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Conserved domains on  [gi|503229768|ref|WP_013464429|]
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MULTISPECIES: response regulator [unclassified Pseudoalteromonas]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PRK11107 super family cl35992
hybrid sensory histidine kinase BarA; Provisional
559-1094 3.45e-112

hybrid sensory histidine kinase BarA; Provisional


The actual alignment was detected with superfamily member PRK11107:

Pssm-ID: 236848 [Multi-domain]  Cd Length: 919  Bit Score: 370.72  E-value: 3.45e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  559 AKAAAEQANIAKSEFLAAMSHEIRTPMNGVLGMLNLILDSSLNEKQHHQVSIALNSANSLLNIINDILDFSKVDAGKLEL 638
Cdd:PRK11107  282 AKKRAQEAARIKSEFLANMSHELRTPLNGVIGFTRQTLKTPLTPTQRDYLQTIERSANNLLAIINDILDFSKLEAGKLVL 361
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  639 EELEFNLCNMLDDFIETIAIHAHSKNIPLMLDIEHLEYAFVIGDAGRLKQILTNLVNNALKFTHKGEVQVIAKLTPINNN 718
Cdd:PRK11107  362 ENIPFSLRETLDEVVTLLAHSAHEKGLELTLNIDPDVPDNVIGDPLRLQQIITNLVGNAIKFTESGNIDILVELRALSNT 441
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  719 QMRFNCQVIDSGIGISAAQQAKLFKSFSQVDSSTTRKYGGTGLGLAIVKKLCHLMEGDIQVQSKENKGSNFSFNVVLKRS 798
Cdd:PRK11107  442 KVQLEVQIRDTGIGISERQQSQLFQAFRQADASISRRHGGTGLGLVITQKLVNEMGGDISFHSQPNRGSTFWFHLPLDLN 521
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  799 KNPqkVLPPVDMSSL---NILIVCSNQTQSSILHKQFTKWGATAVISPSAKQAVQIcqqyiekqnlCFDLIMIDMQLSDG 875
Cdd:PRK11107  522 PNP--IIDGLPTDCLagkRLLYVEPNSAAAQATLDILSETPLEVTYSPTLSQLPEA----------HYDILLLGLPVTFR 589
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  876 DALTLSKTLDKEVDLMAAHVVLMttgeLNKQRDLYQAS--RFSAIV--TKPIITQNLFKMLStcfSDKQHSNSSLITEDL 951
Cdd:PRK11107  590 EPLTMLHERLAKAKSMTDFLILA----LPCHEQVLAEQlkQDGADAclSKPLSHTRLLPALL---EPCHHKQPPLLPPTD 662
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  952 SDTQPLSsddivwdknirILLVEDNNINqivasttLKKIG------INSIDIAENGQHALEYLKQttshNPYSLILMDCQ 1025
Cdd:PRK11107  663 ESRLPLT-----------VMAVDDNPAN-------LKLIGalleeqVEHVVLCDSGHQAVEQAKQ----RPFDLILMDIQ 720
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 503229768 1026 MPVMDGYQATTHIRVNEAGSKNPpitIIAMTANAMVGDKAKCLQVGMNDYISKPIAQDILFKKLLKWLP 1094
Cdd:PRK11107  721 MPGMDGIRACELIRQLPHNQNTP---IIAVTAHAMAGERERLLSAGMDDYLAKPIDEAMLKQVLLRYKP 786
KinE super family cl47428
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome ...
291-791 1.12e-65

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


The actual alignment was detected with superfamily member COG5809:

