAHAWPGNVRELENKvkrAVIMAEGNQITAEDLGLDARERAETPle 395

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*....
gi 490280238  362 --LDQRVEDVERQIITEALNIHQGRINEVAEYLLIPRKKLYLRMKKYGL 408
Cdd:TIGR02915 396 vnLREVRERAEREAVRKAIARVDGNIARAAELLGITRPTLYDLMKKHGI 444
tetrathio_RR NF040749
tetrathionate respiration response regulator TtrR;
8-135 8.01e-25

tetrathionate respiration response regulator TtrR;


Pssm-ID: 468713 [Multi-domain]  Cd Length: 191  Bit Score: 100.51  E-value: 8.01e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280238   8 ILLIDDDADVLDAYTQLLEQAGYHVSACNNPFDAREQVPKDWPGIVLSDVCMPGCSGIDLMTVFHQDDDLLPILLITGHG 87
Cdd:NF040749   2 IHLVDDDVAVTDACRFLLESLGYEVQCWNDSEAFLAQADLYQEGVVLLDMRMPGLDGHQVHQALREQGSTLAVVFLTGHG 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 490280238  88 DVPMAVEAVKKGAWDFLQKPIDPGKLLTLVDAALRQRQSVIARRQYCQ 135
Cdd:NF040749  82 DVPMAVEQMKLGAVDFLQKPVSAAPLQAALERALAVSAAAFERHQIRQ 129
REC smart00448
cheY-homologous receiver domain; CheY regulates the clockwise rotation of E. coli flagellar ...
 7-60 2.00e-10

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: 56.04  E-value: 2.00e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 490280238     7 SILLIDDDADVLDAYTQLLEQAGYHVSACNNPFDAREQVPKDWPGIVLSDVCMP 60
Cdd:smart00448   2 RILVVDDDPLLRELLKALLEKEGYEVDEATDGEEALELLKEEKPDLILLDIMMP 55
 
Name Accession Description Interval E-value
AtoC COG2204
DNA-binding transcriptional response regulator, NtrC family, contains REC, AAA-type ATPase, ...
 7-407 1.21e-98

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: 300.73  E-value: 1.21e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280238   7 SILLIDDDADVLDAYTQLLEQAGYHVSACNNPFDAREQVPKDWPGIVLSDVCMPGCSGIDLMTVFHQDDDLLPILLITGH 86
Cdd:COG2204    4 RILVVDDDPDIRRLLKELLERAGYEVETAASGEEALALLREEPPDLVLLDLRMPGMDGLELLRELRALDPDLPVILLTGY 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280238  87 GDVPMAVEAVKKGAWDFLQKPIDPGKLLTLVDAALRQRQSVIARRQycqqklQVELIGRSQWTVRYRQRLQQLAETDIAV 166
Cdd:COG2204   84 GDVETAVEAIKAGAFDYLTKPFDLEELLAAVERALERRRLRRENAE------DSGLIGRSPAMQEVRRLIEKVAPSDATV 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280238 167 WLYGEPGTGRMTGARYLHQLGRHAEGPFIA--CELTPAN----------------AHTLNE-LIAQAQGGTLVLSHPEHL 227
Cdd:COG2204  158 LITGESGTGKELVARAIHRLSPRADGPFVAvnCAAIPEElleselfghekgaftgAVARRIgKFELADGGTLFLDEIGEM 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280238 228 THEQQHQLVQ-LQSHEKRP----------FRLIGIGSASLVELAASSQIVAELYYCFAMTQIGCQPLSKRPDDIEPLFHH 296
Cdd:COG2204  238 PLALQAKLLRvLQEREFERvggnkpipvdVRVIAATNRDLEELVEEGRFREDLYYRLNVFPIELPPLRERREDIPLLARH 317

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280238 297 YLQKTCQRLNHPVPeVDAGLLKGMMRRVWPNNVRELANAAELFAVgvlpLAETvnplmHIGEPTPLDQRVEDVERQIITE 376
Cdd:COG2204  318 FLARFAAELGKPVK-LSPEALEALLAYDWPGNVRELENVIERAVI----LADG-----EVITAEDLPEALEEVERELIER 387

                        410       420       430
                 ....*....|....*....|....*....|.
gi 490280238 377 ALNIHQGRINEVAEYLLIPRKKLYLRMKKYG 407
Cdd:COG2204  388 ALEETGGNVSRAAELLGISRRTLYRKLKKYG 418
REC_DctD-like cd17549
phosphoacceptor receiver (REC) domain of C4-dicarboxylic acid transport protein D (DctD) and ...
 8-136 3.49e-64

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: 201.95  E-value: 3.49e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280238   8 ILLIDDDADVLDAYTQLLEQAGYHVSACNNPFDAREQVPKDWPGIVLSDVCMPGCSGIDLMTVFHQDDDLLPILLITGHG 87
Cdd:cd17549    1 VLLVDDDADVREALQQTLELAGFRVRAFADAEEALAALSPDFPGVVISDIRMPGMDGLELLAQIRELDPDLPVILITGHG 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 490280238  88 DVPMAVEAVKKGAWDFLQKPIDPGKLLTLVDAALRQRQSVIARRQYCQQ 136
Cdd:cd17549   81 DVPMAVEAMRAGAYDFLEKPFDPERLLDVVRRALEKRRLVLENRRLRQQ 129
PRK11361 PRK11361
acetoacetate metabolism transcriptional regulator AtoC;
8-409 3.65e-42

acetoacetate metabolism transcriptional regulator AtoC;


Pssm-ID: 183099 [Multi-domain]  Cd Length: 457  Bit Score: 154.24  E-value: 3.65e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280238   8 ILLIDDDADVLDAYTQLLEQAGYHVSACNNPFDAREQVPKDWPGIVLSDVCMPGCSGIDLMTVFHQDDDLLPILLITGHG 87
Cdd:PRK11361   7 ILIVDDEDNVRRMLSTAFALQGFETHCANNGRTALHLFADIHPDVVLMDIRMPEMDGIKALKEMRSHETRTPVILMTAYA 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280238  88 DVPMAVEAVKKGAWDFLQKPIDPGKLLTLVDAALR---QRQSVIARRQYCQQKLQVELI-GRSQWTVRYRQRLQQLAETD 163
Cdd:PRK11361  87 EVETAVEALRCGAFDYVIKPFDLDELNLIVQRALQlqsMKKEIRHLHQALSTSWQWGHIlTNSPAMMDICKDTAKIALSQ 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280238 164 IAVWLYGEPGTGRMTGARYLHQLGRHAEGPFIA--CELTP----------------ANAHTLNE-LIAQAQGGTLVLSHP 224
Cdd:PRK11361 167 ASVLISGESGTGKELIARAIHYNSRRAKGPFIKvnCAALPeslleselfghekgafTGAQTLRQgLFERANEGTLLLDEI 246

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280238 225 EHLTHEQQHQLVQ-LQSHE----------KRPFRLIGIGSASLVELAASSQIVAELYYCFAMTQIGCQPLSKRPDDIEPL 293
Cdd:PRK11361 247 GEMPLVLQAKLLRiLQEREferigghqtiKVDIRIIAATNRDLQAMVKEGTFREDLFYRLNVIHLILPPLRDRREDISLL 326

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280238 294 FHHYLQKTCQRLNHPVPEVDAGLLKGMMRRVWPNNVRELANAAE---LFAVGVLPLAETVNPLMHIG-------EPTP-- 361
Cdd:PRK11361 327 ANHFLQKFSSENQRDIIDIDPMAMSLLTAWSWPGNIRELSNVIEravVMNSGPIIFSEDLPPQIRQPvcnagevKTAPvg 406

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|.
gi 490280238 362 ---LDQRVEDVERQIITEALNIHQGRINEVAEYLLIPRKKLYLRMKKYGLN 409
Cdd:PRK11361 407 ernLKEEIKRVEKRIIMEVLEQQEGNRTRTALMLGISRRALMYKLQEYGID 457
PRK10365 PRK10365
sigma-54-dependent response regulator transcription factor ZraR;
1-405 3.97e-41

sigma-54-dependent response regulator transcription factor ZraR;


Pssm-ID: 182412 [Multi-domain]  Cd Length: 441  Bit Score: 150.95  E-value: 3.97e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280238   1 MLSNNCSILLIDDDADVLDAYTQLLEQAGYHVSACNNPFDAREQVPKDWPGIVLSDVCMPGCSGIDLMTVFHQDDDLLPI 80
Cdd:PRK10365   1 MTHDNIDILVVDDDISHCTILQALLRGWGYNVALANSGRQALEQVREQVFDLVLCDVRMAEMDGIATLKEIKALNPAIPV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280238  81 LLITGHGDVPMAVEAVKKGAWDFLQKPIDPGKLLTLVDAALRQRQSVIARRQYCQQKlQVELIGRSQWTVRYRQRLQQLA 160
Cdd:PRK10365  81 LIMTAYSSVETAVEALKTGALDYLIKPLDFDNLQATLEKALAHTHSIDAETPAVTAS-QFGMVGKSPAMQHLLSEIALVA 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280238 161 ETDIAVWLYGEPGTGRMTGARYLHQLGRHAEGPFIACELTPANAHTL-NELIA------------------QAQGGTLVL 221
Cdd:PRK10365 160 PSEATVLIHGDSGTGKELVARAIHASSARSEKPLVTLNCAALNESLLeSELFGhekgaftgadkrregrfvEADGGTLFL 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280238 222 SHPEHLTHEQQHQLVQ-LQSHEKR----------PFRLIGIGSASLVELAASSQIVAELYYCFAMTQIGCQPLSKRPDDI 290
Cdd:PRK10365 240 DEIGDISPMMQVRLLRaIQEREVQrvgsnqtisvDVRLIAATHRDLAAEVNAGRFRQDLYYRLNVVAIEVPSLRQRREDI 319

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280238 291 EPLFHHYLQKTCQRLNHPVPEVDAGLLKGMMRRVWPNNVRELANAAELfAVGVLP---LAETVNPLMHIGEPTPLDQRVE 367
Cdd:PRK10365 320 PLLAGHFLQRFAERNRKAVKGFTPQAMDLLIHYDWPGNIRELENAVER-AVVLLTgeyISERELPLAIASTPIPLGQSQD 398

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|...
gi 490280238 368 -----DVERQIITEALNIHQGRINEVAEYLLIPRKKLYLRMKK 405
Cdd:PRK10365 399 iqplvEVEKEVILAALEKTGGNKTEAARQLGITRKTLLAKLSR 441
FixJ COG4566
DNA-binding response regulator, FixJ family, consists of REC and HTH domains [Signal ...
 8-139 5.22e-41

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: 144.09  E-value: 5.22e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280238   8 ILLIDDDADVLDAYTQLLEQAGYHVSACNNPFDAREQVPKDWPGIVLSDVCMPGCSGIDLMTVFHQDDDLLPILLITGHG 87
Cdd:COG4566    2 VYIVDDDEAVRDSLAFLLESAGLRVETFASAEAFLAALDPDRPGCLLLDVRMPGMSGLELQEELAARGSPLPVIFLTGHG 81

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 490280238  88 DVPMAVEAVKKGAWDFLQKPIDPGKLLTLVDAAL---RQRQSVIARRQYCQQKLQ 139
Cdd:COG4566   82 DVPMAVRAMKAGAVDFLEKPFDDQALLDAVRRALardRARRAERARRAELRARLA 136
RocR COG3829
RocR-type transcriptional regulator, contains PAS, AAA-type ATPase, and DNA-binding Fis ...
 109-409 7.45e-36

RocR-type transcriptional regulator, contains PAS, AAA-type ATPase, and DNA-binding Fis domains [Transcription, Signal transduction mechanisms];


Pssm-ID: 443041 [Multi-domain]  Cd Length: 448  Bit Score: 136.82  E-value: 7.45e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280238 109 DPGKLLTLVDAALRQRQSVIARRQYCQQklqvELIGRSQWTVRYRQRLQQLAETDIAVWLYGEpgTGrmTG----ARYLH 184
Cdd:COG3829  111 DITELKRLERKLREEELERGLSAKYTFD----DIIGKSPAMKELLELAKRVAKSDSTVLILGE--SG--TGkelfARAIH 182

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280238 185 QLGRHAEGPFIA--C----------EL--------TPANahtlNE----LIAQAQGGTL------------------VLs 222
Cdd:COG3829  183 NASPRRDGPFVAvnCaaipenllesELfgyekgafTGAK----KGgkpgLFELADGGTLfldeigemplslqakllrVL- 257

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280238 223 hpehltheQQHQLVQLQSHEKRP--FRLIgigSASLVELAASsqiVAE------LYYCFAMTQIGCQPLSKRPDDIEPLF 294
Cdd:COG3829  258 --------QEKEVRRVGGTKPIPvdVRII---AATNRDLEEM---VEEgrfredLYYRLNVIPIHIPPLRERKEDIPLLA 323

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280238 295 HHYLQKTCQRLNHPVPEVDAGLLKGMMRRVWPNNVRELANAAE---LFAVG------VLP--LAETVNPlMHIGEPTPLD 363
Cdd:COG3829  324 EHFLEKFNKKYGKNIKGISPEALELLLAYDWPGNVRELENVIEravVLSEGdvitpeHLPeyLLEEAEA-ASAAEEGSLK 402

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*.
gi 490280238 364 QRVEDVERQIITEALNIHQGRINEVAEYLLIPRKKLYLRMKKYGLN 409
Cdd:COG3829  403 EALEEVEKELIEEALEKTGGNKSKAAKALGISRSTLYRKLKKYGIK 448
Response_reg pfam00072
Response regulator receiver domain; This domain receives the signal from the sensor partner in ...
 8-118 5.68e-35

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: 125.34  E-value: 5.68e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280238    8 ILLIDDDADVLDAYTQLLEQAGYHVSACNNPFDAREQVPKDWPGIVLSDVCMPGCSGIDLMTVFHQDDDLLPILLITGHG 87
Cdd:pfam00072   1 VLIVDDDPLIRELLRQLLEKEGYVVAEADDGKEALELLKEERPDLILLDINMPGMDGLELLKRIRRRDPTTPVIILTAHG 80

                          90       100       110
                  ....*....|....*....|....*....|.
gi 490280238   88 DVPMAVEAVKKGAWDFLQKPIDPGKLLTLVD 118
Cdd:pfam00072  81 DEDDAVEALEAGADDFLSKPFDPDELLAAIR 111
PEP_resp_reg TIGR02915
PEP-CTERM-box response regulator transcription factor; Members of this protein family share ...
 8-408 2.49e-34

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: 132.56  E-value: 2.49e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280238    8 ILLIDDDadvLDAYTQL-LEQAGYHVSACNNPFDAREQVPKDWPGIVLSDVCMP--GCSGIDLMTVFHQDDDLLP---IL 81
Cdd:TIGR02915   1 LLIVEDD---LGLQKQLkWSFADYELAVAADRESAIALVRRHEPAVVTLDLGLPpdADGASEGLAALQQILAIAPdtkVI 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280238   82 LITGHGDVPMAVEAVKKGAWDFLQKPIDPGKLLTLVDAALR----QRQSVIARRQYCQQKLQvELIGRSQWTVRYRQRLQ 157
Cdd:TIGR02915  78 VITGNDDRENAVKAIGLGAYDFYQKPIDPDVLKLIVDRAFHlytlETENRRLQSALGGTALR-GLITSSPGMQKICRTIE 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280238  158 QLAETDIAVWLYGEPGTGRMTGARYLHQLGRHAEGPFIA--CELTPAN----------------AH--TLNElIAQAQGG 217
Cdd:TIGR02915 157 KIAPSDITVLLLGESGTGKEVLARALHQLSDRKDKRFVAinCAAIPENlleselfgyekgaftgAVkqTLGK-IEYAHGG 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280238  218 TLVLSHPEHLTHEQQHQLVQ-LQS--------HEKRPF--RLIGIGSASLVELAASSQIVAELYYCFAMTQIGCQPLSKR 286
Cdd:TIGR02915 236 TLFLDEIGDLPLNLQAKLLRfLQErvierlggREEIPVdvRIVCATNQDLKRMIAEGTFREDLFYRIAEISITIPPLRSR 315

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280238  287 PDDIEPLFHHYLQKTCQRLNHPVPEVDAGLLKGMMRRVWPNNVRELANA---AELFAVGVLPLAETVNPLMHIGEPTP-- 361
Cdd:TIGR02915 316 DGDAVLLANAFLERFARELKRKTKGFTDDALRALEAHAWPGNVRELENKvkrAVIMAEGNQITAEDLGLDARERAETPle 395

