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Conserved domains on  [gi|1209301716|ref|WP_088346897|]
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MULTISPECIES: ATP-binding protein [Rhodomicrobium]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PRK13557 super family cl36263
histidine kinase; Provisional
166-557 1.75e-139

histidine kinase; Provisional


The actual alignment was detected with superfamily member PRK13557:

Pssm-ID: 237425 [Multi-domain]  Cd Length: 540  Bit Score: 414.84  E-value: 1.75e-139
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209301716 166 RRKAEELLRQAQKMEVVGQLTGGVAHDFNNLLTIVLGGLDIIgrQLPALGPSPEAERIAKARDMAVEGARRSATLTSRLL 245
Cdd:PRK13557  147 RRDAEDALRQAQKMEALGQLTGGIAHDFNNLLQVMSGYLDVI--QAALSHPDADRGRMARSVENIRAAAERAATLTQQLL 224
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209301716 246 AFSRRQPLDPRPLDANKLIASTGELLHRTLGEQIALETVLAAGLWRVHADANQLENSLINLALNARDAMPTGGRMTIETA 325
Cdd:PRK13557  225 AFARKQRLEGRVLNLNGLVSGMGELAERTLGDAVTIETDLAPDLWNCRIDPTQAEVALLNVLINARDAMPEGGRVTIRTR 304
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209301716 326 NCHLDGAYVAGIAePVEPGQYVMVAVTDSGLGMDKSTQEKAFEPFFTTKAVGQGTGLGLSQVYGFVRQSSGHIRIYSELG 405
Cdd:PRK13557  305 NVEIEDEDLAMYH-GLPPGRYVSIAVTDTGSGMPPEILARVMDPFFTTKEEGKGTGLGLSMVYGFAKQSGGAVRIYSEVG 383
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209301716 406 EGSTVKIYLPrYAGAEEAAPFVPPELTARAGGSELILVVEDDASLRGYTVQILTELGYGVLEAADGRIGLKVLAERGDID 485
Cdd:PRK13557  384 EGTTVRLYFP-ASDQAENPEQEPKARAIDRGGTETILIVDDRPDVAELARMILEDFGYRTLVASNGREALEILDSHPEVD 462
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1209301716 486 LLFTDIVMPGGLNGRELADEAVKLHPALKVLFTTGYTRNAIVHHGRLDPGVHFLGKPFSFDELALKIRSVLD 557
Cdd:PRK13557  463 LLFTDLIMPGGMNGVMLAREARRRQPKIKVLLTTGYAEASIERTDAGGSEFDILNKPYRRAELARRVRMVLD 534
PRK09776 super family cl32410
putative diguanylate cyclase; Provisional
18-136 1.90e-14

putative diguanylate cyclase; Provisional


The actual alignment was detected with superfamily member PRK09776:

Pssm-ID: 182070 [Multi-domain]  Cd Length: 1092  Bit Score: 76.63  E-value: 1.90e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209301716   18 EVLALAQEAGRVGIFEWHVPAGTLLVSQQFLVIYGLDcFDGR--HESWLACVFREDVARIVDQTENAFRRRdREMLMEFR 95
Cdd:PRK09776   410 ERITLANEAGGIGIWEWDLKPNIISWDKRMFELYEIP-PHIKptWQVWYACLHPEDRQRVEKEIRDALQGR-SPFKLEFR 487
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 1209301716   96 ILRPGdgGLVWIEARSIIFYDADGRAIRMVGVNADITERKR 136
Cdd:PRK09776   488 IVVKD--GVRHIRALANRVLNKDGEVERLLGINMDMTEVRQ 526
 
Name Accession Description Interval E-value
PRK13557 PRK13557
histidine kinase; Provisional
166-557 1.75e-139

histidine kinase; Provisional


Pssm-ID: 237425 [Multi-domain]  Cd Length: 540  Bit Score: 414.84  E-value: 1.75e-139
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209301716 166 RRKAEELLRQAQKMEVVGQLTGGVAHDFNNLLTIVLGGLDIIgrQLPALGPSPEAERIAKARDMAVEGARRSATLTSRLL 245
Cdd:PRK13557  147 RRDAEDALRQAQKMEALGQLTGGIAHDFNNLLQVMSGYLDVI--QAALSHPDADRGRMARSVENIRAAAERAATLTQQLL 224
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209301716 246 AFSRRQPLDPRPLDANKLIASTGELLHRTLGEQIALETVLAAGLWRVHADANQLENSLINLALNARDAMPTGGRMTIETA 325
Cdd:PRK13557  225 AFARKQRLEGRVLNLNGLVSGMGELAERTLGDAVTIETDLAPDLWNCRIDPTQAEVALLNVLINARDAMPEGGRVTIRTR 304
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209301716 326 NCHLDGAYVAGIAePVEPGQYVMVAVTDSGLGMDKSTQEKAFEPFFTTKAVGQGTGLGLSQVYGFVRQSSGHIRIYSELG 405
Cdd:PRK13557  305 NVEIEDEDLAMYH-GLPPGRYVSIAVTDTGSGMPPEILARVMDPFFTTKEEGKGTGLGLSMVYGFAKQSGGAVRIYSEVG 383
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209301716 406 EGSTVKIYLPrYAGAEEAAPFVPPELTARAGGSELILVVEDDASLRGYTVQILTELGYGVLEAADGRIGLKVLAERGDID 485
Cdd:PRK13557  384 EGTTVRLYFP-ASDQAENPEQEPKARAIDRGGTETILIVDDRPDVAELARMILEDFGYRTLVASNGREALEILDSHPEVD 462
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1209301716 486 LLFTDIVMPGGLNGRELADEAVKLHPALKVLFTTGYTRNAIVHHGRLDPGVHFLGKPFSFDELALKIRSVLD 557
Cdd:PRK13557  463 LLFTDLIMPGGMNGVMLAREARRRQPKIKVLLTTGYAEASIERTDAGGSEFDILNKPYRRAELARRVRMVLD 534
COG4191 COG4191
Signal transduction histidine kinase regulating C4-dicarboxylate transport system [Signal ...
71-416 6.99e-86

Signal transduction histidine kinase regulating C4-dicarboxylate transport system [Signal transduction mechanisms];


Pssm-ID: 443345 [Multi-domain]  Cd Length: 361  Bit Score: 270.52  E-value: 6.99e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209301716  71 DVARIVDQTENAFRRRDREMLMEFRILRPGDGGLVWIEARSIIFYDADGRAIRMVGVNADITERKRAILQLRAFTETMEE 150
Cdd:COG4191    31 LLLALLLLLLALLLALLALLLLLLLLLLLLLLELLLLLLALLGGLLRLLLLLGLLLLLLLEALLLLLLAALDAEENAELE 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209301716 151 AVRERTRELVAENEARRKAEELLRQAQKMEVVGQLTGGVAHDFNNLLTIVLGGLDIIGRQLPAlgpSPEAERIAKARDMA 230
Cdd:COG4191   111 ELERDITELERAEEELRELQEQLVQSEKLAALGELAAGIAHEINNPLAAILGNAELLRRRLED---EPDPEELREALERI 187
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209301716 231 VEGARRSATLTSRLLAFSRRQPLDPRPLDANKLIASTGELLHRTLGEQ-IALETVLAAGLWRVHADANQLENSLINLALN 309
Cdd:COG4191   188 LEGAERAAEIVRSLRAFSRRDEEEREPVDLNELIDEALELLRPRLKARgIEVELDLPPDLPPVLGDPGQLEQVLLNLLIN 267
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209301716 310 ARDAMPTG--GRMTIETAnchldgayvagiaepvEPGQYVMVAVTDSGLGMDKSTQEKAFEPFFTTKAVGQGTGLGLSQV 387
Cdd:COG4191   268 AIDAMEEGegGRITISTR----------------REGDYVVISVRDNGPGIPPEVLERIFEPFFTTKPVGKGTGLGLSIS 331
                         330       340
                  ....*....|....*....|....*....
gi 1209301716 388 YGFVRQSSGHIRIYSELGEGSTVKIYLPR 416
Cdd:COG4191   332 YGIVEKHGGRIEVESEPGGGTTFTITLPL 360
HATPase_CckA-like cd16919
Histidine kinase-like ATPase domain of two-component sensor hybrid histidine kinases, similar ...
299-415 8.08e-54

Histidine kinase-like ATPase domain of two-component sensor hybrid histidine kinases, similar to Brucella abortus 2308 CckA; This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component hybrid sensor histidine kinase (HKs) similar to Brucella abortus 2308 CckA, which is a component of an essential protein phosphorelay that regulates expression of genes required for growth, division, and intracellular survival; phosphoryl transfer initiates from the sensor kinase CckA and proceeds via the ChpT phosphotransferase to two regulatory substrates: the DNA-binding response regulator CtrA and the phospho-receiver protein CpdR. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA), a REC signal receiver domain, and some contain PAS or PAS and GAF sensor domain(s).


Pssm-ID: 340396 [Multi-domain]  Cd Length: 116  Bit Score: 177.96  E-value: 8.08e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209301716 299 LENSLINLALNARDAMPTGGRMTIETANCHLDGAYVAGIAEpVEPGQYVMVAVTDSGLGMDKSTQEKAFEPFFTTKAVGQ 378
Cdd:cd16919     1 LELAILNLAVNARDAMPEGGRLTIETSNQRVDADYALNYRD-LIPGNYVCLEVSDTGSGMPAEVLRRAFEPFFTTKEVGK 79
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1209301716 379 GTGLGLSQVYGFVRQSSGHIRIYSELGEGSTVKIYLP 415
Cdd:cd16919    80 GTGLGLSMVYGFVKQSGGHLRIYSEPGVGTTVRIYLP 116
HATPase_c smart00387
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.
294-415 1.72e-19

Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.


Pssm-ID: 214643 [Multi-domain]  Cd Length: 111  Bit Score: 83.85  E-value: 1.72e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209301716  294 ADANQLENSLINLALNARDAMPTGGRMTIETANChldgayvagiaepvepGQYVMVAVTDSGLGMDKSTQEKAFEPFFTT 373
Cdd:smart00387   1 GDPDRLRQVLSNLLDNAIKYTPEGGRITVTLERD----------------GDHVEITVEDNGPGIPPEDLEKIFEPFFRT 64
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 1209301716  374 KA---VGQGTGLGLSQVYGFVRQSSGHIRIYSELGEGSTVKIYLP 415
Cdd:smart00387  65 DKrsrKIGGTGLGLSIVKKLVELHGGEISVESEPGGGTTFTITLP 109
Response_reg pfam00072
Response regulator receiver domain; This domain receives the signal from the sensor partner in ...
441-553 2.75e-18

Response regulator receiver domain; This domain receives the signal from the sensor partner in bacterial two-component systems. It is usually found N-terminal to a DNA binding effector domain.


Pssm-ID: 395025 [Multi-domain]  Cd Length: 111  Bit Score: 80.66  E-value: 2.75e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209301716 441 ILVVEDDASLRGYTVQILTELGYGVLEAADGRIGLKVLAERgDIDLLFTDIVMPgGLNGRELADEAVKLHPALKVLFTTG 520
Cdd:pfam00072   1 VLIVDDDPLIRELLRQLLEKEGYVVAEADDGKEALELLKEE-RPDLILLDINMP-GMDGLELLKRIRRRDPTTPVIILTA 78
                          90       100       110
                  ....*....|....*....|....*....|....
gi 1209301716 521 YTRNAIVHHGrLDPGVH-FLGKPFSFDELALKIR 553
Cdd:pfam00072  79 HGDEDDAVEA-LEAGADdFLSKPFDPDELLAAIR 111
PRK09776 PRK09776
putative diguanylate cyclase; Provisional
18-136 1.90e-14

putative diguanylate cyclase; Provisional


Pssm-ID: 182070 [Multi-domain]  Cd Length: 1092  Bit Score: 76.63  E-value: 1.90e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209301716   18 EVLALAQEAGRVGIFEWHVPAGTLLVSQQFLVIYGLDcFDGR--HESWLACVFREDVARIVDQTENAFRRRdREMLMEFR 95
Cdd:PRK09776   410 ERITLANEAGGIGIWEWDLKPNIISWDKRMFELYEIP-PHIKptWQVWYACLHPEDRQRVEKEIRDALQGR-SPFKLEFR 487
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 1209301716   96 ILRPGdgGLVWIEARSIIFYDADGRAIRMVGVNADITERKR 136
Cdd:PRK09776   488 IVVKD--GVRHIRALANRVLNKDGEVERLLGINMDMTEVRQ 526
PAS_3 pfam08447
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
41-128 3.85e-14

PAS fold; The PAS fold corresponds to the structural domain that has previously been defined as PAS and PAC motifs. The PAS fold appears in archaea, eubacteria and eukarya.


Pssm-ID: 430001 [Multi-domain]  Cd Length: 89  Bit Score: 68.13  E-value: 3.85e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209301716  41 LLVSQQFLVIYGLDC--FDGRHESWLACVFREDVARIVDQTENAFRRRDREMLmEFRILRPgDGGLVWIEARSIIFYDAD 118
Cdd:pfam08447   2 IYWSPRFEEILGYTPeeLLGKGESWLDLVHPDDRERVREALWEALKGGEPYSG-EYRIRRK-DGEYRWVEARARPIRDEN 79
                          90
                  ....*....|
gi 1209301716 119 GRAIRMVGVN 128
Cdd:pfam08447  80 GKPVRVIGVA 89
nifL_nitrog TIGR02938
nitrogen fixation negative regulator NifL; NifL is a modulator of the nitrogen fixation ...
69-415 1.65e-11

nitrogen fixation negative regulator NifL; NifL is a modulator of the nitrogen fixation positive regulator protein NifA, and is therefore a negative regulator. It binds NifA. NifA and NifL are encoded by adjacent genes. [Central intermediary metabolism, Nitrogen fixation, Regulatory functions, Protein interactions]


Pssm-ID: 131984 [Multi-domain]  Cd Length: 494  Bit Score: 66.47  E-value: 1.65e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209301716  69 REDVARIVDQtENAFRRRdremlmEFRILRPGdgglvwieARSIIFYDADGRAIRMVGVNADI----TERKRAILQLRAF 144
Cdd:TIGR02938 184 REALAENWPQ-QLAFSNR------EARFDRGG--------GRPARWLSCTGSVIGMESDCADSffcaAEQPYLLLTIADI 248
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209301716 145 TETMEEAVRERTRELVAenearrkaeeLLRQAQKMEVVGQLTGGVAHDFNNLLTIVLGGLDIIGRqlpalgpspeaeRIA 224
Cdd:TIGR02938 249 SNLREEQERARLSALQA----------LMAEEERLEAIRETLSAAIHRLQGPMNLISAAISVLQR------------RGD 306
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209301716 225 KARDMAVEGARRSATLTSR--LLAFSRRQPLDP----RPLDANKLIASTGELL-HRTLGEQIALETVLAAGLWRVHADAN 297
Cdd:TIGR02938 307 DAGNPASAAMLQQALSAGRehMEALRQVIPQSPqeivVPVNLNQILRDVITLStPRLLAAGIVVDWQPAATLPAILGREL 386
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209301716 298 QLENSLINLALNARDAMPTGGRMTIETAnchldgayvagIAEPVEpGQYVMVAVTDSGLGMDKSTQEKAFEPFFTTKA-V 376
Cdd:TIGR02938 387 QLRSLFKALVDNAIEAMNIKGWKRRELS-----------ITTALN-GDLIVVSILDSGPGIPQDLRYKVFEPFFTTKGgS 454
                         330       340       350
                  ....*....|....*....|....*....|....*....
gi 1209301716 377 GQGTGLGLSQVYGFVRQSSGHIRIYSELGEGSTVKIYLP 415
Cdd:TIGR02938 455 RKHIGMGLSVAQEIVADHGGIIDLDDDYSEGCRIIVEFR 493
PAS COG2202
PAS domain [Signal transduction mechanisms];
16-250 1.99e-10

PAS domain [Signal transduction mechanisms];


Pssm-ID: 441804 [Multi-domain]  Cd Length: 258  Bit Score: 61.58  E-value: 1.99e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209301716  16 SDEVLALAQEAGRVGIFEWHVPAGTLLVSQQFLVIYGLDCFDGRHESWLACVFREDVARIVDQTENAFRRRdREMLMEFR 95
Cdd:COG2202     9 SERRLRALVESSPDAIIITDLDGRILYVNPAFERLTGYSAEELLGKTLRDLLPPEDDDEFLELLRAALAGG-GVWRGELR 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209301716  96 ILRPgDGGLVWIEARSIIFYDADGRAIRMVGVNADITERKRAilqlraftetmEEAVRERTRELvaenearrkaeELLRQ 175
Cdd:COG2202    88 NRRK-DGSLFWVELSISPVRDEDGEITGFVGIARDITERKRA-----------EEALRESEERL-----------RLLVE 144
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1209301716 176 AQKMEVVGQLTGGVAHDFNNLLTIVLGG--LDIIGRQLPALGPSPEAERIAKARDMAVEGARRSATLTSRLLAFSRR 250
Cdd:COG2202   145 NAPDGIFVLDLDGRILYVNPAAEELLGYspEELLGKSLLDLLHPEDRERLLELLRRLLEGGRESYELELRLKDGDGR 221
PAC smart00086
Motif C-terminal to PAS motifs (likely to contribute to PAS structural domain); PAC motif ...
92-134 2.15e-08

Motif C-terminal to PAS motifs (likely to contribute to PAS structural domain); PAC motif occurs C-terminal to a subset of all known PAS motifs. It is proposed to contribute to the PAS domain fold.


Pssm-ID: 197509  Cd Length: 43  Bit Score: 50.26  E-value: 2.15e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 1209301716   92 MEFRILRPgDGGLVWIEARSIIFYDADGRAIRMVGVNADITER 134
Cdd:smart00086   2 VEYRLRRK-DGSYIWVLVSASPIRDEDGEVEGILGVVRDITER 43
PAS cd00130
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
41-131 4.74e-05

PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising identification of a PAS domain was that in EAG-like K+-channels. PAS domains have been found to bind ligands, and to act as sensors for light and oxygen in signal transduction.


Pssm-ID: 238075 [Multi-domain]  Cd Length: 103  Bit Score: 42.62  E-value: 4.74e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209301716  41 LLVSQQFLVIYGLDCFDGRHESWLACVFREDVARIVDQTENAFRRRDREMLmEFRILRPgDGGLVWIEARSIIFYDADGR 120
Cdd:cd00130    15 LYANPAAEQLLGYSPEELIGKSLLDLIHPEDREELRERLENLLSGGEPVTL-EVRLRRK-DGSVIWVLVSLTPIRDEGGE 92
                          90
                  ....*....|.
gi 1209301716 121 AIRMVGVNADI 131
Cdd:cd00130    93 VIGLLGVVRDI 103
sensory_box TIGR00229
PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain ...
41-137 2.40e-03

PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain occupies the central portion of the PAS domain but is more widely distributed. It is often tandemly repeated. Known prosthetic groups bound in the S-box domain include heme in the oxygen sensor FixL, FAD in the redox potential sensor NifL, and a 4-hydroxycinnamyl chromophore in photoactive yellow protein. Proteins containing the domain often contain other regulatory domains such as response regulator or sensor histidine kinase domains. Other S-box proteins include phytochromes and the aryl hydrocarbon receptor nuclear translocator. [Regulatory functions, Small molecule interactions]


Pssm-ID: 272971 [Multi-domain]  Cd Length: 124  Bit Score: 38.04  E-value: 2.40e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209301716  41 LLVSQQFLVIYGLDCFDGRHESWLACVFREDVARIVDQTENAFRRRDREMLMEFRILRPgDGGLVWIEAR-SIIFydADG 119
Cdd:TIGR00229  26 LYVNPAFEEIFGYSAEELIGRNVLELIPEEDREEVRERIERRLEGEPEPVSEERRVRRK-DGSEIWVEVSvSPIR--TNG 102
                          90
                  ....*....|....*...
gi 1209301716 120 RAIRMVGVNADITERKRA 137
Cdd:TIGR00229 103 GELGVVGIVRDITERKEA 120
 
Name Accession Description Interval E-value
PRK13557 PRK13557
histidine kinase; Provisional
166-557 1.75e-139

histidine kinase; Provisional


Pssm-ID: 237425 [Multi-domain]  Cd Length: 540  Bit Score: 414.84  E-value: 1.75e-139
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209301716 166 RRKAEELLRQAQKMEVVGQLTGGVAHDFNNLLTIVLGGLDIIgrQLPALGPSPEAERIAKARDMAVEGARRSATLTSRLL 245
Cdd:PRK13557  147 RRDAEDALRQAQKMEALGQLTGGIAHDFNNLLQVMSGYLDVI--QAALSHPDADRGRMARSVENIRAAAERAATLTQQLL 224
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209301716 246 AFSRRQPLDPRPLDANKLIASTGELLHRTLGEQIALETVLAAGLWRVHADANQLENSLINLALNARDAMPTGGRMTIETA 325
Cdd:PRK13557  225 AFARKQRLEGRVLNLNGLVSGMGELAERTLGDAVTIETDLAPDLWNCRIDPTQAEVALLNVLINARDAMPEGGRVTIRTR 304
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209301716 326 NCHLDGAYVAGIAePVEPGQYVMVAVTDSGLGMDKSTQEKAFEPFFTTKAVGQGTGLGLSQVYGFVRQSSGHIRIYSELG 405
Cdd:PRK13557  305 NVEIEDEDLAMYH-GLPPGRYVSIAVTDTGSGMPPEILARVMDPFFTTKEEGKGTGLGLSMVYGFAKQSGGAVRIYSEVG 383
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209301716 406 EGSTVKIYLPrYAGAEEAAPFVPPELTARAGGSELILVVEDDASLRGYTVQILTELGYGVLEAADGRIGLKVLAERGDID 485
Cdd:PRK13557  384 EGTTVRLYFP-ASDQAENPEQEPKARAIDRGGTETILIVDDRPDVAELARMILEDFGYRTLVASNGREALEILDSHPEVD 462
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1209301716 486 LLFTDIVMPGGLNGRELADEAVKLHPALKVLFTTGYTRNAIVHHGRLDPGVHFLGKPFSFDELALKIRSVLD 557
Cdd:PRK13557  463 LLFTDLIMPGGMNGVMLAREARRRQPKIKVLLTTGYAEASIERTDAGGSEFDILNKPYRRAELARRVRMVLD 534
COG4191 COG4191
Signal transduction histidine kinase regulating C4-dicarboxylate transport system [Signal ...
71-416 6.99e-86

Signal transduction histidine kinase regulating C4-dicarboxylate transport system [Signal transduction mechanisms];