Pssm-ID: 444511 [Multi-domain]  Cd Length: 489  Bit Score: 230.25  E-value: 1.12e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  291 EAIKQSEARYELAVKGSNDGIWDWDIVTNEVYFSPRISVLLGYDENDknalpHCADALYKLLHPDDITKHKKQIANHLIS 370
Cdd:COG5809     8 LQLRKSEQRFRSLFENAPDAILILDLEGKILKVNPAAERIFGYTEDE-----LLGTNILDFLHPDDEKELREILKLLKEG 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  371 NIPFNYDYRLKTKSGAYRYFTVKGMALRNEHNKAIRMAGSVTDITEQKRSQKALKQAKEQNDLLAQAIEScnvGISIADA 450
Cdd:COG5809    83 ESRDELEFELRHKNGKRLEFSSKLSPIFDQNGDIEGMLAISRDITERKRMEEALRESEEKFRLIFNHSPD---GIIVTDL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  451 SVQgfpLVFLNSEFEKITGYSKEEMLGINCSLLQGPNTDKNAIDIITNAIKTLKTQRIEILNYKKDGTEFWNSLQISPVF 530
Cdd:COG5809   160 DGR---IIYANPAACKLLGISIEELIGKSILELIHSDDQENVAAFISQLLKDGGIAQGEVRFWTKDGRWRLLEASGAPIK 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  531 -NEQQQltAYVGIQQDITEQKAanqlLIEAKAAAEQANIAkSEFLAAMSHEIRTPMNGVLGMLNLILDSSLNEKQHHqVS 609
Cdd:COG5809   237 kNGEVD--GIVIIFRDITERKK----LEELLRKSEKLSVV-GELAAGIAHEIRNPLTSLKGFIQLLKDTIDEEQKTY-LD 308
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  610 IALNSANSLLNIINDILDFSKVDAGKLELeeleFNLCNMLDDFIETIAIHAHSKNIPLMLDIEHLEYaFVIGDAGRLKQI 689
Cdd:COG5809   309 IMLSELDRIESIISEFLVLAKPQAIKYEP----KDLNTLIEEVIPLLQPQALLKNVQIELELEDDIP-DILGDENQLKQV 383
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  690 LTNLVNNALKFTHK-GEVQViaKLTPINNNQMRFncQVIDSGIGISAAQQAKLFKSFSqvdsstTRKYGGTGLGLAIVKK 768
Cdd:COG5809   384 FINLLKNAIEAMPEgGNITI--ETKAEDDDKVVI--SVTDEGCGIPEERLKKLGEPFY------TTKEKGTGLGLMVSYK 453
                         490       500
                  ....*....|....*....|...
gi 503229768  769 LCHLMEGDIQVQSKENKGSNFSF 791
Cdd:COG5809   454 IIEEHGGKITVESEVGKGTTFSI 476
 
Name Accession Description Interval E-value
PRK11107 PRK11107
hybrid sensory histidine kinase BarA; Provisional
559-1094 3.45e-112

hybrid sensory histidine kinase BarA; Provisional


Pssm-ID: 236848 [Multi-domain]  Cd Length: 919  Bit Score: 370.72  E-value: 3.45e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  559 AKAAAEQANIAKSEFLAAMSHEIRTPMNGVLGMLNLILDSSLNEKQHHQVSIALNSANSLLNIINDILDFSKVDAGKLEL 638
Cdd:PRK11107  282 AKKRAQEAARIKSEFLANMSHELRTPLNGVIGFTRQTLKTPLTPTQRDYLQTIERSANNLLAIINDILDFSKLEAGKLVL 361
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  639 EELEFNLCNMLDDFIETIAIHAHSKNIPLMLDIEHLEYAFVIGDAGRLKQILTNLVNNALKFTHKGEVQVIAKLTPINNN 718
Cdd:PRK11107  362 ENIPFSLRETLDEVVTLLAHSAHEKGLELTLNIDPDVPDNVIGDPLRLQQIITNLVGNAIKFTESGNIDILVELRALSNT 441
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  719 QMRFNCQVIDSGIGISAAQQAKLFKSFSQVDSSTTRKYGGTGLGLAIVKKLCHLMEGDIQVQSKENKGSNFSFNVVLKRS 798
Cdd:PRK11107  442 KVQLEVQIRDTGIGISERQQSQLFQAFRQADASISRRHGGTGLGLVITQKLVNEMGGDISFHSQPNRGSTFWFHLPLDLN 521
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  799 KNPqkVLPPVDMSSL---NILIVCSNQTQSSILHKQFTKWGATAVISPSAKQAVQIcqqyiekqnlCFDLIMIDMQLSDG 875
Cdd:PRK11107  522 PNP--IIDGLPTDCLagkRLLYVEPNSAAAQATLDILSETPLEVTYSPTLSQLPEA----------HYDILLLGLPVTFR 589
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  876 DALTLSKTLDKEVDLMAAHVVLMttgeLNKQRDLYQAS--RFSAIV--TKPIITQNLFKMLStcfSDKQHSNSSLITEDL 951
Cdd:PRK11107  590 EPLTMLHERLAKAKSMTDFLILA----LPCHEQVLAEQlkQDGADAclSKPLSHTRLLPALL---EPCHHKQPPLLPPTD 662
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  952 SDTQPLSsddivwdknirILLVEDNNINqivasttLKKIG------INSIDIAENGQHALEYLKQttshNPYSLILMDCQ 1025
Cdd:PRK11107  663 ESRLPLT-----------VMAVDDNPAN-------LKLIGalleeqVEHVVLCDSGHQAVEQAKQ----RPFDLILMDIQ 720
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 503229768 1026 MPVMDGYQATTHIRVNEAGSKNPpitIIAMTANAMVGDKAKCLQVGMNDYISKPIAQDILFKKLLKWLP 1094
Cdd:PRK11107  721 MPGMDGIRACELIRQLPHNQNTP---IIAVTAHAMAGERERLLSAGMDDYLAKPIDEAMLKQVLLRYKP 786
TMAO_torS TIGR02956
TMAO reductase sytem sensor TorS; This protein, TorS, is part of a regulatory system for the ...
559-971 1.22e-75

