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Conserved domains on  [gi|28056667|gb|AAO28546|]
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histidine kinase/response regulator hybrid protein [Xylella fastidiosa Temecula1]

Protein Classification

sensor histidine kinase( domain architecture ID 11467953)

sensor histidine kinase such as C4-dicarboxylate transport sensor protein DctB, a member of the two-component regulatory system DctB/DctD involved in the transport of C4-dicarboxylates. DctB functions as a membrane-associated protein kinase that phosphorylates DctD in response to environmental signals

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
COG4191 COG4191
Signal transduction histidine kinase regulating C4-dicarboxylate transport system [Signal ...
26-361 2.18e-60

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


:

Pssm-ID: 443345 [Multi-domain]  Cd Length: 361  Bit Score: 202.34  E-value: 2.18e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28056667  26 LFNTLREAGLDGSFERVESESALREALYLFAPDIVLSDLSMSGFHGYQALRVVREVGNTPFIFVSSKMGEDIAVEALQEG 105
Cdd:COG4191  17 ALALALALLLLLLLLLLALLLLLLALLLALLALLLLLLLLLLLLLLELLLLLLALLGGLLRLLLLLGLLLLLLLEALLLL 96
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28056667 106 ANDYIIKQNLVRLPSAVTRAVRESRAELERQHVESELMRAQRLESLAMLAAGFSHDLRNILQPLL----IVPDLLAGRTD 181
Cdd:COG4191  97 LLAALDAEENAELEELERDITELERAEEELRELQEQLVQSEKLAALGELAAGIAHEINNPLAAILgnaeLLRRRLEDEPD 176
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28056667 182 DPQLHQLVSIVAECGRRGHEMAESILSFVRGSNKPRERVLLADLFQTVQLLLRSSVPDC-IALRIEECDEYLSVEANYTE 260
Cdd:COG4191 177 PEELREALERILEGAERAAEIVRSLRAFSRRDEEEREPVDLNELIDEALELLRPRLKARgIEVELDLPPDLPPVLGDPGQ 256
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28056667 261 LQQCLLNLALNAIHAMPTG--GCLTLVAqRHDGDRICISVTDTGIGMSEETRARLFSPFFTTKS--DGTGLGLISCKRIA 336
Cdd:COG4191 257 LEQVLLNLLINAIDAMEEGegGRITIST-RREGDYVVISVRDNGPGIPPEVLERIFEPFFTTKPvgKGTGLGLSISYGIV 335
                       330       340
                ....*....|....*....|....*
gi 28056667 337 ESYGGLIQVCSELGVGTRFDLILPA 361
Cdd:COG4191 336 EKHGGRIEVESEPGGGTTFTITLPL 360
PRK09959 super family cl32441
acid-sensing system histidine kinase EvgS;
249-486 7.15e-13

acid-sensing system histidine kinase EvgS;


The actual alignment was detected with superfamily member PRK09959:

Pssm-ID: 182169 [Multi-domain]  Cd Length: 1197  Bit Score: 71.30  E-value: 7.15e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28056667   249 DEYLsVEANYTELQQCLLNLALNAIHAMPTGGCLTLVAQRHDGDR---ICISVTDTGIGMSEETRARLFSPFFTT----K 321
Cdd:PRK09959  818 DHYL-VKIDPQAFKQVLSNLLSNALKFTTEGAVKITTSLGHIDDNhavIKMTIMDSGSGLSQEEQQQLFKRYSQTsagrQ 896
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28056667   322 SDGTGLGLISCKRIAESYGGLIQVCSELGVGTRFDLILPA---RAPASRVSEENVPVVLGHGQRILIVDGEATRLSLLGN 398
Cdd:PRK09959  897 QTGSGLGLMICKELIKNMQGDLSLESHPGIGTTFTITIPVeisQQVATVEAKAEQPITLPEKLSILIADDHPTNRLLLKR 976
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28056667   399 ALASQGYQPQLAPDGGAAL-KLLRHHAepDLVIIDSDILLLSAVCLLPTMQELGYRGPAIVLEDAGQPLRREhfsKDLAV 477
Cdd:PRK09959  977 QLNLLGYDVDEATDGVQALhKVSMQHY--DLLITDVNMPNMDGFELTRKLREQNSSLPIWGLTANAQANERE---KGLSC 1051
                         250
                  ....*....|..
gi 28056667   478 HM---LRKPLEM 486
Cdd:PRK09959 1052 GMnlcLFKPLTL 1063
 
Name Accession Description Interval E-value
COG4191 COG4191
Signal transduction histidine kinase regulating C4-dicarboxylate transport system [Signal ...
26-361 2.18e-60

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


Pssm-ID: 443345 [Multi-domain]  Cd Length: 361  Bit Score: 202.34  E-value: 2.18e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28056667  26 LFNTLREAGLDGSFERVESESALREALYLFAPDIVLSDLSMSGFHGYQALRVVREVGNTPFIFVSSKMGEDIAVEALQEG 105
Cdd:COG4191  17 ALALALALLLLLLLLLLALLLLLLALLLALLALLLLLLLLLLLLLLELLLLLLALLGGLLRLLLLLGLLLLLLLEALLLL 96
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28056667 106 ANDYIIKQNLVRLPSAVTRAVRESRAELERQHVESELMRAQRLESLAMLAAGFSHDLRNILQPLL----IVPDLLAGRTD 181
Cdd:COG4191  97 LLAALDAEENAELEELERDITELERAEEELRELQEQLVQSEKLAALGELAAGIAHEINNPLAAILgnaeLLRRRLEDEPD 176
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28056667 182 DPQLHQLVSIVAECGRRGHEMAESILSFVRGSNKPRERVLLADLFQTVQLLLRSSVPDC-IALRIEECDEYLSVEANYTE 260
Cdd:COG4191 177 PEELREALERILEGAERAAEIVRSLRAFSRRDEEEREPVDLNELIDEALELLRPRLKARgIEVELDLPPDLPPVLGDPGQ 256
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28056667 261 LQQCLLNLALNAIHAMPTG--GCLTLVAqRHDGDRICISVTDTGIGMSEETRARLFSPFFTTKS--DGTGLGLISCKRIA 336
Cdd:COG4191 257 LEQVLLNLLINAIDAMEEGegGRITIST-RREGDYVVISVRDNGPGIPPEVLERIFEPFFTTKPvgKGTGLGLSISYGIV 335
                       330       340
                ....*....|....*....|....*
gi 28056667 337 ESYGGLIQVCSELGVGTRFDLILPA 361
Cdd:COG4191 336 EKHGGRIEVESEPGGGTTFTITLPL 360
PRK13837 PRK13837
two-component system VirA-like sensor kinase;
125-432 4.86e-49

two-component system VirA-like sensor kinase;


Pssm-ID: 237526 [Multi-domain]  Cd Length: 828  Bit Score: 180.26  E-value: 4.86e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28056667  125 AVRESRAELERQHVESELMRAQRLESLAMLAAGFSHDLRNILQPLL----IVPDLLAGRTDDPQ-LHQLVSivaeCGRRG 199
Cdd:PRK13837 424 AIERRRLETERDALERRLEHARRLEAVGTLASGIAHNFNNILGAILgyaeMALNKLARHSRAARyIDEIIS----AGARA 499
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28056667  200 HEMAESILSFVRGSNKPRERVLLADLFQTVQLLLRSSVPDCIALRIEECDEYLSVEANYTELQQCLLNLALNAIHAMPTG 279
Cdd:PRK13837 500 RLIIDQILAFGRKGERNTKPFDLSELVTEIAPLLRVSLPPGVELDFDQDQEPAVVEGNPAELQQVLMNLCSNAAQAMDGA 579
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28056667  280 GCLTLVAQRHD--------------GDRICISVTDTGIGMSEETRARLFSPFFTTKSDGTGLGLISCKRIAESYGGLIQV 345
Cdd:PRK13837 580 GRVDISLSRAKlrapkvlshgvlppGRYVLLRVSDTGAGIDEAVLPHIFEPFFTTRAGGTGLGLATVHGIVSAHAGYIDV 659
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28056667  346 CSELGVGTRFDLILPAR-----APASRVSEENVPvvLGHGQRILIVDGEATRLSLLGNALASQGYQPQLAPDGGAALKLL 420
Cdd:PRK13837 660 QSTVGRGTRFDVYLPPSskvpvAPQAFFGPGPLP--RGRGETVLLVEPDDATLERYEEKLAALGYEPVGFSTLAAAIAWI 737
                        330
                 ....*....|...
gi 28056667  421 RHHAEP-DLVIID 432
Cdd:PRK13837 738 SKGPERfDLVLVD 750
HATPase_c smart00387
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.
256-362 4.38e-30

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


Pssm-ID: 214643 [Multi-domain]  Cd Length: 111  Bit Score: 113.13  E-value: 4.38e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28056667    256 ANYTELQQCLLNLALNAIHAMPTGGCLTLVAqRHDGDRICISVTDTGIGMSEETRARLFSPFFTTKSD-----GTGLGLI 330
Cdd:smart00387   1 GDPDRLRQVLSNLLDNAIKYTPEGGRITVTL-ERDGDHVEITVEDNGPGIPPEDLEKIFEPFFRTDKRsrkigGTGLGLS 79
                           90       100       110
                   ....*....|....*....|....*....|..
gi 28056667    331 SCKRIAESYGGLIQVCSELGVGTRFDLILPAR 362
Cdd:smart00387  80 IVKKLVELHGGEISVESEPGGGTTFTITLPLE 111
HATPase_CckA-like cd16919
Histidine kinase-like ATPase domain of two-component sensor hybrid histidine kinases, similar ...
261-360 2.65e-28

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: 108.62  E-value: 2.65e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28056667 261 LQQCLLNLALNAIHAMPTGGCLTL----------VAQRHD----GDRICISVTDTGIGMSEETRARLFSPFFTTK--SDG 324
Cdd:cd16919   1 LELAILNLAVNARDAMPEGGRLTIetsnqrvdadYALNYRdlipGNYVCLEVSDTGSGMPAEVLRRAFEPFFTTKevGKG 80
                        90       100       110
                ....*....|....*....|....*....|....*.
gi 28056667 325 TGLGLISCKRIAESYGGLIQVCSELGVGTRFDLILP 360
Cdd:cd16919  81 TGLGLSMVYGFVKQSGGHLRIYSEPGVGTTVRIYLP 116
HATPase_c pfam02518
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the ...
261-362 8.28e-26

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: 101.29  E-value: 8.28e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28056667   261 LQQCLLNLALNAIHAMPTGGCLTLVAqrHDGDRICISVTDTGIGMSEETRARLFSPFFTTKSD---GTGLGLISCKRIAE 337
Cdd:pfam02518   6 LRQVLSNLLDNALKHAAKAGEITVTL--SEGGELTLTVEDNGIGIPPEDLPRIFEPFSTADKRgggGTGLGLSIVRKLVE 83
                          90       100
                  ....*....|....*....|....*
gi 28056667   338 SYGGLIQVCSELGVGTRFDLILPAR 362
Cdd:pfam02518  84 LLGGTITVESEPGGGTTVTLTLPLA 108
PRK09959 PRK09959
acid-sensing system histidine kinase EvgS;
249-486 7.15e-13

acid-sensing system histidine kinase EvgS;


Pssm-ID: 182169 [Multi-domain]  Cd Length: 1197  Bit Score: 71.30  E-value: 7.15e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28056667   249 DEYLsVEANYTELQQCLLNLALNAIHAMPTGGCLTLVAQRHDGDR---ICISVTDTGIGMSEETRARLFSPFFTT----K 321
Cdd:PRK09959  818 DHYL-VKIDPQAFKQVLSNLLSNALKFTTEGAVKITTSLGHIDDNhavIKMTIMDSGSGLSQEEQQQLFKRYSQTsagrQ 896
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28056667   322 SDGTGLGLISCKRIAESYGGLIQVCSELGVGTRFDLILPA---RAPASRVSEENVPVVLGHGQRILIVDGEATRLSLLGN 398
Cdd:PRK09959  897 QTGSGLGLMICKELIKNMQGDLSLESHPGIGTTFTITIPVeisQQVATVEAKAEQPITLPEKLSILIADDHPTNRLLLKR 976
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28056667   399 ALASQGYQPQLAPDGGAAL-KLLRHHAepDLVIIDSDILLLSAVCLLPTMQELGYRGPAIVLEDAGQPLRREhfsKDLAV 477
Cdd:PRK09959  977 QLNLLGYDVDEATDGVQALhKVSMQHY--DLLITDVNMPNMDGFELTRKLREQNSSLPIWGLTANAQANERE---KGLSC 1051
                         250
                  ....*....|..
gi 28056667   478 HM---LRKPLEM 486
Cdd:PRK09959 1052 GMnlcLFKPLTL 1063
AtoC COG2204
DNA-binding transcriptional response regulator, NtrC family, contains REC, AAA-type ATPase, ...
382-497 2.30e-08

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: 56.13  E-value: 2.30e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28056667 382 RILIVDGEATRLSLLGNALASQGYQPQLAPDGGAALKLLRHHaEPDLVIidSDILL--LSAVCLLPTMQELGYRGPAIVL 459
Cdd:COG2204   4 RILVVDDDPDIRRLLKELLERAGYEVETAASGEEALALLREE-PPDLVL--LDLRMpgMDGLELLRELRALDPDLPVILL 80
                        90       100       110
                ....*....|....*....|....*....|....*...
gi 28056667 460 EDAGQPLRREHFSKDLAVHMLRKPLEMWRVFRAVAYAL 497
Cdd:COG2204  81 TGYGDVETAVEAIKAGAFDYLTKPFDLEELLAAVERAL 118
REC cd00156
phosphoacceptor receiver (REC) domain of response regulators (RRs) and pseudo response ...
384-483 6.10e-06

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: 44.91  E-value: 6.10e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28056667 384 LIVDGEATRLSLLGNALASQGYQPQLAPDGGAALKLLRHHAePDLVIIDSDILLLSAVCLLPTMQELGYRGPAIVLEDAG 463
Cdd:cd00156   1 LIVDDDPAIRELLKSLLEREGYEVDTAADGEEALELLREER-PDLVLLDLMMPGMDGLELLRKLRELPPDIPVIVLTAKA 79
                        90       100
                ....*....|....*....|
gi 28056667 464 QPLRREHFSKDLAVHMLRKP 483
Cdd:cd00156  80 DEEDAVRALELGADDYLVKP 99
REC smart00448
cheY-homologous receiver domain; CheY regulates the clockwise rotation of E. coli flagellar ...
382-432 1.16e-05

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


Pssm-ID: 214668 [Multi-domain]  Cd Length: 55  Bit Score: 42.56  E-value: 1.16e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 28056667    382 RILIVDGEATRLSLLGNALASQGYQPQLAPDGGAALKLLRHHaEPDLVIID 432
Cdd:smart00448   2 RILVVDDDPLLRELLKALLEKEGYEVDEATDGEEALELLKEE-KPDLILLD 51
 
Name Accession Description Interval E-value
COG4191 COG4191
Signal transduction histidine kinase regulating C4-dicarboxylate transport system [Signal ...
26-361 2.18e-60

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


Pssm-ID: 443345 [Multi-domain]  Cd Length: 361  Bit Score: 202.34  E-value: 2.18e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28056667  26 LFNTLREAGLDGSFERVESESALREALYLFAPDIVLSDLSMSGFHGYQALRVVREVGNTPFIFVSSKMGEDIAVEALQEG 105
Cdd:COG4191  17 ALALALALLLLLLLLLLALLLLLLALLLALLALLLLLLLLLLLLLLELLLLLLALLGGLLRLLLLLGLLLLLLLEALLLL 96
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28056667 106 ANDYIIKQNLVRLPSAVTRAVRESRAELERQHVESELMRAQRLESLAMLAAGFSHDLRNILQPLL----IVPDLLAGRTD 181
Cdd:COG4191  97 LLAALDAEENAELEELERDITELERAEEELRELQEQLVQSEKLAALGELAAGIAHEINNPLAAILgnaeLLRRRLEDEPD 176
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28056667 182 DPQLHQLVSIVAECGRRGHEMAESILSFVRGSNKPRERVLLADLFQTVQLLLRSSVPDC-IALRIEECDEYLSVEANYTE 260
Cdd:COG4191 177 PEELREALERILEGAERAAEIVRSLRAFSRRDEEEREPVDLNELIDEALELLRPRLKARgIEVELDLPPDLPPVLGDPGQ 256
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28056667 261 LQQCLLNLALNAIHAMPTG--GCLTLVAqRHDGDRICISVTDTGIGMSEETRARLFSPFFTTKS--DGTGLGLISCKRIA 336
Cdd:COG4191 257 LEQVLLNLLINAIDAMEEGegGRITIST-RREGDYVVISVRDNGPGIPPEVLERIFEPFFTTKPvgKGTGLGLSISYGIV 335
                       330       340
                ....*....|....*....|....*
gi 28056667 337 ESYGGLIQVCSELGVGTRFDLILPA 361
Cdd:COG4191 336 EKHGGRIEVESEPGGGTTFTITLPL 360
NtrB COG3852
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms];
134-366 7.30e-56

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


Pssm-ID: 443061 [Multi-domain]  Cd Length: 361  Bit Score: 190.44  E-value: 7.30e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28056667 134 ERQHVESELMRAQRLESLAMLAAGFSHDLRNILQPLLIVPDLLAGRTDDPQLHQLVSIVAECGRRGHEMAESILSFVRGS 213
Cdd:COG3852 118 ERKRLERELRRAEKLAAVGELAAGLAHEIRNPLTGIRGAAQLLERELPDDELREYTQLIIEEADRLNNLVDRLLSFSRPR 197
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28056667 214 NKPRERVLLADLFQTVQLLLRSSVPDCIALRiEECDEYL-SVEANYTELQQCLLNLALNAIHAMPTGGCLTL-------- 284
Cdd:COG3852 198 PPEREPVNLHEVLERVLELLRAEAPKNIRIV-RDYDPSLpEVLGDPDQLIQVLLNLVRNAAEAMPEGGTITIrtrverqv 276
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28056667 285 -VAQRHDGDRICISVTDTGIGMSEETRARLFSPFFTTKSDGTGLGLISCKRIAESYGGLIQVCSELGVGTRFDLILPARA 363
Cdd:COG3852 277 tLGGLRPRLYVRIEVIDNGPGIPEEILDRIFEPFFTTKEKGTGLGLAIVQKIVEQHGGTIEVESEPGKGTTFRIYLPLEQ 356

                ...
gi 28056667 364 PAS 366
Cdd:COG3852 357 AEE 359
NtrY COG5000
Signal transduction histidine kinase NtrY involved in nitrogen fixation and metabolism ...
140-365 1.14e-50

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: 178.23  E-value: 1.14e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28056667 140 SELMRAQRLESLAMLAAGFSHDLRNILQPLLivpdLLAGR----------TDDPQLHQLVSIVAECGRRGHEMAESILSF 209
Cdd:COG5000 190 TELLRAERLAAWGELARRIAHEIKNPLTPIQ----LSAERlrrkladkleEDREDLERALDTIIRQVDRLKRIVDEFLDF 265
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28056667 210 VRGSNKPRERVLLADLFQTVQLLLRSSVPDC-IALRIEECDEYLSVEANYTELQQCLLNLALNAIHAMPTGGCLTLVAQR 288
Cdd:COG5000 266 ARLPEPQLEPVDLNELLREVLALYEPALKEKdIRLELDLDPDLPEVLADRDQLEQVLINLLKNAIEAIEEGGEIEVSTRR 345
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 28056667 289 hDGDRICISVTDTGIGMSEETRARLFSPFFTTKSDGTGLGLISCKRIAESYGGLIQVCSELGVGTRFDLILPARAPA 365
Cdd:COG5000 346 -EDGRVRIEVSDNGPGIPEEVLERIFEPFFTTKPKGTGLGLAIVKKIVEEHGGTIELESRPGGGTTFTIRLPLAEEA 421
PRK13837 PRK13837
two-component system VirA-like sensor kinase;
125-432 4.86e-49

two-component system VirA-like sensor kinase;


Pssm-ID: 237526 [Multi-domain]  Cd Length: 828  Bit Score: 180.26  E-value: 4.86e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28056667  125 AVRESRAELERQHVESELMRAQRLESLAMLAAGFSHDLRNILQPLL----IVPDLLAGRTDDPQ-LHQLVSivaeCGRRG 199
Cdd:PRK13837 424 AIERRRLETERDALERRLEHARRLEAVGTLASGIAHNFNNILGAILgyaeMALNKLARHSRAARyIDEIIS----AGARA 499
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28056667  200 HEMAESILSFVRGSNKPRERVLLADLFQTVQLLLRSSVPDCIALRIEECDEYLSVEANYTELQQCLLNLALNAIHAMPTG 279
Cdd:PRK13837 500 RLIIDQILAFGRKGERNTKPFDLSELVTEIAPLLRVSLPPGVELDFDQDQEPAVVEGNPAELQQVLMNLCSNAAQAMDGA 579
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28056667  280 GCLTLVAQRHD--------------GDRICISVTDTGIGMSEETRARLFSPFFTTKSDGTGLGLISCKRIAESYGGLIQV 345
Cdd:PRK13837 580 GRVDISLSRAKlrapkvlshgvlppGRYVLLRVSDTGAGIDEAVLPHIFEPFFTTRAGGTGLGLATVHGIVSAHAGYIDV 659
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28056667  346 CSELGVGTRFDLILPAR-----APASRVSEENVPvvLGHGQRILIVDGEATRLSLLGNALASQGYQPQLAPDGGAALKLL 420
Cdd:PRK13837 660 QSTVGRGTRFDVYLPPSskvpvAPQAFFGPGPLP--RGRGETVLLVEPDDATLERYEEKLAALGYEPVGFSTLAAAIAWI 737
                        330
                 ....*....|...
gi 28056667  421 RHHAEP-DLVIID 432
Cdd:PRK13837 738 SKGPERfDLVLVD 750
BaeS COG0642
Signal transduction histidine kinase [Signal transduction mechanisms];
47-362 4.07e-45

Signal transduction histidine kinase [Signal transduction mechanisms];