Pssm-ID: 443345 [Multi-domain]  Cd Length: 361  Bit Score: 270.52  E-value: 6.99e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209301716  71 DVARIVDQTENAFRRRDREMLMEFRILRPGDGGLVWIEARSIIFYDADGRAIRMVGVNADITERKRAILQLRAFTETMEE 150
Cdd:COG4191    31 LLLALLLLLLALLLALLALLLLLLLLLLLLLLELLLLLLALLGGLLRLLLLLGLLLLLLLEALLLLLLAALDAEENAELE 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209301716 151 AVRERTRELVAENEARRKAEELLRQAQKMEVVGQLTGGVAHDFNNLLTIVLGGLDIIGRQLPAlgpSPEAERIAKARDMA 230
Cdd:COG4191   111 ELERDITELERAEEELRELQEQLVQSEKLAALGELAAGIAHEINNPLAAILGNAELLRRRLED---EPDPEELREALERI 187
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209301716 231 VEGARRSATLTSRLLAFSRRQPLDPRPLDANKLIASTGELLHRTLGEQ-IALETVLAAGLWRVHADANQLENSLINLALN 309
Cdd:COG4191   188 LEGAERAAEIVRSLRAFSRRDEEEREPVDLNELIDEALELLRPRLKARgIEVELDLPPDLPPVLGDPGQLEQVLLNLLIN 267
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209301716 310 ARDAMPTG--GRMTIETAnchldgayvagiaepvEPGQYVMVAVTDSGLGMDKSTQEKAFEPFFTTKAVGQGTGLGLSQV 387
Cdd:COG4191   268 AIDAMEEGegGRITISTR----------------REGDYVVISVRDNGPGIPPEVLERIFEPFFTTKPVGKGTGLGLSIS 331
                         330       340
                  ....*....|....*....|....*....
gi 1209301716 388 YGFVRQSSGHIRIYSELGEGSTVKIYLPR 416
Cdd:COG4191   332 YGIVEKHGGRIEVESEPGGGTTFTITLPL 360
NtrB COG3852
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms];
64-423 2.34e-72

Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms];


Pssm-ID: 443061 [Multi-domain]  Cd Length: 361  Bit Score: 235.51  E-value: 2.34e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209301716  64 LACVFREDvARIVDQTENAFRRRDREMLMEFRILRPgDGGLVWIEARSIIFYDADGRaIRMVGVNADITERKRailqlra 143
Cdd:COG3852    52 LAELFPED-SPLRELLERALAEGQPVTEREVTLRRK-DGEERPVDVSVSPLRDAEGE-GGVLLVLRDITERKR------- 121
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209301716 144 ftetmeeavrertrelvaenearrkAEELLRQAQKMEVVGQLTGGVAHDFNNLLTIVLGGLDIIGRQLPalgPSPEAERI 223
Cdd:COG3852   122 -------------------------LERELRRAEKLAAVGELAAGLAHEIRNPLTGIRGAAQLLERELP---DDELREYT 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209301716 224 akarDMAVEGARRSATLTSRLLAFSRRQPLDPRPLDANKLIASTGELLHRTLGEQIALETVLAAGLWRVHADANQLENSL 303
Cdd:COG3852   174 ----QLIIEEADRLNNLVDRLLSFSRPRPPEREPVNLHEVLERVLELLRAEAPKNIRIVRDYDPSLPEVLGDPDQLIQVL 249
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209301716 304 INLALNARDAMPTGGRMTIETANCHLDgayvagIAEPVEPGQYVMVAVTDSGLGMDKSTQEKAFEPFFTTKavGQGTGLG 383
Cdd:COG3852   250 LNLVRNAAEAMPEGGTITIRTRVERQV------TLGGLRPRLYVRIEVIDNGPGIPEEILDRIFEPFFTTK--EKGTGLG 321
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|
gi 1209301716 384 LSQVYGFVRQSSGHIRIYSELGEGSTVKIYLPRYAGAEEA 423
Cdd:COG3852   322 LAIVQKIVEQHGGTIEVESEPGKGTTFRIYLPLEQAEEEP 361
HATPase_CckA-like cd16919
Histidine kinase-like ATPase domain of two-component sensor hybrid histidine kinases, similar ...
299-415 8.08e-54

Histidine kinase-like ATPase domain of two-component sensor hybrid histidine kinases, similar to Brucella abortus 2308 CckA; This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component hybrid sensor histidine kinase (HKs) similar to Brucella abortus 2308 CckA, which is a component of an essential protein phosphorelay that regulates expression of genes required for growth, division, and intracellular survival; phosphoryl transfer initiates from the sensor kinase CckA and proceeds via the ChpT phosphotransferase to two regulatory substrates: the DNA-binding response regulator CtrA and the phospho-receiver protein CpdR. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA), a REC signal receiver domain, and some contain PAS or PAS and GAF sensor domain(s).


Pssm-ID: 340396 [Multi-domain]  Cd Length: 116  Bit Score: 177.96  E-value: 8.08e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209301716 299 LENSLINLALNARDAMPTGGRMTIETANCHLDGAYVAGIAEpVEPGQYVMVAVTDSGLGMDKSTQEKAFEPFFTTKAVGQ 378
Cdd:cd16919     1 LELAILNLAVNARDAMPEGGRLTIETSNQRVDADYALNYRD-LIPGNYVCLEVSDTGSGMPAEVLRRAFEPFFTTKEVGK 79
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1209301716 379 GTGLGLSQVYGFVRQSSGHIRIYSELGEGSTVKIYLP 415
Cdd:cd16919    80 GTGLGLSMVYGFVKQSGGHLRIYSEPGVGTTVRIYLP 116
PRK13837 PRK13837
two-component system VirA-like sensor kinase;
140-556 6.22e-51

two-component system VirA-like sensor kinase;


Pssm-ID: 237526 [Multi-domain]  Cd Length: 828  Bit Score: 187.58  E-value: 6.22e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209301716 140 QLRAFTETMEEAVRERTRElvaenEARRKAEELLRQAQKMEVVGQLTGGVAHDFNNLLTIVLGGLDIIGRQLPAlgPSPE 219
Cdd:PRK13837  413 LLELALDCLAHAIERRRLE-----TERDALERRLEHARRLEAVGTLASGIAHNFNNILGAILGYAEMALNKLAR--HSRA 485
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209301716 220 AERIAKARDmAVEGARRsatLTSRLLAFSRRQPLDPRPLDANKLIASTGELLHRTLGEQIALETVLAAGLWRVHADANQL 299
Cdd:PRK13837  486 ARYIDEIIS-AGARARL---IIDQILAFGRKGERNTKPFDLSELVTEIAPLLRVSLPPGVELDFDQDQEPAVVEGNPAEL 561
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209301716 300 ENSLINLALNARDAMPTGGRMTIeTANCHLDGAYVAGIAEPVEPGQYVMVAVTDSGLGMDKSTQEKAFEPFFTTKAvgQG 379
Cdd:PRK13837  562 QQVLMNLCSNAAQAMDGAGRVDI-SLSRAKLRAPKVLSHGVLPPGRYVLLRVSDTGAGIDEAVLPHIFEPFFTTRA--GG 638
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209301716 380 TGLGLSQVYGFVRQSSGHIRIYSELGEGSTVKIYLPRYAGAEEAAPFVPPELTARAGGSELILVVEDDASLRGYTVQILT 459
Cdd:PRK13837  639 TGLGLATVHGIVSAHAGYIDVQSTVGRGTRFDVYLPPSSKVPVAPQAFFGPGPLPRGRGETVLLVEPDDATLERYEEKLA 718
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209301716 460 ELGY---GVLEAADGRIGLKVLAERGDIdllftdIVMPGGLNGRELAdeAVKLHPALK--VLFTTGYTRNAIVHHGRLDP 534
Cdd:PRK13837  719 ALGYepvGFSTLAAAIAWISKGPERFDL------VLVDDRLLDEEQA--AAALHAAAPtlPIILGGNSKTMALSPDLLAS 790
                         410       420
                  ....*....|....*....|..
gi 1209301716 535 GVHFLGKPFSFDELALKIRSVL 556
Cdd:PRK13837  791 VAEILAKPISSRTLAYALRTAL 812
NtrY COG5000
Signal transduction histidine kinase NtrY involved in nitrogen fixation and metabolism ...
112-421 1.86e-47

Signal transduction histidine kinase NtrY involved in nitrogen fixation and metabolism regulation [Signal transduction mechanisms];


Pssm-ID: 444024 [Multi-domain]  Cd Length: 422  Bit Score: 170.91  E-value: 1.86e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209301716 112 IIFYDADGR-------AIRMVGVNAD--ITERKRAILQLRAFTETMEEAVRERTRELVAENEARRKAEEL---------- 172
Cdd:COG5000   103 VIVLDADGRitlanpaAERLLGIPLEelIGKPLEELLPELDLAELLREALERGWQEEIELTRDGRRTLLVrasplrddgy 182
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209301716 173 ---------LRQAQKMEVVGQLTGGVAHDFNNLLTIVLGGLDIIGRQLPALGPSpEAERIAKARDMAVEGARRSATLTSR 243
Cdd:COG5000   183 vivfdditeLLRAERLAAWGELARRIAHEIKNPLTPIQLSAERLRRKLADKLEE-DREDLERALDTIIRQVDRLKRIVDE 261
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209301716 244 LLAFSRRQPLDPRPLDANKLIASTGELLHRTLGE-QIALETVLAAGLWRVHADANQLENSLINLALNARDAMPTGGRMTI 322
Cdd:COG5000   262 FLDFARLPEPQLEPVDLNELLREVLALYEPALKEkDIRLELDLDPDLPEVLADRDQLEQVLINLLKNAIEAIEEGGEIEV 341
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209301716 323 ETAnchldgayvagiaepvEPGQYVMVAVTDSGLGMDKSTQEKAFEPFFTTKAvgQGTGLGLSQVYGFVRQSSGHIRIYS 402
Cdd:COG5000   342 STR----------------REDGRVRIEVSDNGPGIPEEVLERIFEPFFTTKP--KGTGLGLAIVKKIVEEHGGTIELES 403
                         330
                  ....*....|....*....
gi 1209301716 403 ELGEGSTVKIYLPRYAGAE 421
Cdd:COG5000   404 RPGGGTTFTIRLPLAEEAE 422
BaeS COG0642
Signal transduction histidine kinase [Signal transduction mechanisms];
82-416 1.32e-45

Signal transduction histidine kinase [Signal transduction mechanisms];


Pssm-ID: 440407 [Multi-domain]  Cd Length: 328  Bit Score: 163.54  E-value: 1.32e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209301716  82 AFRRRDREMLMEFRILRPGDGGLVWIEARSIIFYDADGRAIRMVGVNADITERKRAILQLRAFTETMEEAVRERTRELVA 161
Cdd:COG0642    12 LLLLLLLLLALLLLLLLLLLLALLLLLALLLLLLLLLLLLLLLALALLALLLLLLLLLLLLLLLLLLLLLLLLLLLLLLL 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209301716 162 ENEARRKAEELLRQAQKMEvvGQLTGGVAHDFNNLLTIVLGGLDIIGRQLPalgpspeaERIAKARDMAVEGARRSATLT 241
Cdd:COG0642    92 LLLLLLALLLLLEEANEAK--SRFLANVSHELRTPLTAIRGYLELLLEELD--------EEQREYLETILRSADRLLRLI 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209301716 242 SRLLAFSR----RQPLDPRPLDANKLIASTGELLHRTLGE-QIALETVLAAGLWRVHADANQLENSLINLALNARDAMPT 316
Cdd:COG0642   162 NDLLDLSRleagKLELEPEPVDLAELLEEVVELFRPLAEEkGIELELDLPDDLPTVRGDPDRLRQVLLNLLSNAIKYTPE 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209301716 317 GGRMTIETAnchldgayvagiaepvEPGQYVMVAVTDSGLGMDKSTQEKAFEPFFTTKAV--GQGTGLGLSQVYGFVRQS 394
Cdd:COG0642   242 GGTVTVSVR----------------REGDRVRISVEDTGPGIPPEDLERIFEPFFRTDPSrrGGGTGLGLAIVKRIVELH 305
                         330       340
                  ....*....|....*....|..
gi 1209301716 395 SGHIRIYSELGEGSTVKIYLPR 416
Cdd:COG0642   306 GGTIEVESEPGKGTTFTVTLPL 327
KinC COG5807
Sporulation sensor histidine kinase C [Cell cycle control, cell division, chromosome ...
166-417 1.36e-45

Sporulation sensor histidine kinase C [Cell cycle control, cell division, chromosome partitioning, Signal transduction mechanisms];


Pssm-ID: 444509 [Multi-domain]  Cd Length: 358  Bit Score: 164.19  E-value: 1.36e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209301716 166 RRKAEELLRQAQKMEVVGQLTGGVAHDFNNLLTIVLGGLDIIGRqlpalgpSPEAERIAKARDMAVEGARRSATLTSRLL 245
Cdd:COG5807   131 RKEAEDKLLRSEKLSVAGELAAGIAHEIRNPLTSIKGFLQLLQE-------SREDSEREEYFNIIISEIDRINTIITELL 203
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209301716 246 AFSRRQPLDPRPLDANKLIASTGELL-HRTLGEQIALETVLAAGLWRVHADANQLENSLINLALNARDAMPTGGRMTIET 324
Cdd:COG5807   204 VLSKPKKFNFKKLNLNDVLEDVIALLsTEAILKNISIKYDLADDEPVINGDKNQLKQVFINLIKNAIEAMETGGNITIKT 283
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209301716 325 AnchldgayvagiaepVEpGQYVMVAVTDSGLGMDKSTQEKAFEPFFTTKavGQGTGLGLSQVYGFVRQSSGHIRIYSEL 404
Cdd:COG5807   284 Y---------------VE-GDFVVISVKDEGIGIPEEVLEKIGEPFFTTK--EEGTGLGLSICKKIIEEHNGTIEVESKP 345
                         250
                  ....*....|...
gi 1209301716 405 GEGSTVKIYLPRY 417
Cdd:COG5807   346 GKGTTFTIYLPLY 358
KinA COG5805
Sporulation sensor histidine kinase A (Stage II sporulation protein SpoIIF/SpoIIJ) [Cell cycle ...
101-415 1.74e-42

Sporulation sensor histidine kinase A (Stage II sporulation protein SpoIIF/SpoIIJ) [Cell cycle control, cell division, chromosome partitioning, Signal transduction mechanisms];


Pssm-ID: 444507 [Multi-domain]  Cd Length: 496  Bit Score: 159.13  E-value: 1.74e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209301716 101 DGGLVWIEARSIIFYDADGRAIRMVGVNADITERKRAilqlraftetmeeavrertrelvaenearrkaEELLRQAQKME 180
Cdd:COG5805   238 DGRIRYFEAVIVPLIDTDGSVKGILVILRDITEKKEA--------------------------------EELMARSEKLS 285
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209301716 181 VVGQLTGGVAHDFNNLLTIVLGGLdiigrQLpaLGPSPEAERiaKARDMAVEGARRSATLTSRLLAFSRRQPLDPRPLDA 260
Cdd:COG5805   286 IAGQLAAGIAHEIRNPLTSIKGFL-----QL--LQPGIEDKE--EYFDIMLSELDRIESIISEFLALAKPQAVNKEKENI 356
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209301716 261 NKLIASTGELL-HRTLGEQIALETVLAAGLWRVHADANQLENSLINLALNARDAMPTGGRMTIETanchldgayvagiae 339
Cdd:COG5805   357 NELIQDVVTLLeTEAILHNIQIRLELLDEDPFIYCDENQIKQVFINLIKNAIEAMPNGGTITIHT--------------- 421
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1209301716 340 pVEPGQYVMVAVTDSGLGMDKSTQEKAFEPFFTTKAvgQGTGLGLSQVYGFVRQSSGHIRIYSELGEGSTVKIYLP 415
Cdd:COG5805   422 -EEEDNSVIIRVIDEGIGIPEERLKKLGEPFFTTKE--KGTGLGLMVSYKIIENHNGTIDIDSKVGKGTTFTITLP 494
PRK11360 PRK11360
two-component system sensor histidine kinase AtoS;
165-422 1.88e-39

two-component system sensor histidine kinase AtoS;


Pssm-ID: 236901 [Multi-domain]  Cd Length: 607  Bit Score: 152.04  E-value: 1.88e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209301716 165 ARRKAEELLRQAQKMEVVGQLTGGVAHDFNNLLTIVLGGLDIIgRQLPALGPSPEAERIAkardmaVEGARRSATLTSRL 244
Cdd:PRK11360  373 ERKRLQRRVARQERLAALGELVAGVAHEIRNPLTAIRGYVQIW-RQQTSDPPSQEYLSVV------LREVDRLNKVIDQL 445
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209301716 245 LAFSRRQPLDPRPLDANKLIASTGELLHRTLG-EQIALETVLAAGLWRVHADANQLENSLINLALNARDAMPTGGRMTIE 323
Cdd:PRK11360  446 LEFSRPRESQWQPVSLNALVEEVLQLFQTAGVqARVDFETELDNELPPIWADPELLKQVLLNILINAVQAISARGKIRIR 525
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209301716 324 TANChldgayvagiaepvEPGQyVMVAVTDSGLGMDKSTQEKAFEPFFTTKAvgQGTGLGLSQVYGFVRQSSGHIRIYSE 403
Cdd:PRK11360  526 TWQY--------------SDGQ-VAVSIEDNGCGIDPELLKKIFDPFFTTKA--KGTGLGLALSQRIINAHGGDIEVESE 588
                         250
                  ....*....|....*....
gi 1209301716 404 LGEGSTVKIYLPRYAGAEE 422
Cdd:PRK11360  589 PGVGTTFTLYLPINPQGNQ 607
KinE COG5809
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome ...
67-415 1.16e-38

Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome partitioning, Signal transduction mechanisms];


Pssm-ID: 444511 [Multi-domain]  Cd Length: 489  Bit Score: 148.20  E-value: 1.16e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209301716  67 VFREDVARIVDQTENAFRRRDREMLMEFRILRPgDGGLVWIEARSIIFyDADGRAIRMVGVNADITERKrailqlrafte 146
Cdd:COG5809   189 LIHSDDQENVAAFISQLLKDGGIAQGEVRFWTK-DGRWRLLEASGAPI-KKNGEVDGIVIIFRDITERK----------- 255
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209301716 147 tmeeavrertrelvaenearrKAEELLRQAQKMEVVGQLTGGVAHDFNNLLTIVLGGLDIigrqlpaLGPSPEAERIAKA 226
Cdd:COG5809   256 ---------------------KLEELLRKSEKLSVVGELAAGIAHEIRNPLTSLKGFIQL-------LKDTIDEEQKTYL 307
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209301716 227 RDMAVEGARRSAtLTSRLLAFSRRQPLDPRPLDANKLIASTGELLH-RTLGEQIALETVLAAGLWRVHADANQLENSLIN 305
Cdd:COG5809   308 DIMLSELDRIES-IISEFLVLAKPQAIKYEPKDLNTLIEEVIPLLQpQALLKNVQIELELEDDIPDILGDENQLKQVFIN 386
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209301716 306 LALNARDAMPTGGRMTIETAnchldgayvagiaepVEPGQYVMVAVTDSGLGMDKSTQEKAFEPFFTTKAvgQGTGLGLS 385
Cdd:COG5809   387 LLKNAIEAMPEGGNITIETK---------------AEDDDKVVISVTDEGCGIPEERLKKLGEPFYTTKE--KGTGLGLM 449
                         330       340       350
                  ....*....|....*....|....*....|
gi 1209301716 386 QVYGFVRQSSGHIRIYSELGEGSTVKIYLP 415
Cdd:COG5809   450 VSYKIIEEHGGKITVESEVGKGTTFSITLP 479
REC_hyHK_blue-like cd18161
phosphoacceptor receiver (REC) domain of hybrid sensor histidine kinase/response regulators ...
441-543 6.43e-36

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: 129.77  E-value: 6.43e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209301716 441 ILVVEDDASLRGYTVQILTELGYGVLEAADGRIGLKVLAERGDIDLLFTDIVMPGGLNGRELADEAVKLHPALKVLFTTG 520
Cdd:cd18161     1 VLVVEDDPDVRRLTAEVLEDLGYTVLEAASGDEALDLLESGPDIDLLVTDVIMPGGMNGSQLAEEARRRRPDLKVLLTSG 80
                          90       100
                  ....*....|....*....|...
gi 1209301716 521 YTRNAIVhHGRLDPGVHFLGKPF 543
Cdd:cd18161    81 YAENAIE-GGDLAPGVDVLSKPF 102
KdpD COG2205
K+-sensing histidine kinase KdpD [Signal transduction mechanisms];
158-416 1.54e-35

K+-sensing histidine kinase KdpD [Signal transduction mechanisms];


Pssm-ID: 441807 [Multi-domain]  Cd Length: 239  Bit Score: 133.11  E-value: 1.54e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209301716 158 ELVAENEARRKAEELLRQaqkmevvgqLTGGVAHDFNNLLTIVLGGLDIIGRqlpalGPSPEAERIAKARDMAVEGARRS 237
Cdd:COG2205     1 ELEEALEELEELERLKSE---------FLANVSHELRTPLTSILGAAELLLD-----EEDLSPEERRELLEIIRESAERL 66
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209301716 238 ATLTSRLLAFSR----RQPLDPRPLDANKLIASTGELLHRTLGE-QIALETVLAAGLWRVHADANQLENSLINLALNARD 312
Cdd:COG2205    67 LRLIEDLLDLSRlesgKLSLELEPVDLAELLEEAVEELRPLAEEkGIRLELDLPPELPLVYADPELLEQVLANLLDNAIK 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209301716 313 AMPTGGRMTIETAnchldgayvagiaepvEPGQYVMVAVTDSGLGMDKSTQEKAFEPFFTTKAVG--QGTGLGLSQVYGF 390
Cdd:COG2205   147 YSPPGGTITISAR----------------REGDGVRISVSDNGPGIPEEELERIFERFYRGDNSRgeGGTGLGLAIVKRI 210
                         250       260
                  ....*....|....*....|....*.
gi 1209301716 391 VRQSSGHIRIYSELGEGSTVKIYLPR 416
Cdd:COG2205   211 VEAHGGTIWVESEPGGGTTFTVTLPL 236
WalK COG5002
Sensor histidine kinase WalK [Signal transduction mechanisms];
69-416 1.29e-31

Sensor histidine kinase WalK [Signal transduction mechanisms];


Pssm-ID: 444026 [Multi-domain]  Cd Length: 390  Bit Score: 126.21  E-value: 1.29e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209301716  69 REDVARIVDQTENAFRRRDREMLMEFRILRPGDGGLVWIEARSIIFYDADGRAIRMVGVNADITERKRAILQLRAFTETM 148
Cdd:COG5002    54 LLLLLLLLLLLLLALLLLLLLLLLLLALALLLLALLLLLLLLLLLLALLILLLLLALLILLAALLLLLSELLLLLLLLGR 133
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209301716 149 EEAVRERTRELVAENEARRKAEELLRQAQKMEVvgQLTGGVAHDFNNLLTIVLGGLDIIgrqlpALGPSPEAERIAKARD 228
Cdd:COG5002   134 LSLRLSALLLGLLLLAAVERDITELERLEQMRR--EFVANVSHELRTPLTSIRGYLELL-----LDGAADDPEERREYLE 206
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209301716 229 MAVEGARRSATLTSRLLAFSR----RQPLDPRPLDANKLIASTGELLHRTLGE-QIALETVLAAGLWRVHADANQLENSL 303
Cdd:COG5002   207 IILEEAERLSRLVNDLLDLSRlesgELKLEKEPVDLAELLEEVVEELRPLAEEkGIELELDLPEDPLLVLGDPDRLEQVL 286
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209301716 304 INLALNARDAMPTGGRMTIETAnchldgayvagiaepvEPGQYVMVAVTDSGLGMDKSTQEKAFEPFFTTKAV----GQG 379
Cdd:COG5002   287 TNLLDNAIKYTPEGGTITVSLR----------------EEDDQVRISVRDTGIGIPEEDLPRIFERFYRVDKSrsreTGG 350
                         330       340       350
                  ....*....|....*....|....*....|....*..
gi 1209301716 380 TGLGLSQVYGFVRQSSGHIRIYSELGEGSTVKIYLPR 416
Cdd:COG5002   351 TGLGLAIVKHIVEAHGGRIWVESEPGKGTTFTITLPL 387
PRK10364 PRK10364
two-component system sensor histidine kinase ZraS;
164-415 6.40e-30

two-component system sensor histidine kinase ZraS;


Pssm-ID: 236674 [Multi-domain]  Cd Length: 457  Bit Score: 122.59  E-value: 6.40e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209301716 164 EARRKAEELLRQAQKMEVVGQLTGGVAHDFNNLLTIVLGGLDIIGRQLPALGPSPEAeriakARDMAVEgARRSATLTSR 243
Cdd:PRK10364  219 RSRQLLQDEMKRKEKLVALGHLAAGVAHEIRNPLSSIKGLAKYFAERAPAGGEAHQL-----AQVMAKE-ADRLNRVVSE 292
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209301716 244 LLAFSRRQPLDPRPLDANKLIASTGELLHRTL-GEQIALETVLAAGLWRVHADANQLENSLINLALNARDAMPTGGRMTI 322
Cdd:PRK10364  293 LLELVKPTHLALQAVDLNDLINHSLQLVSQDAnSREIQLRFTANDTLPEIQADPDRLTQVLLNLYLNAIQAIGQHGVISV 372
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209301716 323 ETAnchldgayvagiaepvEPGQYVMVAVTDSGLGMDKSTQEKAFEPFFTTKAvgQGTGLGLSQVYGFVRQSSGHIRIYS 402
Cdd:PRK10364  373 TAS----------------ESGAGVKISVTDSGKGIAADQLEAIFTPYFTTKA--EGTGLGLAVVHNIVEQHGGTIQVAS 434
                         250
                  ....*....|...
gi 1209301716 403 ELGEGSTVKIYLP 415
Cdd:PRK10364  435 QEGKGATFTLWLP 447
HATPase_AtoS-like cd16943
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
298-416 3.01e-26

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Escherichia coli K-12 AtoS; This family includes the histidine kinase-like ATPase (HATPase) domains of various histidine kinases (HKs) of two-component signal transduction systems (TCSs) such as Escherichia coli AtoS, an HK of the AtoS-AtoC TCS. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA); some have accessory domains such as HAMP or PAS sensor domains or CBS-pair domains.