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: 269.73  E-value: 1.22e-75
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768   559 AKAAAEQANIAKSEFLAAMSHEIRTPMNGVLGMLNLILDSSLNEKQHHQVSIALNSANSLLNIINDILDFSKVDAGKLEL 638
Cdd:TIGR02956  453 ARAEAEEANRAKSAFLATMSHEIRTPLNGILGTLELLGDTGLTSQQQQYLQVINRSGESLLDILNDILDYSKIEAGHLSI 532
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768   639 EELEFNLCNMLDDFIETIAIHAHSKNIPLMLDIEHLEYAFVIGDAGRLKQILTNLVNNALKFTHKGEVQVIAKLTPinNN 718
Cdd:TIGR02956  533 SPRPFDLNALLDDVHHLMVSRAQLKGIQLRLNIPEQLPNWWQGDGPRIRQVLINLVGNAIKFTDRGSVVLRVSLND--DS 610
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768   719 QMRFncQVIDSGIGISAAQQAKLFKSFSQVDSSttRKYGGTGLGLAIVKKLCHLMEGDIQVQSKENKGSNFSFNVVLKRS 798
Cdd:TIGR02956  611 SLLF--EVEDTGCGIAEEEQATLFDAFTQADGR--RRSGGTGLGLAISQRLVEAMDGELGVESELGVGSCFWFTLPLTRG 686
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768   799 KNPQKV--LPPVDMSSLNILIVCSNQTQSSILHKQFTKWGATAVISPSAKQAVQICQQYiekqnlCFDLIMIDMQLSDGD 876
Cdd:TIGR02956  687 KPAEDSatLTVIDLPPQRVLLVEDNEVNQMVAQGFLTRLGHKVTLAESGQSALECFHQH------AFDLALLDINLPDGD 760
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768   877 ALTLSKTL------DKEVDLMA--AHVvlmttgeLNKQRDLYQASRFSAIVTKPIITQNLFKMLSTCFSDK--------- 939
Cdd:TIGR02956  761 GVTLLQQLraiygaKNEVKFIAfsAHV-------FNEDVAQYLAAGFDGFLAKPVVEEQLTAMIAVILAGGksnteapvl 833
                          410       420       430
                   ....*....|....*....|....*....|....*.
gi 503229768   940 ----QHSNSSLITEDLSDTQPLSSDDIVWDKNIRIL 971
Cdd:TIGR02956  834 saspSFDSASVIENAQADDIPESNQASEFLLDEEQL 869
BaeS COG0642
Signal transduction histidine kinase [Signal transduction mechanisms];
536-791 3.59e-71

Signal transduction histidine kinase [Signal transduction mechanisms];