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*....
gi 490280238  362 --LDQRVEDVERQIITEALNIHQGRINEVAEYLLIPRKKLYLRMKKYGL 408
Cdd:TIGR02915 396 vnLREVRERAEREAVRKAIARVDGNIARAAELLGITRPTLYDLMKKHGI 444
PRK15115 PRK15115
response regulator GlrR; Provisional
 1-415 2.82e-34

response regulator GlrR; Provisional


Pssm-ID: 185070 [Multi-domain]  Cd Length: 444  Bit Score: 132.27  E-value: 2.82e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280238   1 MLSNNCSILLIDDDADVLDAYTQLLEQAGYHVSACNNPFDAREQVPKDWPGIVLSDVCMPGCSGIDLMTVFHQDDDLLPI 80
Cdd:PRK15115   1 MSRKPAHLLLVDDDPGLLKLLGMRLTSEGYSVVTAESGQEALRVLNREKVDLVISDLRMDEMDGMQLFAEIQKVQPGMPV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280238  81 LLITGHGDVPMAVEAVKKGAWDFLQKPIDPGKLLTLVDAALRQRQSVIarrqycQQKLQVELIGRSQWTVRYRQRLQQLA 160
Cdd:PRK15115  81 IILTAHGSIPDAVAATQQGVFSFLTKPVDRDALYKAIDDALEQSAPAT------DERWREAIVTRSPLMLRLLEQARMVA 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280238 161 ETDIAVWLYGEPGTGRMTGARYLHQLGRHAEGPFIA--CELTP----------------ANAHTLNE-LIAQAQGGTLVL 221
Cdd:PRK15115 155 QSDVSVLINGQSGTGKEILAQAIHNASPRASKPFIAinCGALPeqlleselfghargafTGAVSNREgLFQAAEGGTLFL 234

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280238 222 SHPEHLTHEQQHQLVQ-LQSHEKRPF----------RLIGIGSASLVELAASSQIVAELYYCFAMTQIGCQPLSKRPDDI 290
Cdd:PRK15115 235 DEIGDMPAPLQVKLLRvLQERKVRPLgsnrdididvRIISATHRDLPKAMARGEFREDLYYRLNVVSLKIPALAERTEDI 314

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280238 291 EPLFHHYLQKTCQRLNHPVPEVDAGLLKGMMRRVWPNNVRELANAAE----LFAVGVLPLAETVNPLMhiGEPTPLDQRV 366
Cdd:PRK15115 315 PLLANHLLRQAAERHKPFVRAFSTDAMKRLMTASWPGNVRQLVNVIEqcvaLTSSPVISDALVEQALE--GENTALPTFV 392

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|..
gi 490280238 367 E---DVERQIITEALNIHQGRINEVAEYLLIPRKKLYLRMKKYGLNKEHYKG 415
Cdd:PRK15115 393 EarnQFELNYLRKLLQITKGNVTHAARMAGRNRTEFYKLLSRHELDANDFKE 444
REC_FixJ cd17537
phosphoacceptor receiver (REC) domain of FixJ family response regulators; FixJ family response ...
 8-121 1.84e-32

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: 118.85  E-value: 1.84e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280238   8 ILLIDDDADVLDAYTQLLEQAGYHVSACNNPFDAREQVPKDWPGIVLSDVCMPGCSGIDLMTVFHQDDDLLPILLITGHG 87
Cdd:cd17537    3 VYVVDDDEAVRDSLAFLLRSVGLAVKTFTSASAFLAAAPPDQPGCLVLDVRMPGMSGLELQDELLARGSNIPIIFITGHG 82

                         90       100       110
                 ....*....|....*....|....*....|....
gi 490280238  88 DVPMAVEAVKKGAWDFLQKPIDPGKLLTLVDAAL 121
Cdd:cd17537   83 DVPMAVEAMKAGAVDFLEKPFRDQVLLDAIEQAL 116
AcoR COG3284
Transcriptional regulator DhaR of acetoin/glycerol metabolism [Transcription];
141-407 1.73e-31

Transcriptional regulator DhaR of acetoin/glycerol metabolism [Transcription];


Pssm-ID: 442514 [Multi-domain]  Cd Length: 625  Bit Score: 126.55  E-value: 1.73e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280238 141 ELIGRSQWTVRYRQRLQQLAETDIAVWLYGEPGTGRMTGARYLHQLGRHAEGPFIA--C----------EL--------T 200
Cdd:COG3284  322 ALAGGDPAMRRALRRARRLADRDIPVLILGETGTGKELFARAIHAASPRADGPFVAvnCaaipeeliesELfgyepgafT 401

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280238 201 PANAHTLNELIAQAQGGTLVLSHPEHLTHEQQ---------HQLVQLQSHEKRP--FRLIGIGSASLVELAASSQIVAEL 269
Cdd:COG3284  402 GARRKGRPGKIEQADGGTLFLDEIGDMPLALQarllrvlqeREVTPLGGTKPIPvdVRLIAATHRDLRELVAAGRFREDL 481

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280238 270 YYCFAMTQIGCQPLSKRpDDIEPLFHHYLQKTCQRlnHPVPEVDAGLLKGMMRRVWPNNVRELAN----AAELFAVGVLP 345
Cdd:COG3284  482 YYRLNGLTLTLPPLRER-EDLPALIEHLLRELAAG--RGPLRLSPEALALLAAYPWPGNVRELRNvlrtALALADGGVIT 558

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490280238 346 LA---ETVNPLMHIGEPTPLDQ--RVEDVERQIITEALNIHQGRINEVAEYLLIPRKKLYLRMKKYG 407
Cdd:COG3284  559 VEdlpDELRAELAAAAPAAAAPltSLEEAERDAILRALRACGGNVSAAARALGISRSTLYRKLKRYG 625
glnG PRK10923
nitrogen regulation protein NR(I); Provisional
 8-408 1.15e-30

nitrogen regulation protein NR(I); Provisional


Pssm-ID: 182842 [Multi-domain]  Cd Length: 469  Bit Score: 122.67  E-value: 1.15e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280238   8 ILLIDDDADVLDAYTQLLEQAGYHVSACNNPFDAREQVPKDWPGIVLSDVCMPGCSGIDLMTVFHQDDDLLPILLITGHG 87
Cdd:PRK10923   6 VWVVDDDSSIRWVLERALAGAGLTCTTFENGNEVLEALASKTPDVLLSDIRMPGMDGLALLKQIKQRHPMLPVIIMTAHS 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280238  88 DVPMAVEAVKKGAWDFLQKPIDPGKLLTLVDAALRQRQSVIARRQYCQQKLQVELIGRSQWTVRYRQRLQQLAETDIAVW 167
Cdd:PRK10923  86 DLDAAVSAYQQGAFDYLPKPFDIDEAVALVERAISHYQEQQQPRNIQVNGPTTDIIGEAPAMQDVFRIIGRLSRSSISVL 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280238 168 LYGEPGTGRMTGARYLHQLGRHAEGPFIACEL--------------------TPANaHTLNELIAQAQGGTLVLSHPEHL 227
Cdd:PRK10923 166 INGESGTGKELVAHALHRHSPRAKAPFIALNMaaipkdlieselfghekgafTGAN-TIRQGRFEQADGGTLFLDEIGDM 244

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280238 228 THEQQHQLVQLQSHE-----------KRPFRLIGIGSASLVELAASSQIVAELYYCFAMTQIGCQPLSKRPDDIEPLFHH 296
Cdd:PRK10923 245 PLDVQTRLLRVLADGqfyrvggyapvKVDVRIIAATHQNLEQRVQEGKFREDLFHRLNVIRVHLPPLRERREDIPRLARH 324

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280238 297 YLQKTCQRLN------HPVPEVdagllkGMMRRVWPNNVRELANA-------------------AELF-------AVGVL 344
Cdd:PRK10923 325 FLQVAARELGveakllHPETEA------ALTRLAWPGNVRQLENTcrwltvmaagqevliqdlpGELFestvpesTSQMQ 398

                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280238 345 P------LAETVNPLMHIGEPTPLDQRVEDVERQIITEALNIHQGRINEVAEYLLIPRKKLYLRMKKYGL 408
Cdd:PRK10923 399 PdswatlLAQWADRALRSGHQNLLSEAQPELERTLLTTALRHTQGHKQEAARLLGWGRNTLTRKLKELGM 468
RpfG COG3437
Response regulator c-di-GMP phosphodiesterase, RpfG family, contains REC and HD-GYP domains ...
 7-136 3.73e-29

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: 113.34  E-value: 3.73e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280238   7 SILLIDDDADVLDAYTQLLEQAGYHVSACNNPFDAREQVPKDWPGIVLSDVCMPGCSGIDLMTVFHQDDDL--LPILLIT 84
Cdd:COG3437    8 TVLIVDDDPENLELLRQLLRTLGYDVVTAESGEEALELLLEAPPDLILLDVRMPGMDGFELLRLLRADPSTrdIPVIFLT 87

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 490280238  85 GHGDVPMAVEAVKKGAWDFLQKPIDPGKLLTLVDAALRQRQSVIARRQYCQQ 136
Cdd:COG3437   88 ALADPEDRERALEAGADDYLTKPFDPEELLARVRNALELRRLQRELDDLVLY 139
FhlA COG3604
FhlA-type transcriptional regulator, contains GAF, AAA-type ATPase, and DNA-binding Fis ...
 138-409 6.01e-29

FhlA-type transcriptional regulator, contains GAF, AAA-type ATPase, and DNA-binding Fis domains [Transcription, Signal transduction mechanisms];


Pssm-ID: 442823 [Multi-domain]  Cd Length: 338  Bit Score: 115.72  E-value: 6.01e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280238 138 LQVELIGRSQWTVRYRQRLQQLAETdIAVWLYGEPGTGRMTGARYLHQLGRHAEGPFIA--CELTPANahtlneLIAQAQ 215
Cdd:COG3604   91 LTLDSRRPGAFSEEDLRLLETLASL-AAVAILGETGTGKELVANAIHELSPRADKPFVKvnCAALPES------LLESLQ 163

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280238 216 ggtlvlshpehlthEQQHQLVQLQSHEKRPFRLIGIGSASLVELAASSQIVAELYYCFAMTQIGCQPLSKRPDDIEPLFH 295
Cdd:COG3604  164 --------------EGEFERVGGDETIKVDVRIIAATNRDLEEEVAEGRFREDLYYRLNVFPIRLPPLRERREDIPLLAE 229

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280238 296 HYLQKTCQRLNHPVPEVDAGLLKGMMRRVWPNNVRELANAAELFAVgvlpLAEtvNPLMHIGEPTPLD-QRVEDVERQII 374
Cdd:COG3604  230 HFLEKFSRRLGKPILRLSPEALEALMAYPWPGNVRELENVIERAVI----LAE--GGVLDADDLAPGSrEALEEVEREHI 303

                        250       260       270
                 ....*....|....*....|....*....|....*
gi 490280238 375 TEALNIHQGRINEVAEYLLIPRKKLYLRMKKYGLN 409
Cdd:COG3604  304 LEALERTGGNIAGAARLLGLTPSTLRSRMKKLGIK 338
fixJ PRK09390
response regulator FixJ; Provisional
 11-125 6.75e-29

response regulator FixJ; Provisional


Pssm-ID: 181815 [Multi-domain]  Cd Length: 202  Bit Score: 112.02  E-value: 6.75e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280238  11 IDDDADVLDAYTQLLEQAGYHVSACNNPFDAREQVPKDWPGIVLSDVCMPGCSGIDLMTVFHQDDDLLPILLITGHGDVP 90
Cdd:PRK09390   9 VDDDEAMRDSLAFLLDSAGFEVRLFESAQAFLDALPGLRFGCVVTDVRMPGIDGIELLRRLKARGSPLPVIVMTGHGDVP 88

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 490280238  91 MAVEAVKKGAWDFLQKPIDPGKLLTLVDAALRQRQ 125
Cdd:PRK09390  89 LAVEAMKLGAVDFIEKPFEDERLIGAIERALAQAP 123
REC cd00156
phosphoacceptor receiver (REC) domain of response regulators (RRs) and pseudo response ...
 9-107 6.69e-28

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: 105.77  E-value: 6.69e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280238   9 LLIDDDADVLDAYTQLLEQAGYHVSACNNPFDAREQVPKDWPGIVLSDVCMPGCSGIDLMTVFHQDDDLLPILLITGHGD 88
Cdd:cd00156    1 LIVDDDPAIRELLKSLLEREGYEVDTAADGEEALELLREERPDLVLLDLMMPGMDGLELLRKLRELPPDIPVIVLTAKAD 80

                         90
                 ....*....|....*....
gi 490280238  89 VPMAVEAVKKGAWDFLQKP 107
Cdd:cd00156   81 EEDAVRALELGADDYLVKP 99
REC_NtrX-like cd17550
phosphoacceptor receiver (REC) domain of nitrogen assimilation regulatory protein NtrX and ...
 8-122 2.56e-27

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: 104.89  E-value: 2.56e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280238   8 ILLIDDDADVLDAYTQLLEQAGYHVSACNNPFDAREQVPKDWPGIVLSDVCMPGCSGIDLMTVFHQDDDLLPILLITGHG 87
Cdd:cd17550    1 ILIVDDEEDIRESLSGILEDEGYEVDTAADGEEALKLIKERRPDLVLLDIWLPDMDGLELLKEIKEKYPDLPVIMISGHG 80

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 490280238  88 DVPMAVEAVKKGAWDFLQKPIDPGKLLTLVDAALR 122
Cdd:cd17550   81 TIETAVKATKLGAYDFIEKPLSLDRLLLTIERALE 115
PleD COG3706
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate ...
 7-122 1.22e-26

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


Pssm-ID: 442920 [Multi-domain]  Cd Length: 179  Bit Score: 104.99  E-value: 1.22e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280238   7 SILLIDDDADVLDAYTQLLEQAGYHVSACNNPFDAREQVPKDWPGIVLSDVCMPGCSGIDLMTVFHQDDDL--LPILLIT 84
Cdd:COG3706    3 RILVVDDDPTNRKLLRRLLEAAGYEVVEAADGEEALELLQEHRPDLILLDLEMPDMDGLELCRRLRADPRTadIPIIFLT 82

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 490280238  85 GHGDVPMAVEAVKKGAWDFLQKPIDPGKLLTLVDAALR 122
Cdd:COG3706   83 ALDDEEDRARALEAGADDYLTKPFDPEELLARVDLVAR 120
CheY COG0784
CheY-like REC (receiver) domain, includes chemotaxis protein CheY and sporulation regulator ...
 8-126 5.99e-25

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


Pssm-ID: 440547 [Multi-domain]  Cd Length: 128  Bit Score: 98.77  E-value: 5.99e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280238   8 ILLIDDDADVLDAYTQLLEQAGYHVSACNNPFDAREQVPKDWPGIVLSDVCMPGCSGIDLMTVFHQDDDL--LPILLITG 85
Cdd:COG0784    8 ILVVDDNPDNRELLRRLLERLGYEVTTAEDGAEALELLRAGPPDLILLDINMPGMDGLELLRRIRALPRLpdIPIIALTA 87

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 490280238  86 HGDVPMAVEAVKKGAWDFLQKPIDPGKLLTLVDAALRQRQS 126
Cdd:COG0784   88 YADEEDRERALEAGADDYLTKPVDPEELLEALRRLLARASA 128
tetrathio_RR NF040749
tetrathionate respiration response regulator TtrR;
8-135 8.01e-25

tetrathionate respiration response regulator TtrR;


Pssm-ID: 468713 [Multi-domain]  Cd Length: 191  Bit Score: 100.51  E-value: 8.01e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280238   8 ILLIDDDADVLDAYTQLLEQAGYHVSACNNPFDAREQVPKDWPGIVLSDVCMPGCSGIDLMTVFHQDDDLLPILLITGHG 87
Cdd:NF040749   2 IHLVDDDVAVTDACRFLLESLGYEVQCWNDSEAFLAQADLYQEGVVLLDMRMPGLDGHQVHQALREQGSTLAVVFLTGHG 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 490280238  88 DVPMAVEAVKKGAWDFLQKPIDPGKLLTLVDAALRQRQSVIARRQYCQ 135
Cdd:NF040749  82 DVPMAVEQMKLGAVDFLQKPVSAAPLQAALERALAVSAAAFERHQIRQ 129
OmpR COG0745
DNA-binding response regulator, OmpR family, contains REC and winged-helix (wHTH) domain ...
 8-159 8.94e-25

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: 100.80  E-value: 8.94e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280238   8 ILLIDDDADVLDAYTQLLEQAGYHVSACNNPFDAREQVPKDWPGIVLSDVCMPGCSGIDLMTVFHQDDDLLPILLITGHG 87
Cdd:COG0745    4 ILVVEDDPDIRELLADALEREGYEVDTAADGEEALELLEEERPDLILLDLMLPGMDGLEVCRRLRARPSDIPIIMLTARD 83

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490280238  88 DVPMAVEAVKKGAWDFLQKPIDPGKLLTLVDAALRQRQSVIARRQycqqklqvELIGRSQWTVRYRQRLQQL 159
Cdd:COG0745   84 DEEDRVRGLEAGADDYLTKPFDPEELLARIRALLRRRAAEVLRVG--------DLLDLAAREVTRDGEPVEL 147
PRK11388 PRK11388
DNA-binding transcriptional regulator DhaR; Provisional
 157-414 2.86e-23