Pssm-ID: 440407 [Multi-domain]  Cd Length: 328  Bit Score: 160.84  E-value: 4.07e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28056667  47 ALREALYLFAPDIVLSDLSMSGFHGYQALRVVREVGNTPFIFVSSKMGEDIAVEALQEGANDYIIKQNLVRLPSAVTRAV 126
Cdd:COG0642   7 LLVLLLLLLLLLLLALLLLLLLLLLLALLLLLALLLLLLLLLLLLLLLALALLALLLLLLLLLLLLLLLLLLLLLLLLLL 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28056667 127 RESRAELERQHVESELMRaQRLESLAMLAAGFSHDLRNILQPLLIVPDLLAgRTDDPQLHQLVSIVAECGRRGHEMAESI 206
Cdd:COG0642  87 LLLLLLLLLLLALLLLLE-EANEAKSRFLANVSHELRTPLTAIRGYLELLL-EELDEEQREYLETILRSADRLLRLINDL 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28056667 207 LSFVRGSNK----PRERVLLADLFQTVQLLLRSSVPDC-IALRIEECDEYLSVEANYTELQQCLLNLALNAIHAMPTGGC 281
Cdd:COG0642 165 LDLSRLEAGklelEPEPVDLAELLEEVVELFRPLAEEKgIELELDLPDDLPTVRGDPDRLRQVLLNLLSNAIKYTPEGGT 244
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28056667 282 LTLVAQRhDGDRICISVTDTGIGMSEETRARLFSPFFTTKSD----GTGLGLISCKRIAESYGGLIQVCSELGVGTRFDL 357
Cdd:COG0642 245 VTVSVRR-EGDRVRISVEDTGPGIPPEDLERIFEPFFRTDPSrrggGTGLGLAIVKRIVELHGGTIEVESEPGKGTTFTV 323

                ....*
gi 28056667 358 ILPAR 362
Cdd:COG0642 324 TLPLA 328
KinB COG5806
Sporulation sensor histidine kinase B [Cell cycle control, cell division, chromosome ...
133-361 1.33e-43

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


Pssm-ID: 444508 [Multi-domain]  Cd Length: 412  Bit Score: 158.88  E-value: 1.33e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28056667 133 LERQHVESELMRAQRLESLAMLAAGFSHDLRNilqPLLIVPD----LLAGRTDDPQLHQLVSIV-AECGRrghemAESI- 206
Cdd:COG5806 183 IENILLRKELQRAEKLEVVSELAASIAHEVRN---PLTVVRGfiqlLQEPELSDEKRKQYIRIAlEELDR-----AEAIi 254
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28056667 207 ---LSFVRGSNKPRERVLLADLFQTVQLLLRS-SVPDCIALRIEeCDEYLSVEANYTELQQCLLNLALNAIHAMPTGGCL 282
Cdd:COG5806 255 tdyLTFAKPQPEKLEKIDVSEELEHVIDVLSPyANMNNVEIQTE-LEPGLYIEGDRQKLQQCLINIIKNGIEAMPNGGTL 333
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 28056667 283 TLVAqRHDGDRICISVTDTGIGMSEETRARLFSPFFTTKSDGTGLGLISCKRIAESYGGLIQVCSELGVGTRFDLILPA 361
Cdd:COG5806 334 TIDV-SIDKNKVIISIKDTGVGMTKEQLERLGEPYFSTKEKGTGLGTMVSYRIIEAMNGTIRVESEVGKGTTFTITLPL 411
KinC COG5807
Sporulation sensor histidine kinase C [Cell cycle control, cell division, chromosome ...
134-360 1.24e-42

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: 154.94  E-value: 1.24e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28056667 134 ERQHVESELMRAQRLESLAMLAAGFSHDLRNilqPLLIVP---DLLAGRTDDPQLHQLVSIVAECGRRGHEMAESILSFV 210
Cdd:COG5807 130 KRKEAEDKLLRSEKLSVAGELAAGIAHEIRN---PLTSIKgflQLLQESREDSEREEYFNIIISEIDRINTIITELLVLS 206
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28056667 211 RGSNKPRERVLLADLF-QTVQLLLRSSVPDCIALRIEECDEYLSVEANYTELQQCLLNLALNAIHAMPTGGCLTLVAQRh 289
Cdd:COG5807 207 KPKKFNFKKLNLNDVLeDVIALLSTEAILKNISIKYDLADDEPVINGDKNQLKQVFINLIKNAIEAMETGGNITIKTYV- 285
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 28056667 290 DGDRICISVTDTGIGMSEETRARLFSPFFTTKSDGTGLGLISCKRIAESYGGLIQVCSELGVGTRFDLILP 360
Cdd:COG5807 286 EGDFVVISVKDEGIGIPEEVLEKIGEPFFTTKEEGTGLGLSICKKIIEEHNGTIEVESKPGKGTTFTIYLP 356
KinE COG5809
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome ...
134-362 9.77e-42

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: 155.52  E-value: 9.77e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28056667 134 ERQHVESELMRAQRLESLAMLAAGFSHDLRNILQPLLIVPDLLAGRTDDPQLHQLVSIVAECGRrghemAESILSFVRGS 213
Cdd:COG5809 253 ERKKLEELLRKSEKLSVVGELAAGIAHEIRNPLTSLKGFIQLLKDTIDEEQKTYLDIMLSELDR-----IESIISEFLVL 327
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28056667 214 NKPR----ERVLLADLF-QTVQLLLRSSVPDCIALRIEECDEYLSVEANYTELQQCLLNLALNAIHAMPTGGCLTLVAQR 288
Cdd:COG5809 328 AKPQaikyEPKDLNTLIeEVIPLLQPQALLKNVQIELELEDDIPDILGDENQLKQVFINLLKNAIEAMPEGGNITIETKA 407
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 28056667 289 HDGDRICISVTDTGIGMSEETRARLFSPFFTTKSDGTGLGLISCKRIAESYGGLIQVCSELGVGTRFDLILPAR 362
Cdd:COG5809 408 EDDDKVVISVTDEGCGIPEERLKKLGEPFYTTKEKGTGLGLMVSYKIIEEHGGKITVESEVGKGTTFSITLPIK 481
KinA COG5805
Sporulation sensor histidine kinase A (Stage II sporulation protein SpoIIF/SpoIIJ) [Cell cycle ...
72-360 8.10e-41

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: 153.35  E-value: 8.10e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28056667  72 YQALRVVREVGnTPFIFVSSKM---GEDIAVEAlqegandyiIKQNLVRLPSAVTRAVRESRAELERQHVESELMRAQRL 148
Cdd:COG5805 215 KERIESITEVW-QEFIIEREIItkdGRIRYFEA---------VIVPLIDTDGSVKGILVILRDITEKKEAEELMARSEKL 284
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28056667 149 ESLAMLAAGFSHDLRNilqPLLIVPDLL----AGRTDDPQLHQLvsIVAECGRrghemAESILSFVRGSNKP----RERV 220
Cdd:COG5805 285 SIAGQLAAGIAHEIRN---PLTSIKGFLqllqPGIEDKEEYFDI--MLSELDR-----IESIISEFLALAKPqavnKEKE 354
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28056667 221 LLADLFQ-TVQLLLRSSVPDCIALRIEECDEYLSVEANYTELQQCLLNLALNAIHAMPTGGCLTlVAQRHDGDRICISVT 299
Cdd:COG5805 355 NINELIQdVVTLLETEAILHNIQIRLELLDEDPFIYCDENQIKQVFINLIKNAIEAMPNGGTIT-IHTEEEDNSVIIRVI 433
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 28056667 300 DTGIGMSEETRARLFSPFFTTKSDGTGLGLISCKRIAESYGGLIQVCSELGVGTRFDLILP 360
Cdd:COG5805 434 DEGIGIPEERLKKLGEPFFTTKEKGTGLGLMVSYKIIENHNGTIDIDSKVGKGTTFTITLP 494
PRK10364 PRK10364
two-component system sensor histidine kinase ZraS;
40-363 1.02e-39

two-component system sensor histidine kinase ZraS;


Pssm-ID: 236674 [Multi-domain]  Cd Length: 457  Bit Score: 149.55  E-value: 1.02e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28056667   40 ERVESESALrEALYLFAPdivlsdLSMSGFHGYQALRVVREVGNTPFIFVSSKMGEDIAVEAlQEGANDYIIKQNL--VR 117
Cdd:PRK10364 133 DSADGEPVL-EIYRQFQP------MFAAGMHGMRHMQQYAAANTPQAIFIAFDASNLVSAQA-REQRNTLIILFALatVL 204
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28056667  118 LPSAVT----RAVRESRAELERqhvesELMRAQRLESLAMLAAGFSHDLRNILQPLLIVPDLLAGRT-DDPQLHQLVSIV 192
Cdd:PRK10364 205 LASLLAffwyRRYLRSRQLLQD-----EMKRKEKLVALGHLAAGVAHEIRNPLSSIKGLAKYFAERApAGGEAHQLAQVM 279
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28056667  193 AECGRRGHEMAESILSFVRGSNKPRERVLLADLFQTVQLLLRSsvpDC----IALRIEECDEYLSVEANYTELQQCLLNL 268
Cdd:PRK10364 280 AKEADRLNRVVSELLELVKPTHLALQAVDLNDLINHSLQLVSQ---DAnsreIQLRFTANDTLPEIQADPDRLTQVLLNL 356
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28056667  269 ALNAIHAMPTGGCLTLVAQRHdGDRICISVTDTGIGMSEETRARLFSPFFTTKSDGTGLGLISCKRIAESYGGLIQVCSE 348
Cdd:PRK10364 357 YLNAIQAIGQHGVISVTASES-GAGVKISVTDSGKGIAADQLEAIFTPYFTTKAEGTGLGLAVVHNIVEQHGGTIQVASQ 435
                        330
                 ....*....|....*
gi 28056667  349 LGVGTRFDLILPARA 363
Cdd:PRK10364 436 EGKGATFTLWLPVNI 450
KdpD COG2205
K+-sensing histidine kinase KdpD [Signal transduction mechanisms];
137-364 1.51e-39

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


Pssm-ID: 441807 [Multi-domain]  Cd Length: 239  Bit Score: 143.12  E-value: 1.51e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28056667 137 HVESELMRAQRLESL-AMLAAGFSHDLRNILQPLLIVPDLLAGRTD--DPQLHQLVSIVAECGRRGHEMAESILSFVR-- 211
Cdd:COG2205   1 ELEEALEELEELERLkSEFLANVSHELRTPLTSILGAAELLLDEEDlsPEERRELLEIIRESAERLLRLIEDLLDLSRle 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28056667 212 -GSNKP-RERVLLADLFQTVQLLLRSSVPDC-IALRIEECDEYLSVEANYTELQQCLLNLALNAIHAMPTGGCLTLVAQR 288
Cdd:COG2205  81 sGKLSLeLEPVDLAELLEEAVEELRPLAEEKgIRLELDLPPELPLVYADPELLEQVLANLLDNAIKYSPPGGTITISARR 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28056667 289 hDGDRICISVTDTGIGMSEETRARLFSPFF----TTKSDGTGLGLISCKRIAESYGGLIQVCSELGVGTRFDLILPARAP 364
Cdd:COG2205 161 -EGDGVRISVSDNGPGIPEEELERIFERFYrgdnSRGEGGTGLGLAIVKRIVEAHGGTIWVESEPGGGTTFTVTLPLAES 239
KinD COG5808
Sporulation sensor histidine kinase D [Cell cycle control, cell division, chromosome ...
133-363 3.62e-39

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


Pssm-ID: 444510 [Multi-domain]  Cd Length: 454  Bit Score: 147.97  E-value: 3.62e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28056667 133 LERQHVESElmrAQRLESLAMLAAGFSHDLRNILQPLLIVPDLLAGRTDDPQLHQLVSIVAECGRRGHEMAESILSFVRG 212
Cdd:COG5808 226 LERVIQEIN---TQKLELIGTFAASTAHEIRNPLTSIKGFIQLLQEKYPELEDQKYFDIIQEEIQRINQIVSEFLVLGKP 302
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28056667 213 SNKPRERVLLADLFQTVQLLLRSSVPDC-IALRIEECDEYLSVEANYTELQQCLLNLALNAIHAMPTGGCLTlVAQRHDG 291
Cdd:COG5808 303 TAKKLELDDLNELIEEILSIIDSEANLKnIRVEKQSLDEPLHIKCDKDRIKQVLLNLIKNAIEAMKEGGKLT-ISIENDD 381
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 28056667 292 DRICISVTDTGIGMSEETRARLFSPFFTTKSDGTGLGLISCKRIAESYGGLIQVCSELGVGTRFDLILPARA 363
Cdd:COG5808 382 EKAVIEVIDNGEGIPEDIIDEIFEPFVTTKEGGTGLGLSVCKRIVEMHGGEIDIESEEGKGTTFTIRLPLKK 453
PRK13557 PRK13557
histidine kinase; Provisional
135-432 6.16e-38

histidine kinase; Provisional


Pssm-ID: 237425 [Multi-domain]  Cd Length: 540  Bit Score: 145.97  E-value: 6.16e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28056667  135 RQHVESELMRAQRLESLAMLAAGFSHDLRNILQPLLIVPDLLAGRTD----DPQLHQL-VSIVAECGRRGHEMAESILSF 209
Cdd:PRK13557 147 RRDAEDALRQAQKMEALGQLTGGIAHDFNNLLQVMSGYLDVIQAALShpdaDRGRMARsVENIRAAAERAATLTQQLLAF 226
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28056667  210 VRgSNKPRERVL-LADLFQTVQLLLRSSVPDCIALRIEECDEYLSVEANYTELQQCLLNLALNAIHAMPTGGCLT----- 283
Cdd:PRK13557 227 AR-KQRLEGRVLnLNGLVSGMGELAERTLGDAVTIETDLAPDLWNCRIDPTQAEVALLNVLINARDAMPEGGRVTirtrn 305
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28056667  284 LVAQRHD---------GDRICISVTDTGIGMSEETRARLFSPFFTTKSD--GTGLGLISCKRIAESYGGLIQVCSELGVG 352
Cdd:PRK13557 306 VEIEDEDlamyhglppGRYVSIAVTDTGSGMPPEILARVMDPFFTTKEEgkGTGLGLSMVYGFAKQSGGAVRIYSEVGEG 385
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28056667  353 TRFDLILPA--RAPASRVSEENVPVVLGHGQRILIVDGEATRLSLLGNALASQGYQPQLAPDGGAALKLLRHHAEPDLVI 430
Cdd:PRK13557 386 TTVRLYFPAsdQAENPEQEPKARAIDRGGTETILIVDDRPDVAELARMILEDFGYRTLVASNGREALEILDSHPEVDLLF 465

                 ..
gi 28056667  431 ID 432
Cdd:PRK13557 466 TD 467
WalK COG5002
Sensor histidine kinase WalK [Signal transduction mechanisms];
40-364 9.87e-37

Sensor histidine kinase WalK [Signal transduction mechanisms];


Pssm-ID: 444026 [Multi-domain]  Cd Length: 390  Bit Score: 139.69  E-value: 9.87e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28056667  40 ERVESESALREALYLFAPDIVLSDLSMSGFHGYQALRVVREVGNTPFIFVSSKMGEDIAVEALQEGANDYIIKQNLVRLP 119
Cdd:COG5002  56 LLLLLLLLLLLALLLLLLLLLLLLALALLLLALLLLLLLLLLLLALLILLLLLALLILLAALLLLLSELLLLLLLLGRLS 135
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28056667 120 SAVTRAVRESRAELERQHVESELMRAQRLESlaMLAAGFSHDLRNILQPLLIVPDLLAGR--TDDPQLHQLVSIVAECGR 197
Cdd:COG5002 136 LRLSALLLGLLLLAAVERDITELERLEQMRR--EFVANVSHELRTPLTSIRGYLELLLDGaaDDPEERREYLEIILEEAE 213
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28056667 198 RGHEMAESILSFVRGSNKP----RERVLLADLFQTVQLLLRSSVPDC-IALRIEECDEYLSVEANYTELQQCLLNLALNA 272
Cdd:COG5002 214 RLSRLVNDLLDLSRLESGElkleKEPVDLAELLEEVVEELRPLAEEKgIELELDLPEDPLLVLGDPDRLEQVLTNLLDNA 293
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28056667 273 IHAMPTGGCLTLVAQRhDGDRICISVTDTGIGMSEETRARLFSPFFTT------KSDGTGLGLISCKRIAESYGGLIQVC 346
Cdd:COG5002 294 IKYTPEGGTITVSLRE-EDDQVRISVRDTGIGIPEEDLPRIFERFYRVdksrsrETGGTGLGLAIVKHIVEAHGGRIWVE 372
                       330
                ....*....|....*...
gi 28056667 347 SELGVGTRFDLILPARAP 364
Cdd:COG5002 373 SEPGKGTTFTITLPLARE 390
PRK11360 PRK11360
two-component system sensor histidine kinase AtoS;
134-367 5.88e-36

two-component system sensor histidine kinase AtoS;


Pssm-ID: 236901 [Multi-domain]  Cd Length: 607  Bit Score: 140.87  E-value: 5.88e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28056667  134 ERQHVESELMRAQRLESLAMLAAGFSHDLRNilqPLL----IVPDLLAGRTDDPQLHQLvSIVAECGRRGHEMAESILSF 209
Cdd:PRK11360 373 ERKRLQRRVARQERLAALGELVAGVAHEIRN---PLTairgYVQIWRQQTSDPPSQEYL-SVVLREVDRLNKVIDQLLEF 448
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28056667  210 VRGSNKPRERVLLADLFQ-TVQLLLRSSVPDCIALRIEECDEYLSVEANYTELQQCLLNLALNAIHAMPTGGCLTLVAQR 288
Cdd:PRK11360 449 SRPRESQWQPVSLNALVEeVLQLFQTAGVQARVDFETELDNELPPIWADPELLKQVLLNILINAVQAISARGKIRIRTWQ 528
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 28056667  289 HDGDRICISVTDTGIGMSEETRARLFSPFFTTKSDGTGLGLISCKRIAESYGGLIQVCSELGVGTRFDLILPARAPASR 367
Cdd:PRK11360 529 YSDGQVAVSIEDNGCGIDPELLKKIFDPFFTTKAKGTGLGLALSQRIINAHGGDIEVESEPGVGTTFTLYLPINPQGNQ 607
HATPase_c smart00387
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.
256-362 4.38e-30

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


Pssm-ID: 214643 [Multi-domain]  Cd Length: 111  Bit Score: 113.13  E-value: 4.38e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28056667    256 ANYTELQQCLLNLALNAIHAMPTGGCLTLVAqRHDGDRICISVTDTGIGMSEETRARLFSPFFTTKSD-----GTGLGLI 330
Cdd:smart00387   1 GDPDRLRQVLSNLLDNAIKYTPEGGRITVTL-ERDGDHVEITVEDNGPGIPPEDLEKIFEPFFRTDKRsrkigGTGLGLS 79
                           90       100       110
                   ....*....|....*....|....*....|..
gi 28056667    331 SCKRIAESYGGLIQVCSELGVGTRFDLILPAR 362
Cdd:smart00387  80 IVKKLVELHGGEISVESEPGGGTTFTITLPLE 111
HATPase_CckA-like cd16919
Histidine kinase-like ATPase domain of two-component sensor hybrid histidine kinases, similar ...
261-360 2.65e-28

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: 108.62  E-value: 2.65e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28056667 261 LQQCLLNLALNAIHAMPTGGCLTL----------VAQRHD----GDRICISVTDTGIGMSEETRARLFSPFFTTK--SDG 324
Cdd:cd16919   1 LELAILNLAVNARDAMPEGGRLTIetsnqrvdadYALNYRdlipGNYVCLEVSDTGSGMPAEVLRRAFEPFFTTKevGKG 80
                        90       100       110
                ....*....|....*....|....*....|....*.
gi 28056667 325 TGLGLISCKRIAESYGGLIQVCSELGVGTRFDLILP 360
Cdd:cd16919  81 TGLGLSMVYGFVKQSGGHLRIYSEPGVGTTVRIYLP 116
HATPase_TmoS-FixL-DctS-like cd16920
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
261-360 4.94e-28

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: 107.48  E-value: 4.94e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28056667 261 LQQCLLNLALNAIHAMPTGGC----LTLVAQRHDGDRICISVTDTGIGMSEETRARLFSPFFTTKSDGTGLGLISCKRIA 336
Cdd:cd16920   1 IQQVLINLVRNGIEAMSEGGCerreLTIRTSPADDRAVTISVKDTGPGIAEEVAGQLFDPFYTTKSEGLGMGLSICRSII 80
                        90       100
                ....*....|....*....|....
gi 28056667 337 ESYGGLIQVCSELGVGTRFDLILP 360
Cdd:cd16920  81 EAHGGRLSVESPAGGGATFQFTLP 104
HATPase_AtoS-like cd16943
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
260-360 4.07e-27

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: 104.81  E-value: 4.07e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28056667 260 ELQQCLLNLALNAIHAMPTGGCLTLVAQRHDgDRICISVTDTGIGMSEETRARLFSPFFTTK--SDGTGLGLISCKRIAE 337
Cdd:cd16943   3 QLNQVLLNLLVNAAQAMEGRGRITIRTWAHV-DQVLIEVEDTGSGIDPEILGRIFDPFFTTKpvGEGTGLGLSLSYRIIQ 81
                        90       100
                ....*....|....*....|...
gi 28056667 338 SYGGLIQVCSELGVGTRFDLILP 360
Cdd:cd16943  82 KHGGTIRVASVPGGGTRFTIILP 104
HATPase_EvgS-ArcB-TorS-like cd16922
Histidine kinase-like ATPase domain of two-component sensor histidine kinases, many are hybrid ...
261-360 7.66e-27

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: 104.11  E-value: 7.66e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28056667 261 LQQCLLNLALNAIHAMPTGG---CLTLVAQRHDGDRICISVTDTGIGMSEETRARLFSPF------FTTKSDGTGLGLIS 331
Cdd:cd16922   1 LRQILLNLLGNAIKFTEEGEvtlRVSLEEEEEDGVQLRFSVEDTGIGIPEEQQARLFEPFsqadssTTRKYGGTGLGLAI 80
                        90       100
                ....*....|....*....|....*....
gi 28056667 332 CKRIAESYGGLIQVCSELGVGTRFDLILP 360
Cdd:cd16922  81 SKKLVELMGGDISVESEPGQGSTFTFTLP 109
HATPase_c pfam02518
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the ...
261-362 8.28e-26