Pssm-ID: 440407 [Multi-domain]  Cd Length: 328  Bit Score: 240.58  E-value: 3.59e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  536 LTAYVGIQQDITEQKAANQLLIEAKAAAEQANIAKSEFLAAMSHEIRTPMNGVLGMLNLILDSsLNEKQHHQVSIALNSA 615
Cdd:COG0642    76 LLLLLLLLLLLLLLLLLLLLLLALLLLLEEANEAKSRFLANVSHELRTPLTAIRGYLELLLEE-LDEEQREYLETILRSA 154
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  616 NSLLNIINDILDFSKVDAGKLELEELEFNLCNMLDDFIETIAIHAHSKNIPLMLDIEHlEYAFVIGDAGRLKQILTNLVN 695
Cdd:COG0642   155 DRLLRLINDLLDLSRLEAGKLELEPEPVDLAELLEEVVELFRPLAEEKGIELELDLPD-DLPTVRGDPDRLRQVLLNLLS 233
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  696 NALKFTHKG-EVQVIAKltpINNNQMRFncQVIDSGIGISAAQQAKLFKSFSQVDSSttRKYGGTGLGLAIVKKLCHLME 774
Cdd:COG0642   234 NAIKYTPEGgTVTVSVR---REGDRVRI--SVEDTGPGIPPEDLERIFEPFFRTDPS--RRGGGTGLGLAIVKRIVELHG 306
                         250
                  ....*....|....*..
gi 503229768  775 GDIQVQSKENKGSNFSF 791
Cdd:COG0642   307 GTIEVESEPGKGTTFTV 323
KinE COG5809
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome ...
291-791 1.12e-65

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: 230.25  E-value: 1.12e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  291 EAIKQSEARYELAVKGSNDGIWDWDIVTNEVYFSPRISVLLGYDENDknalpHCADALYKLLHPDDITKHKKQIANHLIS 370
Cdd:COG5809     8 LQLRKSEQRFRSLFENAPDAILILDLEGKILKVNPAAERIFGYTEDE-----LLGTNILDFLHPDDEKELREILKLLKEG 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  371 NIPFNYDYRLKTKSGAYRYFTVKGMALRNEHNKAIRMAGSVTDITEQKRSQKALKQAKEQNDLLAQAIEScnvGISIADA 450
Cdd:COG5809    83 ESRDELEFELRHKNGKRLEFSSKLSPIFDQNGDIEGMLAISRDITERKRMEEALRESEEKFRLIFNHSPD---GIIVTDL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  451 SVQgfpLVFLNSEFEKITGYSKEEMLGINCSLLQGPNTDKNAIDIITNAIKTLKTQRIEILNYKKDGTEFWNSLQISPVF 530
Cdd:COG5809   160 DGR---IIYANPAACKLLGISIEELIGKSILELIHSDDQENVAAFISQLLKDGGIAQGEVRFWTKDGRWRLLEASGAPIK 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  531 -NEQQQltAYVGIQQDITEQKAanqlLIEAKAAAEQANIAkSEFLAAMSHEIRTPMNGVLGMLNLILDSSLNEKQHHqVS 609
Cdd:COG5809   237 kNGEVD--GIVIIFRDITERKK----LEELLRKSEKLSVV-GELAAGIAHEIRNPLTSLKGFIQLLKDTIDEEQKTY-LD 308
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  610 IALNSANSLLNIINDILDFSKVDAGKLELeeleFNLCNMLDDFIETIAIHAHSKNIPLMLDIEHLEYaFVIGDAGRLKQI 689
Cdd:COG5809   309 IMLSELDRIESIISEFLVLAKPQAIKYEP----KDLNTLIEEVIPLLQPQALLKNVQIELELEDDIP-DILGDENQLKQV 383
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  690 LTNLVNNALKFTHK-GEVQViaKLTPINNNQMRFncQVIDSGIGISAAQQAKLFKSFSqvdsstTRKYGGTGLGLAIVKK 768
Cdd:COG5809   384 FINLLKNAIEAMPEgGNITI--ETKAEDDDKVVI--SVTDEGCGIPEERLKKLGEPFY------TTKEKGTGLGLMVSYK 453
                         490       500
                  ....*....|....*....|...
gi 503229768  769 LCHLMEGDIQVQSKENKGSNFSF 791
Cdd:COG5809   454 IIEEHGGKITVESEVGKGTTFSI 476
HATPase_EvgS-ArcB-TorS-like cd16922
Histidine kinase-like ATPase domain of two-component sensor histidine kinases, many are hybrid ...
686-791 5.09e-52

