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Conserved domains on  [gi|511672513|dbj|GAD01570|]
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two-component hybrid sensor and regulator [Agarivorans albus MKT 106]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
CodB COG1457
Purine-cytosine permease or related protein [Nucleotide transport and metabolism];
15-487 1.54e-132

Purine-cytosine permease or related protein [Nucleotide transport and metabolism];


:

Pssm-ID: 441066 [Multi-domain]  Cd Length: 448  Bit Score: 410.41  E-value: 1.54e-132
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513   15 RWVANQTLEDYALRFTSKNARKWSVARVSNTALGAISFLALEAIGGALILNFGFNNSLIAILLVSAIIFFCGLPISYYAA 94
Cdd:COG1457     7 RSNRAETVEDYGLEPVPESERHGSPRSLFWVWFGANVALATFVIGALLGLGLGFWQALLAILLGNLIGFLLGALIAYIGA 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513   95 RYGVDIDLLTRGAgFGYIGSTITSLIYASFTFIFFAIEAAIMASALELLF---NIPLSIGYLISAIVVIPLVTHGITFIS 171
Cdd:COG1457    87 RTGLPTMLLSRAA-FGYRGSTLPSLLNALTTIGWFAVEAAIAAQALAALLgglGIPLVLAYLIVGLLVILLAIFGYRAIS 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  172 RFQLWSQPIWLVLQLAPLIFILWHESsaINNWLQFegklesgnSGEFNLHLFGAASGILFSL-MAQIGEQVDFLRFMPEA 250
Cdd:COG1457   166 RLQRWAVPLLLVLFVLLVVLALSHPG--LSALLAY--------PPGSSPLSFGAAVSVVAGLfISWAPYAADYSRYLPRK 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  251 KKKHRACWWVAllsagPGWIIVGALKILLGSFLVVLAINAGvaedvagDPIQMyqvaFSYMAQSPLLALslAGIFVLVCQ 330
Cdd:COG1457   236 TSGRAVFWATF-----LGFVLGGVLLMLLGALLAAAAPGAA-------DPVGA----LGALLPTGLGVP--ALLVVILSQ 297
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  331 LKINVTNAYAGSIAWSNFFSRLthshpGRVVWLVFNVIIALLIMELGIYAALEDILGIYSNVAVAWVGALVADLVINKPL 410
Cdd:COG1457   298 WTINVLNLYSASLALSNLFPRL-----GRVVATLVVGVIGTLLALLGFLDAFENFLLLLGVVLPPWGGIMLADYFLVRRG 372
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 511672513  411 GYSPKHIEFKRAHLYDINPVGVGSMVIASVLSIYC--YTGNAGDTAQALAPYIGLSTAFVCSPIIAiltkgRYYLAREP 487
Cdd:COG1457   373 RYDPDALFDRRGRYGGVNWVGLIAWLLGSVVGILFvnTPGLFGPALADLSWLVALVVAAVLYLLLA-----RYYLARPE 446
TMAO_torS super family cl37193
TMAO reductase sytem sensor TorS; This protein, TorS, is part of a regulatory system for the ...
637-1102 5.57e-82

TMAO reductase sytem sensor TorS; This protein, TorS, is part of a regulatory system for the torCAD operon that encodes the pterin molybdenum cofactor-containing enzyme trimethylamine-N-oxide (TMAO) reductase (TorA), a cognate chaperone (TorD), and a penta-haem cytochrome (TorC). TorS works together with the inducer-binding protein TorT and the response regulator TorR. TorS contains histidine kinase ATPase (pfam02518), HAMP (pfam00672), phosphoacceptor (pfam00512), and phosphotransfer (pfam01627) domains and a response regulator receiver domain (pfam00072). [Signal transduction, Two-component systems]


The actual alignment was detected with superfamily member TIGR02956:

Pssm-ID: 274362 [Multi-domain]  Cd Length: 968  Bit Score: 288.60  E-value: 5.57e-82
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513   637 QRQTEL------LSREISAHEvtdqalqQAKETAESANQAKSRYLTGISHELRTPLNSVLGYAQLLEKSPsLAPEHSAKV 710
Cdd:TIGR02956  431 QRTQELaetnerLNAEVKNHA-------KARAEAEEANRAKSAFLATMSHEIRTPLNGILGTLELLGDTG-LTSQQQQYL 502
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513   711 SLIKRSGEHLADIIEGLLDISRIEAGRIELQRDEVAIGELLDDLVDMFSLQAKSKGISFVYNPSPYLPNWVTADETQLRQ 790
Cdd:TIGR02956  503 QVINRSGESLLDILNDILDYSKIEAGHLSISPRPFDLNALLDDVHHLMVSRAQLKGIQLRLNIPEQLPNWWQGDGPRIRQ 582
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513   791 ILINLLSNAVKFTQQGSVTLDVYYRNQVA-EFTITDSGVGISEQDIERIFKPFERVEKRDipSSPGTGLGLTITQLLTDI 869
Cdd:TIGR02956  583 VLINLVGNAIKFTDRGSVVLRVSLNDDSSlLFEVEDTGCGIAEEEQATLFDAFTQADGRR--RSGGTGLGLAISQRLVEA 660
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513   870 MGGNISVSSEIGKGSSFKLSIMLASLNKEQQPQSVQApvnsIKGPSKTVMVVDDDPNHRNLVSEILSPLGFVV---HEAN 946
Cdd:TIGR02956  661 MDGELGVESELGVGSCFWFTLPLTRGKPAEDSATLTV----IDLPPQRVLLVEDNEVNQMVAQGFLTRLGHKVtlaESGQ 736
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513   947 DALVCLSNtylSAIDLFLLDISMPDMNGWQLLKKLRS---NGISVPIIMVSADAteapyFNAAEEIHEPALHNDYLAKPM 1023
Cdd:TIGR02956  737 SALECFHQ---HAFDLALLDINLPDGDGVTLLQQLRAiygAKNEVKFIAFSAHV-----FNEDVAQYLAAGFDGFLAKPV 808
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  1024 RDNALLEKVAKALAIDWNYQNTSTQSASPE---------PQALNIQLNQSQREQLQEIAEMAQLGFVQGIDRLIK--NLE 1092
Cdd:TIGR02956  809 VEEQLTAMIAVILAGGKSNTEAPVLSASPSfdsasvienAQADDIPESNQASEFLLDEEQLQQDIEVLGVEKVRQlvALF 888
                          490
                   ....*....|
gi 511672513  1093 KDSALHTITR 1102
Cdd:TIGR02956  889 KTSSAEQLEE 898
 
Name Accession Description Interval E-value
CodB COG1457
Purine-cytosine permease or related protein [Nucleotide transport and metabolism];
15-487 1.54e-132

Purine-cytosine permease or related protein [Nucleotide transport and metabolism];


Pssm-ID: 441066 [Multi-domain]  Cd Length: 448  Bit Score: 410.41  E-value: 1.54e-132
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513   15 RWVANQTLEDYALRFTSKNARKWSVARVSNTALGAISFLALEAIGGALILNFGFNNSLIAILLVSAIIFFCGLPISYYAA 94
Cdd:COG1457     7 RSNRAETVEDYGLEPVPESERHGSPRSLFWVWFGANVALATFVIGALLGLGLGFWQALLAILLGNLIGFLLGALIAYIGA 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513   95 RYGVDIDLLTRGAgFGYIGSTITSLIYASFTFIFFAIEAAIMASALELLF---NIPLSIGYLISAIVVIPLVTHGITFIS 171
Cdd:COG1457    87 RTGLPTMLLSRAA-FGYRGSTLPSLLNALTTIGWFAVEAAIAAQALAALLgglGIPLVLAYLIVGLLVILLAIFGYRAIS 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  172 RFQLWSQPIWLVLQLAPLIFILWHESsaINNWLQFegklesgnSGEFNLHLFGAASGILFSL-MAQIGEQVDFLRFMPEA 250
Cdd:COG1457   166 RLQRWAVPLLLVLFVLLVVLALSHPG--LSALLAY--------PPGSSPLSFGAAVSVVAGLfISWAPYAADYSRYLPRK 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  251 KKKHRACWWVAllsagPGWIIVGALKILLGSFLVVLAINAGvaedvagDPIQMyqvaFSYMAQSPLLALslAGIFVLVCQ 330
Cdd:COG1457   236 TSGRAVFWATF-----LGFVLGGVLLMLLGALLAAAAPGAA-------DPVGA----LGALLPTGLGVP--ALLVVILSQ 297
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  331 LKINVTNAYAGSIAWSNFFSRLthshpGRVVWLVFNVIIALLIMELGIYAALEDILGIYSNVAVAWVGALVADLVINKPL 410
Cdd:COG1457   298 WTINVLNLYSASLALSNLFPRL-----GRVVATLVVGVIGTLLALLGFLDAFENFLLLLGVVLPPWGGIMLADYFLVRRG 372
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 511672513  411 GYSPKHIEFKRAHLYDINPVGVGSMVIASVLSIYC--YTGNAGDTAQALAPYIGLSTAFVCSPIIAiltkgRYYLAREP 487
Cdd:COG1457   373 RYDPDALFDRRGRYGGVNWVGLIAWLLGSVVGILFvnTPGLFGPALADLSWLVALVVAAVLYLLLA-----RYYLARPE 446
TMAO_torS TIGR02956
TMAO reductase sytem sensor TorS; This protein, TorS, is part of a regulatory system for the ...
637-1102 5.57e-82

TMAO reductase sytem sensor TorS; This protein, TorS, is part of a regulatory system for the torCAD operon that encodes the pterin molybdenum cofactor-containing enzyme trimethylamine-N-oxide (TMAO) reductase (TorA), a cognate chaperone (TorD), and a penta-haem cytochrome (TorC). TorS works together with the inducer-binding protein TorT and the response regulator TorR. TorS contains histidine kinase ATPase (pfam02518), HAMP (pfam00672), phosphoacceptor (pfam00512), and phosphotransfer (pfam01627) domains and a response regulator receiver domain (pfam00072). [Signal transduction, Two-component systems]


Pssm-ID: 274362 [Multi-domain]  Cd Length: 968  Bit Score: 288.60  E-value: 5.57e-82
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513   637 QRQTEL------LSREISAHEvtdqalqQAKETAESANQAKSRYLTGISHELRTPLNSVLGYAQLLEKSPsLAPEHSAKV 710
Cdd:TIGR02956  431 QRTQELaetnerLNAEVKNHA-------KARAEAEEANRAKSAFLATMSHEIRTPLNGILGTLELLGDTG-LTSQQQQYL 502
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513   711 SLIKRSGEHLADIIEGLLDISRIEAGRIELQRDEVAIGELLDDLVDMFSLQAKSKGISFVYNPSPYLPNWVTADETQLRQ 790
Cdd:TIGR02956  503 QVINRSGESLLDILNDILDYSKIEAGHLSISPRPFDLNALLDDVHHLMVSRAQLKGIQLRLNIPEQLPNWWQGDGPRIRQ 582
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513   791 ILINLLSNAVKFTQQGSVTLDVYYRNQVA-EFTITDSGVGISEQDIERIFKPFERVEKRDipSSPGTGLGLTITQLLTDI 869
Cdd:TIGR02956  583 VLINLVGNAIKFTDRGSVVLRVSLNDDSSlLFEVEDTGCGIAEEEQATLFDAFTQADGRR--RSGGTGLGLAISQRLVEA 660
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513   870 MGGNISVSSEIGKGSSFKLSIMLASLNKEQQPQSVQApvnsIKGPSKTVMVVDDDPNHRNLVSEILSPLGFVV---HEAN 946
Cdd:TIGR02956  661 MDGELGVESELGVGSCFWFTLPLTRGKPAEDSATLTV----IDLPPQRVLLVEDNEVNQMVAQGFLTRLGHKVtlaESGQ 736
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513   947 DALVCLSNtylSAIDLFLLDISMPDMNGWQLLKKLRS---NGISVPIIMVSADAteapyFNAAEEIHEPALHNDYLAKPM 1023
Cdd:TIGR02956  737 SALECFHQ---HAFDLALLDINLPDGDGVTLLQQLRAiygAKNEVKFIAFSAHV-----FNEDVAQYLAAGFDGFLAKPV 808
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  1024 RDNALLEKVAKALAIDWNYQNTSTQSASPE---------PQALNIQLNQSQREQLQEIAEMAQLGFVQGIDRLIK--NLE 1092
Cdd:TIGR02956  809 VEEQLTAMIAVILAGGKSNTEAPVLSASPSfdsasvienAQADDIPESNQASEFLLDEEQLQQDIEVLGVEKVRQlvALF 888
                          490
                   ....*....|
gi 511672513  1093 KDSALHTITR 1102
Cdd:TIGR02956  889 KTSSAEQLEE 898
BaeS COG0642
Signal transduction histidine kinase [Signal transduction mechanisms];
563-893 4.29e-78

Signal transduction histidine kinase [Signal transduction mechanisms];


Pssm-ID: 440407 [Multi-domain]  Cd Length: 328  Bit Score: 259.84  E-value: 4.29e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  563 RLLNFSGLMALIALLIASLFYLVYSRIPVTEFATKAAVSATLSHVFFLLMIIVGVLVWLFVLANDSRQFALDESQRQTEL 642
Cdd:COG0642     2 LLLLLLLVLLLLLLLLLLLALLLLLLLLLLLALLLLLALLLLLLLLLLLLLLLALALLALLLLLLLLLLLLLLLLLLLLL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  643 LSREISAHEVTDQALQQAKETAESANQAKSRYLTGISHELRTPLNSVLGYAQLLEKSPSlaPEHSAKVSLIKRSGEHLAD 722
Cdd:COG0642    82 LLLLLLLLLLLLLLLLALLLLLEEANEAKSRFLANVSHELRTPLTAIRGYLELLLEELD--EEQREYLETILRSADRLLR 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  723 IIEGLLDISRIEAGRIELQRDEVAIGELLDDLVDMFSLQAKSKGISFVYNPSPYLPnWVTADETQLRQILINLLSNAVKF 802
Cdd:COG0642   160 LINDLLDLSRLEAGKLELEPEPVDLAELLEEVVELFRPLAEEKGIELELDLPDDLP-TVRGDPDRLRQVLLNLLSNAIKY 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  803 TQQGS-VTLDVYYRNQVAEFTITDSGVGISEQDIERIFKPFERVEKRDipSSPGTGLGLTITQLLTDIMGGNISVSSEIG 881
Cdd:COG0642   239 TPEGGtVTVSVRREGDRVRISVEDTGPGIPPEDLERIFEPFFRTDPSR--RGGGTGLGLAIVKRIVELHGGTIEVESEPG 316
                         330
                  ....*....|..
gi 511672513  882 KGSSFKLSIMLA 893
Cdd:COG0642   317 KGTTFTVTLPLA 328
PRK15347 PRK15347
two component system sensor kinase;
633-1100 7.74e-66

two component system sensor kinase;


Pssm-ID: 237951 [Multi-domain]  Cd Length: 921  Bit Score: 240.70  E-value: 7.74e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  633 LDESQRQTELLsrEISAHEVTdQALQQAKETAESANQAKSRYLTGISHELRTPLNSVLGYAQLLEKSPsLAPEHSAKVSL 712
Cdd:PRK15347  363 LDTLNEQYDTL--ENKVAERT-QALAEAKQRAEQANKRKSEHLTTISHEIRTPLNGVLGALELLQNTP-LTAEQMDLADT 438
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  713 IKRSGEHLADIIEGLLDISRIEAGRIELQRDEVAIGELLDDLVDMFSLQAKSKGIS---FVynpSPYLPNWVTADETQLR 789
Cdd:PRK15347  439 ARQCTLSLLAIINNLLDFSRIESGQMTLSLEETALLPLLDQAMLTIQGPAQSKSLTlrtFV---GAHVPLYLHLDSLRLR 515
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  790 QILINLLSNAVKFTQQGSVTLDVYYRNQVAEFTITDSGVGISEQDIERIFKPFERVEKrdipSSPGTGLGLTITQLLTDI 869
Cdd:PRK15347  516 QILVNLLGNAVKFTETGGIRLRVKRHEQQLCFTVEDTGCGIDIQQQQQIFTPFYQADT----HSQGTGLGLTIASSLAKM 591
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  870 MGGNISVSSEIGKGSSFKLSIML-------------------------------------ASLNKE------------QQ 900
Cdd:PRK15347  592 MGGELTLFSTPGVGSCFSLVLPLneyappeplkgelsaplalhrqlsawgitcqpghqnpALLDPElaylpgrlydllQQ 671
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  901 PQSVQAPVNSIKGP----SKTVMVVDDDPNHRNLVSEILSPLG---FVVHEANDALVcLSNTYLsaIDLFLLDISMPDMN 973
Cdd:PRK15347  672 IIQGAPNEPVINLPlqpwQLQILLVDDVETNRDIIGMMLVELGqqvTTAASGTEALE-LGRQHR--FDLVLMDIRMPGLD 748
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  974 GWQLLKKLR--SNGIS--VPIIMVSADAteapyfnAAEEIH--EPALHNDYLAKPMRdnalLEKVAKALAIDWNYQ---N 1044
Cdd:PRK15347  749 GLETTQLWRddPNNLDpdCMIVALTANA-------APEEIHrcKKAGMNHYLTKPVT----LAQLARALELAAEYQllrG 817
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 511672513 1045 TSTQSASPEPQAL----NIQLNQSQREQLQEIAEMAQLGfvqgidrlIKNLEK-DSALHTI 1100
Cdd:PRK15347  818 IELSPQDSSCSPLldtdDMALNSKLYQSLLLLLAQIEQA--------VENQEVlSQLLHTL 870
HATPase_EvgS-ArcB-TorS-like cd16922
Histidine kinase-like ATPase domain of two-component sensor histidine kinases, many are hybrid ...
788-890 7.32e-38

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: 137.24  E-value: 7.32e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  788 LRQILINLLSNAVKFTQQGSVTLDVYYRNQ-----VAEFTITDSGVGISEQDIERIFKPFERVEKRDIPSSPGTGLGLTI 862
Cdd:cd16922     1 LRQILLNLLGNAIKFTEEGEVTLRVSLEEEeedgvQLRFSVEDTGIGIPEEQQARLFEPFSQADSSTTRKYGGTGLGLAI 80
                          90       100
                  ....*....|....*....|....*...
gi 511672513  863 TQLLTDIMGGNISVSSEIGKGSSFKLSI 890
Cdd:cd16922    81 SKKLVELMGGDISVESEPGQGSTFTFTL 108
HATPase_c smart00387
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.
783-893 9.21e-33

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


Pssm-ID: 214643 [Multi-domain]  Cd Length: 111  Bit Score: 122.76  E-value: 9.21e-33
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513    783 ADETQLRQILINLLSNAVKFT-QQGSVTLDVYYRNQVAEFTITDSGVGISEQDIERIFKPFERVEKRDiPSSPGTGLGLT 861
Cdd:smart00387    1 GDPDRLRQVLSNLLDNAIKYTpEGGRITVTLERDGDHVEITVEDNGPGIPPEDLEKIFEPFFRTDKRS-RKIGGTGLGLS 79
                            90       100       110
                    ....*....|....*....|....*....|..
gi 511672513    862 ITQLLTDIMGGNISVSSEIGKGSSFKLSIMLA 893
Cdd:smart00387   80 IVKKLVELHGGEISVESEPGGGTTFTITLPLE 111
HATPase_c pfam02518
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the ...
783-890 1.06e-27

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: 108.22  E-value: 1.06e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513   783 ADETQLRQILINLLSNAVKFT-QQGSVTLDVYYRNQVaEFTITDSGVGISEQDIERIFKPFERVEKRdipSSPGTGLGLT 861
Cdd:pfam02518    1 GDELRLRQVLSNLLDNALKHAaKAGEITVTLSEGGEL-TLTVEDNGIGIPPEDLPRIFEPFSTADKR---GGGGTGLGLS 76
                           90       100
                   ....*....|....*....|....*....
gi 511672513   862 ITQLLTDIMGGNISVSSEIGKGSSFKLSI 890
Cdd:pfam02518   77 IVRKLVELLGGTITVESEPGGGTTVTLTL 105
MtrAB_MtrB NF040691
MtrAB system histidine kinase MtrB;
583-890 2.42e-25

MtrAB system histidine kinase MtrB;


Pssm-ID: 468655 [Multi-domain]  Cd Length: 507  Bit Score: 111.66  E-value: 2.42e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  583 YLVYSRIPVTEfaTKAAVSATLSHVFFLLMIIVGVLVWL---FVL------ANDSRQFAL-DESQRQTELLSREIS--AH 650
Cdd:NF040691  171 YLLFPLEDEQS--TLALVRGTLLLGGLALVVLLGLIAWLvtrQVVapvrsaARTAERFAAgDLSERMPVKGEDDLArlAR 248
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  651 EVTDQA--LQQAKETAESANQAKSRYLTGISHELRTPLNSVLGYAQLL-EKSPSLAPEHSAKVSL----IKRSGEHLADi 723
Cdd:NF040691  249 SFNQMAdsLQRQIRQLEELSRLQQRFVSDVSHELRTPLTTIRMAADVIhDSRDDFDPATARSAELlhteLDRFESLLSD- 327
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  724 iegLLDISRIEAGRIELQRDEVAIGELLDDLVDMFSLQAKSKGISFVYNpSPYLPNWVTADETQLRQILINLLSNAVKFT 803
Cdd:NF040691  328 ---LLEISRFDAGAAELDVEPVDLRPLVRRVVDALRQLAERAGVELRVD-APGTPVVAEVDPRRVERVLRNLVVNAIEHG 403
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  804 QQGSVTLDVYY-RNQVAeFTITDSGVGISEQDIERIFKPFERVEKRDIPSSPGTGLGLTITQLLTDIMGGNISVSSEIGK 882
Cdd:NF040691  404 EGKPVVVTVAQdDTAVA-VTVRDHGVGLKPGEVALVFDRFWRADPARARTTGGTGLGLAIALEDARLHGGWLEAWGRPGQ 482

                  ....*...
gi 511672513  883 GSSFKLSI 890
Cdd:NF040691  483 GSQFRLTL 490
SLC-NCS1sbd_CobB-like cd11484
nucleobase-cation-symport-1 (NCS1) transporter CobB-like; solute-binding domain; This NCS1 ...
47-469 1.41e-18

nucleobase-cation-symport-1 (NCS1) transporter CobB-like; solute-binding domain; This NCS1 subfamily includes Escherichia coli CodB (cytosine permease), and the Saccharomyces cerevisiae transporters: Fcy21p (Purine-cytosine permease), and vitamin B6 transporter Tpn1. NCS1s are essential components of salvage pathways for nucleobases and related metabolites; their known substrates include allantoin, uracil, thiamine, and nicotinamide riboside. NCS1s belong to a superfamily which also contains the solute carrier 5 family sodium/glucose transporters (SLC5s), and solute carrier 6 family neurotransmitter transporters (SLC6s).


Pssm-ID: 271377 [Multi-domain]  Cd Length: 406  Bit Score: 89.59  E-value: 1.41e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513   47 LGAISFLALEAIGGALILNFGFNNSLIAILLVSAIIFFCGLPISYYAARYGVDIDLLTRgAGFGYIGSTITSLIYASFTF 126
Cdd:cd11484    17 LGANFFLASMVTGALLGVGLSLSQAILAVLLGNLIGGAYMALLGYIGARTGLPQMLLSR-ASFGEKGSYLPSLLLGITQI 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  127 IFFAIEAAIMASALELLFNIP--LSIGYLISAIVVIPLVTHGITFISRFQLWSQPIWLVLQLApLIFILWHeSSAINNWL 204
Cdd:cd11484    96 GWFGVGTAMFAIALSKLLGINgsLWLLILIAGVLMTLTAIFGYKALHKLEKIAVPLIIALFVY-SVVLALR-DYGVGGLA 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  205 QFEGKLESGNSGEFNLhlfGAASGILFSLMAQigeqvDFLRFMpeakKKHRACWWVALLSAGPGWIIVGALKILLGSflv 284
Cdd:cd11484   174 ALTATGPLSFLVAVSL---VAGSFISGATYTA-----DYSRYA----KSSKKAFWATFLGFFVGNSLMMILGALLAA--- 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  285 vlainagvaedVAGDPIQMYQVAfsymaqspLLALSLAGIFVLVC-QLKINVTNAYAGSIAWSNFFSRLTHshpgRVVWL 363
Cdd:cd11484   239 -----------ATGTADISEVMI--------AQGLGIPAILVLVLnIWTTNDNNLYSSGLSLSNITKIFRR----KVLTL 295
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  364 VfNVIIALLIMELGIYAALEDILGIYSNVAVAWVGALVAD-LVINKplGYSPKHIEFKRAHLyDINPVGVGSMVIASVLS 442
Cdd:cd11484   296 V-AGIVGTLLAALGIYNHFLNFLLLLGYALPPWGGVMLADyFVVRR--GRYDIDALADPQYG-GVNWAALIAWAVGVAVG 371
                         410       420
                  ....*....|....*....|....*..
gi 511672513  443 IYCYTGNAGDTaqALAPYIGLSTAFVC 469
Cdd:cd11484   372 IPFPYGLLGGG--GIAPINGLLVAAVV 396
BaeS_SmeS NF012163
sensor histidine kinase efflux regulator BaeS;
602-875 1.74e-18

sensor histidine kinase efflux regulator BaeS;


Pssm-ID: 411086 [Multi-domain]  Cd Length: 457  Bit Score: 89.89  E-value: 1.74e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  602 ATLSHVFFLLMIIVGVLVWLFVLANDSRQFALDESQRQTELLSREISAHEVTDqaLQQAKETAESANQAKSRYLTGISHE 681
Cdd:NF012163  173 ALLLAALAAFLLARGLLAPVKRLVEATHRLAAGDYTTRVTPTSNDELGKLAQD--FNQLASTLEKNEQMRRDFMADISHE 250
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  682 LRTPLNSVLGYAQLLEKS-PSLAPEHsakVSLIKRSGEHLADIIEGLLDISRIEAGRIELQRDEVAIGELLDDLVDMFSL 760
Cdd:NF012163  251 LRTPLAVLRAELEAIQDGiRKFTPES---LDSLQAEVGTLTKLVDDLHDLSMSDEGALAYQKASVDLVPLLEVEGGAFRE 327
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  761 QAKSKGISFVYNpspyLPNWVT--ADETQLRQILINLLSNAVKFTQQ-GSVTLDVYYRNQVAEFTITDSGVGISEQDIER 837
Cdd:NF012163  328 RFASAGLELEVS----LPDSSLvfGDRDRLMQLFNNLLENSLRYTDSgGSLHISASQRPKEVTLTVADSAPGVSDEQLAR 403
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 511672513  838 IFKPFERVEKRDIPSSPGTGLGLTITQLLTDIMGGNIS 875
Cdd:NF012163  404 LFERFYRVEVSRNRASGGSGLGLAISLNIVQAHGGTLH 441
AdeS_HK NF012226
two-component sensor histidine kinase AdeS; Mutations in this component of the two-component ...
678-890 3.23e-15

two-component sensor histidine kinase AdeS; Mutations in this component of the two-component regulatory system for the AdeABC efflux pump can confer adaptive resistance to certain antibiotics, including tigecycline.


Pssm-ID: 411090 [Multi-domain]  Cd Length: 353  Bit Score: 78.50  E-value: 3.23e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  678 ISHELRTPLNSVLGYAQ-----LLEKSPSLAPehsakvSLIKRSgEHLADIIEGLLDISRIEAGRIELQRDEVAIGELLD 752
Cdd:NF012226  145 IAHELRTPITILQGRLQgildgVFEPDPALFK------SLLNQV-EGLSHLVEDLRTLSLVENQQLRLNYESVDLKDSIE 217
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  753 DLVDMFSLQAKSKGISFVYNPSPYLpnwVTADETQLRQILINLLSNAVKFTQQGSVTLDVYYRNQVAEFTITDSGVGISE 832
Cdd:NF012226  218 KVLKMFEDRLEQAQLTIVLNLTATP---VFCDRRRIEQVLIALIDNAIRYANAGKLKISSSVIQDDWILQIEDEGPGIAE 294
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 511672513  833 QDIERIFKPFERVEKRDIPSSPGTGLGLTITQLLTDIMGGNISVSSEIGkGSSFKLSI 890
Cdd:NF012226  295 EYQQDLFNPFFRLEQSRNKEFGGTGLGLAVVHAIVIAHKGSIEYSNSQG-NSVFTIKL 351
Transp_cyt_pur pfam02133
Permease for cytosine/purines, uracil, thiamine, allantoin;
34-431 4.54e-07

Permease for cytosine/purines, uracil, thiamine, allantoin;


Pssm-ID: 251109  Cd Length: 439  Bit Score: 53.55  E-value: 4.54e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513    34 ARKWSVARVSNTALGA---ISFLALEAIGGALILNFGfnNSLIAILLVSAIIFFCGLPISYYAARYGVDIDLLTRgAGFG 110
Cdd:pfam02133    6 ERTWSTRNLFSFWLGAnfnINTWVIGALGVALGLNWW--QSVLAIIAGNLIGAIFVALLGRAGAKYGLPFPILSR-ASFG 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513   111 YIGSTITSLIYASFTFIFFAIEAAIMASALELLFNIPLS----------------IGYLISAIVVIPLVTHGITFISRFQ 174
Cdd:pfam02133   83 IRGSLLPSLLRAVIACGWFGIQAWIGSEALLLMLGKIFGhwlwigaipgtgltelVTFFIFWLVHLYIVWLGVSAIRVFF 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513   175 LWSQPIWLVLQLAPLIFILwhesSAINNWLQFEGKLESGNSGEFNLHLFGAASGILfSLMAQIGeqvDFLRFMPEAKKKH 254
Cdd:pfam02133  163 VIAAPLIPVAAFGFLIWAA----VKAGGGPVFDQPVSPGKSELFLSAVAGCAAGWA-TLIANAP---DFTRYAPTARSSS 234
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513   255 RACWwvallSAGPGWIIVGALKILLGSFLVVLAINAGVAedvagDPIQMYQVAfsymaqSPLLALSLAGIFVLVCQLKIN 334
Cdd:pfam02133  235 KIQL-----VAVPGGFTLFALIGILGAAAAYAAYGAPAW-----DPLDILARF------DPTAGVFLPAILVALAQLGTN 298
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513   335 VTNAY--AGSIAWSNFFSRLThshpgRVVWLVFNVIIALLIMELGIYAALEDI----LGIYSNVAVAWVGALVADLVINk 408
Cdd:pfam02133  299 ISANLysAGSDLAALLPKKIN-----RKRGSLIAAIIALVICPWKLLGNSAFMfttfLSLLSGFLSPVAGVIIADYFVV- 372
                          410       420
                   ....*....|....*....|...
gi 511672513   409 plgyspKHIEFKRAHLYDINPVG 431
Cdd:pfam02133  373 ------RRGYLHVAHLYTRRRGS 389
 
Name Accession Description Interval E-value
CodB COG1457
Purine-cytosine permease or related protein [Nucleotide transport and metabolism];
15-487 1.54e-132

Purine-cytosine permease or related protein [Nucleotide transport and metabolism];