Pssm-ID: 340419 [Multi-domain]  Cd Length: 105  Bit Score: 102.89  E-value: 3.01e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209301716 298 QLENSLINLALNARDAMPTGGRMTIETANCHldgayvagiaepvepgQYVMVAVTDSGLGMDKSTQEKAFEPFFTTKAVG 377
Cdd:cd16943     3 QLNQVLLNLLVNAAQAMEGRGRITIRTWAHV----------------DQVLIEVEDTGSGIDPEILGRIFDPFFTTKPVG 66
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1209301716 378 QGTGLGLSQVYGFVRQSSGHIRIYSELGEGSTVKIYLPR 416
Cdd:cd16943    67 EGTGLGLSLSYRIIQKHGGTIRVASVPGGGTRFTIILPI 105
CheY COG0784
CheY-like REC (receiver) domain, includes chemotaxis protein CheY and sporulation regulator ...
434-559 3.96e-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: 100.70  E-value: 3.96e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209301716 434 RAGGSELILVVEDDASLRGYTVQILTELGYGVLEAADGRIGLKvLAERGDIDLLFTDIVMPgGLNGRELADE--AVKLHP 511
Cdd:COG0784     1 PPLGGKRILVVDDNPDNRELLRRLLERLGYEVTTAEDGAEALE-LLRAGPPDLILLDINMP-GMDGLELLRRirALPRLP 78
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1209301716 512 ALKVLFTTGYTRNAIVHHGRLDPGVHFLGKPFSFDELALKIRSVLDED 559
Cdd:COG0784    79 DIPIIALTAYADEEDRERALEAGADDYLTKPVDPEELLEALRRLLARA 126
COG4192 COG4192
Signal transduction histidine kinase regulating phosphoglycerate transport system [Signal ...
141-410 4.41e-24

Signal transduction histidine kinase regulating phosphoglycerate transport system [Signal transduction mechanisms];


Pssm-ID: 443346 [Multi-domain]  Cd Length: 640  Bit Score: 106.69  E-value: 4.41e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209301716 141 LRAFTETMEEavreRTRELVAENEARRKAEELLRQAQ-------KMEVVGQLTGGVAHDFNNLLTIVLGGLDIIGRQLPA 213
Cdd:COG4192   389 LRVFRDQAIE----KTQELETEIEERKRIEKNLRQTQdeliqaaKMAVVGQTMTSLAHELNQPLNAMSMYLFSAKKALEQ 464
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209301716 214 LGPSPEAERIAKARDMavegARRSATLTSRLLAFSRRQPLDPRPLDANKLIASTGELL---HRTLGEQIALETVLaaglw 290
Cdd:COG4192   465 ENYAQLPTSLDKIEGL----IERMDKIIKSLRQFSRKSDTPLQPVDLRQVIEQAWELVesrAKPQQITLHIPDDL----- 535
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209301716 291 RVHADANQLENSLINLALNARDAMPTGGRMTIETanchldgayvagiaepVEPGQYVMVAVTDSGLGMDKStqEKAFEPF 370
Cdd:COG4192   536 MVQGDQVLLEQVLVNLLVNALDAVATQPQISVDL----------------LSNAENLRVAISDNGNGWPLV--DKLFTPF 597
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1209301716 371 FTTKAVGQGTGLGLSQvyGFVRQSSGHIRIYSELGEGSTV 410
Cdd:COG4192   598 TTTKEVGLGLGLSICR--SIMQQFGGDLYLASTLERGAMV 635
COG4251 COG4251
Bacteriophytochrome (light-regulated signal transduction histidine kinase) [Signal ...
67-416 2.24e-20

Bacteriophytochrome (light-regulated signal transduction histidine kinase) [Signal transduction mechanisms];


Pssm-ID: 443393 [Multi-domain]  Cd Length: 503  Bit Score: 94.47  E-value: 2.24e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209301716  67 VFREDVARIVDQTENAFRRRDREMLMEFRILRPGDGGLVWIEARSIIFYDADGRAIRMVGVNADITERKRAILQLraftE 146
Cdd:COG4251   187 VLLLLLLLLLLLLLLLLRLLLELLLLLEAELLLSLGGGLGLLLLLLLLLVLLLLLILLLLLLILVLELLELRLEL----E 262
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209301716 147 TMEEAVRERTRELvaeneaRRKAEELlrqaqkmevvGQLTGGVAHDFNNLLTIVLGGLDIIGRQLPAlGPSPEAERIAka 226
Cdd:COG4251   263 ELEEELEERTAEL------ERSNEEL----------EQFAYVASHDLREPLRKISGFSQLLEEDYGD-KLDEEGREYL-- 323
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209301716 227 rDMAVEGARRSATLTSRLLAFSR--RQPLDPRPLDANKLIASTGELLHRTLGEQIAleTVLAAGLWRVHADANQLENSLI 304
Cdd:COG4251   324 -ERIRDAAERMQALIDDLLAYSRvgRQELEFEPVDLNELLEEVLEDLEPRIEERGA--EIEVGPLPTVRGDPTLLRQVFQ 400
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209301716 305 NLALNA----RDAMPtgGRMTIETanchldgayvagiaepVEPGQYVMVAVTDSGLGMDKSTQEKAFEPFFT--TKAVGQ 378
Cdd:COG4251   401 NLISNAikysRPGEP--PRIEIGA----------------EREGGEWVFSVRDNGIGIDPEYAEKIFEIFQRlhSRDEYE 462
                         330       340       350
                  ....*....|....*....|....*....|....*...
gi 1209301716 379 GTGLGLSQVYGFVRQSSGHIRIYSELGEGSTVKIYLPR 416
Cdd:COG4251   463 GTGIGLAIVKKIVERHGGRIWVESEPGEGATFYFTLPK 500
AtoC COG2204
DNA-binding transcriptional response regulator, NtrC family, contains REC, AAA-type ATPase, ...
441-557 3.86e-20

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: 92.72  E-value: 3.86e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209301716 441 ILVVEDDASLRGYTVQILTELGYGVLEAADGRIGLKVLAERgDIDLLFTDIVMPGGlNGRELADEAVKLHPALKVLFTTG 520
Cdd:COG2204     5 ILVVDDDPDIRRLLKELLERAGYEVETAASGEEALALLREE-PPDLVLLDLRMPGM-DGLELLRELRALDPDLPVILLTG 82
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1209301716 521 YTRNAIVHHGRLDPGVHFLGKPFSFDELALKIRSVLD 557
Cdd:COG2204    83 YGDVETAVEAIKAGAFDYLTKPFDLEELLAAVERALE 119
HATPase_c smart00387
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.
294-415 1.72e-19

Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.


Pssm-ID: 214643 [Multi-domain]  Cd Length: 111  Bit Score: 83.85  E-value: 1.72e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209301716  294 ADANQLENSLINLALNARDAMPTGGRMTIETANChldgayvagiaepvepGQYVMVAVTDSGLGMDKSTQEKAFEPFFTT 373
Cdd:smart00387   1 GDPDRLRQVLSNLLDNAIKYTPEGGRITVTLERD----------------GDHVEITVEDNGPGIPPEDLEKIFEPFFRT 64
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 1209301716  374 KA---VGQGTGLGLSQVYGFVRQSSGHIRIYSELGEGSTVKIYLP 415
Cdd:smart00387  65 DKrsrKIGGTGLGLSIVKKLVELHGGEISVESEPGGGTTFTITLP 109
OmpR COG0745
DNA-binding response regulator, OmpR family, contains REC and winged-helix (wHTH) domain ...
441-556 6.05e-19

DNA-binding response regulator, OmpR family, contains REC and winged-helix (wHTH) domain [Signal transduction mechanisms, Transcription];


Pssm-ID: 440508 [Multi-domain]  Cd Length: 204  Bit Score: 85.39  E-value: 6.05e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209301716 441 ILVVEDDASLRGYTVQILTELGYGVLEAADGRIGLKvLAERGDIDLLFTDIVMPgGLNGRELADEAVKLHPALKVLFTTG 520
Cdd:COG0745     4 ILVVEDDPDIRELLADALEREGYEVDTAADGEEALE-LLEEERPDLILLDLMLP-GMDGLEVCRRLRARPSDIPIIMLTA 81
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1209301716 521 YTRNAIVHHGrLDPGV-HFLGKPFSFDELALKIRSVL 556
Cdd:COG0745    82 RDDEEDRVRG-LEAGAdDYLTKPFDPEELLARIRALL 117
REC_CpdR_CckA-like cd18160
phosphoacceptor receiver (REC) domain of Brucella abortus CpdR and CckA, and similar domains; ...
441-543 1.06e-18

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: 81.39  E-value: 1.06e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209301716 441 ILVVEDDASLRGYTVQILTELGYGVLEAADGRIGLKVLAERGDIDLLFTDIVMPgGLNGRELADEAVKLHPALKVLFTTG 520
Cdd:cd18160     2 ILLADDEPSVRKFIVTTLKKAGYAVTEAESGAEALEKLQQGKDIDIVVTDIVMP-EMDGIELAREARKIDPDVKILFISG 80
                          90       100
                  ....*....|....*....|...
gi 1209301716 521 YTRNAIVHHGRLDPGVHFLGKPF 543
Cdd:cd18160    81 GAAAAPELLSDAVGDNATLKKPF 103
RpfG COG3437
Response regulator c-di-GMP phosphodiesterase, RpfG family, contains REC and HD-GYP domains ...
434-557 1.98e-18

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: 84.45  E-value: 1.98e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209301716 434 RAGGSELILVVEDDASLRGYTVQILTELGYGVLEAADGRIGLKvLAERGDIDLLFTDIVMPgGLNGRELAdEAVKLHPAL 513
Cdd:COG3437     2 RTGQAPTVLIVDDDPENLELLRQLLRTLGYDVVTAESGEEALE-LLLEAPPDLILLDVRMP-GMDGFELL-RLLRADPST 78
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1209301716 514 K---VLFTTGYTRNAIVHHGRLDPGVHFLGKPFSFDELALKIRSVLD 557
Cdd:COG3437    79 RdipVIFLTALADPEDRERALEAGADDYLTKPFDPEELLARVRNALE 125
Response_reg pfam00072
Response regulator receiver domain; This domain receives the signal from the sensor partner in ...
441-553 2.75e-18

Response regulator receiver domain; This domain receives the signal from the sensor partner in bacterial two-component systems. It is usually found N-terminal to a DNA binding effector domain.


Pssm-ID: 395025 [Multi-domain]  Cd Length: 111  Bit Score: 80.66  E-value: 2.75e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209301716 441 ILVVEDDASLRGYTVQILTELGYGVLEAADGRIGLKVLAERgDIDLLFTDIVMPgGLNGRELADEAVKLHPALKVLFTTG 520
Cdd:pfam00072   1 VLIVDDDPLIRELLRQLLEKEGYVVAEADDGKEALELLKEE-RPDLILLDINMP-GMDGLELLKRIRRRDPTTPVIILTA 78
                          90       100       110
                  ....*....|....*....|....*....|....
gi 1209301716 521 YTRNAIVHHGrLDPGVH-FLGKPFSFDELALKIR 553
Cdd:pfam00072  79 HGDEDDAVEA-LEAGADdFLSKPFDPDELLAAIR 111
HATPase_c pfam02518
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the ...
294-415 2.14e-17

Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the structurally related ATPase domains of histidine kinase, DNA gyrase B and HSP90.


Pssm-ID: 460579 [Multi-domain]  Cd Length: 109  Bit Score: 77.79  E-value: 2.14e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209301716 294 ADANQLENSLINLALNARDAMPTGGRMTIEtanchldgayvagiaepVEPGQYVMVAVTDSGLGMDKSTQEKAFEPFFTT 373
Cdd:pfam02518   1 GDELRLRQVLSNLLDNALKHAAKAGEITVT-----------------LSEGGELTLTVEDNGIGIPPEDLPRIFEPFSTA 63
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1209301716 374 KAVGQ-GTGLGLSQVYGFVRQSSGHIRIYSELGEGSTVKIYLP 415
Cdd:pfam02518  64 DKRGGgGTGLGLSIVRKLVELLGGTITVESEPGGGTTVTLTLP 106
YesN COG4753
Two-component response regulator, YesN/AraC family, consists of REC and AraC-type DNA-binding ...
441-542 1.27e-16

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: 75.58  E-value: 1.27e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209301716 441 ILVVEDDASLRGYTVQILTEL-GYG-VLEAADGRIGLKvLAERGDIDLLFTDIVMPGgLNGRELADEAVKLHPALKVLFT 518
Cdd:COG4753     2 VLIVDDEPLIREGLKRILEWEaGFEvVGEAENGEEALE-LLEEHKPDLVITDINMPG-MDGLELLEAIRELDPDTKIIIL 79
                          90       100
                  ....*....|....*....|....
gi 1209301716 519 TGYTRNAIVHHGRLDPGVHFLGKP 542
Cdd:COG4753    80 SGYSDFEYAQEAIKLGADDYLLKP 103
PRK15347 PRK15347
two component system sensor kinase;
141-501 1.81e-16

two component system sensor kinase;


Pssm-ID: 237951 [Multi-domain]  Cd Length: 921  Bit Score: 83.15  E-value: 1.81e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209301716 141 LRAFTETMEEAVRERTRELvaeNEARRKAEelLRQAQKMEvvgQLTgGVAHDFNNLLTIVLGGLDIIGR-QLpalgpSPE 219
Cdd:PRK15347  366 LNEQYDTLENKVAERTQAL---AEAKQRAE--QANKRKSE---HLT-TISHEIRTPLNGVLGALELLQNtPL-----TAE 431
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209301716 220 AERIAkarDMAVEGARRSATLTSRLLAFSR---------RQPLDPRPL--DANKLIAStgellhRTLGEQIALETVLAAG 288
Cdd:PRK15347  432 QMDLA---DTARQCTLSLLAIINNLLDFSRiesgqmtlsLEETALLPLldQAMLTIQG------PAQSKSLTLRTFVGAH 502
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209301716 289 L-WRVHADANQLENSLINLALNARDAMPTGG-RMTIETANCHLdgayvagiaepvepgqyvMVAVTDSGLGMDKSTQEKA 366
Cdd:PRK15347  503 VpLYLHLDSLRLRQILVNLLGNAVKFTETGGiRLRVKRHEQQL------------------CFTVEDTGCGIDIQQQQQI 564
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209301716 367 FEPFFTTKAVGQGTGLGLSQVYGFVRQSSGHIRIYSELGEGSTVKIYLPRYAGAEE-------AAP-------------- 425
Cdd:PRK15347  565 FTPFYQADTHSQGTGLGLTIASSLAKMMGGELTLFSTPGVGSCFSLVLPLNEYAPPeplkgelSAPlalhrqlsawgitc 644
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209301716 426 --------FVPPELTARAG-----------GSEL--------------ILVVEDDASLRGYTVQILTELGYGVLEAADGR 472
Cdd:PRK15347  645 qpghqnpaLLDPELAYLPGrlydllqqiiqGAPNepvinlplqpwqlqILLVDDVETNRDIIGMMLVELGQQVTTAASGT 724
                         410       420
                  ....*....|....*....|....*....
gi 1209301716 473 IGLkVLAERGDIDLLFTDIVMPgGLNGRE 501
Cdd:PRK15347  725 EAL-ELGRQHRFDLVLMDIRMP-GLDGLE 751
REC cd00156
phosphoacceptor receiver (REC) domain of response regulators (RRs) and pseudo response ...
442-542 2.65e-16

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: 74.57  E-value: 2.65e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209301716 442 LVVEDDASLRGYTVQILTELGYGVLEAADGRIGLKvLAERGDIDLLFTDIVMPgGLNGRELADEAVKLHPALKVLFTTGY 521
Cdd:cd00156     1 LIVDDDPAIRELLKSLLEREGYEVDTAADGEEALE-LLREERPDLVLLDLMMP-GMDGLELLRKLRELPPDIPVIVLTAK 78
                          90       100
                  ....*....|....*....|.
gi 1209301716 522 TRNAIVHHGRLDPGVHFLGKP 542
Cdd:cd00156    79 ADEEDAVRALELGADDYLVKP 99
PleD COG3706
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate ...
441-552 1.02e-15

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: 75.33  E-value: 1.02e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209301716 441 ILVVEDDASLRGYTVQILTELGYGVLEAADGRIGLKVLAERgDIDLLFTDIVMPgGLNGRELAdEAVKLHPALK---VLF 517
Cdd:COG3706     4 ILVVDDDPTNRKLLRRLLEAAGYEVVEAADGEEALELLQEH-RPDLILLDLEMP-DMDGLELC-RRLRADPRTAdipIIF 80
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1209301716 518 TTGYTRNAIVHHGrLDPG-VHFLGKPFSFDELALKI 552
Cdd:COG3706    81 LTALDDEEDRARA-LEAGaDDYLTKPFDPEELLARV 115
CitB COG4565
DNA-binding response regulator DpiB of citrate/malate metabolism [Transcription, Signal ...
441-557 5.83e-15

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


Pssm-ID: 443622 [Multi-domain]  Cd Length: 138  Bit Score: 71.92  E-value: 5.83e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209301716 441 ILVVEDDASLRGYTVQILTEL-GYGVL-EAADGRIGLKVLAERgDIDLLFTDIVMPGGlNGRELADEAVKLHPALKVLFT 518
Cdd:COG4565     6 VLIVEDDPMVAELLRRYLERLpGFEVVgVASSGEEALALLAEH-RPDLILLDIYLPDG-DGLELLRELRARGPDVDVIVI 83
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1209301716 519 TGYTRNAIVHHGRLDPGVHFLGKPFSFDELALKIRSVLD 557
Cdd:COG4565    84 TAARDPETVREALRAGVVDYLIKPFTFERLREALERYLE 122
REC_TrrA-like cd17554
phosphoacceptor receiver (REC) domain of Thermotoga maritima response regulator TrrA and ...
441-521 9.16e-15

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: 70.71  E-value: 9.16e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209301716 441 ILVVEDDASLRGYTVQILTELGYGVLEAADGRIGLKVLaERGDIDLLFTDIVMPgGLNGRELADEAVKLHPALKVLFTTG 520
Cdd:cd17554     3 ILVVDDEENIRELYKEELEDEGYEVVTAGNGEEALEKL-ESEDPDLVILDIKMP-GMDGLETLRKIREKKPDLPVIICTA 80

                  .
gi 1209301716 521 Y 521
Cdd:cd17554    81 Y 81
REC_YesN-like cd17536
phosphoacceptor receiver (REC) domain of YesN and related helix-turn-helix containing response ...
441-558 1.42e-14

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: 70.06  E-value: 1.42e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209301716 441 ILVVEDDASLRGYTVQILTELGYG---VLEAADGRIGLKvLAERGDIDLLFTDIVMPgGLNGRELADEAVKLHPALKVLF 517
Cdd:cd17536     1 VLIVDDEPLIREGLKKLIDWEELGfevVGEAENGEEALE-LIEEHKPDIVITDIRMP-GMDGLELIEKIRELYPDIKIII 78
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1209301716 518 TTGYT-----RNAIvhhgRLdpGV-HFLGKPFSFDELALKIRSVLDE 558
Cdd:cd17536    79 LSGYDdfeyaQKAI----RL--GVvDYLLKPVDEEELEEALEKAKEE 119
PRK09776 PRK09776
putative diguanylate cyclase; Provisional
18-136 1.90e-14

putative diguanylate cyclase; Provisional


Pssm-ID: 182070 [Multi-domain]  Cd Length: 1092  Bit Score: 76.63  E-value: 1.90e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209301716   18 EVLALAQEAGRVGIFEWHVPAGTLLVSQQFLVIYGLDcFDGR--HESWLACVFREDVARIVDQTENAFRRRdREMLMEFR 95
Cdd:PRK09776   410 ERITLANEAGGIGIWEWDLKPNIISWDKRMFELYEIP-PHIKptWQVWYACLHPEDRQRVEKEIRDALQGR-SPFKLEFR 487
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 1209301716   96 ILRPGdgGLVWIEARSIIFYDADGRAIRMVGVNADITERKR 136
Cdd:PRK09776   488 IVVKD--GVRHIRALANRVLNKDGEVERLLGINMDMTEVRQ 526
PAS_3 pfam08447
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
41-128 3.85e-14

PAS fold; The PAS fold corresponds to the structural domain that has previously been defined as PAS and PAC motifs. The PAS fold appears in archaea, eubacteria and eukarya.