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: 101.29  E-value: 8.28e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28056667   261 LQQCLLNLALNAIHAMPTGGCLTLVAqrHDGDRICISVTDTGIGMSEETRARLFSPFFTTKSD---GTGLGLISCKRIAE 337
Cdd:pfam02518   6 LRQVLSNLLDNALKHAAKAGEITVTL--SEGGELTLTVEDNGIGIPPEDLPRIFEPFSTADKRgggGTGLGLSIVRKLVE 83
                          90       100
                  ....*....|....*....|....*
gi 28056667   338 SYGGLIQVCSELGVGTRFDLILPAR 362
Cdd:pfam02518  84 LLGGTITVESEPGGGTTVTLTLPLA 108
COG4251 COG4251
Bacteriophytochrome (light-regulated signal transduction histidine kinase) [Signal ...
1-364 5.92e-25

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


Pssm-ID: 443393 [Multi-domain]  Cd Length: 503  Bit Score: 107.95  E-value: 5.92e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28056667   1 MSQQAEKLGLLKILLIGDSLEDAKLLFNTLREAGLDGSFERVESESALREALYLFAPDIVLSDLSMSGFHGYQALRVVRE 80
Cdd:COG4251 135 LLLEELALLRLALALLLLLLLLLLLLLLLLALILALLLAALAELELLLLLLLVLLLLLLLLLLLLLLLLRLLLELLLLLE 214
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28056667  81 VGNTPFIFVSSKMGEDIAVEALQEGANDYIIKQNLVRLPSAVTRAVREsRAELERQHVESELMRA-QRLESLAMLAagfS 159
Cdd:COG4251 215 AELLLSLGGGLGLLLLLLLLLVLLLLLILLLLLLILVLELLELRLELE-ELEEELEERTAELERSnEELEQFAYVA---S 290
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28056667 160 HDLRNILQPLLIVPDLL---AGRTDDPQLHQLVSIVAECGRRGHEMAESILSFVRGSNK--PRERVLLADLFQTVQLLLR 234
Cdd:COG4251 291 HDLREPLRKISGFSQLLeedYGDKLDEEGREYLERIRDAAERMQALIDDLLAYSRVGRQelEFEPVDLNELLEEVLEDLE 370
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28056667 235 SSVPDCIAlRIEeCDEYLSVEANYTELQQCLLNLALNAIHAMPTG--GCLTLVAQRhDGDRICISVTDTGIGMSEETRAR 312
Cdd:COG4251 371 PRIEERGA-EIE-VGPLPTVRGDPTLLRQVFQNLISNAIKYSRPGepPRIEIGAER-EGGEWVFSVRDNGIGIDPEYAEK 447
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 28056667 313 LFSPFFTTKSD----GTGLGLISCKRIAESYGGLIQVCSELGVGTRFDLILPARAP 364
Cdd:COG4251 448 IFEIFQRLHSRdeyeGTGIGLAIVKKIVERHGGRIWVESEPGEGATFYFTLPKAPA 503
PRK15347 PRK15347
two component system sensor kinase;
126-432 9.38e-19

two component system sensor kinase;


Pssm-ID: 237951 [Multi-domain]  Cd Length: 921  Bit Score: 89.70  E-value: 9.38e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28056667  126 VRESRAELERQHVESELMRAQRLESLAMLaagfSHDLRNILQPLLIVPDLLAGRTDDPQLHQLVSIVAECGRRGHEMAES 205
Cdd:PRK15347 377 VAERTQALAEAKQRAEQANKRKSEHLTTI----SHEIRTPLNGVLGALELLQNTPLTAEQMDLADTARQCTLSLLAIINN 452
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28056667  206 ILSFVRGSNKPRERV--------LLADLFQTVQ-------LLLRSSVPDCIALrieecdeYLSVEAnyTELQQCLLNLAL 270
Cdd:PRK15347 453 LLDFSRIESGQMTLSleetallpLLDQAMLTIQgpaqsksLTLRTFVGAHVPL-------YLHLDS--LRLRQILVNLLG 523
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28056667  271 NAIHAMPTGGCLTLVaqRHDGDRICISVTDTGIGMSEETRARLFSPFFTT--KSDGTGLGLISCKRIAESYGGLIQVCSE 348
Cdd:PRK15347 524 NAVKFTETGGIRLRV--KRHEQQLCFTVEDTGCGIDIQQQQQIFTPFYQAdtHSQGTGLGLTIASSLAKMMGGELTLFST 601
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28056667  349 LGVGTRFDLILP---ARAP-------------------------------------------------------ASRVSE 370
Cdd:PRK15347 602 PGVGSCFSLVLPlneYAPPeplkgelsaplalhrqlsawgitcqpghqnpalldpelaylpgrlydllqqiiqgAPNEPV 681
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 28056667  371 ENVPvVLGHGQRILIVDGEATRLSLLGNALASQGYQPQLAPDGGAALKLLRHHAEpDLVIID 432
Cdd:PRK15347 682 INLP-LQPWQLQILLVDDVETNRDIIGMMLVELGQQVTTAASGTEALELGRQHRF-DLVLMD 741
PRK11466 PRK11466
hybrid sensory histidine kinase TorS; Provisional
126-497 2.06e-18

hybrid sensory histidine kinase TorS; Provisional


Pssm-ID: 236914 [Multi-domain]  Cd Length: 914  Bit Score: 88.81  E-value: 2.06e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28056667  126 VRESRAEL-----ERQHVESELMRAQRLESlAMLAAgFSHDLRNILQPLLIVPDLLAGRTDDPQLHQLVSIVAECGRRGH 200
Cdd:PRK11466 416 VKARTAELqelviEHRQARAEAEKASQAKS-AFLAA-MSHEIRTPLYGILGTAQLLADNPALNAQRDDLRAITDSGESLL 493
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28056667  201 EMAESILSF---------VRGSNKPRE-RVLLADLFQTVQLLLRSSVpdcIALRIEECDEYLS-VEANYTELQQCLLNLA 269
Cdd:PRK11466 494 TILNDILDYsaieaggknVSVSDEPFEpRPLLESTLQLMSGRVKGRP---IRLATDIADDLPTaLMGDPRRIRQVITNLL 570
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28056667  270 LNAIHAMPTGgcLTLVAQRHDGDRICISVTDTGIGMSEETRARLFSPF--FTTKSDGTGLGLISCKRIAESYGGLIQVCS 347
Cdd:PRK11466 571 SNALRFTDEG--SIVLRSRTDGEQWLVEVEDSGCGIDPAKLAEIFQPFvqVSGKRGGTGLGLTISSRLAQAMGGELSATS 648
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28056667  348 ELGVGTRFDLILPARAPASRVSEENVPVVLGHGQRILIVDGEATRLSLLGNALASQGYQPQLAPDGGAALKLLRHHAEPD 427
Cdd:PRK11466 649 TPEVGSCFCLRLPLRVATAPVPKTVNQAVRLDGLRLLLIEDNPLTQRITAEMLNTSGAQVVAVGNAAQALETLQNSEPFA 728
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 28056667  428 LVIIDSDI-------LLLSAVCLLPTMQELGYRgpAIVLEDAgqpLRREhfSKDLAVHMLRKPLEMWRVFRAVAYAL 497
Cdd:PRK11466 729 AALVDFDLpdydgitLARQLAQQYPSLVLIGFS--AHVIDET---LRQR--TSSLFRGIIPKPVPREVLGQLLAHYL 798
PRK11091 PRK11091
aerobic respiration control sensor protein ArcB; Provisional
254-432 1.56e-17

aerobic respiration control sensor protein ArcB; Provisional


Pssm-ID: 236842 [Multi-domain]  Cd Length: 779  Bit Score: 85.76  E-value: 1.56e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28056667  254 VEANYTELQQCLLNLALNAIHAMPTGGcLTLVAQRHDGDRICISVTDTGIGMSEETRARLFSPFFTTKSD-------GTG 326
Cdd:PRK11091 392 VITDGTRLRQILWNLISNAVKFTQQGG-VTVRVRYEEGDMLTFEVEDSGIGIPEDELDKIFAMYYQVKDShggkpatGTG 470
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28056667  327 LGLISCKRIAESYGGLIQVCSELGVGTRFDLILPARAPASRVSE-ENVPVVLGHGQRILIVDGEATRLSLLGNALASQGY 405
Cdd:PRK11091 471 IGLAVSKRLAQAMGGDITVTSEEGKGSCFTLTIHAPAVAEEVEDaFDEDDMPLPALNILLVEDIELNVIVARSVLEKLGN 550
                        170       180
                 ....*....|....*....|....*..
gi 28056667  406 QPQLAPDGGAALKLLRHHaEPDLVIID 432
Cdd:PRK11091 551 SVDVAMTGKEALEMFDPD-EYDLVLLD 576
HATPase_HupT_MifS-like cd16976
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
261-359 1.02e-16

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: 75.57  E-value: 1.02e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28056667 261 LQQCLLNLALNAIHAMPT--GGCLTLVAQRhDGDRICISVTDTGIGMSEETRARLFSPFFTTK--SDGTGLGLISCKRIA 336
Cdd:cd16976   1 IQQVLMNLLQNALDAMGKveNPRIRIAARR-LGGRLVLVVRDNGPGIAEEHLSRVFDPFFTTKpvGKGTGLGLSISYGIV 79
                        90       100
                ....*....|....*....|...
gi 28056667 337 ESYGGLIQVCSELGVGTRFDLIL 359
Cdd:cd16976  80 EEHGGRLSVANEEGAGARFTFDL 102
CitA COG3290
Sensor histidine kinase DipB regulating citrate/malate metabolism [Signal transduction ...
241-360 3.09e-15

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


Pssm-ID: 442519 [Multi-domain]  Cd Length: 389  Bit Score: 77.20  E-value: 3.09e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28056667 241 IALRIEECDEYLSVEANYTELQQCLLNLALNAIHAMPTGG------CLTLvaqRHDGDRICISVTDTGIGMSEETRARLF 314
Cdd:COG3290 262 IDLTIDIDSDLPDLPLSDTDLVTILGNLLDNAIEAVEKLPeeerrvELSI---RDDGDELVIEVEDSGPGIPEELLEKIF 338
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 28056667 315 SPFFTTK-SDGTGLGLISCKRIAESYGGLIQVCSELGVGTRFDLILP 360
Cdd:COG3290 339 ERGFSTKlGEGRGLGLALVKQIVEKYGGTIEVESEEGEGTVFTVRLP 385
HATPase_NtrY-like cd16944
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
259-360 8.40e-15

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: 70.26  E-value: 8.40e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28056667 259 TELQQCLLNL---ALNAIHAMPTG-GCLTLVAQRHDGDRICISVTDTGIGMSEETRARLFSPFFTTKSDGTGLGLISCKR 334
Cdd:cd16944   3 TQISQVLTNIlknAAEAIEGRPSDvGEVRIRVEADQDGRIVLIVCDNGKGFPREMRHRATEPYVTTRPKGTGLGLAIVKK 82
                        90       100
                ....*....|....*....|....*.
gi 28056667 335 IAESYGGLIQVCSELGVGTRFDLILP 360
Cdd:cd16944  83 IMEEHGGRISLSNREAGGACIRIILP 108
PRK10841 PRK10841
two-component system sensor histidine kinase RcsC;
261-360 2.95e-14

two-component system sensor histidine kinase RcsC;


Pssm-ID: 182772 [Multi-domain]  Cd Length: 924  Bit Score: 75.40  E-value: 2.95e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28056667  261 LQQCLLNLALNAIHAMPTGgCLTLVAQRhDGDRICISVTDTGIGMSEETRARLFSPFF------TTKSDGTGLGLISCKR 334
Cdd:PRK10841 563 LQQVISNLLSNAIKFTDTG-CIVLHVRV-DGDYLSFRVRDTGVGIPAKEVVRLFDPFFqvgtgvQRNFQGTGLGLAICEK 640
                         90       100
                 ....*....|....*....|....*.
gi 28056667  335 IAESYGGLIQVCSELGVGTRFDLILP 360
Cdd:PRK10841 641 LINMMDGDISVDSEPGMGSQFTIRIP 666
PRK11100 PRK11100
sensory histidine kinase CreC; Provisional
211-363 4.17e-14

sensory histidine kinase CreC; Provisional


Pssm-ID: 236846 [Multi-domain]  Cd Length: 475  Bit Score: 74.50  E-value: 4.17e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28056667  211 RGSNKPRERVLLADLFQTV------QLLLRSsvpdcIALRIEECDeyLSVEANYTELQQCLLNLALNAIHAMPTGGCLTL 284
Cdd:PRK11100 320 RQELEVLEPVALAALLEELveareaQAAAKG-----ITLRLRPDD--ARVLGDPFLLRQALGNLLDNAIDFSPEGGTITL 392
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28056667  285 VAQRHdGDRICISVTDTGIGMSEETRARLFSPFFTT-------KSdgTGLGLISCKRIAESYGGLIQVCSELGVGTRFDL 357
Cdd:PRK11100 393 SAEVD-GEQVALSVEDQGPGIPDYALPRIFERFYSLprpangrKS--TGLGLAFVREVARLHGGEVTLRNRPEGGVLATL 469

                 ....*.
gi 28056667  358 ILPARA 363
Cdd:PRK11100 470 TLPRHF 475
HATPase_DpiB-CitA-like cd16915
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
265-360 5.60e-14

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: 67.70  E-value: 5.60e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28056667 265 LLNLALNAIHAMPTGGCLTLVAQRHDGDRICISVTDTGIGMSEETRARLFSPFFTTKSDGT-GLGLISCKRIAESYGGLI 343
Cdd:cd16915   8 LIDNALDALAATGAPNKQVEVFLRDEGDDLVIEVRDTGPGIAPELRDKVFERGVSTKGQGErGIGLALVRQSVERLGGSI 87
                        90
                ....*....|....*..
gi 28056667 344 QVCSELGVGTRFDLILP 360
Cdd:cd16915  88 TVESEPGGGTTFSIRIP 104
AtoC COG2204
DNA-binding transcriptional response regulator, NtrC family, contains REC, AAA-type ATPase, ...
18-156 1.18e-13

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: 72.69  E-value: 1.18e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28056667  18 DSLEDAKLLFNTLREAGLDgsferVESESALREALYLFA---PDIVLSDLSMSGFHGYQALRVVREVG-NTPFIFVSSKM 93
Cdd:COG2204  10 DDPDIRRLLKELLERAGYE-----VETAASGEEALALLReepPDLVLLDLRMPGMDGLELLRELRALDpDLPVILLTGYG 84
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 28056667  94 GEDIAVEALQEGANDYIIK-QNLVRLPSAVTRAVRESRAELERQHV-----ESELMraQRLESLAMLAA 156
Cdd:COG2204  85 DVETAVEAIKAGAFDYLTKpFDLEELLAAVERALERRRLRRENAEDsgligRSPAM--QEVRRLIEKVA 151
COG4192 COG4192
Signal transduction histidine kinase regulating phosphoglycerate transport system [Signal ...
123-349 1.40e-13

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


Pssm-ID: 443346 [Multi-domain]  Cd Length: 640  Bit Score: 73.18  E-value: 1.40e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28056667 123 TRAVRESRAELERQHVESELMRAQRLESLAMLAAGFSHDLRNILQPLLI----VPDLLAGRTDDPQLHQLVSIVAECGRR 198
Cdd:COG4192 405 TEIEERKRIEKNLRQTQDELIQAAKMAVVGQTMTSLAHELNQPLNAMSMylfsAKKALEQENYAQLPTSLDKIEGLIERM 484
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28056667 199 GHeMAESILSFVRGSNKPRERVLLADLFQTVQLLLRS-SVPDCIALRIEEcdeYLSVEANYTELQQCLLNLALNAIHAMP 277
Cdd:COG4192 485 DK-IIKSLRQFSRKSDTPLQPVDLRQVIEQAWELVESrAKPQQITLHIPD---DLMVQGDQVLLEQVLVNLLVNALDAVA 560
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 28056667 278 TGGCLTLVAQRHDGDrICISVTDTGIGMseETRARLFSPFFTTKSDGTGLGLISCKRIAESYGGLIQVCSEL 349
Cdd:COG4192 561 TQPQISVDLLSNAEN-LRVAISDNGNGW--PLVDKLFTPFTTTKEVGLGLGLSICRSIMQQFGGDLYLASTL 629
PleD COG3706
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate ...
18-112 2.51e-13

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: 68.01  E-value: 2.51e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28056667  18 DSLEDAKLLFNTLREAGLDgsFERVES-ESALrEALYLFAPDIVLSDLSMSGFHGYQALRVVREV---GNTPFIFVSSKM 93
Cdd:COG3706   9 DDPTNRKLLRRLLEAAGYE--VVEAADgEEAL-ELLQEHRPDLILLDLEMPDMDGLELCRRLRADprtADIPIIFLTALD 85
                        90
                ....*....|....*....
gi 28056667  94 GEDIAVEALQEGANDYIIK 112
Cdd:COG3706  86 DEEDRARALEAGADDYLTK 104
REC cd00156
phosphoacceptor receiver (REC) domain of response regulators (RRs) and pseudo response ...
18-112 6.31e-13

phosphoacceptor receiver (REC) domain of response regulators (RRs) and pseudo response regulators (PRRs); Two-component systems (TCSs) involving a sensor and a response regulator are used by bacteria to adapt to changing environments. Processes regulated by two-component systems in bacteria include sporulation, pathogenicity, virulence, chemotaxis, and membrane transport. Response regulators (RRs) share the common phosphoacceptor REC domain and different effector/output domains such as DNA, RNA, ligand-binding, protein-binding, or enzymatic domains. Response regulators regulate transcription, post-transcription or post-translation, or have functions such as methylesterases, adenylate or diguanylate cyclase, c-di-GMP-specific phosphodiesterases, histidine kinases, serine/threonine protein kinases, and protein phosphatases, depending on their output domains. The function of some output domains are still unknown. TCSs are found in all three domains of life - bacteria, archaea, and eukaryotes, however, the presence and abundance of particular RRs vary between the lineages. Archaea encode very few RRs with DNA-binding output domains; most are stand-alone REC domains. Among eukaryotes, TCSs are found primarily in protozoa, fungi, algae, and green plants. REC domains function as phosphorylation-mediated switches within RRs, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381085 [Multi-domain]  Cd Length: 99  Bit Score: 64.56  E-value: 6.31e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28056667  18 DSLEDAKLLFNTLREAGLDgsFERVESESALREALYLFAPDIVLSDLSMSGFHGYQALRVVREVG-NTPFIFVSSKMGED 96
Cdd:cd00156   5 DDPAIRELLKSLLEREGYE--VDTAADGEEALELLREERPDLVLLDLMMPGMDGLELLRKLRELPpDIPVIVLTAKADEE 82
                        90
                ....*....|....*.
gi 28056667  97 IAVEALQEGANDYIIK 112
Cdd:cd00156  83 DAVRALELGADDYLVK 98
PRK09959 PRK09959
acid-sensing system histidine kinase EvgS;
249-486 7.15e-13

acid-sensing system histidine kinase EvgS;


Pssm-ID: 182169 [Multi-domain]  Cd Length: 1197  Bit Score: 71.30  E-value: 7.15e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28056667   249 DEYLsVEANYTELQQCLLNLALNAIHAMPTGGCLTLVAQRHDGDR---ICISVTDTGIGMSEETRARLFSPFFTT----K 321
Cdd:PRK09959  818 DHYL-VKIDPQAFKQVLSNLLSNALKFTTEGAVKITTSLGHIDDNhavIKMTIMDSGSGLSQEEQQQLFKRYSQTsagrQ 896
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28056667   322 SDGTGLGLISCKRIAESYGGLIQVCSELGVGTRFDLILPA---RAPASRVSEENVPVVLGHGQRILIVDGEATRLSLLGN 398
Cdd:PRK09959  897 QTGSGLGLMICKELIKNMQGDLSLESHPGIGTTFTITIPVeisQQVATVEAKAEQPITLPEKLSILIADDHPTNRLLLKR 976
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28056667   399 ALASQGYQPQLAPDGGAAL-KLLRHHAepDLVIIDSDILLLSAVCLLPTMQELGYRGPAIVLEDAGQPLRREhfsKDLAV 477
Cdd:PRK09959  977 QLNLLGYDVDEATDGVQALhKVSMQHY--DLLITDVNMPNMDGFELTRKLREQNSSLPIWGLTANAQANERE---KGLSC 1051
                         250
                  ....*....|..
gi 28056667   478 HM---LRKPLEM 486
Cdd:PRK09959 1052 GMnlcLFKPLTL 1063
PRK09303 PRK09303
histidine kinase;
145-360 7.68e-13

histidine kinase;


Pssm-ID: 236462 [Multi-domain]  Cd Length: 380  Bit Score: 69.98  E-value: 7.68e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28056667  145 AQRLES----LAMLAagfsHDLRNILQPLLIVPDLLAGRTDDPQLHQLVSIVA---ECGRRGHEMAES----ILSFVRGS 213
Cdd:PRK09303 145 LEQLKFkdrvLAMLA----HDLRTPLTAASLALETLELGQIDEDTELKPALIEqlqDQARRQLEEIERlitdLLEVGRTR 220
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28056667  214 N-----KPRERVL----------LADLFQTVQLLLRSSVPDCIALrieecdeylsVEANYTELQQCLLNLALNAIHAMPT 278
Cdd:PRK09303 221 WealrfNPQKLDLgslcqevileLEKRWLAKSLEIQTDIPSDLPS----------VYADQERIRQVLLNLLDNAIKYTPE 290
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28056667  279 GGCLTLVAQRHDGDRICISVTDTGIGMSEETRARLFSPFFTTKSD----GTGLGLISCKRIAESYGGLIQVCSELGVGTR 354
Cdd:PRK09303 291 GGTITLSMLHRTTQKVQVSICDTGPGIPEEEQERIFEDRVRLPRDegteGYGIGLSVCRRIVRVHYGQIWVDSEPGQGSC 370