Pssm-ID: 441066 [Multi-domain]  Cd Length: 448  Bit Score: 410.41  E-value: 1.54e-132
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513   15 RWVANQTLEDYALRFTSKNARKWSVARVSNTALGAISFLALEAIGGALILNFGFNNSLIAILLVSAIIFFCGLPISYYAA 94
Cdd:COG1457     7 RSNRAETVEDYGLEPVPESERHGSPRSLFWVWFGANVALATFVIGALLGLGLGFWQALLAILLGNLIGFLLGALIAYIGA 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513   95 RYGVDIDLLTRGAgFGYIGSTITSLIYASFTFIFFAIEAAIMASALELLF---NIPLSIGYLISAIVVIPLVTHGITFIS 171
Cdd:COG1457    87 RTGLPTMLLSRAA-FGYRGSTLPSLLNALTTIGWFAVEAAIAAQALAALLgglGIPLVLAYLIVGLLVILLAIFGYRAIS 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  172 RFQLWSQPIWLVLQLAPLIFILWHESsaINNWLQFegklesgnSGEFNLHLFGAASGILFSL-MAQIGEQVDFLRFMPEA 250
Cdd:COG1457   166 RLQRWAVPLLLVLFVLLVVLALSHPG--LSALLAY--------PPGSSPLSFGAAVSVVAGLfISWAPYAADYSRYLPRK 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  251 KKKHRACWWVAllsagPGWIIVGALKILLGSFLVVLAINAGvaedvagDPIQMyqvaFSYMAQSPLLALslAGIFVLVCQ 330
Cdd:COG1457   236 TSGRAVFWATF-----LGFVLGGVLLMLLGALLAAAAPGAA-------DPVGA----LGALLPTGLGVP--ALLVVILSQ 297
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  331 LKINVTNAYAGSIAWSNFFSRLthshpGRVVWLVFNVIIALLIMELGIYAALEDILGIYSNVAVAWVGALVADLVINKPL 410
Cdd:COG1457   298 WTINVLNLYSASLALSNLFPRL-----GRVVATLVVGVIGTLLALLGFLDAFENFLLLLGVVLPPWGGIMLADYFLVRRG 372
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 511672513  411 GYSPKHIEFKRAHLYDINPVGVGSMVIASVLSIYC--YTGNAGDTAQALAPYIGLSTAFVCSPIIAiltkgRYYLAREP 487
Cdd:COG1457   373 RYDPDALFDRRGRYGGVNWVGLIAWLLGSVVGILFvnTPGLFGPALADLSWLVALVVAAVLYLLLA-----RYYLARPE 446
TMAO_torS TIGR02956
TMAO reductase sytem sensor TorS; This protein, TorS, is part of a regulatory system for the ...
637-1102 5.57e-82

TMAO reductase sytem sensor TorS; This protein, TorS, is part of a regulatory system for the torCAD operon that encodes the pterin molybdenum cofactor-containing enzyme trimethylamine-N-oxide (TMAO) reductase (TorA), a cognate chaperone (TorD), and a penta-haem cytochrome (TorC). TorS works together with the inducer-binding protein TorT and the response regulator TorR. TorS contains histidine kinase ATPase (pfam02518), HAMP (pfam00672), phosphoacceptor (pfam00512), and phosphotransfer (pfam01627) domains and a response regulator receiver domain (pfam00072). [Signal transduction, Two-component systems]


Pssm-ID: 274362 [Multi-domain]  Cd Length: 968  Bit Score: 288.60  E-value: 5.57e-82
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513   637 QRQTEL------LSREISAHEvtdqalqQAKETAESANQAKSRYLTGISHELRTPLNSVLGYAQLLEKSPsLAPEHSAKV 710
Cdd:TIGR02956  431 QRTQELaetnerLNAEVKNHA-------KARAEAEEANRAKSAFLATMSHEIRTPLNGILGTLELLGDTG-LTSQQQQYL 502
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513   711 SLIKRSGEHLADIIEGLLDISRIEAGRIELQRDEVAIGELLDDLVDMFSLQAKSKGISFVYNPSPYLPNWVTADETQLRQ 790
Cdd:TIGR02956  503 QVINRSGESLLDILNDILDYSKIEAGHLSISPRPFDLNALLDDVHHLMVSRAQLKGIQLRLNIPEQLPNWWQGDGPRIRQ 582
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513   791 ILINLLSNAVKFTQQGSVTLDVYYRNQVA-EFTITDSGVGISEQDIERIFKPFERVEKRDipSSPGTGLGLTITQLLTDI 869
Cdd:TIGR02956  583 VLINLVGNAIKFTDRGSVVLRVSLNDDSSlLFEVEDTGCGIAEEEQATLFDAFTQADGRR--RSGGTGLGLAISQRLVEA 660
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513   870 MGGNISVSSEIGKGSSFKLSIMLASLNKEQQPQSVQApvnsIKGPSKTVMVVDDDPNHRNLVSEILSPLGFVV---HEAN 946
Cdd:TIGR02956  661 MDGELGVESELGVGSCFWFTLPLTRGKPAEDSATLTV----IDLPPQRVLLVEDNEVNQMVAQGFLTRLGHKVtlaESGQ 736
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513   947 DALVCLSNtylSAIDLFLLDISMPDMNGWQLLKKLRS---NGISVPIIMVSADAteapyFNAAEEIHEPALHNDYLAKPM 1023
Cdd:TIGR02956  737 SALECFHQ---HAFDLALLDINLPDGDGVTLLQQLRAiygAKNEVKFIAFSAHV-----FNEDVAQYLAAGFDGFLAKPV 808
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  1024 RDNALLEKVAKALAIDWNYQNTSTQSASPE---------PQALNIQLNQSQREQLQEIAEMAQLGFVQGIDRLIK--NLE 1092
Cdd:TIGR02956  809 VEEQLTAMIAVILAGGKSNTEAPVLSASPSfdsasvienAQADDIPESNQASEFLLDEEQLQQDIEVLGVEKVRQlvALF 888
                          490
                   ....*....|
gi 511672513  1093 KDSALHTITR 1102
Cdd:TIGR02956  889 KTSSAEQLEE 898
BaeS COG0642
Signal transduction histidine kinase [Signal transduction mechanisms];
563-893 4.29e-78

Signal transduction histidine kinase [Signal transduction mechanisms];


Pssm-ID: 440407 [Multi-domain]  Cd Length: 328  Bit Score: 259.84  E-value: 4.29e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  563 RLLNFSGLMALIALLIASLFYLVYSRIPVTEFATKAAVSATLSHVFFLLMIIVGVLVWLFVLANDSRQFALDESQRQTEL 642
Cdd:COG0642     2 LLLLLLLVLLLLLLLLLLLALLLLLLLLLLLALLLLLALLLLLLLLLLLLLLLALALLALLLLLLLLLLLLLLLLLLLLL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  643 LSREISAHEVTDQALQQAKETAESANQAKSRYLTGISHELRTPLNSVLGYAQLLEKSPSlaPEHSAKVSLIKRSGEHLAD 722
Cdd:COG0642    82 LLLLLLLLLLLLLLLLALLLLLEEANEAKSRFLANVSHELRTPLTAIRGYLELLLEELD--EEQREYLETILRSADRLLR 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  723 IIEGLLDISRIEAGRIELQRDEVAIGELLDDLVDMFSLQAKSKGISFVYNPSPYLPnWVTADETQLRQILINLLSNAVKF 802
Cdd:COG0642   160 LINDLLDLSRLEAGKLELEPEPVDLAELLEEVVELFRPLAEEKGIELELDLPDDLP-TVRGDPDRLRQVLLNLLSNAIKY 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  803 TQQGS-VTLDVYYRNQVAEFTITDSGVGISEQDIERIFKPFERVEKRDipSSPGTGLGLTITQLLTDIMGGNISVSSEIG 881
Cdd:COG0642   239 TPEGGtVTVSVRREGDRVRISVEDTGPGIPPEDLERIFEPFFRTDPSR--RGGGTGLGLAIVKRIVELHGGTIEVESEPG 316
                         330
                  ....*....|..
gi 511672513  882 KGSSFKLSIMLA 893
Cdd:COG0642   317 KGTTFTVTLPLA 328
KdpD COG2205
K+-sensing histidine kinase KdpD [Signal transduction mechanisms];
656-894 6.35e-77

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


Pssm-ID: 441807 [Multi-domain]  Cd Length: 239  Bit Score: 253.29  E-value: 6.35e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  656 ALQQAKETAESANQAKSRYLTGISHELRTPLNSVLGYAQLLEKSPSLAPEHSAK-VSLIKRSGEHLADIIEGLLDISRIE 734
Cdd:COG2205     1 ELEEALEELEELERLKSEFLANVSHELRTPLTSILGAAELLLDEEDLSPEERRElLEIIRESAERLLRLIEDLLDLSRLE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  735 AGRIELQRDEVAIGELLDDLVDMFSLQAKSKGISFVYNPSPYLPnWVTADETQLRQILINLLSNAVKFTQQGS-VTLDVY 813
Cdd:COG2205    81 SGKLSLELEPVDLAELLEEAVEELRPLAEEKGIRLELDLPPELP-LVYADPELLEQVLANLLDNAIKYSPPGGtITISAR 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  814 YRNQVAEFTITDSGVGISEQDIERIFKPFERVEKRDipSSPGTGLGLTITQLLTDIMGGNISVSSEIGKGSSFKLSIMLA 893
Cdd:COG2205   160 REGDGVRISVSDNGPGIPEEELERIFERFYRGDNSR--GEGGTGLGLAIVKRIVEAHGGTIWVESEPGGGTTFTVTLPLA 237

                  .
gi 511672513  894 S 894
Cdd:COG2205   238 E 238
WalK COG5002
Sensor histidine kinase WalK [Signal transduction mechanisms];
538-890 7.17e-70

Sensor histidine kinase WalK [Signal transduction mechanisms];


Pssm-ID: 444026 [Multi-domain]  Cd Length: 390  Bit Score: 239.07  E-value: 7.17e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  538 ARFGQQLSQFVSLVLPKAVSSLMNTRLLNFSGLMALIALLIASLFYLVYSRIPVTEFATKAAVSATLSHVFFLLMIIVGV 617
Cdd:COG5002    32 LLLLLLLLLLLLLLLLLLLLLALLLLLLLLLLLLLALLLLLLLLLLLLALALLLLALLLLLLLLLLLLALLILLLLLALL 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  618 LVWLFVLANDSRQFALDESQRQTELLSREISAHEVTDQALQQAKETAESANQAKSRYLTGISHELRTPLNSVLGYAQLLE 697
Cdd:COG5002   112 ILLAALLLLLSELLLLLLLLGRLSLRLSALLLGLLLLAAVERDITELERLEQMRREFVANVSHELRTPLTSIRGYLELLL 191
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  698 KSPSLAPEHSAK-VSLIKRSGEHLADIIEGLLDISRIEAGRIELQRDEVAIGELLDDLVDMFSLQAKSKGISFVYNPSPY 776
Cdd:COG5002   192 DGAADDPEERREyLEIILEEAERLSRLVNDLLDLSRLESGELKLEKEPVDLAELLEEVVEELRPLAEEKGIELELDLPED 271
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  777 LPnWVTADETQLRQILINLLSNAVKFTQQGS-VTLDVYYRNQVAEFTITDSGVGISEQDIERIFKPFERVEKRDIPSSPG 855
Cdd:COG5002   272 PL-LVLGDPDRLEQVLTNLLDNAIKYTPEGGtITVSLREEDDQVRISVRDTGIGIPEEDLPRIFERFYRVDKSRSRETGG 350
                         330       340       350
                  ....*....|....*....|....*....|....*
gi 511672513  856 TGLGLTITQLLTDIMGGNISVSSEIGKGSSFKLSI 890
Cdd:COG5002   351 TGLGLAIVKHIVEAHGGRIWVESEPGKGTTFTITL 385
PRK15347 PRK15347
two component system sensor kinase;
633-1100 7.74e-66

two component system sensor kinase;


Pssm-ID: 237951 [Multi-domain]  Cd Length: 921  Bit Score: 240.70  E-value: 7.74e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  633 LDESQRQTELLsrEISAHEVTdQALQQAKETAESANQAKSRYLTGISHELRTPLNSVLGYAQLLEKSPsLAPEHSAKVSL 712
Cdd:PRK15347  363 LDTLNEQYDTL--ENKVAERT-QALAEAKQRAEQANKRKSEHLTTISHEIRTPLNGVLGALELLQNTP-LTAEQMDLADT 438
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  713 IKRSGEHLADIIEGLLDISRIEAGRIELQRDEVAIGELLDDLVDMFSLQAKSKGIS---FVynpSPYLPNWVTADETQLR 789
Cdd:PRK15347  439 ARQCTLSLLAIINNLLDFSRIESGQMTLSLEETALLPLLDQAMLTIQGPAQSKSLTlrtFV---GAHVPLYLHLDSLRLR 515
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  790 QILINLLSNAVKFTQQGSVTLDVYYRNQVAEFTITDSGVGISEQDIERIFKPFERVEKrdipSSPGTGLGLTITQLLTDI 869
Cdd:PRK15347  516 QILVNLLGNAVKFTETGGIRLRVKRHEQQLCFTVEDTGCGIDIQQQQQIFTPFYQADT----HSQGTGLGLTIASSLAKM 591
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  870 MGGNISVSSEIGKGSSFKLSIML-------------------------------------ASLNKE------------QQ 900
Cdd:PRK15347  592 MGGELTLFSTPGVGSCFSLVLPLneyappeplkgelsaplalhrqlsawgitcqpghqnpALLDPElaylpgrlydllQQ 671
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  901 PQSVQAPVNSIKGP----SKTVMVVDDDPNHRNLVSEILSPLG---FVVHEANDALVcLSNTYLsaIDLFLLDISMPDMN 973
Cdd:PRK15347  672 IIQGAPNEPVINLPlqpwQLQILLVDDVETNRDIIGMMLVELGqqvTTAASGTEALE-LGRQHR--FDLVLMDIRMPGLD 748
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  974 GWQLLKKLR--SNGIS--VPIIMVSADAteapyfnAAEEIH--EPALHNDYLAKPMRdnalLEKVAKALAIDWNYQ---N 1044
Cdd:PRK15347  749 GLETTQLWRddPNNLDpdCMIVALTANA-------APEEIHrcKKAGMNHYLTKPVT----LAQLARALELAAEYQllrG 817
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 511672513 1045 TSTQSASPEPQAL----NIQLNQSQREQLQEIAEMAQLGfvqgidrlIKNLEK-DSALHTI 1100
Cdd:PRK15347  818 IELSPQDSSCSPLldtdDMALNSKLYQSLLLLLAQIEQA--------VENQEVlSQLLHTL 870
PRK11091 PRK11091
aerobic respiration control sensor protein ArcB; Provisional
659-1072 3.92e-61

aerobic respiration control sensor protein ArcB; Provisional


Pssm-ID: 236842 [Multi-domain]  Cd Length: 779  Bit Score: 224.43  E-value: 3.92e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  659 QAKETAESANQAKSRYLTGISHELRTPLNSVLGYAQLLEKSPsLAPEHSAKVSLIKRSGEHLADIIEGLLDISRIEAGRI 738
Cdd:PRK11091  271 RYQDALEKASRDKTTFISTISHELRTPLNGIVGLSRILLDTE-LTAEQRKYLKTIHVSAITLGNIFNDIIDMDKMERRKL 349
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  739 ELQRDEVAIGELLDDLVDMFSLQAKSKGISFVYNPSPYLPNWVTADETQLRQILINLLSNAVKFTQQGSVTLDVYY-RNQ 817
Cdd:PRK11091  350 QLDNQPIDFTDFLADLENLSGLQAEQKGLRFDLEPLLPLPHKVITDGTRLRQILWNLISNAVKFTQQGGVTVRVRYeEGD 429
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  818 VAEFTITDSGVGISEQDIERIFKPFERVEKR-DIPSSPGTGLGLTITQLLTDIMGGNISVSSEIGKGSSFKLSIMLASLN 896
Cdd:PRK11091  430 MLTFEVEDSGIGIPEDELDKIFAMYYQVKDShGGKPATGTGIGLAVSKRLAQAMGGDITVTSEEGKGSCFTLTIHAPAVA 509
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  897 KEQQPqsvQAPVNSIKGPSKTVMVVDDDPNHRNLVSEILSPLGFVVHEANDALVCLSNTYLSAIDLFLLDISMPDMNGWQ 976
Cdd:PRK11091  510 EEVED---AFDEDDMPLPALNILLVEDIELNVIVARSVLEKLGNSVDVAMTGKEALEMFDPDEYDLVLLDIQLPDMTGLD 586
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  977 LLKKLRSNGIS---VPIIMVSADATEAP--YFNAAeeihepalHNDYLAKPMRDNALLEKVAKAlaidWNYQNTSTQSAS 1051
Cdd:PRK11091  587 IARELRERYPRedlPPLVALTANVLKDKkeYLDAG--------MDDVLSKPLSVPALTAMIKKF----WDTQDDEESTVT 654
                         410       420
                  ....*....|....*....|...
gi 511672513 1052 PE--PQALNIQLNQSQREQLQEI 1072
Cdd:PRK11091  655 TEesSKANEALLDIPMLEQYVEL 677
COG4251 COG4251
Bacteriophytochrome (light-regulated signal transduction histidine kinase) [Signal ...
559-890 6.71e-54

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


Pssm-ID: 443393 [Multi-domain]  Cd Length: 503  Bit Score: 196.93  E-value: 6.71e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  559 LMNTRLLNFSGLMALIALLIASLFYLVYSRIPVTEFATKAAVSATLSHVFFLLMIIVGVLVWLFVLANDSRQFALDESQR 638
Cdd:COG4251   171 LLAALAELELLLLLLLVLLLLLLLLLLLLLLLLRLLLELLLLLEAELLLSLGGGLGLLLLLLLLLVLLLLLILLLLLLIL 250
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  639 QTELLSREISAHEVTDQaLQQAKETAESANQAKSRYLTGISHELRTPLNSVLGYAQLLEK--SPSLAPEHSAKVSLIKRS 716
Cdd:COG4251   251 VLELLELRLELEELEEE-LEERTAELERSNEELEQFAYVASHDLREPLRKISGFSQLLEEdyGDKLDEEGREYLERIRDA 329
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  717 GEHLADIIEGLLDISRIeaGRIELQRDEVAIGELLDDLVDMFSLQAKSKGISFVYNPSPylpnWVTADETQLRQILINLL 796
Cdd:COG4251   330 AERMQALIDDLLAYSRV--GRQELEFEPVDLNELLEEVLEDLEPRIEERGAEIEVGPLP----TVRGDPTLLRQVFQNLI 403
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  797 SNAVKFTQQGS---VTLDVYYRNQVAEFTITDSGVGISEQDIERIFKPFERVEKRDipSSPGTGLGLTITQLLTDIMGGN 873
Cdd:COG4251   404 SNAIKYSRPGEpprIEIGAEREGGEWVFSVRDNGIGIDPEYAEKIFEIFQRLHSRD--EYEGTGIGLAIVKKIVERHGGR 481
                         330
                  ....*....|....*..
gi 511672513  874 ISVSSEIGKGSSFKLSI 890
Cdd:COG4251   482 IWVESEPGEGATFYFTL 498
PRK11466 PRK11466
hybrid sensory histidine kinase TorS; Provisional
638-995 4.27e-51

hybrid sensory histidine kinase TorS; Provisional


Pssm-ID: 236914 [Multi-domain]  Cd Length: 914  Bit Score: 195.51  E-value: 4.27e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  638 RQTELLSREISAHEVTDQAL----QQAKETAESANQAKSRYLTGISHELRTPLNSVLGYAQLLEKSPsLAPEHSAKVSLI 713
Cdd:PRK11466  407 RHREQLAAQVKARTAELQELviehRQARAEAEKASQAKSAFLAAMSHEIRTPLYGILGTAQLLADNP-ALNAQRDDLRAI 485
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  714 KRSGEHLADIIEGLLDISRIEAG--RIELQRDEVAIGELLDDLVDMFSLQAKSKGISFVYNPSPYLPNWVTADETQLRQI 791
Cdd:PRK11466  486 TDSGESLLTILNDILDYSAIEAGgkNVSVSDEPFEPRPLLESTLQLMSGRVKGRPIRLATDIADDLPTALMGDPRRIRQV 565
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  792 LINLLSNAVKFTQQGSVTLDVYYRNQVAEFTITDSGVGISEQDIERIFKPFERVEKRdipsSPGTGLGLTITQLLTDIMG 871
Cdd:PRK11466  566 ITNLLSNALRFTDEGSIVLRSRTDGEQWLVEVEDSGCGIDPAKLAEIFQPFVQVSGK----RGGTGLGLTISSRLAQAMG 641
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  872 GNISVSSEIGKGSSFKLSIMLaslnKEQQPQSVQAPVNSIKGPSKTVMVVDDDPNHRNLVSEILSPLGFVVH---EANDA 948
Cdd:PRK11466  642 GELSATSTPEVGSCFCLRLPL----RVATAPVPKTVNQAVRLDGLRLLLIEDNPLTQRITAEMLNTSGAQVVavgNAAQA 717
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*..
gi 511672513  949 LVCLSNTylSAIDLFLLDISMPDMNGWQLLKKLRSNGISVPIIMVSA 995
Cdd:PRK11466  718 LETLQNS--EPFAAALVDFDLPDYDGITLARQLAQQYPSLVLIGFSA 762
PRK11107 PRK11107
hybrid sensory histidine kinase BarA; Provisional
660-948 5.92e-48

hybrid sensory histidine kinase BarA; Provisional


Pssm-ID: 236848 [Multi-domain]  Cd Length: 919  Bit Score: 185.82  E-value: 5.92e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  660 AKETAESANQAKSRYLTGISHELRTPLNSVLGYAQLLEKSPsLAPEHSAKVSLIKRSGEHLADIIEGLLDISRIEAGRIE 739
Cdd:PRK11107  282 AKKRAQEAARIKSEFLANMSHELRTPLNGVIGFTRQTLKTP-LTPTQRDYLQTIERSANNLLAIINDILDFSKLEAGKLV 360
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  740 LQRDEVAIGELLDDLVDMFSLQAKSKGISFVYNPSPYLPNWVTADETQLRQILINLLSNAVKFTQQGSVTLDVYYR---- 815
Cdd:PRK11107  361 LENIPFSLRETLDEVVTLLAHSAHEKGLELTLNIDPDVPDNVIGDPLRLQQIITNLVGNAIKFTESGNIDILVELRalsn 440
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  816 NQVA-EFTITDSGVGISEQDIERIFKPFervekRDIPSS-----PGTGLGLTITQLLTDIMGGNISVSSEIGKGSSFKLS 889
Cdd:PRK11107  441 TKVQlEVQIRDTGIGISERQQSQLFQAF-----RQADASisrrhGGTGLGLVITQKLVNEMGGDISFHSQPNRGSTFWFH 515
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 511672513  890 ImlaSLNKEQQPQSVQAPVNSIKGpsKTVMVVDDDPNHRNLVSEILS--PLgFVVHEANDA 948
Cdd:PRK11107  516 L---PLDLNPNPIIDGLPTDCLAG--KRLLYVEPNSAAAQATLDILSetPL-EVTYSPTLS 570
PRK09959 PRK09959
acid-sensing system histidine kinase EvgS;
655-997 6.16e-47

acid-sensing system histidine kinase EvgS;


Pssm-ID: 182169 [Multi-domain]  Cd Length: 1197  Bit Score: 183.78  E-value: 6.16e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  655 QALQQAKETAESANQAKSRYLTGISHELRTPLNSVLGYAQLLEKSPSLAPEHSAKVSLIKRSGEHLADIIEGLLDISRIE 734
Cdd:PRK09959  696 HALEVERNKAINATVAKSQFLATMSHEIRTPISSIMGFLELLSGSGLSKEQRVEAISLAYATGQSLLGLIGEILDVDKIE 775
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  735 AGRIELQRDEVAIGELLDDLVDMFSLQAKSKGISFVYN---PSPYLpnwVTADETQLRQILINLLSNAVKFTQQGSVTLD 811
Cdd:PRK09959  776 SGNYQLQPQWVDIPTLVQNTCHSFGAIAASKSIALSCSstfPDHYL---VKIDPQAFKQVLSNLLSNALKFTTEGAVKIT 852
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  812 VYY-----RNQVAEFTITDSGVGISEQDIERIFKPFERVEKRDipSSPGTGLGLTITQLLTDIMGGNISVSSEIGKGSSF 886
Cdd:PRK09959  853 TSLghiddNHAVIKMTIMDSGSGLSQEEQQQLFKRYSQTSAGR--QQTGSGLGLMICKELIKNMQGDLSLESHPGIGTTF 930
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  887 KLSIMLASLnkeQQPQSVQAPVNS-IKGPSK-TVMVVDDDPNHRNLVSEILSPLGFVVHEANDALVCLSNTYLSAIDLFL 964
Cdd:PRK09959  931 TITIPVEIS---QQVATVEAKAEQpITLPEKlSILIADDHPTNRLLLKRQLNLLGYDVDEATDGVQALHKVSMQHYDLLI 1007
                         330       340       350
                  ....*....|....*....|....*....|...
gi 511672513  965 LDISMPDMNGWQLLKKLRSNGISVPIIMVSADA 997
Cdd:PRK09959 1008 TDVNMPNMDGFELTRKLREQNSSLPIWGLTANA 1040
COG4191 COG4191
Signal transduction histidine kinase regulating C4-dicarboxylate transport system [Signal ...
538-890 7.69e-47

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


Pssm-ID: 443345 [Multi-domain]  Cd Length: 361  Bit Score: 172.29  E-value: 7.69e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  538 ARFGQQLSQFVSLVLPKAVSSLMNTRLLNFSGLMALIALLIASLFYLVYSRIPVTEFATKAAVSATLSHVFFLLMIIVGV 617
Cdd:COG4191    14 LLRALALALALLLLLLLLLLALLLLLLALLLALLALLLLLLLLLLLLLLELLLLLLALLGGLLRLLLLLGLLLLLLLEAL 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  618 LVWLFVLANDSRQFALDESQRQTELLSREISAHEVTDQALQQAkETAESANQaksryLT-GISHELRTPLNSVLGYAQLL 696
Cdd:COG4191    94 LLLLLAALDAEENAELEELERDITELERAEEELRELQEQLVQS-EKLAALGE-----LAaGIAHEINNPLAAILGNAELL 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  697 EK---SPSLAPEHSAKVSLIKRSGEHLADIIEGLLDISRIEagriELQRDEVAIGELLDDLVDMFSLQAKSKGISFVYNP 773
Cdd:COG4191   168 RRrleDEPDPEELREALERILEGAERAAEIVRSLRAFSRRD----EEEREPVDLNELIDEALELLRPRLKARGIEVELDL 243
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  774 SPYLPnWVTADETQLRQILINLLSN---AVKFTQQGSVTLDVYYRNQVAEFTITDSGVGISEQDIERIFKPF---ERVEK 847
Cdd:COG4191   244 PPDLP-PVLGDPGQLEQVLLNLLINaidAMEEGEGGRITISTRREGDYVVISVRDNGPGIPPEVLERIFEPFfttKPVGK 322
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|...
gi 511672513  848 rdipsspGTGLGLTITQLLTDIMGGNISVSSEIGKGSSFKLSI 890
Cdd:COG4191   323 -------GTGLGLSISYGIVEKHGGRIEVESEPGGGTTFTITL 358
phoR_proteo TIGR02966
phosphate regulon sensor kinase PhoR; Members of this protein family are the regulatory ...
678-887 2.08e-43

phosphate regulon sensor kinase PhoR; Members of this protein family are the regulatory histidine kinase PhoR associated with the phosphate ABC transporter in most Proteobacteria. Related proteins from Gram-positive organisms are not included in this model. The phoR gene usually is adjacent to the response regulator phoB gene (TIGR02154). [Signal transduction, Two-component systems]


Pssm-ID: 274368 [Multi-domain]  Cd Length: 333  Bit Score: 161.22  E-value: 2.08e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513   678 ISHELRTPLNSVLGYAQLLEKSPSLAPEHSAK-VSLIKRSGEHLADIIEGLLDISRIEAGRIELQRDEVAIGELLDDLVD 756
Cdd:TIGR02966  121 VSHELRTPLTVLRGYLETLADGPDEDPEEWNRaLEIMLEQSQRMQSLVEDLLTLSRLESAASPLEDEPVDMPALLDHLRD 200
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513   757 mfSLQAKSKG----ISFVYNPSPylpnWVTADETQLRQILINLLSNAVKFTQ-QGSVTLDVYYRNQVAEFTITDSGVGIS 831
Cdd:TIGR02966  201 --EAEALSQGknhqITFEIDGGV----DVLGDEDELRSAFSNLVSNAIKYTPeGGTITVRWRRDGGGAEFSVTDTGIGIA 274
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 511672513   832 EQDIERIFKPFERVEKRDIPSSPGTGLGLTITQLLTDIMGGNISVSSEIGKGSSFK 887
Cdd:TIGR02966  275 PEHLPRLTERFYRVDKSRSRDTGGTGLGLAIVKHVLSRHHARLEIESELGKGSTFS 330
PRK10841 PRK10841
two-component system sensor histidine kinase RcsC;
646-997 3.11e-42

two-component system sensor histidine kinase RcsC;


Pssm-ID: 182772 [Multi-domain]  Cd Length: 924  Bit Score: 167.84  E-value: 3.11e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  646 EISAHEVTDQALQQAKETAESANQAKSRYLTGISHELRTPLNSVLGYAQLLeKSPSLAPEHSAKVSLIKRSGEHLADIIE 725
Cdd:PRK10841  422 DVSARVKMEESLQEMAQAAEQASQSKSMFLATVSHELRTPLYGIIGNLDLL-QTKELPKGVDRLVTAMNNSSSLLLKIIS 500
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  726 GLLDISRIEAGRIELQRDEVAIGELLDDLV-DMFSLQAKsKGISFVYNPSPYLPNWVTADETQLRQILINLLSNAVKFTQ 804
Cdd:PRK10841  501 DILDFSKIESEQLKIEPREFSPREVINHITaNYLPLVVK-KRLGLYCFIEPDVPVALNGDPMRLQQVISNLLSNAIKFTD 579
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  805 QGSVTLDVYYRNQVAEFTITDSGVGISEQDIERIFKPFERVEKRDIPSSPGTGLGLTITQLLTDIMGGNISVSSEIGKGS 884
Cdd:PRK10841  580 TGCIVLHVRVDGDYLSFRVRDTGVGIPAKEVVRLFDPFFQVGTGVQRNFQGTGLGLAICEKLINMMDGDISVDSEPGMGS 659
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  885 SFKLSIML-------------------------ASLNK--------------------------------EQQPQSVQA- 906
Cdd:PRK10841  660 QFTIRIPLygaqypqkkgveglqgkrcwlavrnASLEQfletllqrsgiqvqryegqeptpedvlitddpVQKKWQGRAv 739
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  907 -------------------------------------------PVNSIKGPSK----------TVMVVDDDPNHRNLVSE 933
Cdd:PRK10841  740 itfcrrhigipleiapgewvhstatphelpallariyrielesDDSANALPSTdkavsdnddmMILVVDDHPINRRLLAD 819
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 511672513  934 ILSPLGFVVHEAND---ALVCLSNtylSAIDLFLLDISMPDMNGWQLLKKLRSNGISVPIIMVSADA 997
Cdd:PRK10841  820 QLGSLGYQCKTANDgvdALNVLSK---NHIDIVLTDVNMPNMDGYRLTQRLRQLGLTLPVIGVTANA 883
NtrB COG3852
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms];
642-890 3.99e-40

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


Pssm-ID: 443061 [Multi-domain]  Cd Length: 361  Bit Score: 152.69  E-value: 3.99e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  642 LLSREISAHEVTDQALQQAkETAESANQaksryLT-GISHELRTPLNSVLGYAQLLEKSPSlAPEHSAKVSLIKRSGEHL 720
Cdd:COG3852   111 LVLRDITERKRLERELRRA-EKLAAVGE-----LAaGLAHEIRNPLTGIRGAAQLLERELP-DDELREYTQLIIEEADRL 183
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  721 ADIIEGLLDISRieagRIELQRDEVAIGELLDDLVDMFSLQAKsKGISFVYNPSPYLPNwVTADETQLRQILINLLSNAV 800
Cdd:COG3852   184 NNLVDRLLSFSR----PRPPEREPVNLHEVLERVLELLRAEAP-KNIRIVRDYDPSLPE-VLGDPDQLIQVLLNLVRNAA 257
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  801 K-FTQQGSVTLDVYYRNQV----------AEFTITDSGVGISEQDIERIFKPF----ERvekrdipsspGTGLGLTITQL 865
Cdd:COG3852   258 EaMPEGGTITIRTRVERQVtlgglrprlyVRIEVIDNGPGIPEEILDRIFEPFfttkEK----------GTGLGLAIVQK 327
                         250       260
                  ....*....|....*....|....*
gi 511672513  866 LTDIMGGNISVSSEIGKGSSFKLSI 890
Cdd:COG3852   328 IVEQHGGTIEVESEPGKGTTFRIYL 352
KinE COG5809
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome ...
657-900 1.67e-38