DNA-binding transcriptional regulator DhaR; Provisional


Pssm-ID: 183114 [Multi-domain]  Cd Length: 638  Bit Score: 102.06  E-value: 2.86e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280238 157 QQLAETDIAVWLYGEPGTGRMTGARYLHQLGRHAEGPFIA--CELTPANAhTLNELIAQ---------------AQGGTL 219
Cdd:PRK11388 342 RQAAKSSFPVLLCGEEGVGKALLAQAIHNESERAAGPYIAvnCQLYPDEA-LAEEFLGSdrtdsengrlskfelAHGGTL 420

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280238 220 VLSHPEHLTHEQQHQLVQL---------QSHEKRP--FRLIGIGSASLVELAASSQIVAELYYCFAMTQIGCQPLSKRPD 288
Cdd:PRK11388 421 FLEKVEYLSPELQSALLQVlktgvitrlDSRRLIPvdVRVIATTTADLAMLVEQNRFSRQLYYALHAFEITIPPLRMRRE 500

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280238 289 DIEPLFHHYLQKTCQRLNHPVpEVDAGLLKGMMRRVWPNNVRELANAAELFAV----GVLPLAETVNPLMH-------IG 357
Cdd:PRK11388 501 DIPALVNNKLRSLEKRFSTRL-KIDDDALARLVSYRWPGNDFELRSVIENLALssdnGRIRLSDLPEHLFTeqatddvSA 579

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 490280238 358 EPTPLDQRVEDVERQIITEALNIHQGRINEVAEYLLIPRKKLYLRMKKYGL--NKEHYK 414
Cdd:PRK11388 580 TRLSTSLSLAELEKEAIINAAQVCGGRIQEMAALLGIGRTTLWRKMKQHGIdaGQFKRR 638
REC_NtrC1-like cd17572
phosphoacceptor receiver (REC) domain of nitrogen regulatory protein C 1 (NtrC1) from Aquifex ...
 8-125 5.15e-22

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: 90.72  E-value: 5.15e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280238   8 ILLIDDDADVLDAYTQLLEQAGYHVSACNNPFDAREQVPKDWPGIVLSDVCMPGCSGIDLMTVFHQDDDLLPILLITGHG 87
Cdd:cd17572    1 VLLVEDSPSLAALYQEYLSDEGYKVTHVETGKEALAFLSDQPPDVVLLDLKLPDMSGMEILKWIQERSLPTSVIVITAHG 80

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 490280238  88 DVPMAVEAVKKGAWDFLQKPIDPGKLLTLVDAALRQRQ 125
Cdd:cd17572   81 SVDIAVEAMRLGAYDFLEKPFDADRLRVTVRNALKHRK 118
COG4567 COG4567
DNA-binding response regulator, ActR/RegA family, consists of REC and Fis-type HTH domains ...
 7-126 1.42e-20

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: 88.43  E-value: 1.42e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280238   7 SILLIDDDADVLDAYTQLLEQAGYHVSACNNPFDAREQVPKDWPGIVLSDVCMPGCSGIDLMTVFHQDDDLLPILLITGH 86
Cdd:COG4567    6 SLLLVDDDEAFARVLARALERRGFEVTTAASVEEALALLEQAPPDYAVLDLRLGDGSGLDLIEALRERDPDARIVVLTGY 85

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 490280238  87 GDVPMAVEAVKKGAWDFLQKPIDPGKLLtlvdAALRQRQS 126
Cdd:COG4567   86 ASIATAVEAIKLGADDYLAKPADADDLL----AALERAEG 121
CitB COG4565
DNA-binding response regulator DpiB of citrate/malate metabolism [Transcription, Signal ...
 8-132 1.80e-20

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


Pssm-ID: 443622 [Multi-domain]  Cd Length: 138  Bit Score: 86.95  E-value: 1.80e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280238   8 ILLIDDDADVLDAYTQLLEQ-AGYHVSA-CNNPFDAREQVPKDWPGIVLSDVCMPGCSGIDLMTVFHQDDDLLPILLITG 85
Cdd:COG4565    6 VLIVEDDPMVAELLRRYLERlPGFEVVGvASSGEEALALLAEHRPDLILLDIYLPDGDGLELLRELRARGPDVDVIVITA 85

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 490280238  86 HGDVPMAVEAVKKGAWDFLQKPIDPGKLLTLVDAALRQRQSVIARRQ 132
Cdd:COG4565   86 ARDPETVREALRAGVVDYLIKPFTFERLREALERYLEYRRLLREDQE 132
REC_RpfG-like cd17551
phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase response regulator ...
 8-110 2.92e-20

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: 85.57  E-value: 2.92e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280238   8 ILLIDDDADVLDAYTQLLEQAGY-HVSACNNPFDAREQVPKDWPGIVLSDVCMPGCSGIDLMTVFHQD--DDLLPILLIT 84
Cdd:cd17551    3 ILIVDDNPTNLLLLEALLRSAGYlEVVSFTDPREALAWCRENPPDLILLDYMMPGMDGLEFIRRLRALpgLEDVPIVMIT 82

                         90       100
                 ....*....|....*....|....*.
gi 490280238  85 GHGDVPMAVEAVKKGAWDFLQKPIDP 110
Cdd:cd17551   83 ADTDREVRLRALEAGATDFLTKPFDP 108
REC_NtrC cd19919
phosphoacceptor receiver (REC) domain of DNA-binding transcriptional regulator NtrC; ...
 7-121 1.90e-19

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: 83.48  E-value: 1.90e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280238   7 SILLIDDDADVLDAYTQLLEQAGYHVSACNNPFDAREQVPKDWPGIVLSDVCMPGCSGIDLMTVFHQDDDLLPILLITGH 86
Cdd:cd19919    2 TVWIVDDDSSIRWVLERALAGAGLTVTSFENAQEALAALASSQPDVLISDIRMPGMDGLALLAQIKQRHPDLPVIIMTAH 81

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 490280238  87 GDVPMAVEAVKKGAWDFLQKPIDPGKLLTLVDAAL 121
Cdd:cd19919   82 SDLDSAVSAYQGGAFEYLPKPFDIDEAVALVERAI 116
REC_RegA-like cd17563
phosphoacceptor receiver (REC) domain of photosynthetic apparatus regulatory protein RegA; ...
 7-109 4.01e-19

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: 82.11  E-value: 4.01e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280238   7 SILLIDDDADVLDAYTQLLEQAGYHVSACNNPFDAREQVPKDWPGIVLSDVCMPGCSGIDLMTVFHQDDDLLPILLITGH 86
Cdd:cd17563    2 SLLLVDDDEVFAERLARALERRGFEVETAHSVEEALALAREEKPDYAVLDLRLGGDSGLDLIPPLRALQPDARIVVLTGY 81

                         90       100
                 ....*....|....*....|...
gi 490280238  87 GDVPMAVEAVKKGAWDFLQKPID 109
Cdd:cd17563   82 ASIATAVEAIKLGADDYLAKPAD 104
YesN COG4753
Two-component response regulator, YesN/AraC family, consists of REC and AraC-type DNA-binding ...
 7-107 6.85e-19

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


Pssm-ID: 443786 [Multi-domain]  Cd Length: 103  Bit Score: 81.36  E-value: 6.85e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280238   7 SILLIDDDADVLDAYTQLLEQ-AGYH-VSACNNPFDAREQVPKDWPGIVLSDVCMPGCSGIDLMTVFHQDDDLLPILLIT 84
Cdd:COG4753    1 KVLIVDDEPLIREGLKRILEWeAGFEvVGEAENGEEALELLEEHKPDLVITDINMPGMDGLELLEAIRELDPDTKIIILS 80

                         90       100
                 ....*....|....*....|...
gi 490280238  85 GHGDVPMAVEAVKKGAWDFLQKP 107
Cdd:COG4753   81 GYSDFEYAQEAIKLGADDYLLKP 103
REC_HupR-like cd17569
phosphoacceptor receiver (REC) domain of hydrogen uptake protein regulator (HupR) and similar ...
 7-122 3.36e-18

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: 79.75  E-value: 3.36e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280238   7 SILLIDDDADVLDAYTQLLEQAGYHVSACNNPFDAREQVPKDWPGIVLSDVCMPGCSGIDLMTVFHQDD-DLLPILLiTG 85
Cdd:cd17569    2 TILLVDDEPNILKALKRLLRREGYEVLTATSGEEALEILKQEPVDVVISDQRMPGMDGAELLKRVRERYpDTVRILL-TG 80

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 490280238  86 HGDVPMAVEAVKKGA-WDFLQKPIDPGKLLTLVDAALR 122
Cdd:cd17569   81 YADLDAAIEAINEGEiYRFLTKPWDDEELKETIRQALE 118
REC_RssB-like cd17555
phosphoacceptor receiver (REC) domain of Pseudomonas aeruginosa RssB and similar domains; ...
 7-108 4.99e-18

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: 79.17  E-value: 4.99e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280238   7 SILLIDDDADVLDAYTQLLEQAGYHVSACNNPFDAREQVPKDWPGIVLSDVCMPGCSGIDLMTVFHQDDDLLPILLITGH 86
Cdd:cd17555    2 TILVIDDDEVVRESIAAYLEDSGFQVLQAADGRQGLELFRSEQPDLVLCDLRMPEMDGLEVLKQITKESPDTPVIVVSGA 81

                         90       100
                 ....*....|....*....|..
gi 490280238  87 GDVPMAVEAVKKGAWDFLQKPI 108
Cdd:cd17555   82 GVMSDAVEALRLGAWDYLTKPI 103
AmiR COG3707
Two-component response regulator, AmiR/NasT family, consists of REC and RNA-binding ...
 7-132 6.24e-18

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: 81.54  E-value: 6.24e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280238   7 SILLIDDDADVLDAYTQLLEQAGYHVSA-CNNPFDAREQVPKDWPGIVLSDVCMPGCSGIDLMTVFHQDDdLLPILLITG 85
Cdd:COG3707    5 RVLVVDDEPLRRADLREGLREAGYEVVAeAADGEDAVELVRELKPDLVIVDIDMPDRDGLEAARQISEER-PAPVILLTA 83

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 490280238  86 HGDVPMAVEAVKKGAWDFLQKPIDPGKLLTLVDAALRQRQSVIARRQ 132
Cdd:COG3707   84 YSDPELIERALEAGVSAYLVKPLDPEDLLPALELALARFRELRALRR 130
REC_OmpR_CpxR cd17623
phosphoacceptor receiver (REC) domain of CpxR-like OmpR family response regulators; CpxR is ...
 8-122 1.23e-16

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: 75.42  E-value: 1.23e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280238   8 ILLIDDDADVLDAYTQLLEQAGYHVSACNNPFDAREQVPKDWPGIVLSDVCMPGCSGIDLMTVFHQDDDlLPILLITGHG 87
Cdd:cd17623    1 ILLIDDDRELTELLTEYLEMEGFNVRAAHDGEQGLAALLEGSPDLVVLDVMLPKMNGLDVLKELRKTSQ-VPVLMLTARG 79

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 490280238  88 DVPMAVEAVKKGAWDFLQKPIDPGKLLTLVDAALR 122
Cdd:cd17623   80 DDIDRILGLELGADDYLPKPFNPRELVARIRAILR 114
PRK15424 PRK15424
propionate catabolism operon regulatory protein PrpR; Provisional
 141-405 1.41e-16

propionate catabolism operon regulatory protein PrpR; Provisional


Pssm-ID: 237963 [Multi-domain]  Cd Length: 538  Bit Score: 81.69  E-value: 1.41e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280238 141 ELIGRSQWTVRYRQRLQQLAETDIAVWLYGEPGTGRMTGARYLHQ---------LGRHAeGPFIA--CEltpANAHTLNE 209
Cdd:PRK15424 220 DLLGQSPQMEQVRQTILLYARSSAAVLIQGETGTGKELAAQAIHReyfarhdarQGKKS-HPFVAvnCG---AIAESLLE 295

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280238 210 ---------------------LIAQAQGGTLVLSHPEHLTHEQQHQLVQ-LQSHE------KRPF----RLIGIGSASLV 257
Cdd:PRK15424 296 aelfgyeegaftgsrrggragLFEIAHGGTLFLDEIGEMPLPLQTRLLRvLEEKEvtrvggHQPVpvdvRVISATHCDLE 375

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280238 258 ELAASSQIVAELYYCFAMTQIGCQPLSKRPDDIEPLFHHYLQKTCQRLNHPV-PEVDAGLLK---GMMRRVWPNNVRELA 333
Cdd:PRK15424 376 EDVRQGRFRRDLFYRLSILRLQLPPLRERVADILPLAESFLKQSLAALSAPFsAALRQGLQQcetLLLHYDWPGNVRELR 455

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490280238 334 NAAELFAV--GVLPLAETVNPLMHIGEP----TPLDQRVEDVERQIITEALNIHQGRINEVAEYLLIPRKKLYLRMKK 405
Cdd:PRK15424 456 NLMERLALflSVEPTPDLTPQFLQLLLPelarESAKTPAPRLLAATLQQALERFNGDKTAAANYLGISRTTLWRRLKA 533
PRK15429 PRK15429
formate hydrogenlyase transcriptional activator FlhA;
141-411 3.84e-16

formate hydrogenlyase transcriptional activator FlhA;


Pssm-ID: 237965 [Multi-domain]  Cd Length: 686  Bit Score: 80.65  E-value: 3.84e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280238 141 ELIGRSQWTVRYRQRLQQLAETDIAVWLYGEPGTGRMTGARYLHQL-GR------------------------HAEGPFi 195
Cdd:PRK15429 377 EIIGRSEAMYSVLKQVEMVAQSDSTVLILGETGTGKELIARAIHNLsGRnnrrmvkmncaampagllesdlfgHERGAF- 455

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280238 196 acelTPANAHTLN--ELiaqAQGGTLVLSHPEHLTHEQQHQLVQ-LQSHE----------KRPFRLIGIGSASLVELAAS 262
Cdd:PRK15429 456 ----TGASAQRIGrfEL---ADKSSLFLDEVGDMPLELQPKLLRvLQEQEferlgsnkiiQTDVRLIAATNRDLKKMVAD 528

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280238 263 SQIVAELYYCFAMTQIGCQPLSKRPDDIEPLFHHYLQKTCQRLNHPVPEVDAGLLKGMMRRVWPNNVRELANAAE---LF 339
Cdd:PRK15429 529 REFRSDLYYRLNVFPIHLPPLRERPEDIPLLVKAFTFKIARRMGRNIDSIPAETLRTLSNMEWPGNVRELENVIEravLL 608

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280238 340 AVG-----VLPLAETVNPLMHiGEPTPLDQRVEDvERQIITEALNIHQGRI---NEVAEYLLIPRKKLYLRMKKYGLNKE 411
Cdd:PRK15429 609 TRGnvlqlSLPDITLPEPETP-PAATVVAQEGED-EYQLIVRVLKETNGVVagpKGAAQRLGLKRTTLLSRMKRLGIDKS 686
REC_YesN-like cd17536
phosphoacceptor receiver (REC) domain of YesN and related helix-turn-helix containing response ...
 8-125 4.67e-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: 73.91  E-value: 4.67e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280238   8 ILLIDDDADVLDAYTQLLEQAGYH---VSACNNPFDAREQVPKDWPGIVLSDVCMPGCSGIDLMTVFHQDDDLLPILLIT 84
Cdd:cd17536    1 VLIVDDEPLIREGLKKLIDWEELGfevVGEAENGEEALELIEEHKPDIVITDIRMPGMDGLELIEKIRELYPDIKIIILS 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 490280238  85 GHGDVPMAVEAVKKGAWDFLQKPIDPGKLLTLVDAALRQRQ 125
Cdd:cd17536   81 GYDDFEYAQKAIRLGVVDYLLKPVDEEELEEALEKAKEELD 121
Sigma54_activ_2 pfam14532
Sigma-54 interaction domain;
143-283 6.72e-16

Sigma-54 interaction domain;


Pssm-ID: 434021 [Multi-domain]  Cd Length: 138  Bit Score: 73.92  E-value: 6.72e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280238  143 IGRSQWTVRYRQRLQQLAETDIAVWLYGEPGTGRMTGARYLHQLGRHAEGPFIACELtpanAHTLNELIAQAQGGTLVLS 222
Cdd:pfam14532   1 LGASAAIQEIKRRLEQAAQSTLPVFLTGEPGSGKEFCARYLHNPSTPWVQPFDIEYL----AHAPLELLEQAKGGTLYLK 76

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490280238  223 HPEHLTHEQQHQLVQ-LQSHEKRPFRLIGIGSASLVELAASSQIVAELYYCFAMTQIGCQPL 283
Cdd:pfam14532  77 DIADLSKALQKGLLLlLAKAEGYRVRLVCTSSKDLPQLAAAGLFDEQLYFELSALRLHVPPL 138
REC_typeB_ARR-like cd17584
phosphoacceptor receiver (REC) domain of type B Arabidopsis response regulators (ARRs) and ...
 8-113 9.72e-16