                 ....*.
gi 28056667  355 FDLILP 360
Cdd:PRK09303 371 FHFTLP 376
PRK11107 PRK11107
hybrid sensory histidine kinase BarA; Provisional
261-495 1.21e-12

hybrid sensory histidine kinase BarA; Provisional


Pssm-ID: 236848 [Multi-domain]  Cd Length: 919  Bit Score: 70.26  E-value: 1.21e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28056667  261 LQQCLLNLALNAIHAMPTGGC---LTLVAQRHDGDRICISVTDTGIGMSEETRARLFSPFftTKSD--------GTGLGL 329
Cdd:PRK11107 409 LQQIITNLVGNAIKFTESGNIdilVELRALSNTKVQLEVQIRDTGIGISERQQSQLFQAF--RQADasisrrhgGTGLGL 486
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28056667  330 ISCKRIAESYGGLIQVCSELGVGTRFDLILPARAPASRVSEEnVPVVLGHGQRILIVdgEAtrlsllgNALASQGYQPQL 409
Cdd:PRK11107 487 VITQKLVNEMGGDISFHSQPNRGSTFWFHLPLDLNPNPIIDG-LPTDCLAGKRLLYV--EP-------NSAAAQATLDIL 556
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28056667  410 APDGgaaLKLLRHHAEPDLVIIDSDILLLS-AVCLLPTMQELGYR--------GPAIVLEDAGQPLRREHFSKDLAVHML 480
Cdd:PRK11107 557 SETP---LEVTYSPTLSQLPEAHYDILLLGlPVTFREPLTMLHERlakaksmtDFLILALPCHEQVLAEQLKQDGADACL 633
                        250
                 ....*....|....*
gi 28056667  481 RKPLEMWRVFRAVAY 495
Cdd:PRK11107 634 SKPLSHTRLLPALLE 648
HATPase_FilI-like cd16921
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
261-360 1.27e-12

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: 63.89  E-value: 1.27e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28056667 261 LQQCLLNLALNAIHAMPTGGCLTL-VAQRHDGDRICISVTDTGIGMSEETRARLFSPFFTTKSD----GTGLGLISCKRI 335
Cdd:cd16921   1 LGQVLTNLLGNAIKFRRPRRPPRIeVGAEDVGEEWTFYVRDNGIGIDPEYAEKVFGIFQRLHSReeyeGTGVGLAIVRKI 80
                        90       100
                ....*....|....*....|....*
gi 28056667 336 AESYGGLIQVCSELGVGTRFDLILP 360
Cdd:cd16921  81 IERHGGRIWLESEPGEGTTFYFTLP 105
HATPase_Glnl-NtrB-like cd16918
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
261-360 4.61e-12

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: 62.42  E-value: 4.61e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28056667 261 LQQCLLNLALNAIHAMP-TGGCLTL-------VAQRHDGDRIC--ISVTDTGIGMSEETRARLFSPFFTTKSDGTGLGLI 330
Cdd:cd16918   1 LIQVFLNLVRNAAQALAgSGGEIILrtrtqrqVTLGHPRHRLAlrVSVIDNGPGIPPDLQDTIFYPMVSGRENGTGLGLA 80
                        90       100       110
                ....*....|....*....|....*....|
gi 28056667 331 SCKRIAESYGGLIQVCSELGvGTRFDLILP 360
Cdd:cd16918  81 IAQNIVSQHGGVIECDSQPG-HTVFSVSLP 109
PRK11086 PRK11086
sensory histidine kinase DcuS; Provisional
259-360 6.02e-12

sensory histidine kinase DcuS; Provisional


Pssm-ID: 236839 [Multi-domain]  Cd Length: 542  Bit Score: 67.63  E-value: 6.02e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28056667  259 TELQQCLLNLALNAIHAM-PTGGCLTLVAQRHDGDRICISVTDTGIGMSEETRARLFSPFFTTKSDGTGLGLISCKRIAE 337
Cdd:PRK11086 432 HELITILGNLIENALEAVgGEEGGEISVSLHYRNGWLHCEVSDDGPGIAPDEIDAIFDKGYSTKGSNRGVGLYLVKQSVE 511
                         90       100
                 ....*....|....*....|...
gi 28056667  338 SYGGLIQVCSELGVGTRFDLILP 360
Cdd:PRK11086 512 NLGGSIAVESEPGVGTQFFVQIP 534
YesM COG2972
Sensor histidine kinase YesM [Signal transduction mechanisms];
132-362 6.16e-12

Sensor histidine kinase YesM [Signal transduction mechanisms];


Pssm-ID: 442211 [Multi-domain]  Cd Length: 445  Bit Score: 67.35  E-value: 6.16e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28056667 132 ELERQHVESELMRaQRLESLAMLAAGFSHDLRNILqpllivpDLLAG--RTDDPQlhqlvsivaecgrRGHEMAESILSF 209
Cdd:COG2972 227 ELIEEVYELELEK-KEAELKALQAQINPHFLFNTL-------NSIRWlaELEDPE-------------EAEEMLEALSKL 285
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28056667 210 VRGS-NKPRERVLLADLFQTVQLLL---RSSVPDCIALRIEECDEYLSVEanytelqqcLLNLAL-----NAI-HA---M 276
Cdd:COG2972 286 LRYSlSKGDELVTLEEELELIKSYLeiqKLRFGDRLEVEIEIDEELLDLL---------IPKLILqplveNAIeHGiepK 356
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28056667 277 PTGGCLTLVAQRhDGDRICISVTDTGIGMSEETRARLFSPfFTTKSDGTGLGLIS-CKRIAESYGG--LIQVCSELGVGT 353
Cdd:COG2972 357 EGGGTIRISIRK-EGDRLVITVEDNGVGMPEEKLEKLLEE-LSSKGEGRGIGLRNvRERLKLYYGEeyGLEIESEPGEGT 434

                ....*....
gi 28056667 354 RFDLILPAR 362
Cdd:COG2972 435 TVTIRIPLE 443
YesN COG4753
Two-component response regulator, YesN/AraC family, consists of REC and AraC-type DNA-binding ...
39-112 6.67e-12

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


Pssm-ID: 443786 [Multi-domain]  Cd Length: 103  Bit Score: 61.71  E-value: 6.67e-12
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 28056667  39 FERVESESALREALYLFA---PDIVLSDLSMSGFHGYQALRVVREVG-NTPFIFVSSKMGEDIAVEALQEGANDYIIK 112
Cdd:COG4753  25 FEVVGEAENGEEALELLEehkPDLVITDINMPGMDGLELLEAIRELDpDTKIIILSGYSDFEYAQEAIKLGADDYLLK 102
OmpR COG0745
DNA-binding response regulator, OmpR family, contains REC and winged-helix (wHTH) domain ...
18-112 7.55e-12

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


Pssm-ID: 440508 [Multi-domain]  Cd Length: 204  Bit Score: 64.59  E-value: 7.55e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28056667  18 DSLEDAKLLFNTLREAGLdgsfeRVESESALREALYLFA---PDIVLSDLSMSGFHGYQALRVVREVG-NTPFIFVSSKM 93
Cdd:COG0745   9 DDPDIRELLADALEREGY-----EVDTAADGEEALELLEeerPDLILLDLMLPGMDGLEVCRRLRARPsDIPIIMLTARD 83
                        90
                ....*....|....*....
gi 28056667  94 GEDIAVEALQEGANDYIIK 112
Cdd:COG0745  84 DEEDRVRGLEAGADDYLTK 102
CheY COG0784
CheY-like REC (receiver) domain, includes chemotaxis protein CheY and sporulation regulator ...
18-131 1.80e-11

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: 61.40  E-value: 1.80e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28056667  18 DSLEDAKLLFNTLREAGLDgsFERVES-ESALrEALYLFAPDIVLSDLSMSGFHGYQALRVVREV---GNTPFIFVSSKM 93
Cdd:COG0784  13 DNPDNRELLRRLLERLGYE--VTTAEDgAEAL-ELLRAGPPDLILLDINMPGMDGLELLRRIRALprlPDIPIIALTAYA 89
                        90       100       110
                ....*....|....*....|....*....|....*....
gi 28056667  94 GEDIAVEALQEGANDYIIKQ-NLVRLPSAVTRAVRESRA 131
Cdd:COG0784  90 DEEDRERALEAGADDYLTKPvDPEELLEALRRLLARASA 128
HATPase_TutC-TodS-like cd16925
Histidine kinase-like ATPase domain of hybrid sensor histidine kinases similar to Pseudomonas ...
261-360 3.66e-11

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: 60.20  E-value: 3.66e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28056667 261 LQQCLLNLALNAIHAMPTGGCLTLVAQRHDGDRICISVTDTGIGMSEETRARLFSPF------FTTKSDGTGLGLISCKR 334
Cdd:cd16925   5 YERVVLNLLSNAFKFTPDGGRIRCILEKFRLNRFLLTVSDSGPGIPPNLREEIFERFrqgdgsSTRAHGGTGLGLSIVKE 84
                        90       100
                ....*....|....*....|....*.
gi 28056667 335 IAESYGGLIQVCSELGVGTRFDLILP 360
Cdd:cd16925  85 FVELHGGTVTVSDAPGGGALFQVELP 110
HATPase_BceS-YxdK-YvcQ-like cd16948
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
271-360 3.73e-11

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: 59.99  E-value: 3.73e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28056667 271 NAIHAMPTGGCLTLVAQrHDGDRICISVTDTGIGMSEETRARLFSPFFTTKSD-----GTGLGLISCKRIAESYGGLIQV 345
Cdd:cd16948  16 NALKYSKQGGKIEIYSE-TNEQGVVLSIKDFGIGIPEEDLPRVFDKGFTGENGrnfqeSTGMGLYLVKKLCDKLGHKIDV 94
                        90
                ....*....|....*
gi 28056667 346 CSELGVGTRFDLILP 360
Cdd:cd16948  95 ESEVGEGTTFTITFP 109
REC_RssB-like cd17555
phosphoacceptor receiver (REC) domain of Pseudomonas aeruginosa RssB and similar domains; ...
36-125 4.94e-11

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


Pssm-ID: 381107 [Multi-domain]  Cd Length: 116  Bit Score: 59.91  E-value: 4.94e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28056667  36 DGSFERVESESAlREALYLFA---PDIVLSDLSMSGFHGYQALRVVREVG-NTPFIFVSSKMGEDIAVEALQEGANDYII 111
Cdd:cd17555  22 DSGFQVLQAADG-RQGLELFRseqPDLVLCDLRMPEMDGLEVLKQITKESpDTPVIVVSGAGVMSDAVEALRLGAWDYLT 100
                        90
                ....*....|....*.
gi 28056667 112 K--QNLVRLPSAVTRA 125
Cdd:cd17555 101 KpiEDLAVLEHAVRRA 116
HATPase_BaeS-like cd16946
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
261-360 1.64e-10

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 BaeS HK of the BaeS/BaeR two-component regulatory system (TCS), which responds to envelope stress. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA), and a HAMP sensory domain.


Pssm-ID: 340422 [Multi-domain]  Cd Length: 109  Bit Score: 58.24  E-value: 1.64e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28056667 261 LQQCLLNLALNAIHAMPTGGCLTLVAQRHDgDRICISVTDTGIGMSEETRARLFSPFFTTKSD------GTGLGLISCKR 334
Cdd:cd16946   5 LQQLFVNLLENSLRYTDTGGKLRIRAAQTP-QEVRLDVEDSAPGVSDDQLARLFERFYRVESSrnrasgGSGLGLAICHN 83
                        90       100
                ....*....|....*....|....*..
gi 28056667 335 IAESYGGLIQVC-SELGvGTRFDLILP 360
Cdd:cd16946  84 IALAHGGTISAEhSPLG-GLRLVLTLP 109
Response_reg pfam00072
Response regulator receiver domain; This domain receives the signal from the sensor partner in ...
23-122 2.65e-10

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: 57.55  E-value: 2.65e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28056667    23 AKLLFNTLREAGLdgsfeRVESESALREALYLF---APDIVLSDLSMSGFHGYQALRVVREVG-NTPFIFVSSKMGEDIA 98
Cdd:pfam00072  11 RELLRQLLEKEGY-----VVAEADDGKEALELLkeeRPDLILLDINMPGMDGLELLKRIRRRDpTTPVIILTAHGDEDDA 85
                          90       100
                  ....*....|....*....|....*
gi 28056667    99 VEALQEGANDYIIKQ-NLVRLPSAV 122
Cdd:pfam00072  86 VEALEAGADDFLSKPfDPDELLAAI 110
CitB COG4565
DNA-binding response regulator DpiB of citrate/malate metabolism [Transcription, Signal ...
18-137 2.90e-10

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


Pssm-ID: 443622 [Multi-domain]  Cd Length: 138  Bit Score: 58.44  E-value: 2.90e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28056667  18 DSLEDAKLLFNTLREaglDGSFERVESESALREALYLFA---PDIVLSDLSMSGFHGYQALRVVREVG-NTPFIFVSSKM 93
Cdd:COG4565  11 DDPMVAELLRRYLER---LPGFEVVGVASSGEEALALLAehrPDLILLDIYLPDGDGLELLRELRARGpDVDVIVITAAR 87
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 28056667  94 GEDIAVEALQEGANDYIIKQ-NLVRLPSAVTRAVRESRAELERQH 137
Cdd:COG4565  88 DPETVREALRAGVVDYLIKPfTFERLREALERYLEYRRLLREDQE 132
REC_OmpR cd17574
phosphoacceptor receiver (REC) domain of OmpR family response regulators; OmpR-like proteins ...
23-112 7.47e-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: 55.88  E-value: 7.47e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28056667  23 AKLLFNTLREAGLdgsfeRVESESALREALYLFA---PDIVLSDLSMSGFHGYQALRVVREVG-NTPFIFVSSKMGEDIA 98
Cdd:cd17574  10 AELLSDYLEKEGY-----EVDTAADGEEALELAReeqPDLIILDVMLPGMDGFEVCRRLREKGsDIPIIMLTAKDEEEDK 84
                        90
                ....*....|....
gi 28056667  99 VEALQEGANDYIIK 112
Cdd:cd17574  85 VLGLELGADDYITK 98
HATPase_CpxA-like cd16949
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
261-361 1.45e-09

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: 55.41  E-value: 1.45e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28056667 261 LQQCLLNLALNAIHAMPTggcLTLVAQRHDGDRICISVTDTGIGMSEETRARLFSPFF------TTKSDGTGLGLISCKR 334
Cdd:cd16949   1 LARALENVLRNALRYSPS---KILLDISQDGDQWTITITDDGPGVPEDQLEQIFLPFYrvdsarDRESGGTGLGLAIAER 77
                        90       100
                ....*....|....*....|....*..
gi 28056667 335 IAESYGGLIQVCSELGVGTRFDLILPA 361
Cdd:cd16949  78 AIEQHGGKIKASNRKPGGLRVRIWLPA 104
RpfG COG3437
Response regulator c-di-GMP phosphodiesterase, RpfG family, contains REC and HD-GYP domains ...
18-148 2.45e-09

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: 57.48  E-value: 2.45e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28056667  18 DSLEDAKLLFNTLREAGLDgsFERVES-ESALrEALYLFAPDIVLSDLSMSGFHGYQALRVVREVGNT---PFIFVSSKM 93
Cdd:COG3437  14 DDPENLELLRQLLRTLGYD--VVTAESgEEAL-ELLLEAPPDLILLDVRMPGMDGFELLRLLRADPSTrdiPVIFLTALA 90
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 28056667  94 GEDIAVEALQEGANDYIIKQ-NLVRLPSAVTRAVRESRAELERQHVESELMRAQRL 148
Cdd:COG3437  91 DPEDRERALEAGADDYLTKPfDPEELLARVRNALELRRLQRELDDLVLYLKLAAPL 146
HATPase_CreC-like cd16945
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
261-345 2.77e-09

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: 54.39  E-value: 2.77e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28056667 261 LQQCLLNLALNAIHAMPTGGCLTLVAQRhDGDRICISVTDTGIGMSEETRARLFSPFFT-----TKSDGTGLGLISCKRI 335
Cdd:cd16945   5 LRQAINNLLDNAIDFSPEGGLIALQLEA-DTEGIELLVFDEGSGIPDYALNRVFERFYSlprphSGQKSTGLGLAFVQEV 83
                        90
                ....*....|
gi 28056667 336 AESYGGLIQV 345
Cdd:cd16945  84 AQLHGGRITL 93
HATPase_RstB-like cd16939
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
261-361 3.54e-09

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Salmonella typhimurium RstB; This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component sensor histidine kinase (HKs) such as Salmonella typhimurium RstB HK of the RstA-RstB two-component regulatory system (TCS), which regulates expression of the constituents participating in pyrimidine metabolism and iron acquisition, and may be required for regulation of Salmonella motility and invasion. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA), and a HAMP sensor domain.


Pssm-ID: 340416 [Multi-domain]  Cd Length: 104  Bit Score: 54.36  E-value: 3.54e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28056667 261 LQQCLLNLALNAI-HAMPTggclTLVAQRHDGDRICISVTDTGIGMSEETRARLFSPFF------TTKSDGTGLGLISCK 333
Cdd:cd16939   1 MARALDNLLRNALrYAHRT----VRIALLVSGGRLTLIVEDDGPGIPAAARERVFEPFVrldpsrDRATGGFGLGLAIVH 76
                        90       100
                ....*....|....*....|....*....
gi 28056667 334 RIAESYGGLIQVC-SELGvGTRFDLILPA 361
Cdd:cd16939  77 RVALWHGGHVECDdSELG-GACFRLTWPR 104
REC_OmpR_NsrR-like cd18159
phosphoacceptor receiver (REC) domain of Streptococcus agalactiae NsrR-like OmpR family ...
21-112 4.92e-09

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


Pssm-ID: 381143 [Multi-domain]  Cd Length: 113  Bit Score: 54.21  E-value: 4.92e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28056667  21 EDAKLLFNTLREAgLDGSFERVESESALREALYLFA---PDIVLSDLSMSGFHGYQALRVVREVGNTPFIFVSSKMGEDI 97
Cdd:cd18159   5 EDDETIASLLKKH-LEKWGYEVVLIEDFEDVLEEFLqfkPDLVLLDINLPYFDGFYWCREIRQISNVPIIFISSRDDNMD 83
                        90
                ....*....|....*
gi 28056667  98 AVEALQEGANDYIIK 112
Cdd:cd18159  84 QVMAINMGGDDYITK 98
HATPase_YcbM-like cd16947
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
249-359 5.64e-09

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Bacillus subtilis YcbM; This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component sensor histidine kinase (HKs) such as Bacillus subtilis YcbM, a HK of the two-component system YcbM-YcbL. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA).


Pssm-ID: 340423 [Multi-domain]  Cd Length: 125  Bit Score: 54.06  E-value: 5.64e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28056667 249 DEYLSVEANYTELQQCLLNLALNAIHAMPTGGCLTLVAqRHDGDRICISVTDTGIGMSEETRARLFSPFFTTKSD----- 323
Cdd:cd16947   9 DRPIYANANTEALQRILKNLISNAIKYGSDGKFLGMTL-REDEKHVYIDIWDKGKGISETEKDHVFERLYTLEDSrnsak 87
                        90       100       110
                ....*....|....*....|....*....|....*..
gi 28056667 324 -GTGLGLISCKRIAESYGGLIQVCSELGVGTRFDLIL 359
Cdd:cd16947  88 qGNGLGLTITKRLAESMGGSIYVNSKPYEKTVFTVTL 124
REC_PA4781-like cd19920
phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase PA4781 and similar ...
18-112 9.03e-09

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


Pssm-ID: 381147 [Multi-domain]  Cd Length: 103  Bit Score: 52.90  E-value: 9.03e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28056667  18 DSLEDAKLLFNTLREAG------LDGsfervesESALREALYLfAPDIVLSDLSMSGFHGYQALRVVREVGNT---PFIF 88
Cdd:cd19920   6 DVPDNLRLLSELLRAAGyrvlvaTDG-------QQALQRAQAE-PPDLILLDVMMPGMDGFEVCRRLKADPATrhiPVIF 77
                        90       100
                ....*....|....*....|....
gi 28056667  89 VSSKMGEDIAVEALQEGANDYIIK 112
Cdd:cd19920  78 LTALTDTEDKVKGFELGAVDYITK 101
REC_OmpR_KdpE-like cd17620
phosphoacceptor receiver (REC) domain of KdpE-like OmpR family response regulators; KdpE is a ...
21-112 1.70e-08

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


Pssm-ID: 381135 [Multi-domain]  Cd Length: 99  Bit Score: 52.17  E-value: 1.70e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28056667  21 EDAKLLFNTLREAGLDGSFERVESESAlREALYLFA---PDIVLSDLSMSGFHGYQALRVVREVGNTPFIFVSSKMGEDI 97
Cdd:cd17620   5 EDEPQIRRFLRTALEAHGYRVFEAETG-QEGLLEAAtrkPDLIILDLGLPDMDGLEVIRRLREWSAVPVIVLSARDEESD 83
                        90
                ....*....|....*
gi 28056667  98 AVEALQEGANDYIIK 112
Cdd:cd17620  84 KIAALDAGADDYLTK 98
HATPase_EcPhoR-like cd16952
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
261-362 1.96e-08

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Escherichia coli PhoR; This family includes histidine kinase-like ATPase (HATPase) domain of two-component sensor histidine kinases similar to Escherichia coli or Vibrio cholera PhoR, the histidine kinase (HK) of PhoB-PhoR a two-component signal transduction system (TCS) involved in phosphate regulation. PhoR monitors extracellular inorganic phosphate (Pi) availability and PhoB, the response regulator, regulates transcription of genes of the phosphate regulon. PhoR is a bifunctional histidine autokinase/phospho-PhoB phosphatase; in phosphate deficiency, it autophosphorylates and Pi is transferred to PhoB, and when environmental Pi is abundant, it removes the phosphoryl group from phosphorylated PhoB. Other roles of PhoB-PhoR TCS have been described, including motility, biofilm formation, intestinal colonization, and virulence in V. cholera. E.coli PhoR and Bacillus subtilis PhoR (whose HATPase domain belongs to a different family) sense very different signals in each bacterium. In E. coli the PhoR signal comes from phosphate transport mediated by the PstSCAB2 phosphate transporter and the PhoU chaperone-like protein while in B. subtilis, the PhoR activation signal comes from wall teichoic acid (WTA) metabolism.