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


Pssm-ID: 444511 [Multi-domain]  Cd Length: 489  Bit Score: 150.90  E-value: 1.67e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  657 LQQAKETAESANQAkSRYLTGISHELRTPLNSVLGYAQLLEksPSLAPEHSAKVSLIKRSGEHLADIIEGLLDISRIEAG 736
Cdd:COG5809   257 LEELLRKSEKLSVV-GELAAGIAHEIRNPLTSLKGFIQLLK--DTIDEEQKTYLDIMLSELDRIESIISEFLVLAKPQAI 333
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  737 RIElqrdEVAIGELLDDLVDMFSLQAKSKGISFVYNPSPYLPNwVTADETQLRQILINLLSNAVKFT-QQGSVTLDV-YY 814
Cdd:COG5809   334 KYE----PKDLNTLIEEVIPLLQPQALLKNVQIELELEDDIPD-ILGDENQLKQVFINLLKNAIEAMpEGGNITIETkAE 408
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  815 RNQVAEFTITDSGVGISEQDIERIFKPF-ERVEKrdipsspGTGLGLTITQLLTDIMGGNISVSSEIGKGSSFKLSIMLA 893
Cdd:COG5809   409 DDDKVVISVTDEGCGIPEERLKKLGEPFyTTKEK-------GTGLGLMVSYKIIEEHGGKITVESEVGKGTTFSITLPIK 481

                  ....*..
gi 511672513  894 SLNKEQQ 900
Cdd:COG5809   482 LSEQVSM 488
NtrY COG5000
Signal transduction histidine kinase NtrY involved in nitrogen fixation and metabolism ...
677-893 5.19e-38

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: 148.19  E-value: 5.19e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  677 GISHELRTPLNSVLGYAQLLE-----KSPSLAPEHSAKVSLIKRSGEHLADIIEGLLDISRIEagriELQRDEVAIGELL 751
Cdd:COG5000   207 RIAHEIKNPLTPIQLSAERLRrkladKLEEDREDLERALDTIIRQVDRLKRIVDEFLDFARLP----EPQLEPVDLNELL 282
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  752 DDLVDMFSLQAKSKGISFVYNPSPYLPnWVTADETQLRQILINLLSNAVKFT-QQGSVTLDVYYRNQVAEFTITDSGVGI 830
Cdd:COG5000   283 REVLALYEPALKEKDIRLELDLDPDLP-EVLADRDQLEQVLINLLKNAIEAIeEGGEIEVSTRREDGRVRIEVSDNGPGI 361
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 511672513  831 SEQDIERIFKPF----ERvekrdipsspGTGLGLTITQLLTDIMGGNISVSSEIGKGSSFKLSIMLA 893
Cdd:COG5000   362 PEEVLERIFEPFfttkPK----------GTGLGLAIVKKIVEEHGGTIELESRPGGGTTFTIRLPLA 418
HATPase_EvgS-ArcB-TorS-like cd16922
Histidine kinase-like ATPase domain of two-component sensor histidine kinases, many are hybrid ...
788-890 7.32e-38

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: 137.24  E-value: 7.32e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  788 LRQILINLLSNAVKFTQQGSVTLDVYYRNQ-----VAEFTITDSGVGISEQDIERIFKPFERVEKRDIPSSPGTGLGLTI 862
Cdd:cd16922     1 LRQILLNLLGNAIKFTEEGEVTLRVSLEEEeedgvQLRFSVEDTGIGIPEEQQARLFEPFSQADSSTTRKYGGTGLGLAI 80
                          90       100
                  ....*....|....*....|....*...
gi 511672513  863 TQLLTDIMGGNISVSSEIGKGSSFKLSI 890
Cdd:cd16922    81 SKKLVELMGGDISVESEPGQGSTFTFTL 108
HATPase_c smart00387
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.
783-893 9.21e-33

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


Pssm-ID: 214643 [Multi-domain]  Cd Length: 111  Bit Score: 122.76  E-value: 9.21e-33
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513    783 ADETQLRQILINLLSNAVKFT-QQGSVTLDVYYRNQVAEFTITDSGVGISEQDIERIFKPFERVEKRDiPSSPGTGLGLT 861
Cdd:smart00387    1 GDPDRLRQVLSNLLDNAIKYTpEGGRITVTLERDGDHVEITVEDNGPGIPPEDLEKIFEPFFRTDKRS-RKIGGTGLGLS 79
                            90       100       110
                    ....*....|....*....|....*....|..
gi 511672513    862 ITQLLTDIMGGNISVSSEIGKGSSFKLSIMLA 893
Cdd:smart00387   80 IVKKLVELHGGEISVESEPGGGTTFTITLPLE 111
PRK09303 PRK09303
histidine kinase;
633-886 2.75e-29

histidine kinase;


Pssm-ID: 236462 [Multi-domain]  Cd Length: 380  Bit Score: 121.21  E-value: 2.75e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  633 LDESQRQTELLSREISAHEV--TDQ--ALQQAKETAESANQAKSRYLTGISHELRTPLnSVLGYA----QLLEKSPSLAP 704
Cdd:PRK09303  109 LGENLQPSEIDSGRYSQELLqlSDElfVLRQENETLLEQLKFKDRVLAMLAHDLRTPL-TAASLAletlELGQIDEDTEL 187
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  705 EHSAKVSL---IKRSGEHLADIIEGLLDISRIEAGRIELQRDEVAIGELLDDLVDMFSLQAKSKGISFVYNPSPYLPNwV 781
Cdd:PRK09303  188 KPALIEQLqdqARRQLEEIERLITDLLEVGRTRWEALRFNPQKLDLGSLCQEVILELEKRWLAKSLEIQTDIPSDLPS-V 266
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  782 TADETQLRQILINLLSNAVKFTQ-QGSVTLDVYYR-NQVAEFTITDSGVGISEQDIERIFKpfERVE-KRDiPSSPGTGL 858
Cdd:PRK09303  267 YADQERIRQVLLNLLDNAIKYTPeGGTITLSMLHRtTQKVQVSICDTGPGIPEEEQERIFE--DRVRlPRD-EGTEGYGI 343
                         250       260
                  ....*....|....*....|....*...
gi 511672513  859 GLTITQLLTDIMGGNISVSSEIGKGSSF 886
Cdd:PRK09303  344 GLSVCRRIVRVHYGQIWVDSEPGQGSCF 371
PRK11360 PRK11360
two-component system sensor histidine kinase AtoS;
642-888 1.32e-28

two-component system sensor histidine kinase AtoS;


Pssm-ID: 236901 [Multi-domain]  Cd Length: 607  Bit Score: 122.77  E-value: 1.32e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  642 LLSREISAHEVTDQALQQAKETAesanqAKSRYLTGISHELRTPLNSVLGYAQLLEKSPSLaPEHSAKVSLIKRSGEHLA 721
Cdd:PRK11360  366 VIFSDLTERKRLQRRVARQERLA-----ALGELVAGVAHEIRNPLTAIRGYVQIWRQQTSD-PPSQEYLSVVLREVDRLN 439
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  722 DIIEGLLDISRIEagriELQRDEVAIGELLDDLVDMFSLQAKSKGISFVYNPSPYLPNwVTADETQLRQILINLLSNAVK 801
Cdd:PRK11360  440 KVIDQLLEFSRPR----ESQWQPVSLNALVEEVLQLFQTAGVQARVDFETELDNELPP-IWADPELLKQVLLNILINAVQ 514
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  802 -FTQQGSVTLDV-YYRNQVAEFTITDSGVGISEQDIERIFKPFERVEKRdipsspGTGLGLTITQLLTDIMGGNISVSSE 879
Cdd:PRK11360  515 aISARGKIRIRTwQYSDGQVAVSIEDNGCGIDPELLKKIFDPFFTTKAK------GTGLGLALSQRIINAHGGDIEVESE 588

                  ....*....
gi 511672513  880 IGKGSSFKL 888
Cdd:PRK11360  589 PGVGTTFTL 597
HATPase_c pfam02518
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the ...
783-890 1.06e-27

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: 108.22  E-value: 1.06e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513   783 ADETQLRQILINLLSNAVKFT-QQGSVTLDVYYRNQVaEFTITDSGVGISEQDIERIFKPFERVEKRdipSSPGTGLGLT 861
Cdd:pfam02518    1 GDELRLRQVLSNLLDNALKHAaKAGEITVTLSEGGEL-TLTVEDNGIGIPPEDLPRIFEPFSTADKR---GGGGTGLGLS 76
                           90       100
                   ....*....|....*....|....*....
gi 511672513   862 ITQLLTDIMGGNISVSSEIGKGSSFKLSI 890
Cdd:pfam02518   77 IVRKLVELLGGTITVESEPGGGTTVTLTL 105
CheY COG0784
CheY-like REC (receiver) domain, includes chemotaxis protein CheY and sporulation regulator ...
913-1037 1.44e-27

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: 108.40  E-value: 1.44e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  913 GPSKTVMVVDDDPNHRNLVSEILSPLGFVVHEAND---ALVCLSNTylsAIDLFLLDISMPDMNGWQLLKKLRSN--GIS 987
Cdd:COG0784     3 LGGKRILVVDDNPDNRELLRRLLERLGYEVTTAEDgaeALELLRAG---PPDLILLDINMPGMDGLELLRRIRALprLPD 79
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 511672513  988 VPIIMVSAdateapyfNAAEEIHEPALH---NDYLAKPMRDNALLEKVAKALA 1037
Cdd:COG0784    80 IPIIALTA--------YADEEDRERALEagaDDYLTKPVDPEELLEALRRLLA 124
PRK13837 PRK13837
two-component system VirA-like sensor kinase;
618-1056 2.08e-27

two-component system VirA-like sensor kinase;


Pssm-ID: 237526 [Multi-domain]  Cd Length: 828  Bit Score: 120.17  E-value: 2.08e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  618 LVWLFVLANDSRQFALDESQRQTELLSREISAHEVTDQALQQAKETAESANQAKSRYLT------GISHELRTPLNSVLG 691
Cdd:PRK13837  391 IVALLGLGRQRYGLRPPAGELQLLELALDCLAHAIERRRLETERDALERRLEHARRLEAvgtlasGIAHNFNNILGAILG 470
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  692 YAQLLEKSPSLAPEHSAKVSLIKRSGEHLADIIEGLLDISRIEAGRIElqrdEVAIGELLDDLVdmfSLQAKSKG----I 767
Cdd:PRK13837  471 YAEMALNKLARHSRAARYIDEIISAGARARLIIDQILAFGRKGERNTK----PFDLSELVTEIA---PLLRVSLPpgveL 543
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  768 SFVYNPSPYLpnwVTADETQLRQILINLLSNAVK-FTQQGSVTLDVYYRNQVAEFTIT---------------DSGVGIS 831
Cdd:PRK13837  544 DFDQDQEPAV---VEGNPAELQQVLMNLCSNAAQaMDGAGRVDISLSRAKLRAPKVLShgvlppgryvllrvsDTGAGID 620
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  832 EQDIERIFKPF--ERvekrdipsSPGTGLGLTITQLLTDIMGGNISVSSEIGKGSSFKLSIMLASlNKEQQPQSVQAPVN 909
Cdd:PRK13837  621 EAVLPHIFEPFftTR--------AGGTGLGLATVHGIVSAHAGYIDVQSTVGRGTRFDVYLPPSS-KVPVAPQAFFGPGP 691
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  910 SIKGPSKTVMVVDDDPNHRNLVSEILS-----PLGFVvhEANDALVCLSNTYlSAIDLFLLDISMPDMNgwQLLKKLRSN 984
Cdd:PRK13837  692 LPRGRGETVLLVEPDDATLERYEEKLAalgyePVGFS--TLAAAIAWISKGP-ERFDLVLVDDRLLDEE--QAAAALHAA 766
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 511672513  985 GISVPIIMVSADATEApyfnAAEEIHepALHNDYLAKPMRDNALLEKVAKALAidwnyqntsTQSASPEPQA 1056
Cdd:PRK13837  767 APTLPIILGGNSKTMA----LSPDLL--ASVAEILAKPISSRTLAYALRTALA---------TARAAAARAE 823
cztS_silS_copS TIGR01386
heavy metal sensor kinase; Members of this family contain a sensor histidine kinase domain ...
633-889 6.81e-27

heavy metal sensor kinase; Members of this family contain a sensor histidine kinase domain (pfam00512) and a domain found in bacterial signal proteins (pfam00672). This group is separated phylogenetically from related proteins with similar architecture and contains a number of proteins associated with heavy metal resistance efflux systems for copper, silver, cadmium, and/or zinc.


Pssm-ID: 273593 [Multi-domain]  Cd Length: 457  Bit Score: 115.56  E-value: 6.81e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513   633 LDESQRQTELlsREISahevtdQALQQAKETAESANQAKSRYLTGISHELRTPLNSVLGYAQLLEKSPSLAPEHSAKVSL 712
Cdd:TIGR01386  211 LDPSRAPAEL--RELA------QSFNAMLGRLEDAFQRLSQFSADLAHELRTPLTNLLGQTQVALSQPRTGEEYREVLES 282
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513   713 IKRSGEHLADIIEGLLDISRIEAGRIELQRDEVAIGELLDDLVDMFSLQAKSKGISFVYNPSPYLPnwvtADETQLRQIL 792
Cdd:TIGR01386  283 NLEELERLSRMVSDMLFLARADNGQLALERVRLDLAAELAKVAEYFEPLAEERGVRIRVEGEGLVR----GDPQMFRRAI 358
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513   793 INLLSNAVKFTQQGSvTLDVYYRNQVAEFT--ITDSGVGISEQDIERIFKPFERVEKRDIPSSPGTGLGLTITQLLTDIM 870
Cdd:TIGR01386  359 SNLLSNALRHTPDGG-TITVRIERRSDEVRvsVSNPGPGIPPEHLSRLFDRFYRVDPARSNSGEGTGLGLAIVRSIMEAH 437
                          250
                   ....*....|....*....
gi 511672513   871 GGNISVSSEIGKgSSFKLS 889
Cdd:TIGR01386  438 GGRASAESPDGK-TRFILR 455
MtrAB_MtrB NF040691
MtrAB system histidine kinase MtrB;
583-890 2.42e-25

MtrAB system histidine kinase MtrB;


Pssm-ID: 468655 [Multi-domain]  Cd Length: 507  Bit Score: 111.66  E-value: 2.42e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  583 YLVYSRIPVTEfaTKAAVSATLSHVFFLLMIIVGVLVWL---FVL------ANDSRQFAL-DESQRQTELLSREIS--AH 650
Cdd:NF040691  171 YLLFPLEDEQS--TLALVRGTLLLGGLALVVLLGLIAWLvtrQVVapvrsaARTAERFAAgDLSERMPVKGEDDLArlAR 248
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  651 EVTDQA--LQQAKETAESANQAKSRYLTGISHELRTPLNSVLGYAQLL-EKSPSLAPEHSAKVSL----IKRSGEHLADi 723
Cdd:NF040691  249 SFNQMAdsLQRQIRQLEELSRLQQRFVSDVSHELRTPLTTIRMAADVIhDSRDDFDPATARSAELlhteLDRFESLLSD- 327
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  724 iegLLDISRIEAGRIELQRDEVAIGELLDDLVDMFSLQAKSKGISFVYNpSPYLPNWVTADETQLRQILINLLSNAVKFT 803
Cdd:NF040691  328 ---LLEISRFDAGAAELDVEPVDLRPLVRRVVDALRQLAERAGVELRVD-APGTPVVAEVDPRRVERVLRNLVVNAIEHG 403
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  804 QQGSVTLDVYY-RNQVAeFTITDSGVGISEQDIERIFKPFERVEKRDIPSSPGTGLGLTITQLLTDIMGGNISVSSEIGK 882
Cdd:NF040691  404 EGKPVVVTVAQdDTAVA-VTVRDHGVGLKPGEVALVFDRFWRADPARARTTGGTGLGLAIALEDARLHGGWLEAWGRPGQ 482

                  ....*...
gi 511672513  883 GSSFKLSI 890
Cdd:NF040691  483 GSQFRLTL 490
REC cd00156
phosphoacceptor receiver (REC) domain of response regulators (RRs) and pseudo response ...
919-1022 5.06e-25

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: 100.38  E-value: 5.06e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  919 MVVDDDPNHRNLVSEILSPLGFVVHEANDALVCLSNTYLSAIDLFLLDISMPDMNGWQLLKKLRSNGISVPIIMVSADAT 998
Cdd:cd00156     1 LIVDDDPAIRELLKSLLEREGYEVDTAADGEEALELLREERPDLVLLDLMMPGMDGLELLRKLRELPPDIPVIVLTAKAD 80
                          90       100
                  ....*....|....*....|....
gi 511672513  999 EApyfNAAEEIHEPAlhNDYLAKP 1022
Cdd:cd00156    81 EE---DAVRALELGA--DDYLVKP 99
PRK11100 PRK11100
sensory histidine kinase CreC; Provisional
607-876 1.71e-24

sensory histidine kinase CreC; Provisional


Pssm-ID: 236846 [Multi-domain]  Cd Length: 475  Bit Score: 108.39  E-value: 1.71e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  607 VFFLLMIIVGVLV--WLFVLANDSRQFALDESQrQTELLSREISAHEVTD--QALQQAKETAESANQAKsRYLTGISHEL 682
Cdd:PRK11100  190 LLLGIALLIGAGVvwWLNRSIRRLTRYADAVTE-GKPVPLPKLGSSELRElaQALESMRVKLEGKAYVE-QYVQTLTHEL 267
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  683 RTPLNSVLGYAQLLEKSPSlaPEHSAK-VSLIKRSGEHLADIIEGLLDISRIEAGRIELQRDEVAIGELLDDLVDMFSLQ 761
Cdd:PRK11100  268 KSPLAAIRGAAELLQEDPP--PEDRARfTGNILTQSARLQQLIDRLLELARLEQRQELEVLEPVALAALLEELVEAREAQ 345
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  762 AKSKGISFVYNPSpylPNWVTADETQLRQILINLLSNAVKFTQQGS-VTLDVYYRNQVAEFTITDSGVGISEQDIERIFK 840
Cdd:PRK11100  346 AAAKGITLRLRPD---DARVLGDPFLLRQALGNLLDNAIDFSPEGGtITLSAEVDGEQVALSVEDQGPGIPDYALPRIFE 422
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 511672513  841 PFErvekrdipSSP-------GTGLGLTITQLLTDIMGGNISV 876
Cdd:PRK11100  423 RFY--------SLPrpangrkSTGLGLAFVREVARLHGGEVTL 457
AtoC COG2204
DNA-binding transcriptional response regulator, NtrC family, contains REC, AAA-type ATPase, ...
914-1037 1.99e-24

DNA-binding transcriptional response regulator, NtrC family, contains REC, AAA-type ATPase, and a Fis-type DNA-binding domains [Signal transduction mechanisms];


Pssm-ID: 441806 [Multi-domain]  Cd Length: 418  Bit Score: 107.36  E-value: 1.99e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  914 PSKTVMVVDDDPNHRNLVSEILSPLGFVVHEAND---ALVCLSNtylSAIDLFLLDISMPDMNGWQLLKKLRSNGISVPI 990
Cdd:COG2204     1 SMARILVVDDDPDIRRLLKELLERAGYEVETAASgeeALALLRE---EPPDLVLLDLRMPGMDGLELLRELRALDPDLPV 77
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 511672513  991 IMVSADATEApyfNAAEEIHEPALhnDYLAKPMRDNALLEKVAKALA 1037
Cdd:COG2204    78 ILLTGYGDVE---TAVEAIKAGAF--DYLTKPFDLEELLAAVERALE 119
OmpR COG0745
DNA-binding response regulator, OmpR family, contains REC and winged-helix (wHTH) domain ...
915-1036 2.20e-24

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: 101.96  E-value: 2.20e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  915 SKTVMVVDDDPNHRNLVSEILSPLGFVVHEANDALVCLSNTYLSAIDLFLLDISMPDMNGWQLLKKLRSNGISVPIIMVS 994
Cdd:COG0745     1 MPRILVVEDDPDIRELLADALEREGYEVDTAADGEEALELLEEERPDLILLDLMLPGMDGLEVCRRLRARPSDIPIIMLT 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 511672513  995 ADATEAPYFNAAEeihepALHNDYLAKPMRDNALLEKVAKAL 1036
Cdd:COG0745    81 ARDDEEDRVRGLE-----AGADDYLTKPFDPEELLARIRALL 117
PRK10364 PRK10364
two-component system sensor histidine kinase ZraS;
677-900 2.23e-23

two-component system sensor histidine kinase ZraS;


Pssm-ID: 236674 [Multi-domain]  Cd Length: 457  Bit Score: 104.87  E-value: 2.23e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  677 GISHELRTPLNSVLGYAQLL-EKSPSLAPEHSAKVSLIKRSgEHLADIIEGLLDISRieAGRIELQrdEVAIGELLDDLV 755
Cdd:PRK10364  243 GVAHEIRNPLSSIKGLAKYFaERAPAGGEAHQLAQVMAKEA-DRLNRVVSELLELVK--PTHLALQ--AVDLNDLINHSL 317
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  756 DMFSLQAKSKGISFVYNPSPYLPNwVTADETQLRQILINLLSNAVK-FTQQGSVTLDVYYRNQVAEFTITDSGVGISEQD 834
Cdd:PRK10364  318 QLVSQDANSREIQLRFTANDTLPE-IQADPDRLTQVLLNLYLNAIQaIGQHGVISVTASESGAGVKISVTDSGKGIAADQ 396
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 511672513  835 IERIFKPFERVEkrdipsSPGTGLGLTITQLLTDIMGGNISVSSEIGKGSSFKLSIMLASLNKEQQ 900
Cdd:PRK10364  397 LEAIFTPYFTTK------AEGTGLGLAVVHNIVEQHGGTIQVASQEGKGATFTLWLPVNITRRDPQ 456
PRK10490 PRK10490
sensor protein KdpD; Provisional
616-892 2.93e-22

sensor protein KdpD; Provisional


Pssm-ID: 236701 [Multi-domain]  Cd Length: 895  Bit Score: 103.58  E-value: 2.93e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  616 GVLVwlfVLANDSRQFALDESQRQTELLSREI-SAHE---VTDQAlQQAKETAESaNQAKSRYLTGISHELRTPLNSVLG 691
Cdd:PRK10490  610 GLLA---VEPGNLRQLMIPEQQRLLETFTLLIaNALErltLTASE-EQARLASER-EQLRNALLAALSHDLRTPLTVLFG 684
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  692 YAQLL------EKSPslapeHSAKVSLIKRSGEHLADIIEGLLDISRIEAGRIELQRDEVAIGELLDDLVDMFSLQAKSK 765
Cdd:PRK10490  685 QAEILtldlasEGSP-----HARQASEIRQQVLNTTRLVNNLLDMARIQSGGFNLRKEWLTLEEVVGSALQMLEPGLSGH 759
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  766 GISfVYNPSPYLpnWVTADETQLRQILINLLSNAVKFT-QQGSVTLDVYYRNQVAEFTITDSGVGISEQDIERIFKPFER 844
Cdd:PRK10490  760 PIN-LSLPEPLT--LIHVDGPLFERVLINLLENAVKYAgAQAEIGIDAHVEGERLQLDVWDNGPGIPPGQEQLIFDKFAR 836
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 511672513  845 VEKRDipSSPGTGLGLTITQLLTDIMGGNISVSSEIGKGSSFKLSIML 892
Cdd:PRK10490  837 GNKES--AIPGVGLGLAICRAIVEVHGGTIWAENRPEGGACFRVTLPL 882
RpfG COG3437
Response regulator c-di-GMP phosphodiesterase, RpfG family, contains REC and HD-GYP domains ...
912-1038 3.72e-22

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: 96.39  E-value: 3.72e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  912 KGPSKTVMVVDDDPNHRNLVSEILSPLGFVVHEANDALVCLSNTYLSAIDLFLLDISMPDMNGWQLLKKLRSN--GISVP 989
Cdd:COG3437     3 TGQAPTVLIVDDDPENLELLRQLLRTLGYDVVTAESGEEALELLLEAPPDLILLDVRMPGMDGFELLRLLRADpsTRDIP 82
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 511672513  990 IIMVSADATEAPYFNAAEeihepALHNDYLAKPMRDNALLEKVAKALAI 1038
Cdd:COG3437    83 VIFLTALADPEDRERALE-----AGADDYLTKPFDPEELLARVRNALEL 126
phoR PRK11006
phosphate regulon sensor histidine kinase PhoR;
678-886 7.70e-22

phosphate regulon sensor histidine kinase PhoR;


Pssm-ID: 182895 [Multi-domain]  Cd Length: 430  Bit Score: 99.70  E-value: 7.70e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  678 ISHELRTPLNSVLGYAQLLEKSPSLAPEHSAKVSLIKRSGEHLADIIEGLLDISRIEAG-RIELQrDEVAIGELLDDLV- 755
Cdd:PRK11006  211 VSHELRTPLTVLQGYLEMMQDQPLEGALREKALHTMREQTQRMEGLVKQLLTLSKIEAApTIDLN-EKVDVPMMLRVLEr 289
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  756 DMFSLQAKSKGISFVYNPSPYlpnwVTADETQLRQILINLLSNAVKFTQQGSvTLDV-YYRN-QVAEFTITDSGVGISEQ 833
Cdd:PRK11006  290 EAQTLSQGKHTITFEVDNSLK----VFGNEDQLRSAISNLVYNAVNHTPEGT-HITVrWQRVpQGAEFSVEDNGPGIAPE 364
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 511672513  834 DIERIFKPFERVEKRDIPSSPGTGLGLTITQLLTDIMGGNISVSSEIGKGSSF 886
Cdd:PRK11006  365 HIPRLTERFYRVDKARSRQTGGSGLGLAIVKHALSHHDSRLEIESEVGKGTRF 417
KinA COG5805
Sporulation sensor histidine kinase A (Stage II sporulation protein SpoIIF/SpoIIJ) [Cell cycle ...
677-889 8.57e-22

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: 100.58  E-value: 8.57e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  677 GISHELRTPLNSVLGYAQLLekspslapehsaKVSLIKRsgEHLADIIegLLDISRIEAGRIEL---------QRDEVAI 747
Cdd:COG5805   293 GIAHEIRNPLTSIKGFLQLL------------QPGIEDK--EEYFDIM--LSELDRIESIISEFlalakpqavNKEKENI 356
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  748 GELLDDLVDMFSLQAKSKGISFVYNPSPYLPNwVTADETQLRQILINLLSNAVK-FTQQGSVTLDVYYRNQVAEFTITDS 826
Cdd:COG5805   357 NELIQDVVTLLETEAILHNIQIRLELLDEDPF-IYCDENQIKQVFINLIKNAIEaMPNGGTITIHTEEEDNSVIIRVIDE 435
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 511672513  827 GVGISEQDIERIFKPFERVEKRdipsspGTGLGLTITQLLTDIMGGNISVSSEIGKGSSFKLS 889
Cdd:COG5805   436 GIGIPEERLKKLGEPFFTTKEK------GTGLGLMVSYKIIENHNGTIDIDSKVGKGTTFTIT 492
PleD COG3706
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate ...
915-1032 1.57e-21

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: 93.05  E-value: 1.57e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  915 SKTVMVVDDDPNHRNLVSEILSPLGFVVHEAND---ALVCLSNTylsAIDLFLLDISMPDMNGWQLLKKLRSN--GISVP 989
Cdd:COG3706     1 PARILVVDDDPTNRKLLRRLLEAAGYEVVEAADgeeALELLQEH---RPDLILLDLEMPDMDGLELCRRLRADprTADIP 77
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 511672513  990 IIMVSADATeapyfnaaEEIHEPALH---NDYLAKPMRDNALLEKV 1032
Cdd:COG3706    78 IIFLTALDD--------EEDRARALEagaDDYLTKPFDPEELLARV 115
Response_reg pfam00072
Response regulator receiver domain; This domain receives the signal from the sensor partner in ...
918-1033 2.37e-21

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: 90.29  E-value: 2.37e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513   918 VMVVDDDPNHRNLVSEILSPLGFVVHEANDALVCLSNTYLSAIDLFLLDISMPDMNGWQLLKKLRSNGISVPIIMVSADA 997
Cdd:pfam00072    1 VLIVDDDPLIRELLRQLLEKEGYVVAEADDGKEALELLKEERPDLILLDINMPGMDGLELLKRIRRRDPTTPVIILTAHG 80
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 511672513   998 TEaPYFNAAEEIHepAlhNDYLAKPMRDNALLEKVA 1033
Cdd:pfam00072   81 DE-DDAVEALEAG--A--DDFLSKPFDPDELLAAIR 111
CitB COG4565
DNA-binding response regulator DpiB of citrate/malate metabolism [Transcription, Signal ...
917-1037 7.72e-21

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


Pssm-ID: 443622 [Multi-domain]  Cd Length: 138  Bit Score: 89.64  E-value: 7.72e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  917 TVMVVDDDPNHRNLVSEILSPLGF--VVHEAND---ALVCLSNTylsAIDLFLLDISMPDMNGWQLLKKLRSNGISVPII 991
Cdd:COG4565     5 RVLIVEDDPMVAELLRRYLERLPGfeVVGVASSgeeALALLAEH---RPDLILLDIYLPDGDGLELLRELRARGPDVDVI 81
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 511672513  992 MVSADATEAPyfnAAEEIHEPAlhNDYLAKPMRDNALLEKVAKALA 1037
Cdd:COG4565    82 VITAARDPET---VREALRAGV--VDYLIKPFTFERLREALERYLE 122
REC_OmpR cd17574
phosphoacceptor receiver (REC) domain of OmpR family response regulators; OmpR-like proteins ...
919-999 1.79e-20

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: 87.08  E-value: 1.79e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  919 MVVDDDPNHRNLVSEILSPLGFVVHEANDALVCLSNTYLSAIDLFLLDISMPDMNGWQLLKKLRSNGISVPIIMVSADAT 998
Cdd:cd17574     1 LVVEDDEEIAELLSDYLEKEGYEVDTAADGEEALELAREEQPDLIILDVMLPGMDGFEVCRRLREKGSDIPIIMLTAKDE 80

                  .
gi 511672513  999 E 999
Cdd:cd17574    81 E 81
cpxA PRK09470
envelope stress sensor histidine kinase CpxA;
606-863 2.13e-20

envelope stress sensor histidine kinase CpxA;


Pssm-ID: 236532 [Multi-domain]  Cd Length: 461  Bit Score: 95.77  E-value: 2.13e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  606 HVFFLLMIIVGV----LVWL-FVLANDSRQFaldesQRQTELLSR-EISAHEVTDQALQQAKETAESANQ---------- 669
Cdd:PRK09470  167 RPLLLLLVTMLVstplLLWLaWSLAKPARKL-----KNAADEVAQgNLRQHPELETGPQEFRQAGASFNQmvtalermmt 241
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  670 AKSRYLTGISHELRTPLNSV-LGYAQLLEKSPSlapehSAKVSLIKRSGEHLADIIEGLLDISRIEAgRIELQRDEVAIG 748
Cdd:PRK09470  242 SQQRLLSDISHELRTPLTRLqLATALLRRRQGE-----SKELERIETEAQRLDSMINDLLVLSRNQQ-KNHLERETFKAN 315
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  749 ELLDDLVDMFSLQAKSKGISFVYNPSPylPNW-VTADETQLRQILINLLSNAVKFTQQgSVTLDVYYRNQVAEFTITDSG 827
Cdd:PRK09470  316 SLWSEVLEDAKFEAEQMGKSLTVSAPP--GPWpINGNPNALASALENIVRNALRYSHT-KIEVAFSVDKDGLTITVDDDG 392
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 511672513  828 VGISEQDIERIFKPFERV-EKRDiPSSPGTGLGLTIT 863
Cdd:PRK09470  393 PGVPEEEREQIFRPFYRVdEARD-RESGGTGLGLAIV 428
REC_hyHK_CKI1_RcsC-like cd17546
phosphoacceptor receiver (REC) domain of hybrid sensor histidine kinases/response regulators ...
918-1032 8.94e-20

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


Pssm-ID: 381099 [Multi-domain]  Cd Length: 113  Bit Score: 85.60  E-value: 8.94e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  918 VMVVDDDPNHRNLVSEILSPLGFVVHEANDALVCL----SNTYlsaiDLFLLDISMPDMNGWQLLKKLR---SNGISVPI 990
Cdd:cd17546     1 VLVVDDNPVNRKVLKKLLEKLGYEVDVAENGQEALellkEEPF----DLVLMDLQMPVMDGLEATRRIReleGGGRRTPI 76
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 511672513  991 IMVSADATEapyfnAAEEIHEPALHNDYLAKPMRDNALLEKV 1032
Cdd:cd17546    77 IALTANALE-----EDREKCLEAGMDDYLSKPVKLDQLKEVL 113
SLC-NCS1sbd_CobB-like cd11484
nucleobase-cation-symport-1 (NCS1) transporter CobB-like; solute-binding domain; This NCS1 ...
47-469 1.41e-18

nucleobase-cation-symport-1 (NCS1) transporter CobB-like; solute-binding domain; This NCS1 subfamily includes Escherichia coli CodB (cytosine permease), and the Saccharomyces cerevisiae transporters: Fcy21p (Purine-cytosine permease), and vitamin B6 transporter Tpn1. NCS1s are essential components of salvage pathways for nucleobases and related metabolites; their known substrates include allantoin, uracil, thiamine, and nicotinamide riboside. NCS1s belong to a superfamily which also contains the solute carrier 5 family sodium/glucose transporters (SLC5s), and solute carrier 6 family neurotransmitter transporters (SLC6s).