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: 73.05  E-value: 9.72e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280238   8 ILLIDDDADVLDAYTQLLEQAGYHVSACNNPFDA----REQvpKDWPGIVLSDVCMPGCSGIDLMTVFHQDDDLlPILLI 83
Cdd:cd17584    1 VLVVDDDPTCLAILKRMLLRCGYQVTTCTDAEEAlsmlREN--KDEFDLVITDVHMPDMDGFEFLELIRLEMDL-PVIMM 77

                         90       100       110
                 ....*....|....*....|....*....|
gi 490280238  84 TGHGDVPMAVEAVKKGAWDFLQKPIDPGKL 113
Cdd:cd17584   78 SADGSTSTVMKGLAHGACDYLLKPVSIEDL 107
REC_OmpR_PrrA-like cd17627
phosphoacceptor receiver (REC) domain of PrrA-like OmpR family response regulators; The ...
 8-123 2.03e-15

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: 72.03  E-value: 2.03e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280238   8 ILLIDDDADVLDAYTQLLEQAGYHVSACNNPFDAREQVPKDWPGIVLSDVCMPGCSGIDLMTVFHQDDDLLPILLITGHG 87
Cdd:cd17627    1 ILVVDDDRAVRESLRRSLRFEGYEVETAVDGAEALRVISGNRPDAVVLDVMMPRLDGLEVCRRLRAAGNDLPILVLTARD 80

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 490280238  88 DVPMAVEAVKKGAWDFLQKPIDPGKLLTLVDAALRQ 123
Cdd:cd17627   81 SVSDRVAGLDAGADDYLVKPFALEELLARVRALLRR 116
LytT COG3279
DNA-binding response regulator, LytR/AlgR family [Transcription, Signal transduction ...
 8-171 2.03e-14

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


Pssm-ID: 442510 [Multi-domain]  Cd Length: 235  Bit Score: 72.16  E-value: 2.03e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280238   8 ILLIDDDADVLDAYTQLLEQAGYH--VSACNNPFDAREQVPKDWPGIVLSDVCMPGCSGIDLMTVFHQDDDLLPILLITG 85
Cdd:COG3279    4 ILIVDDEPLARERLERLLEKYPDLevVGEASNGEEALELLEEHKPDLVFLDIQMPGLDGFELARQLRELDPPPPIIFTTA 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280238  86 HGDvpMAVEAVKKGAWDFLQKPIDPGKLLTLVDAALRQRQSviarrqycQQKLQVELIGRSQWTVRYRQRLQQLAETDIa 165
Cdd:COG3279   84 YDE--YALEAFEVNAVDYLLKPIDEERLAKALEKAKERLEA--------KAAAEASPEEKDRIFVKSGGKLVKIPLDDI- 152


                 ....*.
gi 490280238 166 VWLYGE 171
Cdd:COG3279  153 LYIEAE 158
REC_CheY cd17542
phosphoacceptor receiver (REC) domain of chemotaxis protein CheY; The chemotaxis response ...
 8-121 5.77e-14

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: 68.07  E-value: 5.77e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280238   8 ILLIDDDADVLDAYTQLLEQAGYHVSA-CNNPFDAREQVPKDWPGIVLSDVCMPGCSGIDLMTVFHQDDDLLPILLITGH 86
Cdd:cd17542    3 VLIVDDAAFMRMMLKDILTKAGYEVVGeAANGEEAVEKYKELKPDLVTMDITMPEMDGIEALKEIKKIDPNAKVIMCSAM 82

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 490280238  87 GDVPMAVEAVKKGAWDFLQKPIDPGKLLTLVDAAL 121
Cdd:cd17542   83 GQEEMVKEAIKAGAKDFIVKPFQPERVLEAVEKVL 117
REC_2_DhkD-like cd17580
second phosphoacceptor receiver (REC) domain of Dictyostelium discoideum hybrid signal ...
 8-117 6.86e-14

second phosphoacceptor receiver (REC) domain of Dictyostelium discoideum hybrid signal transduction histidine kinase D and similar domains; Dictyostelium discoideum hybrid signal transduction histidine kinase D (DhkD) is a large protein that contains two histidine kinase (HK) and two REC domains on the intracellular side of a single pass transmembrane domain, and extracellular PAS and PAC domains that likely are involved in ligand binding. This model represents the second REC domain and similar domains. DhkD activates the cAMP phosphodiesterase RegA to ensure proper prestalk and prespore patterning, tip formation, and the vertical elongation of the mound into a finger, in Dictyostelium discoideum. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381118 [Multi-domain]  Cd Length: 112  Bit Score: 67.48  E-value: 6.86e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280238   8 ILLIDDDADVLDAYTQLLEQAGYHVSACNNPFDAREQVPKDWPGIVLSDVCMPGCSGIDLMTVFHQDDDL--LPILLITG 85
Cdd:cd17580    1 ILVVDDNEDAAEMLALLLELEGAEVTTAHSGEEALEAAQRFRPDVILSDIGMPGMDGYELARRLRELPWLanTPAIALTG 80

                         90       100       110
                 ....*....|....*....|....*....|...
gi 490280238  86 HGDvPMAVEAVKKGAWDF-LQKPIDPGKLLTLV 117
Cdd:cd17580   81 YGQ-PEDRERALEAGFDAhLVKPVDPDELIELI 112
REC_OmpR_PhoB cd17618
phosphoacceptor receiver (REC) domain of PhoB response regulator from the OmpR family; The ...
 8-121 1.10e-13

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: 67.27  E-value: 1.10e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280238   8 ILLIDDDADVLDAYTQLLEQAGYHVSACNNPFDAREQVPKDWPGIVLSDVCMPGCSGIDLMTVFHQDDDL--LPILLITG 85
Cdd:cd17618    3 ILIVEDEPAIREMIAFNLERAGFDVVEAEDAESAVNLIVEPRPDLILLDWMLPGGSGIQFIRRLKRDEMTrdIPIIMLTA 82

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 490280238  86 HGDVPMAVEAVKKGAWDFLQKPIDPGKLLTLVDAAL 121
Cdd:cd17618   83 RGEEEDKVRGLEAGADDYITKPFSPRELVARIKAVL 118
REC_CpdR_CckA-like cd18160
phosphoacceptor receiver (REC) domain of Brucella abortus CpdR and CckA, and similar domains; ...
 8-107 1.47e-13

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


Pssm-ID: 381144 [Multi-domain]  Cd Length: 103  Bit Score: 66.37  E-value: 1.47e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280238   8 ILLIDDDADVLDAYTQLLEQAGYHVSACNNPFDAREQVPKDWP-GIVLSDVCMPGCSGIDLMTVFHQDDDLLPILLITGH 86
Cdd:cd18160    2 ILLADDEPSVRKFIVTTLKKAGYAVTEAESGAEALEKLQQGKDiDIVVTDIVMPEMDGIELAREARKIDPDVKILFISGG 81

                         90       100
                 ....*....|....*....|.
gi 490280238  87 GDVPMAVEAVKKGAWDFLQKP 107
Cdd:cd18160   82 AAAAPELLSDAVGDNATLKKP 102
REC_NarL-like cd17535
phosphoacceptor receiver (REC) domain of NarL (Nitrate/Nitrite response regulator L) family ...
 8-122 4.94e-13

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: 65.23  E-value: 4.94e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280238   8 ILLIDDDADVLDAYTQLLEQAGYH--VSACNNPFDAREQVPKDWPGIVLSDVCMPGCSGIDLMTVFHQDDDLLPILLITG 85
Cdd:cd17535    1 VLIVDDHPLVREGLRRLLESEPDIevVGEAADGEEALALLRELRPDVVLMDLSMPGMDGIEALRRLRRRYPDLKVIVLTA 80

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 490280238  86 HGDVPMAVEAVKKGAWDFLQKPIDPGKLLTLVDAALR 122
Cdd:cd17535   81 HDDPEYVLRALKAGAAGYLLKDSSPEELIEAIRAVAA 117
REC_PilR cd19926
phosphoacceptor receiver (REC) domain of type 4 fimbriae expression regulatory protein PilR ...
 8-107 1.40e-12

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: 63.33  E-value: 1.40e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280238   8 ILLIDDDADVLDAYTQLLEQAGYHVSACNNPFDAREQVPKDWPGIVLSDVCMPGCSGIDLMTVFHQDDDLLPILLITGHG 87
Cdd:cd19926    1 VLVVDDEPDIRELLEITLGRMGLDVRSARNVKEARELLASEPYDLCLTDMRLPDGSGLELVQHIQQRLPQTPVAVITAYG 80

                         90       100
                 ....*....|....*....|
gi 490280238  88 DVPMAVEAVKKGAWDFLQKP 107
Cdd:cd19926   81 SLDTAIEALKAGAFDFLTKP 100
TyrR COG3283
Transcriptional regulator TyrR of aromatic amino acids metabolism [Transcription, Amino acid ...
 142-375 4.61e-12

Transcriptional regulator TyrR of aromatic amino acids metabolism [Transcription, Amino acid transport and metabolism];


Pssm-ID: 442513 [Multi-domain]  Cd Length: 514  Bit Score: 67.52  E-value: 4.61e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280238 142 LIGRSQwtvRYRQRLQQ---LAETDIAVWLYGEPGTGRMTGARYLHQLGRHAEGPFIA--C----------EL------- 199
Cdd:COG3283  206 IVASSP---KMRQVIRQakkMAMLDAPLLIQGETGTGKELLARACHLASPRGDKPFLAlnCaalpddvaesELfgyapga 282

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280238 200 TPANAHTLNELIAQAQGGTLVLSHPEHLTHEQQHQLVQLQSHEKrpFRLIG----------IGSAS---LVELAASSQIV 266
Cdd:COG3283  283 FGNAREGKKGLFEQANGGTVFLDEIGEMSPQLQAKLLRFLQDGT--FRRVGeeqevkvdvrVICATqkdLAELVQEGEFR 360

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280238 267 AELYYCFAMTQIGCQPLSKRPDDIEPLFHHYLQKTCQRLNHPVPEVDAGLLKGMMRRVWPNNVRELANAaeLF-AVG--- 342
Cdd:COG3283  361 EDLYYRLNVLTLTLPPLRERKSDILPLAEHFVARFSQQLGRPRPRLSPDLVDFLQSYPWPGNVRQLENA--LYrAVSlle 438

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 490280238 343 ---------VLPLAETVNPLMHIGEPTPLDQRVEDVERQIIT 375
Cdd:COG3283  439 gdeltpedlQLPEYAASAGLLDDLLEGSLDEIVKRFERSLLR 480
REC_RcNtrC-like cd19928
phosphoacceptor receiver (REC) domain of Rhodobacter capsulatus nitrogen regulatory protein C ...
 8-107 6.45e-12

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: 61.75  E-value: 6.45e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280238   8 ILLIDDDADVLDAYTQLLEQAGYHVSACNNPFDAREQVPKDWPGIVLSDVCMPGCSGIDLMTVFHQDDDLLPILLITGHG 87
Cdd:cd19928    1 ILVADDDRAIRTVLTQALGRAGYEVRTTGNAATLWRWVEEGEGDLVITDVVMPDENGLDLIPRIKKARPDLPIIVMSAQN 80

                         90       100
                 ....*....|....*....|
gi 490280238  88 DVPMAVEAVKKGAWDFLQKP 107
Cdd:cd19928   81 TLMTAVKAAERGAFEYLPKP 100
REC_OmpR cd17574
phosphoacceptor receiver (REC) domain of OmpR family response regulators; OmpR-like proteins ...
 9-107 6.87e-12

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


Pssm-ID: 381116 [Multi-domain]  Cd Length: 99  Bit Score: 61.27  E-value: 6.87e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280238   9 LLIDDDADVLDAYTQLLEQAGYHVSACNNPFDAREQVPKDWPGIVLSDVCMPGCSGIDLMTVFHQDDDLLPILLITGHGD 88
Cdd:cd17574    1 LVVEDDEEIAELLSDYLEKEGYEVDTAADGEEALELAREEQPDLIILDVMLPGMDGFEVCRRLREKGSDIPIIMLTAKDE 80

                         90
                 ....*....|....*....
gi 490280238  89 VPMAVEAVKKGAWDFLQKP 107
Cdd:cd17574   81 EEDKVLGLELGADDYITKP 99
REC_OmpR_BsPhoP-like cd19937
phosphoacceptor receiver (REC) domain of BsPhoP-like OmpR family response regulators; Bacillus ...
 9-122 9.18e-12

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: 61.52  E-value: 9.18e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280238   9 LLIDDDADVLDAYTQLLEQAGYHVSACNNPFDAREQVPKDWPGIVLSDVCMPGCSGIDLMTVFHQDDDL--LPILLITGH 86
Cdd:cd19937    1 LVVDDEEDIVELLKYNLEKEGYEVVTAYDGEEALKRAKDEKPDLIILDLMLPGIDGLEVCRILRSDPKTssIPIIMLTAK 80

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 490280238  87 GDVPMAVEAVKKGAWDFLQKPIDPGKLLTLVDAALR 122
Cdd:cd19937   81 GEEFDKVLGLELGADDYITKPFSPRELLARVKAVLR 116
REC_D1_PleD-like cd17538
first (D1) phosphoacceptor receiver (REC) domain of response regulator PleD and similar ...
 8-108 2.02e-11

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: 60.20  E-value: 2.02e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280238   8 ILLIDDDADVLDAYTQLLEQAGYHVSACNNPFDAREQVPKDWPGIVLSDVCMPGCSGIDLMTVFHQDDD--LLPILLITG 85
Cdd:cd17538    2 ILVVDDEPANRELLEALLSAEGYEVLTADSGQEALALAEEELPDLILLDVMMPGMDGFEVCRRLKEDPEtrHIPVIMITA 81

                         90       100
                 ....*....|....*....|...
gi 490280238  86 HGDVPMAVEAVKKGAWDFLQKPI 108
Cdd:cd17538   82 LDDREDRIRGLEAGADDFLSKPI 104
REC_OmpR_MtrA-like cd17626
phosphoacceptor receiver (REC) domain of MtrA-like OmpR family response regulators; MtrA is ...
 8-121 7.55e-11

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: 59.02  E-value: 7.55e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280238   8 ILLIDDDADVLDAYTQLLEQAGYHVSACNNPFDAREQVPKDWPGIVLSDVCMPGCSGIDLMTVFHQDDDlLPILLITGHG 87
Cdd:cd17626    3 ILVVDDDAALAEMIGIVLRGEGFDPAFCGDGTQALAAFREVRPDLVLLDLMLPGIDGIEVCRQIRAESG-VPIVMLTAKS 81

                         90       100       110
                 ....*....|....*....|....*....|....
gi 490280238  88 DVPMAVEAVKKGAWDFLQKPIDPGKLLTLVDAAL 121
Cdd:cd17626   82 DTVDVVLGLESGADDYVAKPFKPKELVARIRARL 115
REC_OmpR_DrrD-like cd17625
phosphoacceptor receiver (REC) domain of DrrD-like OmpR family response regulators; DrrD is a ...
 9-123 7.60e-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: 7.60e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280238   9 LLIDDDADVLDAYTQLLEQAGYHVSACNNPFDAREQVPKDWPGIVLSDVCMPGCSGIDLMTVFHQDDDLLPILLITGHGD 88
Cdd:cd17625    1 LVVEDEKDLSEAITKHLKKEGYTVDVCFDGEEGLEYALSGIYDLIILDIMLPGMDGLEVLKSLREEGIETPVLLLTALDA 80

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 490280238  89 VPMAVEAVKKGAWDFLQKPIDPGKLLTLVDAALRQ 123
Cdd:cd17625   81 VEDRVKGLDLGADDYLPKPFSLAELLARIRALLRR 115
psREC_PRR cd17582
pseudo receiver domain of pseudo-response regulators; In Arabidopsis, five pseudo-response ...
 8-107 9.48e-11

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: 58.57  E-value: 9.48e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280238   8 ILLIDDDADVLDAYTQLLEQAGYHVSACNNPFDAREqVPKDWPG---IVLSDVCMPGCSGIDLMTVFHQDDDL--LPILL 82
Cdd:cd17582    1 VLLVENDDSTRQIVTALLRKCSYEVTAASDGLQAWD-VLEDEQNeidLILTEVDLPVSSGFKLLSYIMRHKICknIPVIM 79

                         90       100
                 ....*....|....*....|....*
gi 490280238  83 ITGHGDVPMAVEAVKKGAWDFLQKP 107
Cdd:cd17582   80 MSSQDSVGVVFKCLSKGAADYLVKP 104
REC_HupR cd17596
phosphoacceptor receiver (REC) domain of hydrogen uptake protein regulator (HupR); Members of ...
 7-142 1.06e-10