Pssm-ID: 430001 [Multi-domain]  Cd Length: 89  Bit Score: 68.13  E-value: 3.85e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209301716  41 LLVSQQFLVIYGLDC--FDGRHESWLACVFREDVARIVDQTENAFRRRDREMLmEFRILRPgDGGLVWIEARSIIFYDAD 118
Cdd:pfam08447   2 IYWSPRFEEILGYTPeeLLGKGESWLDLVHPDDRERVREALWEALKGGEPYSG-EYRIRRK-DGEYRWVEARARPIRDEN 79
                          90
                  ....*....|
gi 1209301716 119 GRAIRMVGVN 128
Cdd:pfam08447  80 GKPVRVIGVA 89
CitA COG3290
Sensor histidine kinase DipB regulating citrate/malate metabolism [Signal transduction ...
67-416 2.50e-13

Sensor histidine kinase DipB regulating citrate/malate metabolism [Signal transduction mechanisms];


Pssm-ID: 442519 [Multi-domain]  Cd Length: 389  Bit Score: 71.80  E-value: 2.50e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209301716  67 VFREDVARIVDQTENAFRRRDREMLME------FRILRPGDGGLVWIEARSIIFYDADGRAIRMVGVNADITERKRAILQ 140
Cdd:COG3290    65 LLLLAALLLKLLEEIARLVEEREAVLEsiregvIAVDRDGRITLINDAARRLLGLDAIGRPIDEVLAEVLETGERDEEIL 144
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209301716 141 LRAFTETMEEAVRERTRELVAENEARRKAEELLRQAQKMEVVGQLTG---GVAHDFNNLLTIVLGGLdiigrqlpalgps 217
Cdd:COG3290   145 LNGRVLVVNRVPIRDDGRVVGAVATFRDRTELERLEEELEGVKELAEalrAQRHDFRNHLHTISGLL------------- 211
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209301716 218 pEAERIAKARDMAVEGARRSATLTSRLLAFSRRQPLDPRPLDAN--------KLIASTGELLHRTLGEQIALETVLAagl 289
Cdd:COG3290   212 -QLGEYDEALEYIDEISEELQELIDSLLSRIGNPVLAALLLGKAararergiDLTIDIDSDLPDLPLSDTDLVTILG--- 287
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209301716 290 wrvhadaNQLENslinlALNARDAMPTGGRmTIE-TANCHldgayvagiaepvepGQYVMVAVTDSGLGMDKSTQEKAFE 368
Cdd:COG3290   288 -------NLLDN-----AIEAVEKLPEEER-RVElSIRDD---------------GDELVIEVEDSGPGIPEELLEKIFE 339
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*...
gi 1209301716 369 PFFTTKAvGQGTGLGLSQVYGFVRQSSGHIRIYSELGEGSTVKIYLPR 416
Cdd:COG3290   340 RGFSTKL-GEGRGLGLALVKQIVEKYGGTIEVESEEGEGTVFTVRLPK 386
HATPase_HupT_MifS-like cd16976
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
299-408 5.48e-12

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Rhodobacter capsulatus HupT and Pseudomonas aeruginosa MifS; This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component sensor histidine kinase (HKs) such as Rhodobacter capsulatus HupT of the HupT-HupR two-component regulatory system (TCS), which regulates the synthesis of HupSL, a membrane bound [NiFe]hydrogenase. It also contains the HATPase domain of Pseudomonas aeruginosa MifS, the HK of the MifS-MifR TCS, which may be involved in sensing alpha-ketoglutarate and regulating its transport and subsequent metabolism. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA); some also have a C-terminal PAS sensor domain.


Pssm-ID: 340435 [Multi-domain]  Cd Length: 102  Bit Score: 62.47  E-value: 5.48e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209301716 299 LENSLINLALNARDAMPTGGRMTIETANCHLDGAYVagiaepvepgqyvmVAVTDSGLGMDKSTQEKAFEPFFTTKAVGQ 378
Cdd:cd16976     1 IQQVLMNLLQNALDAMGKVENPRIRIAARRLGGRLV--------------LVVRDNGPGIAEEHLSRVFDPFFTTKPVGK 66
                          90       100       110
                  ....*....|....*....|....*....|
gi 1209301716 379 GTGLGLSQVYGFVRQSSGHIRIYSELGEGS 408
Cdd:cd16976    67 GTGLGLSISYGIVEEHGGRLSVANEEGAGA 96
HATPase_EvgS-ArcB-TorS-like cd16922
Histidine kinase-like ATPase domain of two-component sensor histidine kinases, many are hybrid ...
342-415 8.34e-12

Histidine kinase-like ATPase domain of two-component sensor histidine kinases, many are hybrid sensor histidine kinases, similar to Escherichia coli EvgS, ArcB, TorS, BarA, RcsC; This family contains the histidine kinase-like ATPase (HATPase) domains of various two-component hybrid sensor histidine kinases (HKs), including the following Escherichia coli HKs: EvgS, a HK of the EvgS-EvgA two-component system (TCS) that confers acid resistance; ArcB, a HK of the ArcB-ArcA TCS that modulates the expression of numerous genes in response to respiratory growth conditions; TorS, a HK of the TorS-TorR TCS which is involved in the anaerobic utilization of trimethylamine-N-oxide; BarA, a HK of the BarA-UvrY TCS involved in the regulation of carbon metabolism; and RcsC, a HK of the RcsB-RcsC TCS which regulates the expression of the capsule operon and of the cell division gene ftsZ. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA), with most having accessory sensor domain(s) such as GAF, PAS and CHASE; many are hybrid sensor histidine kinases as they also contain a REC signal receiver domain.


Pssm-ID: 340399 [Multi-domain]  Cd Length: 110  Bit Score: 62.13  E-value: 8.34e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1209301716 342 EPGQYVMVAVTDSGLGMDKSTQEKAFEPFF-----TTKAVGqGTGLGLSQVYGFVRQSSGHIRIYSELGEGSTVKIYLP 415
Cdd:cd16922    32 EDGVQLRFSVEDTGIGIPEEQQARLFEPFSqadssTTRKYG-GTGLGLAISKKLVELMGGDISVESEPGQGSTFTFTLP 109
PRK09959 PRK09959
acid-sensing system histidine kinase EvgS;
292-548 1.45e-11

acid-sensing system histidine kinase EvgS;


Pssm-ID: 182169 [Multi-domain]  Cd Length: 1197  Bit Score: 67.45  E-value: 1.45e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209301716  292 VHADANQLENSLINLALNARDaMPTGGRMTIETANCHLDGAYVAgiaepvepgqyVMVAVTDSGLGMDKSTQEKAFEPFF 371
Cdd:PRK09959   822 VKIDPQAFKQVLSNLLSNALK-FTTEGAVKITTSLGHIDDNHAV-----------IKMTIMDSGSGLSQEEQQQLFKRYS 889
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209301716  372 TTKAVGQ--GTGLGLSQVYGFVRQSSGHIRIYSELGEGSTVKIYLP-----RYAGAEEAA--PFVPPELTAraggselIL 442
Cdd:PRK09959   890 QTSAGRQqtGSGLGLMICKELIKNMQGDLSLESHPGIGTTFTITIPveisqQVATVEAKAeqPITLPEKLS-------IL 962
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209301716  443 VVEDDASLRGYTVQILTELGYGVLEAADGRIGLKVLAERgDIDLLFTDIVMPgGLNGRELADEAVKLHPALKVLfttGYT 522
Cdd:PRK09959   963 IADDHPTNRLLLKRQLNLLGYDVDEATDGVQALHKVSMQ-HYDLLITDVNMP-NMDGFELTRKLREQNSSLPIW---GLT 1037
                          250       260
                   ....*....|....*....|....*....
gi 1209301716  523 RNAIVHHGR--LDPGVHF-LGKPFSFDEL 548
Cdd:PRK09959  1038 ANAQANEREkgLSCGMNLcLFKPLTLDVL 1066
nifL_nitrog TIGR02938
nitrogen fixation negative regulator NifL; NifL is a modulator of the nitrogen fixation ...
69-415 1.65e-11

nitrogen fixation negative regulator NifL; NifL is a modulator of the nitrogen fixation positive regulator protein NifA, and is therefore a negative regulator. It binds NifA. NifA and NifL are encoded by adjacent genes. [Central intermediary metabolism, Nitrogen fixation, Regulatory functions, Protein interactions]


Pssm-ID: 131984 [Multi-domain]  Cd Length: 494  Bit Score: 66.47  E-value: 1.65e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209301716  69 REDVARIVDQtENAFRRRdremlmEFRILRPGdgglvwieARSIIFYDADGRAIRMVGVNADI----TERKRAILQLRAF 144
Cdd:TIGR02938 184 REALAENWPQ-QLAFSNR------EARFDRGG--------GRPARWLSCTGSVIGMESDCADSffcaAEQPYLLLTIADI 248
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209301716 145 TETMEEAVRERTRELVAenearrkaeeLLRQAQKMEVVGQLTGGVAHDFNNLLTIVLGGLDIIGRqlpalgpspeaeRIA 224
Cdd:TIGR02938 249 SNLREEQERARLSALQA----------LMAEEERLEAIRETLSAAIHRLQGPMNLISAAISVLQR------------RGD 306
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209301716 225 KARDMAVEGARRSATLTSR--LLAFSRRQPLDP----RPLDANKLIASTGELL-HRTLGEQIALETVLAAGLWRVHADAN 297
Cdd:TIGR02938 307 DAGNPASAAMLQQALSAGRehMEALRQVIPQSPqeivVPVNLNQILRDVITLStPRLLAAGIVVDWQPAATLPAILGREL 386
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209301716 298 QLENSLINLALNARDAMPTGGRMTIETAnchldgayvagIAEPVEpGQYVMVAVTDSGLGMDKSTQEKAFEPFFTTKA-V 376
Cdd:TIGR02938 387 QLRSLFKALVDNAIEAMNIKGWKRRELS-----------ITTALN-GDLIVVSILDSGPGIPQDLRYKVFEPFFTTKGgS 454
                         330       340       350
                  ....*....|....*....|....*....|....*....
gi 1209301716 377 GQGTGLGLSQVYGFVRQSSGHIRIYSELGEGSTVKIYLP 415
Cdd:TIGR02938 455 RKHIGMGLSVAQEIVADHGGIIDLDDDYSEGCRIIVEFR 493
REC_2_GGDEF cd17544
second phosphoacceptor receiver (REC) domain of uncharacterized GGDEF domain proteins; This ...
441-548 5.27e-11

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: 60.23  E-value: 5.27e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209301716 441 ILVVEDDASLRGYTVQILTELGYGVLEAADGRIGLKVLAERGDIDLLFTDIVMPgGLNGRELADEAVKLHP--ALKVLFT 518
Cdd:cd17544     3 VLVVDDSATSRNHLRALLRRHNFQVLEAANGQEALEVLEQHPDIKLVITDYNMP-EMDGFELVREIRKKYSrdQLAIIGI 81
                          90       100       110
                  ....*....|....*....|....*....|....
gi 1209301716 519 TGYTRNAI----VHHGRLDpgvhFLGKPFSFDEL 548
Cdd:cd17544    82 SASGDNALsarfIKAGAND----FLTKPFLPEEF 111
PRK11091 PRK11091
aerobic respiration control sensor protein ArcB; Provisional
67-505 7.78e-11

aerobic respiration control sensor protein ArcB; Provisional


Pssm-ID: 236842 [Multi-domain]  Cd Length: 779  Bit Score: 64.96  E-value: 7.78e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209301716  67 VFREDVAR-IVDQTENAFRrrDREMLMEFRILRPGDGGLVWIEARSIIFYDADGRAIRMVGVNADITERKRAilqlrafT 145
Cdd:PRK11091  203 VYSPEAAEkVIETDEKVFR--HNVSLTYEQWLDYPDGRKACFELRKVPFYDRVGKRHGLMGFGRDITERKRY-------Q 273
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209301716 146 ETMEEAVRERTR-------EL-------VAenearrkaeeLLRqaqkMEVVGQLTggvAHDFNNLLTI-----VLGGL-- 204
Cdd:PRK11091  274 DALEKASRDKTTfistishELrtplngiVG----------LSR----ILLDTELT---AEQRKYLKTIhvsaiTLGNIfn 336
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209301716 205 DIIgrqlpalgpspeaeriakarDMAvegarrsatltsrllAFSRRQ-PLDPRPLDANKLIASTgELLHRTLGEQIALET 283
Cdd:PRK11091  337 DII--------------------DMD---------------KMERRKlQLDNQPIDFTDFLADL-ENLSGLQAEQKGLRF 380
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209301716 284 VLAAGL---WRVHADANQLENSLINLALNARDAMPTGG-RMTIEtanchldgayvagiaepVEPGQYVMVAVTDSGLGMD 359
Cdd:PRK11091  381 DLEPLLplpHKVITDGTRLRQILWNLISNAVKFTQQGGvTVRVR-----------------YEEGDMLTFEVEDSGIGIP 443
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209301716 360 KSTQEKAFEPFFTTK-------AVGQGTGLGLSQvyGFVRQSSGHIRIYSELGEGSTVKIYLPRYAGAEEAA-PFVPPEL 431
Cdd:PRK11091  444 EDELDKIFAMYYQVKdshggkpATGTGIGLAVSK--RLAQAMGGDITVTSEEGKGSCFTLTIHAPAVAEEVEdAFDEDDM 521
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209301716 432 TARAggseL-ILVVEDDA-------SLrgytvqiLTELGYGVLEAADGRIGLKVLAErGDIDLLFTDIVMPgGLNGRELA 503
Cdd:PRK11091  522 PLPA----LnILLVEDIElnvivarSV-------LEKLGNSVDVAMTGKEALEMFDP-DEYDLVLLDIQLP-DMTGLDIA 588

                  ..
gi 1209301716 504 DE 505
Cdd:PRK11091  589 RE 590
HATPase_TmoS-FixL-DctS-like cd16920
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
299-415 8.09e-11

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Rhizobium meliloti FixL, and Rhodobacter capsulatus DctS; includes hybrid sensor histidine kinase similar to Pseudomonas mendocina TmoS; This family includes the histidine kinase-like ATPase (HATPase) domains of various histidine kinases (HKs) of two-component signal transduction systems (TCSs), such as Pseudomonas mendocina TmoS HK of the TmoS-TmoT TCS, which controls the expression of the toluene-4-monooxygenase pathway, Rhizobium meliloti FixL HK of the FixL-FixJ TCS, which regulates the expression of the genes related to nitrogen fixation in the root nodule in response to O(2) levels, and Rhodobacter capsulatus DctS of the DctS-DctR TCS, which controls synthesis of the high-affinity C4-dicarboxylate transport system. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA) and PAS sensor domain(s); many are hybrid sensor histidine kinases as they also contain a REC signal receiver domain.


Pssm-ID: 340397 [Multi-domain]  Cd Length: 104  Bit Score: 58.95  E-value: 8.09e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209301716 299 LENSLINLALNARDAM----PTGGRMTIETanchldgayvagiaEPVEPGqYVMVAVTDSGLGMDKSTQEKAFEPFFTTK 374
Cdd:cd16920     1 IQQVLINLVRNGIEAMseggCERRELTIRT--------------SPADDR-AVTISVKDTGPGIAEEVAGQLFDPFYTTK 65
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1209301716 375 AvgQGTGLGLSQVYGFVRQSSGHIRIYSELGEGSTVKIYLP 415
Cdd:cd16920    66 S--EGLGMGLSICRSIIEAHGGRLSVESPAGGGATFQFTLP 104
REC smart00448
cheY-homologous receiver domain; CheY regulates the clockwise rotation of E. coli flagellar ...
441-494 1.45e-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: 56.81  E-value: 1.45e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1209301716  441 ILVVEDDASLRGYTVQILTELGYGVLEAADGRIGLKvLAERGDIDLLFTDIVMP 494
Cdd:smart00448   3 ILVVDDDPLLRELLKALLEKEGYEVDEATDGEEALE-LLKEEKPDLILLDIMMP 55
REC_OmpR_DrrD-like cd17625
phosphoacceptor receiver (REC) domain of DrrD-like OmpR family response regulators; DrrD is a ...
442-556 1.72e-10

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: 58.39  E-value: 1.72e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209301716 442 LVVEDDASLRGYTVQILTELGYGVLEAADGRIGLKvLAERGDIDLLFTDIVMPgGLNGRELADEAVKLHPALKVLFTTGy 521
Cdd:cd17625     1 LVVEDEKDLSEAITKHLKKEGYTVDVCFDGEEGLE-YALSGIYDLIILDIMLP-GMDGLEVLKSLREEGIETPVLLLTA- 77
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1209301716 522 tRNAI------VHHGRLDpgvhFLGKPFSFDELALKIRSVL 556
Cdd:cd17625    78 -LDAVedrvkgLDLGADD----YLPKPFSLAELLARIRALL 113
REC_CheY4-like cd17562
phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY4 and similar CheY ...
441-556 1.74e-10

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: 58.47  E-value: 1.74e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209301716 441 ILVVEDDASLRGYTVQILTELGYGVLEAADGRIGLkVLAERGDIDLLFTDIVMPgGLNGRELAdEAVKLHPALK---VLF 517
Cdd:cd17562     3 ILAVDDSASIRQMVSFTLRGAGYEVVEAADGRDAL-SKAQSKKFDLIITDQNMP-NMDGIELI-KELRKLPAYKftpILM 79
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1209301716 518 TTGYTRNAIVHHGRLDPGVHFLGKPFSFDELALKIRSVL 556
Cdd:cd17562    80 LTTESSDEKKQEGKAAGATGWLVKPFDPEQLLEVVKKVL 118
PAS COG2202
PAS domain [Signal transduction mechanisms];
16-250 1.99e-10

PAS domain [Signal transduction mechanisms];


Pssm-ID: 441804 [Multi-domain]  Cd Length: 258  Bit Score: 61.58  E-value: 1.99e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209301716  16 SDEVLALAQEAGRVGIFEWHVPAGTLLVSQQFLVIYGLDCFDGRHESWLACVFREDVARIVDQTENAFRRRdREMLMEFR 95
Cdd:COG2202     9 SERRLRALVESSPDAIIITDLDGRILYVNPAFERLTGYSAEELLGKTLRDLLPPEDDDEFLELLRAALAGG-GVWRGELR 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209301716  96 ILRPgDGGLVWIEARSIIFYDADGRAIRMVGVNADITERKRAilqlraftetmEEAVRERTRELvaenearrkaeELLRQ 175
Cdd:COG2202    88 NRRK-DGSLFWVELSISPVRDEDGEITGFVGIARDITERKRA-----------EEALRESEERL-----------RLLVE 144
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1209301716 176 AQKMEVVGQLTGGVAHDFNNLLTIVLGG--LDIIGRQLPALGPSPEAERIAKARDMAVEGARRSATLTSRLLAFSRR 250
Cdd:COG2202   145 NAPDGIFVLDLDGRILYVNPAAEELLGYspEELLGKSLLDLLHPEDRERLLELLRRLLEGGRESYELELRLKDGDGR 221
REC_NtrX-like cd17550
phosphoacceptor receiver (REC) domain of nitrogen assimilation regulatory protein NtrX and ...
441-557 2.61e-10

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: 57.89  E-value: 2.61e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209301716 441 ILVVEDDASLRGYTVQILTELGYGVLEAADGRIGLKVLAERgDIDLLFTDIVMPgGLNGRELADEAVKLHPALKVLFTTG 520
Cdd:cd17550     1 ILIVDDEEDIRESLSGILEDEGYEVDTAADGEEALKLIKER-RPDLVLLDIWLP-DMDGLELLKEIKEKYPDLPVIMISG 78
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1209301716 521 ytrnaivhHGRLDPGVH--------FLGKPFSFDELALKIRSVLD 557
Cdd:cd17550    79 --------HGTIETAVKatklgaydFIEKPLSLDRLLLTIERALE 115
REC_OmpR cd17574
phosphoacceptor receiver (REC) domain of OmpR family response regulators; OmpR-like proteins ...
442-519 3.97e-10

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


Pssm-ID: 381116 [Multi-domain]  Cd Length: 99  Bit Score: 56.65  E-value: 3.97e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1209301716 442 LVVEDDASLRGYTVQILTELGYGVLEAADGRIGLKvLAERGDIDLLFTDIVMPgGLNGRELADEAVKLHPALKVLFTT 519
Cdd:cd17574     1 LVVEDDEEIAELLSDYLEKEGYEVDTAADGEEALE-LAREEQPDLIILDVMLP-GMDGFEVCRRLREKGSDIPIIMLT 76
PRK11466 PRK11466
hybrid sensory histidine kinase TorS; Provisional
344-514 4.80e-10

hybrid sensory histidine kinase TorS; Provisional


Pssm-ID: 236914 [Multi-domain]  Cd Length: 914  Bit Score: 62.62  E-value: 4.80e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209301716 344 GQYVMVAVTDSGLGMDKSTQEKAFEPFFTTKAVGQGTGLGLSQVYGFVRQSSGHIRIYSELGEGSTVKIYLP-RYAgaee 422
Cdd:PRK11466  590 GEQWLVEVEDSGCGIDPAKLAEIFQPFVQVSGKRGGTGLGLTISSRLAQAMGGELSATSTPEVGSCFCLRLPlRVA---- 665
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209301716 423 AAPfvPPELTARA---GGSELILvVEDDASLRGYTVQILTELGYGVLEAADGRIGLKVLAERGDIDLLFTDIVMPgGLNG 499
Cdd:PRK11466  666 TAP--VPKTVNQAvrlDGLRLLL-IEDNPLTQRITAEMLNTSGAQVVAVGNAAQALETLQNSEPFAAALVDFDLP-DYDG 741
                         170
                  ....*....|....*
gi 1209301716 500 RELADEAVKLHPALK 514
Cdd:PRK11466  742 ITLARQLAQQYPSLV 756
REC_NarL-like cd17535
phosphoacceptor receiver (REC) domain of NarL (Nitrate/Nitrite response regulator L) family ...
441-556 5.10e-10

phosphoacceptor receiver (REC) domain of NarL (Nitrate/Nitrite response regulator L) family response regulators; The NarL family is one of the more abundant families of DNA-binding response regulators (RRs). Members of the NarL family contain a REC domain and a helix-turn-helix (HTH) DNA-binding output domain, with a majority of members containing a LuxR-type HTH domain. They function as transcriptional regulators. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381090 [Multi-domain]  Cd Length: 117  Bit Score: 57.14  E-value: 5.10e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209301716 441 ILVVEDDASLRGYTVQIL-TELGY-GVLEAADGRIGLKvLAERGDIDLLFTDIVMPgGLNGRELADEAVKLHPALKVLFT 518
Cdd:cd17535     1 VLIVDDHPLVREGLRRLLeSEPDIeVVGEAADGEEALA-LLRELRPDVVLMDLSMP-GMDGIEALRRLRRRYPDLKVIVL 78
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1209301716 519 TGYTRNAIVHHGrLDPGVH-FLGKPFSFDELALKIRSVL 556
Cdd:cd17535    79 TAHDDPEYVLRA-LKAGAAgYLLKDSSPEELIEAIRAVA 116
REC_DC-like cd17534
phosphoacceptor receiver (REC) domain of modulated diguanylate cyclase and similar domains; ...
441-548 6.41e-10