Pssm-ID: 271377 [Multi-domain]  Cd Length: 406  Bit Score: 89.59  E-value: 1.41e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513   47 LGAISFLALEAIGGALILNFGFNNSLIAILLVSAIIFFCGLPISYYAARYGVDIDLLTRgAGFGYIGSTITSLIYASFTF 126
Cdd:cd11484    17 LGANFFLASMVTGALLGVGLSLSQAILAVLLGNLIGGAYMALLGYIGARTGLPQMLLSR-ASFGEKGSYLPSLLLGITQI 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  127 IFFAIEAAIMASALELLFNIP--LSIGYLISAIVVIPLVTHGITFISRFQLWSQPIWLVLQLApLIFILWHeSSAINNWL 204
Cdd:cd11484    96 GWFGVGTAMFAIALSKLLGINgsLWLLILIAGVLMTLTAIFGYKALHKLEKIAVPLIIALFVY-SVVLALR-DYGVGGLA 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  205 QFEGKLESGNSGEFNLhlfGAASGILFSLMAQigeqvDFLRFMpeakKKHRACWWVALLSAGPGWIIVGALKILLGSflv 284
Cdd:cd11484   174 ALTATGPLSFLVAVSL---VAGSFISGATYTA-----DYSRYA----KSSKKAFWATFLGFFVGNSLMMILGALLAA--- 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  285 vlainagvaedVAGDPIQMYQVAfsymaqspLLALSLAGIFVLVC-QLKINVTNAYAGSIAWSNFFSRLTHshpgRVVWL 363
Cdd:cd11484   239 -----------ATGTADISEVMI--------AQGLGIPAILVLVLnIWTTNDNNLYSSGLSLSNITKIFRR----KVLTL 295
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  364 VfNVIIALLIMELGIYAALEDILGIYSNVAVAWVGALVAD-LVINKplGYSPKHIEFKRAHLyDINPVGVGSMVIASVLS 442
Cdd:cd11484   296 V-AGIVGTLLAALGIYNHFLNFLLLLGYALPPWGGVMLADyFVVRR--GRYDIDALADPQYG-GVNWAALIAWAVGVAVG 371
                         410       420
                  ....*....|....*....|....*..
gi 511672513  443 IYCYTGNAGDTaqALAPYIGLSTAFVC 469
Cdd:cd11484   372 IPFPYGLLGGG--GIAPINGLLVAAVV 396
BaeS_SmeS NF012163
sensor histidine kinase efflux regulator BaeS;
602-875 1.74e-18

sensor histidine kinase efflux regulator BaeS;


Pssm-ID: 411086 [Multi-domain]  Cd Length: 457  Bit Score: 89.89  E-value: 1.74e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  602 ATLSHVFFLLMIIVGVLVWLFVLANDSRQFALDESQRQTELLSREISAHEVTDqaLQQAKETAESANQAKSRYLTGISHE 681
Cdd:NF012163  173 ALLLAALAAFLLARGLLAPVKRLVEATHRLAAGDYTTRVTPTSNDELGKLAQD--FNQLASTLEKNEQMRRDFMADISHE 250
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  682 LRTPLNSVLGYAQLLEKS-PSLAPEHsakVSLIKRSGEHLADIIEGLLDISRIEAGRIELQRDEVAIGELLDDLVDMFSL 760
Cdd:NF012163  251 LRTPLAVLRAELEAIQDGiRKFTPES---LDSLQAEVGTLTKLVDDLHDLSMSDEGALAYQKASVDLVPLLEVEGGAFRE 327
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  761 QAKSKGISFVYNpspyLPNWVT--ADETQLRQILINLLSNAVKFTQQ-GSVTLDVYYRNQVAEFTITDSGVGISEQDIER 837
Cdd:NF012163  328 RFASAGLELEVS----LPDSSLvfGDRDRLMQLFNNLLENSLRYTDSgGSLHISASQRPKEVTLTVADSAPGVSDEQLAR 403
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 511672513  838 IFKPFERVEKRDIPSSPGTGLGLTITQLLTDIMGGNIS 875
Cdd:NF012163  404 LFERFYRVEVSRNRASGGSGLGLAISLNIVQAHGGTLH 441
PRK10604 PRK10604
sensor protein RstB; Provisional
677-889 2.60e-18

sensor protein RstB; Provisional


Pssm-ID: 236724 [Multi-domain]  Cd Length: 433  Bit Score: 88.89  E-value: 2.60e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  677 GISHELRTPLnsvlgyAQL---LEKSPSL-APEHSAkvslIKRSGEHLADIIEGLLDISRIEAGRIELQRDEVAIGELLD 752
Cdd:PRK10604  218 GIAHELRTPL------VRLryrLEMSDNLsAAESQA----LNRDIGQLEALIEELLTYARLDRPQNELHLSEPDLPAWLS 287
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  753 DLVDMFSLQAKSKGISFVYNPSPylpNWVTADETQLRQILINLLSNAVKFTQQgSVTLDVYYRNQVAEFTITDSGVGISE 832
Cdd:PRK10604  288 THLADIQAVTPEKTVRLDTPHQG---DYGALDMRLMERVLDNLLNNALRYAHS-RVRVSLLLDGNQACLIVEDDGPGIPP 363
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 511672513  833 QDIERIFKPFERVEKRDIPSSPGTGLGLTITQLLTDIMGGNISV-SSEIGkGSSFKLS 889
Cdd:PRK10604  364 EERERVFEPFVRLDPSRDRATGGCGLGLAIVHSIALAMGGSVNCdESELG-GARFSFS 420
YesN COG4753
Two-component response regulator, YesN/AraC family, consists of REC and AraC-type DNA-binding ...
917-1022 3.58e-18

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


Pssm-ID: 443786 [Multi-domain]  Cd Length: 103  Bit Score: 80.97  E-value: 3.58e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  917 TVMVVDDDPNHRNLVSEILSPL-GF-VVHEAND---ALVCLSNTylsAIDLFLLDISMPDMNGWQLLKKLRSNGISVPII 991
Cdd:COG4753     1 KVLIVDDEPLIREGLKRILEWEaGFeVVGEAENgeeALELLEEH---KPDLVITDINMPGMDGLELLEAIRELDPDTKII 77
                          90       100       110
                  ....*....|....*....|....*....|.
gi 511672513  992 MVSADATEApyfNAAEEIHEPAlhNDYLAKP 1022
Cdd:COG4753    78 ILSGYSDFE---YAQEAIKLGA--DDYLLKP 103
HATPase_AtoS-like cd16943
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
787-890 5.52e-18

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: 80.54  E-value: 5.52e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  787 QLRQILINLLSNAVK-FTQQGSVTLDVYYRNQVAEFTITDSGVGISEQDIERIFKPFERVEkrdiPSSPGTGLGLTITQL 865
Cdd:cd16943     3 QLNQVLLNLLVNAAQaMEGRGRITIRTWAHVDQVLIEVEDTGSGIDPEILGRIFDPFFTTK----PVGEGTGLGLSLSYR 78
                          90       100
                  ....*....|....*....|....*
gi 511672513  866 LTDIMGGNISVSSEIGKGSSFKLSI 890
Cdd:cd16943    79 IIQKHGGTIRVASVPGGGTRFTIIL 103
PRK13557 PRK13557
histidine kinase; Provisional
654-982 4.26e-17

histidine kinase; Provisional


Pssm-ID: 237425 [Multi-domain]  Cd Length: 540  Bit Score: 85.88  E-value: 4.26e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  654 DQALQQAKETaESANQaksryLTG-ISHELRTPLNSVLGYAQLLEkspSLAPEHSAKVSLIKRSGEHLADIIE------- 725
Cdd:PRK13557  151 EDALRQAQKM-EALGQ-----LTGgIAHDFNNLLQVMSGYLDVIQ---AALSHPDADRGRMARSVENIRAAAEraatltq 221
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  726 GLLDISRieagRIELQRDEVAIGELLDDLVDMFSlQAKSKGISFVYNPSPYLPNwVTADETQLRQILINLLSNA------ 799
Cdd:PRK13557  222 QLLAFAR----KQRLEGRVLNLNGLVSGMGELAE-RTLGDAVTIETDLAPDLWN-CRIDPTQAEVALLNVLINArdampe 295
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  800 ----------VKFTQQGSVTLDVYYRNQVAEFTITDSGVGISEQDIERIFKPF--ERVEKRdipsspGTGLGLTITQLLT 867
Cdd:PRK13557  296 ggrvtirtrnVEIEDEDLAMYHGLPPGRYVSIAVTDTGSGMPPEILARVMDPFftTKEEGK------GTGLGLSMVYGFA 369
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  868 DIMGGNISVSSEIGKGSSFKLSIMlASLNKEQQPQSVQAPVNSIKGpSKTVMVVDDDPNHRNLVSEILSPLGF---VVHE 944
Cdd:PRK13557  370 KQSGGAVRIYSEVGEGTTVRLYFP-ASDQAENPEQEPKARAIDRGG-TETILIVDDRPDVAELARMILEDFGYrtlVASN 447
                         330       340       350
                  ....*....|....*....|....*....|....*....
gi 511672513  945 ANDALVCLSNTylSAIDLFLLDISMP-DMNGWQLLKKLR 982
Cdd:PRK13557  448 GREALEILDSH--PEVDLLFTDLIMPgGMNGVMLAREAR 484
COG4192 COG4192
Signal transduction histidine kinase regulating phosphoglycerate transport system [Signal ...
624-883 6.47e-17

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


Pssm-ID: 443346 [Multi-domain]  Cd Length: 640  Bit Score: 85.89  E-value: 6.47e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  624 LANDSRQFaLDESQRQTELLSREISAHEVTDQALQQAKE----TAESANQAKSryLTGISHELRTPLNSVLGY-----AQ 694
Cdd:COG4192   385 IARLLRVF-RDQAIEKTQELETEIEERKRIEKNLRQTQDeliqAAKMAVVGQT--MTSLAHELNQPLNAMSMYlfsakKA 461
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  695 LLEKSPSLAPEHSAKV-SLIKRsgehLADIIEGLLDISRieagRIELQRDEVAIGELLDDLVDMFSLQAKSKGISFVYNP 773
Cdd:COG4192   462 LEQENYAQLPTSLDKIeGLIER----MDKIIKSLRQFSR----KSDTPLQPVDLRQVIEQAWELVESRAKPQQITLHIPD 533
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  774 spylPNWVTADETQLRQILINLLSNAVK-FTQQGSVTLDVYYRNQVAEFTITDSGVGISeqDIERIFKPFerVEKRDIps 852
Cdd:COG4192   534 ----DLMVQGDQVLLEQVLVNLLVNALDaVATQPQISVDLLSNAENLRVAISDNGNGWP--LVDKLFTPF--TTTKEV-- 603
                         250       260       270
                  ....*....|....*....|....*....|.
gi 511672513  853 spGTGLGLTITQLLTDIMGGNISVSSEIGKG 883
Cdd:COG4192   604 --GLGLGLSICRSIMQQFGGDLYLASTLERG 632
REC_CheY_CheY3 cd19923
phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY3 and similar CheY ...
918-1036 7.51e-17

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: 77.76  E-value: 7.51e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  918 VMVVDDDPNHRNLVSEILSPLGFV-VHEANDALVCLSNTYLSAIDLFLLDISMPDMNGWQLLKKLRSNG--ISVPIIMVS 994
Cdd:cd19923     3 VLVVDDFSTMRRIIKNLLKELGFNnVEEAEDGVDALEKLKAGGFDFVITDWNMPNMDGLELLKTIRADGalSHLPVLMVT 82
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 511672513  995 ADATEAPYFNAAEeihepALHNDYLAKPMRDNALLEKVAKAL 1036
Cdd:cd19923    83 AEAKKENVIAAAQ-----AGVNNYIVKPFTAATLKEKLEKIF 119
HATPase_FilI-like cd16921
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
788-890 8.39e-17

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: 76.98  E-value: 8.39e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  788 LRQILINLLSNAVKFTQQGSV-TLDVYYRNQVAE--FTITDSGVGISEQDIERIFKPFERVEKRDipSSPGTGLGLTITQ 864
Cdd:cd16921     1 LGQVLTNLLGNAIKFRRPRRPpRIEVGAEDVGEEwtFYVRDNGIGIDPEYAEKVFGIFQRLHSRE--EYEGTGVGLAIVR 78
                          90       100
                  ....*....|....*....|....*.
gi 511672513  865 LLTDIMGGNISVSSEIGKGSSFKLSI 890
Cdd:cd16921    79 KIIERHGGRIWLESEPGEGTTFYFTL 104
FixJ COG4566
DNA-binding response regulator, FixJ family, consists of REC and HTH domains [Signal ...
917-1075 8.51e-17

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: 79.76  E-value: 8.51e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  917 TVMVVDDDPNHRNLVSEILSPLGFVVHEANDALVCLSNTYLSAIDLFLLDISMPDMNGWQLLKKLRSNGISVPIIMVSAD 996
Cdd:COG4566     1 TVYIVDDDEAVRDSLAFLLESAGLRVETFASAEAFLAALDPDRPGCLLLDVRMPGMSGLELQEELAARGSPLPVIFLTGH 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  997 ATEAPyfnAAEEIHEPALhnDYLAKPMRDNALLEKVAKALAIDwnyqnTSTQSASPEPQALNIQLNQ-SQREqlQEIAEM 1075
Cdd:COG4566    81 GDVPM---AVRAMKAGAV--DFLEKPFDDQALLDAVRRALARD-----RARRAERARRAELRARLASlTPRE--REVLDL 148
HisKA cd00082
Histidine Kinase A (dimerization/phosphoacceptor) domain; Histidine Kinase A dimers are formed ...
668-732 2.23e-16

Histidine Kinase A (dimerization/phosphoacceptor) domain; Histidine Kinase A dimers are formed through parallel association of 2 domains creating 4-helix bundles; usually these domains contain a conserved His residue and are activated via trans-autophosphorylation by the catalytic domain of the histidine kinase. They subsequently transfer the phosphoryl group to the Asp acceptor residue of a response regulator protein. Two-component signalling systems, consisting of a histidine protein kinase that senses a signal input and a response regulator that mediates the output, are ancient and evolutionarily conserved signaling mechanisms in prokaryotes and eukaryotes.


Pssm-ID: 119399 [Multi-domain]  Cd Length: 65  Bit Score: 74.56  E-value: 2.23e-16
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 511672513  668 NQAKSRYLTGISHELRTPLNSVLGYAQLLEKSPSLAPEHSAKVSLIKRSGEHLADIIEGLLDISR 732
Cdd:cd00082     1 LQAKGEFLANVSHELRTPLTAIRGALELLEEELLDDEEQREYLERIREEAERLLRLINDLLDLSR 65
CitA COG3290
Sensor histidine kinase DipB regulating citrate/malate metabolism [Signal transduction ...
655-890 4.31e-16

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


Pssm-ID: 442519 [Multi-domain]  Cd Length: 389  Bit Score: 81.82  E-value: 4.31e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  655 QALQQAKETAESanqaksryLTGISHELRTPLNSVLGYAQLLEkspslapehsakvslIKRSGEHLADIIEGLLDISRIE 734
Cdd:COG3290   181 EELEGVKELAEA--------LRAQRHDFRNHLHTISGLLQLGE---------------YDEALEYIDEISEELQELIDSL 237
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  735 AGRIElqrdEVAIGELLDDlvdmFSLQAKSKGISFVYNPSPYLPNWvTADETQLRQILINLLSNAV-----KFTQQGSVT 809
Cdd:COG3290   238 LSRIG----NPVLAALLLG----KAARARERGIDLTIDIDSDLPDL-PLSDTDLVTILGNLLDNAIeavekLPEEERRVE 308
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  810 LDVYYRNQVAEFTITDSGVGISEQDIERIFkpferveKRDIPS--SPGTGLGLTITQLLTDIMGGNISVSSEIGKGSSFK 887
Cdd:COG3290   309 LSIRDDGDELVIEVEDSGPGIPEELLEKIF-------ERGFSTklGEGRGLGLALVKQIVEKYGGTIEVESEEGEGTVFT 381

                  ...
gi 511672513  888 LSI 890
Cdd:COG3290   382 VRL 384
Spo0F COG5803
Stage 0 sporulation initiation response regulator Spo0F [Cell cycle control, cell division, ...
915-1037 5.08e-16

Stage 0 sporulation initiation response regulator Spo0F [Cell cycle control, cell division, chromosome partitioning, Signal transduction mechanisms];


Pssm-ID: 444505 [Multi-domain]  Cd Length: 119  Bit Score: 75.22  E-value: 5.08e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  915 SKTVMVVDDDPNHRNLVSEILSPLGFVVHEANDALVCLSNTYLSAIDLFLLDISMPDMNGWQLLKKLRSNGISVPIIMVS 994
Cdd:COG5803     2 MKKILIVDDQAGIRMLLKEVLKKEGYEVFQAANGKEALEKVKELKPDLVLLDMKMPGMDGIEILKEIKEIDPDIPVIMMT 81
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 511672513  995 ADATEapyfnaaEEIHEpALHN---DYLAKPMRDNALLEKVAKALA 1037
Cdd:COG5803    82 AYGEL-------DMVEE-AKELgakGYFTKPFDIDELREAVNKLLK 119
HATPase_YcbM-like cd16947
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
775-878 5.15e-16

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: 75.63  E-value: 5.15e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  775 PYLPNWVTADETQLRQILINLLSNAVKFTQQGS-VTLDVYYRNQVAEFTITDSGVGISEQDIERIFKPFERVEKRDIPSS 853
Cdd:cd16947     8 PDRPIYANANTEALQRILKNLISNAIKYGSDGKfLGMTLREDEKHVYIDIWDKGKGISETEKDHVFERLYTLEDSRNSAK 87
                          90       100
                  ....*....|....*....|....*
gi 511672513  854 PGTGLGLTITQLLTDIMGGNISVSS 878
Cdd:cd16947    88 QGNGLGLTITKRLAESMGGSIYVNS 112
REC_RssB-like cd17555
phosphoacceptor receiver (REC) domain of Pseudomonas aeruginosa RssB and similar domains; ...
916-1030 5.67e-16

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: 74.93  E-value: 5.67e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  916 KTVMVVDDDPNHRNLVSEILSPLGFVVHEANDALVCLSNTYLSAIDLFLLDISMPDMNGWQLLKKLRSNGISVPIIMVS- 994
Cdd:cd17555     1 ATILVIDDDEVVRESIAAYLEDSGFQVLQAADGRQGLELFRSEQPDLVLCDLRMPEMDGLEVLKQITKESPDTPVIVVSg 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 511672513  995 ----ADATEAPYFNAAeeihepalhnDYLAKPMRDNALLE 1030
Cdd:cd17555    81 agvmSDAVEALRLGAW----------DYLTKPIEDLAVLE 110
HATPase_BasS-like cd16940
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
781-883 5.77e-16

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: 74.75  E-value: 5.77e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  781 VTADETQLRQILINLLSNAVKFTQQGSVTLDVYYRNQVAEFTITDSGVGISEQDIERIFKPFERVEKRdipSSPGTGLGL 860
Cdd:cd16940     7 VQGDALLLFLLLRNLVDNAVRYSPQGSRVEIKLSADDGAVIRVEDNGPGIDEEELEALFERFYRSDGQ---NYGGSGLGL 83
                          90       100
                  ....*....|....*....|...
gi 511672513  861 TITQLLTDIMGGNISVSSEIGKG 883
Cdd:cd16940    84 SIVKRIVELHGGQIFLGNAQGGG 106
HisKA pfam00512
His Kinase A (phospho-acceptor) domain; dimerization and phospho-acceptor domain of histidine ...
670-736 7.11e-16

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


Pssm-ID: 459839 [Multi-domain]  Cd Length: 66  Bit Score: 73.01  E-value: 7.11e-16
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 511672513   670 AKSRYLTGISHELRTPLNSVLGYAQLLEKSPsLAPEHSAKVSLIKRSGEHLADIIEGLLDISRIEAG 736
Cdd:pfam00512    1 AKSEFLANLSHELRTPLTAIRGYLELLRDEK-LDEEQREYLETILRSAERLLRLINDLLDLSRIEAG 66
HATPase_BceS-YxdK-YvcQ-like cd16948
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
784-889 9.58e-16

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: 74.24  E-value: 9.58e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  784 DETQLRQILINLLSNAVKFTQQGS-VTLDVYYRNQVAEFTITDSGVGISEQDIERIFKPF-----ERVEKRdipsspGTG 857
Cdd:cd16948     2 DAKWLSFIIGQIVSNALKYSKQGGkIEIYSETNEQGVVLSIKDFGIGIPEEDLPRVFDKGftgenGRNFQE------STG 75
                          90       100       110
                  ....*....|....*....|....*....|..
gi 511672513  858 LGLTITQLLTDIMGGNISVSSEIGKGSSFKLS 889
Cdd:cd16948    76 MGLYLVKKLCDKLGHKIDVESEVGEGTTFTIT 107
HisKA smart00388
His Kinase A (phosphoacceptor) domain; Dimerisation and phosphoacceptor domain of histidine ...
670-736 1.20e-15

His Kinase A (phosphoacceptor) domain; Dimerisation and phosphoacceptor domain of histidine kinases.


Pssm-ID: 214644 [Multi-domain]  Cd Length: 66  Bit Score: 72.21  E-value: 1.20e-15
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 511672513    670 AKSRYLTGISHELRTPLNSVLGYAQLLEKSPsLAPEHSAKVSLIKRSGEHLADIIEGLLDISRIEAG 736
Cdd:smart00388    1 AKREFLANLSHELRTPLTAIRGYLELLLDTE-LSEEQREYLETILREAERLLRLINDLLDLSRIEAG 66
PRK10955 PRK10955
envelope stress response regulator transcription factor CpxR;
918-1067 1.22e-15

envelope stress response regulator transcription factor CpxR;


Pssm-ID: 182864 [Multi-domain]  Cd Length: 232  Bit Score: 77.54  E-value: 1.22e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  918 VMVVDDDPNHRNLVSEILSPLGF---VVHEANDALVCLSNTylsaIDLFLLDISMPDMNGWQLLKKLRSNGiSVPIIMVS 994
Cdd:PRK10955    4 ILLVDDDRELTSLLKELLEMEGFnviVAHDGEQALDLLDDS----IDLLLLDVMMPKKNGIDTLKELRQTH-QTPVIMLT 78
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 511672513  995 ADATEAPYFNAAEeihepALHNDYLAKPMRDNALlekVAKALAI----DWNYQNTSTQSASPEPQALNIQLNQSQRE 1067
Cdd:PRK10955   79 ARGSELDRVLGLE-----LGADDYLPKPFNDREL---VARIRAIlrrsHWSEQQQNNDNGSPTLEVDALSLNPGRQE 147
REC_D1_PleD-like cd17538
first (D1) phosphoacceptor receiver (REC) domain of response regulator PleD and similar ...
917-1022 1.68e-15

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: 73.30  E-value: 1.68e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  917 TVMVVDDDPNHRNLVSEILSPLGFVVHEANDALVCLSNTYLSAIDLFLLDISMPDMNGWQLLKKLRSNGIS--VPIIMVS 994
Cdd:cd17538     1 KILVVDDEPANRELLEALLSAEGYEVLTADSGQEALALAEEELPDLILLDVMMPGMDGFEVCRRLKEDPETrhIPVIMIT 80
                          90       100
                  ....*....|....*....|....*....
gi 511672513  995 A-DATEapyfNAAEEIHEPAlhNDYLAKP 1022
Cdd:cd17538    81 AlDDRE----DRIRGLEAGA--DDFLSKP 103
AdeS_HK NF012226
two-component sensor histidine kinase AdeS; Mutations in this component of the two-component ...
678-890 3.23e-15

two-component sensor histidine kinase AdeS; Mutations in this component of the two-component regulatory system for the AdeABC efflux pump can confer adaptive resistance to certain antibiotics, including tigecycline.


Pssm-ID: 411090 [Multi-domain]  Cd Length: 353  Bit Score: 78.50  E-value: 3.23e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  678 ISHELRTPLNSVLGYAQ-----LLEKSPSLAPehsakvSLIKRSgEHLADIIEGLLDISRIEAGRIELQRDEVAIGELLD 752
Cdd:NF012226  145 IAHELRTPITILQGRLQgildgVFEPDPALFK------SLLNQV-EGLSHLVEDLRTLSLVENQQLRLNYESVDLKDSIE 217
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  753 DLVDMFSLQAKSKGISFVYNPSPYLpnwVTADETQLRQILINLLSNAVKFTQQGSVTLDVYYRNQVAEFTITDSGVGISE 832
Cdd:NF012226  218 KVLKMFEDRLEQAQLTIVLNLTATP---VFCDRRRIEQVLIALIDNAIRYANAGKLKISSSVIQDDWILQIEDEGPGIAE 294
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 511672513  833 QDIERIFKPFERVEKRDIPSSPGTGLGLTITQLLTDIMGGNISVSSEIGkGSSFKLSI 890
Cdd:NF012226  295 EYQQDLFNPFFRLEQSRNKEFGGTGLGLAVVHAIVIAHKGSIEYSNSQG-NSVFTIKL 351
REC_TrrA-like cd17554
phosphoacceptor receiver (REC) domain of Thermotoga maritima response regulator TrrA and ...
916-995 3.81e-15

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


Pssm-ID: 381106 [Multi-domain]  Cd Length: 113  Bit Score: 72.64  E-value: 3.81e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  916 KTVMVVDDDPNHRNLVSEILSPLGFVVHEANDALVCLSNTYLSAIDLFLLDISMPDMNGWQLLKKLRSNGISVPIIMVSA 995
Cdd:cd17554     1 KKILVVDDEENIRELYKEELEDEGYEVVTAGNGEEALEKLESEDPDLVILDIKMPGMDGLETLRKIREKKPDLPVIICTA 80
PRK10618 PRK10618
phosphotransfer intermediate protein in two-component regulatory system with RcsBC; Provisional
657-900 5.75e-15

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


Pssm-ID: 236726 [Multi-domain]  Cd Length: 894  Bit Score: 79.98  E-value: 5.75e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  657 LQQAKETAESANQAKSRYLTGISHELRTPLNSVLGYAQLLEKSPSLAPEHSAKVSLIKRSgEHLADIIEGLLDISRIEAG 736
Cdd:PRK10618  436 LQQAQREYEKNQQARKAFLQNIGDELKQPLQSLAQLAAQLRQTSDEEQQQPELDQLAEQS-DVLVRLVDNIQLLNMLETQ 514
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  737 RIELQRDEVAIGELLDDLVDMFSLQAKSKGISFVYNPSPYLPNWVTADETQLRQILINLLSNAVKFTQQGSVTLDVYYRN 816
Cdd:PRK10618  515 DWKPEQELFSLQDLIDEVLPEVLPAIKRKGLQLLIHNHLKAEQLRIGDRDALRKILLLLLNYAITTTAYGKITLEVDQDE 594
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  817 QVAE---FTITDSGVGISEQDIERIFKPFERVEKRDIPSSpGTGLGLTITQLLTDIMGGNISVSSEIGKGSSFKLSIMLA 893
Cdd:PRK10618  595 SSPDrltIRILDTGAGVSIKELDNLHFPFLNQTQGDRYGK-ASGLTFFLCNQLCRKLGGHLTIKSREGLGTRYSIHLKML 673

                  ....*..
gi 511672513  894 SLNKEQQ 900
Cdd:PRK10618  674 AADPEVE 680
LytT COG3279
DNA-binding response regulator, LytR/AlgR family [Transcription, Signal transduction ...
917-1037 5.80e-15

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


Pssm-ID: 442510 [Multi-domain]  Cd Length: 235  Bit Score: 75.62  E-value: 5.80e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  917 TVMVVDDDPNHRNLVSEILSPLGF--VVHEANDALVCLSNTYLSAIDLFLLDISMPDMNGWQLLKKLRSNGISVPIIMVS 994
Cdd:COG3279     3 KILIVDDEPLARERLERLLEKYPDleVVGEASNGEEALELLEEHKPDLVFLDIQMPGLDGFELARQLRELDPPPPIIFTT 82
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 511672513  995 AD---ATEAPYFNAAeeihepalhnDYLAKPMRDNALLEKVAKALA 1037
Cdd:COG3279    83 AYdeyALEAFEVNAV----------DYLLKPIDEERLAKALEKAKE 118
REC_2_DhkD-like cd17580
second phosphoacceptor receiver (REC) domain of Dictyostelium discoideum hybrid signal ...
918-1032 6.61e-15

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: 71.72  E-value: 6.61e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  918 VMVVDDDPNHRNLVSEILSPLGFVV---HEANDALVCLSNtylSAIDLFLLDISMPDMNGWQLLKKLRSN--GISVPIIM 992
Cdd:cd17580     1 ILVVDDNEDAAEMLALLLELEGAEVttaHSGEEALEAAQR---FRPDVILSDIGMPGMDGYELARRLRELpwLANTPAIA 77
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 511672513  993 VSAdateapYfnAAEEIHEPALH---NDYLAKPMRDNALLEKV 1032
Cdd:cd17580    78 LTG------Y--GQPEDRERALEagfDAHLVKPVDPDELIELI 112
REC_DivK-like cd17548
phosphoacceptor receiver (REC) domain of DivK and similar proteins; Caulobacter crescentus ...
917-1034 8.07e-15

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: 71.80  E-value: 8.07e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  917 TVMVVDDDPNHRNLVSEILSPLGFVVHEANDALVCLSNTYLSAIDLFLLDISMPDMNGWQLLKKLRSNG--ISVPIIMVS 994
Cdd:cd17548     1 KILIVEDNPLNMKLARDLLESAGYEVLEAADGEEALEIARKEKPDLILMDIQLPGMDGLEATRLLKEDPatRDIPVIALT 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 511672513  995 ADATEAPyfnaAEEIHEpALHNDYLAKPMRDNALLEKVAK 1034
Cdd:cd17548    81 AYAMKGD----REKILE-AGCDGYISKPIDTREFLETVAK 115
REC_OmpR_DrrD-like cd17625
phosphoacceptor receiver (REC) domain of DrrD-like OmpR family response regulators; DrrD is a ...
919-1022 9.83e-15