Pssm-ID: 340428 [Multi-domain]  Cd Length: 108  Bit Score: 52.20  E-value: 1.96e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28056667 261 LQQCLLNLALNAIHAMPTGGCLTLVAQRHD-GDRIciSVTDTGIGMSEETRARLFSPFFTTKSD------GTGLGLISCK 333
Cdd:cd16952   1 LRSAFSNLVSNAVKYTPPSDTITVRWSQEEsGARL--SVEDTGPGIPPEHIPRLTERFYRVDIErcrntgGTGLGLAIVK 78
                        90       100
                ....*....|....*....|....*....
gi 28056667 334 RIAESYGGLIQVCSELGVGTRFDLILPAR 362
Cdd:cd16952  79 HVMSRHDARLLIASELGKGSRFTCLFPSS 107
glnL PRK11073
nitrogen regulation protein NR(II);
154-362 2.30e-08

nitrogen regulation protein NR(II);


Pssm-ID: 182947 [Multi-domain]  Cd Length: 348  Bit Score: 55.86  E-value: 2.30e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28056667  154 LAAGFSHDLRNILQPLLIVPDLLAGRTDDPQLHQLVSIVAECGRRGHEMAESILsfvrGSNKPRERVL--LADLFQTVQL 231
Cdd:PRK11073 133 LVRGLAHEIKNPLGGLRGAAQLLSKALPDPALTEYTKVIIEQADRLRNLVDRLL----GPQRPGTHVTesIHKVAERVVQ 208
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28056667  232 LLRSSVPDCIALrIEECDEYLSVEANYTE-LQQCLLNLALNAIHAM-PTGGC----------LTLVAQRHdgdRIC--IS 297
Cdd:PRK11073 209 LVSLELPDNVRL-IRDYDPSLPELAHDPDqIEQVLLNIVRNALQALgPEGGTitlrtrtafqLTLHGERY---RLAarID 284
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 28056667  298 VTDTGIGMSEETRARLFSPFFTTKSDGTGLGLISCKRIAESYGGLIQVCSELGvGTRFDLILPAR 362
Cdd:PRK11073 285 IEDNGPGIPPHLQDTLFYPMVSGREGGTGLGLSIARNLIDQHSGKIEFTSWPG-HTEFSVYLPIR 348
AtoC COG2204
DNA-binding transcriptional response regulator, NtrC family, contains REC, AAA-type ATPase, ...
382-497 2.30e-08

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: 56.13  E-value: 2.30e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28056667 382 RILIVDGEATRLSLLGNALASQGYQPQLAPDGGAALKLLRHHaEPDLVIidSDILL--LSAVCLLPTMQELGYRGPAIVL 459
Cdd:COG2204   4 RILVVDDDPDIRRLLKELLERAGYEVETAASGEEALALLREE-PPDLVL--LDLRMpgMDGLELLRELRALDPDLPVILL 80
                        90       100       110
                ....*....|....*....|....*....|....*...
gi 28056667 460 EDAGQPLRREHFSKDLAVHMLRKPLEMWRVFRAVAYAL 497
Cdd:COG2204  81 TGYGDVETAVEAIKAGAFDYLTKPFDLEELLAAVERAL 118
phoR PRK11006
phosphate regulon sensor histidine kinase PhoR;
249-362 3.38e-08

phosphate regulon sensor histidine kinase PhoR;


Pssm-ID: 182895 [Multi-domain]  Cd Length: 430  Bit Score: 55.79  E-value: 3.38e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28056667  249 DEYLSVEANYTELQQCLLNLALNAIHAMPTGGCLTlVAQRHDGDRICISVTDTGIGMSEETRARLFSPFF------TTKS 322
Cdd:PRK11006 306 DNSLKVFGNEDQLRSAISNLVYNAVNHTPEGTHIT-VRWQRVPQGAEFSVEDNGPGIAPEHIPRLTERFYrvdkarSRQT 384
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 28056667  323 DGTGLGLISCKRIAESYGGLIQVCSELGVGTRFDLILPAR 362
Cdd:PRK11006 385 GGSGLGLAIVKHALSHHDSRLEIESEVGKGTRFSFVLPER 424
HATPase_BasS-like cd16940
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
261-354 4.65e-08

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: 51.25  E-value: 4.65e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28056667 261 LQQCLLNLALNAIHAMPTGGCLTLVAQRHDGDRICISvtDTGIGMSEETRARLFSPFF---TTKSDGTGLGLISCKRIAE 337
Cdd:cd16940  14 LFLLLRNLVDNAVRYSPQGSRVEIKLSADDGAVIRVE--DNGPGIDEEELEALFERFYrsdGQNYGGSGLGLSIVKRIVE 91
                        90
                ....*....|....*..
gi 28056667 338 SYGGLIQVCSELGVGTR 354
Cdd:cd16940  92 LHGGQIFLGNAQGGGLE 108
PRK11361 PRK11361
acetoacetate metabolism transcriptional regulator AtoC;
49-137 5.17e-08

acetoacetate metabolism transcriptional regulator AtoC;


Pssm-ID: 183099 [Multi-domain]  Cd Length: 457  Bit Score: 55.24  E-value: 5.17e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28056667   49 REALYLFA---PDIVLSDLSMSGFHGYQALRVVREVG-NTPFIFVSSKMGEDIAVEALQEGANDYIIKQ-NLVRLPSAVT 123
Cdd:PRK11361  38 RTALHLFAdihPDVVLMDIRMPEMDGIKALKEMRSHEtRTPVILMTAYAEVETAVEALRCGAFDYVIKPfDLDELNLIVQ 117
                         90
                 ....*....|....*.
gi 28056667  124 RA--VRESRAELERQH 137
Cdd:PRK11361 118 RAlqLQSMKKEIRHLH 133
REC_CheY cd17542
phosphoacceptor receiver (REC) domain of chemotaxis protein CheY; The chemotaxis response ...
21-112 5.95e-08

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: 51.13  E-value: 5.95e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28056667  21 EDAKLLFNTLREAGLDGSFERVESESALREALYLF---APDIVLSDLSMSGFHGYQALRVVREVG-NTPFIFVSSKMGED 96
Cdd:cd17542   7 DDAAFMRMMLKDILTKAGYEVVGEAANGEEAVEKYkelKPDLVTMDITMPEMDGIEALKEIKKIDpNAKVIMCSAMGQEE 86
                        90
                ....*....|....*.
gi 28056667  97 IAVEALQEGANDYIIK 112
Cdd:cd17542  87 MVKEAIKAGAKDFIVK 102
HATPase_CheA-like cd16916
Histidine kinase-like ATPase domain of the chemotaxis protein histidine kinase CheA, and some ...
280-360 1.33e-07

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: 51.43  E-value: 1.33e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28056667 280 GCLTLVAqRHDGDRICISVTDTGIGM---------------SEETRARL---------FSPFFTTKSD-----GTGLGLI 330
Cdd:cd16916  70 GTITLRA-EHQGNQVVIEVSDDGRGIdrekirekaiergliTADEAATLsddevlnliFAPGFSTAEQvtdvsGRGVGMD 148
                        90       100       110
                ....*....|....*....|....*....|
gi 28056667 331 SCKRIAESYGGLIQVCSELGVGTRFDLILP 360
Cdd:cd16916 149 VVKRSIESLGGTIEVESEPGQGTTFTIRLP 178
envZ PRK09467
osmolarity sensor protein; Provisional
246-345 1.52e-07

osmolarity sensor protein; Provisional


Pssm-ID: 236531 [Multi-domain]  Cd Length: 435  Bit Score: 53.76  E-value: 1.52e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28056667  246 EECD------EYLSVEANY-----TELQQCLLNLALNAI-----------HAMPTGGCLTLVAQRHDGDRICISVTDTGI 303
Cdd:PRK09467 292 EMADlnallgEVIAAESGYereieTALQPGPIEVPMNPIaikralanlvvNAARYGNGWIKVSSGTEGKRAWFQVEDDGP 371
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 28056667  304 GMSEETRARLFSPFftTKSD------GTGLGLISCKRIAESYGGLIQV 345
Cdd:PRK09467 372 GIPPEQLKHLFQPF--TRGDsargssGTGLGLAIVKRIVDQHNGKVEL 417
AmiR COG3707
Two-component response regulator, AmiR/NasT family, consists of REC and RNA-binding ...
18-150 1.73e-07

Two-component response regulator, AmiR/NasT family, consists of REC and RNA-binding antiterminator (ANTAR) domains [Signal transduction mechanisms, Transcription];


Pssm-ID: 442921 [Multi-domain]  Cd Length: 194  Bit Score: 51.50  E-value: 1.73e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28056667  18 DSLEDAKLLFNTLREAGLDGSFERVESESALREALYLfAPDIVLSDLSMSGFHGYQALRVVREVGNTPFIFVSSKMGEDI 97
Cdd:COG3707  11 DEPLRRADLREGLREAGYEVVAEAADGEDAVELVREL-KPDLVIVDIDMPDRDGLEAARQISEERPAPVILLTAYSDPEL 89
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 28056667  98 AVEALQEGANDYIIKQ-NLVRLPSAVTRAVRESRaelERQHVESELMRAQ-RLES 150
Cdd:COG3707  90 IERALEAGVSAYLVKPlDPEDLLPALELALARFR---ELRALRRELAKLReALEE 141
RpfG COG3437
Response regulator c-di-GMP phosphodiesterase, RpfG family, contains REC and HD-GYP domains ...
378-497 2.81e-07

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: 51.32  E-value: 2.81e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28056667 378 GHGQRILIVDGEATRLSLLGNALASQGYQPQLAPDGGAALKLLRHHaEPDLVIIDSD------ILLLSAVCLLPTMQELg 451
Cdd:COG3437   4 GQAPTVLIVDDDPENLELLRQLLRTLGYDVVTAESGEEALELLLEA-PPDLILLDVRmpgmdgFELLRLLRADPSTRDI- 81
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 28056667 452 yrgPAIVLEDAGQPLRREHFSKDLAVHMLRKPLEMWRVFRAVAYAL 497
Cdd:COG3437  82 ---PVIFLTALADPEDRERALEAGADDYLTKPFDPEELLARVRNAL 124
OmpR COG0745
DNA-binding response regulator, OmpR family, contains REC and winged-helix (wHTH) domain ...
382-432 3.06e-07

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: 51.11  E-value: 3.06e-07
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|.
gi 28056667 382 RILIVDGEATRLSLLGNALASQGYQPQLAPDGGAALKLLRHHaEPDLVIID 432
Cdd:COG0745   3 RILVVEDDPDIRELLADALEREGYEVDTAADGEEALELLEEE-RPDLILLD 52
CheY COG0784
CheY-like REC (receiver) domain, includes chemotaxis protein CheY and sporulation regulator ...
378-497 3.45e-07

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: 49.08  E-value: 3.45e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28056667 378 GHGQRILIVDGEATRLSLLGNALASQGYQPQLAPDGGAALKLLRHHaEPDLVIIDsdilllsavCLLPTM---------- 447
Cdd:COG0784   3 LGGKRILVVDDNPDNRELLRRLLERLGYEVTTAEDGAEALELLRAG-PPDLILLD---------INMPGMdglellrrir 72
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 28056667 448 -QELGYRGPAIVLEDAGQPLRREHFSKDLAVHMLRKPLEMWRVFRAVAYAL 497
Cdd:COG0784  73 aLPRLPDIPIIALTAYADEEDRERALEAGADDYLTKPVDPEELLEALRRLL 123
PRK10604 PRK10604
sensor protein RstB; Provisional
261-367 4.03e-07

sensor protein RstB; Provisional


Pssm-ID: 236724 [Multi-domain]  Cd Length: 433  Bit Score: 52.30  E-value: 4.03e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28056667  261 LQQCLLNLALNAI-HAmptGGCLTLVAQRhDGDRICISVTDTGIGMSEETRARLFSPFF------TTKSDGTGLGLISCK 333
Cdd:PRK10604 320 MERVLDNLLNNALrYA---HSRVRVSLLL-DGNQACLIVEDDGPGIPPEERERVFEPFVrldpsrDRATGGCGLGLAIVH 395
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 28056667  334 RIAESYGGLIQV-CSELGvGTRFDLILPARAPASR 367
Cdd:PRK10604 396 SIALAMGGSVNCdESELG-GARFSFSWPVWHNLPQ 429
HATPase_EnvZ-like cd16950
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
261-360 4.23e-07

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: 48.21  E-value: 4.23e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28056667 261 LQQCLLNLALNAIHampTGGCLTLVAQRHDGDRICISVTDTGIGMSEETRARLFSPFF----TTKSDGTGLGLISCKRIA 336
Cdd:cd16950   1 LKRVLSNLVDNALR---YGGGWVEVSSDGEGNRTRIQVLDNGPGIAPEEVDELFQPFYrgdnARGTSGTGLGLAIVQRIS 77
                        90       100
                ....*....|....*....|....
gi 28056667 337 ESYGGLIQVCSELGVGTRFDLILP 360
Cdd:cd16950  78 DAHGGSLTLANRAGGGLCARIELP 101
REC_CheY_CheY3 cd19923
phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY3 and similar CheY ...
28-112 4.57e-07

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: 48.49  E-value: 4.57e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28056667  28 NTLREAGldgsFERVESESALREALYLFAP---DIVLSDLSMSGFHGYQALRVVREVGN---TPFIFVSSKMGEDIAVEA 101
Cdd:cd19923  18 NLLKELG----FNNVEEAEDGVDALEKLKAggfDFVITDWNMPNMDGLELLKTIRADGAlshLPVLMVTAEAKKENVIAA 93
                        90
                ....*....|.
gi 28056667 102 LQEGANDYIIK 112
Cdd:cd19923  94 AQAGVNNYIVK 104
PleD COG3706
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate ...
382-432 5.18e-07

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: 49.91  E-value: 5.18e-07
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|.
gi 28056667 382 RILIVDGEATRLSLLGNALASQGYQPQLAPDGGAALKLLRHHaEPDLVIID 432
Cdd:COG3706   3 RILVVDDDPTNRKLLRRLLEAAGYEVVEAADGEEALELLQEH-RPDLILLD 52
REC_typeB_ARR-like cd17584
phosphoacceptor receiver (REC) domain of type B Arabidopsis response regulators (ARRs) and ...
58-112 6.16e-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: 48.01  E-value: 6.16e-07
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*
gi 28056667  58 DIVLSDLSMSGFHGYQALRVVREVGNTPFIFVSSKMGEDIAVEALQEGANDYIIK 112
Cdd:cd17584  46 DLVITDVHMPDMDGFEFLELIRLEMDLPVIMMSADGSTSTVMKGLAHGACDYLLK 100
REC_CheB-like cd17541
phosphoacceptor receiver (REC) domain of chemotaxis response regulator protein-glutamate ...
49-133 1.30e-06

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: 47.39  E-value: 1.30e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28056667  49 REALYLFA---PDIVLSDLSMSGFHGYQALRVVREVGNTPFIFVSS--KMGEDIAVEALQEGANDYIIKqnlvrlPSA-V 122
Cdd:cd17541  36 EEALEKIKelkPDVITLDIEMPVMDGLEALRRIMAERPTPVVMVSSltEEGAEITLEALELGAVDFIAK------PSGgI 109
                        90
                ....*....|.
gi 28056667 123 TRAVRESRAEL 133
Cdd:cd17541 110 SLDLEEIAEEL 120
PRK11517 PRK11517
DNA-binding response regulator HprR;
30-138 1.63e-06

DNA-binding response regulator HprR;


Pssm-ID: 183172 [Multi-domain]  Cd Length: 223  Bit Score: 49.13  E-value: 1.63e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28056667   30 LREAGLdgsfeRVESESALREALYLFAPD---IVLSDLSMSGFHGYQALRVVREVGNTPFIFVSSKMGEDIAVEALQEGA 106
Cdd:PRK11517  20 LSEAGY-----VIDAVSDGRDGLYLALKDdyaLIILDIMLPGMDGWQILQTLRTAKQTPVICLTARDSVDDRVRGLDSGA 94
                         90       100       110
                 ....*....|....*....|....*....|..
gi 28056667  107 NDYIIKqnlvrlPSAVTRAVRESRAELeRQHV 138
Cdd:PRK11517  95 NDYLVK------PFSFSELLARVRAQL-RQHH 119
REC_OmpR_BfmR-like cd19939
phosphoacceptor receiver (REC) domain of BfmR-like OmpR family response regulators; ...
18-112 2.96e-06

phosphoacceptor receiver (REC) domain of BfmR-like OmpR family response regulators; Acinetobacter baumannii BfmR is part of the BfmR/S two-component system that functions as the master regulator of biofilm initiation. BfmR confers resistance to complement-mediated bactericidal activity, independent of capsular polysaccharide, and also increases resistance to the clinically important antimicrobials meropenem and colistin, making it a potential antimicrobial target. Its inhibition would have the dual benefit of significantly decreasing in vivo survival and increasing sensitivity to selected antimicrobials. Members of this subfamily belong to the OmpR family of DNA-binding response regulators, which are characterized by a REC domain and a winged helix-turn-helix (wHTH) DNA-binding output effector domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381166 [Multi-domain]  Cd Length: 116  Bit Score: 46.21  E-value: 2.96e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28056667  18 DSLEDAKLLFNTLREAGLDGSFErVESESALREALYlFAPDIVLSDLSMSGFHGYQALRVVREVGNTPFIFVSSKMGEDI 97
Cdd:cd19939   7 DELELARLTRDYLIKAGLEVSVF-TDGQRAVRRIID-EQPSLVVLDIMLPGMDGLTVCREVREHSHVPILMLTARTEEMD 84
                        90
                ....*....|....*
gi 28056667  98 AVEALQEGANDYIIK 112
Cdd:cd19939  85 RVLGLEMGADDYLCK 99
REC_OmpR_YycF-like cd17614
phosphoacceptor receiver (REC) domain of YrcF-like OmpR family response regulators; YycF ...
49-112 3.24e-06

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


Pssm-ID: 381130 [Multi-domain]  Cd Length: 115  Bit Score: 45.88  E-value: 3.24e-06
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 28056667  49 REAL---YLFAPDIVLSDLSMSGFHGYQALRVVREVGNTPFIFVSSKMGEDIAVEALQEGANDYIIK 112
Cdd:cd17614  32 REALekvEEEQPDLILLDLMLPEKDGLEVCREVRKTSNVPIIMLTAKDSEVDKVLGLELGADDYVTK 98
REC_OmpR_MtrA-like cd17626
phosphoacceptor receiver (REC) domain of MtrA-like OmpR family response regulators; MtrA is ...
23-112 3.32e-06

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


Pssm-ID: 381141 [Multi-domain]  Cd Length: 115  Bit Score: 45.92  E-value: 3.32e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28056667  23 AKLLFNTLREAGLDGSFerVESESALREALYLFAPDIVLSDLSMSGFHGYQALRVVREVGNTPFIFVSSKMGEDIAVEAL 102
Cdd:cd17626  13 AEMIGIVLRGEGFDPAF--CGDGTQALAAFREVRPDLVLLDLMLPGIDGIEVCRQIRAESGVPIVMLTAKSDTVDVVLGL 90
                        90
                ....*....|
gi 28056667 103 QEGANDYIIK 112
Cdd:cd17626  91 ESGADDYVAK 100
PRK10549 PRK10549
two-component system sensor histidine kinase BaeS;
261-367 4.02e-06

two-component system sensor histidine kinase BaeS;


Pssm-ID: 182539 [Multi-domain]  Cd Length: 466  Bit Score: 49.25  E-value: 4.02e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28056667  261 LQQCLLNLALNAIHAMPTGGCLTLVAQRHDgDRICISVTDTGIGMSEETRARLFSPFFTTK------SDGTGLGLISCKR 334
Cdd:PRK10549 353 LMQLFNNLLENSLRYTDSGGSLHISAEQRD-KTLRLTFADSAPGVSDEQLQKLFERFYRTEgsrnraSGGSGLGLAICLN 431
                         90       100       110
                 ....*....|....*....|....*....|....
gi 28056667  335 IAESYGGLIQVC-SELGvGTRFDLILPARAPASR 367
Cdd:PRK10549 432 IVEAHNGRIIAAhSPFG-GVSITVELPLERDLQR 464
PRK10547 PRK10547
chemotaxis protein CheA; Provisional
280-360 4.02e-06

chemotaxis protein CheA; Provisional


Pssm-ID: 236712 [Multi-domain]  Cd Length: 670  Bit Score: 49.34  E-value: 4.02e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28056667  280 GCLTLVAQrHDGDRICISVTDTGIG--------------------MSEETRARL-FSPFFTTKS-----DGTGLGLISCK 333
Cdd:PRK10547 417 GNLILSAE-HQGGNICIEVTDDGAGlnrerilakaasqglavsenMSDEEVGMLiFAPGFSTAEqvtdvSGRGVGMDVVK 495
                         90       100
                 ....*....|....*....|....*..
gi 28056667  334 RIAESYGGLIQVCSELGVGTRFDLILP 360
Cdd:PRK10547 496 RNIQEMGGHVEIQSKQGKGTTIRILLP 522
REC_Rcp-like cd17557
phosphoacceptor receiver (REC) domain of cyanobacterial phytochrome response regulator Rcp and ...
18-112 5.26e-06

phosphoacceptor receiver (REC) domain of cyanobacterial phytochrome response regulator Rcp and similar domains; This family is composed of response regulators (RRs) that are members of phytochrome-associated, light-sensing two-component signal transduction pathways such as Synechocystis sp. Rcp1, Tolypothrix sp. RcpA, and Agrobacterium tumefaciens bacteriophytochrome response regulator AtBRR. They are stand-alone RRs containing only a REC domain with no output/effector domain. The REC domain itself functions as an effector domain. Also included in this family us Methanosaeta harundinacea methanogenesis regulatory protein FilR2, also a stand-alone RR. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381108 [Multi-domain]  Cd Length: 129  Bit Score: 45.87  E-value: 5.26e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28056667  18 DSLEDAKLLFNTLREAGLDGSFERVES-ESAL----REALYLFA--PDIVLSDLSMSGFHGYQALRVVRE--------Vg 82
Cdd:cd17557   7 DNPGDAELIQEAFKEAGVPNELHVVRDgEEALdflrGEGEYADAprPDLILLDLNMPRMDGFEVLREIKAdpdlrripV- 85
                        90       100       110
                ....*....|....*....|....*....|
gi 28056667  83 ntpFIFVSSKMGEDIaVEALQEGANDYIIK 112
Cdd:cd17557  86 ---VVLTTSDAEEDI-ERAYELGANSYIVK 111
REC_CheV-like cd19924
phosphoacceptor receiver (REC) domain of chemotaxis protein CheV and similar proteins; This ...
18-112 5.59e-06