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: 56.65  E-value: 6.41e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209301716 441 ILVVEDDASLRGYTVQILTELGYGVLE-AADGRIGLKvLAERGDIDLLFTDIVMPGGLNGRELADEAVKLHPaLKVLFTT 519
Cdd:cd17534     3 ILIVEDEAIIALDLKEILESLGYEVVGiADSGEEAIE-LAEENKPDLILMDINLKGDMDGIEAAREIREKFD-IPVIFLT 80
                          90       100
                  ....*....|....*....|....*....
gi 1209301716 520 GYTRNAIVHHGRLDPGVHFLGKPFSFDEL 548
Cdd:cd17534    81 AYSDEETLERAKETNPYGYLVKPFNEREL 109
LytT COG3279
DNA-binding response regulator, LytR/AlgR family [Transcription, Signal transduction ...
441-549 7.96e-10

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


Pssm-ID: 442510 [Multi-domain]  Cd Length: 235  Bit Score: 59.44  E-value: 7.96e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209301716 441 ILVVEDDASLRGYTVQILTEL-GYGVL-EAADGRIGLKVLaERGDIDLLFTDIVMPGgLNGRELADEAVKLHPALKVLFT 518
Cdd:COG3279     4 ILIVDDEPLARERLERLLEKYpDLEVVgEASNGEEALELL-EEHKPDLVFLDIQMPG-LDGFELARQLRELDPPPPIIFT 81
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1209301716 519 TGYTRNAI----VHhgrldpGVHFLGKPFSFDELA 549
Cdd:COG3279    82 TAYDEYALeafeVN------AVDYLLKPIDEERLA 110
REC_OmpR_CusR-like cd19935
phosphoacceptor receiver (REC) domain of CusR-like OmpR family response regulators; ...
441-519 1.07e-09

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: 55.52  E-value: 1.07e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1209301716 441 ILVVEDDASLRGYTVQILTELGYGVLEAADGRIGLkVLAERGDIDLLFTDIVMPgGLNGRELADEAVKLHPALKVLFTT 519
Cdd:cd19935     1 ILVVEDEKKLAEYLKKGLTEEGYAVDVAYDGEDGL-HLALTNEYDLIILDVMLP-GLDGLEVLRRLRAAGKQTPVLMLT 77
glnL PRK11073
nitrogen regulation protein NR(II);
158-415 1.63e-09

nitrogen regulation protein NR(II);


Pssm-ID: 182947 [Multi-domain]  Cd Length: 348  Bit Score: 59.71  E-value: 1.63e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209301716 158 ELVAENEARRKAEELLRQAQKMeVVGQLTGGVAHDFNNlltiVLGGLDIIGRQLPALGPSPEAERIAKardMAVEGARRS 237
Cdd:PRK11073  107 EMAPMDNQRRLSQEQLQHAQQV-AARDLVRGLAHEIKN----PLGGLRGAAQLLSKALPDPALTEYTK---VIIEQADRL 178
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209301716 238 ATLTSRLLAfsRRQPLDPRPLDANKLIASTGELLHRTLGEQIALETVLAAGLWRVHADANQLENSLINLALNARDAM-PT 316
Cdd:PRK11073  179 RNLVDRLLG--PQRPGTHVTESIHKVAERVVQLVSLELPDNVRLIRDYDPSLPELAHDPDQIEQVLLNIVRNALQALgPE 256
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209301716 317 GGRMTIET-----ANCHldgayvagiaepvepGQ-YVMVA---VTDSGLGMDKSTQEKAFEPFFTTKAvgQGTGLGLSQV 387
Cdd:PRK11073  257 GGTITLRTrtafqLTLH---------------GErYRLAAridIEDNGPGIPPHLQDTLFYPMVSGRE--GGTGLGLSIA 319
                         250       260
                  ....*....|....*....|....*...
gi 1209301716 388 YGFVRQSSGHIRIYSELGEgSTVKIYLP 415
Cdd:PRK11073  320 RNLIDQHSGKIEFTSWPGH-TEFSVYLP 346
REC_CheY_CheY3 cd19923
phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY3 and similar CheY ...
441-556 5.28e-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: 5.28e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209301716 441 ILVVEDDASLRGYTVQILTELGY-GVLEAADGRIGLKVLaERGDIDLLFTDIVMPgGLNGREL-----ADEAVKLHPALK 514
Cdd:cd19923     3 VLVVDDFSTMRRIIKNLLKELGFnNVEEAEDGVDALEKL-KAGGFDFVITDWNMP-NMDGLELlktirADGALSHLPVLM 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1209301716 515 VlfTTGYTRNAIVHhgRLDPGVH-FLGKPFSFDELALKIRSVL 556
Cdd:cd19923    81 V--TAEAKKENVIA--AAQAGVNnYIVKPFTAATLKEKLEKIF 119
REC_hyHK_CKI1_RcsC-like cd17546
phosphoacceptor receiver (REC) domain of hybrid sensor histidine kinases/response regulators ...
441-548 5.90e-09

phosphoacceptor receiver (REC) domain of hybrid sensor histidine kinases/response regulators similar to Arabidopsis thaliana CKI1 and Escherichia coli RcsC; This family is composed of hybrid sensor histidine kinases/response regulators that are sensor histidine kinases (HKs) fused with a REC domain, similar to the sensor histidine kinase CKI1 from Arabidopsis thaliana, which is involved in multi-step phosphorelay (MSP) signaling that mediates responses to a variety of important stimuli in plants. MSP involves a signal being transferred from HKs via histidine phosphotransfer proteins (AHP1-AHP5) to nuclear response regulators. The CKI1 REC domain specifically interacts with the downstream signaling protein AHP2, AHP3 and AHP5. The plant MSP system has evolved from the prokaryotic two-component system (TCS), which allows organisms to sense and respond to changes in environmental conditions. This family also includes bacterial hybrid sensor HKs such as Escherichia coli RcsC, which is a component of the Rcs signalling pathway that controls a variety of physiological functions like capsule synthesis, cell division, and motility. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381099 [Multi-domain]  Cd Length: 113  Bit Score: 54.01  E-value: 5.90e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209301716 441 ILVVEDDASLRGYTVQILTELGYGVLEAADGRIGLKVLAERgDIDLLFTDIVMPgGLNGRELAD---EAVKLHPALKVLF 517
Cdd:cd17546     1 VLVVDDNPVNRKVLKKLLEKLGYEVDVAENGQEALELLKEE-PFDLVLMDLQMP-VMDGLEATRrirELEGGGRRTPIIA 78
                          90       100       110
                  ....*....|....*....|....*....|..
gi 1209301716 518 TTGYTRNAIVHHgRLDPGV-HFLGKPFSFDEL 548
Cdd:cd17546    79 LTANALEEDREK-CLEAGMdDYLSKPVKLDQL 109
PAS COG2202
PAS domain [Signal transduction mechanisms];
16-141 6.59e-09

PAS domain [Signal transduction mechanisms];


Pssm-ID: 441804 [Multi-domain]  Cd Length: 258  Bit Score: 56.96  E-value: 6.59e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209301716  16 SDEVLALAQEAGRVGIFEWHVPAGTLLVSQQFLVIYGLDCFDGRHESWLACVFREDVARIVDQTENAFRRRDREMLMEFR 95
Cdd:COG2202   135 SEERLRLLVENAPDGIFVLDLDGRILYVNPAAEELLGYSPEELLGKSLLDLLHPEDRERLLELLRRLLEGGRESYELELR 214
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1209301716  96 ILRpGDGGLVWIEARSIIFYDaDGRAIRMVGVNADITERKRAILQL 141
Cdd:COG2202   215 LKD-GDGRWVWVEASAVPLRD-GGEVIGVLGIVRDITERKRAEEAL 258
PRK09303 PRK09303
histidine kinase;
146-419 7.15e-09

histidine kinase;


Pssm-ID: 236462 [Multi-domain]  Cd Length: 380  Bit Score: 58.04  E-value: 7.15e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209301716 146 ETMEEAVRERTRELVAENEA---RRKAEELLRQAQKMEvvgQLTGGVAHDFNNLLT---IVLGGLDIiGRQlpalgpSPE 219
Cdd:PRK09303  115 PSEIDSGRYSQELLQLSDELfvlRQENETLLEQLKFKD---RVLAMLAHDLRTPLTaasLALETLEL-GQI------DED 184
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209301716 220 AERIAKARDMAVEGARRS----ATLTSRLLAFSRRQ----PLDPRPLDANKLIASTGELLH-RTLGEQIALETVLAAGLW 290
Cdd:PRK09303  185 TELKPALIEQLQDQARRQleeiERLITDLLEVGRTRwealRFNPQKLDLGSLCQEVILELEkRWLAKSLEIQTDIPSDLP 264
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209301716 291 RVHADANQLENSLINLALNARDAMPTGGrmTIETANCHldgayvagiaepvEPGQYVMVAVTDSGLGMDKSTQEKAFEPF 370
Cdd:PRK09303  265 SVYADQERIRQVLLNLLDNAIKYTPEGG--TITLSMLH-------------RTTQKVQVSICDTGPGIPEEEQERIFEDR 329
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1209301716 371 FTTKAVGQ--GTGLGLSQVYGFVRQSSGHIRIYSELGEGSTVKIYLPRYAG 419
Cdd:PRK09303  330 VRLPRDEGteGYGIGLSVCRRIVRVHYGQIWVDSEPGQGSCFHFTLPVYRG 380
PAC smart00086
Motif C-terminal to PAS motifs (likely to contribute to PAS structural domain); PAC motif ...
92-134 2.15e-08

Motif C-terminal to PAS motifs (likely to contribute to PAS structural domain); PAC motif occurs C-terminal to a subset of all known PAS motifs. It is proposed to contribute to the PAS domain fold.


Pssm-ID: 197509  Cd Length: 43  Bit Score: 50.26  E-value: 2.15e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 1209301716   92 MEFRILRPgDGGLVWIEARSIIFYDADGRAIRMVGVNADITER 134
Cdd:smart00086   2 VEYRLRRK-DGSYIWVLVSASPIRDEDGEVEGILGVVRDITER 43
HATPase_FilI-like cd16921
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
350-415 2.74e-08

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Methanosaeta harundinacea FilI and some hybrid sensor histidine kinases; This family includes FilI, the histidine kinase (HK) component of FilI-FilRs, a two-component signal transduction system (TCS) of the methanogenic archaeon, Methanosaeta harundinacea, which is involved in regulating methanogenesis. The cytoplasmic HK core consists of a C-terminal HK-like ATPase domain (represented here) and a histidine kinase dimerization and phosphoacceptor domain (HisKA) domain, which, in FilI, are coupled to CHASE, HAMP, PAS, and GAF sensor domains. FilI-FilRs catalyzes the phosphotransfer between FilI (HK) and FilRs (FilR1 and FilR2, response regulators) of the TCS. TCSs are predicted to be of bacterial origin, and acquired by archaea by horizontal gene transfer. This model also includes related HATPase domains such as that of Synechocystis sp. PCC6803 phytochrome-like protein Cph1. Proteins having this HATPase domain and HisKA domain also have accessory sensor domains such as CHASE, GAF, HAMP and PAS; some are hybrid sensor histidine kinases as they also contain a REC signal receiver domain.


Pssm-ID: 340398 [Multi-domain]  Cd Length: 105  Bit Score: 51.94  E-value: 2.74e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1209301716 350 AVTDSGLGMDKSTQEKAFEPF--FTTKAVGQGTGLGLSQVYGFVRQSSGHIRIYSELGEGSTVKIYLP 415
Cdd:cd16921    38 YVRDNGIGIDPEYAEKVFGIFqrLHSREEYEGTGVGLAIVRKIIERHGGRIWLESEPGEGTTFYFTLP 105
HATPase_Glnl-NtrB-like cd16918
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
299-415 2.78e-08

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Escherichia coli GlnL (synonyms NtrB and NRII); This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component sensor histidine kinase (HKs), similar to Escherichia coli GlnL/NtrB/NRII HK of the two-component regulatory system (TCS) GlnL/GlnG (NtrB-NtrC, or NRII-NRI), which regulates the transcription of genes encoding metabolic enzymes and permeases in response to carbon and nitrogen status in E. coli and related bacteria. Also included in this family are Rhodobacter capsulatus NtrB, Azospirillum brasilense NtrB, Vibrio alginolyticus NtrB, Rhizobium leguminosarum biovar phaseoli NtrB, and Herbaspirillum seropedicae NtrB. Escherichia coli GlnL/NtrB/NRII is both a kinase and a phosphatase, catalyzing the phosphorylation and dephosphorylation of GlnG/NtrC/NRI. The kinase and phosphatase activities of GlnL/NtrB/NRII are regulated by the PII signal transduction protein, which on binding to GlnL/NtrB/NRII, inhibits the kinase activity of GlnL/NtrB/NRII and activates the GlnL/NtrB/NRII phosphatase activity. Proteins having this HATPase domain also have a histidine kinase dimerization and phosphoacceptor domain (HisKA); some also contain PAS sensor domain(s).


Pssm-ID: 340395 [Multi-domain]  Cd Length: 109  Bit Score: 52.02  E-value: 2.78e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209301716 299 LENSLINLALNARDAMP-TGGRMTIETANCHldGAYVAGiaepvePGQYV--MVAVTDSGLGMDKSTQEKAFEPFFTTKA 375
Cdd:cd16918     1 LIQVFLNLVRNAAQALAgSGGEIILRTRTQR--QVTLGH------PRHRLalRVSVIDNGPGIPPDLQDTIFYPMVSGRE 72
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1209301716 376 vgQGTGLGLSQVYGFVRQSSGHIRIYSELGEgsTV-KIYLP 415
Cdd:cd16918    73 --NGTGLGLAIAQNIVSQHGGVIECDSQPGH--TVfSVSLP 109
PRK11517 PRK11517
DNA-binding response regulator HprR;
441-556 3.01e-08

DNA-binding response regulator HprR;


Pssm-ID: 183172 [Multi-domain]  Cd Length: 223  Bit Score: 54.52  E-value: 3.01e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209301716 441 ILVVEDDASLRGYTVQILTELGYGVLEAADGRIGLKvLAERGDIDLLFTDIVMPgGLNGRELAdEAVKLHPALKVLFTTG 520
Cdd:PRK11517    3 ILLIEDNQRTQEWVTQGLSEAGYVIDAVSDGRDGLY-LALKDDYALIILDIMLP-GMDGWQIL-QTLRTAKQTPVICLTA 79
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1209301716 521 ytRNAIVHHGR-LDPGVH-FLGKPFSFDELALKIRSVL 556
Cdd:PRK11517   80 --RDSVDDRVRgLDSGANdYLVKPFSFSELLARVRAQL 115
REC_RssB-like cd17555
phosphoacceptor receiver (REC) domain of Pseudomonas aeruginosa RssB and similar domains; ...
441-520 5.19e-08

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: 51.43  E-value: 5.19e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209301716 441 ILVVEDDASLRGYTVQILTELGYGVLEAADGRIGLKVLAERgDIDLLFTDIVMPgGLNGRELADEAVKLHPALKVLFTTG 520
Cdd:cd17555     3 ILVIDDDEVVRESIAAYLEDSGFQVLQAADGRQGLELFRSE-QPDLVLCDLRMP-EMDGLEVLKQITKESPDTPVIVVSG 80
COG4567 COG4567
DNA-binding response regulator, ActR/RegA family, consists of REC and Fis-type HTH domains ...
438-549 6.12e-08

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: 52.61  E-value: 6.12e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209301716 438 SELILVVEDDASLRGYTVQILTELGYGVLEAADGRIGLKvLAERGDIDLLFTDIVMPGGlNGRELADEAVKLHPALKVLF 517
Cdd:COG4567     4 DRSLLLVDDDEAFARVLARALERRGFEVTTAASVEEALA-LLEQAPPDYAVLDLRLGDG-SGLDLIEALRERDPDARIVV 81
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1209301716 518 TTGY----TRNAIVHHGrldpGVHFLGKPFSFDELA 549
Cdd:COG4567    82 LTGYasiaTAVEAIKLG----ADDYLAKPADADDLL 113
orf27 CHL00148
Ycf27; Reviewed
439-556 6.73e-08

Ycf27; Reviewed


Pssm-ID: 214376 [Multi-domain]  Cd Length: 240  Bit Score: 53.57  E-value: 6.73e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209301716 439 ELILVVEDDASLRGYTVQILTELGYGVLEAADGRIGLKVLaERGDIDLLFTDIVMPgGLNGRELADEaVKLHPALKVLFT 518
Cdd:CHL00148    7 EKILVVDDEAYIRKILETRLSIIGYEVITASDGEEALKLF-RKEQPDLVILDVMMP-KLDGYGVCQE-IRKESDVPIIML 83
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1209301716 519 TGYTRNAIVHHGRLDPGVHFLGKPFSFDELALKIRSVL 556
Cdd:CHL00148   84 TALGDVSDRITGLELGADDYVVKPFSPKELEARIRSVL 121
REC_PdtaR-like cd19932
phosphoacceptor receiver (REC) domain of PdtaR and similar proteins; This subfamily includes ...
441-548 1.61e-07

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: 50.10  E-value: 1.61e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209301716 441 ILVVEDDASLRGYTVQILTELGYGVL-EAADGRIGLKvLAERGDIDLLFTDIVMPGgLNGRELADEAVKLHPAlKVLFTT 519
Cdd:cd19932     3 VLIAEDEALIRMDLREMLEEAGYEVVgEASDGEEAVE-LAKKHKPDLVIMDVKMPR-LDGIEAAKIITSENIA-PIVLLT 79
                          90       100
                  ....*....|....*....|....*....
gi 1209301716 520 GYTRNAIVHHGRLDPGVHFLGKPFSFDEL 548
Cdd:cd19932    80 AYSQQDLVERAKEAGAMAYLVKPFSESDL 108
PRK11100 PRK11100
sensory histidine kinase CreC; Provisional
215-418 1.96e-07

sensory histidine kinase CreC; Provisional


Pssm-ID: 236846 [Multi-domain]  Cd Length: 475  Bit Score: 53.69  E-value: 1.96e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209301716 215 GPSPEAERIAKARDMAVEgARRSATLTSRLLAFSR---RQPLDPR-PLDANKLIASTGELLH-RTLGEQIALEtVLAAGL 289
Cdd:PRK11100  283 EDPPPEDRARFTGNILTQ-SARLQQLIDRLLELARleqRQELEVLePVALAALLEELVEAREaQAAAKGITLR-LRPDDA 360
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209301716 290 WrVHADANQLENSLINLALNARDAMPTGGRMTIEtanchldgayvagiAEPVepGQYVMVAVTDSGLGMDKSTQEKAFEP 369
Cdd:PRK11100  361 R-VLGDPFLLRQALGNLLDNAIDFSPEGGTITLS--------------AEVD--GEQVALSVEDQGPGIPDYALPRIFER 423
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1209301716 370 FFTTKAVGQG---TGLGLSQVYGFVRQSSGHIRIYSELGEGSTVKIYLPRYA 418
Cdd:PRK11100  424 FYSLPRPANGrksTGLGLAFVREVARLHGGEVTLRNRPEGGVLATLTLPRHF 475
REC_CheY cd17542
phosphoacceptor receiver (REC) domain of chemotaxis protein CheY; The chemotaxis response ...
441-556 2.09e-07

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


Pssm-ID: 381097 [Multi-domain]  Cd Length: 117  Bit Score: 49.58  E-value: 2.09e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209301716 441 ILVVEDDASLRGYTVQILTELGYGVL-EAADGRIGLKVLAERgDIDLLFTDIVMPgGLNGRELADEAVKLHPALKVLFTT 519
Cdd:cd17542     3 VLIVDDAAFMRMMLKDILTKAGYEVVgEAANGEEAVEKYKEL-KPDLVTMDITMP-EMDGIEALKEIKKIDPNAKVIMCS 80
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1209301716 520 GYTRNAIVHHGRLDPGVHFLGKPFSFDELALKIRSVL 556
Cdd:cd17542    81 AMGQEEMVKEAIKAGAKDFIVKPFQPERVLEAVEKVL 117
HATPase_NtrY-like cd16944
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
295-415 2.50e-07

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Azorhizobium caulinodans NtrY; This family includes the histidine kinase-like ATPase (HATPase) domains of various histidine kinases (HKs) of two-component signal transduction systems (TCSs) such as Azorhizobium caulinodans ORS571 NtrY of the NtrY-NtrX TCS, which is involved in nitrogen fixation and metabolism. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA) and a HAMP sensor domain; some also have PAS sensor domains.


Pssm-ID: 340420 [Multi-domain]  Cd Length: 108  Bit Score: 49.07  E-value: 2.50e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209301716 295 DANQLENSLINLALNARDAmptggrmtIETANchLDGAYVAGIAEPVEPGQYVMVaVTDSGLGMDKSTQEKAFEPFFTTK 374
Cdd:cd16944     1 DTTQISQVLTNILKNAAEA--------IEGRP--SDVGEVRIRVEADQDGRIVLI-VCDNGKGFPREMRHRATEPYVTTR 69
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1209301716 375 AvgQGTGLGLSQVYGFVRQSSGHIRIYSELGEGSTVKIYLP 415
Cdd:cd16944    70 P--KGTGLGLAIVKKIMEEHGGRISLSNREAGGACIRIILP 108
HATPase_TutC-TodS-like cd16925
Histidine kinase-like ATPase domain of hybrid sensor histidine kinases similar to Pseudomonas ...
295-415 2.52e-07

Histidine kinase-like ATPase domain of hybrid sensor histidine kinases similar to Pseudomonas putida TodS and Thauera aromatica TutC; This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component hybrid sensor histidine kinase (HKs) such Pseudomonas putida TodS HK of the TodS-TodT two-component regulatory system (TCS) which controls the expression of a toluene degradation pathway. Thauera aromatica TutC may be part of a TCS that is involved in anaerobic toluene metabolism. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA), PAS sensor domain(s) and a REC domain.