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: 71.48  E-value: 9.83e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  919 MVVDDDPNHRNLVSEILSPLGFVVHEANDALVCLSNTYLSAIDLFLLDISMPDMNGWQLLKKLRSNGISVPIIMVSA-DA 997
Cdd:cd17625     1 LVVEDEKDLSEAITKHLKKEGYTVDVCFDGEEGLEYALSGIYDLIILDIMLPGMDGLEVLKSLREEGIETPVLLLTAlDA 80
                          90       100
                  ....*....|....*....|....*...
gi 511672513  998 TEapyfnaaEEI---HEPAlhNDYLAKP 1022
Cdd:cd17625    81 VE-------DRVkglDLGA--DDYLPKP 99
REC_RpfG-like cd17551
phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase response regulator ...
917-1022 1.18e-14

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: 71.32  E-value: 1.18e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  917 TVMVVDDDPNHRNLVSEILSPLGFV-VHEANDAL----VCLSNTYlsaiDLFLLDISMPDMNGWQLLKKLRS--NGISVP 989
Cdd:cd17551     2 RILIVDDNPTNLLLLEALLRSAGYLeVVSFTDPRealaWCRENPP----DLILLDYMMPGMDGLEFIRRLRAlpGLEDVP 77
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 511672513  990 IIMVSADATeapyfnaaEEIHEPALH---NDYLAKP 1022
Cdd:cd17551    78 IVMITADTD--------REVRLRALEagaTDFLTKP 105
REC_NtrX-like cd17550
phosphoacceptor receiver (REC) domain of nitrogen assimilation regulatory protein NtrX and ...
918-1037 2.91e-14

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: 70.22  E-value: 2.91e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  918 VMVVDDDPNHRNLVSEILSPLGFVVHEANDALVCLSNTYLSAIDLFLLDISMPDMNGWQLLKKLRSNGISVPIIMVSADA 997
Cdd:cd17550     1 ILIVDDEEDIRESLSGILEDEGYEVDTAADGEEALKLIKERRPDLVLLDIWLPDMDGLELLKEIKEKYPDLPVIMISGHG 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 511672513  998 TEApyfNAAEEIHEPALhnDYLAKPMRDNALLEKVAKALA 1037
Cdd:cd17550    81 TIE---TAVKATKLGAY--DFIEKPLSLDRLLLTIERALE 115
REC_OmpR_CusR-like cd19935
phosphoacceptor receiver (REC) domain of CusR-like OmpR family response regulators; ...
918-1022 3.88e-14

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


Pssm-ID: 381162 [Multi-domain]  Cd Length: 100  Bit Score: 69.39  E-value: 3.88e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  918 VMVVDDDPNHRNLVSEILSPLGFVVHEANDALVCL----SNTYlsaiDLFLLDISMPDMNGWQLLKKLRSNGISVPIIMV 993
Cdd:cd19935     1 ILVVEDEKKLAEYLKKGLTEEGYAVDVAYDGEDGLhlalTNEY----DLIILDVMLPGLDGLEVLRRLRAAGKQTPVLML 76
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 511672513  994 SA-DATE---------ApyfnaaeeihepalhNDYLAKP 1022
Cdd:cd19935    77 TArDSVEdrvkgldlgA---------------DDYLVKP 100
HATPase_CpxA-like cd16949
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
788-877 3.93e-14

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: 69.28  E-value: 3.93e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  788 LRQILINLLSNAVKFTQQgSVTLDVYYRNQVAEFTITDSGVGISEQDIERIFKPFERVEKRDIPSSPGTGLGLTITQLLT 867
Cdd:cd16949     1 LARALENVLRNALRYSPS-KILLDISQDGDQWTITITDDGPGVPEDQLEQIFLPFYRVDSARDRESGGTGLGLAIAERAI 79
                          90
                  ....*....|
gi 511672513  868 DIMGGNISVS 877
Cdd:cd16949    80 EQHGGKIKAS 89
envZ PRK09467
osmolarity sensor protein; Provisional
585-877 4.13e-14

osmolarity sensor protein; Provisional


Pssm-ID: 236531 [Multi-domain]  Cd Length: 435  Bit Score: 76.10  E-value: 4.13e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  585 VYSRIPVTEFAtkaavSATLSHVFFLLMIIvGVLV----WLFVlandsRQ-----FALDESQRQT----------ELLSR 645
Cdd:PRK09467  138 IWVRVPLTEIH-----QGDFSPLFRYTLAI-GLLSvaggWLFI-----RIqnrplVALEHAALQVgkgeippplrEYGAS 206
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  646 EISAheVTdQALQQAKETAESANQAKSRYLTGISHELRTPLNSVlgyaQLleKSPSLAPEHS-AKVSLIKRSgEHLADII 724
Cdd:PRK09467  207 EVRS--VT-RAFNQMAAGIKQLEDDRTLLMAGVSHDLRTPLTRI----RL--ATEMMSEEDGyLAESINKDI-EECNAII 276
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  725 EGLLDISRIEAgriELQRDEVAIGELLDDLVdmfslQAKS---KGISFVYNPSPYLpnwVTADETQLRQILINLLSNAVK 801
Cdd:PRK09467  277 EQFIDYLRTGQ---EMPMEMADLNALLGEVI-----AAESgyeREIETALQPGPIE---VPMNPIAIKRALANLVVNAAR 345
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 511672513  802 FTQqGSVTLDVYYRNQVAEFTITDSGVGISEQDIERIFKPFERVEK-RdipSSPGTGLGLTITQLLTDIMGGNISVS 877
Cdd:PRK09467  346 YGN-GWIKVSSGTEGKRAWFQVEDDGPGIPPEQLKHLFQPFTRGDSaR---GSSGTGLGLAIVKRIVDQHNGKVELG 418
HATPase_EcPhoR-like cd16952
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
788-886 1.20e-13

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: 68.00  E-value: 1.20e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  788 LRQILINLLSNAVKFT-QQGSVTLDVYYRNQVAEFTITDSGVGISEQDIERIFKPFERVEKRDIPSSPGTGLGLTITQLL 866
Cdd:cd16952     1 LRSAFSNLVSNAVKYTpPSDTITVRWSQEESGARLSVEDTGPGIPPEHIPRLTERFYRVDIERCRNTGGTGLGLAIVKHV 80
                          90       100
                  ....*....|....*....|
gi 511672513  867 TDIMGGNISVSSEIGKGSSF 886
Cdd:cd16952    81 MSRHDARLLIASELGKGSRF 100
PRK10610 PRK10610
chemotaxis protein CheY;
919-1034 1.51e-13

chemotaxis protein CheY;


Pssm-ID: 170568 [Multi-domain]  Cd Length: 129  Bit Score: 68.46  E-value: 1.51e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  919 MVVDDDPNHRNLVSEILSPLGF-VVHEANDALVCLSNTYLSAIDLFLLDISMPDMNGWQLLKKLRSNG--ISVPIIMVSA 995
Cdd:PRK10610    9 LVVDDFSTMRRIVRNLLKELGFnNVEEAEDGVDALNKLQAGGFGFVISDWNMPNMDGLELLKTIRADGamSALPVLMVTA 88
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 511672513  996 DATEAPYFNAAEeihepALHNDYLAKPMRDNALLEKVAK 1034
Cdd:PRK10610   89 EAKKENIIAAAQ-----AGASGYVVKPFTAATLEEKLNK 122
PRK11361 PRK11361
acetoacetate metabolism transcriptional regulator AtoC;
914-1038 1.67e-13

acetoacetate metabolism transcriptional regulator AtoC;


Pssm-ID: 183099 [Multi-domain]  Cd Length: 457  Bit Score: 74.11  E-value: 1.67e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  914 PSKTVMVVDDDPNHRNLVSEILSPLGFVVHEANDALVCLSNTYLSAIDLFLLDISMPDMNGWQLLKKLRSNGISVPIIMV 993
Cdd:PRK11361    3 AINRILIVDDEDNVRRMLSTAFALQGFETHCANNGRTALHLFADIHPDVVLMDIRMPEMDGIKALKEMRSHETRTPVILM 82
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 511672513  994 SADATEApyfNAAEEIHEPALhnDYLAKPMRDNALLEKVAKALAI 1038
Cdd:PRK11361   83 TAYAEVE---TAVEALRCGAF--DYVIKPFDLDELNLIVQRALQL 122
REC_OmpR_KdpE-like cd17620
phosphoacceptor receiver (REC) domain of KdpE-like OmpR family response regulators; KdpE is a ...
918-1022 2.25e-13

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: 67.19  E-value: 2.25e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  918 VMVVDDDPNHRNLVSEILSPLGFVVHEANDALVCLSNTYLSAIDLFLLDISMPDMNGWQLLKKLRSNGiSVPIIMVSADA 997
Cdd:cd17620     1 ILVIEDEPQIRRFLRTALEAHGYRVFEAETGQEGLLEAATRKPDLIILDLGLPDMDGLEVIRRLREWS-AVPVIVLSARD 79
                          90       100
                  ....*....|....*....|....*...
gi 511672513  998 TEapyfnaAEEIHepALH---NDYLAKP 1022
Cdd:cd17620    80 EE------SDKIA--ALDagaDDYLTKP 99
REC_FixJ cd17537
phosphoacceptor receiver (REC) domain of FixJ family response regulators; FixJ family response ...
917-1036 2.35e-13

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


Pssm-ID: 381092 [Multi-domain]  Cd Length: 116  Bit Score: 67.62  E-value: 2.35e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  917 TVMVVDDDPNHRNLVSEILSPLGFVVHEANDALVCLSNTYLSAIDLFLLDISMPDMNGWQLLKKLRSNGISVPIIMVSAD 996
Cdd:cd17537     2 TVYVVDDDEAVRDSLAFLLRSVGLAVKTFTSASAFLAAAPPDQPGCLVLDVRMPGMSGLELQDELLARGSNIPIIFITGH 81
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 511672513  997 ATeAPYfnAAEEIHEPALhnDYLAKPMRDNALLEKVAKAL 1036
Cdd:cd17537    82 GD-VPM--AVEAMKAGAV--DFLEKPFRDQVLLDAIEQAL 116
REC_OmpR_MtPhoP-like cd17615
phosphoacceptor receiver (REC) domain of MtPhoP-like OmpR family response regulators; ...
917-1038 3.12e-13

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: 67.38  E-value: 3.12e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  917 TVMVVDDDPNHRNLVSEILSPLGFVVHEANDALVCLSNTYLSAIDLFLLDISMPDMNGWQLLKKLRSNGISVPIIMVSA- 995
Cdd:cd17615     1 RVLVVDDEPNITELLSMALRYEGWDVETAADGAEALAAAREFRPDAVVLDIMLPDMDGLEVLRRLRADGPDVPVLFLTAk 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 511672513  996 DATEapyfnaaEEIHE-PALHNDYLAKPMrdnALLEKVAKALAI 1038
Cdd:cd17615    81 DSVE-------DRIAGlTAGGDDYVTKPF---SLEEVVARLRAL 114
REC_OmpR_CpxR cd17623
phosphoacceptor receiver (REC) domain of CpxR-like OmpR family response regulators; CpxR is ...
918-1038 3.12e-13

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: 67.33  E-value: 3.12e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  918 VMVVDDDPNHRNLVSEILSPLGFVVHEANDALVCLSNTYLSAIDLFLLDISMPDMNGWQLLKKLRSNGiSVPIIMVSADA 997
Cdd:cd17623     1 ILLIDDDRELTELLTEYLEMEGFNVRAAHDGEQGLAALLEGSPDLVVLDVMLPKMNGLDVLKELRKTS-QVPVLMLTARG 79
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 511672513  998 TEAPYFNAAEeihepALHNDYLAKPMRDNALlekVAKALAI 1038
Cdd:cd17623    80 DDIDRILGLE-----LGADDYLPKPFNPREL---VARIRAI 112
HATPase_EnvZ-like cd16950
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
788-883 3.46e-13

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: 66.70  E-value: 3.46e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  788 LRQILINLLSNAVKFTQqGSVTLDVYYRNQVAEFTITDSGVGISEQDIERIFKPFERVEK-RDIpssPGTGLGLTITQLL 866
Cdd:cd16950     1 LKRVLSNLVDNALRYGG-GWVEVSSDGEGNRTRIQVLDNGPGIAPEEVDELFQPFYRGDNaRGT---SGTGLGLAIVQRI 76
                          90
                  ....*....|....*..
gi 511672513  867 TDIMGGNISVSSEIGKG 883
Cdd:cd16950    77 SDAHGGSLTLANRAGGG 93
REC_typeB_ARR-like cd17584
phosphoacceptor receiver (REC) domain of type B Arabidopsis response regulators (ARRs) and ...
918-1028 3.96e-13

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: 66.88  E-value: 3.96e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  918 VMVVDDDPNHRNLVSEILSPLGFVV---HEANDALVCLSNTYLSaIDLFLLDISMPDMNGWQLLKKLRSNgISVPIIMVS 994
Cdd:cd17584     1 VLVVDDDPTCLAILKRMLLRCGYQVttcTDAEEALSMLRENKDE-FDLVITDVHMPDMDGFEFLELIRLE-MDLPVIMMS 78
                          90       100       110
                  ....*....|....*....|....*....|....
gi 511672513  995 ADATEAPYFNAAEeiHEPAlhnDYLAKPMRDNAL 1028
Cdd:cd17584    79 ADGSTSTVMKGLA--HGAC---DYLLKPVSIEDL 107
REC_OmpR_PrrA-like cd17627
phosphoacceptor receiver (REC) domain of PrrA-like OmpR family response regulators; The ...
918-1038 4.61e-13

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: 66.64  E-value: 4.61e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  918 VMVVDDDPNHRNLVSEILSPLGFVVHEANDALVCLSNTYLSAIDLFLLDISMPDMNGWQLLKKLRSNGISVPIIMVSADA 997
Cdd:cd17627     1 ILVVDDDRAVRESLRRSLRFEGYEVETAVDGAEALRVISGNRPDAVVLDVMMPRLDGLEVCRRLRAAGNDLPILVLTARD 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 511672513  998 TEAPYFNAAEeihepALHNDYLAKPMrdnALLEKVAKALAI 1038
Cdd:cd17627    81 SVSDRVAGLD-----AGADDYLVKPF---ALEELLARVRAL 113
PRK10549 PRK10549
two-component system sensor histidine kinase BaeS;
655-875 5.02e-13

two-component system sensor histidine kinase BaeS;


Pssm-ID: 182539 [Multi-domain]  Cd Length: 466  Bit Score: 72.74  E-value: 5.02e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  655 QALQQAKETAESANQAKSRYLTGISHELRTPLNSVLGYAQLLE---KSPSLAPEHS--AKVSLikrsgehLADIIEGLLD 729
Cdd:PRK10549  224 QDFNQLASTLEKNEQMRRDFMADISHELRTPLAVLRGELEAIQdgvRKFTPESVASlqAEVGT-------LTKLVDDLHQ 296
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  730 ISRIEAGRIELQRDEVAIGELLDDLVDMFSLQAKSKGISFVYNpspyLPNWVT--ADETQLRQILINLLSNAVKFT-QQG 806
Cdd:PRK10549  297 LSLSDEGALAYRKTPVDLVPLLEVAGGAFRERFASRGLTLQLS----LPDSATvfGDPDRLMQLFNNLLENSLRYTdSGG 372
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 511672513  807 SVTLDVYYRNQVAEFTITDSGVGISEQDIERIFKPFERVEKRDIPSSPGTGLGLTITQLLTDIMGGNIS 875
Cdd:PRK10549  373 SLHISAEQRDKTLRLTFADSAPGVSDEQLQKLFERFYRTEGSRNRASGGSGLGLAICLNIVEAHNGRII 441
REC_CheY4-like cd17562
phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY4 and similar CheY ...
916-1036 5.40e-13

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: 66.56  E-value: 5.40e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  916 KTVMVVDDDPNHRNLVSEILSPLGFVVHEANDALVCLSNTYLSAIDLFLLDISMPDMNGWQLLKKLRSNGI--SVPIIMV 993
Cdd:cd17562     1 KKILAVDDSASIRQMVSFTLRGAGYEVVEAADGRDALSKAQSKKFDLIITDQNMPNMDGIELIKELRKLPAykFTPILML 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 511672513  994 SADATEAPYFNAAEeihepALHNDYLAKPMRDNALLEKVAKAL 1036
Cdd:cd17562    81 TTESSDEKKQEGKA-----AGATGWLVKPFDPEQLLEVVKKVL 118
glnL PRK11073
nitrogen regulation protein NR(II);
654-878 5.75e-13

nitrogen regulation protein NR(II);


Pssm-ID: 182947 [Multi-domain]  Cd Length: 348  Bit Score: 71.65  E-value: 5.75e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  654 DQALQQAKETAESANQAKSRYLT-GISHELRTPLNSVLGYAQLLEKS---PSLApEHSaKVsLIKRsgehlADIIEGLLD 729
Cdd:PRK11073  112 DNQRRLSQEQLQHAQQVAARDLVrGLAHEIKNPLGGLRGAAQLLSKAlpdPALT-EYT-KV-IIEQ-----ADRLRNLVD 183
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  730 isRIEAGRIELQRDEVAIGELLDDLVDMFSLQaKSKGISFV--YNPSpyLPNwVTADETQLRQILINLLSNAVKFTQQ-- 805
Cdd:PRK11073  184 --RLLGPQRPGTHVTESIHKVAERVVQLVSLE-LPDNVRLIrdYDPS--LPE-LAHDPDQIEQVLLNIVRNALQALGPeg 257
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  806 GSVTL-----------DVYYRnQVAEFTITDSGVGISEQDIERIFKPFerVEKRDipssPGTGLGLTITQLLTDIMGGNI 874
Cdd:PRK11073  258 GTITLrtrtafqltlhGERYR-LAARIDIEDNGPGIPPHLQDTLFYPM--VSGRE----GGTGLGLSIARNLIDQHSGKI 330

                  ....
gi 511672513  875 SVSS 878
Cdd:PRK11073  331 EFTS 334
HATPase_RstB-like cd16939
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
788-889 6.69e-13

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: 65.91  E-value: 6.69e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  788 LRQILINLLSNAVKFTQQgSVTLDVYYRNQVAEFTITDSGVGISEQDIERIFKPFERVEKRDIPSSPGTGLGLTITQLLT 867
Cdd:cd16939     1 MARALDNLLRNALRYAHR-TVRIALLVSGGRLTLIVEDDGPGIPAAARERVFEPFVRLDPSRDRATGGFGLGLAIVHRVA 79
                          90       100
                  ....*....|....*....|...
gi 511672513  868 DIMGGNISV-SSEIGkGSSFKLS 889
Cdd:cd16939    80 LWHGGHVECdDSELG-GACFRLT 101
HATPase_BaeS-like cd16946
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
784-881 6.93e-13

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: 65.95  E-value: 6.93e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  784 DETQLRQILINLLSNAVKFTQQG-SVTLDVYYRNQVAEFTITDSGVGISEQDIERIFKPFERVEKRDIPSSPGTGLGLTI 862
Cdd:cd16946     1 DRDRLQQLFVNLLENSLRYTDTGgKLRIRAAQTPQEVRLDVEDSAPGVSDDQLARLFERFYRVESSRNRASGGSGLGLAI 80
                          90       100
                  ....*....|....*....|
gi 511672513  863 TQLLTDIMGGNISVS-SEIG 881
Cdd:cd16946    81 CHNIALAHGGTISAEhSPLG 100
REC_YesN-like cd17536
phosphoacceptor receiver (REC) domain of YesN and related helix-turn-helix containing response ...
918-1037 7.67e-13

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: 66.21  E-value: 7.67e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  918 VMVVDDDPNHRNLVSEIL--SPLGF-VVHEAND---ALVCLSNTylsAIDLFLLDISMPDMNGWQLLKKLRSNGISVPII 991
Cdd:cd17536     1 VLIVDDEPLIREGLKKLIdwEELGFeVVGEAENgeeALELIEEH---KPDIVITDIRMPGMDGLELIEKIRELYPDIKII 77
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 511672513  992 MVSAdateapY--FNAAEEihepALHN---DYLAKPMRDNALLEKVAKALA 1037
Cdd:cd17536    78 ILSG------YddFEYAQK----AIRLgvvDYLLKPVDEEELEEALEKAKE 118
REC_CheY cd17542
phosphoacceptor receiver (REC) domain of chemotaxis protein CheY; The chemotaxis response ...
916-1036 9.76e-13

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: 65.76  E-value: 9.76e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  916 KTVMVVDDDPNHRNLVSEILSPLGF-VVHEAND-ALVCLSNTYLSaIDLFLLDISMPDMNGWQLLKKLRSNGISVPIIMV 993
Cdd:cd17542     1 KKVLIVDDAAFMRMMLKDILTKAGYeVVGEAANgEEAVEKYKELK-PDLVTMDITMPEMDGIEALKEIKKIDPNAKVIMC 79
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 511672513  994 SAdateapyfNAAEEIHEPALHN---DYLAKPMRDNALLEKVAKAL 1036
Cdd:cd17542    80 SA--------MGQEEMVKEAIKAgakDFIVKPFQPERVLEAVEKVL 117
HATPase_TutC-TodS-like cd16925
Histidine kinase-like ATPase domain of hybrid sensor histidine kinases similar to Pseudomonas ...
784-890 1.19e-12

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: 65.21  E-value: 1.19e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  784 DETQLRQILINLLSNAVKFTQQG---SVTLDVYYRNQvAEFTITDSGVGISEQDIERIFKPFERVEKRDIPSSPGTGLGL 860
Cdd:cd16925     1 DAEKYERVVLNLLSNAFKFTPDGgriRCILEKFRLNR-FLLTVSDSGPGIPPNLREEIFERFRQGDGSSTRAHGGTGLGL 79
                          90       100       110
                  ....*....|....*....|....*....|
gi 511672513  861 TITQLLTDIMGGNISVSSEIGKGSSFKLSI 890
Cdd:cd16925    80 SIVKEFVELHGGTVTVSDAPGGGALFQVEL 109
REC_hyHK_blue-like cd18161
phosphoacceptor receiver (REC) domain of hybrid sensor histidine kinase/response regulators ...
918-1022 1.83e-12

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: 64.68  E-value: 1.83e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  918 VMVVDDDPNHRNLVSEILSPLGFVVHEAND---ALVCLSNTylSAIDLFLLDISMPD-MNGWQLLKKLRSNGISVPIIMV 993
Cdd:cd18161     1 VLVVEDDPDVRRLTAEVLEDLGYTVLEAASgdeALDLLESG--PDIDLLVTDVIMPGgMNGSQLAEEARRRRPDLKVLLT 78
                          90       100
                  ....*....|....*....|....*....
gi 511672513  994 SADATEApyfnAAEEIHEPALhnDYLAKP 1022
Cdd:cd18161    79 SGYAENA----IEGGDLAPGV--DVLSKP 101
PRK10755 PRK10755
two-component system sensor histidine kinase PmrB;
678-872 2.97e-12

two-component system sensor histidine kinase PmrB;


Pssm-ID: 236751 [Multi-domain]  Cd Length: 356  Bit Score: 69.61  E-value: 2.97e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  678 ISHELRTPLNSVLGYAQLLEKSpslapeHSAKVS-LIKRSgEHLADIIEGLLDISRIEagrielqrDEVAIG-----ELL 751
Cdd:PRK10755  144 VAHELRTPLAGIRLHLELLEKQ------HHIDVApLIARL-DQMMHTVEQLLQLARAG--------QSFSSGhyqtvKLL 208
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  752 DDLV----DMFSLQAKSKGISFVYnPSPYLPNWVTADETQLRQILINLLSNAVKFTQQGS-VTLDVYYRNQVAEFTITDS 826
Cdd:PRK10755  209 EDVIlpsqDELSEMLEQRQQTLLL-PESAADITVQGDATLLRLLLRNLVENAHRYSPEGStITIKLSQEDGGAVLAVEDE 287
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 511672513  827 GVGISEQDIERIFKPFERVEKRdipsSPGTGLGLTITQLLTDIMGG 872
Cdd:PRK10755  288 GPGIDESKCGELSKAFVRMDSR----YGGIGLGLSIVSRITQLHHG 329
HATPase_ETR2_ERS2-EIN4-like cd16938
Histidine kinase-like ATPase domain of Arabidopsis thaliana ETR2, ERS2, and EIN4, and related ...
777-890 3.82e-12

Histidine kinase-like ATPase domain of Arabidopsis thaliana ETR2, ERS2, and EIN4, and related domains; This family includes the histidine kinase-like ATPase domains (HATPase) of three out of the five receptors that recognize the plant hormone ethylene in Arabidopsis thaliana. These three proteins have been classified as belonging to subfamily 2: ETR2, ERS2, and EIN4. They lack most of the motifs characteristic of histidine kinases, and EIN4 is the only one in this group containing the conserved histidine that is phosphorylated in two-component and phosphorelay systems. This family also includes the HATPase domains of Escherichia coli RcsD phosphotransferase which is a component of the Rcs-signaling system, a complex multistep phosphorelay involving five proteins, and is involved in many transcriptional networks such as cell division, biofilm formation, and virulence, among others. Also included is Schizosaccharomyces pombe Mak3 (Phk1) which participates in a multi-step two-component related system which regulates H2O2-induced activation of the Sty1 stress-activated protein kinase pathway. Most proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA), and a GAF sensor domain; most are hybrid sensor histidine kinases as they also contain a REC signal receiver domain.


Pssm-ID: 340415 [Multi-domain]  Cd Length: 133  Bit Score: 64.79  E-value: 3.82e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  777 LPNWVTADETQLRQILINLLSNAVKFTQQ-GSVTLDVYYRNQVAEFTITDSG----------------VGISEQDIERIF 839
Cdd:cd16938     1 LPDVVVGDERRVFQVLLHMLGNLLKMRNGgGNITFRVFLEGGSEDRSDRDWGpwrpsmsdesveirfeVEINDSGSPSIE 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 511672513  840 KPFERVE--KRDIPSSPGTGLGLTITQLLTDIMGGNISVSSEIGKGSSFKLSI 890
Cdd:cd16938    81 SASMRNSlnRRYNLSELGEHLSFSICKQLVQLMGGNIWIVPGSGLGTTMSLLL 133
REC_Ycf29 cd19927
phosphoacceptor receiver (REC) domain of probable transcriptional regulator Ycf29; Ycf29 is a ...
918-995 7.56e-12

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


Pssm-ID: 381154 [Multi-domain]  Cd Length: 102  Bit Score: 62.78  E-value: 7.56e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  918 VMVVDDDPNHRNLVSEILSPLGFVVHEANDALVCLSNTYLSAIDLFLLDISMPDMNGWQLLKKLRSNG--ISVPIIMVSA 995
Cdd:cd19927     1 ILLVDDDPGIRLAVKDYLEDQGFTVIAASNGLEALDLLNQYIPDLIISDIIMPGVDGYSLLGKLRKNAdfDTIPVIFLTA 80
REC_citrate_TCS cd19925
phosphoacceptor receiver (REC) domain of citrate family two-component system response ...
917-1022 1.08e-11

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: 63.03  E-value: 1.08e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  917 TVMVVDDDPN----HRNLVSEIlsPlGFVV----HEANDALVCLSNTylsAIDLFLLDISMPDMNGWQLLKKLRSNGISV 988
Cdd:cd19925     2 NVLIVEDDPMvaeiHRAYVEQV--P-GFTVigtaGTGEEALKLLKER---QPDLILLDIYLPDGNGLDLLRELRAAGHDV 75
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 511672513  989 PIIMVSADateapyfNAAEEIHEpALHN---DYLAKP 1022
Cdd:cd19925    76 DVIVVTAA-------NDVETVRE-ALRLgvvDYLIKP 104
HATPase_SpaK_NisK-like cd16975
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
784-890 1.69e-11

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: 62.09  E-value: 1.69e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  784 DETQLRQILINLLSNAVKFT-QQGSVTLDVYYRNQVAEFTITDSGVGISEQDIERIFKPFERvEKRDIPSSPGTGLGLTI 862
Cdd:cd16975     1 DTLLLSRALINIISNACQYApEGGTVSISIYDEEEYLYFEIWDNGHGFSEQDLKKALELFYR-DDTSRRSGGHYGMGLYI 79
                          90       100
                  ....*....|....*....|....*...
gi 511672513  863 TQLLTDIMGGNISVSSEIGKGSSFKLSI 890
Cdd:cd16975    80 AKNLVEKHGGSLIIENSQKGGAEVTVKI 107
HATPase_TmoS-FixL-DctS-like cd16920
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
788-890 2.39e-11

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


Pssm-ID: 340397 [Multi-domain]  Cd Length: 104  Bit Score: 61.26  E-value: 2.39e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  788 LRQILINLLSNAVKFTQQGSVTLDV----YYRNQVAEFTI--TDSGVGISEQDIERIFKPFERVEkrdipsSPGTGLGLT 861
Cdd:cd16920     1 IQQVLINLVRNGIEAMSEGGCERREltirTSPADDRAVTIsvKDTGPGIAEEVAGQLFDPFYTTK------SEGLGMGLS 74
                          90       100
                  ....*....|....*....|....*....
gi 511672513  862 ITQLLTDIMGGNISVSSEIGKGSSFKLSI 890
Cdd:cd16920    75 ICRSIIEAHGGRLSVESPAGGGATFQFTL 103
PRK11086 PRK11086
sensory histidine kinase DcuS; Provisional
762-890 2.64e-11

sensory histidine kinase DcuS; Provisional


Pssm-ID: 236839 [Multi-domain]  Cd Length: 542  Bit Score: 67.63  E-value: 2.64e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  762 AKSKGISFVYNPSPYLPNwvTADETQ---LRQILINLLSN---AVKFTQQGSVTLDVYYRNQVAEFTITDSGVGISEQDI 835
Cdd:PRK11086  407 ARELGITLIISEDSQLPD--SGDEDQvheLITILGNLIENaleAVGGEEGGEISVSLHYRNGWLHCEVSDDGPGIAPDEI 484
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 511672513  836 ERIF-KPFervekrdipSSPGT--GLGLTITQLLTDIMGGNISVSSEIGKGSSFKLSI 890
Cdd:PRK11086  485 DAIFdKGY---------STKGSnrGVGLYLVKQSVENLGGSIAVESEPGVGTQFFVQI 533
REC_OmpR_PmrA-like cd17624
phosphoacceptor receiver (REC) domain of PmrA-like OmpR family response regulators; This ...
918-1037 6.95e-11

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


Pssm-ID: 381139 [Multi-domain]  Cd Length: 115  Bit Score: 60.58  E-value: 6.95e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  918 VMVVDDDPNHRNLVSEILSPLGFVV------HEANDALVclSNTYlsaiDLFLLDISMPDMNGWQLLKKLRSNGISVPII 991
Cdd:cd17624     1 ILLVEDDALLGDGLKTGLRKAGYAVdwvrtgAEAEAALA--SGPY----DLVILDLGLPDGDGLDLLRRWRRQGQSLPVL 74
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 511672513  992 MVSA-DATEapyfnaaEEIHepALH---NDYLAKPMrdnALLEKVA--KALA 1037
Cdd:cd17624    75 ILTArDGVD-------DRVA--GLDagaDDYLVKPF---ALEELLArlRALL 114
PRK10651 PRK10651
transcriptional regulator NarL; Provisional
917-1037 7.81e-11

transcriptional regulator NarL; Provisional


Pssm-ID: 182619 [Multi-domain]  Cd Length: 216  Bit Score: 63.12  E-value: 7.81e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  917 TVMVVDDDPNHRNLVSEILS--PLGFVVHEANDALVCLSNTYLSAIDLFLLDISMPDMNGWQLLKKLRSNGISVPIIMVS 994
Cdd:PRK10651    8 TILLIDDHPMLRTGVKQLISmaPDITVVGEASNGEQGIELAESLDPDLILLDLNMPGMNGLETLDKLREKSLSGRIVVFS 87
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 511672513  995 ADateapyfNAAEEIHEpALHN---DYLAKPMRDNALLEKVAKALA 1037
Cdd:PRK10651   88 VS-------NHEEDVVT-ALKRgadGYLLKDMEPEDLLKALQQAAA 125
REC_PA4781-like cd19920
phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase PA4781 and similar ...
918-995 8.51e-11