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


Pssm-ID: 381127 [Multi-domain]  Cd Length: 133  Bit Score: 59.30  E-value: 1.06e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280238   7 SILLIDDDADVLDAYTQLLEQaGYHVSACNNPFDAREQVPKDWPGIVLSDVCMPGCSGIDLMT-VFHQDDDLLPIlLITG 85
Cdd:cd17596    2 TILVVDDEVRSLEALRRTLEE-DFDVLTAASAEEALAILEEEWVQVILCDQRMPGTTGVEFLKeVRERWPEVVRI-IISG 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 490280238  86 HGDVPMAVEAVKK-GAWDFLQKPIDPGKLLTLVDAALRQRQsvIARRqycQQKLQVEL 142
Cdd:cd17596   80 YTDSEDIIAGINEaGIYQYLTKPWHPDQLLLTVRNAARLFE--LQRE---NERLSLEL 132
REC_OmpR_BfmR-like cd19939
phosphoacceptor receiver (REC) domain of BfmR-like OmpR family response regulators; ...
 7-123 1.85e-10

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: 57.77  E-value: 1.85e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280238   7 SILLIDDDADVLDAYTQLLEQAGYHVSACNNPFDAREQVPKDWPGIVLSDVCMPGCSGIDLMTVFHQDDDlLPILLITGH 86
Cdd:cd19939    1 RILIVEDELELARLTRDYLIKAGLEVSVFTDGQRAVRRIIDEQPSLVVLDIMLPGMDGLTVCREVREHSH-VPILMLTAR 79

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 490280238  87 GDVPMAVEAVKKGAWDFLQKPIDPGKLLTLVDAALRQ 123
Cdd:cd19939   80 TEEMDRVLGLEMGADDYLCKPFSPRELLARVRALLRR 116
PRK10161 PRK10161
phosphate response regulator transcription factor PhoB;
8-123 1.95e-10

phosphate response regulator transcription factor PhoB;


Pssm-ID: 182277 [Multi-domain]  Cd Length: 229  Bit Score: 60.50  E-value: 1.95e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280238   8 ILLIDDDADVLDAYTQLLEQAGYHVSACNNPFDAREQVPKDWPGIVLSDVCMPGCSGIDLMTVFHQDDDL--LPILLITG 85
Cdd:PRK10161   5 ILVVEDEAPIREMVCFVLEQNGFQPVEAEDYDSAVNQLNEPWPDLILLDWMLPGGSGIQFIKHLKRESMTrdIPVVMLTA 84

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 490280238  86 HGDVPMAVEAVKKGAWDFLQKPIDPGKLLTLVDAALRQ 123
Cdd:PRK10161  85 RGEEEDRVRGLETGADDYITKPFSPKELVARIKAVMRR 122
REC smart00448
cheY-homologous receiver domain; CheY regulates the clockwise rotation of E. coli flagellar ...
 7-60 2.00e-10

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: 56.04  E-value: 2.00e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 490280238     7 SILLIDDDADVLDAYTQLLEQAGYHVSACNNPFDAREQVPKDWPGIVLSDVCMP 60
Cdd:smart00448   2 RILVVDDDPLLRELLKALLEKEGYEVDEATDGEEALELLKEEKPDLILLDIMMP 55
REC_OmpR_CusR-like cd19935
phosphoacceptor receiver (REC) domain of CusR-like OmpR family response regulators; ...
 8-107 2.42e-10

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: 57.06  E-value: 2.42e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280238   8 ILLIDDDADVLDAYTQLLEQAGYHVSACNNPFDAREQVPK-DWPGIVLsDVCMPGCSGIDLMTVFHQDDDLLPILLITGH 86
Cdd:cd19935    1 ILVVEDEKKLAEYLKKGLTEEGYAVDVAYDGEDGLHLALTnEYDLIIL-DVMLPGLDGLEVLRRLRAAGKQTPVLMLTAR 79

                         90       100
                 ....*....|....*....|.
gi 490280238  87 GDVPMAVEAVKKGAWDFLQKP 107
Cdd:cd19935   80 DSVEDRVKGLDLGADDYLVKP 100
orf27 CHL00148
Ycf27; Reviewed
 1-135 3.84e-10

Ycf27; Reviewed


Pssm-ID: 214376 [Multi-domain]  Cd Length: 240  Bit Score: 59.73  E-value: 3.84e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280238   1 MLSNNCSILLIDDDADVLDAYTQLLEQAGYHVSACNNPFDAREQVPKDWPGIVLSDVCMPGCSGIDLMTVFHQDDDlLPI 80
Cdd:CHL00148   2 MENSKEKILVVDDEAYIRKILETRLSIIGYEVITASDGEEALKLFRKEQPDLVILDVMMPKLDGYGVCQEIRKESD-VPI 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 490280238  81 LLITGHGDVPMAVEAVKKGAWDFLQKPIDPGKLLTLVDAALRQRQSVIARRQYCQ 135
Cdd:CHL00148  81 IMLTALGDVSDRITGLELGADDYVVKPFSPKELEARIRSVLRRTNKKSFSSKIPN 135
REC_hyHK_CKI1_RcsC-like cd17546
phosphoacceptor receiver (REC) domain of hybrid sensor histidine kinases/response regulators ...
 8-117 4.86e-10

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: 56.71  E-value: 4.86e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280238   8 ILLIDDDADVLDAYTQLLEQAGYHVSACNNPFDAREQVPKDWPGIVLSDVCMPGCSGIDLMTVFHQDDDL---LPILLIT 84
Cdd:cd17546    1 VLVVDDNPVNRKVLKKLLEKLGYEVDVAENGQEALELLKEEPFDLVLMDLQMPVMDGLEATRRIRELEGGgrrTPIIALT 80

                         90       100       110
                 ....*....|....*....|....*....|...
gi 490280238  85 GHGDVPMAVEAVKKGAWDFLQKPIDPGKLLTLV 117
Cdd:cd17546   81 ANALEEDREKCLEAGMDDYLSKPVKLDQLKEVL 113
PRK09836 PRK09836
DNA-binding transcriptional activator CusR; Provisional
 8-145 4.88e-10

DNA-binding transcriptional activator CusR; Provisional


Pssm-ID: 182102 [Multi-domain]  Cd Length: 227  Bit Score: 59.17  E-value: 4.88e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280238   8 ILLIDDDADVLDAYTQLLEQAGYHVSACNNPFDARE-QVPKDWPGIVLsDVCMPGCSGIDLMTVFHQDDDLLPILLITGH 86
Cdd:PRK09836   3 LLIVEDEKKTGEYLTKGLTEAGFVVDLADNGLNGYHlAMTGDYDLIIL-DIMLPDVNGWDIVRMLRSANKGMPILLLTAL 81

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 490280238  87 GDVPMAVEAVKKGAWDFLQKPIDPGKLLTLVDAALRQRQSVIARRQYCQQKLQVELIGR 145
Cdd:PRK09836  82 GTIEHRVKGLELGADDYLVKPFAFAELLARVRTLLRRGAAVIIESQFQVADLMVDLVSR 140
pspF PRK11608
phage shock protein operon transcriptional activator; Provisional
 142-409 5.50e-10

phage shock protein operon transcriptional activator; Provisional


Pssm-ID: 236936 [Multi-domain]  Cd Length: 326  Bit Score: 60.45  E-value: 5.50e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280238 142 LIGRSQWTVRYRQRLQQLAETDIAVWLYGEPGTGRMTGARYLHQLGRHAEGPFIACELTPANAHTLN-ELI--------- 211
Cdd:PRK11608   8 LLGEANSFLEVLEQVSRLAPLDKPVLIIGERGTGKELIASRLHYLSSRWQGPFISLNCAALNENLLDsELFgheagaftg 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280238 212 AQ---------AQGGTLVLShpEHLTHEQQHQLVQLQSHE---------KRPF----RLIGIGSASLVELAASSQIVAEL 269
Cdd:PRK11608  88 AQkrhpgrferADGGTLFLD--ELATAPMLVQEKLLRVIEygelervggSQPLqvnvRLVCATNADLPAMVAEGKFRADL 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280238 270 YYCFAMTQIGCQPLSKRPDDIEPLFHHYLQKTCQRLNHPV-PEVDAGLLKGMMRRVWPNNVRELANAAE----------- 337
Cdd:PRK11608 166 LDRLAFDVVQLPPLRERQSDIMLMAEHFAIQMCRELGLPLfPGFTERARETLLNYRWPGNIRELKNVVErsvyrhgtsey 245

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280238 338 -LFAVGVLPLAETVNPLMHIGEPT------PLDQR--VEDVERQIITEALNihQGRINE--VAEYLLIPRKKLYLRMKKY 406
Cdd:PRK11608 246 pLDNIIIDPFKRRPAEEAIAVSETtslptlPLDLRewQHQQEKELLQRSLQ--QAKFNQkrAAELLGLTYHQLRALLKKH 323


                 ...
gi 490280238 407 GLN 409
Cdd:PRK11608 324 QIL 326
REC_OmpR_VirG cd17594
phosphoacceptor receiver (REC) domain of VirG-like OmpR family response regulators; VirG is ...
 8-119 5.80e-10

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: 56.30  E-value: 5.80e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280238   8 ILLIDDDADVLDAYTQLLEQAGYHVSACNNPFDAREQVPKDWPGIVLSDVCMPGCSGIDLMTVFHQDDDLlPILLITGHG 87
Cdd:cd17594    2 VLVVDDDAAMRHLLILYLRERGFDVTAAADGAEEARLMLHRRVDLVLLDLRLGQESGLDLLRTIRARSDV-PIIIISGDR 80

                         90       100       110
                 ....*....|....*....|....*....|...
gi 490280238  88 DVPMA-VEAVKKGAWDFLQKPIDPGKLLTLVDA 119
Cdd:cd17594   81 RDEIDrVVGLELGADDYLAKPFGLRELLARVRA 113
PRK10820 PRK10820
transcriptional regulator TyrR;
151-335 5.91e-10

transcriptional regulator TyrR;


Pssm-ID: 236769 [Multi-domain]  Cd Length: 520  Bit Score: 60.86  E-value: 5.91e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280238 151 RYRQRLQQ---LAETDIAVWLYGEPGTGRMTGARYLHQLGRHAEGPFIA--CELTP-----------ANAHTLNEL---- 210
Cdd:PRK10820 212 KMRQVVEQarkLAMLDAPLLITGDTGTGKDLLAYACHLRSPRGKKPFLAlnCASIPddvveselfghAPGAYPNALegkk 291

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280238 211 --IAQAQGGTLVLSHPEHLTHEQQHQLVQL----------QSHE-KRPFRLIGIGSASLVELAASSQIVAELYYCFAMTQ 277
Cdd:PRK10820 292 gfFEQANGGSVLLDEIGEMSPRMQAKLLRFlndgtfrrvgEDHEvHVDVRVICATQKNLVELVQKGEFREDLYYRLNVLT 371

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 490280238 278 IGCQPLSKRPDDIEPLFHHYLQKTCQRLNHPVPEVDAGLLKGMMRRVWPNNVRELANA 335
Cdd:PRK10820 372 LNLPPLRDRPQDIMPLTELFVARFADEQGVPRPKLAADLNTVLTRYGWPGNVRQLKNA 429
REC_CheY4-like cd17562
phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY4 and similar CheY ...
 7-117 1.28e-09

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: 55.77  E-value: 1.28e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280238   7 SILLIDDDADVLDAYTQLLEQAGYHVSACNNPFDAREQVPKDWPGIVLSDVCMPGCSGIDLMTVF--HQDDDLLPILLIT 84
Cdd:cd17562    2 KILAVDDSASIRQMVSFTLRGAGYEVVEAADGRDALSKAQSKKFDLIITDQNMPNMDGIELIKELrkLPAYKFTPILMLT 81

                         90       100       110
                 ....*....|....*....|....*....|...
gi 490280238  85 GHGDVPMAVEAVKKGAWDFLQKPIDPGKLLTLV 117
Cdd:cd17562   82 TESSDEKKQEGKAAGATGWLVKPFDPEQLLEVV 114
REC_OmpR_ChvI-like cd19936
phosphoacceptor receiver (REC) domain of ChvI-like OmpR family response regulators; ...
 8-107 1.53e-09

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: 54.76  E-value: 1.53e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280238   8 ILLIDDDADVLDAYTQLLEQAGYHVSACNNPFDAREQVPKDWPGIVLSDVCMPGCSGIDLMTVFHQDDDlLPILLITGHG 87
Cdd:cd19936    1 IALVDDDRNILTSVSMALEAEGFSVETYTDGASALDGLNARPPDLAILDIKMPRMDGMELLQRLRQKST-LPVIFLTSKD 79

                         90       100
                 ....*....|....*....|
gi 490280238  88 DVPMAVEAVKKGAWDFLQKP 107
Cdd:cd19936   80 DEIDEVFGLRMGADDYITKP 99
REC_PA4781-like cd19920
phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase PA4781 and similar ...
 8-108 1.68e-09

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: 54.82  E-value: 1.68e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280238   8 ILLIDDDADVLDAYTQLLEQAGYHVSACNNPFDAREQVPKDWPGIVLSDVCMPGCSGIDLMTVFHQDDDL--LPILLITG 85
Cdd:cd19920    1 ILIVDDVPDNLRLLSELLRAAGYRVLVATDGQQALQRAQAEPPDLILLDVMMPGMDGFEVCRRLKADPATrhIPVIFLTA 80

                         90       100
                 ....*....|....*....|...
gi 490280238  86 HGDVPMAVEAVKKGAWDFLQKPI 108
Cdd:cd19920   81 LTDTEDKVKGFELGAVDYITKPF 103
REC_OmpR_EcPhoP-like cd19934
phosphoacceptor receiver (REC) domain of EcPhoP-like OmpR family response regulators; ...
 8-122 1.76e-09

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: 54.98  E-value: 1.76e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280238   8 ILLIDDDADVLDAYTQLLEQAGYHVSACNNPFDAREQVPKDWPGIVLSDVCMPGCSGIDLMTVFHQDDDLLPILLITGHG 87
Cdd:cd19934    1 LLLVEDDALLAAQLKEQLSDAGYVVDVAEDGEEALFQGEEEPYDLVVLDLGLPGMDGLSVLRRWRSEGRATPVLILTARD 80

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 490280238  88 DVPMAVEAVKKGAWDFLQKPIDPGKLLTLVDAALR 122
Cdd:cd19934   81 SWQDKVEGLDAGADDYLTKPFHIEELLARLRALIR 115
Sigma54_activat pfam00158
Sigma-54 interaction domain;
142-221 2.30e-09

Sigma-54 interaction domain;


Pssm-ID: 425491 [Multi-domain]  Cd Length: 168  Bit Score: 56.26  E-value: 2.30e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280238  142 LIGRSQWTVRYRQRLQQLAETDIAVWLYGEPGTGRMTGARYLHQLGRHAEGPFIA--C----------EL--------TP 201
Cdd:pfam00158   1 IIGESPAMQEVLEQAKRVAPTDAPVLITGESGTGKELFARAIHQLSPRADGPFVAvnCaaipeellesELfghekgafTG 80

                          90       100
                  ....*....|....*....|
gi 490280238  202 ANAHTLNeLIAQAQGGTLVL 221
Cdd:pfam00158  81 ADSDRKG-LFELADGGTLFL 99
REC_CheB-like cd17541
phosphoacceptor receiver (REC) domain of chemotaxis response regulator protein-glutamate ...
 8-113 2.49e-09

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


Pssm-ID: 381096 [Multi-domain]  Cd Length: 125  Bit Score: 55.09  E-value: 2.49e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280238   8 ILLIDDDADVLDAYTQLLEQAGYH--VSACNNPFDAREQVPKDWPGIVLSDVCMPGCSGID----LMtvfhqDDDLLPIL 81
Cdd:cd17541    3 VLIVDDSAVMRKLLSRILESDPDIevVGTARDGEEALEKIKELKPDVITLDIEMPVMDGLEalrrIM-----AERPTPVV 77

                         90       100       110
                 ....*....|....*....|....*....|....
gi 490280238  82 LITGH--GDVPMAVEAVKKGAWDFLQKPIDPGKL 113
Cdd:cd17541   78 MVSSLteEGAEITLEALELGAVDFIAKPSGGISL 111
REC_Ycf29 cd19927
phosphoacceptor receiver (REC) domain of probable transcriptional regulator Ycf29; Ycf29 is a ...
 8-107 2.64e-09

phosphoacceptor receiver (REC) domain of probable transcriptional regulator Ycf29; Ycf29 is a probable response regulator of a two-component system (TCS), typically consisting a sensor and a response regulator, that functions in adaptation to changing environments. Processes regulated by TCSs in bacteria include sporulation, pathogenicity, virulence, chemotaxis, and membrane transport. Ycf29 contains an N-terminal REC domain and a LuxR-type helix-turn-helix DNA-binding output domain. REC domains function as phosphorylation-mediated switches within RRs, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381154 [Multi-domain]  Cd Length: 102  Bit Score: 54.31  E-value: 2.64e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280238   8 ILLIDDDADVLDAYTQLLEQAGYHVSACNNPFDAREQVPKDWPGIVLSDVCMPGCSGIDLMTVFHQDDDL--LPILLITG 85
Cdd:cd19927    1 ILLVDDDPGIRLAVKDYLEDQGFTVIAASNGLEALDLLNQYIPDLIISDIIMPGVDGYSLLGKLRKNADFdtIPVIFLTA 80