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: 45.45  E-value: 5.59e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28056667  18 DSLEDAKLLFNTLREAGLDgSFERVESESALrEALYLFAP---------DIVLSDLSMSGFHGYQALRVVRE---VGNTP 85
Cdd:cd19924   6 DSPTARKQLRDLLKNLGFE-IAEAVDGEEAL-NKLENLAKegndlskelDLIITDIEMPKMDGYELTFELRDdprLANIP 83
                        90       100
                ....*....|....*....|....*..
gi 28056667  86 FIFVSSKMGEDIAVEALQEGANDYIIK 112
Cdd:cd19924  84 VILNSSLSGEFSRARGKKVGADAYLAK 110
REC cd00156
phosphoacceptor receiver (REC) domain of response regulators (RRs) and pseudo response ...
384-483 6.10e-06

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: 44.91  E-value: 6.10e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28056667 384 LIVDGEATRLSLLGNALASQGYQPQLAPDGGAALKLLRHHAePDLVIIDSDILLLSAVCLLPTMQELGYRGPAIVLEDAG 463
Cdd:cd00156   1 LIVDDDPAIRELLKSLLEREGYEVDTAADGEEALELLREER-PDLVLLDLMMPGMDGLELLRKLRELPPDIPVIVLTAKA 79
                        90       100
                ....*....|....*....|
gi 28056667 464 QPLRREHFSKDLAVHMLRKP 483
Cdd:cd00156  80 DEEDAVRALELGADDYLVKP 99
REC_NarL-like cd17535
phosphoacceptor receiver (REC) domain of NarL (Nitrate/Nitrite response regulator L) family ...
31-112 7.57e-06

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: 45.20  E-value: 7.57e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28056667  31 REAGLDGSFERVESESALReALYLFAPDIVLSDLSMSGFHGYQAL-RVVREVGNTPFIFVSSKMGEDIAVEALQEGANDY 109
Cdd:cd17535  20 SEPDIEVVGEAADGEEALA-LLRELRPDVVLMDLSMPGMDGIEALrRLRRRYPDLKVIVLTAHDDPEYVLRALKAGAAGY 98

                ...
gi 28056667 110 IIK 112
Cdd:cd17535  99 LLK 101
REC_D1_PleD-like cd17538
first (D1) phosphoacceptor receiver (REC) domain of response regulator PleD and similar ...
382-432 8.24e-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: 44.41  E-value: 8.24e-06
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|.
gi 28056667 382 RILIVDGEATRLSLLGNALASQGYQPQLAPDGGAALKLLRHHaEPDLVIID 432
Cdd:cd17538   1 KILVVDDEPANRELLEALLSAEGYEVLTADSGQEALALAEEE-LPDLILLD 50
REC_OmpR_DrrD-like cd17625
phosphoacceptor receiver (REC) domain of DrrD-like OmpR family response regulators; DrrD is a ...
45-112 8.58e-06

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: 44.90  E-value: 8.58e-06
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28056667  45 ESALREALY-LFapDIVLSDLSMSGFHGYQALRVVREVGN-TPFIFVSSKMGEDIAVEALQEGANDYIIK 112
Cdd:cd17625  31 EEGLEYALSgIY--DLIILDIMLPGMDGLEVLKSLREEGIeTPVLLLTALDAVEDRVKGLDLGADDYLPK 98
AmiR COG3707
Two-component response regulator, AmiR/NasT family, consists of REC and RNA-binding ...
380-497 8.92e-06

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: 46.49  E-value: 8.92e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28056667 380 GQRILIVDGEATRLSLLGNALASQGYQP-QLAPDGGAALKLLRHHaEPDLVIIDSDILLLSAVCLLPTMQELGYRgPAIV 458
Cdd:COG3707   3 GLRVLVVDDEPLRRADLREGLREAGYEVvAEAADGEDAVELVREL-KPDLVIVDIDMPDRDGLEAARQISEERPA-PVIL 80
                        90       100       110
                ....*....|....*....|....*....|....*....
gi 28056667 459 LEDAGQPLRREHFSKDLAVHMLRKPLEMWRVFRAVAYAL 497
Cdd:COG3707  81 LTAYSDPELIERALEAGVSAYLVKPLDPEDLLPALELAL 119
REC_RpfG-like cd17551
phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase response regulator ...
30-112 9.03e-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: 44.74  E-value: 9.03e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28056667  30 LREAGldgsFERVESESALREALYLFA---PDIVLSDLSMSGFHGYQALRVVREV---GNTPFIFVSSKMGEDIAVEALQ 103
Cdd:cd17551  20 LRSAG----YLEVVSFTDPREALAWCRenpPDLILLDYMMPGMDGLEFIRRLRALpglEDVPIVMITADTDREVRLRALE 95

                ....*....
gi 28056667 104 EGANDYIIK 112
Cdd:cd17551  96 AGATDFLTK 104
COG4567 COG4567
DNA-binding response regulator, ActR/RegA family, consists of REC and Fis-type HTH domains ...
381-432 1.14e-05

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: 45.68  E-value: 1.14e-05
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 28056667 381 QRILIVDGEATRLSLLGNALASQGYQPQLAPDGGAALKLLRHHAePDLVIID 432
Cdd:COG4567   5 RSLLLVDDDEAFARVLARALERRGFEVTTAASVEEALALLEQAP-PDYAVLD 55
REC smart00448
cheY-homologous receiver domain; CheY regulates the clockwise rotation of E. coli flagellar ...
382-432 1.16e-05

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


Pssm-ID: 214668 [Multi-domain]  Cd Length: 55  Bit Score: 42.56  E-value: 1.16e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 28056667    382 RILIVDGEATRLSLLGNALASQGYQPQLAPDGGAALKLLRHHaEPDLVIID 432
Cdd:smart00448   2 RILVVDDDPLLRELLKALLEKEGYEVDEATDGEEALELLKEE-KPDLILLD 51
FixJ COG4566
DNA-binding response regulator, FixJ family, consists of REC and HTH domains [Signal ...
43-159 1.38e-05

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


Pssm-ID: 443623 [Multi-domain]  Cd Length: 196  Bit Score: 45.86  E-value: 1.38e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28056667  43 ESESALREALYLFAPDIVLSDLSMSGFHGYQALRVVREVGNT-PFIFVSskmGE-DI--AVEALQEGANDYIIK----QN 114
Cdd:COG4566  30 ASAEAFLAALDPDRPGCLLLDVRMPGMSGLELQEELAARGSPlPVIFLT---GHgDVpmAVRAMKAGAVDFLEKpfddQA 106
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 28056667 115 LVRlpsAVTRAVRESRAELERQHVESELmrAQRLESL--------AMLAAGFS 159
Cdd:COG4566 107 LLD---AVRRALARDRARRAERARRAEL--RARLASLtprerevlDLVVAGLS 154
PRK10618 PRK10618
phosphotransfer intermediate protein in two-component regulatory system with RcsBC; Provisional
292-371 1.74e-05

phosphotransfer intermediate protein in two-component regulatory system with RcsBC; Provisional


Pssm-ID: 236726 [Multi-domain]  Cd Length: 894  Bit Score: 47.62  E-value: 1.74e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28056667  292 DRICISVTDTGIGMSEETRARLFSPFFT-TKSD----GTGLGLISCKRIAESYGGLIQVCSELGVGTRFDLILPARAPAS 366
Cdd:PRK10618 598 DRLTIRILDTGAGVSIKELDNLHFPFLNqTQGDrygkASGLTFFLCNQLCRKLGGHLTIKSREGLGTRYSIHLKMLAADP 677

                 ....*
gi 28056667  367 RVSEE 371
Cdd:PRK10618 678 EVEEE 682
REC_DctD-like cd17549
phosphoacceptor receiver (REC) domain of C4-dicarboxylic acid transport protein D (DctD) and ...
29-142 1.75e-05

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: 44.40  E-value: 1.75e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28056667  29 TLREAGLdgsfeRVESESALREALYLFAPD---IVLSDLSMSGFHGYQALRVVREVGNT-PFIFVSskmGE-DI--AVEA 101
Cdd:cd17549  17 TLELAGF-----RVRAFADAEEALAALSPDfpgVVISDIRMPGMDGLELLAQIRELDPDlPVILIT---GHgDVpmAVEA 88
                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 28056667 102 LQEGANDYIIKQ-NLVRLPSAVTRAVRESRAELERQHVESEL 142
Cdd:cd17549  89 MRAGAYDFLEKPfDPERLLDVVRRALEKRRLVLENRRLRQQL 130
REC_OmpR_RegX3-like cd17621
phosphoacceptor receiver (REC) domain of RegX3-like OmpR family response regulators; RegX3 is ...
58-112 2.00e-05

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


Pssm-ID: 381136 [Multi-domain]  Cd Length: 99  Bit Score: 43.34  E-value: 2.00e-05
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*
gi 28056667  58 DIVLSDLSMSGFHGYQALRVVREVGNTPFIFVSSKMGEDIAVEALQEGANDYIIK 112
Cdd:cd17621  44 DIVLLDLMLPGLSGTEVCRQLRARSNVPVIMVTAKDSEIDKVVGLELGADDYVTK 98
LytT COG3279
DNA-binding response regulator, LytR/AlgR family [Transcription, Signal transduction ...
45-142 2.00e-05

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


Pssm-ID: 442510 [Multi-domain]  Cd Length: 235  Bit Score: 45.96  E-value: 2.00e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28056667  45 ESALrEALYLFAPDIVLSDLSMSGFHGYQALRVVREVGNTP-FIFVSSKmgEDIAVEALQEGANDYIIK-QNLVRLPSAV 122
Cdd:COG3279  37 EEAL-ELLEEHKPDLVFLDIQMPGLDGFELARQLRELDPPPpIIFTTAY--DEYALEAFEVNAVDYLLKpIDEERLAKAL 113
                        90       100
                ....*....|....*....|
gi 28056667 123 TRAVRESRAELERQHVESEL 142
Cdd:COG3279 114 EKAKERLEAKAAAEASPEEK 133
HATPase_YehU-like cd16956
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
276-360 2.45e-05

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: 43.19  E-value: 2.45e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28056667 276 MPTGGCLTLVAQRHDGDRIcISVTDTGIGMSEETRARLFSPffttKSDGTGLGLIScKRIAESYG---GLiQVCSELGVG 352
Cdd:cd16956  21 LLDGGRVEITARLDGQHLL-LEVEDNGGGMDPDTLARILIR----SSNGLGLNLVD-KRLRQAFGndyGL-DIECAPGEG 93

                ....*...
gi 28056667 353 TRFDLILP 360
Cdd:cd16956  94 TRITIRLP 101
REC_OmpR cd17574
phosphoacceptor receiver (REC) domain of OmpR family response regulators; OmpR-like proteins ...
384-432 2.52e-05

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


Pssm-ID: 381116 [Multi-domain]  Cd Length: 99  Bit Score: 43.17  E-value: 2.52e-05
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*....
gi 28056667 384 LIVDGEATRLSLLGNALASQGYQPQLAPDGGAALKLLRHHaEPDLVIID 432
Cdd:cd17574   1 LVVEDDEEIAELLSDYLEKEGYEVDTAADGEEALELAREE-QPDLIILD 48
CheA COG0643
Chemotaxis protein histidine kinase CheA [Signal transduction mechanisms];
280-360 2.98e-05

Chemotaxis protein histidine kinase CheA [Signal transduction mechanisms];


Pssm-ID: 440408 [Multi-domain]  Cd Length: 563  Bit Score: 46.71  E-value: 2.98e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28056667 280 GCLTLVAqRHDGDRICISVTDTGIGM---------------SEETRARL---------FSPFFTTK---SD--GTGLGLI 330
Cdd:COG0643 309 GTITLSA-YHEGGRVVIEVSDDGRGLdlekirakaiekgliTAEEAAALsdeelleliFAPGFSTAeevTDlsGRGVGMD 387
                        90       100       110
                ....*....|....*....|....*....|
gi 28056667 331 SCKRIAESYGGLIQVCSELGVGTRFDLILP 360
Cdd:COG0643 388 VVKTNIEALGGTIEIESEPGKGTTFTLRLP 417
HATPase_BvrS-ChvG-like cd16953
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
261-360 3.30e-05

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Brucella abortus BvrS and Sinorhizobium meliloti ChvG; This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component sensor histidine kinase (HKs) such as Brucella abortus BvrS of the BvrR-BvrS two-component regulatory system (TCS), which controls cell invasion and intracellular survival, as well as Sinorhizobium meliloti and Agrobacterium tumefaciens ChvG of the ChvI-ChvG TCS necessary for endosymbiosis and pathogenicity in plants. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA), an accessory HAMP sensor domain, a periplasmic stimulus-sensing domain, and some also have a sensor N-terminal transmembrane domain.


Pssm-ID: 340429 [Multi-domain]  Cd Length: 110  Bit Score: 42.94  E-value: 3.30e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28056667 261 LQQCLLNLALNAIHAMPTGGCLTLVAQRHDGDRICISVTDTGIGMSEETRARLFSPFFTTKSDG------TGLGLISCKR 334
Cdd:cd16953   1 LGQVLRNLIGNAISFSPPDTGRITVSAMPTGKMVTISVEDEGPGIPQEKLESIFDRFYTERPANeafgqhSGLGLSISRQ 80
                        90       100       110
                ....*....|....*....|....*....|
gi 28056667 335 IAESYGGLI----QVCSELGVGTRFDLILP 360
Cdd:cd16953  81 IIEAHGGISvaenHNQPGQVIGARFTVQLP 110
REC_NtrX-like cd17550
phosphoacceptor receiver (REC) domain of nitrogen assimilation regulatory protein NtrX and ...
383-497 4.32e-05

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: 42.87  E-value: 4.32e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28056667 383 ILIVDGEATRLSLLGNALASQGYQPQLAPDGGAALKLLRHHaEPDLVIIdsDILL--LSAVCLLPTMQELGYRGPAIVLe 460
Cdd:cd17550   1 ILIVDDEEDIRESLSGILEDEGYEVDTAADGEEALKLIKER-RPDLVLL--DIWLpdMDGLELLKEIKEKYPDLPVIMI- 76
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 28056667 461 dAGqplrreHFSKDLAVHMLR--------KPLEMWRVFRAVAYAL 497
Cdd:cd17550  77 -SG------HGTIETAVKATKlgaydfieKPLSLDRLLLTIERAL 114
REC_OmpR_MtPhoP-like cd17615
phosphoacceptor receiver (REC) domain of MtPhoP-like OmpR family response regulators; ...
23-112 4.45e-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: 4.45e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28056667  23 AKLLFNTLREAGLDgsferVESESALREALYL---FAPDIVLSDLSMSGFHGYQALRVVREVG-NTPFIFVSSKMGEDIA 98
Cdd:cd17615  12 TELLSMALRYEGWD-----VETAADGAEALAAareFRPDAVVLDIMLPDMDGLEVLRRLRADGpDVPVLFLTAKDSVEDR 86
                        90
                ....*....|....
gi 28056667  99 VEALQEGANDYIIK 112
Cdd:cd17615  87 IAGLTAGGDDYVTK 100
REC_PA4781-like cd19920
phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase PA4781 and similar ...
383-432 6.73e-05

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: 42.11  E-value: 6.73e-05
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 28056667 383 ILIVDGEATRLSLLGNALASQGYQPQLAPDGGAALKLLRhHAEPDLVIID 432
Cdd:cd19920   1 ILIVDDVPDNLRLLSELLRAAGYRVLVATDGQQALQRAQ-AEPPDLILLD 49
REC_2_DhkD-like cd17580
second phosphoacceptor receiver (REC) domain of Dictyostelium discoideum hybrid signal ...
383-435 6.97e-05

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


Pssm-ID: 381118 [Multi-domain]  Cd Length: 112  Bit Score: 42.06  E-value: 6.97e-05
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|...
gi 28056667 383 ILIVDGEATRLSLLGNALASQGYQPQLAPDGGAALKLLRHHAePDLVIidSDI 435
Cdd:cd17580   1 ILVVDDNEDAAEMLALLLELEGAEVTTAHSGEEALEAAQRFR-PDVIL--SDI 50
REC_OmpR_ChvI-like cd19936
phosphoacceptor receiver (REC) domain of ChvI-like OmpR family response regulators; ...
45-112 7.21e-05

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


Pssm-ID: 381163 [Multi-domain]  Cd Length: 99  Bit Score: 41.66  E-value: 7.21e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 28056667  45 ESALrEALYLFAPDIVLSDLSMSGFHGYQALRVVREVGNTPFIFVSSKMGEDIAVEALQEGANDYIIK 112
Cdd:cd19936  32 ASAL-DGLNARPPDLAILDIKMPRMDGMELLQRLRQKSTLPVIFLTSKDDEIDEVFGLRMGADDYITK 98
orf27 CHL00148
Ycf27; Reviewed
50-144 9.65e-05

Ycf27; Reviewed


Pssm-ID: 214376 [Multi-domain]  Cd Length: 240  Bit Score: 43.94  E-value: 9.65e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28056667   50 EALYLFA---PDIVLSDLSMSGFHGYQALRVVREVGNTPFIFVSSKmgEDIA--VEALQEGANDYIIKQNLVRLPSAVTR 124
Cdd:CHL00148  41 EALKLFRkeqPDLVILDVMMPKLDGYGVCQEIRKESDVPIIMLTAL--GDVSdrITGLELGADDYVVKPFSPKELEARIR 118
                         90       100
                 ....*....|....*....|..
gi 28056667  125 AV--RESRAELERQHVESELMR 144
Cdd:CHL00148 119 SVlrRTNKKSFSSKIPNSSIIR 140
REC_OmpR_kpRstA-like cd17622
phosphoacceptor receiver (REC) domain of kpRstA-like OmpR family response regulators; ...
50-112 1.06e-04

phosphoacceptor receiver (REC) domain of kpRstA-like OmpR family response regulators; Klebsiella pneumoniae RstA (kpRstA) is part of the RstA/RstB two-component regulatory system that may play a regulatory role in virulence. It belongs to the OmpR family of DNA-binding response regulators that contain N-terminal receiver (REC) and C-terminal DNA-binding winged helix-turn-helix effector domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381137 [Multi-domain]  Cd Length: 116  Bit Score: 41.60  E-value: 1.06e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 28056667  50 EALYLFAPDIVLSDLSMSGFHGYQALRVVREVGNTPFIFVSSKMGEDIAVEALQEGANDYIIK 112
Cdd:cd17622  38 EVIAREKPDAVLLDIMLPGIDGLTLCRDLRPKYQGPILLLTALDSDIDHILGLELGADDYVVK 100
REC_hyHK cd17598
phosphoacceptor receiver (REC) domain of uncharacterized hybrid sensor histidine kinase ...
383-437 1.07e-04

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


Pssm-ID: 381128 [Multi-domain]  Cd Length: 118  Bit Score: 41.93  E-value: 1.07e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*
gi 28056667 383 ILIVDGEATRLSLLGNALASQGYQPQLAPDGGAALKLLRHHaEPDLVIidSDILL 437
Cdd:cd17598   1 ILIVEDSPTQAEQLKHILEEQGYKVQVARNGREALAMLAEH-RPTLVI--SDIVM 52
PRK11361 PRK11361
acetoacetate metabolism transcriptional regulator AtoC;
381-459 1.53e-04

acetoacetate metabolism transcriptional regulator AtoC;


Pssm-ID: 183099 [Multi-domain]  Cd Length: 457  Bit Score: 44.07  E-value: 1.53e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 28056667  381 QRILIVDGEATRLSLLGNALASQGYQPQLAPDGGAALKLLRHHaEPDLVIIDSDILLLSAVCLLPTMQELGYRGPAIVL 459
Cdd:PRK11361   5 NRILIVDDEDNVRRMLSTAFALQGFETHCANNGRTALHLFADI-HPDVVLMDIRMPEMDGIKALKEMRSHETRTPVILM 82
HATPase_c_5 pfam14501
GHKL domain; This family represents the structurally related ATPase domains of histidine ...
317-350 1.68e-04

GHKL domain; This family represents the structurally related ATPase domains of histidine kinase, DNA gyrase B and HSP90.