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


Pssm-ID: 381147 [Multi-domain]  Cd Length: 103  Bit Score: 59.83  E-value: 8.51e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  918 VMVVDDDPNHRNLVSEILSPLGFVVHEANDALVCLSNTYLSAIDLFLLDISMPDMNGWQLLKKLRSN----GIsvPIIMV 993
Cdd:cd19920     1 ILIVDDVPDNLRLLSELLRAAGYRVLVATDGQQALQRAQAEPPDLILLDVMMPGMDGFEVCRRLKADpatrHI--PVIFL 78

                  ..
gi 511672513  994 SA 995
Cdd:cd19920    79 TA 80
REC_NarL-like cd17535
phosphoacceptor receiver (REC) domain of NarL (Nitrate/Nitrite response regulator L) family ...
918-1037 9.42e-11

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: 60.22  E-value: 9.42e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  918 VMVVDDDPNHRN-LVSEILSPLGF-VVHEANDALVCLSNTYLSAIDLFLLDISMPDMNGWQLLKKLRSNGISVPIIMVSA 995
Cdd:cd17535     1 VLIVDDHPLVREgLRRLLESEPDIeVVGEAADGEEALALLRELRPDVVLMDLSMPGMDGIEALRRLRRRYPDLKVIVLTA 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 511672513  996 dateapyFNAAEEIhEPALHND---YLAKPMRDNALLEKVAKALA 1037
Cdd:cd17535    81 -------HDDPEYV-LRALKAGaagYLLKDSSPEELIEAIRAVAA 117
REC_DctD-like cd17549
phosphoacceptor receiver (REC) domain of C4-dicarboxylic acid transport protein D (DctD) and ...
918-1036 9.73e-11

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


Pssm-ID: 381101 [Multi-domain]  Cd Length: 130  Bit Score: 60.58  E-value: 9.73e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  918 VMVVDDDPNHRNLVSEILSPLGFVVHEANDALVCLSNTYLSAIDLFLLDISMPDMNGWQLLKKLRSNGISVPIIMVSA-- 995
Cdd:cd17549     1 VLLVDDDADVREALQQTLELAGFRVRAFADAEEALAALSPDFPGVVISDIRMPGMDGLELLAQIRELDPDLPVILITGhg 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 511672513  996 D---ATEApyfnaaeeIHEPALhnDYLAKPMRDNALLEKVAKAL 1036
Cdd:cd17549    81 DvpmAVEA--------MRAGAY--DFLEKPFDPERLLDVVRRAL 114
AmiR COG3707
Two-component response regulator, AmiR/NasT family, consists of REC and RNA-binding ...
914-1037 1.11e-10

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: 62.28  E-value: 1.11e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  914 PSKTVMVVDDDPNHRNLVSEILSPLGF-VVHEANDALVCLSNTYLSAIDLFLLDISMPDMNGWQLLKKLRSNGIsVPIIM 992
Cdd:COG3707     2 RGLRVLVVDDEPLRRADLREGLREAGYeVVAEAADGEDAVELVRELKPDLVIVDIDMPDRDGLEAARQISEERP-APVIL 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 511672513  993 VSADATEApYFNAAEEIHEPAlhndYLAKPMRDNALLEKVAKALA 1037
Cdd:COG3707    81 LTAYSDPE-LIERALEAGVSA----YLVKPLDPEDLLPALELALA 120
REC_CheV-like cd19924
phosphoacceptor receiver (REC) domain of chemotaxis protein CheV and similar proteins; This ...
918-1022 1.31e-10

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: 59.70  E-value: 1.31e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  918 VMVVDDDPNHRNLVSEILSPLGFVVHEAND---ALVCLSNTYLSA------IDLFLLDISMPDMNGWQLLKKLRSNGI-- 986
Cdd:cd19924     1 ILVVDDSPTARKQLRDLLKNLGFEIAEAVDgeeALNKLENLAKEGndlskeLDLIITDIEMPKMDGYELTFELRDDPRla 80
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 511672513  987 SVPIIMVSADATEapyFNAAEEihEPALHNDYLAKP 1022
Cdd:cd19924    81 NIPVILNSSLSGE---FSRARG--KKVGADAYLAKF 111
REC_OmpR_PhoB cd17618
phosphoacceptor receiver (REC) domain of PhoB response regulator from the OmpR family; The ...
916-1036 1.44e-10

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: 59.57  E-value: 1.44e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  916 KTVMVVDDDPNHRNLVSEILSPLGFVVHEANDALVCLSNTYLSAIDLFLLDISMPDMNGWQLLKKLRSNGI--SVPIIMV 993
Cdd:cd17618     1 RTILIVEDEPAIREMIAFNLERAGFDVVEAEDAESAVNLIVEPRPDLILLDWMLPGGSGIQFIRRLKRDEMtrDIPIIML 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 511672513  994 SADATEAPYFNAAEeihepALHNDYLAKPMRDNALLEKVaKAL 1036
Cdd:cd17618    81 TARGEEEDKVRGLE-----AGADDYITKPFSPRELVARI-KAV 117
HATPase_VanS-like cd16923
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
788-890 1.57e-10

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Enterococcus faecium VanS; This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component sensor histidine kinase (HKs) such as Enterococcus faecium VanS HK of the VanS-VanR two-component regulatory system (TCS) which activates the transcription of vanH, vanA and vanX vancomycin resistance genes. It also contains Ecoli YedV and PcoS, probable members of YedW-YedV TCS and PcoS-PcoR TCS, repectively. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA); most also have a HAMP sensor domain.


Pssm-ID: 340400 [Multi-domain]  Cd Length: 102  Bit Score: 58.94  E-value: 1.57e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  788 LRQILINLLSNAVKFTQQGS-VTLDVYYRNQVAEFTITDSGVGISEQDIERIFKPFERVEK-RDipsSPGTGLGLTITQL 865
Cdd:cd16923     1 LQRVFSNLLSNAIKYSPENTrIYITSFLTDDVVNIMFKNPSSHPLDFKLEKLFERFYRGDNsRN---TEGAGLGLSIAKA 77
                          90       100
                  ....*....|....*....|....*
gi 511672513  866 LTDIMGGNISVSSEiGKGSSFKLSI 890
Cdd:cd16923    78 IIELHGGSASAEYD-DNHDLFKVRL 101
HATPase_HupT_MifS-like cd16976
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
788-888 1.76e-10

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: 59.01  E-value: 1.76e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  788 LRQILINLLSNA---VKFTQQGSVTLDVYYRNQVAEFTITDSGVGISEQDIERIFKPFERVEkrdiPSSPGTGLGLTITQ 864
Cdd:cd16976     1 IQQVLMNLLQNAldaMGKVENPRIRIAARRLGGRLVLVVRDNGPGIAEEHLSRVFDPFFTTK----PVGKGTGLGLSISY 76
                          90       100
                  ....*....|....*....|....
gi 511672513  865 LLTDIMGGNISVSSEIGKGSSFKL 888
Cdd:cd16976    77 GIVEEHGGRLSVANEEGAGARFTF 100
REC_OmpR_BsPhoP-like cd19937
phosphoacceptor receiver (REC) domain of BsPhoP-like OmpR family response regulators; Bacillus ...
919-1036 1.79e-10

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: 59.21  E-value: 1.79e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  919 MVVDDDPNHRNLVSEILSPLGFVVHEANDALVCLSNTYLSAIDLFLLDISMPDMNGWQLLKKLRSNGI--SVPIIMVSAD 996
Cdd:cd19937     1 LVVDDEEDIVELLKYNLEKEGYEVVTAYDGEEALKRAKDEKPDLIILDLMLPGIDGLEVCRILRSDPKtsSIPIIMLTAK 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 511672513  997 ATEapyfnaAEEIHEPAL-HNDYLAKPMRDNALLEKVaKAL 1036
Cdd:cd19937    81 GEE------FDKVLGLELgADDYITKPFSPRELLARV-KAV 114
REC_OmpR_ArcA_TorR-like cd17619
phosphoacceptor receiver (REC) domain of ArcA- and TorR-like OmpR family response regulators; ...
918-995 1.84e-10

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: 59.32  E-value: 1.84e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  918 VMVVDDDPNHRNLVSEILSPLGFVVHEANDA---LVCLSNtylSAIDLFLLDISMPDMNGWQLLKKLRSNGiSVPIIMVS 994
Cdd:cd17619     3 ILIVEDEPVTRATLKSYFEQEGYDVSEAGDGeemRQILAR---QDIDLVLLDINLPGKDGLSLTRELREQS-EVGIILVT 78

                  .
gi 511672513  995 A 995
Cdd:cd17619    79 G 79
marine_sort_HK TIGR03785
proteobacterial dedicated sortase system histidine kinase; This histidine kinase protein is ...
678-876 1.86e-10

proteobacterial dedicated sortase system histidine kinase; This histidine kinase protein is paired with an adjacent response regulator (TIGR03787) gene. It co-occurs with a variant sortase enzyme (TIGR03784), usually in the same gene neighborhood, in proteobacterial species most of which are marine, and with an LPXTG motif-containing sortase target conserved protein (TIGR03788). Sortases and LPXTG proteins are far more common in Gram-positive bacteria, where sortase systems mediate attachment to the cell wall or cross-linking of pilin structures. We give this predicted sensor histidine kinase the gene symbol psdS, for Proteobacterial Dedicated Sortase system Sensor histidine kinase.


Pssm-ID: 163497 [Multi-domain]  Cd Length: 703  Bit Score: 65.15  E-value: 1.86e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513   678 ISHELRTPLNSVlgyaqllekSPSLapEHSAKVSLIKRSGEHLADIIEGLLDISRI-----EAGRIE--LQRDEVA---I 747
Cdd:TIGR03785  492 LSHELRTPVAVV---------RSSL--ENLELQALEQEKQKYLERAREGTERLSMIlnnmsEATRLEqaIQSAEVEdfdL 560
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513   748 GELLDDLvdMFSLQAKSKGISFVYN-PSPYLPNWVTADetQLRQILINLLSNAVKFTQQGSVT-LDVYYRNQVAEFTITD 825
Cdd:TIGR03785  561 SEVLSGC--MQGYQMTYPPQRFELNiPETPLVMRGSPE--LIAQMLDKLVDNAREFSPEDGLIeVGLSQNKSHALLTVSN 636
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 511672513   826 SGVGISEQDIERIFKPFERVEKRDIPSSPGTGLGLTITQLLTDIMGGNISV 876
Cdd:TIGR03785  637 EGPPLPEDMGEQLFDSMVSVRDQGAQDQPHLGLGLYIVRLIADFHQGRIQA 687
REC_Rcp-like cd17557
phosphoacceptor receiver (REC) domain of cyanobacterial phytochrome response regulator Rcp and ...
917-1040 2.17e-10

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: 59.35  E-value: 2.17e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  917 TVMVVDDDPNHRNLVSEILSPLGFV--VHEAND---ALVCLS--NTYLSAI--DLFLLDISMPDMNGWQLLKKLRSNGI- 986
Cdd:cd17557     1 TILLVEDNPGDAELIQEAFKEAGVPneLHVVRDgeeALDFLRgeGEYADAPrpDLILLDLNMPRMDGFEVLREIKADPDl 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 511672513  987 -SVPIIMVSadATEAPyfnaaEEIHEP-ALH-NDYLAKPMRDNALLEKVaKALAIDW 1040
Cdd:cd17557    81 rRIPVVVLT--TSDAE-----EDIERAyELGaNSYIVKPVDFEEFVEAI-RSLGEYW 129
REC_CheB-like cd17541
phosphoacceptor receiver (REC) domain of chemotaxis response regulator protein-glutamate ...
918-1036 2.62e-10

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


Pssm-ID: 381096 [Multi-domain]  Cd Length: 125  Bit Score: 58.94  E-value: 2.62e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  918 VMVVDDDPNHRNLVSEILS--PLGFVVHEANDALVCLSNTYLSAIDLFLLDISMPDMNGWQLLKKLRSNGiSVPIIMVSA 995
Cdd:cd17541     3 VLIVDDSAVMRKLLSRILEsdPDIEVVGTARDGEEALEKIKELKPDVITLDIEMPVMDGLEALRRIMAER-PTPVVMVSS 81
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 511672513  996 DATEapyfnAAEEIHEpALHN---DYLAKP-MRDNALLEKVAKAL 1036
Cdd:cd17541    82 LTEE-----GAEITLE-ALELgavDFIAKPsGGISLDLEEIAEEL 120
PRK10365 PRK10365
sigma-54-dependent response regulator transcription factor ZraR;
918-1037 3.08e-10

sigma-54-dependent response regulator transcription factor ZraR;


Pssm-ID: 182412 [Multi-domain]  Cd Length: 441  Bit Score: 63.90  E-value: 3.08e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  918 VMVVDDDPNHRNLVSEILSPLGFVVHEANDALVCLSNTYLSAIDLFLLDISMPDMNGWQLLKKLRSNGISVPIIMVSADA 997
Cdd:PRK10365    8 ILVVDDDISHCTILQALLRGWGYNVALANSGRQALEQVREQVFDLVLCDVRMAEMDGIATLKEIKALNPAIPVLIMTAYS 87
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 511672513  998 TEApyfNAAEEIHEPALhnDYLAKPMRDNALLEKVAKALA 1037
Cdd:PRK10365   88 SVE---TAVEALKTGAL--DYLIKPLDFDNLQATLEKALA 122
PRK09835 PRK09835
Cu(+)/Ag(+) sensor histidine kinase;
756-890 3.16e-10

Cu(+)/Ag(+) sensor histidine kinase;


Pssm-ID: 182101 [Multi-domain]  Cd Length: 482  Bit Score: 64.02  E-value: 3.16e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  756 DMFSLQAKSKGISFVYNPSPYlpnWVTADETQLRQILINLLSNAVKFTQQG-SVTLDVYYRNQVAEFTITDSGVGISEQD 834
Cdd:PRK09835  347 DFFEAWAEERGVELRFVGDPC---QVAGDPLMLRRAISNLLSNALRYTPAGeAITVRCQEVDHQVQLVVENPGTPIAPEH 423
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 511672513  835 IERIFKPFERVEKRDIPSSPGTGLGLTITQLLTDIMGGNISVSSEIgKGSSFKLSI 890
Cdd:PRK09835  424 LPRLFDRFYRVDPSRQRKGEGSGIGLAIVKSIVVAHKGTVAVTSDA-RGTRFVISL 478
REC_CpdR_CckA-like cd18160
phosphoacceptor receiver (REC) domain of Brucella abortus CpdR and CckA, and similar domains; ...
917-1005 3.57e-10

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


Pssm-ID: 381144 [Multi-domain]  Cd Length: 103  Bit Score: 57.90  E-value: 3.57e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  917 TVMVVDDDPNHRNLVSEILSPLGFVVHEANDALVCLSNTYL-SAIDLFLLDISMPDMNGWQLLKKLRSNGISVPIIMVSA 995
Cdd:cd18160     1 TILLADDEPSVRKFIVTTLKKAGYAVTEAESGAEALEKLQQgKDIDIVVTDIVMPEMDGIELAREARKIDPDVKILFISG 80
                          90
                  ....*....|
gi 511672513  996 DATEAPYFNA 1005
Cdd:cd18160    81 GAAAAPELLS 90
HATPase_CckA-like cd16919
Histidine kinase-like ATPase domain of two-component sensor hybrid histidine kinases, similar ...
788-888 3.86e-10

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: 58.55  E-value: 3.86e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  788 LRQILINLLSNAVKFTQQG--------SVTLDVYYRNQVAE--------FTITDSGVGISEQDIERIFKPFERVEkrdiP 851
Cdd:cd16919     1 LELAILNLAVNARDAMPEGgrltietsNQRVDADYALNYRDlipgnyvcLEVSDTGSGMPAEVLRRAFEPFFTTK----E 76
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 511672513  852 SSPGTGLGLTITQLLTDIMGGNISVSSEIGKGSSFKL 888
Cdd:cd16919    77 VGKGTGLGLSMVYGFVKQSGGHLRIYSEPGVGTTVRI 113
orf27 CHL00148
Ycf27; Reviewed
912-1065 4.11e-10

Ycf27; Reviewed


Pssm-ID: 214376 [Multi-domain]  Cd Length: 240  Bit Score: 61.27  E-value: 4.11e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  912 KGPSKTVMVVDDDPNHRNLVSEILSPLGFVVHEANDALVCLSNTYLSAIDLFLLDISMPDMNGWQLLKKLRSNGiSVPII 991
Cdd:CHL00148    3 ENSKEKILVVDDEAYIRKILETRLSIIGYEVITASDGEEALKLFRKEQPDLVILDVMMPKLDGYGVCQEIRKES-DVPII 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  992 MVSA-----DATEAPYFNAaeeihepalhNDYLAKPMRDNALLEKVAKALAidwNYQNTSTQSASPEPQ-----ALNIQL 1061
Cdd:CHL00148   82 MLTAlgdvsDRITGLELGA----------DDYVVKPFSPKELEARIRSVLR---RTNKKSFSSKIPNSSiirigFLKIDL 148

                  ....
gi 511672513 1062 NQSQ 1065
Cdd:CHL00148  149 NKKQ 152
PRK09836 PRK09836
DNA-binding transcriptional activator CusR; Provisional
918-1036 4.31e-10

DNA-binding transcriptional activator CusR; Provisional


Pssm-ID: 182102 [Multi-domain]  Cd Length: 227  Bit Score: 61.09  E-value: 4.31e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  918 VMVVDDDPNHRNLVSEILSPLGFVVHEANDALVCLSNTYLSAIDLFLLDISMPDMNGWQLLKKLRSNGISVPIIMVSADA 997
Cdd:PRK09836    3 LLIVEDEKKTGEYLTKGLTEAGFVVDLADNGLNGYHLAMTGDYDLIILDIMLPDVNGWDIVRMLRSANKGMPILLLTALG 82
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 511672513  998 TEAPYFNAAEeihepALHNDYLAKPMRDNALLEKVAKAL 1036
Cdd:PRK09836   83 TIEHRVKGLE-----LGADDYLVKPFAFAELLARVRTLL 116
HATPase_PhoQ-like cd16954
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
749-878 4.46e-10

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Escherichia coli PhoQ and Providencia stuartii AarG; This family includes histidine kinase-like ATPase (HATPase) domain of two-component sensor histidine kinases similar to Escherichia coli PhoQ and Providencia stuartii AarG. PhoQ is the histidine kinase (HK) of the PhoP-PhoQ two-component regulatory system (TCS), which responds to the levels of Mg2+ and Ca2+, controls virulence, mediates the adaptation to Mg2+-limiting environments, and regulates numerous cellular activities. Providencia stuartii AarG is a putative sensor kinase which controls the expression of the 2'-N-acetyltransferase and an intrinsic multiple antibiotic resistance (Mar) response in Providencia stuartii. The AarG product is similar to PhoQ in that it is able to restore wild-type levels of resistance to a Salmonella typhimurium phoQ mutant. However, the expression of the 2'-N-acetyltransferase gene and of aarP (a gene encoding a transcriptional activator of 2'-N-acetyltransferase) are not significantly affected by the levels of Mg2+ or Ca2+. Most proteins in this group contain a histidine kinase dimerization and phosphoacceptor domain (HisKA); some have an accessory HAMP sensor domain, and some have an intracellular membrane -interaction PhoQ sensor domain.


Pssm-ID: 340430 [Multi-domain]  Cd Length: 135  Bit Score: 58.80  E-value: 4.46e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  749 ELLDDLVDMFSLQAKSKGISFVYNPSPYLpNWVtADETQLRQILINLLSNAVKFTQqGSVTLDVYYRNQVAEFTITDSGV 828
Cdd:cd16954     1 PLLDSLCSALNKVYQRKGVSISLDISPEL-RFP-GERNDLMELLGNLLDNACKWCL-EFVEVTARQTDGGLHLIVDDDGP 77
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 511672513  829 GISEQDIERIFKPFERVEKrdipSSPGTGLGLTITQLLTDIMGGNISVSS 878
Cdd:cd16954    78 GVPESQRSKIFQRGQRLDE----QRPGQGLGLAIAKEIVEQYGGELSLSD 123
SLC-NCS1sbd cd10323
nucleobase-cation-symport-1 (NCS1) transporters; solute-binding domain; NCS1s are essential ...
72-469 5.08e-10

nucleobase-cation-symport-1 (NCS1) transporters; solute-binding domain; NCS1s are essential components of salvage pathways for nucleobases and related metabolites; their known substrates include allantoin, uracil, thiamine, and nicotinamide riboside. This family includes Microbacterium liquefaciens Mhp1, a transporter that mediates the uptake of indolyl methyl- and benzyl-hydantoins as part of a metabolic salvage pathway for their conversion to amino acids. It also includes various Saccharomyces cerevisiae transporters: Fcy21p (Purine-cytosine permease), vitamin B6 transporter Tpn1, nicotinamide riboside transporter 1 (Nrt1p, also called Thi71p), Dal4p (allantoin permease), Fui1p (uridine permease), and Fur4p (uracil permease). Mhp1 has 12 transmembrane (TM) helices (an inverted topology repeat: TMs1-5 and TMs6-10, and TMs11-12; TMs numbered to conform to the solute carrier 6 family Aquifex aeolicus LeuT). NCS1s belong to a superfamily which also contains the solute carrier 5 family sodium/glucose transporters (SLC5s), and SLC6 neurotransmitter transporters.


Pssm-ID: 271358  Cd Length: 414  Bit Score: 63.07  E-value: 5.08e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513   72 LIAILLVSAIIFFCGlpisYYAARYGVDIDLLTRgAGFGYIGSTITSLIYASFTFIFFAIEAAIMASALELLF------- 144
Cdd:cd10323    41 LIGCLIIGIFLVLNG----RIGYKYGIPFAVQLR-ASFGIKGSHIPSLLRGVPAIVWFGFQTWLGALALNEISgllfgfd 115
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  145 NIPLsiGYLISAIVVIPLVTHGITFISRFQLWSQPIWLVLqlapLIFILWhesSAINNWLQFEGKLESGNSGEFNLHLFG 224
Cdd:cd10323   116 NIVL--CFIIFGLLQIVLSFFGIKAIKWLENIAAPAIIAA----LVYMFY---LLVNKAGDEIGENLWYKAGTWGLPFLV 186
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  225 AAS---GILFSLMAQIGeqvDFLRFMpEAKKKHRACWWVALLSAGPGWIIVGalkiLLGsflVVLAINAGVAedvagDPI 301
Cdd:cd10323   187 AIMafvGNWAALALNAP---DYSREL-KPGKRNRNVGLAQFVALVPAFLFMG----LIG---AMSTAATGIW-----NPV 250
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  302 QMYQVAFsymaqSPLLALSLAGIFVLVCQLKinvTNAYAGSIAWSNFFSRLTHSHPGRVVWLVFNVIIALLIMELGIY-- 379
Cdd:cd10323   251 DVIQGVV-----SNGFLLVLTLVFIVLAQWS---TNIAANIVPPAYVFMNLFPRKITYKTGVVIAGILGLCICPWLLVnd 322
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  380 -AALEDILGIYSNVAVAWVGALVADLVINKplgysPKHIEFkrAHLYD----------INPVGVGSMVIASVLSIYCYtg 448
Cdd:cd10323   323 lSALTTFLGIYSAFLGPIFGIMIADYYVLR-----RRRVNV--DDLYDangqykyfkgVNWAAIIAMAVGAAAALLLV-- 393
                         410       420
                  ....*....|....*....|.
gi 511672513  449 nagdtaqALAPYIGLSTAFVC 469
Cdd:cd10323   394 -------DLSWFVGLIVAGLL 407
REC_OmpR_EcPhoP-like cd19934
phosphoacceptor receiver (REC) domain of EcPhoP-like OmpR family response regulators; ...
918-1036 6.62e-10

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


Pssm-ID: 381161 [Multi-domain]  Cd Length: 117  Bit Score: 57.68  E-value: 6.62e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  918 VMVVDDDPNHRNLVSEILSPLGFVVHEANDAL--VCLSNTYlsAIDLFLLDISMPDMNGWQLLKKLRSNGISVPIIMVSA 995
Cdd:cd19934     1 LLLVEDDALLAAQLKEQLSDAGYVVDVAEDGEeaLFQGEEE--PYDLVVLDLGLPGMDGLSVLRRWRSEGRATPVLILTA 78
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 511672513  996 DATEApyfNAAEEIHEPAlhNDYLAKPMRDNALLEKVaKAL 1036
Cdd:cd19934    79 RDSWQ---DKVEGLDAGA--DDYLTKPFHIEELLARL-RAL 113
fixJ PRK09390
response regulator FixJ; Provisional
917-1037 9.14e-10

response regulator FixJ; Provisional


Pssm-ID: 181815 [Multi-domain]  Cd Length: 202  Bit Score: 59.63  E-value: 9.14e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  917 TVMVVDDDPNHRNLVSEILSPLGF--VVHEAN----DALVCLSNTYLsaidlfLLDISMPDMNGWQLLKKLRSNGISVPI 990
Cdd:PRK09390    5 VVHVVDDDEAMRDSLAFLLDSAGFevRLFESAqaflDALPGLRFGCV------VTDVRMPGIDGIELLRRLKARGSPLPV 78
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 511672513  991 IMVSADAtEAPYfnAAEEIHEPALhnDYLAKPMRDNALLEKVAKALA 1037
Cdd:PRK09390   79 IVMTGHG-DVPL--AVEAMKLGAV--DFIEKPFEDERLIGAIERALA 120
ompR PRK09468
osmolarity response regulator; Provisional
918-1032 1.50e-09

osmolarity response regulator; Provisional


Pssm-ID: 181883 [Multi-domain]  Cd Length: 239  Bit Score: 59.60  E-value: 1.50e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  918 VMVVDDDPNHRNLVSEILSPLGFVVHEANDALVClsNTYLS--AIDLFLLDISMPDMNGWQLLKKLRSNGISVPIIMVSA 995
Cdd:PRK09468    8 ILVVDDDMRLRALLERYLTEQGFQVRSAANAEQM--DRLLTreSFHLMVLDLMLPGEDGLSICRRLRSQNNPTPIIMLTA 85
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 511672513  996 DATEAPYFNAAEeihepALHNDYLAKPMRDNALLEKV 1032
Cdd:PRK09468   86 KGEEVDRIVGLE-----IGADDYLPKPFNPRELLARI 117
REC_PatA-like cd17602
phosphoacceptor receiver (REC) domain of PatA and similar domains; Nostoc sp. (or Anabaena sp.) ...
918-994 1.58e-09

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


Pssm-ID: 381129 [Multi-domain]  Cd Length: 102  Bit Score: 56.22  E-value: 1.58e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 511672513  918 VMVVDDDPNHRNLVSEILSPLGFVVHEANDALVCLSNTYLSAIDLFLLDISMPDMNGWQLLKKLRSNGI--SVPIIMVS 994
Cdd:cd17602     1 VACVDDRPSIQKMIEYFLEKQGFRVVVIDDPLRALTTLLNSKPDLILIDIDMPDLDGYELCSLLRKSSAlkDTPIIMLT 79
REC_HupR-like cd17569
phosphoacceptor receiver (REC) domain of hydrogen uptake protein regulator (HupR) and similar ...
916-1037 1.74e-09

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: 56.64  E-value: 1.74e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  916 KTVMVVDDDPNHRNLVSEILSPLGFVVHEAND---ALVCLSNtylSAIDLFLLDISMPDMNGWQLLKKLRSNGISVPIIM 992
Cdd:cd17569     1 PTILLVDDEPNILKALKRLLRREGYEVLTATSgeeALEILKQ---EPVDVVISDQRMPGMDGAELLKRVRERYPDTVRIL 77
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 511672513  993 VSADATeapyFNAAEE-IHEPALHNdYLAKPMRDNALLEKVAKALA 1037
Cdd:cd17569    78 LTGYAD----LDAAIEaINEGEIYR-FLTKPWDDEELKETIRQALE 118
REC_NtrC1-like cd17572
phosphoacceptor receiver (REC) domain of nitrogen regulatory protein C 1 (NtrC1) from Aquifex ...
918-1036 1.97e-09

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: 56.44  E-value: 1.97e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  918 VMVVDDDPNHRNLVSEILSPLGF---VVHEANDALVCLSNtylSAIDLFLLDISMPDMNGWQLLKKLRSNGISVPIIMVS 994
Cdd:cd17572     1 VLLVEDSPSLAALYQEYLSDEGYkvtHVETGKEALAFLSD---QPPDVVLLDLKLPDMSGMEILKWIQERSLPTSVIVIT 77
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 511672513  995 ADATeapyFN-AAEEIHEPALhnDYLAKPMRDNALLEKVAKAL 1036
Cdd:cd17572    78 AHGS----VDiAVEAMRLGAY--DFLEKPFDADRLRVTVRNAL 114
REC_CheC-like cd17593
phosphoacceptor receiver (REC) domain of uncharacterized response regulators containing a CheC ...
916-996 2.15e-09

phosphoacceptor receiver (REC) domain of uncharacterized response regulators containing a CheC domain; This subfamily is composed of uncharacterized proteins containing an N-terminal REC domain and a C-terminal CheC domain that may function as the output/effector domain of a response regulator. CheC is a CheY-P phosphatase, affecting the level of phosphorylated CheY which controls the sense of flagella rotation and determine swimming behavior of chemotactic bacteria. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381124 [Multi-domain]  Cd Length: 117  Bit Score: 56.39  E-value: 2.15e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  916 KTVMVVDDDPNHRNLVSEILSP-LGFVVHEA---NDALVCLSNtylSAIDLFLLDISMPDMNGWQLLKKLRSNGISVPII 991
Cdd:cd17593     1 MKVLICDDSSMARKQLARALPAdWDVEITFAengEEALEILRE---GRIDVLFLDLTMPVMDGYEVLEALPVEQLETKVI 77

                  ....*
gi 511672513  992 MVSAD 996
Cdd:cd17593    78 VVSGD 82
REC_OmpR_YycF-like cd17614
phosphoacceptor receiver (REC) domain of YrcF-like OmpR family response regulators; YycF ...
918-1032 4.14e-09

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: 55.51  E-value: 4.14e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  918 VMVVDDDPNHRNLVSEILSPLGFVVHEANDALVCLSNTYLSAIDLFLLDISMPDMNGWQLLKKLRsNGISVPIIMVSADA 997
Cdd:cd17614     1 ILVVDDEKPISDILKFNLTKEGYEVVTAYDGREALEKVEEEQPDLILLDLMLPEKDGLEVCREVR-KTSNVPIIMLTAKD 79
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 511672513  998 TEapyFNAAEEIHEPAlhNDYLAKPMRDNALLEKV 1032
Cdd:cd17614    80 SE---VDKVLGLELGA--DDYVTKPFSNRELLARV 109
REC_RR468-like cd17552
phosphoacceptor receiver (REC) domain of Thermotoga maritima response regulator RR468 and ...
915-997 4.50e-09

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


Pssm-ID: 381104 [Multi-domain]  Cd Length: 121  Bit Score: 55.64  E-value: 4.50e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  915 SKTVMVVDDDPNHRNLVS---EILSplGFVVHEANDALVCLSNTYLSAIDLFLLDISMPDMNGWQLLKKLRSNG--ISVP 989
Cdd:cd17552     1 SKRILVIDDEEDIREVVQaclEKLA--GWEVLTASSGQEGLEKAATEQPDAILLDVMMPDMDGLATLKKLQANPetQSIP 78

                  ....*...
gi 511672513  990 IIMVSADA 997
Cdd:cd17552    79 VILLTAKA 86
COG4567 COG4567
DNA-binding response regulator, ActR/RegA family, consists of REC and Fis-type HTH domains ...
914-1022 4.79e-09