                         90       100
                 ....*....|....*....|..
gi 490280238  86 HGDVPMAVEAVKKGAWDFLQKP 107
Cdd:cd19927   81 KGMTSDRIKGYNAGCDGYLSKP 102
ompR PRK09468
osmolarity response regulator; Provisional
 1-124 3.16e-09

osmolarity response regulator; Provisional


Pssm-ID: 181883 [Multi-domain]  Cd Length: 239  Bit Score: 56.91  E-value: 3.16e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280238   1 MLSNNCSILLIDDDADVLDAYTQLLEQAGYHVSACNNPfdarEQVPKDWPG-----IVLsDVCMPGCSGIDLMTVFHQDD 75
Cdd:PRK09468   1 MMQENYKILVVDDDMRLRALLERYLTEQGFQVRSAANA----EQMDRLLTResfhlMVL-DLMLPGEDGLSICRRLRSQN 75

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 490280238  76 DLLPILLITGHGDVPMAVEAVKKGAWDFLQKPIDPGKLLTLVDAALRQR 124
Cdd:PRK09468  76 NPTPIIMLTAKGEEVDRIVGLEIGADDYLPKPFNPRELLARIRAVLRRQ 124
REC_Spo0F-like cd17553
phosphoacceptor receiver (REC) domain of Spo0F and similar domains; Spo0F, a stand-alone ...
 8-109 3.57e-09

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: 54.48  E-value: 3.57e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280238   8 ILLIDDDADVLDAYTQLLEQAGYHVSACNNPFDAREQVPKDWPGIVLSDVCMPGCSGIDLMTVFHQDDDLLPILLITGHG 87
Cdd:cd17553    3 ILIVDDQYGIRILLNEVFNKEGYQTFQAANGLQALDIVTKERPDLVLLDMKIPGMDGIEILKRMKVIDENIRVIIMTAYG 82

                         90       100
                 ....*....|....*....|..
gi 490280238  88 DVPMAVEAVKKGAWDFLQKPID 109
Cdd:cd17553   83 ELDMIQESKELGALTHFAKPFD 104
REC_hyHK cd17598
phosphoacceptor receiver (REC) domain of uncharacterized hybrid sensor histidine kinase ...
 17-115 3.70e-09

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


Pssm-ID: 381128 [Multi-domain]  Cd Length: 118  Bit Score: 54.25  E-value: 3.70e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280238  17 VLDAYTQ------LLEQAGYHVSACNNPFDAREQVPKDWPGIVLSDVCMPGCSGIDLMTVFHQDDDL--LPILLITGHGD 88
Cdd:cd17598    4 VEDSPTQaeqlkhILEEQGYKVQVARNGREALAMLAEHRPTLVISDIVMPEMDGYELCRKIKSDPDLkdIPVILLTTLSD 83

                         90       100
                 ....*....|....*....|....*..
gi 490280238  89 VPMAVEAVKKGAWDFLQKPIDPGKLLT 115
Cdd:cd17598   84 PRDVIRGLECGADNFITKPYDEKYLLS 110
REC_CheY_CheY3 cd19923
phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY3 and similar CheY ...
 7-113 4.17e-09

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: 54.27  E-value: 4.17e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280238   7 SILLIDDDADVLDAYTQLLEQAGY-HVSACNNPFDAREQVPKDWPGIVLSDVCMPGCSGIDLMTVFHQDDDL--LPILLI 83
Cdd:cd19923    2 KVLVVDDFSTMRRIIKNLLKELGFnNVEEAEDGVDALEKLKAGGFDFVITDWNMPNMDGLELLKTIRADGALshLPVLMV 81

                         90       100       110
                 ....*....|....*....|....*....|
gi 490280238  84 TGHGDVPMAVEAVKKGAWDFLQKPIDPGKL 113
Cdd:cd19923   82 TAEAKKENVIAAAQAGVNNYIVKPFTAATL 111
REC_2_GGDEF cd17544
second phosphoacceptor receiver (REC) domain of uncharacterized GGDEF domain proteins; This ...
 6-107 4.45e-09

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: 54.06  E-value: 4.45e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280238   6 CSILLIDDDADVLDAYTQLLEQAGYHVSACNNPFDAREQVPKDwPGI--VLSDVCMPGCSGIDLM-TVFHQ-DDDLLPIL 81
Cdd:cd17544    1 IKVLVVDDSATSRNHLRALLRRHNFQVLEAANGQEALEVLEQH-PDIklVITDYNMPEMDGFELVrEIRKKySRDQLAII 79

                         90       100
                 ....*....|....*....|....*.
gi 490280238  82 LITGHGDVPMAVEAVKKGAWDFLQKP 107
Cdd:cd17544   80 GISASGDNALSARFIKAGANDFLTKP 105
REC_DC-like cd17534
phosphoacceptor receiver (REC) domain of modulated diguanylate cyclase and similar domains; ...
 7-121 8.14e-09

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: 53.18  E-value: 8.14e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280238   7 SILLIDDDADVLDAYTQLLEQAGYHVSA-CNNPFDAREQVPKDWPGIVLSDVCMPG-CSGIDLMTVFHQDDDlLPILLIT 84
Cdd:cd17534    2 KILIVEDEAIIALDLKEILESLGYEVVGiADSGEEAIELAEENKPDLILMDINLKGdMDGIEAAREIREKFD-IPVIFLT 80

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 490280238  85 GHGDVPMaVEAVKK-GAWDFLQKPIDPGKLLTLVDAAL 121
Cdd:cd17534   81 AYSDEET-LERAKEtNPYGYLVKPFNERELKAAIELAL 117
REC_OmpR_PmrA-like cd17624
phosphoacceptor receiver (REC) domain of PmrA-like OmpR family response regulators; This ...
 8-122 1.37e-08

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: 52.49  E-value: 1.37e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280238   8 ILLIDDDADVLDAYTQLLEQAGYHVSACNNPFDAREQVPKDWPGIVLSDVCMPGCSGIDLMTVFHQDDDLLPILLITGHG 87
Cdd:cd17624    1 ILLVEDDALLGDGLKTGLRKAGYAVDWVRTGAEAEAALASGPYDLVILDLGLPDGDGLDLLRRWRRQGQSLPVLILTARD 80

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 490280238  88 DVPMAVEAVKKGAWDFLQKPIDPGKLLTLVDAALR 122
Cdd:cd17624   81 GVDDRVAGLDAGADDYLVKPFALEELLARLRALLR 115
REC_TrrA-like cd17554
phosphoacceptor receiver (REC) domain of Thermotoga maritima response regulator TrrA and ...
 7-88 1.92e-08

phosphoacceptor receiver (REC) domain of Thermotoga maritima response regulator TrrA and similar domains; Thermotoga maritima contains a two-component signal transduction system (TCS) composed of the ThkA sensory histidine kinase (HK) and its cognate response regulator (RR) TrrA; the specific function of the system is unknown. TCSs couple environmental stimuli to adaptive responses. TrrA is a stand-alone RR containing only a REC domain with no output/effector domain. The REC domain itself functions as an effector domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381106 [Multi-domain]  Cd Length: 113  Bit Score: 52.22  E-value: 1.92e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280238   7 SILLIDDDADVLDAYTQLLEQAGYHVSACNNPFDAREQVPKDWPGIVLSDVCMPGCSGIDLMTVFHQDDDLLPILLITGH 86
Cdd:cd17554    2 KILVVDDEENIRELYKEELEDEGYEVVTAGNGEEALEKLESEDPDLVILDIKMPGMDGLETLRKIREKKPDLPVIICTAY 81


                 ..
gi 490280238  87 GD 88
Cdd:cd17554   82 SE 83
REC_OmpR_kpRstA-like cd17622
phosphoacceptor receiver (REC) domain of kpRstA-like OmpR family response regulators; ...
 8-122 6.70e-08

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: 50.45  E-value: 6.70e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280238   8 ILLIDDDADVLDAYTQLLEQAGYHVSACNNPFDAREQVPKDWPGIVLSDVCMPGCSGI----DLMTVFHqdddlLPILLI 83
Cdd:cd17622    3 ILLVEDDPKLARLIADFLESHGFNVVVEHRGDRALEVIAREKPDAVLLDIMLPGIDGLtlcrDLRPKYQ-----GPILLL 77

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 490280238  84 TGHGDVPMAVEAVKKGAWDFLQKPIDPGKLLTLVDAALR 122
Cdd:cd17622   78 TALDSDIDHILGLELGADDYVVKPVEPAVLLARLRALLR 116
HTH_8 pfam02954
Bacterial regulatory protein, Fis family;
366-405 7.22e-08

Bacterial regulatory protein, Fis family;


Pssm-ID: 427077 [Multi-domain]  Cd Length: 40  Bit Score: 48.16  E-value: 7.22e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 490280238  366 VEDVERQIITEALNIHQGRINEVAEYLLIPRKKLYLRMKK 405
Cdd:pfam02954   1 LEEVEKELIEAALERTGGNKSKAARLLGISRRTLYRKLKK 40
PRK05022 PRK05022
nitric oxide reductase transcriptional regulator NorR;
116-408 8.36e-08

nitric oxide reductase transcriptional regulator NorR;


Pssm-ID: 235331 [Multi-domain]  Cd Length: 509  Bit Score: 54.02  E-value: 8.36e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280238 116 LVDAALRQRQSVIARRQycQQKLQVELIGRSQWTVRYRQRLQQLAETDIAVWLYGEPGTGRMTGARYLHQLGRHAEGPFI 195
Cdd:PRK05022 165 LESQAELPQDVAEFLRQ--EALKEGEMIGQSPAMQQLKKEIEVVAASDLNVLILGETGVGKELVARAIHAASPRADKPLV 242

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280238 196 A--C----------EL--------TPANAHTLN--ELiaqAQGGTLVLSHPEHLTHEQQHQLVQ-LQSHE------KRPF 246
Cdd:PRK05022 243 YlnCaalpeslaesELfghvkgafTGAISNRSGkfEL---ADGGTLFLDEIGELPLALQAKLLRvLQYGEiqrvgsDRSL 319

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280238 247 ----RLIGIGSASLVELAASSQIVAELYYCFAMTQIGCQPLSKRPDDIEPLFHHYLQKTCQRLNHPVPEVDAGLLKGMMR 322
Cdd:PRK05022 320 rvdvRVIAATNRDLREEVRAGRFRADLYHRLSVFPLSVPPLRERGDDVLLLAGYFLEQNRARLGLRSLRLSPAAQAALLA 399

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280238 323 RVWPNNVRELANA---AELFAVG--------------------VLPlAETVNPLMHIGEPTPLDQRVEDVERQIITEALN 379
Cdd:PRK05022 400 YDWPGNVRELEHVisrAALLARArgagrivtleaqhldlpaevALP-PPEAAAAPAAVVSQNLREATEAFQRQLIRQALA 478

                        330       340
                 ....*....|....*....|....*....
gi 490280238 380 IHQGRINEVAEYLLIPRKKLYLRMKKYGL 408
Cdd:PRK05022 479 QHQGNWAAAARALELDRANLHRLAKRLGL 507
PRK11517 PRK11517
DNA-binding response regulator HprR;
8-132 1.21e-07

DNA-binding response regulator HprR;


Pssm-ID: 183172 [Multi-domain]  Cd Length: 223  Bit Score: 52.21  E-value: 1.21e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280238   8 ILLIDDDADVLDAYTQLLEQAGYHVSACNNPFDAREQVPKDWPGIVLSDVCMPGCSGIDLMTVFHQDDDLlPILLITGHG 87
Cdd:PRK11517   3 ILLIEDNQRTQEWVTQGLSEAGYVIDAVSDGRDGLYLALKDDYALIILDIMLPGMDGWQILQTLRTAKQT-PVICLTARD 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 490280238  88 DVPMAVEAVKKGAWDFLQKPIDPGKLLTLVDAALRQRQSVIARRQ 132
Cdd:PRK11517  82 SVDDRVRGLDSGANDYLVKPFSFSELLARVRAQLRQHHALNSTLE 126
REC_citrate_TCS cd19925
phosphoacceptor receiver (REC) domain of citrate family two-component system response ...
 8-124 1.42e-07

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: 49.55  E-value: 1.42e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280238   8 ILLIDDDADVLDAYTQLLEQ-AGYHVSA-CNNPFDAREQVPKDWPGIVLSDVCMPGCSGIDLMTVFHQDDDLLPILLITG 85
Cdd:cd19925    3 VLIVEDDPMVAEIHRAYVEQvPGFTVIGtAGTGEEALKLLKERQPDLILLDIYLPDGNGLDLLRELRAAGHDVDVIVVTA 82

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 490280238  86 HGDVPMAVEAVKKGAWDFLQKPIDpgklltlvDAALRQR 124
Cdd:cd19925   83 ANDVETVREALRLGVVDYLIKPFT--------FERLRQR 113
PRK15369 PRK15369
two component system response regulator;
4-169 1.91e-07

two component system response regulator;


Pssm-ID: 185267 [Multi-domain]  Cd Length: 211  Bit Score: 51.23  E-value: 1.91e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280238   4 NNCSILLIDDDADVLDAYTQLLE-QAGYH-VSACNNPFDAREQVPKDWPGIVLSDVCMPGCSGIDLMTVFHQDDDLLPIL 81
Cdd:PRK15369   2 KNYKILLVDDHELIINGIKNMLApYPRYKiVGQVDNGLEVYNACRQLEPDIVILDLGLPGMNGLDVIPQLHQRWPAMNIL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280238  82 LITGHGDVPMAVEAVKKGAWDFLQKPIDPGKLLtlvdAALrqrQSVIARRQYCQQKLQVELIGR---------SQWTVRY 152
Cdd:PRK15369  82 VLTARQEEHMASRTLAAGALGYVLKKSPQQILL----AAI---QTVAVGKRYIDPALNREAILAllnaddtnpPLLTPRE 154

                        170       180
                 ....*....|....*....|.
gi 490280238 153 RQRLQQLAE----TDIAVWLY 169
Cdd:PRK15369 155 RQILKLITEgytnRDIAEQLS 175
PRK15479 PRK15479
transcriptional regulator TctD;
8-132 4.14e-07

transcriptional regulator TctD;


Pssm-ID: 185376 [Multi-domain]  Cd Length: 221  Bit Score: 50.49  E-value: 4.14e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280238   8 ILLIDDDADVLDAYTQLLEQAGYHVSACNNPFDAREQVPKDWPGIVLSDVCMPGCSGIDLMTVFHQDDDLLPILLITGHG 87
Cdd:PRK15479   3 LLLAEDNRELAHWLEKALVQNGFAVDCVFDGLAADHLLQSEMYALAVLDINMPGMDGLEVLQRLRKRGQTLPVLLLTARS 82

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 490280238  88 DVPMAVEAVKKGAWDFLQKPIDPGKLLTLVDAALRQRQSVIARRQ 132
Cdd:PRK15479  83 AVADRVKGLNVGADDYLPKPFELEELDARLRALLRRSAGQVQEVQ 127
PRK10955 PRK10955
envelope stress response regulator transcription factor CpxR;
8-123 4.66e-07

envelope stress response regulator transcription factor CpxR;


Pssm-ID: 182864 [Multi-domain]  Cd Length: 232  Bit Score: 50.57  E-value: 4.66e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280238   8 ILLIDDDADVLDAYTQLLEQAGYHVSACNNPFDAREQVpKDWPGIVLSDVCMPGCSGIDLMTVFHQDDDlLPILLITGHG 87
Cdd:PRK10955   4 ILLVDDDRELTSLLKELLEMEGFNVIVAHDGEQALDLL-DDSIDLLLLDVMMPKKNGIDTLKELRQTHQ-TPVIMLTARG 81

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 490280238  88 DVPMAVEAVKKGAWDFLQKPIDPGKLLTLVDAALRQ 123
Cdd:PRK10955  82 SELDRVLGLELGADDYLPKPFNDRELVARIRAILRR 117
REC_DivK-like cd17548
phosphoacceptor receiver (REC) domain of DivK and similar proteins; Caulobacter crescentus ...
 8-117 8.91e-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: 47.53  E-value: 8.91e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280238   8 ILLIDDDADVLDAYTQLLEQAGYHVSACNNPFDAREQVPKDWPGIVLSDVCMPGCSGIDLMTVFHQDDDL--LPILLITG 85
Cdd:cd17548    2 ILIVEDNPLNMKLARDLLESAGYEVLEAADGEEALEIARKEKPDLILMDIQLPGMDGLEATRLLKEDPATrdIPVIALTA 81

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 490280238  86 H---GDVPMAVEAvkkGAWDFLQKPIDPGKLLTLV 117
Cdd:cd17548   82 YamkGDREKILEA---GCDGYISKPIDTREFLETV 113
PRK10360 PRK10360
transcriptional regulator UhpA;
7-187 1.44e-06

transcriptional regulator UhpA;