Pssm-ID: 340402 [Multi-domain]  Cd Length: 110  Bit Score: 49.41  E-value: 2.52e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209301716 295 DANQLENSLINLALNARDAMPTGGRMtietaNCHLDgayvagiaepVEPGQYVMVAVTDSGLGMDKSTQEKAFEPFFTTK 374
Cdd:cd16925     1 DAEKYERVVLNLLSNAFKFTPDGGRI-----RCILE----------KFRLNRFLLTVSDSGPGIPPNLREEIFERFRQGD 65
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1209301716 375 AVGQ----GTGLGLSQVYGFVRQSSGHIRIYSELGEGSTVKIYLP 415
Cdd:cd16925    66 GSSTrahgGTGLGLSIVKEFVELHGGTVTVSDAPGGGALFQVELP 110
REC_RcNtrC-like cd19928
phosphoacceptor receiver (REC) domain of Rhodobacter capsulatus nitrogen regulatory protein C ...
441-516 2.75e-07

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


Pssm-ID: 381155 [Multi-domain]  Cd Length: 100  Bit Score: 49.04  E-value: 2.75e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1209301716 441 ILVVEDDASLRGYTVQILTELGYGVlEAADGRIGLKVLAERGDIDLLFTDIVMPGGlNGRELADEAVKLHPALKVL 516
Cdd:cd19928     1 ILVADDDRAIRTVLTQALGRAGYEV-RTTGNAATLWRWVEEGEGDLVITDVVMPDE-NGLDLIPRIKKARPDLPII 74
HATPase_DpiB-CitA-like cd16915
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
344-415 3.35e-07

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Escherichia coli K-12 DpiB, DcuS, and Bacillus subtilis CitS, DctS, and YufL; This family includes histidine kinase-like ATPase domains of Escherichia coli K-12 DpiB and DcuS, and Bacillus subtilis CitS, DctS and MalK histidine kinases (HKs) all of which are two component transduction systems (TCSs). E. coli K-12 DpiB (also known as CitA) is the histidine kinase (HK) of DpiA-DpiB, a two-component signal transduction system (TCS) required for the expression of citrate-specific fermentation genes and genes involved in plasmid inheritance. E. coli K-12 DcuS (also known as YjdH) is the HK of DcuS-DcuR, a TCS that in the presence of the extracellular C4-dicarboxlates, activates the expression of the genes of anaerobic fumarate respiration and of aerobic C4-dicarboxylate uptake. CitS is the HK of Bacillus subtilis CitS-CitT, a TCS which regulates expression of CitM, the Mg-citrate transporter. Bacillus subtilis DctS forms a tripartite sensor unit (DctS/DctA/DctB) for sensing C4 dicarboxylates. Bacillus subtilis MalK (also known as YfuL) is the HK of MalK-MalR (YufL-YufM) a TCS which regulates the expression of the malate transporters MaeN (YufR) and YflS, and is essential for utilization of malate in minimal medium. Proteins having this DpiB-CitA-like HATPase domain generally have sensor domains such as Cache and PAS, and a histidine kinase A (HisKA)-like SpoOB-type, alpha-helical domain.


Pssm-ID: 340392 [Multi-domain]  Cd Length: 104  Bit Score: 48.82  E-value: 3.35e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1209301716 344 GQYVMVAVTDSGLGMDKSTQEKAFEPFFTTKAVGqGTGLGLSQVYGFVRQSSGHIRIYSELGEGSTVKIYLP 415
Cdd:cd16915    34 GDDLVIEVRDTGPGIAPELRDKVFERGVSTKGQG-ERGIGLALVRQSVERLGGSITVESEPGGGTTFSIRIP 104
REC_typeB_ARR-like cd17584
phosphoacceptor receiver (REC) domain of type B Arabidopsis response regulators (ARRs) and ...
441-549 3.78e-07

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: 48.78  E-value: 3.78e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209301716 441 ILVVEDDASLRGYTVQILTELGYGVLEAADGRIGLKVLAERGD-IDLLFTDIVMPgGLNGRELAdEAVKLHPALKV-LFT 518
Cdd:cd17584     1 VLVVDDDPTCLAILKRMLLRCGYQVTTCTDAEEALSMLRENKDeFDLVITDVHMP-DMDGFEFL-ELIRLEMDLPViMMS 78
                          90       100       110
                  ....*....|....*....|....*....|....
gi 1209301716 519 TGYTRNAI---VHHGrldpGVHFLGKPFSFDELA 549
Cdd:cd17584    79 ADGSTSTVmkgLAHG----ACDYLLKPVSIEDLK 108
REC_OmpR_VirG cd17594
phosphoacceptor receiver (REC) domain of VirG-like OmpR family response regulators; VirG is ...
440-553 4.11e-07

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: 48.60  E-value: 4.11e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209301716 440 LILVVEDDASLRGYTVQILTELGYGVLEAADGRIGLKVLAERgDIDLLFTDIvMPGGLNGRELAdEAVKLHPALKVLFTT 519
Cdd:cd17594     1 HVLVVDDDAAMRHLLILYLRERGFDVTAAADGAEEARLMLHR-RVDLVLLDL-RLGQESGLDLL-RTIRARSDVPIIIIS 77
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1209301716 520 GYTRNAIVHHGRLDPGV-HFLGKPFSFDELALKIR 553
Cdd:cd17594    78 GDRRDEIDRVVGLELGAdDYLAKPFGLRELLARVR 112
REC_Spo0F-like cd17553
phosphoacceptor receiver (REC) domain of Spo0F and similar domains; Spo0F, a stand-alone ...
439-556 6.28e-07

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: 48.32  E-value: 6.28e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209301716 439 ELILVVEDDASLRGYTVQILTELGYGVLEAADGRIGLKVLaERGDIDLLFTDIVMPgGLNGRELADEAVKLHPALKVLFT 518
Cdd:cd17553     1 EKILIVDDQYGIRILLNEVFNKEGYQTFQAANGLQALDIV-TKERPDLVLLDMKIP-GMDGIEILKRMKVIDENIRVIIM 78
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1209301716 519 TGYTRNAIVHHGR-LDPGVHFlGKPFSFDELALKIRSVL 556
Cdd:cd17553    79 TAYGELDMIQESKeLGALTHF-AKPFDIDEIRDAVKKYL 116
REC_CheV-like cd19924
phosphoacceptor receiver (REC) domain of chemotaxis protein CheV and similar proteins; This ...
441-517 7.31e-07

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: 47.76  E-value: 7.31e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209301716 441 ILVVEDDASLRGYTVQILTELGYGVLEAADGRIGLKVL--------AERGDIDLLFTDIVMPgGLNGRELADEaVKLHPA 512
Cdd:cd19924     1 ILVVDDSPTARKQLRDLLKNLGFEIAEAVDGEEALNKLenlakegnDLSKELDLIITDIEMP-KMDGYELTFE-LRDDPR 78

                  ....*
gi 1209301716 513 LKVLF 517
Cdd:cd19924    79 LANIP 83
PRK10841 PRK10841
two-component system sensor histidine kinase RcsC;
344-466 1.62e-06

two-component system sensor histidine kinase RcsC;


Pssm-ID: 182772 [Multi-domain]  Cd Length: 924  Bit Score: 51.13  E-value: 1.62e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209301716 344 GQYVMVAVTDSGLGMDKSTQEKAFEPFFTtkaVG-------QGTGLGLSQVYGFVRQSSGHIRIYSELGEGSTVKIYLPR 416
Cdd:PRK10841  591 GDYLSFRVRDTGVGIPAKEVVRLFDPFFQ---VGtgvqrnfQGTGLGLAICEKLINMMDGDISVDSEPGMGSQFTIRIPL 667
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1209301716 417 YagaeeAAPFVPPELTARAGGSELILVVEdDASLRGYTVQILTELGYGVL 466
Cdd:PRK10841  668 Y-----GAQYPQKKGVEGLQGKRCWLAVR-NASLEQFLETLLQRSGIQVQ 711
REC_HupR-like cd17569
phosphoacceptor receiver (REC) domain of hydrogen uptake protein regulator (HupR) and similar ...
441-557 1.83e-06

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


Pssm-ID: 381113 [Multi-domain]  Cd Length: 118  Bit Score: 47.01  E-value: 1.83e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209301716 441 ILVVEDDASLRGYTVQILTELGYGVLEAADGRIGLKVLAERgDIDLLFTDIVMPgGLNGRELADEAVKLHP-ALKVLFtT 519
Cdd:cd17569     3 ILLVDDEPNILKALKRLLRREGYEVLTATSGEEALEILKQE-PVDVVISDQRMP-GMDGAELLKRVRERYPdTVRILL-T 79
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1209301716 520 GYT-RNAIVH---HGRldpgVH-FLGKPFSFDELALKIRSVLD 557
Cdd:cd17569    80 GYAdLDAAIEainEGE----IYrFLTKPWDDEELKETIRQALE 118
PRK11086 PRK11086
sensory histidine kinase DcuS; Provisional
303-415 2.16e-06

sensory histidine kinase DcuS; Provisional


Pssm-ID: 236839 [Multi-domain]  Cd Length: 542  Bit Score: 50.30  E-value: 2.16e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209301716 303 LINLALNARDAMPTGgrmTIETANCHLDGayvagiaepvepgqYVMVAVTDSGLGMDKSTQEKAFEPFFTTKavGQGTGL 382
Cdd:PRK11086  441 LIENALEAVGGEEGG---EISVSLHYRNG--------------WLHCEVSDDGPGIAPDEIDAIFDKGYSTK--GSNRGV 501
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1209301716 383 GLSqvygFVRQS----SGHIRIYSELGEGSTVKIYLP 415
Cdd:PRK11086  502 GLY----LVKQSvenlGGSIAVESEPGVGTQFFVQIP 534
REC_OmpR_EcPhoP-like cd19934
phosphoacceptor receiver (REC) domain of EcPhoP-like OmpR family response regulators; ...
441-556 2.18e-06

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: 46.89  E-value: 2.18e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209301716 441 ILVVEDDASLRGYTVQILTELGYGVLEAADGRIGLkVLAERGDIDLLFTDIVMPgGLNGRELADEAVKLHPALKVLFTTG 520
Cdd:cd19934     1 LLLVEDDALLAAQLKEQLSDAGYVVDVAEDGEEAL-FQGEEEPYDLVVLDLGLP-GMDGLSVLRRWRSEGRATPVLILTA 78
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1209301716 521 YTRNAIVHHGrLDPGV-HFLGKPFSFDELALKIRSVL 556
Cdd:cd19934    79 RDSWQDKVEG-LDAGAdDYLTKPFHIEELLARLRALI 114
REC_OmpR_ArcA_TorR-like cd17619
phosphoacceptor receiver (REC) domain of ArcA- and TorR-like OmpR family response regulators; ...
441-520 2.21e-06

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: 46.61  E-value: 2.21e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209301716 441 ILVVEDDASLRGYTVQILTELGYGVLEAADGRIGLKVLAeRGDIDLLFTDIVMPgGLNGRELADEaVKLHPALKVLFTTG 520
Cdd:cd17619     3 ILIVEDEPVTRATLKSYFEQEGYDVSEAGDGEEMRQILA-RQDIDLVLLDINLP-GKDGLSLTRE-LREQSEVGIILVTG 79
HATPase_BceS-YxdK-YvcQ-like cd16948
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
344-415 2.23e-06

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Bacillus subtilis BceS, YxdK, and Bacillus thuringiensis YvcQ; This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component sensor histidine kinase (HKs) such as Bacillus subtilis BceS and Bacillus thuringiensis YvcQ, the HKs of the two-component regulatory system (TCSs) BceS-BceR and YvcQ-YvcP, repsectively, which are both involved in regulating bacitracin resistance. It also includes the HATPase domain of YxdK, the HK of YxdK-YxdJ TCS involved in sensing antimicrobial compounds.


Pssm-ID: 340424 [Multi-domain]  Cd Length: 109  Bit Score: 46.51  E-value: 2.23e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1209301716 344 GQYVMVAVTDSGLGMDKSTQEKAFEPFFTTK---AVGQGTGLGLsqvYgFVRQSS---GH-IRIYSELGEGSTVKIYLP 415
Cdd:cd16948    35 EQGVVLSIKDFGIGIPEEDLPRVFDKGFTGEngrNFQESTGMGL---Y-LVKKLCdklGHkIDVESEVGEGTTFTITFP 109
REC_D1_PleD-like cd17538
first (D1) phosphoacceptor receiver (REC) domain of response regulator PleD and similar ...
441-501 2.40e-06

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: 46.34  E-value: 2.40e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1209301716 441 ILVVEDDASLRGYTVQILTELGYGVLEAADGRIGLKvLAERGDIDLLFTDIVMPgGLNGRE 501
Cdd:cd17538     2 ILVVDDEPANRELLEALLSAEGYEVLTADSGQEALA-LAEEELPDLILLDVMMP-GMDGFE 60
REC_DctD-like cd17549
phosphoacceptor receiver (REC) domain of C4-dicarboxylic acid transport protein D (DctD) and ...
441-548 2.55e-06

phosphoacceptor receiver (REC) domain of C4-dicarboxylic acid transport protein D (DctD) and similar proteins; C4-dicarboxylic acid transport protein D (DctD) is part of the two-component regulatory system DctB/DctD, which regulates C4-dicarboxylate transport via regulation of expression of the dctPQM operon and dctA. It is an activator of sigma(54)-RNA polymerase holoenzyme that uses the energy released from ATP hydrolysis to stimulate the isomerization of a closed promoter complex to an open complex capable of initiating transcription. DctD is a member of the NtrC family, characterized by a domain architecture containing an N-terminal REC domain, followed by a central sigma-54 interaction/ATPase domain, and a C-terminal DNA binding domain. The ability of the central domain to hydrolyze ATP and thus to interact effectively with a complex of RNA polymerase, sigma54, and promoter, is controlled by the phosphorylation status of the REC domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381101 [Multi-domain]  Cd Length: 130  Bit Score: 46.71  E-value: 2.55e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209301716 441 ILVVEDDASLRGYTVQILTELGYGVLEAADGRIGLKVLAERGDiDLLFTDIVMPgGLNGRELADEAVKLHPALKVLFTTG 520
Cdd:cd17549     1 VLLVDDDADVREALQQTLELAGFRVRAFADAEEALAALSPDFP-GVVISDIRMP-GMDGLELLAQIRELDPDLPVILITG 78
                          90       100       110
                  ....*....|....*....|....*....|...
gi 1209301716 521 Y-----TRNAIvHHGRLDpgvhFLGKPFSFDEL 548
Cdd:cd17549    79 HgdvpmAVEAM-RAGAYD----FLEKPFDPERL 106
REC_2_DhkD-like cd17580
second phosphoacceptor receiver (REC) domain of Dictyostelium discoideum hybrid signal ...
441-548 2.66e-06

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


Pssm-ID: 381118 [Multi-domain]  Cd Length: 112  Bit Score: 46.30  E-value: 2.66e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209301716 441 ILVVEDDASLRGYTVQILTELGYGVLEAADGRIGLKVLAERgDIDLLFTDIVMPgGLNGRELAdEAVKLHPALK---VLF 517
Cdd:cd17580     1 ILVVDDNEDAAEMLALLLELEGAEVTTAHSGEEALEAAQRF-RPDVILSDIGMP-GMDGYELA-RRLRELPWLAntpAIA 77
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1209301716 518 TTGYT----RNAIVHHGrLDpgvHFLGKPFSFDEL 548
Cdd:cd17580    78 LTGYGqpedRERALEAG-FD---AHLVKPVDPDEL 108
PRK11361 PRK11361
acetoacetate metabolism transcriptional regulator AtoC;
441-556 2.91e-06

acetoacetate metabolism transcriptional regulator AtoC;


Pssm-ID: 183099 [Multi-domain]  Cd Length: 457  Bit Score: 49.85  E-value: 2.91e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209301716 441 ILVVEDDASLRGYTVQILTELGYGVLEAADGRIGLKVLAE-RGDIDLLftDIVMPgGLNGRELADEAVKLHPALKVLFTT 519
Cdd:PRK11361    7 ILIVDDEDNVRRMLSTAFALQGFETHCANNGRTALHLFADiHPDVVLM--DIRMP-EMDGIKALKEMRSHETRTPVILMT 83
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1209301716 520 GYTRNAIVHHGRLDPGVHFLGKPFSFDELALKIRSVL 556
Cdd:PRK11361   84 AYAEVETAVEALRCGAFDYVIKPFDLDELNLIVQRAL 120
REC_DesR-like cd19930
phosphoacceptor receiver (REC) domain of DesR and similar proteins; This group is composed of ...
441-557 3.56e-06

phosphoacceptor receiver (REC) domain of DesR and similar proteins; This group is composed of Bacillus subtilis DesR, Streptococcus pneumoniae response regulator spr1814, and similar proteins, all containing an N-terminal REC domain and a C-terminal LuxR family helix-turn-helix (HTH) DNA-binding output domain. DesR is a response regulator that, together with its cognate sensor kinase DesK, comprises a two-component regulatory system that controls membrane fluidity. Phosphorylation of the REC domain of DesR is allosterically coupled to two distinct exposed surfaces of the protein, controlling noncanonical dimerization/tetramerization, cooperative activation, and DesK binding. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381157 [Multi-domain]  Cd Length: 117  Bit Score: 46.11  E-value: 3.56e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209301716 441 ILVVEDDASLRGYTVQILTELGYG--VLEAADGRIGLKvLAERGDIDLLFTDIVMPGgLNGRELADEAVKLHPALKVLFT 518
Cdd:cd19930     1 VLIAEDQEMVRGALAALLELEDDLevVAQASNGQEALR-LVLKHSPDVAILDIEMPG-RTGLEVAAELREELPDTKVLIV 78
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1209301716 519 T-----GYTRNAivhhgrLDPGVH-FLGKPFSFDELALKIRSVLD 557
Cdd:cd19930    79 TtfgrpGYFRRA------LAAGVDgYVLKDRPIEELADAIRTVHA 117
PRK11173 PRK11173
two-component response regulator; Provisional
441-556 6.30e-06

two-component response regulator; Provisional


Pssm-ID: 183013 [Multi-domain]  Cd Length: 237  Bit Score: 47.70  E-value: 6.30e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209301716 441 ILVVEDDASLRGYTVQILTELGYGVLEAADGRIGLKVLAERgDIDLLFTDIVMPGGlNGRELADEaVKLHPALKVLFTTG 520
Cdd:PRK11173    6 ILIVEDELVTRNTLKSIFEAEGYDVFEATDGAEMHQILSEN-DINLVIMDINLPGK-NGLLLARE-LREQANVALMFLTG 82
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1209301716 521 ytRNAIVHH--GrLDPGV-HFLGKPFSFDELALKIRSVL 556
Cdd:PRK11173   83 --RDNEVDKilG-LEIGAdDYITKPFNPRELTIRARNLL 118
YesM COG2972
Sensor histidine kinase YesM [Signal transduction mechanisms];
344-416 6.56e-06

Sensor histidine kinase YesM [Signal transduction mechanisms];


Pssm-ID: 442211 [Multi-domain]  Cd Length: 445  Bit Score: 48.86  E-value: 6.56e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209301716 344 GQYVMVAVTDSGLGMDKSTQEKAFEPFFTTkavGQGTGLGLSQV-------YGfvrqSSGHIRIYSELGEGSTVKIYLPR 416
Cdd:COG2972   370 GDRLVITVEDNGVGMPEEKLEKLLEELSSK---GEGRGIGLRNVrerlklyYG----EEYGLEIESEPGEGTTVTIRIPL 442
REC_OmpR_PmrA-like cd17624
phosphoacceptor receiver (REC) domain of PmrA-like OmpR family response regulators; This ...
441-556 7.02e-06

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


Pssm-ID: 381139 [Multi-domain]  Cd Length: 115  Bit Score: 45.17  E-value: 7.02e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209301716 441 ILVVEDDASLRGYTVQILTELGYGVLEAADGRIGLKVLAErGDIDLLFTDIVMPGGlNGRELADEAVKLHPALKVLFTTG 520
Cdd:cd17624     1 ILLVEDDALLGDGLKTGLRKAGYAVDWVRTGAEAEAALAS-GPYDLVILDLGLPDG-DGLDLLRRWRRQGQSLPVLILTA 78
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1209301716 521 YTRNAIVHHGrLDPGVH-FLGKPFSFDELALKIRSVL 556
Cdd:cd17624    79 RDGVDDRVAG-LDAGADdYLVKPFALEELLARLRALL 114
REC_RpfG-like cd17551
phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase response regulator ...
441-553 9.09e-06

phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase response regulator RpfG and similar proteins; Cyclic di-GMP phosphodiesterase response regulator RpfG, together with sensory/regulatory protein RpfC, constitute a two-component system implicated in sensing and responding to the diffusible signal factor (DSF) that is essential for cell-cell signaling. RpfC is a hybrid sensor/histidine kinase that phosphorylates and activates RpfG, which degrades cyclic di-GMP to GMP, leading to the activation of Clp, a global transcriptional regulator that regulates a large set of genes in the DSF pathway. RpfG contains a CheY-like receiver domain attached to a histidine-aspartic acid-glycine-tyrosine-proline (HD-GYP) cyclic di-GMP phosphodiesterase domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381103 [Multi-domain]  Cd Length: 118  Bit Score: 45.13  E-value: 9.09e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209301716 441 ILVVEDDASLRGYTVQILTELGYG-VLEAADGRIGLkVLAERGDIDLLFTDIVMPgGLNGRELAdEAVKLHPALK---VL 516
Cdd:cd17551     3 ILIVDDNPTNLLLLEALLRSAGYLeVVSFTDPREAL-AWCRENPPDLILLDYMMP-GMDGLEFI-RRLRALPGLEdvpIV 79
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1209301716 517 FTTGYTRNAIVHHGrLDPGVH-FLGKPFSFDELALKIR 553
Cdd:cd17551    80 MITADTDREVRLRA-LEAGATdFLTKPFDPVELLARVR 116
REC_DivK-like cd17548
phosphoacceptor receiver (REC) domain of DivK and similar proteins; Caulobacter crescentus ...
441-514 9.95e-06

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


Pssm-ID: 381100 [Multi-domain]  Cd Length: 115  Bit Score: 44.84  E-value: 9.95e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1209301716 441 ILVVEDDASLRGYTVQILTELGYGVLEAADGRIGLKvLAERGDIDLLFTDIVMPgGLNGRELAdEAVKLHPALK 514
Cdd:cd17548     2 ILIVEDNPLNMKLARDLLESAGYEVLEAADGEEALE-IARKEKPDLILMDIQLP-GMDGLEAT-RLLKEDPATR 72
REC_OmpR_PhoB cd17618
phosphoacceptor receiver (REC) domain of PhoB response regulator from the OmpR family; The ...
441-556 1.27e-05

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: 44.55  E-value: 1.27e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209301716 441 ILVVEDDASLRGYTVQILTELGYGVLEAADGRIGLKVLAERGDiDLLFTDIVMPGGlNGRELA-----DEAVKLHPALkV 515
Cdd:cd17618     3 ILIVEDEPAIREMIAFNLERAGFDVVEAEDAESAVNLIVEPRP-DLILLDWMLPGG-SGIQFIrrlkrDEMTRDIPII-M 79
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1209301716 516 LFTTGYTRNAIvhHGrLDPGV-HFLGKPFSFDELALKIRSVL 556
Cdd:cd17618    80 LTARGEEEDKV--RG-LEAGAdDYITKPFSPRELVARIKAVL 118
PRK09836 PRK09836
DNA-binding transcriptional activator CusR; Provisional
441-556 1.29e-05

DNA-binding transcriptional activator CusR; Provisional


Pssm-ID: 182102 [Multi-domain]  Cd Length: 227  Bit Score: 46.46  E-value: 1.29e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209301716 441 ILVVEDDASLRGYTVQILTELGYGVLEAADGRIGLKvLAERGDIDLLFTDIVMPGgLNGRELADEAVKLHPALKVLFTTG 520
Cdd:PRK09836    3 LLIVEDEKKTGEYLTKGLTEAGFVVDLADNGLNGYH-LAMTGDYDLIILDIMLPD-VNGWDIVRMLRSANKGMPILLLTA 80
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1209301716 521 YtrNAIVHHGR-LDPGVH-FLGKPFSFDELALKIRSVL 556
Cdd:PRK09836   81 L--GTIEHRVKgLELGADdYLVKPFAFAELLARVRTLL 116
REC_TPR cd17589
phosphoacceptor receiver (REC) domain of uncharacterized tetratricopeptide repeat (TPR) ...
441-552 1.51e-05

phosphoacceptor receiver (REC) domain of uncharacterized tetratricopeptide repeat (TPR)-containing response regulators; Response regulators share the common phosphoacceptor REC domain and different output domains. This subfamily contains uncharacterized response regulators with TPR repeats as the effector or output domain, which might contain between 3 to 16 TPR repeats (each about 34 amino acids). TPR-containing proteins occur in all domains of life and the abundance of TPR-containing proteins in a bacterial proteome is not indicative of virulence. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays. Some members in this subfamily may contain inactive REC domains lacking canonical metal-binding and active site residues.