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: 56.85  E-value: 4.79e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  914 PSKTVMVVDDDPNHRNLVSEILSPLGFVVHEAND---ALVCLSNtylSAIDLFLLDISMPDMNGWQLLKKLRSNGISVPI 990
Cdd:COG4567     3 EDRSLLLVDDDEAFARVLARALERRGFEVTTAASveeALALLEQ---APPDYAVLDLRLGDGSGLDLIEALRERDPDARI 79
                          90       100       110
                  ....*....|....*....|....*....|..
gi 511672513  991 IMVSADATEApyfNAAEEIHEPALHndYLAKP 1022
Cdd:COG4567    80 VVLTGYASIA---TAVEAIKLGADD--YLAKP 106
HATPase_DpiB-CitA-like cd16915
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
791-890 6.11e-09

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: 54.60  E-value: 6.11e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  791 ILINLLSNAV-----KFTQQGSVTLDVYYRNQVAEFTITDSGVGISEQDIERIFkpferveKRDIPSSPGT--GLGLTIT 863
Cdd:cd16915     4 IVGNLIDNALdalaaTGAPNKQVEVFLRDEGDDLVIEVRDTGPGIAPELRDKVF-------ERGVSTKGQGerGIGLALV 76
                          90       100
                  ....*....|....*....|....*..
gi 511672513  864 QLLTDIMGGNISVSSEIGKGSSFKLSI 890
Cdd:cd16915    77 RQSVERLGGSITVESEPGGGTTFSIRI 103
REC_2_GGDEF cd17544
second phosphoacceptor receiver (REC) domain of uncharacterized GGDEF domain proteins; This ...
918-1022 8.11e-09

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


Pssm-ID: 381098 [Multi-domain]  Cd Length: 122  Bit Score: 54.83  E-value: 8.11e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  918 VMVVDDDPNHRNLVSEILSPLGFVVHEAND---ALVCLSNTylSAIDLFLLDISMPDMNGWQLLKKLRSNGIS--VPIIM 992
Cdd:cd17544     3 VLVVDDSATSRNHLRALLRRHNFQVLEAANgqeALEVLEQH--PDIKLVITDYNMPEMDGFELVREIRKKYSRdqLAIIG 80
                          90       100       110
                  ....*....|....*....|....*....|....
gi 511672513  993 VSA--DATEAPYF--NAAeeihepalhNDYLAKP 1022
Cdd:cd17544    81 ISAsgDNALSARFikAGA---------NDFLTKP 105
PRK10337 PRK10337
sensor protein QseC; Provisional
673-864 1.13e-08

sensor protein QseC; Provisional


Pssm-ID: 182388 [Multi-domain]  Cd Length: 449  Bit Score: 58.89  E-value: 1.13e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  673 RYLTGISHELRTPLNSV---LGYAQLLEKSPslAPEHSAKVSL---IKRSgehlADIIEGLLDISRIEAGRIELQRDEVA 746
Cdd:PRK10337  239 RFTSDAAHELRSPLAALkvqTEVAQLSDDDP--QARKKALLQLhagIDRA----TRLVDQLLTLSRLDSLDNLQDVAEIP 312
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  747 IGELLDDLV-DMFSL-QAKSKGISFVYNPSPYlpnwVTADETQLRQILI-NLLSNAVKFTQQGS-VTLDVYYRnqvaEFT 822
Cdd:PRK10337  313 LEDLLQSAVmDIYHTaQQAGIDVRLTLNAHPV----IRTGQPLLLSLLVrNLLDNAIRYSPQGSvVDVTLNAR----NFT 384
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 511672513  823 ITDSGVGISEQDIERIFKPFERVEKRDipsSPGTGLGLTITQ 864
Cdd:PRK10337  385 VRDNGPGVTPEALARIGERFYRPPGQE---ATGSGLGLSIVR 423
REC_NarL cd19931
phosphoacceptor receiver (REC) domain of Nitrate/Nitrite response regulator L (NarL); Nitrate ...
918-1037 1.16e-08

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: 54.28  E-value: 1.16e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  918 VMVVDDDPNHRNLVSEILS--PLGFVVHEANDALVCLSNTYLSAIDLFLLDISMPDMNGWQLLKKLRSNGISVPIIMVSA 995
Cdd:cd19931     1 VLLIDDHPLLRKGIKQLIEldPDFTVVGEASSGEEGIELAERLDPDLILLDLNMKGMSGLDTLKALREEGVSARIVILTV 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 511672513  996 DATEAPYFNAAEeihepALHNDYLAKPMRDNALLEKVAKALA 1037
Cdd:cd19931    81 SDAEDDVVTALR-----AGADGYLLKDMEPEDLLEALKQAAS 117
REC smart00448
cheY-homologous receiver domain; CheY regulates the clockwise rotation of E. coli flagellar ...
916-970 1.20e-08

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: 52.19  E-value: 1.20e-08
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*
gi 511672513    916 KTVMVVDDDPNHRNLVSEILSPLGFVVHEANDALVCLSNTYLSAIDLFLLDISMP 970
Cdd:smart00448    1 MRILVVDDDPLLRELLKALLEKEGYEVDEATDGEEALELLKEEKPDLILLDIMMP 55
PRK10693 PRK10693
two-component system response regulator RssB;
943-1032 1.39e-08

two-component system response regulator RssB;


Pssm-ID: 182652 [Multi-domain]  Cd Length: 303  Bit Score: 57.69  E-value: 1.39e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  943 HEANDALVCLSNTYLSAIDLFLLDISMPDMNGWQLLKKLRSNGISVPIIMVSadATEapyfNAAEEIHepALH---NDYL 1019
Cdd:PRK10693    1 VLAANGVDALELLGGFTPDLIICDLAMPRMNGIEFVEHLRNRGDQTPVLVIS--ATE----NMADIAK--ALRlgvQDVL 72
                          90
                  ....*....|....
gi 511672513 1020 AKPMRD-NALLEKV 1032
Cdd:PRK10693   73 LKPVKDlNRLREMV 86
REC_OmpR_CtrA cd17616
phosphoacceptor receiver (REC) domain of CtrA-like OmpR family response regulators; CtrA is ...
918-1032 1.56e-08

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


Pssm-ID: 381132 [Multi-domain]  Cd Length: 114  Bit Score: 53.57  E-value: 1.56e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  918 VMVVDDDPNHRNLVSEILSPLGFVVHEANDALVCLSNTYLSAIDLFLLDISMPDMNGWQLLKKLRSNGISVPIIMVSA-- 995
Cdd:cd17616     1 VLLIEDDSATAQSIELMLKSEGFNVYTTDLGEEGLDLGKLYDYDIILLDLNLPDMSGYEVLRTLRLAKVKTPILILSGla 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 511672513  996 ---DATEAPYFNAaeeihepalhNDYLAKPMRDNALLEKV 1032
Cdd:cd17616    81 dieDKVKGLGFGA----------DDYMTKPFHKDELVARI 110
REC_OmpR_VirG cd17594
phosphoacceptor receiver (REC) domain of VirG-like OmpR family response regulators; VirG is ...
917-1034 1.73e-08

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: 53.60  E-value: 1.73e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  917 TVMVVDDDPNHRNLVSEILSPLGFVVHEAND----ALVCLSNTylsaIDLFLLDISMPDMNGWQLLKKLRSNGiSVPIIM 992
Cdd:cd17594     1 HVLVVDDDAAMRHLLILYLRERGFDVTAAADgaeeARLMLHRR----VDLVLLDLRLGQESGLDLLRTIRARS-DVPIII 75
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 511672513  993 VSADATEapyfnaaEEIHEPALH---NDYLAKPMRDNALLEKVAK 1034
Cdd:cd17594    76 ISGDRRD-------EIDRVVGLElgaDDYLAKPFGLRELLARVRA 113
HATPase_NtrY-like cd16944
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
784-890 2.94e-08

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: 52.92  E-value: 2.94e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  784 DETQLRQILINLLSNAVKFTQ-----QGSVTLDVyYRNQVAEF--TITDSGVGISEQDIERIFKPFerVEKRdipsSPGT 856
Cdd:cd16944     1 DTTQISQVLTNILKNAAEAIEgrpsdVGEVRIRV-EADQDGRIvlIVCDNGKGFPREMRHRATEPY--VTTR----PKGT 73
                          90       100       110
                  ....*....|....*....|....*....|....
gi 511672513  857 GLGLTITQLLTDIMGGNISVSSEIGKGSSFKLSI 890
Cdd:cd16944    74 GLGLAIVKKIMEEHGGRISLSNREAGGACIRIIL 107
REC_RocR cd17530
phosphoacceptor receiver (REC) domain of response regulator RocR; The response regulator RocR ...
917-995 3.48e-08

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


Pssm-ID: 381086 [Multi-domain]  Cd Length: 123  Bit Score: 52.83  E-value: 3.48e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  917 TVMVVDDDPNHRNLVSEILSPLGFV-VHEANDALVCLSNTYLSAIDLFLLDISMPDMNGWQLLKKLRSNGISVPIIMVSA 995
Cdd:cd17530     2 RVLVLDDDPFQCMMAATILEDLGPGnVDEADDGREALVILLCNAPDIIICDLKMPDMDGIEFLRHLAESHSNAAVILMSG 81
REC_OmpR_ChvI-like cd19936
phosphoacceptor receiver (REC) domain of ChvI-like OmpR family response regulators; ...
918-999 3.73e-08

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: 52.06  E-value: 3.73e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  918 VMVVDDDPNHRNLVSEILSPLGFVVHEANDALVCLSNTYLSAIDLFLLDISMPDMNGWQLLKKLRSNGiSVPIIMVSADA 997
Cdd:cd19936     1 IALVDDDRNILTSVSMALEAEGFSVETYTDGASALDGLNARPPDLAILDIKMPRMDGMELLQRLRQKS-TLPVIFLTSKD 79

                  ..
gi 511672513  998 TE 999
Cdd:cd19936    80 DE 81
PRK00742 PRK00742
chemotaxis-specific protein-glutamate methyltransferase CheB;
918-1037 6.57e-08

chemotaxis-specific protein-glutamate methyltransferase CheB;


Pssm-ID: 234828 [Multi-domain]  Cd Length: 354  Bit Score: 55.93  E-value: 6.57e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  918 VMVVDDDPNHRNLVSEILS--PLGFVVHEANDALVCLSNTYLSAIDLFLLDISMPDMNGWQLLKKL-RSNgiSVPIIMVS 994
Cdd:PRK00742    6 VLVVDDSAFMRRLISEILNsdPDIEVVGTAPDGLEAREKIKKLNPDVITLDVEMPVMDGLDALEKImRLR--PTPVVMVS 83
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 511672513  995 AdATEApyfNAAEEIHepALHN---DYLAKP-------MRDNA--LLEKVaKALA 1037
Cdd:PRK00742   84 S-LTER---GAEITLR--ALELgavDFVTKPflgislgMDEYKeeLAEKV-RAAA 131
REC_RcNtrC-like cd19928
phosphoacceptor receiver (REC) domain of Rhodobacter capsulatus nitrogen regulatory protein C ...
918-1022 9.16e-08

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


Pssm-ID: 381155 [Multi-domain]  Cd Length: 100  Bit Score: 50.97  E-value: 9.16e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  918 VMVVDDDPNHRNLVSEILSPLGFVVHEANDALVCLSNTYLSAIDLFLLDISMPDMNGWQLLKKLRSNGISVPIIMVSADA 997
Cdd:cd19928     1 ILVADDDRAIRTVLTQALGRAGYEVRTTGNAATLWRWVEEGEGDLVITDVVMPDENGLDLIPRIKKARPDLPIIVMSAQN 80
                          90       100
                  ....*....|....*....|....*
gi 511672513  998 TEAPYFNAAEeihepALHNDYLAKP 1022
Cdd:cd19928    81 TLMTAVKAAE-----RGAFEYLPKP 100
HATPase_Glnl-NtrB-like cd16918
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
788-890 1.12e-07

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: 51.25  E-value: 1.12e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  788 LRQILINLLSNAVKFT--QQGSVTLDVYYRNQV----------AEFTITDSGVGISEQDIERIFKPFerVEKRDipssPG 855
Cdd:cd16918     1 LIQVFLNLVRNAAQALagSGGEIILRTRTQRQVtlghprhrlaLRVSVIDNGPGIPPDLQDTIFYPM--VSGRE----NG 74
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 511672513  856 TGLGLTITQLLTDIMGGNISVSSEIGKgSSFKLSI 890
Cdd:cd16918    75 TGLGLAIAQNIVSQHGGVIECDSQPGH-TVFSVSL 108
REC_GlnL-like cd17565
phosphoacceptor receiver (REC) domain of transcriptional regulatory protein GlnL and similar ...
919-994 1.16e-07

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: 50.73  E-value: 1.16e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 511672513  919 MVVDDDPNHRNLVSEILSP--LGFVVHEANDALVCLSNTYLSAIDLFLLDISMPDMNGWQLLKKLRSNGISVPIIMVS 994
Cdd:cd17565     2 YIVDDDKNIIKILSDIIEDddLGEVVGEADNGAQAYDEILFLQPDIVLIDLLMPGMDGIQLVRKLKDTGSNGKFIMIS 79
REC_OmpR_RegX3-like cd17621
phosphoacceptor receiver (REC) domain of RegX3-like OmpR family response regulators; RegX3 is ...
918-999 1.22e-07

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: 50.66  E-value: 1.22e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  918 VMVVDDDPNHRNLVSEILSPLGFVVHEANDALVCLSNTYLSAIDLFLLDISMPDMNGWQLLKKLRSNGiSVPIIMVSADA 997
Cdd:cd17621     1 VLVVEDEESFSDPLAYLLRKEGFEVTVATDGPAALAEFDRAGADIVLLDLMLPGLSGTEVCRQLRARS-NVPVIMVTAKD 79

                  ..
gi 511672513  998 TE 999
Cdd:cd17621    80 SE 81
REC_TPR cd17589
phosphoacceptor receiver (REC) domain of uncharacterized tetratricopeptide repeat (TPR) ...
918-1032 2.16e-07

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


Pssm-ID: 381123 [Multi-domain]  Cd Length: 115  Bit Score: 50.34  E-value: 2.16e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  918 VMVVDDDPNHRNLVSEILSPLGF----VVHEANDAL-VCLSNTYlsaiDLFLLDISMPD-MNGWQLLKKLRSNGISVP-- 989
Cdd:cd17589     1 FLIVDDQPTFRSMLKSMLRSLGVtridTASSGEEALrMCENKTY----DIVLCDYNLGKgKNGQQLLEELRHKKLISPst 76
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 511672513  990 -IIMVSADATEAPYFNAAEeiHEPalhNDYLAKPMRDNALLEKV 1032
Cdd:cd17589    77 vFIMVTGESSRAMVLSALE--LEP---DDYLLKPFTVSELRERL 115
PRK11517 PRK11517
DNA-binding response regulator HprR;
918-1036 2.20e-07

DNA-binding response regulator HprR;


Pssm-ID: 183172 [Multi-domain]  Cd Length: 223  Bit Score: 52.98  E-value: 2.20e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  918 VMVVDDDPNHRNLVSEILSPLGFVVHEANDALVCLSNTYLSAIDLFLLDISMPDMNGWQLLKKLRSNGISVPIIMVSADA 997
Cdd:PRK11517    3 ILLIEDNQRTQEWVTQGLSEAGYVIDAVSDGRDGLYLALKDDYALIILDIMLPGMDGWQILQTLRTAKQTPVICLTARDS 82
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 511672513  998 TEapyfNAAEEIHEPAlhNDYLAKPMRDNALLEKVAKAL 1036
Cdd:PRK11517   83 VD----DRVRGLDSGA--NDYLVKPFSFSELLARVRAQL 115
REC_OmpR_BaeR-like cd19938
phosphoacceptor receiver (REC) domain of BaeR-like OmpR family response regulators; BaeR is ...
917-999 4.19e-07

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: 49.68  E-value: 4.19e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  917 TVMVVDDDPNHRNLVSEILSPLGFVVHEANDALVCLSNTYLSAIDLFLLDISMPDMNGWQLLKKLRSNGiSVPIIMVSAD 996
Cdd:cd19938     1 RILIVEDEPKLAQLLIDYLRAAGYAPTLLAHGDQVLPYVRHTPPDLILLDLMLPGTDGLTLCREIRRFS-DVPIIMVTAR 79

                  ...
gi 511672513  997 ATE 999
Cdd:cd19938    80 VEE 82
REC_LytTR_AlgR-like cd17532
phosphoacceptor receiver (REC) domain of LytTR/AlgR family response regulators similar to AlgR; ...
918-1035 4.52e-07

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


Pssm-ID: 381087 [Multi-domain]  Cd Length: 118  Bit Score: 49.46  E-value: 4.52e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  918 VMVVDDDPNHRNLVSEILSPLG--FVVHEANDALVCLSNTYLSAIDLFLLDISMPDMNGWQLLKKLRSNGISVPIIMVSA 995
Cdd:cd17532     1 ALIVDDEPLAREELRYLLEEHPdiEIVGEAENGEEALEAIEELKPDVVFLDIQMPGLDGLELAKKLSKLAKPPLIVFVTA 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 511672513  996 -D--ATEAPYFNAAeeihepalhnDYLAKPMRDNALLEKVAKA 1035
Cdd:cd17532    81 yDeyAVEAFELNAV----------DYLLKPFSEERLAEALAKL 113
Transp_cyt_pur pfam02133
Permease for cytosine/purines, uracil, thiamine, allantoin;
34-431 4.54e-07

Permease for cytosine/purines, uracil, thiamine, allantoin;


Pssm-ID: 251109  Cd Length: 439  Bit Score: 53.55  E-value: 4.54e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513    34 ARKWSVARVSNTALGA---ISFLALEAIGGALILNFGfnNSLIAILLVSAIIFFCGLPISYYAARYGVDIDLLTRgAGFG 110
Cdd:pfam02133    6 ERTWSTRNLFSFWLGAnfnINTWVIGALGVALGLNWW--QSVLAIIAGNLIGAIFVALLGRAGAKYGLPFPILSR-ASFG 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513   111 YIGSTITSLIYASFTFIFFAIEAAIMASALELLFNIPLS----------------IGYLISAIVVIPLVTHGITFISRFQ 174
Cdd:pfam02133   83 IRGSLLPSLLRAVIACGWFGIQAWIGSEALLLMLGKIFGhwlwigaipgtgltelVTFFIFWLVHLYIVWLGVSAIRVFF 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513   175 LWSQPIWLVLQLAPLIFILwhesSAINNWLQFEGKLESGNSGEFNLHLFGAASGILfSLMAQIGeqvDFLRFMPEAKKKH 254
Cdd:pfam02133  163 VIAAPLIPVAAFGFLIWAA----VKAGGGPVFDQPVSPGKSELFLSAVAGCAAGWA-TLIANAP---DFTRYAPTARSSS 234
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513   255 RACWwvallSAGPGWIIVGALKILLGSFLVVLAINAGVAedvagDPIQMYQVAfsymaqSPLLALSLAGIFVLVCQLKIN 334
Cdd:pfam02133  235 KIQL-----VAVPGGFTLFALIGILGAAAAYAAYGAPAW-----DPLDILARF------DPTAGVFLPAILVALAQLGTN 298
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513   335 VTNAY--AGSIAWSNFFSRLThshpgRVVWLVFNVIIALLIMELGIYAALEDI----LGIYSNVAVAWVGALVADLVINk 408
Cdd:pfam02133  299 ISANLysAGSDLAALLPKKIN-----RKRGSLIAAIIALVICPWKLLGNSAFMfttfLSLLSGFLSPVAGVIIADYFVV- 372
                          410       420
                   ....*....|....*....|...
gi 511672513   409 plgyspKHIEFKRAHLYDINPVG 431
Cdd:pfam02133  373 ------RRGYLHVAHLYTRRRGS 389
HATPase_CreC-like cd16945
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
788-876 5.31e-07

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: 49.00  E-value: 5.31e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  788 LRQILINLLSNAVKFTQQ-GSVTLDVYYRNQVAEFTITDSGVGISEQDIERIFKPFERVeKRDIPSSPGTGLGLTITQLL 866
Cdd:cd16945     5 LRQAINNLLDNAIDFSPEgGLIALQLEADTEGIELLVFDEGSGIPDYALNRVFERFYSL-PRPHSGQKSTGLGLAFVQEV 83
                          90
                  ....*....|
gi 511672513  867 TDIMGGNISV 876
Cdd:cd16945    84 AQLHGGRITL 93
REC_OmpR_MtrA-like cd17626
phosphoacceptor receiver (REC) domain of MtrA-like OmpR family response regulators; MtrA is ...
918-1032 5.60e-07

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: 49.39  E-value: 5.60e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  918 VMVVDDDPNHRNLVSEILSPLGFVVHEANDALVCLSNTYLSAIDLFLLDISMPDMNGWQLLKKLRSNGiSVPIIMVSADA 997
Cdd:cd17626     3 ILVVDDDAALAEMIGIVLRGEGFDPAFCGDGTQALAAFREVRPDLVLLDLMLPGIDGIEVCRQIRAES-GVPIVMLTAKS 81
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 511672513  998 TEAPYFNAAEeihepALHNDYLAKPMRDNALLEKV 1032
Cdd:cd17626    82 DTVDVVLGLE-----SGADDYVAKPFKPKELVARI 111
glnG PRK10923
nitrogen regulation protein NR(I); Provisional
918-1095 7.61e-07

nitrogen regulation protein NR(I); Provisional


Pssm-ID: 182842 [Multi-domain]  Cd Length: 469  Bit Score: 52.95  E-value: 7.61e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  918 VMVVDDDPNHRNLVSEILSPLGF---VVHEANDALVCLSNtylSAIDLFLLDISMPDMNGWQLLKKLRSNGISVPIIMVS 994
Cdd:PRK10923    6 VWVVDDDSSIRWVLERALAGAGLtctTFENGNEVLEALAS---KTPDVLLSDIRMPGMDGLALLKQIKQRHPMLPVIIMT 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  995 A----DATEAPYFNAAeeihepalhNDYLAKPMRDNALLEKVAKALAidwNYQNtstqsaspEPQALNIQLNQSQREQLQ 1070
Cdd:PRK10923   83 AhsdlDAAVSAYQQGA---------FDYLPKPFDIDEAVALVERAIS---HYQE--------QQQPRNIQVNGPTTDIIG 142
                         170       180
                  ....*....|....*....|....*
gi 511672513 1071 EIAEMaqlgfvQGIDRLIKNLEKDS 1095
Cdd:PRK10923  143 EAPAM------QDVFRIIGRLSRSS 161
REC_DC-like cd17534
phosphoacceptor receiver (REC) domain of modulated diguanylate cyclase and similar domains; ...
916-1036 8.65e-07

phosphoacceptor receiver (REC) domain of modulated diguanylate cyclase and similar domains; This groups includes a modulated diguanylate cyclase containing a PAS sensor domain from Desulfovibrio desulfuricans G20. Members of this group contain N-terminal REC domains and various output domains including the GGDEF, histidine kinase, and helix-turn-helix (HTH) DNA binding domains. Also included in this family is Mycobacterium tuberculosis PdtaR, a transcriptional antiterminator that contains a REC domain and an ANTAR RNA-binding output domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381089 [Multi-domain]  Cd Length: 117  Bit Score: 48.94  E-value: 8.65e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  916 KTVMVVDDDPNHRNLVSEILSPLGF----VVHEANDALVCLSNTylsAIDLFLLDISMP-DMNGWQLLKKLRSNgISVPI 990
Cdd:cd17534     1 KKILIVEDEAIIALDLKEILESLGYevvgIADSGEEAIELAEEN---KPDLILMDINLKgDMDGIEAAREIREK-FDIPV 76
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 511672513  991 IMVSADATEApYFNAAEEIhEPAlhnDYLAKPMRDNALLEKVAKAL 1036
Cdd:cd17534    77 IFLTAYSDEE-TLERAKET-NPY---GYLVKPFNERELKAAIELAL 117
pleD PRK09581
response regulator PleD; Reviewed
915-1032 1.13e-06

response regulator PleD; Reviewed


Pssm-ID: 236577 [Multi-domain]  Cd Length: 457  Bit Score: 52.60  E-value: 1.13e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  915 SKTVMVVDDDPNHRNLVSEILSPLGFVVHEAND---AL-VCLSntylSAIDLFLLDISMPDMNGWQLLKKLRSN--GISV 988
Cdd:PRK09581    2 TARILVVDDIPANVKLLEAKLLAEYYTVLTASSgaeAIaICER----EQPDIILLDVMMPGMDGFEVCRRLKSDpaTTHI 77
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 511672513  989 PIIMVSA-DATEapyfNAAEEIHEPAlhNDYLAKPMRDNALLEKV 1032
Cdd:PRK09581   78 PVVMVTAlDDPE----DRVRGLEAGA--DDFLTKPINDVALFARV 116
CitB COG2197
DNA-binding response regulator, NarL/FixJ family, contains REC and HTH domains [Signal ...
917-981 1.31e-06

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


Pssm-ID: 441799 [Multi-domain]  Cd Length: 131  Bit Score: 48.73  E-value: 1.31e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 511672513  917 TVMVVDDDPNHRNLVSEILS--PLGFVVHEANDALVCLSNTYLSAIDLFLLDISMPDMNGWQLLKKL 981
Cdd:COG2197     3 RVLIVDDHPLVREGLRALLEaePDIEVVGEAADGEEALELLEELRPDVVLLDIRMPGMDGLEALRRL 69
PutP COG0591
Na+/proline symporter [Amino acid transport and metabolism];
19-478 1.49e-06

Na+/proline symporter [Amino acid transport and metabolism];


Pssm-ID: 440356 [Multi-domain]  Cd Length: 476  Bit Score: 52.13  E-value: 1.49e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513   19 NQTLEDYALrfTSKNARKWSVArVSNTA--LGAISFLALeaigGALILNFGFNNSLIAILLVSAIIFFcGLPISYYAARY 96
Cdd:COG0591    27 TKSLEDYFL--AGRSLGWWVLA-LSLGAtwLSAWTFLGV----PGLAYAYGLSALWYALGYALGALLL-ALFFAPRLRRL 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513   97 GVD--IDLLtrGAGFGYIGSTITSLIYASFTFIFFAIEAAIMASALELLFNIPLSIGYLISAIVVIPLVTHG----ITFI 170
Cdd:COG0591    99 GALtiPEFL--EKRFGRGLRLLAAIIILLFLLGYLAAQLVALGKLLEALFGIPYWLGILIGALIVLLYTVLGglraVAWT 176
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  171 SRFQLwsqpIWLVLQLAPLIFILWHE---SSAINNWLQFEGKLESGNSGEFNLhLFGAASGILFSLMAQIGEQVDFLRFM 247
Cdd:COG0591   177 DVLQG----ILMLVGLILLLIVALSAlggFGELFAALPAPGLLSLFPGLGFTG-WLAFLGLFLAIGLGYFGQPHIVQRFL 251
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  248 -----PEAKKkhracwwvALLSAGPGWIIVGALKILLGSFLVVLainagVAEDVAGDPiqmyQVAFSYMAQS----PLLA 318
Cdd:COG0591   252 aakseKEARK--------AALIGGLLYLLFYLLAALIGLLARAL-----FPDLPLADP----DLALPLLILEllppGLAG 314
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  319 LSLAGIFVLV-----CQLkinvtNAYAGSIAWsNFFSRLTHSHP--------GRVVWLVFnVIIALLIMELGIYAALEDI 385
Cdd:COG0591   315 LLLAAILAAAmstadSQL-----LAASSVFTR-DIYKPFIKPKAsdkqllrvSRLAVLVV-GLLALLLALLFPSSILDLV 387
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  386 LGIYSNVAVAWVGALVADLVinkplgyspkhieFKRAHlydiNPVGVGSMVIASVLSIYCYTGNAGDTAQAL--APYIGL 463
Cdd:COG0591   388 LLAWGGLGAALLPPLLLGLF-------------WKRAT----KAGALAGMIAGLVVVLLWKLLGGPLGPFGWlyPILPGL 450
                         490
                  ....*....|....*
gi 511672513  464 STAFVCSPIIAILTK 478
Cdd:COG0591   451 LVSLLVFVVVSLLTK 465
psREC_PRR cd17582
pseudo receiver domain of pseudo-response regulators; In Arabidopsis, five pseudo-response ...
918-995 1.63e-06

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


Pssm-ID: 381120 [Multi-domain]  Cd Length: 104  Bit Score: 47.78  E-value: 1.63e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  918 VMVVDDDPNHRNLVSEILSPLGFVVHEANDALVCLS--NTYLSAIDLFLLDISMPDMNGWQLLKKLRSNGI--SVPIIMV 993
Cdd:cd17582     1 VLLVENDDSTRQIVTALLRKCSYEVTAASDGLQAWDvlEDEQNEIDLILTEVDLPVSSGFKLLSYIMRHKIckNIPVIMM 80

                  ..
gi 511672513  994 SA 995
Cdd:cd17582    81 SS 82
ComP COG4585
Signal transduction histidine kinase ComP [Signal transduction mechanisms];
600-890 1.64e-06

Signal transduction histidine kinase ComP [Signal transduction mechanisms];


Pssm-ID: 443642 [Multi-domain]  Cd Length: 252  Bit Score: 50.77  E-value: 1.64e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  600 VSATLSHVFFLLMIIVGVLVWLFVLANDSRQFALDESQRQTELLSREIS-------AHEVTDQALQQaketaesanqaks 672
Cdd:COG4585     2 LALALLGALALLVGALLGLLLALVLLRARRAERAAELERELAARAEEAReeerrriARELHDGVGQS------------- 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  673 ryLTGISHelrtplnsvlgYAQLLEKSPSLAPEHSAKvsLIKRSGEHLADIIEGLLDISRieagriELQRDEVAIGELLD 752
Cdd:COG4585    69 --LSAIKL-----------QLEAARRLLDADPEAARE--ELEEIRELAREALAELRRLVR------GLRPPALDDLGLAA 127
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  753 DLVDMFSLQAKSKGISFVYNPSPYLPNWVTADETQLRQILINLLSNAVKFTQQGSVTLDVYYRNQVAEFTITDSGVGIse 832
Cdd:COG4585   128 ALEELAERLLRAAGIRVELDVDGDPDRLPPEVELALYRIVQEALTNALKHAGATRVTVTLEVDDGELTLTVRDDGVGF-- 205
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 511672513  833 qdierifkpfervekrDIPSSPGTGLGLTITQLLTDIMGGNISVSSEIGKGSSFKLSI 890
Cdd:COG4585   206 ----------------DPEAAPGGGLGLRGMRERAEALGGTLTIGSAPGGGTRVRATL 247
REC_typeA_ARR cd17581
phosphoacceptor receiver (REC) domain of type A Arabidopsis response regulators (ARRs) and ...
918-1024 1.88e-06

phosphoacceptor receiver (REC) domain of type A Arabidopsis response regulators (ARRs) and similar proteins; Type-A response regulators of Arabidopsis (ARRs) are involved in cytokinin signaling, which involves a phosphorelay cascade by histidine kinase receptors (AHKs), histidine phosphotransfer proteins (AHPs) and downstream ARRs. Cytokinin is a plant hormone implicated in many growth and development processes including shoot organogenesis, leaf senescence, sink/source relationships, vascular development, lateral bud release, and photomorphogenic development. Type-A ARRs function downstream of and are regulated by type-B ARRs, which are a class of MYB-type transcription factors. As primary cytokinin response genes, type-A ARRs act as redundant negative feedback regulators of cytokinin signaling by inactivating the phosphorelay. ARRs are divided into two groups, type-A and -B, according to their sequence and domain structure. Type-A ARRs are similar in domain structure to CheY, in that they lack a typical output domain and only contain a stand-alone receiver (REC) domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381119 [Multi-domain]  Cd Length: 122  Bit Score: 48.13  E-value: 1.88e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  918 VMVVDDDPNHRNLVSEILSPLGF---VVHEANDALVCL--------SNTYLSAIDLFLLDISMPDMNGWQLLKKLR--SN 984
Cdd:cd17581     1 VLAVDDSLVDRKVIERLLRISSCrvtAVDSGKRALEFLgledeedsSNFNEPKVNMIITDYCMPGMTGYDLLKKVKesSA 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 511672513  985 GISVPIIMVSADateapyfNAAEEIH----EPAlhNDYLAKPMR 1024
Cdd:cd17581    81 LKEIPVVIMSSE-------NIPTRISrcleEGA--EDFLLKPVK 115
COG3920 COG3920
Two-component sensor histidine kinase, HisKA and HATPase domains [Signal transduction ...
743-896 2.10e-06