Pssm-ID: 182408 [Multi-domain]  Cd Length: 196  Bit Score: 48.43  E-value: 1.44e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280238   7 SILLIDDDADVLDAYTQLLE-QAGYHVSAcnnPFDAREQVPKDWPG----IVLSDVCMPGCSGIDLMTvfhQDDDLLPIL 81
Cdd:PRK10360   3 TVALIDDHLIVRSGFAQLLGlEPDLQVVA---EFGSGREALAGLPGrgvqVCICDISMPDISGLELLS---QLPKGMATI 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280238  82 LITGHgDVPMAVE-AVKKGAWDFLQKPIDPGKLLtlvdAALRqrqSVIARRQYCQQKLQVELIGRSQ--WTVRYRQRLQQ 158
Cdd:PRK10360  77 MLSVH-DSPALVEqALNAGARGFLSKRCSPDELI----AAVH---TVATGGCYLTPDIAIKLASGRQdpLTKRERQVAEK 148

                        170       180       190
                 ....*....|....*....|....*....|...
gi 490280238 159 LAE----TDIAVWLYGEPGTGRMTGARYLHQLG 187
Cdd:PRK10360 149 LAQgmavKEIAAELGLSPKTVHVHRANLMEKLG 181
PRK11697 PRK11697
two-component system response regulator BtsR;
7-113 1.63e-06

two-component system response regulator BtsR;


Pssm-ID: 236956 [Multi-domain]  Cd Length: 238  Bit Score: 49.07  E-value: 1.63e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280238   7 SILLIDDDADVLDAYTQLLEQAG--YHVSACNNPFDAREQVPKDWPGIVLSDVCMPGCSGIDLMTVFhqDDDLLP-ILLI 83
Cdd:PRK11697   3 KVLIVDDEPLAREELRELLQEEGdiEIVGECSNAIEAIGAIHRLKPDVVFLDIQMPRISGLELVGML--DPEHMPyIVFV 80

                         90       100       110
                 ....*....|....*....|....*....|
gi 490280238  84 TGHGDvpMAVEAVKKGAWDFLQKPIDPGKL 113
Cdd:PRK11697  81 TAFDE--YAIKAFEEHAFDYLLKPIDPARL 108
CitB COG2197
DNA-binding response regulator, NarL/FixJ family, contains REC and HTH domains [Signal ...
 8-68 1.75e-06

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


Pssm-ID: 441799 [Multi-domain]  Cd Length: 131  Bit Score: 46.81  E-value: 1.75e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490280238   8 ILLIDDDADVLDAYTQLLEQA-GYHVSA-CNNPFDAREQVPKDWPGIVLSDVCMPGCSGIDLM 68
Cdd:COG2197    4 VLIVDDHPLVREGLRALLEAEpDIEVVGeAADGEEALELLEELRPDVVLLDIRMPGMDGLEAL 66
REC_OmpR_RegX3-like cd17621
phosphoacceptor receiver (REC) domain of RegX3-like OmpR family response regulators; RegX3 is ...
 8-107 1.97e-06

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: 46.04  E-value: 1.97e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280238   8 ILLIDDDADVLDAYTQLLEQAGYHVSACNNPFDAREQVPKDWPGIVLSDVCMPGCSGIDLMTVFHQDDDlLPILLITGHG 87
Cdd:cd17621    1 VLVVEDEESFSDPLAYLLRKEGFEVTVATDGPAALAEFDRAGADIVLLDLMLPGLSGTEVCRQLRARSN-VPVIMVTAKD 79

                         90       100
                 ....*....|....*....|
gi 490280238  88 DVPMAVEAVKKGAWDFLQKP 107
Cdd:cd17621   80 SEIDKVVGLELGADDYVTKP 99
REC_OmpR_YycF-like cd17614
phosphoacceptor receiver (REC) domain of YrcF-like OmpR family response regulators; YycF ...
 8-123 3.33e-06

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: 45.88  E-value: 3.33e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280238   8 ILLIDDDADVLDAYTQLLEQAGYHVSACNNPFDAREQVPKDWPGIVLSDVCMPGCSGIDLMTVFHQDDDlLPILLITGHG 87
Cdd:cd17614    1 ILVVDDEKPISDILKFNLTKEGYEVVTAYDGREALEKVEEEQPDLILLDLMLPEKDGLEVCREVRKTSN-VPIIMLTAKD 79

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 490280238  88 DVPMAVEAVKKGAWDFLQKPIDPGKLLTLVDAALRQ 123
Cdd:cd17614   80 SEVDKVLGLELGADDYVTKPFSNRELLARVKANLRR 115
REC_PdtaR-like cd19932
phosphoacceptor receiver (REC) domain of PdtaR and similar proteins; This subfamily includes ...
 8-121 3.74e-06

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


Pssm-ID: 381159 [Multi-domain]  Cd Length: 118  Bit Score: 45.87  E-value: 3.74e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280238   8 ILLIDDDADVLDAYTQLLEQAGYHVSA-CNNPFDAREQVPKDWPGIVLSDVCMPGCSGIDLMTVFhQDDDLLPILLITGH 86
Cdd:cd19932    3 VLIAEDEALIRMDLREMLEEAGYEVVGeASDGEEAVELAKKHKPDLVIMDVKMPRLDGIEAAKII-TSENIAPIVLLTAY 81

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 490280238  87 GDVPMAVEAVKKGAWDFLQKPIDPGKLLTLVDAAL 121
Cdd:cd19932   82 SQQDLVERAKEAGAMAYLVKPFSESDLIPAIEMAI 116
PRK10430 PRK10430
two-component system response regulator DcuR;
8-156 1.06e-05

two-component system response regulator DcuR;


Pssm-ID: 182454 [Multi-domain]  Cd Length: 239  Bit Score: 46.64  E-value: 1.06e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280238   8 ILLIDDDADVLD---------------AYTQLLEQAGYHVSACNNPFDareqvpkdwpgIVLSDVCMPGCSGIDLMTVFH 72
Cdd:PRK10430   4 VLIVDDDAMVAElnrryvaqipgfqccGTASTLEQAKEIIFNSDTPID-----------LILLDIYMQQENGLDLLPVLH 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280238  73 QDDDLLPILLITGHGDVPMAVEAVKKGAWDFLQKPIDPGKLltlvDAAL---RQRQSVIARRQYCQQKLQVELIGRSQWT 149
Cdd:PRK10430  73 EAGCKSDVIVISSAADAATIKDSLHYGVVDYLIKPFQASRF----EEALtgwRQKKMALEKHQYYDQAELDQLIHGSSSN 148


                 ....*..
gi 490280238 150 VRYRQRL 156
Cdd:PRK10430 149 EQDPRRL 155
REC_OmpR_BaeR-like cd19938
phosphoacceptor receiver (REC) domain of BaeR-like OmpR family response regulators; BaeR is ...
 8-121 1.10e-05

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: 44.29  E-value: 1.10e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280238   8 ILLIDDDADVLDAYTQLLEQAGYHVSACNNPFDAREQVPKDWPGIVLSDVCMPGCSGIDLMTVFHQDDDlLPILLITGHG 87
Cdd:cd19938    2 ILIVEDEPKLAQLLIDYLRAAGYAPTLLAHGDQVLPYVRHTPPDLILLDLMLPGTDGLTLCREIRRFSD-VPIIMVTARV 80

                         90       100       110
                 ....*....|....*....|....*....|....
gi 490280238  88 DVPMAVEAVKKGAWDFLQKPIDPGKLLTLVDAAL 121
Cdd:cd19938   81 EEIDRLLGLELGADDYICKPYSPREVVARVKAIL 114
PRK10610 PRK10610
chemotaxis protein CheY;
1-113 1.66e-05

chemotaxis protein CheY;


Pssm-ID: 170568 [Multi-domain]  Cd Length: 129  Bit Score: 44.19  E-value: 1.66e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280238   1 MLSNNCSILLIDDDADVLDAYTQLLEQAGYH-VSACNNPFDAREQVPKDWPGIVLSDVCMPGCSGIDLMTVFHQDDDL-- 77
Cdd:PRK10610   1 MADKELKFLVVDDFSTMRRIVRNLLKELGFNnVEEAEDGVDALNKLQAGGFGFVISDWNMPNMDGLELLKTIRADGAMsa 80

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 490280238  78 LPILLITGHGDVPMAVEAVKKGAWDFLQKPIDPGKL 113
Cdd:PRK10610  81 LPVLMVTAEAKKENIIAAAQAGASGYVVKPFTAATL 116
REC_WspR-like cd17575
phosphoacceptor receiver (REC) domain of WspR response regulator and similar proteins; The ...
 7-114 2.09e-05

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: 43.94  E-value: 2.09e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280238   7 SILLIDDDADVLDAYTQLL-EQAGYHVSACNNPFDAREQVPKDWPGIVLSDVCMPGCSGIDLMTVFHQDDDL--LPILLI 83
Cdd:cd17575    2 MVLLVDDQAIIGEAVRRALaDEEDIDFHYCSDPTEAIEVASQIKPTVILQDLVMPGVDGLTLVRFFRANPATrdIPIIVL 81

                         90       100       110
                 ....*....|....*....|....*....|.
gi 490280238  84 TGHGDVPMAVEAVKKGAWDFLQKPIDPGKLL 114
Cdd:cd17575   82 STKEEPEVKSEAFALGANDYLVKLPDKIELV 112
dpiA PRK10046
two-component response regulator DpiA; Provisional
 7-137 2.12e-05

two-component response regulator DpiA; Provisional


Pssm-ID: 182208 [Multi-domain]  Cd Length: 225  Bit Score: 45.39  E-value: 2.12e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280238   7 SILLIDDDADVLDAYTQLLEQ-AGY-HVSACNNPFDAREQVPKDWPGIVLSDVCMPGCSGIDLMTVFHQDDDLLPILLIT 84
Cdd:PRK10046   6 TLLIVEDETPLAEMHAEYIRHiPGFsQILLAGNLAQARMMIERFKPGLILLDNYLPDGRGINLLHELVQAHYPGDVVFTT 85

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 490280238  85 GHGDVPMAVEAVKKGAWDFLQKPI---DPGKLLTlvdaALRQRQSVIARRQYCQQK 137
Cdd:PRK10046  86 AASDMETVSEAVRCGVFDYLIKPIayeRLGQTLT----RFRQRKHMLESIDSASQK 137
REC_OmpR_MtPhoP-like cd17615
phosphoacceptor receiver (REC) domain of MtPhoP-like OmpR family response regulators; ...
 8-123 2.21e-05

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: 43.50  E-value: 2.21e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280238   8 ILLIDDDADVLDAYTQLLEQAGYHVSACNNPFDAREQVPKDWPGIVLSDVCMPGCSGIDLMTVFHQDDDLLPILLITGHG 87
Cdd:cd17615    2 VLVVDDEPNITELLSMALRYEGWDVETAADGAEALAAAREFRPDAVVLDIMLPDMDGLEVLRRLRADGPDVPVLFLTAKD 81

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 490280238  88 DVPMAVEAVKKGAWDFLQKPIDPGKLLTLVDAALRQ 123
Cdd:cd17615   82 SVEDRIAGLTAGGDDYVTKPFSLEEVVARLRALLRR 117
REC_OmpR_KdpE-like cd17620
phosphoacceptor receiver (REC) domain of KdpE-like OmpR family response regulators; KdpE is a ...
 8-107 2.55e-05

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: 42.92  E-value: 2.55e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280238   8 ILLIDDDADVLDAYTQLLEQAGYHVSACNNPFDAREQVPKDWPGIVLSDVCMPGCSGIDLMTVFHQDDDlLPILLITGHG 87
Cdd:cd17620    1 ILVIEDEPQIRRFLRTALEAHGYRVFEAETGQEGLLEAATRKPDLIILDLGLPDMDGLEVIRRLREWSA-VPVIVLSARD 79

                         90       100
                 ....*....|....*....|
gi 490280238  88 DVPMAVEAVKKGAWDFLQKP 107
Cdd:cd17620   80 EESDKIAALDAGADDYLTKP 99
REC_PatA-like cd17602
phosphoacceptor receiver (REC) domain of PatA and similar domains; Nostoc sp. (or Anabaena sp.) ...
 8-107 4.25e-05

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: 42.36  E-value: 4.25e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280238   8 ILLIDDDADVLDAYTQLLEQAGYHVSACNNPFDAREQVPKDWPGIVLSDVCMPGCSGIDLMTVFHQDDDL--LPILLITG 85
Cdd:cd17602    1 VACVDDRPSIQKMIEYFLEKQGFRVVVIDDPLRALTTLLNSKPDLILIDIDMPDLDGYELCSLLRKSSALkdTPIIMLTG 80

                         90       100
                 ....*....|....*....|..
gi 490280238  86 HGDVPMAVEAVKKGAWDFLQKP 107
Cdd:cd17602   81 KDGLVDRIRAKMAGASGYLTKP 102
PRK10336 PRK10336
two-component system response regulator QseB;
8-122 5.47e-05

two-component system response regulator QseB;


Pssm-ID: 182387 [Multi-domain]  Cd Length: 219  Bit Score: 44.12  E-value: 5.47e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280238   8 ILLIDDDADVLDAYTQLLEQAGYHV-----------SACNNPFDAreqvpkdwpgiVLSDVCMPGCSGIDLMTVFHQDDD 76
Cdd:PRK10336   3 ILLIEDDMLIGDGIKTGLSKMGFSVdwftqgrqgkeALYSAPYDA-----------VILDLTLPGMDGRDILREWREKGQ 71

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 490280238  77 LLPILLITGHGDVPMAVEAVKKGAWDFLQKPidpgklLTLVDAALR 122
Cdd:PRK10336  72 REPVLILTARDALAERVEGLRLGADDYLCKP------FALIEVAAR 111
REC_OmpR_ArcA_TorR-like cd17619
phosphoacceptor receiver (REC) domain of ArcA- and TorR-like OmpR family response regulators; ...
 7-114 5.77e-05

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: 41.99  E-value: 5.77e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280238   7 SILLIDDDADVLDAYTQLLEQAGYHVSACNNPFDAREQVPKDWPGIVLSDVCMPGCSGIDLMTVFHQDDDlLPILLITGH 86
Cdd:cd17619    2 HILIVEDEPVTRATLKSYFEQEGYDVSEAGDGEEMRQILARQDIDLVLLDINLPGKDGLSLTRELREQSE-VGIILVTGR 80

                         90       100
                 ....*....|....*....|....*...
gi 490280238  87 GDVPMAVEAVKKGAWDFLQKPIDPGKLL 114
Cdd:cd17619   81 DDEVDRIVGLEIGADDYVTKPFNPRELL 108
PRK10816 PRK10816
two-component system response regulator PhoP;
8-142 5.96e-05

two-component system response regulator PhoP;


Pssm-ID: 182755 [Multi-domain]  Cd Length: 223  Bit Score: 43.96  E-value: 5.96e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280238   8 ILLIDDDADVLDAYTQLLEQAGYHVSACNNPFDAREQVPKDWPGIVLSDVCMPGCSGIDLMTVFHQDDDLLPILLITGHG 87
Cdd:PRK10816   3 VLVVEDNALLRHHLKVQLQDAGHQVDAAEDAKEADYYLNEHLPDIAIVDLGLPDEDGLSLIRRWRSNDVSLPILVLTARE 82

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 490280238  88 DVPMAVEAVKKGAWDFLQKPIDPGKLLTLVDAALRqRQSVIARRQYCQQKLQVEL 142
Cdd:PRK10816  83 SWQDKVEVLSAGADDYVTKPFHIEEVMARMQALMR-RNSGLASQVISLPPFQVDL 136
REC_RR468-like cd17552
phosphoacceptor receiver (REC) domain of Thermotoga maritima response regulator RR468 and ...
 8-113 7.51e-05

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


Pssm-ID: 381104 [Multi-domain]  Cd Length: 121  Bit Score: 42.15  E-value: 7.51e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280238   8 ILLIDDDADVLD-AYTQLLEQAGYHVSACNNPFDAREQVPKDWPGIVLSDVCMPGCSGIdlmTVFH--QDDDL---LPIL 81
Cdd:cd17552    4 ILVIDDEEDIREvVQACLEKLAGWEVLTASSGQEGLEKAATEQPDAILLDVMMPDMDGL---ATLKklQANPEtqsIPVI 80

                         90       100       110
                 ....*....|....*....|....*....|..
gi 490280238  82 LITGHGDVPMAVEAVKKGAWDFLQKPIDPGKL 113
Cdd:cd17552   81 LLTAKAQPSDRQRFASLGVAGVIAKPFDPLTL 112
PRK10643 PRK10643
two-component system response regulator PmrA;
8-174 7.69e-05

two-component system response regulator PmrA;


Pssm-ID: 182612 [Multi-domain]  Cd Length: 222  Bit Score: 43.87  E-value: 7.69e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280238   8 ILLIDDDADVLDAYTQLLEQAGYHVSACNNPFDAREQVPKDWPGIVLSDVCMPGCSGIDLMTVFHQDDDLLPILLITGHG 87
Cdd:PRK10643   3 ILIVEDDTLLLQGLILALQTEGYACDCASTAREAEALLESGHYSLVVLDLGLPDEDGLHLLRRWRQKKYTLPVLILTARD 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280238  88 DVPMAVEAVKKGAWDFLQKPIDPGKLLTLVDAALRQRQSV-------------IARRQYCQQKLQVE-----------LI 143
Cdd:PRK10643  83 TLEDRVAGLDVGADDYLVKPFALEELHARIRALIRRHQGQgenelqvgnltlnLGRQQVWLDGQELIltpkefallsrLM 162