Pssm-ID: 433996 [Multi-domain]  Cd Length: 102  Bit Score: 40.66  E-value: 1.68e-04
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 28056667   317 FFTTKSDGT--GLGLISCKRIAESYGGLIQVCSELG 350
Cdd:pfam14501  59 LPSTKTKGDghGIGLKSIRRIVKKYGGNLSTEIENG 94
REC_NarL cd19931
phosphoacceptor receiver (REC) domain of Nitrate/Nitrite response regulator L (NarL); Nitrate ...
35-112 1.71e-04

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


Pssm-ID: 381158 [Multi-domain]  Cd Length: 117  Bit Score: 41.18  E-value: 1.71e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28056667  35 LDGSFERVESESALREALYL---FAPDIVLSDLSMSGFHGYQALRVVREVGNTP--FIFVSSKMGEDIaVEALQEGANDY 109
Cdd:cd19931  20 LDPDFTVVGEASSGEEGIELaerLDPDLILLDLNMKGMSGLDTLKALREEGVSAriVILTVSDAEDDV-VTALRAGADGY 98

                ...
gi 28056667 110 IIK 112
Cdd:cd19931  99 LLK 101
REC_CheY4-like cd17562
phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY4 and similar CheY ...
382-469 1.82e-04

phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY4 and similar CheY family proteins; CheY family chemotaxis response regulators (RRs) comprise about 17% of bacterial RRs and almost half of all RRs in archaea. This subfamily contains Vibrio cholerae CheY4 and similar CheY family RRs. CheY proteins control bacterial motility and participate in signaling phosphorelays and in protein-protein interactions. CheY RRs contain only the REC domain with no output/effector domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381110 [Multi-domain]  Cd Length: 118  Bit Score: 41.13  E-value: 1.82e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28056667 382 RILIVDGEATRLSLLGNALASQGYQPQLAPDGGAALKLLRhhAEP-DLVIIDSDILLLSAVCLLPTMQEL-GYRG-PAIV 458
Cdd:cd17562   2 KILAVDDSASIRQMVSFTLRGAGYEVVEAADGRDALSKAQ--SKKfDLIITDQNMPNMDGIELIKELRKLpAYKFtPILM 79
                        90
                ....*....|.
gi 28056667 459 LEDAGQPLRRE 469
Cdd:cd17562  80 LTTESSDEKKQ 90
REC_2_GGDEF cd17544
second phosphoacceptor receiver (REC) domain of uncharacterized GGDEF domain proteins; This ...
382-432 1.82e-04

second phosphoacceptor receiver (REC) domain of uncharacterized GGDEF domain proteins; This family is composed of uncharacterized PleD-like response regulators that contain two N-terminal REC domains and a C-terminal diguanylate cyclase output domain with the characteristic GGDEF motif at the active site. Unlike PleD which contains a REC-like adaptor domain, the second REC domain of these uncharacterized GGDEF domain proteins, described in this model, contains characteristic metal-binding and active site residues. PleD response regulators are global regulators of cell metabolism in some important human pathogens. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381098 [Multi-domain]  Cd Length: 122  Bit Score: 41.35  E-value: 1.82e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|.
gi 28056667 382 RILIVDGEATRLSLLGNALASQGYQPQLAPDGGAALKLLRHHAEPDLVIID 432
Cdd:cd17544   2 KVLVVDDSATSRNHLRALLRRHNFQVLEAANGQEALEVLEQHPDIKLVITD 52
REC_D1_PleD-like cd17538
first (D1) phosphoacceptor receiver (REC) domain of response regulator PleD and similar ...
49-112 1.85e-04

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: 40.56  E-value: 1.85e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28056667  49 REALYLFA---PDIVLSDLSMSGFHGYQALRVVREVGNT---PFIFVSSKMGEDIAVEALQEGANDYIIK 112
Cdd:cd17538  33 QEALALAEeelPDLILLDVMMPGMDGFEVCRRLKEDPETrhiPVIMITALDDREDRIRGLEAGADDFLSK 102
PRK10336 PRK10336
two-component system response regulator QseB;
49-138 2.08e-04

two-component system response regulator QseB;


Pssm-ID: 182387 [Multi-domain]  Cd Length: 219  Bit Score: 42.57  E-value: 2.08e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28056667   49 REALYLFAPDIVLSDLSMSGFHGYQALRVVREVGNT-PFIFVSSKMGEDIAVEALQEGANDYIIK-----QNLVRLPSAV 122
Cdd:PRK10336  37 KEALYSAPYDAVILDLTLPGMDGRDILREWREKGQRePVLILTARDALAERVEGLRLGADDYLCKpfaliEVAARLEALM 116
                         90
                 ....*....|....*.
gi 28056667  123 TRAVRESRAELERQHV 138
Cdd:PRK10336 117 RRTNGQASNELRHGNV 132
REC_OmpR_MtrA-like cd17626
phosphoacceptor receiver (REC) domain of MtrA-like OmpR family response regulators; MtrA is ...
381-432 2.25e-04

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


Pssm-ID: 381141 [Multi-domain]  Cd Length: 115  Bit Score: 40.92  E-value: 2.25e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 28056667 381 QRILIVDGEATRLSLLGNALASQGYQPQLAPDGGAALKLLrHHAEPDLVIID 432
Cdd:cd17626   1 ARILVVDDDAALAEMIGIVLRGEGFDPAFCGDGTQALAAF-REVRPDLVLLD 51
fixJ PRK09390
response regulator FixJ; Provisional
43-151 2.45e-04

response regulator FixJ; Provisional


Pssm-ID: 181815 [Multi-domain]  Cd Length: 202  Bit Score: 42.30  E-value: 2.45e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28056667   43 ESESALREALYLFAPDIVLSDLSMSGFHGYQALRVVREVGNTPFIFVSSKMGeDI--AVEALQEGANDYIIKQ-NLVRLP 119
Cdd:PRK09390  34 ESAQAFLDALPGLRFGCVVTDVRMPGIDGIELLRRLKARGSPLPVIVMTGHG-DVplAVEAMKLGAVDFIEKPfEDERLI 112
                         90       100       110
                 ....*....|....*....|....*....|..
gi 28056667  120 SAVTRAVRESRAELERQHVESELmrAQRLESL 151
Cdd:PRK09390 113 GAIERALAQAPEAAKSEAVAADI--RARIASL 142
REC_YesN-like cd17536
phosphoacceptor receiver (REC) domain of YesN and related helix-turn-helix containing response ...
49-112 2.48e-04

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: 40.78  E-value: 2.48e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 28056667  49 REALYLFA---PDIVLSDLSMSGFHGYQALRVVREVG-NTPFIFVSSkMGE-DIAVEALQEGANDYIIK 112
Cdd:cd17536  35 EEALELIEehkPDIVITDIRMPGMDGLELIEKIRELYpDIKIIILSG-YDDfEYAQKAIRLGVVDYLLK 102
REC_OmpR_CpxR cd17623
phosphoacceptor receiver (REC) domain of CpxR-like OmpR family response regulators; CpxR is ...
44-112 2.60e-04

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


Pssm-ID: 381138 [Multi-domain]  Cd Length: 115  Bit Score: 40.75  E-value: 2.60e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28056667  44 SESALREALYLfAPDIVLSDLSMSGFHGYQALRVVREVGNTPFIFVSSKmGEDI-AVEALQEGANDYIIK 112
Cdd:cd17623  31 GEQGLAALLEG-SPDLVVLDVMLPKMNGLDVLKELRKTSQVPVLMLTAR-GDDIdRILGLELGADDYLPK 98
REC_WspR-like cd17575
phosphoacceptor receiver (REC) domain of WspR response regulator and similar proteins; The ...
57-112 2.89e-04

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


Pssm-ID: 381117 [Multi-domain]  Cd Length: 128  Bit Score: 40.85  E-value: 2.89e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 28056667  57 PDIVLSDLSMSGFHGYQALRVVR---EVGNTPFIFVSSKMGEDIAVEALQEGANDYIIK 112
Cdd:cd17575  46 PTVILQDLVMPGVDGLTLVRFFRanpATRDIPIIVLSTKEEPEVKSEAFALGANDYLVK 104
HATPase_LytS-like cd16957
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
268-360 2.99e-04

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Bacillus subtilis LytS and Staphylococcus aureus LytS; This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component sensor histidine kinase (HKs) such as Bacillus subtilis LytS, a HK of the two-component system (TCS) LytS-LytR needed for growth on pyruvate, and Staphylococcus aureus LytS-LytR TCS involved in the adaptation of S. aureus to cationic antimicrobial peptides. Proteins having this HATPase domain also contain a histidine kinase domain (His-kinase), and a GAF sensor domain; most contain a DUF3816 domain.


Pssm-ID: 340433 [Multi-domain]  Cd Length: 106  Bit Score: 40.10  E-value: 2.99e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28056667 268 LALNAI-HAMPT--GGCLTLVAQRHDGDRICISVTDTGIGMSEETRARLFSPFFTTKSdGTGLGLISC-KRIAESYG--G 341
Cdd:cd16957   9 LVENAIrHAFPKrkENNEVRVVVKKDQHKVHVSVSDNGQGIPEERLDLLGKTTVTSEK-GTGTALENLnRRLIGLFGseA 87
                        90
                ....*....|....*....
gi 28056667 342 LIQVCSELGVGTRFDLILP 360
Cdd:cd16957  88 CLHIESEVHGGTEVWFVIP 106
PRK10651 PRK10651
transcriptional regulator NarL; Provisional
57-112 3.36e-04

transcriptional regulator NarL; Provisional


Pssm-ID: 182619 [Multi-domain]  Cd Length: 216  Bit Score: 41.94  E-value: 3.36e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 28056667   57 PDIVLSDLSMSGFHGYQALRVVREVGNTPFI--FVSSKMGEDIaVEALQEGANDYIIK 112
Cdd:PRK10651  53 PDLILLDLNMPGMNGLETLDKLREKSLSGRIvvFSVSNHEEDV-VTALKRGADGYLLK 109
REC_DivK-like cd17548
phosphoacceptor receiver (REC) domain of DivK and similar proteins; Caulobacter crescentus ...
382-432 3.60e-04

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: 40.22  E-value: 3.60e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|.
gi 28056667 382 RILIVDGEATRLSLLGNALASQGYQPQLAPDGGAALKLLRHHAePDLVIID 432
Cdd:cd17548   1 KILIVEDNPLNMKLARDLLESAGYEVLEAADGEEALEIARKEK-PDLILMD 50
orf27 CHL00148
Ycf27; Reviewed
379-432 4.13e-04

Ycf27; Reviewed


Pssm-ID: 214376 [Multi-domain]  Cd Length: 240  Bit Score: 42.01  E-value: 4.13e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 28056667  379 HGQRILIVDGEATRLSLLGNALASQGYQPQLAPDGGAALKLLRHHaEPDLVIID 432
Cdd:CHL00148   5 SKEKILVVDDEAYIRKILETRLSIIGYEVITASDGEEALKLFRKE-QPDLVILD 57
PRK15115 PRK15115
response regulator GlrR; Provisional
382-497 4.24e-04

response regulator GlrR; Provisional


Pssm-ID: 185070 [Multi-domain]  Cd Length: 444  Bit Score: 42.90  E-value: 4.24e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28056667  382 RILIVDGEATRLSLLGNALASQGYQPQLAPDGGAALKLLrHHAEPDLVIIDSDILLLSAVCLLPTMQELGYRGPAIVLE- 460
Cdd:PRK15115   7 HLLLVDDDPGLLKLLGMRLTSEGYSVVTAESGQEALRVL-NREKVDLVISDLRMDEMDGMQLFAEIQKVQPGMPVIILTa 85
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 28056667  461 -----DAGQPLRREHFSkdlavhMLRKPLEMWRVFRAVAYAL 497
Cdd:PRK15115  86 hgsipDAVAATQQGVFS------FLTKPVDRDALYKAIDDAL 121
REC_OmpR_BsPhoP-like cd19937
phosphoacceptor receiver (REC) domain of BsPhoP-like OmpR family response regulators; Bacillus ...
384-432 5.03e-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: 39.95  E-value: 5.03e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*....
gi 28056667 384 LIVDGEATRLSLLGNALASQGYQPQLAPDGGAALKLLRHHaEPDLVIID 432
Cdd:cd19937   1 LVVDDEEDIVELLKYNLEKEGYEVVTAYDGEEALKRAKDE-KPDLIILD 48
REC_OmpR_CusR-like cd19935
phosphoacceptor receiver (REC) domain of CusR-like OmpR family response regulators; ...
30-112 5.21e-04

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: 39.35  E-value: 5.21e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28056667  30 LREAG--LDGSFERVESESALREALYlfapDIVLSDLSMSGFHGYQALRVVREVGN-TPFIFVSSKMGEDIAVEALQEGA 106
Cdd:cd19935  18 LTEEGyaVDVAYDGEDGLHLALTNEY----DLIILDVMLPGLDGLEVLRRLRAAGKqTPVLMLTARDSVEDRVKGLDLGA 93

                ....*.
gi 28056667 107 NDYIIK 112
Cdd:cd19935  94 DDYLVK 99
REC_OmpR_BaeR-like cd19938
phosphoacceptor receiver (REC) domain of BaeR-like OmpR family response regulators; BaeR is ...
382-432 5.56e-04

phosphoacceptor receiver (REC) domain of BaeR-like OmpR family response regulators; BaeR is part of the BaeSR two-component system that is involved in regulating genes that confer multidrug and metal resistance. In Salmonella, BaeSR induces AcrD and MdtABC drug efflux systems, increasing multidrug and metal resistance. In Escherichia coli, BaeR stimulates multidrug resistance via mdtABC (multidrug transporter ABC, formerly known as yegMNO) genes, which encode a resistance-nodulation-cell division (RND) drug efflux system. Members of this subfamily belong to the OmpR family of DNA-binding response regulators, which are characterized by a REC domain and a winged helix-turn-helix (wHTH) DNA-binding output effector domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381165 [Multi-domain]  Cd Length: 114  Bit Score: 39.67  E-value: 5.56e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|.
gi 28056667 382 RILIVDGEATRLSLLGNALASQGYQPQLAPDGGAALKLLRHHAePDLVIID 432
Cdd:cd19938   1 RILIVEDEPKLAQLLIDYLRAAGYAPTLLAHGDQVLPYVRHTP-PDLILLD 50
REC_TrrA-like cd17554
phosphoacceptor receiver (REC) domain of Thermotoga maritima response regulator TrrA and ...
382-432 5.68e-04

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: 39.51  E-value: 5.68e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|.
gi 28056667 382 RILIVDGEATRLSLLGNALASQGYQPQLAPDGGAALKLLRhHAEPDLVIID 432
Cdd:cd17554   2 KILVVDDEENIRELYKEELEDEGYEVVTAGNGEEALEKLE-SEDPDLVILD 51
REC_GlnL-like cd17565
phosphoacceptor receiver (REC) domain of transcriptional regulatory protein GlnL and similar ...
47-112 5.98e-04

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


Pssm-ID: 381112 [Multi-domain]  Cd Length: 103  Bit Score: 39.18  E-value: 5.98e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 28056667  47 ALREALYLfAPDIVLSDLSMSGFHGYQALRVVREVGNTP-FIFVSSKMGEDIAVEALQEGANDYIIK 112
Cdd:cd17565  36 AYDEILFL-QPDIVLIDLLMPGMDGIQLVRKLKDTGSNGkFIMISQVSDKEMIGKAYQAGIEFFINK 101
HATPase_UhpB-NarQ-NarX-like cd16917
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
288-360 6.67e-04

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Escherichia coli UhpB, NarQ and NarX, and Bacillus subtilis YdfH, YhcY and YfiJ; 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 UhpB, a HK of the UhpB-UhpA TCS, NarQ and NarX, HKs of the NarQ-NarP and NarX-NarL TCSs, respectively, and Bacillus YdfH, YhcY and YfiJ HKs, of the YdfH-YdfI, YhcY-YhcZ and YfiJ-YfiK TCSs, respectively. In addition, it includes Bacillus YxjM, ComP, LiaS and DesK, HKs of the YxjM-YxjML, ComP-ComA, LiaS-LiaR, DesR-DesK TCSs, respectively. Proteins having this HATPase domain have a histidine kinase dimerization and phosphoacceptor domain; some have accessory domains such as GAF, HAMP, PAS and MASE sensor domains.


Pssm-ID: 340394 [Multi-domain]  Cd Length: 87  Bit Score: 38.69  E-value: 6.67e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 28056667 288 RHDGDRICISVTDTGIGMSEETRARlfspffttksdGTGLGLISCKRIAESYGGLIQVCSELGVGTRFDLILP 360
Cdd:cd16917  26 SYTADELTLTVVDDGVGFDGPAPPG-----------GGGFGLLGMRERAELLGGTLTIGSRPGGGTRVTARLP 87
REC_OmpR_BsPhoP-like cd19937
phosphoacceptor receiver (REC) domain of BsPhoP-like OmpR family response regulators; Bacillus ...
49-112 7.05e-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: 39.18  E-value: 7.05e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28056667  49 REALYLFA---PDIVLSDLSMSGFHGYQALRVVR---EVGNTPFIFVSSKMGEDIAVEALQEGANDYIIK 112
Cdd:cd19937  31 EEALKRAKdekPDLIILDLMLPGIDGLEVCRILRsdpKTSSIPIIMLTAKGEEFDKVLGLELGADDYITK 100
REC_Spo0F-like cd17553
phosphoacceptor receiver (REC) domain of Spo0F and similar domains; Spo0F, a stand-alone ...
381-486 7.11e-04

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: 39.46  E-value: 7.11e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28056667 381 QRILIVDGEATRLSLLGNALASQGYQPQLAPDGGAALKLLRHHaEPDLVIIDSDILLLSAVCLLPTMQELGYRGPAIVLE 460
Cdd:cd17553   1 EKILIVDDQYGIRILLNEVFNKEGYQTFQAANGLQALDIVTKE-RPDLVLLDMKIPGMDGIEILKRMKVIDENIRVIIMT 79
                        90       100
                ....*....|....*....|....*..
gi 28056667 461 DAGQpLRREHFSKDL-AVHMLRKPLEM 486
Cdd:cd17553  80 AYGE-LDMIQESKELgALTHFAKPFDI 105
REC_OmpR_MtPhoP-like cd17615
phosphoacceptor receiver (REC) domain of MtPhoP-like OmpR family response regulators; ...
382-432 7.42e-04

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: 39.26  E-value: 7.42e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|.
gi 28056667 382 RILIVDGEATRLSLLGNALASQGYQPQLAPDGGAALKLLRHHAePDLVIID 432
Cdd:cd17615   1 RVLVVDDEPNITELLSMALRYEGWDVETAADGAEALAAAREFR-PDAVVLD 50
REC_2_DhkD-like cd17580
second phosphoacceptor receiver (REC) domain of Dictyostelium discoideum hybrid signal ...
49-112 7.57e-04

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: 38.98  E-value: 7.57e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 28056667  49 REALYL---FAPDIVLSDLSMSGFHGYQALRVVRE---VGNTPFIFVS-SKMGEDIaVEALQEGANDYIIK 112
Cdd:cd17580  32 EEALEAaqrFRPDVILSDIGMPGMDGYELARRLRElpwLANTPAIALTgYGQPEDR-ERALEAGFDAHLVK 101
REC_OmpR_PhoB cd17618
phosphoacceptor receiver (REC) domain of PhoB response regulator from the OmpR family; The ...
30-112 7.67e-04

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: 39.15  E-value: 7.67e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28056667  30 LREAGldgsFERVESESA--LREALYLFAPDIVLSDLSMSGFHGYQALRVVRE---VGNTPFIFVSSKMGEDIAVEALQE 104
Cdd:cd17618  20 LERAG----FDVVEAEDAesAVNLIVEPRPDLILLDWMLPGGSGIQFIRRLKRdemTRDIPIIMLTARGEEEDKVRGLEA 95

                ....*...
gi 28056667 105 GANDYIIK 112
Cdd:cd17618  96 GADDYITK 103
cpxA PRK09470
envelope stress sensor histidine kinase CpxA;
290-329 8.52e-04

envelope stress sensor histidine kinase CpxA;


Pssm-ID: 236532 [Multi-domain]  Cd Length: 461  Bit Score: 41.84  E-value: 8.52e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 28056667  290 DGDRICISVTDTGIGMSEETRARLFSPFFTT------KSDGTGLGL 329
Cdd:PRK09470 380 DKDGLTITVDDDGPGVPEEEREQIFRPFYRVdeardrESGGTGLGL 425
PRK10610 PRK10610
chemotaxis protein CheY;
24-112 8.93e-04

chemotaxis protein CheY;


Pssm-ID: 170568 [Multi-domain]  Cd Length: 129  Bit Score: 39.57  E-value: 8.93e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28056667   24 KLLFNTLREAGLDGSFERVESESALREaLYLFAPDIVLSDLSMSGFHGYQALRVVRE---VGNTPFIFVSSKMGEDIAVE 100
Cdd:PRK10610  19 RIVRNLLKELGFNNVEEAEDGVDALNK-LQAGGFGFVISDWNMPNMDGLELLKTIRAdgaMSALPVLMVTAEAKKENIIA 97
                         90
                 ....*....|..
gi 28056667  101 ALQEGANDYIIK 112
Cdd:PRK10610  98 AAQAGASGYVVK 109
REC_hyHK_blue-like cd18161
phosphoacceptor receiver (REC) domain of hybrid sensor histidine kinase/response regulators ...
383-432 8.95e-04

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


Pssm-ID: 381145 [Multi-domain]  Cd Length: 102  Bit Score: 38.87  E-value: 8.95e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 28056667 383 ILIVDGEATRLSLLGNALASQGYQPQLAPDGGAALKLLRHHAEPDLVIID 432
Cdd:cd18161   1 VLVVEDDPDVRRLTAEVLEDLGYTVLEAASGDEALDLLESGPDIDLLVTD 50
glnG PRK10923
nitrogen regulation protein NR(I); Provisional
43-112 8.99e-04

nitrogen regulation protein NR(I); Provisional


Pssm-ID: 182842 [Multi-domain]  Cd Length: 469  Bit Score: 41.78  E-value: 8.99e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 28056667   43 ESESALREALYLFAPDIVLSDLSMSGFHGYQALRVVREVGNT-PFIFVSSKMGEDIAVEALQEGANDYIIK 112
Cdd:PRK10923  34 ENGNEVLEALASKTPDVLLSDIRMPGMDGLALLKQIKQRHPMlPVIIMTAHSDLDAAVSAYQQGAFDYLPK 104
REC_NtrC cd19919
phosphoacceptor receiver (REC) domain of DNA-binding transcriptional regulator NtrC; ...
29-112 9.43e-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: 39.18  E-value: 9.43e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28056667  29 TLREAGLD-GSFERveSESALrEALYLFAPDIVLSDLSMSGFHGYQALRVVRE-VGNTPFIFVSSKMGEDIAVEALQEGA 106
Cdd:cd19919  19 ALAGAGLTvTSFEN--AQEAL-AALASSQPDVLISDIRMPGMDGLALLAQIKQrHPDLPVIIMTAHSDLDSAVSAYQGGA 95

                ....*.
gi 28056667 107 NDYIIK 112
Cdd:cd19919  96 FEYLPK 101
REC_RegA-like cd17563
phosphoacceptor receiver (REC) domain of photosynthetic apparatus regulatory protein RegA; ...
381-432 9.84e-04

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: 38.96  E-value: 9.84e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 28056667 381 QRILIVDGEATRLSLLGNALASQGYQPQLAPDGGAALKLLRHHAePDLVIID 432
Cdd:cd17563   1 KSLLLVDDDEVFAERLARALERRGFEVETAHSVEEALALAREEK-PDYAVLD 51
HATPase_PDK-like cd16929
Histidine kinase-like ATPase domain of pyruvate dehydrogenase kinase, branched-chain ...
285-354 1.17e-03

Histidine kinase-like ATPase domain of pyruvate dehydrogenase kinase, branched-chain alpha-ketoacid dehydrogenase kinase and related domains; This family includes the histidine kinase-like ATPase (HATPase) domains of all four PDK isoforms (pyruvate dehydrogenase kinases 1-4) that have been described in mammals, and other PDKs including Saccharomyces Pkp1p and Pkp2p. PDKs and phosphatases tightly regulate the mitochondrial pyruvate dehydrogenase complex (PDC) by reversible phosphorylation. PDC catalyzes the oxidative decarboxylation of pyruvate to acetyl-CoA, connecting glycolysis and the TCA acid cycle. Also included in this family is mammalian branched-chain alpha-ketoacid dehydrogenase kinase (BDK), a mitochondrial protein kinase that phosphorylates a subunit of the branched-chain a-ketoacid dehydrogenase (BCKD) complex, which catalyzes the oxidative decarboxylation of branched-chain alpha-ketoacids derived from leucine, isoleucine, and valine, a rate-limiting step in the oxidative degradation of these branched-chain amino acids.