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


Pssm-ID: 443125 [Multi-domain]  Cd Length: 495  Bit Score: 51.83  E-value: 2.10e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  743 DEVAIGELLDDLVDMFSLQAKSKGISFVynpspylpnwVTADETQLRQ-------ILIN-LLSNAVKF----TQQGSVTL 810
Cdd:COG3920   357 EGVDLRDYLRELLEPLRDSYGGRGIRIE----------LDGPDVELPAdaavplgLILNeLVTNALKHaflsGEGGRIRV 426
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  811 DVYYRNQVAEFTITDSGVGISEqdierifkpfervekrDIPSSPGTGLGLTITQLLTDIMGGNISVSSEigKGSSFKLSI 890
Cdd:COG3920   427 SWRREDGRLRLTVSDNGVGLPE----------------DVDPPARKGLGLRLIRALVRQLGGTLELDRP--EGTRVRITF 488

                  ....*.
gi 511672513  891 MLASLN 896
Cdd:COG3920   489 PLAELA 494
PRK15479 PRK15479
transcriptional regulator TctD;
918-1036 2.99e-06

transcriptional regulator TctD;


Pssm-ID: 185376 [Multi-domain]  Cd Length: 221  Bit Score: 49.72  E-value: 2.99e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  918 VMVVDDDPNHRNLVSEILSPLGFVVHEANDALVCLSNTYLSAIDLFLLDISMPDMNGWQLLKKLRSNGISVPIIMVSADA 997
Cdd:PRK15479    3 LLLAEDNRELAHWLEKALVQNGFAVDCVFDGLAADHLLQSEMYALAVLDINMPGMDGLEVLQRLRKRGQTLPVLLLTARS 82
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 511672513  998 TEApyfNAAEEIHEPAlhNDYLAKPMrDNALLEKVAKAL 1036
Cdd:PRK15479   83 AVA---DRVKGLNVGA--DDYLPKPF-ELEELDARLRAL 115
REC_PdtaR-like cd19932
phosphoacceptor receiver (REC) domain of PdtaR and similar proteins; This subfamily includes ...
916-1037 3.06e-06

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


Pssm-ID: 381159 [Multi-domain]  Cd Length: 118  Bit Score: 47.41  E-value: 3.06e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  916 KTVMVVDDDPNHRNLVSEILSPLGF-VVHEANDALVCLSNTYLSAIDLFLLDISMPDMNGWQLLKKLRSNGIsVPIIMVS 994
Cdd:cd19932     1 VRVLIAEDEALIRMDLREMLEEAGYeVVGEASDGEEAVELAKKHKPDLVIMDVKMPRLDGIEAAKIITSENI-APIVLLT 79
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 511672513  995 ADAtEAPYFNAAEEIHEPAlhndYLAKPMRDNALLEKVAKALA 1037
Cdd:cd19932    80 AYS-QQDLVERAKEAGAMA----YLVKPFSESDLIPAIEMAIA 117
PRK10529 PRK10529
DNA-binding transcriptional activator KdpE; Provisional
917-1052 3.68e-06

DNA-binding transcriptional activator KdpE; Provisional


Pssm-ID: 182522 [Multi-domain]  Cd Length: 225  Bit Score: 49.42  E-value: 3.68e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  917 TVMVVDDDPNHRNLVSEILSPLGFVVHEANDALVCLSNTYLSAIDLFLLDISMPDMNGWQLLKKLRSNGiSVPIIMVSAD 996
Cdd:PRK10529    3 NVLIVEDEQAIRRFLRTALEGDGMRVFEAETLQRGLLEAATRKPDLIILDLGLPDGDGIEFIRDLRQWS-AIPVIVLSAR 81
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 511672513  997 ATEAPYFNAAEeihepALHNDYLAKPMRDNALLEKVAKALAidwnyQNTSTQSASP 1052
Cdd:PRK10529   82 SEESDKIAALD-----AGADDYLSKPFGIGELQARLRVALR-----RHSATPAPDP 127
PRK10766 PRK10766
two-component system response regulator TorR;
915-994 4.41e-06

two-component system response regulator TorR;


Pssm-ID: 182711 [Multi-domain]  Cd Length: 221  Bit Score: 48.88  E-value: 4.41e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  915 SKTVMVVDDDPNHRNLVSEILSPLGFVVHEANDALVCLSNTYLSAIDLFLLDISMPDMNGWQLLKKLRSNGiSVPIIMVS 994
Cdd:PRK10766    2 SYHILVVEDEPVTRARLQGYFEQEGYTVSEAASGAGMREIMQNQHVDLILLDINLPGEDGLMLTRELRSRS-TVGIILVT 80
REC_OmpR_BfmR-like cd19939
phosphoacceptor receiver (REC) domain of BfmR-like OmpR family response regulators; ...
918-1032 5.48e-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: 46.60  E-value: 5.48e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  918 VMVVDDDPNHRNLVSEILSPLGF---VVHEANDALVCLSNTylsAIDLFLLDISMPDMNGWQLLKKLRSNgISVPIIMVS 994
Cdd:cd19939     2 ILIVEDELELARLTRDYLIKAGLevsVFTDGQRAVRRIIDE---QPSLVVLDIMLPGMDGLTVCREVREH-SHVPILMLT 77
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 511672513  995 ADATEAPYFNAAEeihepALHNDYLAKPMRDNALLEKV 1032
Cdd:cd19939    78 ARTEEMDRVLGLE-----MGADDYLCKPFSPRELLARV 110
HATPase_Phy-like cd16932
Histidine kinase-like ATPase domain of plant phytochromes similar to Arabidopsis thaliana ...
784-892 5.82e-06

Histidine kinase-like ATPase domain of plant phytochromes similar to Arabidopsis thaliana Phytochrome A, B, C, D and E; This family includes the histidine kinase-like ATPase (HATPase) domains of plant red/far-red photoreceptors, the phytochromes, and includes the Arabidopsis thaliana phytochrome family phyA-phyE. Following red light absorption, biologically inactive forms of phytochromes convert to active forms, which rapidly convert back to inactive forms upon far-red light irradiation. Phytochromes can be considered as having an N-terminal photosensory region to which a bilin chromophore is bound, and a C-terminal output region, which includes the HATPase domain represented here, and is involved in dimerization and presumably contributes to relaying the light signal to downstream signaling events.


Pssm-ID: 340409 [Multi-domain]  Cd Length: 113  Bit Score: 46.50  E-value: 5.82e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  784 DETQLRQILINLLSNAVKFTQ--QGSVTLDVYYR-NQVA--------EFTITDSGVGISEQDIERIFKPfervekrdips 852
Cdd:cd16932     3 DQIRLQQVLADFLLNAVRFTPspGGWVEIKVSPTkKQIGdgvhvihlEFRITHPGQGLPEELVQEMFEE----------- 71
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 511672513  853 SPGT---GLGLTITQLLTDIMGGNISVSSEIGKgSSFKLSIML 892
Cdd:cd16932    72 NQWTtqeGLGLSISRKLVKLMNGDVRYLREAGR-SYFLITLEL 113
REC_NtrC cd19919
phosphoacceptor receiver (REC) domain of DNA-binding transcriptional regulator NtrC; ...
916-1036 8.01e-06

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


Pssm-ID: 381146 [Multi-domain]  Cd Length: 116  Bit Score: 46.11  E-value: 8.01e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  916 KTVMVVDDDPNHRNLVSEILSPLGFVVH---EANDALVCLSNtylSAIDLFLLDISMPDMNGWQLLKKLRSNGISVPIIM 992
Cdd:cd19919     1 KTVWIVDDDSSIRWVLERALAGAGLTVTsfeNAQEALAALAS---SQPDVLISDIRMPGMDGLALLAQIKQRHPDLPVII 77
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 511672513  993 VSA----DATEAPYFNAAEEihepalhndYLAKPMRDNALLEKVAKAL 1036
Cdd:cd19919    78 MTAhsdlDSAVSAYQGGAFE---------YLPKPFDIDEAVALVERAI 116
PRK10643 PRK10643
two-component system response regulator PmrA;
953-1067 1.12e-05

two-component system response regulator PmrA;


Pssm-ID: 182612 [Multi-domain]  Cd Length: 222  Bit Score: 47.72  E-value: 1.12e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  953 SNTYlsaiDLFLLDISMPDMNGWQLLKKLRSNGISVPIIMVSA-DATEapyfnaaEEIHE-PALHNDYLAKPMrdnALLE 1030
Cdd:PRK10643   42 SGHY----SLVVLDLGLPDEDGLHLLRRWRQKKYTLPVLILTArDTLE-------DRVAGlDVGADDYLVKPF---ALEE 107
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 511672513 1031 KVAKALAIDWNYQNTSTQsaspEPQALNIQLNQSQRE 1067
Cdd:PRK10643  108 LHARIRALIRRHQGQGEN----ELQVGNLTLNLGRQQ 140
REC_OmpR_kpRstA-like cd17622
phosphoacceptor receiver (REC) domain of kpRstA-like OmpR family response regulators; ...
918-1029 2.20e-05

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: 44.68  E-value: 2.20e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  918 VMVVDDDPNHRNLVSEILSPLGF---VVHEANDALVCLSNtylSAIDLFLLDISMPDMNGWQLLKKLRSNgISVPIIMVS 994
Cdd:cd17622     3 ILLVEDDPKLARLIADFLESHGFnvvVEHRGDRALEVIAR---EKPDAVLLDIMLPGIDGLTLCRDLRPK-YQGPILLLT 78
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 511672513  995 AdateapyfNAAEEIHEPALH---NDYLAKPMRDNALL 1029
Cdd:cd17622    79 A--------LDSDIDHILGLElgaDDYVVKPVEPAVLL 108
REC_RegA-like cd17563
phosphoacceptor receiver (REC) domain of photosynthetic apparatus regulatory protein RegA; ...
916-1022 2.45e-05

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: 44.36  E-value: 2.45e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  916 KTVMVVDDDPNHRNLVSEILSPLGFVVHEANDA----LVCLSNTYlsaiDLFLLDISMPDMNGWQLLKKLRSNGISVPII 991
Cdd:cd17563     1 KSLLLVDDDEVFAERLARALERRGFEVETAHSVeealALAREEKP----DYAVLDLRLGGDSGLDLIPPLRALQPDARIV 76
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 511672513  992 MVS-----ADATEAPYFNAAeeihepalhnDYLAKP 1022
Cdd:cd17563    77 VLTgyasiATAVEAIKLGAD----------DYLAKP 102
PRK10403 PRK10403
nitrate/nitrite response regulator protein NarP;
918-1037 2.86e-05

nitrate/nitrite response regulator protein NarP;


Pssm-ID: 182431 [Multi-domain]  Cd Length: 215  Bit Score: 46.38  E-value: 2.86e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  918 VMVVDDDPNHRNLVSEILS--PLGFVVHEANDALVCLSNTYLSAIDLFLLDISMPDMNGWQLLKKLRSNGISVPIIMVSA 995
Cdd:PRK10403    9 VLIVDDHPLMRRGVRQLLEldPGFEVVAEAGDGASAIDLANRLDPDVILLDLNMKGMSGLDTLNALRRDGVTAQIIILTV 88
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 511672513  996 DateapyfNAAEEIHE--PALHNDYLAKPMRDNALLEKVAKALA 1037
Cdd:PRK10403   89 S-------DASSDVFAliDAGADGYLLKDSDPEVLLEAIRAGAK 125
REC_Spo0F-like cd17553
phosphoacceptor receiver (REC) domain of Spo0F and similar domains; Spo0F, a stand-alone ...
916-995 4.05e-05

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: 44.08  E-value: 4.05e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  916 KTVMVVDDDPNHRNLVSEILSPLGFVVHEANDALVCLSNTYLSAIDLFLLDISMPDMNGWQLLKKLRSNGISVPIIMVSA 995
Cdd:cd17553     1 EKILIVDDQYGIRILLNEVFNKEGYQTFQAANGLQALDIVTKERPDLVLLDMKIPGMDGIEILKRMKVIDENIRVIIMTA 80
REC_OmpR_NsrR-like cd18159
phosphoacceptor receiver (REC) domain of Streptococcus agalactiae NsrR-like OmpR family ...
918-1036 4.06e-05

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: 43.81  E-value: 4.06e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  918 VMVVDDDPNHRNLVSEILSPLGFVVHEANDALVCLSNTYLSAIDLFLLDISMPDMNGWQLLKKLRSngIS-VPIIMVSAD 996
Cdd:cd18159     1 ILIVEDDETIASLLKKHLEKWGYEVVLIEDFEDVLEEFLQFKPDLVLLDINLPYFDGFYWCREIRQ--ISnVPIIFISSR 78
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 511672513  997 ATEapyfnaAEEIHepALHN---DYLAKPMRDNALLEKVAKAL 1036
Cdd:cd18159    79 DDN------MDQVM--AINMggdDYITKPFDLDVLLAKIKAIL 113
PRK11083 PRK11083
DNA-binding response regulator CreB; Provisional
917-995 7.17e-05

DNA-binding response regulator CreB; Provisional


Pssm-ID: 236838 [Multi-domain]  Cd Length: 228  Bit Score: 45.34  E-value: 7.17e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  917 TVMVVDDDPNHRNLVSEILSPLGFVVHE---ANDALVCLSNTylsAIDLFLLDISMPDMNGWQLLKKLRSNGISVPIIMV 993
Cdd:PRK11083    5 TILLVEDEQAIADTLVYALQSEGFTVEWferGLPALDKLRQQ---PPDLVILDVGLPDISGFELCRQLLAFHPALPVIFL 81

                  ..
gi 511672513  994 SA 995
Cdd:PRK11083   82 TA 83
PRK10336 PRK10336
two-component system response regulator QseB;
918-1038 1.60e-04

two-component system response regulator QseB;


Pssm-ID: 182387 [Multi-domain]  Cd Length: 219  Bit Score: 44.50  E-value: 1.60e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  918 VMVVDDDPNHRNLVSEILSPLGFVVHEANDALVCLSNTYLSAIDLFLLDISMPDMNGWQLLKKLRSNGISVPIIMVSA-D 996
Cdd:PRK10336    3 ILLIEDDMLIGDGIKTGLSKMGFSVDWFTQGRQGKEALYSAPYDAVILDLTLPGMDGRDILREWREKGQREPVLILTArD 82
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 511672513  997 ATeapyfnaAEEIHEPAL-HNDYLAKPMrdnALLEKVAKALAI 1038
Cdd:PRK10336   83 AL-------AERVEGLRLgADDYLCKPF---ALIEVAARLEAL 115
PRK15115 PRK15115
response regulator GlrR; Provisional
915-1037 1.72e-04

response regulator GlrR; Provisional


Pssm-ID: 185070 [Multi-domain]  Cd Length: 444  Bit Score: 45.60  E-value: 1.72e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  915 SKTVMVVDDDPNHRNLVSEILSPLGFVVHEAN---DALVCLSNtylSAIDLFLLDISMPDMNGWQLLKKLRSNGISVPII 991
Cdd:PRK15115    5 PAHLLLVDDDPGLLKLLGMRLTSEGYSVVTAEsgqEALRVLNR---EKVDLVISDLRMDEMDGMQLFAEIQKVQPGMPVI 81
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 511672513  992 MVSAD--------ATEAPYFNaaeeihepalhndYLAKPMRDNALLEKVAKALA 1037
Cdd:PRK15115   82 ILTAHgsipdavaATQQGVFS-------------FLTKPVDRDALYKAIDDALE 122
PRK10710 PRK10710
DNA-binding transcriptional regulator BaeR; Provisional
917-1091 1.95e-04

DNA-binding transcriptional regulator BaeR; Provisional


Pssm-ID: 182665 [Multi-domain]  Cd Length: 240  Bit Score: 44.29  E-value: 1.95e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  917 TVMVVDDDPNHRNLVSEILSPLGFVVHEANDALVCLSNTYLSAIDLFLLDISMPDMNGWQLLKKLR--SNgisVPIIMVS 994
Cdd:PRK10710   12 RILIVEDEPKLGQLLIDYLQAASYATTLLSHGDEVLPYVRQTPPDLILLDLMLPGTDGLTLCREIRrfSD---IPIVMVT 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  995 AdateapyfnAAEEIHE-PALH---NDYLAKPMRDNallEKVAKALAIDWNYQNTSTQSASPEPQALNIQLNQSQREQLQ 1070
Cdd:PRK10710   89 A---------KIEEIDRlLGLEigaDDYICKPYSPR---EVVARVKTILRRCKPQRELQQQDAESPLIIDESRFQASWRG 156
                         170       180
                  ....*....|....*....|.
gi 511672513 1071 EIAEMAQLGFvqgidRLIKNL 1091
Cdd:PRK10710  157 KMLDLTPAEF-----RLLKTL 172
PRK10430 PRK10430
two-component system response regulator DcuR;
918-1022 2.47e-04

two-component system response regulator DcuR;


Pssm-ID: 182454 [Multi-domain]  Cd Length: 239  Bit Score: 43.94  E-value: 2.47e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  918 VMVVDDDPN----HRNLVSEILsplGF----VVHEANDALVCLSNTYLsAIDLFLLDISMPDMNGWQLLKKLRSNGISVP 989
Cdd:PRK10430    4 VLIVDDDAMvaelNRRYVAQIP---GFqccgTASTLEQAKEIIFNSDT-PIDLILLDIYMQQENGLDLLPVLHEAGCKSD 79
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 511672513  990 IIMVS--ADATEApyfnaaeeihEPALHN---DYLAKP 1022
Cdd:PRK10430   80 VIVISsaADAATI----------KDSLHYgvvDYLIKP 107
YesM COG2972
Sensor histidine kinase YesM [Signal transduction mechanisms];
795-890 2.72e-04

Sensor histidine kinase YesM [Signal transduction mechanisms];


Pssm-ID: 442211 [Multi-domain]  Cd Length: 445  Bit Score: 44.62  E-value: 2.72e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  795 LLSNAVKF-----TQQGSVTLDVYYRNQVAEFTITDSGVGISEQDIERIFKPFERVEKrdipsspGTGLGL-TITQLLTD 868
Cdd:COG2972   344 LVENAIEHgiepkEGGGTIRISIRKEGDRLVITVEDNGVGMPEEKLEKLLEELSSKGE-------GRGIGLrNVRERLKL 416
                          90       100
                  ....*....|....*....|....
gi 511672513  869 IMGGN--ISVSSEIGKGSSFKLSI 890
Cdd:COG2972   417 YYGEEygLEIESEPGEGTTVTIRI 440
REC_HP-RR-like cd17573
phosphoacceptor receiver (REC) domain of orphan response regulator HP-RR and similar proteins; ...
918-1032 3.01e-04

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


Pssm-ID: 381115 [Multi-domain]  Cd Length: 110  Bit Score: 41.26  E-value: 3.01e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  918 VMVVDDDPNHRNLVSEILSPLGF---VVHEANDAlvclsnTYLSAI---DLFLLDISMPDMNGWQLLKKLRSNGISVPII 991
Cdd:cd17573     1 ILLIEDDSTLGKEISKGLNEKGYqadVAESLKDG------EYYIDIrnyDLVLVSDKLPDGNGLSIVSRIKEKHPSIVVI 74
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 511672513  992 MVSA-DATEapyfnaAEEIHEPALHNDYLAKPMRDNALLEKV 1032
Cdd:cd17573    75 VLSDnPKTE------QEIEAFKEGADDYIAKPFDFKVLVARI 110
REC_PilR cd19926
phosphoacceptor receiver (REC) domain of type 4 fimbriae expression regulatory protein PilR ...
918-1022 3.39e-04

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


Pssm-ID: 381153 [Multi-domain]  Cd Length: 100  Bit Score: 40.98  E-value: 3.39e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  918 VMVVDDDPNHRNLVSEILSPLGFVVHEANDALVCLSNTYLSAIDLFLLDISMPDMNGWQLLKKLRSNGISVPIIMVSADA 997
Cdd:cd19926     1 VLVVDDEPDIRELLEITLGRMGLDVRSARNVKEARELLASEPYDLCLTDMRLPDGSGLELVQHIQQRLPQTPVAVITAYG 80
                          90       100
                  ....*....|....*....|....*
gi 511672513  998 TEApyfNAAEEIHEPALhnDYLAKP 1022
Cdd:cd19926    81 SLD---TAIEALKAGAF--DFLTKP 100
REC_Spo0A cd17561
phosphoacceptor receiver (REC) domain of Spo0A; Spo0A is a response regulator of the ...
918-995 3.74e-04

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


Pssm-ID: 381109 [Multi-domain]  Cd Length: 108  Bit Score: 41.05  E-value: 3.74e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  918 VMVVDDDPNHRNLVSEILS--PLGFVVHEANDALVCLSNTYLSAIDLFLLDISMPDMNGWQLLKKLRS-NGISVP-IIMV 993
Cdd:cd17561     4 VLIADDNREFVQLLEEYLNsqPDMEVVGVAHNGQEALELIEEKEPDVLLLDIIMPHLDGIGVLEKLRRmRLEKRPkIIML 83

                  ..
gi 511672513  994 SA 995
Cdd:cd17561    84 TA 85
HATPase_UhpB-NarQ-NarX-like cd16917
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
796-892 5.80e-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: 39.84  E-value: 5.80e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  796 LSNAVKFTQQGSVTLDVYYRNQVAEFTITDSGVGIseqdierifkpfervekRDIPSSPGTGLGLTITQLLTDIMGGNIS 875
Cdd:cd16917     9 LTNALKHAGASRVRVTLSYTADELTLTVVDDGVGF-----------------DGPAPPGGGGFGLLGMRERAELLGGTLT 71
                          90
                  ....*....|....*..
gi 511672513  876 VSSEIGKGssFKLSIML 892
Cdd:cd16917    72 IGSRPGGG--TRVTARL 86
REC_hyHK cd17598
phosphoacceptor receiver (REC) domain of uncharacterized hybrid sensor histidine kinase ...
918-995 6.34e-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: 40.77  E-value: 6.34e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  918 VMVVDDDPNHRNLVSEILSPLGFVVHEANDALVCLSNTYLSAIDLFLLDISMPDMNGWQLLKKLRSNG--ISVPIIMVSA 995
Cdd:cd17598     1 ILIVEDSPTQAEQLKHILEEQGYKVQVARNGREALAMLAEHRPTLVISDIVMPEMDGYELCRKIKSDPdlKDIPVILLTT 80
SLC5sbd cd10322
Solute carrier 5 family, sodium/glucose transporters and related proteins; solute-binding ...
25-473 6.95e-04

Solute carrier 5 family, sodium/glucose transporters and related proteins; solute-binding domain; This family represents the solute-binding domain of SLC5 proteins (also called the sodium/glucose cotransporter family or solute sodium symporter family) that co-transport Na+ with sugars, amino acids, inorganic ions or vitamins. Family members include: the human glucose (SGLT1, 2, 4, 5), chiro-inositol (SGLT5), myo-inositol (SMIT), choline (CHT), iodide (NIS), multivitamin (SMVT), and monocarboxylate (SMCT) cotransporters, as well as Vibrio parahaemolyticus glucose/galactose (vSGLT), and Escherichia coli proline (PutP) and pantothenate (PutF) cotransporters. Vibrio parahaemolyticus Na(+)/galactose cotransporter (vSGLT) has 13 transmembrane helices (TMs): TM-1, an inverted topology repeat: TMs1-5 and TMs6-10, and TMs 11-12 (TMs numbered to conform to the solute carrier 6 family Aquifex aeolicus LeuT). One member of this family, human SGLT3, has been characterized as a glucose sensor and not a transporter. Members of this family are important in human physiology and disease.


Pssm-ID: 271357 [Multi-domain]  Cd Length: 454  Bit Score: 43.31  E-value: 6.95e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513   25 YALRFTSKNARKWSVA-RVSNTALGAISFLAlEAIGGALILN---FGFNN---SLIAILLVSAIIFFCGLPISYYAARYG 97
Cdd:cd10322    18 LYASKKVKSSEDFFLAgRSLGPWLLAGTLAA-TWISAGSFVGvagLAYTYglsAIWYILGAALGALLLALFLAPRLRRLG 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513   98 VDIDLLT-RGAGFGYIGSTITSLIYASFTFIFFAIEAAIMASALELLFNIPLSIGYLISAIVVIPLVT----HGITFISR 172
Cdd:cd10322    97 KTTIPETiLERYYSKGLRLLVAIIIIIALIPYLALQLIGGGYILSTLLGIPYTVAVIIAAVIVILYTVfggmRAVAWTDV 176
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  173 FQLWsqpIWLVLQLAPLIFILWH----ESSAINNWLQFEGKLESGNSGefnLHLFGAASGILFSLMAQIGEQVDFLRFMP 248
Cdd:cd10322   177 IQGI---VMLIGVLVAAIFILSKvgggGFSALAAALPALLLALGPGGG---LGWSTILSLILLTGLGVLALPQVFQRILA 250
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  249 eAKKKHRACWwvALLSAGPGWIIVGALKILLGsfLVVLAINAGVAedvagDPIQMYQVAFSYMAQSPLLALSLAGIFVLV 328
Cdd:cd10322   251 -AKDEKTARR--AFLLAGLLLLLIGFLVALIG--LAARALFPDLE-----NPDLALPTLINSLLPPGLAGLVLAGLLAAA 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  329 cqlkINVTNAY--AGSIAWSN-FFSRLTHSHPGRVVWLVFNVIIALLIMELGIYAAL--EDILGIYSNVAVAWVGALVAD 403
Cdd:cd10322   321 ----MSTADSLllAASTLFTRdIYKPLINPKASDKKLLRVSRIAVVVVGVLALLLALlpPSILLLLSLAAGLLAAALFPP 396
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 511672513  404 LVinkpLGYSpkhieFKRAhlydiNPVG-VGSMVIASVLSIYCYTGNAGDTAQALAPYIGLSTAFVCSPII 473
Cdd:cd10322   397 LL----GGLF-----WKRA-----TKAGaIAGIIVGLIVTLVWLLLPLASPLGIDPIIPALLVSLIVFVVV 453
PRK10815 PRK10815
two-component system sensor histidine kinase PhoQ;
585-878 9.13e-04

two-component system sensor histidine kinase PhoQ;


Pssm-ID: 182754 [Multi-domain]  Cd Length: 485  Bit Score: 43.08  E-value: 9.13e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  585 VYSRIPVtEFATKAAVSATLSHVFFLLMIIVGVLVWLfvlandsrqfALDESQRQTELLSREISAHEVTDQALQQAKETA 664
Cdd:PRK10815  175 VVDTIPQ-ELQRSYMVWSWFSYVLLANLLLVIPLLWL----------AAWWSLRPIEALAKQVRELEEGEREQLDPNPPR 243
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  665 E-------------SANQAKSRY---LTGISHELRTPLnSVLgyaqllekspslapeHSAKVSLikRSGEHLAdiIEG-- 726
Cdd:PRK10815  244 EltslvrnlnrllkNERERYTKYrttLTDLTHSLKTPL-AVL---------------QSTLRSL--RSGKQMS--VEQae 303
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  727 ---LLDISRI-------------EAGRIELQRDEVAIGELLDDLVDMFSLQAKSKGISFVYNPSPYLpNWVtADETQLRQ 790
Cdd:PRK10815  304 pimLEQISRIsqqigyylhrasmRSEHNLLSRELHSVAPLLDNLTSALNKVYQRKGVNITLDISPEI-TFV-GEKNDFME 381
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  791 ILINLLSNAVKFTQQgSVTLDVYYRNQVAEFTITDSGVGISEQDIERIFKPFERVEK-RdipssPGTGLGLTITQLLTDI 869
Cdd:PRK10815  382 VMGNVLDNACKYCLE-FVEISARQTDEHLHIVVEDDGPGIPESKRELIFDRGQRADTlR-----PGQGLGLSVAREITEQ 455

                  ....*....
gi 511672513  870 MGGNISVSS 878
Cdd:PRK10815  456 YEGKISAGD 464
PRK09958 PRK09958
acid-sensing system DNA-binding response regulator EvgA;
917-995 1.44e-03

acid-sensing system DNA-binding response regulator EvgA;


Pssm-ID: 182168 [Multi-domain]  Cd Length: 204  Bit Score: 41.42  E-value: 1.44e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  917 TVMVVDDDPNHRNLVSEILSPLGF-VVHEANDALVCLSNTYLSAIDLFLLDISMPDMNGWQLLKKLRSNGISVPIIMVSA 995
Cdd:PRK09958    2 NAIIIDDHPLAIAAIRNLLIKNDIeILAELTEGGSAVQRVETLKPDIVIIDVDIPGVNGIQVLETLRKRQYSGIIIIVSA 81
HATPase_BvrS-ChvG-like cd16953
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
788-874 1.74e-03

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: 39.09  E-value: 1.74e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  788 LRQILINLLSNAVKFT--QQGSVTLDVYYRNQVAEFTITDSGVGISEQDIERIFKPFERVEKRDIPSSPGTGLGLTITQL 865
Cdd:cd16953     1 LGQVLRNLIGNAISFSppDTGRITVSAMPTGKMVTISVEDEGPGIPQEKLESIFDRFYTERPANEAFGQHSGLGLSISRQ 80

                  ....*....
gi 511672513  866 LTDIMGGNI 874
Cdd:cd16953    81 IIEAHGGIS 89
RsbW COG2172
Anti-sigma regulatory factor (Ser/Thr protein kinase) [Signal transduction mechanisms];
795-868 2.85e-03

Anti-sigma regulatory factor (Ser/Thr protein kinase) [Signal transduction mechanisms];


Pssm-ID: 441775 [Multi-domain]  Cd Length: 127  Bit Score: 39.13  E-value: 2.85e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 511672513  795 LLSNAVKFTQQ----GSVTLDVYYRNQVAEFTITDSGVGISEQDIERifkpfervekrDIPSSPGTGLGLTITQLLTD 868
Cdd:COG2172    42 AVTNAVRHAYGgdpdGPVEVELELDPDGLEIEVRDEGPGFDPEDLPD-----------PYSTLAEGGRGLFLIRRLMD 108
PRK11173 PRK11173
two-component response regulator; Provisional
918-985 3.98e-03

two-component response regulator; Provisional


Pssm-ID: 183013 [Multi-domain]  Cd Length: 237  Bit Score: 40.38  E-value: 3.98e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 511672513  918 VMVVDDDPNHRNLVSEILSPLGFVVHEANDAL---VCLSNtylSAIDLFLLDISMPDMNGWQLLKKLRSNG 985
Cdd:PRK11173    6 ILIVEDELVTRNTLKSIFEAEGYDVFEATDGAemhQILSE---NDINLVIMDINLPGKNGLLLARELREQA 73
REC_HupR cd17596
phosphoacceptor receiver (REC) domain of hydrogen uptake protein regulator (HupR); Members of ...
917-1036 6.40e-03

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


Pssm-ID: 381127 [Multi-domain]  Cd Length: 133  Bit Score: 38.12  E-value: 6.40e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511672513  917 TVMVVDDDPNHRNLVSEILSPlGFVVHEA---NDALVCLSNTYLSAIdlfLLDISMPDMNGWQLLKKLRSNGISVPIIMV 993
Cdd:cd17596     2 TILVVDDEVRSLEALRRTLEE-DFDVLTAasaEEALAILEEEWVQVI---LCDQRMPGTTGVEFLKEVRERWPEVVRIII 77
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 511672513  994 SAdATEAPYFNAAeeIHEPALHNdYLAKPMRDNALLEKVAKAL 1036
Cdd:cd17596    78 SG-YTDSEDIIAG--INEAGIYQ-YLTKPWHPDQLLLTVRNAA 116
 
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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