                        170       180       190
                 ....*....|....*....|....*....|.
gi 490280238 144 GRSQWTVrYRQRLQQlaetDIAVWlYGEPGT 174
Cdd:PRK10643 163 LKAGSPV-HREILYQ----DIYNW-DDEPSS 187
PRK13856 PRK13856
two-component response regulator VirG; Provisional
 8-155 1.01e-04

two-component response regulator VirG; Provisional


Pssm-ID: 172377 [Multi-domain]  Cd Length: 241  Bit Score: 43.65  E-value: 1.01e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280238   8 ILLIDDDADVLDAYTQLLEQAGYHVSACNNPFDAREQVPKDWPGIVLSDVCMPGCSGIDLMTVFHQDDDLlPILLITGHG 87
Cdd:PRK13856   4 VLVIDDDVAMRHLIVEYLTIHAFKVTAVADSQQFNRVLASETVDVVVVDLNLGREDGLEIVRSLATKSDV-PIIIISGDR 82

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490280238  88 -DVPMAVEAVKKGAWDFLQKPIDPGKLLTLVDAALRQRQSVIA---RRQYCqqklqveligRSQWTVRYRQR 155
Cdd:PRK13856  83 lEEADKVVALELGATDFIAKPFGTREFLARIRVALRVRPNVVRtkdRRSFC----------FADWTLNLRQR 144
REC_NarL cd19931
phosphoacceptor receiver (REC) domain of Nitrate/Nitrite response regulator L (NarL); Nitrate ...
 8-121 1.08e-04

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


Pssm-ID: 381158 [Multi-domain]  Cd Length: 117  Bit Score: 41.56  E-value: 1.08e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280238   8 ILLIDDDADVLDAYTQLLEQAGYH--VSACNNPFDAREQVPKDWPGIVLSDVCMPGCSGIDLMTVFHQDDDLLPILLIT- 84
Cdd:cd19931    1 VLLIDDHPLLRKGIKQLIELDPDFtvVGEASSGEEGIELAERLDPDLILLDLNMKGMSGLDTLKALREEGVSARIVILTv 80

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 490280238  85 --GHGDVpmaVEAVKKGAWDFLQKPIDPGKLLTLVDAAL 121
Cdd:cd19931   81 sdAEDDV---VTALRAGADGYLLKDMEPEDLLEALKQAA 116
REC_LytTR_AlgR-like cd17532
phosphoacceptor receiver (REC) domain of LytTR/AlgR family response regulators similar to AlgR; ...
 8-125 1.09e-04

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: 41.37  E-value: 1.09e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280238   8 ILLIDDDADVLDAYTQLLEQAGYH--VSACNNPFDAREQVPKDWPGIVLSDVCMPGCSGIDLMTVFHQDDDLLPILLITG 85
Cdd:cd17532    1 ALIVDDEPLAREELRYLLEEHPDIeiVGEAENGEEALEAIEELKPDVVFLDIQMPGLDGLELAKKLSKLAKPPLIVFVTA 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 490280238  86 HGDvpMAVEAVKKGAWDFLQKPIDPGKLLTLVDAALRQRQ 125
Cdd:cd17532   81 YDE--YAVEAFELNAVDYLLKPFSEERLAEALAKLRKRLS 118
REC_OmpR_NsrR-like cd18159
phosphoacceptor receiver (REC) domain of Streptococcus agalactiae NsrR-like OmpR family ...
 8-121 1.11e-04

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: 41.50  E-value: 1.11e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280238   8 ILLIDDDADVLDAYTQLLEQAGYHVSACNNPFDAREQVPKDWPGIVLSDVCMPG------CSGI-DLMTVfhqdddllPI 80
Cdd:cd18159    1 ILIVEDDETIASLLKKHLEKWGYEVVLIEDFEDVLEEFLQFKPDLVLLDINLPYfdgfywCREIrQISNV--------PI 72

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 490280238  81 LLIT---GHGDVPMAVEAvkkGAWDFLQKPIDPGKLLTLVDAAL 121
Cdd:cd18159   73 IFISsrdDNMDQVMAINM---GGDDYITKPFDLDVLLAKIKAIL 113
pleD PRK09581
response regulator PleD; Reviewed
 8-130 1.18e-04

response regulator PleD; Reviewed


Pssm-ID: 236577 [Multi-domain]  Cd Length: 457  Bit Score: 44.12  E-value: 1.18e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280238   8 ILLIDDdadvLDAYTQLLE---QAGYH-VSACNNPFDAREQVPKDWPGIVLSDVCMPGCSGI--------DLMTVFhqdd 75
Cdd:PRK09581   5 ILVVDD----IPANVKLLEaklLAEYYtVLTASSGAEAIAICEREQPDIILLDVMMPGMDGFevcrrlksDPATTH---- 76

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490280238  76 dlLPILLITGHGDVPMAVEAVKKGAWDFLQKPIDPGKLL----------TLVDaALRQRQSVIAR 130
Cdd:PRK09581  77 --IPVVMVTALDDPEDRVRGLEAGADDFLTKPINDVALFarvksltrlkMVID-ELRLRASTNAE 138
PRK13557 PRK13557
histidine kinase; Provisional
 8-121 4.63e-04

histidine kinase; Provisional


Pssm-ID: 237425 [Multi-domain]  Cd Length: 540  Bit Score: 42.35  E-value: 4.63e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280238   8 ILLIDDDADVLDAYTQLLEQAGYHVSACNNPFDAREQV-PKDWPGIVLSDVCMPG-CSGIDLMTVFHQDDDLLPILLITG 85
Cdd:PRK13557 418 ILIVDDRPDVAELARMILEDFGYRTLVASNGREALEILdSHPEVDLLFTDLIMPGgMNGVMLAREARRRQPKIKVLLTTG 497

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 490280238  86 HGDVPMAVEAVKKGAWDFLQKPIDPGKLLTLVDAAL 121
Cdd:PRK13557 498 YAEASIERTDAGGSEFDILNKPYRRAELARRVRMVL 533
REC_CheC-like cd17593
phosphoacceptor receiver (REC) domain of uncharacterized response regulators containing a CheC ...
 9-116 5.67e-04

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: 39.44  E-value: 5.67e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280238   9 LLIDDDADVldAYTQLL----EQAGYHVSACNNPFDAREQVPKDWPGIVLSDVCMPGCSGIDLMTVFHQDDdlLPILLIT 84
Cdd:cd17593    3 VLICDDSSM--ARKQLAralpADWDVEITFAENGEEALEILREGRIDVLFLDLTMPVMDGYEVLEALPVEQ--LETKVIV 78

                         90       100       110
                 ....*....|....*....|....*....|....
gi 490280238  85 GHGDV-PMAVEAVKK-GAWDFLQKPIDPGKLLTL 116
Cdd:cd17593   79 VSGDVqPEAKERVLElGALAFLKKPFDPEKLAQL 112
REC_hyHK_blue-like cd18161
phosphoacceptor receiver (REC) domain of hybrid sensor histidine kinase/response regulators ...
 8-107 6.65e-04

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


Pssm-ID: 381145 [Multi-domain]  Cd Length: 102  Bit Score: 38.87  E-value: 6.65e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280238   8 ILLIDDDADVLDAYTQLLEQAGYHVSACNNPFDAREQVPKDW-PGIVLSDVCMPG-CSGIDLMTVFHQDDDLLPILLITG 85
Cdd:cd18161    1 VLVVEDDPDVRRLTAEVLEDLGYTVLEAASGDEALDLLESGPdIDLLVTDVIMPGgMNGSQLAEEARRRRPDLKVLLTSG 80

                         90       100
                 ....*....|....*....|..
gi 490280238  86 HGDVPMAVEAVKKGAWdFLQKP 107
Cdd:cd18161   81 YAENAIEGGDLAPGVD-VLSKP 101
REC_HP-RR-like cd17573
phosphoacceptor receiver (REC) domain of orphan response regulator HP-RR and similar proteins; ...
 8-114 7.09e-04

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: 38.95  E-value: 7.09e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280238   8 ILLIDDDADVLDAYTQLLEQAGYHVSACNNPFDAREQVPKDWPGIVLSDVCMPGCSGIDLMTVFHQDDDLLPILLITGHG 87
Cdd:cd17573    1 ILLIEDDSTLGKEISKGLNEKGYQADVAESLKDGEYYIDIRNYDLVLVSDKLPDGNGLSIVSRIKEKHPSIVVIVLSDNP 80

                         90       100
                 ....*....|....*....|....*..
gi 490280238  88 DVPMAVEAVKKGAWDFLQKPIDPGKLL 114
Cdd:cd17573   81 KTEQEIEAFKEGADDYIAKPFDFKVLV 107
PRK11083 PRK11083
DNA-binding response regulator CreB; Provisional
 8-125 7.34e-04

DNA-binding response regulator CreB; Provisional


Pssm-ID: 236838 [Multi-domain]  Cd Length: 228  Bit Score: 40.72  E-value: 7.34e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280238   8 ILLIDDDADVLDAYTQLLEQAGYHVSACNNPFDAREQVPKDWPGIVLSDVCMPGCSGIDL---MTVFHQDddlLPILLIT 84
Cdd:PRK11083   6 ILLVEDEQAIADTLVYALQSEGFTVEWFERGLPALDKLRQQPPDLVILDVGLPDISGFELcrqLLAFHPA---LPVIFLT 82

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 490280238  85 GHGDVPMAVEAVKKGAWDFLQKPIDPGKLLTLVDAALRQRQ 125
Cdd:PRK11083  83 ARSDEVDRLVGLEIGADDYVAKPFSPREVAARVRTILRRVK 123
REC_GlnL-like cd17565
phosphoacceptor receiver (REC) domain of transcriptional regulatory protein GlnL and similar ...
 8-108 1.08e-03

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: 1.08e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280238   8 ILLIDDDADVLDAYTQLLEQA--GYHVSACNNPFDAREQVPKDWPGIVLSDVCMPGCSGIDLMTVFHQDDDLLPILLITG 85
Cdd:cd17565    1 FYIVDDDKNIIKILSDIIEDDdlGEVVGEADNGAQAYDEILFLQPDIVLIDLLMPGMDGIQLVRKLKDTGSNGKFIMISQ 80

                         90       100
                 ....*....|....*....|...
gi 490280238  86 HGDVPMAVEAVKKGAWDFLQKPI 108
Cdd:cd17565   81 VSDKEMIGKAYQAGIEFFINKPI 103
REC_CheV-like cd19924
phosphoacceptor receiver (REC) domain of chemotaxis protein CheV and similar proteins; This ...
 8-107 1.17e-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: 38.51  E-value: 1.17e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280238   8 ILLIDDDADVLDAYTQLLEQAGYHVSACNNPFDA---------REQVPKDWPGIVLSDVCMPGCSGIDLMTVFHQDDDL- 77
Cdd:cd19924    1 ILVVDDSPTARKQLRDLLKNLGFEIAEAVDGEEAlnklenlakEGNDLSKELDLIITDIEMPKMDGYELTFELRDDPRLa 80

                         90       100       110
                 ....*....|....*....|....*....|.
gi 490280238  78 -LPILLITGHGDVPMAVEAVKKGAWDFLQKP 107
Cdd:cd19924   81 nIPVILNSSLSGEFSRARGKKVGADAYLAKF 111
PRK10710 PRK10710
DNA-binding transcriptional regulator BaeR; Provisional
 4-173 1.97e-03

DNA-binding transcriptional regulator BaeR; Provisional


Pssm-ID: 182665 [Multi-domain]  Cd Length: 240  Bit Score: 39.67  E-value: 1.97e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280238   4 NNCSILLIDDDADVLDAYTQLLEQAGYHVSACNNPFDAREQVPKDWPGIVLSDVCMPGCSGIDLMTVFHQDDDlLPILLI 83
Cdd:PRK10710   9 NTPRILIVEDEPKLGQLLIDYLQAASYATTLLSHGDEVLPYVRQTPPDLILLDLMLPGTDGLTLCREIRRFSD-IPIVMV 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280238  84 TGHGDVPMAVEAVKKGAWDFLQKPIDPGKLLTLVDAALRQrqsviARRQYCQQKLQVE---LIGRSQWTVRYRQRLQQL- 159
Cdd:PRK10710  88 TAKIEEIDRLLGLEIGADDYICKPYSPREVVARVKTILRR-----CKPQRELQQQDAEsplIIDESRFQASWRGKMLDLt 162

                        170
                 ....*....|....*
gi 490280238 160 -AETDIAVWLYGEPG 173
Cdd:PRK10710 163 pAEFRLLKTLSHEPG 177
psREC-like_D2_PleD cd17539
REC-like adaptor domain (D2) of response regulator PleD; PleD contains a REC domain (D1) with ...
 78-124 2.07e-03

REC-like adaptor domain (D2) of response regulator PleD; PleD contains a REC domain (D1) with the phosphorylatable aspartate, a pseudo receiver (psREC)-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 the REC-like adaptor domain D2 of PleD, which is an inactive domain.


Pssm-ID: 381094 [Multi-domain]  Cd Length: 124  Bit Score: 38.06  E-value: 2.07e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 490280238  78 LPILLITGHGDVPMAVEAVKKGAWDFLQKPIDPGKLLTLVDAALRQR 124
Cdd:cd17539   72 LPILAVADPGDRGRLIRALEIGVNDYLVRPIDPNELLARVRTQIRRK 118
PRK10529 PRK10529
DNA-binding transcriptional activator KdpE; Provisional
 5-123 2.79e-03

DNA-binding transcriptional activator KdpE; Provisional


Pssm-ID: 182522 [Multi-domain]  Cd Length: 225  Bit Score: 39.02  E-value: 2.79e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280238   5 NCSILLIDDDADVLDAYTQLLEQAGYHVsacnnpFDARE------QVPKDWPGIVLSDVCMPGCSGIDLMTVFHQDDDLl 78
Cdd:PRK10529   1 MTNVLIVEDEQAIRRFLRTALEGDGMRV------FEAETlqrgllEAATRKPDLIILDLGLPDGDGIEFIRDLRQWSAI- 73

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 490280238  79 PILLITGHGDVPMAVEAVKKGAWDFLQKPIDPGKLLTLVDAALRQ 123
Cdd:PRK10529  74 PVIVLSARSEESDKIAALDAGADDYLSKPFGIGELQARLRVALRR 118
REC_TrxB cd17595
phosphoacceptor receiver (REC) domain a fused response regulator with a thioredoxin reductase ...
 8-110 4.06e-03

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


Pssm-ID: 381126 [Multi-domain]  Cd Length: 135  Bit Score: 37.32  E-value: 4.06e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280238   8 ILLIDDDADVLDAYTQLLE---QAGYHV---SACNNPFDAREQVPK--DWPGIVLSDVCMPGCSGIDLMtvfHQDDDLLP 79
Cdd:cd17595    3 ILTVDDDPQVLRAVARDLRrqyGKDYRVlraDSGAEALDALKELKLrgEAVALFLVDQRMPEMDGVEFL---EKAMELFP 79

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 490280238  80 I---LLITGHGDVPMAVEAVKKGAWDF-LQKPIDP 110
Cdd:cd17595   80 EakrVLLTAYADTDAAIRAINDVQLDYyLLKPWDP 114
PRK10693 PRK10693
two-component system response regulator RssB;
37-129 4.24e-03

two-component system response regulator RssB;


Pssm-ID: 182652 [Multi-domain]  Cd Length: 303  Bit Score: 38.82  E-value: 4.24e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490280238  37 NPFDAREQVPKDWPGIVLSDVCMPGCSGIDLMTVFHQDDDLLPILLITGHGDVPMAVEAVKKGAWDFLQKPIdpgKLLTl 116
Cdd:PRK10693   5 NGVDALELLGGFTPDLIICDLAMPRMNGIEFVEHLRNRGDQTPVLVISATENMADIAKALRLGVQDVLLKPV---KDLN- 80

                         90
                 ....*....|...
gi 490280238 117 vdaalRQRQSVIA 129
Cdd:PRK10693  81 -----RLREMVFA 88
pleD PRK09581
response regulator PleD; Reviewed
 77-138 7.85e-03

response regulator PleD; Reviewed


Pssm-ID: 236577 [Multi-domain]  Cd Length: 457  Bit Score: 38.34  E-value: 7.85e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490280238  77 LLPILLITGHGDVPMAVEAVKKGAWDFLQKPIDPGKLLTLVDAALRQRQSVIARRQYCQQKL 138
Cdd:PRK09581 228 YVPILLLVDEDDDPRLVKALELGVNDYLMRPIDKNELLARVRTQIRRKRYQDALRNNLEQSI 289
 
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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