Pssm-ID: 381123 [Multi-domain]  Cd Length: 115  Bit Score: 44.17  E-value: 1.51e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209301716 441 ILVVEDDASLRGYTVQILTELGYGVLE-AADGRIGLKvLAERGDIDLLFTDIVMPGGLNGRELADEaVKLHPALK----V 515
Cdd:cd17589     1 FLIVDDQPTFRSMLKSMLRSLGVTRIDtASSGEEALR-MCENKTYDIVLCDYNLGKGKNGQQLLEE-LRHKKLISpstvF 78
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1209301716 516 LFTTGYTRNAIVHHG-RLDPGvHFLGKPFSFDELALKI 552
Cdd:cd17589    79 IMVTGESSRAMVLSAlELEPD-DYLLKPFTVSELRERL 115
PRK10955 PRK10955
envelope stress response regulator transcription factor CpxR;
441-556 1.58e-05

envelope stress response regulator transcription factor CpxR;


Pssm-ID: 182864 [Multi-domain]  Cd Length: 232  Bit Score: 46.33  E-value: 1.58e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209301716 441 ILVVEDDASLRGYTVQILTELGYGVLEAADGRIGLKVLAErgDIDLLFTDIVMPGGlNGRELADEAVKLHPALKVLFTT- 519
Cdd:PRK10955    4 ILLVDDDRELTSLLKELLEMEGFNVIVAHDGEQALDLLDD--SIDLLLLDVMMPKK-NGIDTLKELRQTHQTPVIMLTAr 80
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1209301716 520 GYTRNAIVHhgrLDPGV-HFLGKPFSFDELALKIRSVL 556
Cdd:PRK10955   81 GSELDRVLG---LELGAdDYLPKPFNDRELVARIRAIL 115
psREC_PRR cd17582
pseudo receiver domain of pseudo-response regulators; In Arabidopsis, five pseudo-response ...
441-495 2.35e-05

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: 43.54  E-value: 2.35e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1209301716 441 ILVVEDDASLRGYTVQILTELGYGVLEAADGRIGLKVL-AERGDIDLLFTDIVMPG 495
Cdd:cd17582     1 VLLVENDDSTRQIVTALLRKCSYEVTAASDGLQAWDVLeDEQNEIDLILTEVDLPV 56
PRK10841 PRK10841
two-component system sensor histidine kinase RcsC;
386-548 2.47e-05

two-component system sensor histidine kinase RcsC;


Pssm-ID: 182772 [Multi-domain]  Cd Length: 924  Bit Score: 47.28  E-value: 2.47e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209301716 386 QVYGFVRQSSGHIRIYSELGEG----STV----------KIYLPRYAgAEEAAPFVPPELTARAGGSE-LILVVEDDASL 450
Cdd:PRK10841  735 QGRAVITFCRRHIGIPLEIAPGewvhSTAtphelpallaRIYRIELE-SDDSANALPSTDKAVSDNDDmMILVVDDHPIN 813
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209301716 451 RGYTVQILTELGYGVLEAADGRIGLKVLAeRGDIDLLFTDIVMPgGLNGRELADEAVKLHPALKVLfttGYTRNAIVHHG 530
Cdd:PRK10841  814 RRLLADQLGSLGYQCKTANDGVDALNVLS-KNHIDIVLTDVNMP-NMDGYRLTQRLRQLGLTLPVI---GVTANALAEEK 888
                         170       180
                  ....*....|....*....|.
gi 1209301716 531 R--LDPGV-HFLGKPFSFDEL 548
Cdd:PRK10841  889 QrcLEAGMdSCLSKPVTLDVL 909
AmiR COG3707
Two-component response regulator, AmiR/NasT family, consists of REC and RNA-binding ...
441-544 3.26e-05

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: 44.95  E-value: 3.26e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209301716 441 ILVVEDDASLRGYTVQILTELGYGVLEAADGRIGLKVLAERGDIDLLFTDIVMPgGLNGRELADEAVKLHPALKVLFTTG 520
Cdd:COG3707     6 VLVVDDEPLRRADLREGLREAGYEVVAEAADGEDAVELVRELKPDLVIVDIDMP-DRDGLEAARQISEERPAPVILLTAY 84
                          90       100
                  ....*....|....*....|....*
gi 1209301716 521 YTRNAIvhHGRLDPGVH-FLGKPFS 544
Cdd:COG3707    85 SDPELI--ERALEAGVSaYLVKPLD 107
PRK10766 PRK10766
two-component system response regulator TorR;
441-505 3.90e-05

two-component system response regulator TorR;


Pssm-ID: 182711 [Multi-domain]  Cd Length: 221  Bit Score: 45.03  E-value: 3.90e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1209301716 441 ILVVEDDASLRGYTVQILTELGYGVLEAADGRiGLKVLAERGDIDLLFTDIVMPgGLNGRELADE 505
Cdd:PRK10766    5 ILVVEDEPVTRARLQGYFEQEGYTVSEAASGA-GMREIMQNQHVDLILLDINLP-GEDGLMLTRE 67
HATPase_SpoIIAB-like cd16942
Histidine kinase-like ATPase domain of SpoIIAB, an anti sigma-F factor and serine-protein ...
330-410 3.92e-05

Histidine kinase-like ATPase domain of SpoIIAB, an anti sigma-F factor and serine-protein kinase involved in regulating sigma-F during sporulation in Bacilli, and related domains; This family includes histidine kinase-like ATPase (HATPase) domain of SpoIIAB, an anti sigma-F factor and a serine-protein kinase involved in regulating sigma-F during sporulation in Bacilli where, early in sporulation, the cell divides into two unequal compartments: a larger mother cell and a smaller forespore. Sigma-F transcription factor is activated in the forespore directly after the asymmetric septum forms, and its spatial and temporal activation is required for sporulation. Free sigma-F can associate with the RNA polymerase core and activate transcription of the sigma-F regulon, its regulation may comprise a partner-switching mechanism involving SpoIIAB, SpoIIAA, and sigma-F as follows: SpoIIAB can form alternative complexes with either: i) sigma-F, holding it in an inactive form and preventing its association with RNA polymerase, or ii) unphosphorylated SpoIIAA and a nucleotide, either ATP or ADP. In the presence of ATP, SpoIIAB acts as a kinase to specifically phosphorylate a serine residue of SpoIIAA; this phosphorylated form has low affinity for SpoIIAB and dissociates, making SpoIIAB available to capture sigma-F. SpoIIAA may then be dephosphorylated by a SpoIIE serine phosphatase and be free to attack the SpoIIAB sigma-F complex to induce the release of sigma-F.


Pssm-ID: 340418 [Multi-domain]  Cd Length: 135  Bit Score: 43.68  E-value: 3.92e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209301716 330 DGAYVAGIAEPVEPGQyVMVAVTDSGLGMDKStqEKAFEPFFTTKAVGQGTGLGLSQVYGFVRQssghIRIYSELGEGST 409
Cdd:cd16942    58 DPNGIVSISVIIEDGV-VHLTVRDEGVGIPDI--EEARQPLFTTKPELERSGMGFTIMENFMDE----VIVESEVNKGTT 130

                  .
gi 1209301716 410 V 410
Cdd:cd16942   131 V 131
PAS cd00130
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
41-131 4.74e-05

PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising identification of a PAS domain was that in EAG-like K+-channels. PAS domains have been found to bind ligands, and to act as sensors for light and oxygen in signal transduction.


Pssm-ID: 238075 [Multi-domain]  Cd Length: 103  Bit Score: 42.62  E-value: 4.74e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209301716  41 LLVSQQFLVIYGLDCFDGRHESWLACVFREDVARIVDQTENAFRRRDREMLmEFRILRPgDGGLVWIEARSIIFYDADGR 120
Cdd:cd00130    15 LYANPAAEQLLGYSPEELIGKSLLDLIHPEDREELRERLENLLSGGEPVTL-EVRLRRK-DGSVIWVLVSLTPIRDEGGE 92
                          90
                  ....*....|.
gi 1209301716 121 AIRMVGVNADI 131
Cdd:cd00130    93 VIGLLGVVRDI 103
REC_NtrC1-like cd17572
phosphoacceptor receiver (REC) domain of nitrogen regulatory protein C 1 (NtrC1) from Aquifex ...
441-557 4.81e-05

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: 42.96  E-value: 4.81e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209301716 441 ILVVEDDASLRGYTVQILTELGYGVLEAADGRIGLKVLAERgDIDLLFTDIVMPgGLNGRELADEAVKLHPALKVLFTTG 520
Cdd:cd17572     1 VLLVEDSPSLAALYQEYLSDEGYKVTHVETGKEALAFLSDQ-PPDVVLLDLKLP-DMSGMEILKWIQERSLPTSVIVITA 78
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1209301716 521 ytrnaivhHGRLDPGVH--------FLGKPFSFDELALKIRSVLD 557
Cdd:cd17572    79 --------HGSVDIAVEamrlgaydFLEKPFDADRLRVTVRNALK 115
PRK11107 PRK11107
hybrid sensory histidine kinase BarA; Provisional
347-409 5.86e-05

hybrid sensory histidine kinase BarA; Provisional


Pssm-ID: 236848 [Multi-domain]  Cd Length: 919  Bit Score: 46.00  E-value: 5.86e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1209301716 347 VMVAVTDSGLGMDKSTQEKAFEPFfttkavGQ----------GTGLGLSQVYGFVRQSSGHIRIYSELGEGST 409
Cdd:PRK11107  445 LEVQIRDTGIGISERQQSQLFQAF------RQadasisrrhgGTGLGLVITQKLVNEMGGDISFHSQPNRGST 511
REC_OmpR_MtPhoP-like cd17615
phosphoacceptor receiver (REC) domain of MtPhoP-like OmpR family response regulators; ...
441-556 6.11e-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: 42.72  E-value: 6.11e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209301716 441 ILVVEDDASLRGYTVQILTELGYGVLEAADGRIGLKVlAERGDIDLLFTDIVMPGgLNGRELADEAVKLHPALKVLFTTG 520
Cdd:cd17615     2 VLVVDDEPNITELLSMALRYEGWDVETAADGAEALAA-AREFRPDAVVLDIMLPD-MDGLEVLRRLRADGPDVPVLFLTA 79
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1209301716 521 ytRNAIVH--HGRLDPGVHFLGKPFSFDELALKIRSVL 556
Cdd:cd17615    80 --KDSVEDriAGLTAGGDDYVTKPFSLEEVVARLRALL 115
REC_OmpR_CpxR cd17623
phosphoacceptor receiver (REC) domain of CpxR-like OmpR family response regulators; CpxR is ...
441-556 6.29e-05

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


Pssm-ID: 381138 [Multi-domain]  Cd Length: 115  Bit Score: 42.68  E-value: 6.29e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209301716 441 ILVVEDDASLRGYTVQILTELGYGVLEAADGRIGLKVLAErGDIDLLFTDIVMPgGLNGRELADEaVKLHPALKVLFTT- 519
Cdd:cd17623     1 ILLIDDDRELTELLTEYLEMEGFNVRAAHDGEQGLAALLE-GSPDLVVLDVMLP-KMNGLDVLKE-LRKTSQVPVLMLTa 77
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1209301716 520 -GYTRNAIVHhgrLDPGV-HFLGKPFSFDELALKIRSVL 556
Cdd:cd17623    78 rGDDIDRILG---LELGAdDYLPKPFNPRELVARIRAIL 113
REC_citrate_TCS cd19925
phosphoacceptor receiver (REC) domain of citrate family two-component system response ...
441-548 6.78e-05

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: 42.62  E-value: 6.78e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209301716 441 ILVVEDDASLRGYTVQILTELGY--GVLEAADGRIGLKVLAERgDIDLLFTDIVMPGGlNGRELADEAVKLHPALKVLFT 518
Cdd:cd19925     3 VLIVEDDPMVAEIHRAYVEQVPGftVIGTAGTGEEALKLLKER-QPDLILLDIYLPDG-NGLDLLRELRAAGHDVDVIVV 80
                          90       100       110
                  ....*....|....*....|....*....|....
gi 1209301716 519 TGY----TRNAIVHHGRLDpgvhFLGKPFSFDEL 548
Cdd:cd19925    81 TAAndveTVREALRLGVVD----YLIKPFTFERL 110
HATPase_BasS-like cd16940
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
292-414 6.83e-05

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Escherichia coli BasS; This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component sensor histidine kinase (HKs) similar to Escherichia coli BasS HK of the BasS-BasR two-component regulatory system (TCS). Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA); some contain a HAMP sensory domain, while some an N-terminal two-component sensor kinase domain.


Pssm-ID: 340417 [Multi-domain]  Cd Length: 113  Bit Score: 42.39  E-value: 6.83e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209301716 292 VHADANQLENSLINLALNARDAMPTGGRMTIEtanchldgayvagiaepVEPGQYVMVAVTDSGLGMDKSTQEKAFEPFF 371
Cdd:cd16940     7 VQGDALLLFLLLRNLVDNAVRYSPQGSRVEIK-----------------LSADDGAVIRVEDNGPGIDEEELEALFERFY 69
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1209301716 372 -TTKAVGQGTGLGLSQVYGFVRQSSGHIRIYSELGEGSTVKIYL 414
Cdd:cd16940    70 rSDGQNYGGSGLGLSIVKRIVELHGGQIFLGNAQGGGLEAWVRL 113
envZ PRK09467
osmolarity sensor protein; Provisional
259-415 7.03e-05

osmolarity sensor protein; Provisional


Pssm-ID: 236531 [Multi-domain]  Cd Length: 435  Bit Score: 45.29  E-value: 7.03e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209301716 259 DANKLIastGELLHRTLGEQIALETVLAAGLWRVHADANQLENSLINLALNArdAMPTGGRMTIETancHLDGayvagia 338
Cdd:PRK09467  295 DLNALL---GEVIAAESGYEREIETALQPGPIEVPMNPIAIKRALANLVVNA--ARYGNGWIKVSS---GTEG------- 359
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209301716 339 epvepgQYVMVAVTDSGLGMDKSTQEKAFEPFftT---KAVG-QGTGLGLSQVYGFVRQSSGHIRI-YSELGeGSTVKIY 413
Cdd:PRK09467  360 ------KRAWFQVEDDGPGIPPEQLKHLFQPF--TrgdSARGsSGTGLGLAIVKRIVDQHNGKVELgNSEEG-GLSARAW 430

                  ..
gi 1209301716 414 LP 415
Cdd:PRK09467  431 LP 432
REC_OmpR_PrrA-like cd17627
phosphoacceptor receiver (REC) domain of PrrA-like OmpR family response regulators; The ...
441-556 7.45e-05

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: 42.37  E-value: 7.45e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209301716 441 ILVVEDDASLRGYTVQILTELGYGVLEAADGRIGLKVLAERgDIDLLFTDIVMPGgLNGRELADEAVKLHPALKVLFTTG 520
Cdd:cd17627     1 ILVVDDDRAVRESLRRSLRFEGYEVETAVDGAEALRVISGN-RPDAVVLDVMMPR-LDGLEVCRRLRAAGNDLPILVLTA 78
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1209301716 521 ytRNAIVHHGR-LDPGVH-FLGKPFSFDELALKIRSVL 556
Cdd:cd17627    79 --RDSVSDRVAgLDAGADdYLVKPFALEELLARVRALL 114
REC_Ycf29 cd19927
phosphoacceptor receiver (REC) domain of probable transcriptional regulator Ycf29; Ycf29 is a ...
441-502 8.34e-05

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: 41.98  E-value: 8.34e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1209301716 441 ILVVEDDASLRGYTVQILTELGYGVLEAADGRIGLKvLAERGDIDLLFTDIVMPGGlNGREL 502
Cdd:cd19927     1 ILLVDDDPGIRLAVKDYLEDQGFTVIAASNGLEALD-LLNQYIPDLIISDIIMPGV-DGYSL 60
ompR PRK09468
osmolarity response regulator; Provisional
441-556 9.21e-05

osmolarity response regulator; Provisional


Pssm-ID: 181883 [Multi-domain]  Cd Length: 239  Bit Score: 44.19  E-value: 9.21e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209301716 441 ILVVEDDASLRGYTVQILTELGYGVLEAADGRiGLKVLAERGDIDLLFTDIVMPG--GLN-GRELADEAVKLhPALkVLF 517
Cdd:PRK09468    8 ILVVDDDMRLRALLERYLTEQGFQVRSAANAE-QMDRLLTRESFHLMVLDLMLPGedGLSiCRRLRSQNNPT-PII-MLT 84
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1209301716 518 TTGYTRNAIVHhgrLDPGV-HFLGKPFSFDELALKIRSVL 556
Cdd:PRK09468   85 AKGEEVDRIVG---LEIGAdDYLPKPFNPRELLARIRAVL 121
HATPase_CreC-like cd16945
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
295-400 1.06e-04

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Escherichia coli CreC; This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component sensor histidine kinase (HKs) such as Escherichia coli CreC of the CreC-CreB two-component regulatory system (TCS) involved in catabolic regulation. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA), and accessory sensory domain(s) such as HAMP, CACHE or PAS.


Pssm-ID: 340421 [Multi-domain]  Cd Length: 106  Bit Score: 41.68  E-value: 1.06e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209301716 295 DANQLENSLINLALNARDAMPTGGRMTIETancHLDGAYVAgiaepvepgqyvmVAVTDSGLGMDKSTQEKAFEPFFT-- 372
Cdd:cd16945     1 DPFLLRQAINNLLDNAIDFSPEGGLIALQL---EADTEGIE-------------LLVFDEGSGIPDYALNRVFERFYSlp 64
                          90       100
                  ....*....|....*....|....*....
gi 1209301716 373 TKAVGQ-GTGLGLSQVYGFVRQSSGHIRI 400
Cdd:cd16945    65 RPHSGQkSTGLGLAFVQEVAQLHGGRITL 93
REC_OmpR_BsPhoP-like cd19937
phosphoacceptor receiver (REC) domain of BsPhoP-like OmpR family response regulators; Bacillus ...
442-556 1.15e-04

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: 41.88  E-value: 1.15e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209301716 442 LVVEDDASLRGYTVQILTELGYGVLEAADGRIGLKvLAERGDIDLLFTDIVMPgGLNGREL-----ADEAVKLHPalkVL 516
Cdd:cd19937     1 LVVDDEEDIVELLKYNLEKEGYEVVTAYDGEEALK-RAKDEKPDLIILDLMLP-GIDGLEVcrilrSDPKTSSIP---II 75
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1209301716 517 FTT--GYTRNAIVHhgrLDPGV-HFLGKPFSFDELALKIRSVL 556
Cdd:cd19937    76 MLTakGEEFDKVLG---LELGAdDYITKPFSPRELLARVKAVL 115
glnG PRK10923
nitrogen regulation protein NR(I); Provisional
440-555 1.21e-04

nitrogen regulation protein NR(I); Provisional


Pssm-ID: 182842 [Multi-domain]  Cd Length: 469  Bit Score: 44.86  E-value: 1.21e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209301716 440 LILVVEDDASLRGYTVQILTELGYGVLEAADGRIGLKVLAERGDiDLLFTDIVMPgGLNGRELADEAVKLHPALKVLFTT 519
Cdd:PRK10923    5 IVWVVDDDSSIRWVLERALAGAGLTCTTFENGNEVLEALASKTP-DVLLSDIRMP-GMDGLALLKQIKQRHPMLPVIIMT 82
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1209301716 520 GYTR-NAIV---HHGRLDpgvhFLGKPFSFDE-LALKIRSV 555
Cdd:PRK10923   83 AHSDlDAAVsayQQGAFD----YLPKPFDIDEaVALVERAI 119
PRK10365 PRK10365
sigma-54-dependent response regulator transcription factor ZraR;
441-548 1.66e-04

sigma-54-dependent response regulator transcription factor ZraR;


Pssm-ID: 182412 [Multi-domain]  Cd Length: 441  Bit Score: 44.25  E-value: 1.66e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209301716 441 ILVVEDDASLRGYTVQILTELGYGVLEAADGRIGLKVLAERgDIDLLFTDIVMpGGLNGRELADEAVKLHPALKVLFTTG 520
Cdd:PRK10365    8 ILVVDDDISHCTILQALLRGWGYNVALANSGRQALEQVREQ-VFDLVLCDVRM-AEMDGIATLKEIKALNPAIPVLIMTA 85
                          90       100       110
                  ....*....|....*....|....*....|..
gi 1209301716 521 Y----TRNAIVHHGRLDpgvhFLGKPFSFDEL 548
Cdd:PRK10365   86 YssveTAVEALKTGALD----YLIKPLDFDNL 113
REC_LytTR_AlgR-like cd17532
phosphoacceptor receiver (REC) domain of LytTR/AlgR family response regulators similar to AlgR; ...
441-549 1.92e-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: 1.92e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209301716 441 ILVVEDDASLRGYTVQILTELGYGVL--EAADGRIGLKVLaERGDIDLLFTDIVMPgGLNGRELADEAVKLHPALKVLFT 518
Cdd:cd17532     1 ALIVDDEPLAREELRYLLEEHPDIEIvgEAENGEEALEAI-EELKPDVVFLDIQMP-GLDGLELAKKLSKLAKPPLIVFV 78
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1209301716 519 TGYTRNAI----VHhgrldpGVHFLGKPFSFDELA 549
Cdd:cd17532    79 TAYDEYAVeafeLN------AVDYLLKPFSEERLA 107
cpxA PRK09470
envelope stress sensor histidine kinase CpxA;
214-415 1.93e-04

envelope stress sensor histidine kinase CpxA;


Pssm-ID: 236532 [Multi-domain]  Cd Length: 461  Bit Score: 44.15  E-value: 1.93e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209301716 214 LGPSPEAERIakarDMAvegARRSATLTSRLLAFSRRQ---PLDPRPLDANKLIAstgELLHRTLGE----QIALETVLA 286
Cdd:PRK09470  272 QGESKELERI----ETE---AQRLDSMINDLLVLSRNQqknHLERETFKANSLWS---EVLEDAKFEaeqmGKSLTVSAP 341
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209301716 287 AGLWRVHADANQLENSLINLALNArdamptggrmtIETANCHLDGAYVAgiaepvePGQYVMVAVTDSGLGMDKSTQEKA 366
Cdd:PRK09470  342 PGPWPINGNPNALASALENIVRNA-----------LRYSHTKIEVAFSV-------DKDGLTITVDDDGPGVPEEEREQI 403
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1209301716 367 FEPFFTT-----KAVGqGTGLGLSQVYGFVRQSSGHIRIY-SELGeGSTVKIYLP 415
Cdd:PRK09470  404 FRPFYRVdeardRESG-GTGLGLAIVENAIQQHRGWVKAEdSPLG-GLRLTIWLP 456
REC_RR468-like cd17552
phosphoacceptor receiver (REC) domain of Thermotoga maritima response regulator RR468 and ...
441-557 2.45e-04