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: 177.68  E-value: 5.09e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  686 LKQILTNLVNNALKFTHKGEVQVIAKLTPINNNQMRFNCQVIDSGIGISAAQQAKLFKSFSQVDSSTTRKYGGTGLGLAI 765
Cdd:cd16922     1 LRQILLNLLGNAIKFTEEGEVTLRVSLEEEEEDGVQLRFSVEDTGIGIPEEQQARLFEPFSQADSSTTRKYGGTGLGLAI 80
                          90       100
                  ....*....|....*....|....*.
gi 503229768  766 VKKLCHLMEGDIQVQSKENKGSNFSF 791
Cdd:cd16922    81 SKKLVELMGGDISVESEPGQGSTFTF 106
PRK13558 PRK13558
bacterio-opsin activator; Provisional
427-566 1.45e-35

bacterio-opsin activator; Provisional


Pssm-ID: 237426 [Multi-domain]  Cd Length: 665  Bit Score: 144.98  E-value: 1.45e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  427 AKEQNDLLAQAIESCNVGISIADASVQGFPLVFLNSEFEKITGYSKEEMLGINCSLLQGPNTDKNAIDIITNAIKTLKTQ 506
Cdd:PRK13558  143 VESDRRLKERALDEAPVGITIADATLPDEPLIYINDAFERITGYSPDEVLGRNCRFLQGEDTNEERVAELREAIDEERPT 222
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  507 RIEILNYKKDGTEFWNSLQISPVFNEQQQLTAYVGIQQDITEQKAAnqlliEAKAAAEQA 566
Cdd:PRK13558  223 SVELRNYRKDGSTFWNQVDIAPIRDEDGTVTHYVGFQTDVTERKEA-----ELALQRERR 277
HATPase_c smart00387
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.
681-791 1.57e-30

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


Pssm-ID: 214643 [Multi-domain]  Cd Length: 111  Bit Score: 116.21  E-value: 1.57e-30
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768    681 GDAGRLKQILTNLVNNALKFTHK-GEVQVIAKLTPinnnqMRFNCQVIDSGIGISAAQQAKLFKSFSQVDSsTTRKYGGT 759
Cdd:smart00387    1 GDPDRLRQVLSNLLDNAIKYTPEgGRITVTLERDG-----DHVEITVEDNGPGIPPEDLEKIFEPFFRTDK-RSRKIGGT 74
                            90       100       110
                    ....*....|....*....|....*....|..
gi 503229768    760 GLGLAIVKKLCHLMEGDIQVQSKENKGSNFSF 791
Cdd:smart00387   75 GLGLSIVKKLVELHGGEISVESEPGGGTTFTI 106
HATPase_c pfam02518
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the ...
681-791 3.72e-26

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


Pssm-ID: 460579 [Multi-domain]  Cd Length: 109  Bit Score: 103.99  E-value: 3.72e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768   681 GDAGRLKQILTNLVNNALKFTHK-GEVQViaKLTPINNNQMRfncqVIDSGIGISAAQQAKLFKSFSQVDSsttRKYGGT 759
Cdd:pfam02518    1 GDELRLRQVLSNLLDNALKHAAKaGEITV--TLSEGGELTLT----VEDNGIGIPPEDLPRIFEPFSTADK---RGGGGT 71
                           90       100       110
                   ....*....|....*....|....*....|..
gi 503229768   760 GLGLAIVKKLCHLMEGDIQVQSKENKGSNFSF 791
Cdd:pfam02518   72 GLGLSIVRKLVELLGGTITVESEPGGGTTVTL 103
BaeS_SmeS NF012163
sensor histidine kinase efflux regulator BaeS;
553-777 4.34e-21

sensor histidine kinase efflux regulator BaeS;