Pssm-ID: 340406 [Multi-domain]  Cd Length: 169  Bit Score: 39.63  E-value: 1.17e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28056667 285 VAQRHDGDRICISVTDTGIGMSEETRARLFSPFFTTKSD-------------------GTGLGLISCKRIAESYGGLIQV 345
Cdd:cd16929  75 VTVAKGDEDLTIKISDRGGGIPREDLARLFSYMYSTAPQpslddfsdlisgtqpsplaGFGYGLPMSRLYAEYFGGDLDL 154

                ....*....
gi 28056667 346 CSELGVGTR 354
Cdd:cd16929 155 QSMEGYGTD 163
PRK10529 PRK10529
DNA-binding transcriptional activator KdpE; Provisional
20-132 1.19e-03

DNA-binding transcriptional activator KdpE; Provisional


Pssm-ID: 182522 [Multi-domain]  Cd Length: 225  Bit Score: 40.56  E-value: 1.19e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28056667   20 LEDAKLLFNTLREAgLDGSFERVESESALREALYLFA---PDIVLSDLSMSGFHGYQALRVVREVGNTPFIFVSSKMGED 96
Cdd:PRK10529   7 VEDEQAIRRFLRTA-LEGDGMRVFEAETLQRGLLEAAtrkPDLIILDLGLPDGDGIEFIRDLRQWSAIPVIVLSARSEES 85
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 28056667   97 IAVEALQEGANDYI-----IKQNLVRLPSAVTRAVRESRAE 132
Cdd:PRK10529  86 DKIAALDAGADDYLskpfgIGELQARLRVALRRHSATPAPD 126
REC_LytTR_AlgR-like cd17532
phosphoacceptor receiver (REC) domain of LytTR/AlgR family response regulators similar to AlgR; ...
36-112 1.27e-03

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


Pssm-ID: 381087 [Multi-domain]  Cd Length: 118  Bit Score: 38.67  E-value: 1.27e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28056667  36 DGSFERVESESALREALYLF---APDIVLSDLSMSGFHGYQALRVVREVGNTPFI-FVSSKmgEDIAVEALQEGANDYII 111
Cdd:cd17532  21 HPDIEIVGEAENGEEALEAIeelKPDVVFLDIQMPGLDGLELAKKLSKLAKPPLIvFVTAY--DEYAVEAFELNAVDYLL 98

                .
gi 28056667 112 K 112
Cdd:cd17532  99 K 99
HATPase_YpdA-YehU-LytS-like cd16924
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
268-360 1.32e-03

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Escherichia coli YpdA, YehU, Bacillus subtilis LytS, and some hybrid sensor histidine kinases; This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component sensor histidine kinase (HKs) such as Bacillus subtilis LytS, a HK of the two-component system (TCS) LytS-LytR needed for growth on pyruvate, and Staphylococcus aureus LytS-LytR TCS involved in the adaptation of S. aureus to cationic antimicrobial peptides. It also includes the HATPase domains of Escherichia coli YpdA and YehU, HKs of YpdA-YpdB and YehU-YehTCSs, which are involved together in a nutrient sensing regulatory network. Proteins having this HATPase domain also contain a histidine kinase domain (His-kinase), some having accessory sensor domain(s) such as Cache, HAMP or GAF; some are hybrid sensor histidine kinases as they also contain a REC signal receiver domain.


Pssm-ID: 340401 [Multi-domain]  Cd Length: 103  Bit Score: 38.20  E-value: 1.32e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28056667 268 LALNAI-HAMP--TGGCLTLVAQRHDGDRICISVTDTGIGMSEETRARLFSpfftTKSDGTGLGLISC-KRIAESYGG-- 341
Cdd:cd16924   9 LVENAIqHGLSplTDKGVVTISALKEDNHVMIEVEDNGRGIDPKVLNILGK----KPKEGNGIGLYNVhQRLILLFGEdy 84
                        90
                ....*....|....*....
gi 28056667 342 LIQVCSELGVGTRFDLILP 360
Cdd:cd16924  85 GIHIASEPDKGTRITFTIP 103
REC_RpfG-like cd17551
phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase response regulator ...
382-432 1.71e-03

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: 38.19  E-value: 1.71e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 28056667 382 RILIVDGEATRLSLLGNALASQGY-QPQLAPDGGAALKLLRHHaEPDLVIID 432
Cdd:cd17551   2 RILIVDDNPTNLLLLEALLRSAGYlEVVSFTDPREALAWCREN-PPDLILLD 52
HATPase_SpaK_NisK-like cd16975
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
261-343 1.74e-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: 1.74e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28056667 261 LQQCLLNLALNAIHAMPTGGCLTLVAQrhdGDRICIS--VTDTGIGMSEETRARLFSPFFTTKSDGT-----GLGLISCK 333
Cdd:cd16975   5 LSRALINIISNACQYAPEGGTVSISIY---DEEEYLYfeIWDNGHGFSEQDLKKALELFYRDDTSRRsgghyGMGLYIAK 81
                        90
                ....*....|
gi 28056667 334 RIAESYGGLI 343
Cdd:cd16975  82 NLVEKHGGSL 91
REC_OmpR_CpxR cd17623
phosphoacceptor receiver (REC) domain of CpxR-like OmpR family response regulators; CpxR is ...
383-433 1.76e-03

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


Pssm-ID: 381138 [Multi-domain]  Cd Length: 115  Bit Score: 38.06  E-value: 1.76e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|.
gi 28056667 383 ILIVDGEATRLSLLGNALASQGYQPQLAPDGGAALKLLRHHAePDLVIIDS 433
Cdd:cd17623   1 ILLIDDDRELTELLTEYLEMEGFNVRAAHDGEQGLAALLEGS-PDLVVLDV 50
REC_OmpR_ArcA_TorR-like cd17619
phosphoacceptor receiver (REC) domain of ArcA- and TorR-like OmpR family response regulators; ...
58-112 1.77e-03

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: 38.14  E-value: 1.77e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*
gi 28056667  58 DIVLSDLSMSGFHGYQALRVVREVGNTPFIFVSSKMGEDIAVEALQEGANDYIIK 112
Cdd:cd17619  46 DLVLLDINLPGKDGLSLTRELREQSEVGIILVTGRDDEVDRIVGLEIGADDYVTK 100
REC_NtrC1-like cd17572
phosphoacceptor receiver (REC) domain of nitrogen regulatory protein C 1 (NtrC1) from Aquifex ...
57-112 1.85e-03

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: 38.33  E-value: 1.85e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 28056667  57 PDIVLSDLSMSGFHGYQALRVVREVG-NTPFIFVSSKMGEDIAVEALQEGANDYIIK 112
Cdd:cd17572  43 PDVVLLDLKLPDMSGMEILKWIQERSlPTSVIVITAHGSVDIAVEAMRLGAYDFLEK 99
PRK10337 PRK10337
sensor protein QseC; Provisional
267-340 2.04e-03

sensor protein QseC; Provisional


Pssm-ID: 182388 [Multi-domain]  Cd Length: 449  Bit Score: 40.40  E-value: 2.04e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28056667  267 NLALNAIHAMPTGG--CLTLVAQRhdgdricISVTDTGIGMSEETRARLFSPFF----TTKSdGTGLGLISCKRIAESYG 340
Cdd:PRK10337 359 NLLDNAIRYSPQGSvvDVTLNARN-------FTVRDNGPGVTPEALARIGERFYrppgQEAT-GSGLGLSIVRRIAKLHG 430
REC_OmpR_BaeR-like cd19938
phosphoacceptor receiver (REC) domain of BaeR-like OmpR family response regulators; BaeR is ...
23-112 2.54e-03

phosphoacceptor receiver (REC) domain of BaeR-like OmpR family response regulators; BaeR is part of the BaeSR two-component system that is involved in regulating genes that confer multidrug and metal resistance. In Salmonella, BaeSR induces AcrD and MdtABC drug efflux systems, increasing multidrug and metal resistance. In Escherichia coli, BaeR stimulates multidrug resistance via mdtABC (multidrug transporter ABC, formerly known as yegMNO) genes, which encode a resistance-nodulation-cell division (RND) drug efflux system. Members of this subfamily belong to the OmpR family of DNA-binding response regulators, which are characterized by a REC domain and a winged helix-turn-helix (wHTH) DNA-binding output effector domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381165 [Multi-domain]  Cd Length: 114  Bit Score: 37.74  E-value: 2.54e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28056667  23 AKLLFNTLREAGLDGS--FERVESESALREAlylfAPDIVLSDLSMSGFHGYQALRVVREVGNTPFIFVSSKMGEDIAVE 100
Cdd:cd19938  12 AQLLIDYLRAAGYAPTllAHGDQVLPYVRHT----PPDLILLDLMLPGTDGLTLCREIRRFSDVPIIMVTARVEEIDRLL 87
                        90
                ....*....|..
gi 28056667 101 ALQEGANDYIIK 112
Cdd:cd19938  88 GLELGADDYICK 99
PRK10693 PRK10693
two-component system response regulator RssB;
49-136 2.54e-03

two-component system response regulator RssB;


Pssm-ID: 182652 [Multi-domain]  Cd Length: 303  Bit Score: 39.97  E-value: 2.54e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28056667   49 REALYL---FAPDIVLSDLSMSGFHGYQALRVVREVGN-TPFIFVS--SKMGeDIAvEALQEGANDYIIK--QNLVRLPS 120
Cdd:PRK10693   7 VDALELlggFTPDLIICDLAMPRMNGIEFVEHLRNRGDqTPVLVISatENMA-DIA-KALRLGVQDVLLKpvKDLNRLRE 84
                         90       100
                 ....*....|....*....|
gi 28056667  121 AVTR----AVRESRAELERQ 136
Cdd:PRK10693  85 MVFAclypSMFNSRVEEEER 104
REC_NtrX-like cd17550
phosphoacceptor receiver (REC) domain of nitrogen assimilation regulatory protein NtrX and ...
49-127 2.59e-03

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: 37.86  E-value: 2.59e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28056667  49 REALYLF---APDIVLSDLSMSGFHGYQALRVVREVG-NTPFIFVSSKMGEDIAVEALQEGANDYIIKQ-NLVRLPSAVT 123
Cdd:cd17550  32 EEALKLIkerRPDLVLLDIWLPDMDGLELLKEIKEKYpDLPVIMISGHGTIETAVKATKLGAYDFIEKPlSLDRLLLTIE 111

                ....
gi 28056667 124 RAVR 127
Cdd:cd17550 112 RALE 115
HATPase_AgrC-ComD-like cd16935
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
290-351 3.52e-03

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Staphylococcus aureus AgrC and Streptococcus pneumoniae ComD which are involved in quorum sensing; This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component sensor histidine kinase (HKs) including Staphylococcus aureus AgrC which is an HK of the accessory gene regulator (agr) quorum sensing two-component regulatory system (TCS) AgrC-AgrA. The agr system plays a part in the transition from persistent to virulent phenotype. This family also includes Streptococcus pneumoniae ComD HK of the ComD-ComE TCS, involved in quorum sensing and genetic competence.


Pssm-ID: 340412 [Multi-domain]  Cd Length: 134  Bit Score: 37.56  E-value: 3.52e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 28056667 290 DGDRICISVTDTgigMSEETRaRLFSPFFTTKSD-GTGLGLISCKRIAESYGGLIQVCSELGV 351
Cdd:cd16935  69 KKGFLIISIENS---YEGELK-KKNGLFLSTKKDkNHGIGLKSIREIVKKYNGNLSIEYENGI 127
HATPase_SpoIIAB-like cd16942
Histidine kinase-like ATPase domain of SpoIIAB, an anti sigma-F factor and serine-protein ...
279-358 3.74e-03

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: 37.90  E-value: 3.74e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28056667 279 GGCLTLVAQRHDgDRICISVTDTGIGMSEETRARlfSPFFTTKS--DGTGLGLisckRIAESYGGLIQVCSELGVGTRFD 356
Cdd:cd16942  60 NGIVSISVIIED-GVVHLTVRDEGVGIPDIEEAR--QPLFTTKPelERSGMGF----TIMENFMDEVIVESEVNKGTTVY 132

                ..
gi 28056667 357 LI 358
Cdd:cd16942 133 LK 134
REC_typeB_ARR-like cd17584
phosphoacceptor receiver (REC) domain of type B Arabidopsis response regulators (ARRs) and ...
383-484 3.84e-03

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: 37.22  E-value: 3.84e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28056667 383 ILIVDGEATRLSLLGNALASQGYQPQLAPDGGAALKLLRHHA-EPDLVIID---SDI---LLLSAVCLLPTMqelgyrgP 455
Cdd:cd17584   1 VLVVDDDPTCLAILKRMLLRCGYQVTTCTDAEEALSMLRENKdEFDLVITDvhmPDMdgfEFLELIRLEMDL-------P 73
                        90       100
                ....*....|....*....|....*....
gi 28056667 456 AIVLEDAGQPLRREHFSKDLAVHMLRKPL 484
Cdd:cd17584  74 VIMMSADGSTSTVMKGLAHGACDYLLKPV 102
ComP COG4585
Signal transduction histidine kinase ComP [Signal transduction mechanisms];
288-364 3.89e-03

Signal transduction histidine kinase ComP [Signal transduction mechanisms];


Pssm-ID: 443642 [Multi-domain]  Cd Length: 252  Bit Score: 39.22  E-value: 3.89e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 28056667 288 RHDGDRICISVTDTGIGMSEETRArlfspffttksdGTGLGLISCKRIAESYGGLIQVCSELGVGTRFDLILPARAP 364
Cdd:COG4585 188 EVDDGELTLTVRDDGVGFDPEAAP------------GGGLGLRGMRERAEALGGTLTIGSAPGGGTRVRATLPLAAA 252
REC_OmpR_VirG cd17594
phosphoacceptor receiver (REC) domain of VirG-like OmpR family response regulators; VirG is ...
18-112 4.33e-03

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: 37.04  E-value: 4.33e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28056667  18 DSLEDAKLLFNTLREAGLD--GSFERVESESALREAlylfAPDIVLSDLSMSGFHGYQALRVVREVGNTPFIFVSSKMGE 95
Cdd:cd17594   7 DDAAMRHLLILYLRERGFDvtAAADGAEEARLMLHR----RVDLVLLDLRLGQESGLDLLRTIRARSDVPIIIISGDRRD 82
                        90
                ....*....|....*...
gi 28056667  96 DIA-VEALQEGANDYIIK 112
Cdd:cd17594  83 EIDrVVGLELGADDYLAK 100
COG3920 COG3920
Two-component sensor histidine kinase, HisKA and HATPase domains [Signal transduction ...
30-366 4.72e-03

Two-component sensor histidine kinase, HisKA and HATPase domains [Signal transduction mechanisms];


Pssm-ID: 443125 [Multi-domain]  Cd Length: 495  Bit Score: 39.50  E-value: 4.72e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28056667  30 LREAGLDGSFERVESESALREALYLFAPDIVLSDLSMSGFHGYQALRVVREVGNTPFIFVSSKMGEDIAVEALQEGANDY 109
Cdd:COG3920 178 LLLLAALLDLGLALAALAAAALLALLLALELLLALLLLLLLLLALLLVLLAALLRLRAAVLEELERRRRARGLGRLLLLL 257
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28056667 110 IIKQNLVRLPSAVTRAVRESRAELERQhvesELMRAQRLESLAMLAAGFSHDLRNILQpllIVPDLL---AGRTDDPQLH 186
Cdd:COG3920 258 LLLLLLLRALLLLAAGIRLVITERKRA----EEELEASLEEKELLLRELHHRVKNNLQ---VVSSLLrlqARRADDPEAR 330
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28056667 187 QlvsIVAECGRRGHEMAESILSFVRGSNkpRERVLLADLFQT-VQLLLRSSVPDCIALRIEECDEYLSVEAnyteLQQC- 264
Cdd:COG3920 331 E---ALEESQNRIQALALVHELLYQSED--WEGVDLRDYLRElLEPLRDSYGGRGIRIELDGPDVELPADA----AVPLg 401
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28056667 265 -LLN-LALNAI-HAMPTG--GCLTLVAQRhDGDRICISVTDTGIGMSEETRARlfspffttKSDGTGLGLIscKRIAESY 339
Cdd:COG3920 402 lILNeLVTNALkHAFLSGegGRIRVSWRR-EDGRLRLTVSDNGVGLPEDVDPP--------ARKGLGLRLI--RALVRQL 470
                       330       340
                ....*....|....*....|....*..
gi 28056667 340 GGLIQVcsELGVGTRFDLILPARAPAS 366
Cdd:COG3920 471 GGTLEL--DRPEGTRVRITFPLAELAA 495
PRK10710 PRK10710
DNA-binding transcriptional regulator BaeR; Provisional
56-112 4.75e-03

DNA-binding transcriptional regulator BaeR; Provisional


Pssm-ID: 182665 [Multi-domain]  Cd Length: 240  Bit Score: 38.90  E-value: 4.75e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 28056667   56 APDIVLSDLSMSGFHGYQALRVVREVGNTPFIFVSSKMGEDIAVEALQEGANDYIIK 112
Cdd:PRK10710  54 PPDLILLDLMLPGTDGLTLCREIRRFSDIPIVMVTAKIEEIDRLLGLEIGADDYICK 110
REC_citrate_TCS cd19925
phosphoacceptor receiver (REC) domain of citrate family two-component system response ...
49-112 5.21e-03

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: 36.84  E-value: 5.21e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 28056667  49 REALYLFAPDIVLSDLSMSGFHGYQALRVVREVG-NTPFIFVSSKMGEDIAVEALQEGANDYIIK 112
Cdd:cd19925  39 LKLLKERQPDLILLDIYLPDGNGLDLLRELRAAGhDVDVIVVTAANDVETVREALRLGVVDYLIK 103
REC_OmpR_CtrA cd17616
phosphoacceptor receiver (REC) domain of CtrA-like OmpR family response regulators; CtrA is ...
58-112 5.24e-03

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


Pssm-ID: 381132 [Multi-domain]  Cd Length: 114  Bit Score: 37.00  E-value: 5.24e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 28056667  58 DIVLSDLSMSGFHGYQALRVVREVG-NTPFIFVSSKMGEDIAVEALQEGANDYIIK 112
Cdd:cd17616  44 DIILLDLNLPDMSGYEVLRTLRLAKvKTPILILSGLADIEDKVKGLGFGADDYMTK 99
REC_OmpR_PrrA-like cd17627
phosphoacceptor receiver (REC) domain of PrrA-like OmpR family response regulators; The ...
42-135 5.53e-03

phosphoacceptor receiver (REC) domain of PrrA-like OmpR family response regulators; The Mycobacterium tuberculosis PrrA is part of the PrrA/PrrB two-component system (TCS) that has been implicated in early intracellular multiplication and is essential for viability. Also included in this subfamily is Mycobacterium tuberculosis MprA, part of the MprAB TCS that regulates EspR, a key regulator of the ESX-1 secretion system, and is required for establishment and maintenance of persistent infection in a tissue- and stage-specific fashion. PrrA and MprA belong to the OmpR family of DNA-binding response regulators, which contain N-terminal receiver (REC) and C-terminal DNA-binding winged helix-turn-helix effector domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381142 [Multi-domain]  Cd Length: 116  Bit Score: 36.98  E-value: 5.53e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28056667  42 VESESALREALYlFAPDIVLSDLSMSGFHGYQALRVVREVGN-TPFIFVSSKMGEDIAVEALQEGANDYIIKqnlvrlPS 120
Cdd:cd17627  29 VDGAEALRVISG-NRPDAVVLDVMMPRLDGLEVCRRLRAAGNdLPILVLTARDSVSDRVAGLDAGADDYLVK------PF 101
                        90
                ....*....|....*
gi 28056667 121 AVTRAVRESRAELER 135
Cdd:cd17627 102 ALEELLARVRALLRR 116
HisKA pfam00512
His Kinase A (phospho-acceptor) domain; dimerization and phospho-acceptor domain of histidine ...
150-211 5.64e-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: 5.64e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 28056667   150 SLAMLAAGFSHDLRNILQPLLIVPDLLAGRTDDPQLHQLVSIVAECGRRGHEMAESILSFVR 211
Cdd:pfam00512   1 AKSEFLANLSHELRTPLTAIRGYLELLRDEKLDEEQREYLETILRSAERLLRLINDLLDLSR 62
REC_OmpR_KdpE-like cd17620
phosphoacceptor receiver (REC) domain of KdpE-like OmpR family response regulators; KdpE is a ...
383-432 6.95e-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: 35.99  E-value: 6.95e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 28056667 383 ILIVDGEATRLSLLGNALASQGYQPQLAPDGGAALKLLRHHaEPDLVIID 432
Cdd:cd17620   1 ILVIEDEPQIRRFLRTALEAHGYRVFEAETGQEGLLEAATR-KPDLIILD 49
PRK11083 PRK11083
DNA-binding response regulator CreB; Provisional
382-432 8.10e-03

DNA-binding response regulator CreB; Provisional


Pssm-ID: 236838 [Multi-domain]  Cd Length: 228  Bit Score: 38.02  E-value: 8.10e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 28056667  382 RILIVDGEATRLSLLGNALASQGYQPQLAPDGGAALKLLRHHAePDLVIID 432
Cdd:PRK11083   5 TILLVEDEQAIADTLVYALQSEGFTVEWFERGLPALDKLRQQP-PDLVILD 54
YesN COG4753
Two-component response regulator, YesN/AraC family, consists of REC and AraC-type DNA-binding ...
382-432 8.23e-03

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: 35.90  E-value: 8.23e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|...
gi 28056667 382 RILIVDGEATRLSLLGNAL-ASQGYQP-QLAPDGGAALKLLRHHaEPDLVIID 432
Cdd:COG4753   1 KVLIVDDEPLIREGLKRILeWEAGFEVvGEAENGEEALELLEEH-KPDLVITD 52
REC_HupR-like cd17569
phosphoacceptor receiver (REC) domain of hydrogen uptake protein regulator (HupR) and similar ...
382-432 9.68e-03

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: 36.23  E-value: 9.68e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|.
gi 28056667 382 RILIVDGEATRLSLLGNALASQGYQPQLAPDGGAALKLLRHHaEPDLVIID 432
Cdd:cd17569   2 TILLVDDEPNILKALKRLLRREGYEVLTATSGEEALEILKQE-PVDVVISD 51
 
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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