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: 41.00  E-value: 2.45e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209301716 441 ILVVEDDASLRgYTVQILTEL--GYGVLEAADGRIGLKVL-AERGDIDLLftDIVMPgGLNGRELAdEAVKLHPALK--- 514
Cdd:cd17552     4 ILVIDDEEDIR-EVVQACLEKlaGWEVLTASSGQEGLEKAaTEQPDAILL--DVMMP-DMDGLATL-KKLQANPETQsip 78
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1209301716 515 VLFTTGYTRNAivHHGRLdpgvHFLG------KPFSFDELALKIRSVLD 557
Cdd:cd17552    79 VILLTAKAQPS--DRQRF----ASLGvagviaKPFDPLTLAEQIAKLLG 121
REC_PA4781-like cd19920
phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase PA4781 and similar ...
441-543 5.79e-04

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


Pssm-ID: 381147 [Multi-domain]  Cd Length: 103  Bit Score: 39.42  E-value: 5.79e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209301716 441 ILVVEDDASLRGYTVQILTELGYGVLEAADGRIGLK-VLAERGDIDLLftDIVMPgGLNGREL-----ADEAVKLHPalk 514
Cdd:cd19920     1 ILIVDDVPDNLRLLSELLRAAGYRVLVATDGQQALQrAQAEPPDLILL--DVMMP-GMDGFEVcrrlkADPATRHIP--- 74
                          90       100       110
                  ....*....|....*....|....*....|...
gi 1209301716 515 VLFTTGYT----RNAIVHHGrldpGVHFLGKPF 543
Cdd:cd19920    75 VIFLTALTdtedKVKGFELG----AVDYITKPF 103
REC_NtrC cd19919
phosphoacceptor receiver (REC) domain of DNA-binding transcriptional regulator NtrC; ...
441-547 6.08e-04

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: 39.56  E-value: 6.08e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209301716 441 ILVVEDDASLRGYTVQILTELGYGVLEAADGRIGLKVLaERGDIDLLFTDIVMPgGLNGRELADEAVKLHPALKVLFTTG 520
Cdd:cd19919     3 VWIVDDDSSIRWVLERALAGAGLTVTSFENAQEALAAL-ASSQPDVLISDIRMP-GMDGLALLAQIKQRHPDLPVIIMTA 80
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1209301716 521 ytrnaivhHGRLDPGV--------HFLGKPFSFDE 547
Cdd:cd19919    81 --------HSDLDSAVsayqggafEYLPKPFDIDE 107
PRK15479 PRK15479
transcriptional regulator TctD;
441-556 9.70e-04

transcriptional regulator TctD;


Pssm-ID: 185376 [Multi-domain]  Cd Length: 221  Bit Score: 40.86  E-value: 9.70e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209301716 441 ILVVEDDASLRGYTVQILTELGYGVLEAADGRIGLKVLAERgDIDLLFTDIVMPGgLNGRELADEAVKLHPALKVLFTTG 520
Cdd:PRK15479    3 LLLAEDNRELAHWLEKALVQNGFAVDCVFDGLAADHLLQSE-MYALAVLDINMPG-MDGLEVLQRLRKRGQTLPVLLLTA 80
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1209301716 521 YTRNAIVHHGrLDPGVH-FLGKPFSFDELALKIRSVL 556
Cdd:PRK15479   81 RSAVADRVKG-LNVGADdYLPKPFELEELDARLRALL 116
REC_RocR cd17530
phosphoacceptor receiver (REC) domain of response regulator RocR; The response regulator RocR ...
441-548 1.24e-03

phosphoacceptor receiver (REC) domain of response regulator RocR; The response regulator RocR from some pathogens contains an N-terminal phosphoreceiver (REC) domain and a C-terminal EAL domain that possesses c-di-GMP specific phosphodiesterase activity. The RocR REC domain is phosphorylated and modulates its EAL domain enzymatic activity, regulating the local level of c-di-GMP. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381086 [Multi-domain]  Cd Length: 123  Bit Score: 38.96  E-value: 1.24e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209301716 441 ILVVEDDASLRGYTVQILTELGYG-VLEAADGRIGLKVLaERGDIDLLFTDIVMPgGLNGRELADEAVKLHPALKVLFTT 519
Cdd:cd17530     3 VLVLDDDPFQCMMAATILEDLGPGnVDEADDGREALVIL-LCNAPDIIICDLKMP-DMDGIEFLRHLAESHSNAAVILMS 80
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1209301716 520 GYTrNAIVHHGR---LDPGVHFLG---KPFSFDEL 548
Cdd:cd17530    81 GLD-GGILESAEtlaGANGLNLLGtlsKPFSPEEL 114
HATPase_YehU-like cd16956
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
344-415 1.47e-03

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Escherichia coli YehU; This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component sensor histidine kinase (HKs) including Escherichia coli YehU, a HK of the two-component system (TCS) YehU-YehT which is involved in a nutrient sensing regulatory network. Proteins having this HATPase domain also contain a histidine kinase domain (His-kinase); some have a GAF sensor domain while some have a cupin domain.


Pssm-ID: 340432 [Multi-domain]  Cd Length: 101  Bit Score: 38.19  E-value: 1.47e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1209301716 344 GQYVMVAVTDSGLGMDKSTQEKAFEPffttkavgQGTGLGLSQVYGFVRQSSGH---IRIYSELGEGSTVKIYLP 415
Cdd:cd16956    35 GQHLLLEVEDNGGGMDPDTLARILIR--------SSNGLGLNLVDKRLRQAFGNdygLDIECAPGEGTRITIRLP 101
PRK10549 PRK10549
two-component system sensor histidine kinase BaeS;
257-415 1.60e-03

two-component system sensor histidine kinase BaeS;


Pssm-ID: 182539 [Multi-domain]  Cd Length: 466  Bit Score: 41.16  E-value: 1.60e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209301716 257 PLDANKLI-ASTGELLHRTLGEQIALETVLAAGLwRVHADA---NQLENSLINLALNARDAmptGGRMTIETANCHldga 332
Cdd:PRK10549  311 PVDLVPLLeVAGGAFRERFASRGLTLQLSLPDSA-TVFGDPdrlMQLFNNLLENSLRYTDS---GGSLHISAEQRD---- 382
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209301716 333 yvagiaepvepgQYVMVAVTDSGLGMDKSTQEKAFEPFFTT-----KAVGqGTGLGLSQVYGFVRQSSGHIRI-YSELGe 406
Cdd:PRK10549  383 ------------KTLRLTFADSAPGVSDEQLQKLFERFYRTegsrnRASG-GSGLGLAICLNIVEAHNGRIIAaHSPFG- 448

                  ....*....
gi 1209301716 407 GSTVKIYLP 415
Cdd:PRK10549  449 GVSITVELP 457
HATPase_SpaK_NisK-like cd16975
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
295-412 1.62e-03

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Bacillus subtilis SpaK and Lactococcus lactis NisK; This family includes histidine kinase-like ATPase (HATPase) domain of two-component sensor histidine kinases similar to Bacillus subtilis SpaK and Lactococcus lactis NisK. SpaK is the histidine kinase (HK) of the SpaK-SpaR two-component regulatory system (TCS), which is involved in the regulation of the biosynthesis of lantibiotic subtilin. NisK is the HK of the NisK-NisR TCS, which is involved in the regulation of the biosynthesis of lantibiotic nisin. SpaK and NisK may function as membrane-associated protein kinases that phosphorylate SpaR and NisR, respectively, in response to environmental signals.


Pssm-ID: 340434 [Multi-domain]  Cd Length: 107  Bit Score: 38.21  E-value: 1.62e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209301716 295 DANQLENSLINLALNARDAMPTGGRMTIETANchldgayvagiaepvePGQYVMVAVTDSGLGMDKSTQEKAFEPFFTTK 374
Cdd:cd16975     1 DTLLLSRALINIISNACQYAPEGGTVSISIYD----------------EEEYLYFEIWDNGHGFSEQDLKKALELFYRDD 64
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1209301716 375 AV---GQGTGLGLSQVYGFVRQSSGHIRIYSELGEGSTVKI 412
Cdd:cd16975    65 TSrrsGGHYGMGLYIAKNLVEKHGGSLIIENSQKGGAEVTV 105
PRK13560 PRK13560
hypothetical protein; Provisional
65-143 1.82e-03

hypothetical protein; Provisional


Pssm-ID: 106506 [Multi-domain]  Cd Length: 807  Bit Score: 41.20  E-value: 1.82e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1209301716  65 ACVFREDVARIVDQTENAFRRRDREMLMEFRILRPGdGGLVWIEARSIIFYDADGRAIRMVGVNADITERKRAILQLRA 143
Cdd:PRK13560  523 AIIHPADLEQVAAEVAEFAAQGVDRFEQEYRILGKG-GAVCWIDDQSAAERDEEGQISHFEGIVIDISERKHAEEKIKA 600
HATPase_CpxA-like cd16949
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
341-415 2.26e-03

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Escherichia coli CpxA; This family includes the histidine kinase-like ATPase (HATPase) domains of two-component sensor histidine kinase (HKs) similar to Escherichia coli CpxA, HK of the CpxA-CpxR two-component regulatory system (TCS) which may function in acid stress and in cell wall stability. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA) and a HAMP sensor domain; some also contain a CpxA family periplasmic domain.


Pssm-ID: 340425 [Multi-domain]  Cd Length: 104  Bit Score: 37.69  E-value: 2.26e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1209301716 341 VEPGQYVMVaVTDSGLGMDKSTQEKAFEPFFTT----KAVGQGTGLGLSQVYGFVRQSSGHIRIYSELGEGSTVKIYLP 415
Cdd:cd16949    26 QDGDQWTIT-ITDDGPGVPEDQLEQIFLPFYRVdsarDRESGGTGLGLAIAERAIEQHGGKIKASNRKPGGLRVRIWLP 103
sensory_box TIGR00229
PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain ...
41-137 2.40e-03

PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain occupies the central portion of the PAS domain but is more widely distributed. It is often tandemly repeated. Known prosthetic groups bound in the S-box domain include heme in the oxygen sensor FixL, FAD in the redox potential sensor NifL, and a 4-hydroxycinnamyl chromophore in photoactive yellow protein. Proteins containing the domain often contain other regulatory domains such as response regulator or sensor histidine kinase domains. Other S-box proteins include phytochromes and the aryl hydrocarbon receptor nuclear translocator. [Regulatory functions, Small molecule interactions]


Pssm-ID: 272971 [Multi-domain]  Cd Length: 124  Bit Score: 38.04  E-value: 2.40e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209301716  41 LLVSQQFLVIYGLDCFDGRHESWLACVFREDVARIVDQTENAFRRRDREMLMEFRILRPgDGGLVWIEAR-SIIFydADG 119
Cdd:TIGR00229  26 LYVNPAFEEIFGYSAEELIGRNVLELIPEEDREEVRERIERRLEGEPEPVSEERRVRRK-DGSEIWVEVSvSPIR--TNG 102
                          90
                  ....*....|....*...
gi 1209301716 120 RAIRMVGVNADITERKRA 137
Cdd:TIGR00229 103 GELGVVGIVRDITERKEA 120
PRK10490 PRK10490
sensor protein KdpD; Provisional
131-415 3.78e-03

sensor protein KdpD; Provisional


Pssm-ID: 236701 [Multi-domain]  Cd Length: 895  Bit Score: 40.40  E-value: 3.78e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209301716 131 ITERKRAilqLRAFTETMEEAVrERTRELVAENEARRKAE-ELLRQAqkmevvgqLTGGVAHDFNNLLTIVLGGLDIIGR 209
Cdd:PRK10490  624 IPEQQRL---LETFTLLIANAL-ERLTLTASEEQARLASErEQLRNA--------LLAALSHDLRTPLTVLFGQAEILTL 691
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209301716 210 QLPALGpSPEAERIAKARDMAVEGARrsatLTSRLLAFSRRQP----LDPRPLDANKLIASTGELLHRTL-GEQIALEtv 284
Cdd:PRK10490  692 DLASEG-SPHARQASEIRQQVLNTTR----LVNNLLDMARIQSggfnLRKEWLTLEEVVGSALQMLEPGLsGHPINLS-- 764
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209301716 285 LAAGLWRVHADANQLENSLINLALNArdAMPTGGRMTIetanchldgayvaGIAEPVEpGQYVMVAVTDSGLGMDKSTQE 364
Cdd:PRK10490  765 LPEPLTLIHVDGPLFERVLINLLENA--VKYAGAQAEI-------------GIDAHVE-GERLQLDVWDNGPGIPPGQEQ 828
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1209301716 365 KAFEPFfttkAVGQ------GTGLGLSQVYGFVRQSSGHIRIYSELGEGSTVKIYLP 415
Cdd:PRK10490  829 LIFDKF----ARGNkesaipGVGLGLAICRAIVEVHGGTIWAENRPEGGACFRVTLP 881
PAS_4 pfam08448
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
35-136 4.16e-03

PAS fold; The PAS fold corresponds to the structural domain that has previously been defined as PAS and PAC motifs. The PAS fold appears in archaea, eubacteria and eukarya. This domain is associated to signalling systems and works as a signal sensor domain. It recognizes differently substituted aromatic hydrocarbons, oxygen, different dodecanoic acids, autoinducers, 3,5-dimethyl-pyrazin-2-ol and N-alanyl-aminoacetone (Matilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).


Pssm-ID: 312075 [Multi-domain]  Cd Length: 110  Bit Score: 37.01  E-value: 4.16e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209301716  35 HVPAGTLLVSQQFLVIY----GLDCFDGRHESWLACVFREdVARIVDQTEnaFRRRDREMLME-----FRILRPGDGGLV 105
Cdd:pfam08448   3 SLPDALAVLDPDGRVRYanaaAAELFGLPPEELLGKTLAE-LLPPEDAAR--LERALRRALEGeepidFLEELLLNGEER 79
                          90       100       110
                  ....*....|....*....|....*....|.
gi 1209301716 106 WIEARSIIFYDADGRAIRMVGVNADITERKR 136
Cdd:pfam08448  80 HYELRLTPLRDPDGEVIGVLVISRDITERRR 110
REC_RegA-like cd17563
phosphoacceptor receiver (REC) domain of photosynthetic apparatus regulatory protein RegA; ...
441-548 4.23e-03

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: 37.04  E-value: 4.23e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209301716 441 ILVVEDDASLRGYTVQILTELGYGVLEAADGRIGLKVLAERgDIDLLFTDIVMPGGlNGRELADEAVKLHPALKVLFTTG 520
Cdd:cd17563     3 LLLVDDDEVFAERLARALERRGFEVETAHSVEEALALAREE-KPDYAVLDLRLGGD-SGLDLIPPLRALQPDARIVVLTG 80
                          90       100       110
                  ....*....|....*....|....*....|..
gi 1209301716 521 Y----TRNAIVHHGrldpGVHFLGKPFSFDEL 548
Cdd:cd17563    81 YasiaTAVEAIKLG----ADDYLAKPADADEI 108
REC_OmpR_KdpE-like cd17620
phosphoacceptor receiver (REC) domain of KdpE-like OmpR family response regulators; KdpE is a ...
441-487 4.28e-03

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


Pssm-ID: 381135 [Multi-domain]  Cd Length: 99  Bit Score: 36.76  E-value: 4.28e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1209301716 441 ILVVEDDASLRGYTVQILTELGYGVLEAADGRIGLKVLAERG-DIDLL 487
Cdd:cd17620     1 ILVIEDEPQIRRFLRTALEAHGYRVFEAETGQEGLLEAATRKpDLIIL 48
REC_ETR-like cd19933
phosphoacceptor receiver (REC) domain of plant ethylene receptors ETR1, ETR2, and EIN4, and ...
441-511 4.53e-03

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


Pssm-ID: 381160 [Multi-domain]  Cd Length: 117  Bit Score: 37.38  E-value: 4.53e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1209301716 441 ILVVEDDASLRGYTVQILTELGYGVLEAADGRIGLKVLAERG-DIDLLFTDIVMPgGLNGRELADEAVKLHP 511
Cdd:cd19933     3 VLLVDDNAVNRMVTKGLLEKLGCEVTTVSSGEECLNLLASAEhSFQLVLLDLCMP-EMDGFEVALRIRKLFG 73
REC_FixJ cd17537
phosphoacceptor receiver (REC) domain of FixJ family response regulators; FixJ family response ...
439-556 4.65e-03

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: 37.19  E-value: 4.65e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209301716 439 ELILVVEDDASLRGYTVQILTELGYGVLEAADGRIGLKVlAERGDIDLLFTDIVMPgGLNGRELADEAVKLHPALKVLFT 518
Cdd:cd17537     1 ATVYVVDDDEAVRDSLAFLLRSVGLAVKTFTSASAFLAA-APPDQPGCLVLDVRMP-GMSGLELQDELLARGSNIPIIFI 78
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1209301716 519 TGytrnaivhHGRLDPGVH--------FLGKPFSFDELALKIRSVL 556
Cdd:cd17537    79 TG--------HGDVPMAVEamkagavdFLEKPFRDQVLLDAIEQAL 116
PRK10161 PRK10161
phosphate response regulator transcription factor PhoB;
441-556 5.00e-03

phosphate response regulator transcription factor PhoB;


Pssm-ID: 182277 [Multi-domain]  Cd Length: 229  Bit Score: 38.93  E-value: 5.00e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209301716 441 ILVVEDDASLRGYTVQILTELGYGVLEAADGRIGLKVLAERGDiDLLFTDIVMPGGlNG----RELADEAVKLHPALKVL 516
Cdd:PRK10161    5 ILVVEDEAPIREMVCFVLEQNGFQPVEAEDYDSAVNQLNEPWP-DLILLDWMLPGG-SGiqfiKHLKRESMTRDIPVVML 82
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1209301716 517 FTTGYTRNAIvhHGRLDPGVHFLGKPFSFDELALKIRSVL 556
Cdd:PRK10161   83 TARGEEEDRV--RGLETGADDYITKPFSPKELVARIKAVM 120
HATPase_CheA-like cd16916
Histidine kinase-like ATPase domain of the chemotaxis protein histidine kinase CheA, and some ...
344-415 5.78e-03

Histidine kinase-like ATPase domain of the chemotaxis protein histidine kinase CheA, and some hybrid sensor histidine kinases; This family includes the cytoplasmic histidine kinase (HK) CheA, a transmembrane receptor which, together with cytoplasmic adaptor protein (CheW), forms the lattice at the core of the chemosensory array that controls the cellular chemotaxis of motile bacteria and archaea. CheA forms a two-component signal transduction system (TCS) with the response regulator CheY. Proteins having this CheA-like HATPase domain generally also have a histidine-phosphotransfer domain, a histidine kinase homodimeric domain, and a regulatory domain; some are hybrid sensor histidine kinases as they contain a REC signal receiver domain.


Pssm-ID: 340393 [Multi-domain]  Cd Length: 178  Bit Score: 37.95  E-value: 5.78e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209301716 344 GQYVMVAVTDSGLGMDKST-QEKA-----------------------FEPFFTTKA-VGQ--GTGLGLSQVYGFVRQSSG 396
Cdd:cd16916    80 GNQVVIEVSDDGRGIDREKiREKAierglitadeaatlsddevlnliFAPGFSTAEqVTDvsGRGVGMDVVKRSIESLGG 159
                          90
                  ....*....|....*....
gi 1209301716 397 HIRIYSELGEGSTVKIYLP 415
Cdd:cd16916   160 TIEVESEPGQGTTFTIRLP 178
HATPase_EnvZ-like cd16950
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
344-415 5.79e-03

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Escherichia coli EnvZ and Pseudomonas aeruginosa BfmS; This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component sensor histidine kinase (HKs) such as Escherichia coli EnvZ of the EnvZ-OmpR two-component regulatory system (TCS), which functions in osmoregulation. It also contains the HATPase domain of Pseudomonas aeruginosa BfmS, the HK of the BfmSR TCS, which functions in the regulation of the rhl quorum-sensing system and bacterial virulence in P. aeruginosa. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA) and a HAMP sensor domain; some also contain a periplasmic domain.


Pssm-ID: 340426 [Multi-domain]  Cd Length: 101  Bit Score: 36.66  E-value: 5.79e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1209301716 344 GQYVMVAVTDSGLGMDKSTQEKAFEPFFTTKAV--GQGTGLGLSQVYGFVRQSSGHIRIYSELGEGSTVKIYLP 415
Cdd:cd16950    28 GNRTRIQVLDNGPGIAPEEVDELFQPFYRGDNArgTSGTGLGLAIVQRISDAHGGSLTLANRAGGGLCARIELP 101
HisKA pfam00512
His Kinase A (phospho-acceptor) domain; dimerization and phospho-acceptor domain of histidine ...
183-251 7.17e-03

His Kinase A (phospho-acceptor) domain; dimerization and phospho-acceptor domain of histidine kinases.


Pssm-ID: 459839 [Multi-domain]  Cd Length: 66  Bit Score: 35.26  E-value: 7.17e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1209301716 183 GQLTGGVAHDFNNLLTIVLGGLDIIGRqlpalgpSPEAERIAKARDMAVEGARRSATLTSRLLAFSRRQ 251
Cdd:pfam00512   3 SEFLANLSHELRTPLTAIRGYLELLRD-------EKLDEEQREYLETILRSAERLLRLINDLLDLSRIE 64
REC_CheB-like cd17541
phosphoacceptor receiver (REC) domain of chemotaxis response regulator protein-glutamate ...
441-553 7.78e-03

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: 36.60  E-value: 7.78e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209301716 441 ILVVEDDASLRGYTVQILTELGYG--VLEAADGRIGLKvLAERGDIDLLFTDIVMPgGLNGRELADEAVKLHPALKVLFT 518
Cdd:cd17541     3 VLIVDDSAVMRKLLSRILESDPDIevVGTARDGEEALE-KIKELKPDVITLDIEMP-VMDGLEALRRIMAERPTPVVMVS 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1209301716 519 TGYTRNAIV-----HHGRLDpgvhFLGKPF---------SFDELALKIR 553
Cdd:cd17541    81 SLTEEGAEItlealELGAVD----FIAKPSggisldleeIAEELIEKIK 125
CitB COG2197
DNA-binding response regulator, NarL/FixJ family, contains REC and HTH domains [Signal ...
441-503 9.28e-03

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: 36.79  E-value: 9.28e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1209301716 441 ILVVEDDASLRGYTVQIL-TELGYGVL-EAADGRIGLKvLAERGDIDLLFTDIVMPgGLNGRELA 503
Cdd:COG2197     4 VLIVDDHPLVREGLRALLeAEPDIEVVgEAADGEEALE-LLEELRPDVVLLDIRMP-GMDGLEAL 66
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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