Pssm-ID: 411086 [Multi-domain]  Cd Length: 457  Bit Score: 97.98  E-value: 4.34e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  553 NQLlieaKAAAEQANIAKSEFLAAMSHEIRTPMNGVLGMLNLILDSSLNEKQHHQVSIaLNSANSLLNIINDILDFSKVD 632
Cdd:NF012163  227 NQL----ASTLEKNEQMRRDFMADISHELRTPLAVLRAELEAIQDGIRKFTPESLDSL-QAEVGTLTKLVDDLHDLSMSD 301
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  633 AGKLELEELEFNLCNMLDDFIETIAIHAHSKNIPLMLDIEhlEYAFVIGDAGRLKQILTNLVNNALKFTHK-GEVQVIAK 711
Cdd:NF012163  302 EGALAYQKASVDLVPLLEVEGGAFRERFASAGLELEVSLP--DSSLVFGDRDRLMQLFNNLLENSLRYTDSgGSLHISAS 379
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 503229768  712 LTPinnnQMRFnCQVIDSGIGISAAQQAKLFKSFSQVDSSTTRKYGGTGLGLAIVKKLCHLMEGDI 777
Cdd:NF012163  380 QRP----KEVT-LTVADSAPGVSDEQLARLFERFYRVEVSRNRASGGSGLGLAISLNIVQAHGGTL 440
PAS_9 pfam13426
PAS domain; This domain is found in many signalling proteins in which it functions as a sensor ...
455-548 1.15e-16

PAS domain; This domain is found in many signalling proteins in which it functions as a sensor domain. It recognizes FMN, Zn(II), FAD and riboflavin (MAtilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).


Pssm-ID: 463873 [Multi-domain]  Cd Length: 93  Bit Score: 76.35  E-value: 1.15e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768   455 FPLVFLNSEFEKITGYSKEEMLGINCSLLQGpntDKNAIDIITNAIKTLKTQR-IEILNYKKDGTEFWNSLQISPVFNEQ 533
Cdd:pfam13426    2 GRIIYVNDAALRLLGYTREELLGKSITDLFA---EPEDSERLREALREGKAVReFEVVLYRKDGEPFPVLVSLAPIRDDG 78
                           90
                   ....*....|....*
gi 503229768   534 QQLTAYVGIQQDITE 548
Cdd:pfam13426   79 GELVGIIAILRDITE 93
sensory_box TIGR00229
PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain ...
432-556 1.43e-14

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


Pssm-ID: 272971 [Multi-domain]  Cd Length: 124  Bit Score: 71.17  E-value: 1.43e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768   432 DLLAQAIESCNVGISIADasVQGFpLVFLNSEFEKITGYSKEEMLGINCS-LLQGPNTDKNAIDIITNAIKTLKTQRIEI 510
Cdd:TIGR00229    3 ERYRAIFESSPDAIIVID--LEGN-ILYVNPAFEEIFGYSAEELIGRNVLeLIPEEDREEVRERIERRLEGEPEPVSEER 79
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 503229768   511 LNYKKDGTEFWNSLQISPVFnEQQQLTAYVGIQQDITEQKAANQLL 556
Cdd:TIGR00229   80 RVRRKDGSEIWVEVSVSPIR-TNGGELGVVGIVRDITERKEAEEAL 124
PAS cd00130
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
307-414 3.62e-12

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


Pssm-ID: 238075 [Multi-domain]  Cd Length: 103  Bit Score: 63.81  E-value: 3.62e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  307 SNDGIWDWDIVTNEVYFSPRISVLLGYDENDKNALPhcadaLYKLLHPDDITKHKKQIANHLISNIPFNYDYRLKTKSGA 386
Cdd:cd00130     1 LPDGVIVLDLDGRILYANPAAEQLLGYSPEELIGKS-----LLDLIHPEDREELRERLENLLSGGEPVTLEVRLRRKDGS 75
                          90       100
                  ....*....|....*....|....*...
gi 503229768  387 YRYFTVKGMALRNEHNKAIRMAGSVTDI 414
Cdd:cd00130    76 VIWVLVSLTPIRDEGGEVIGLLGVVRDI 103
MtrAB_MtrB NF040691
MtrAB system histidine kinase MtrB;
573-789 2.03e-11

MtrAB system histidine kinase MtrB;


Pssm-ID: 468655 [Multi-domain]  Cd Length: 507  Bit Score: 67.74  E-value: 2.03e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  573 FLAAMSHEIRTPMNGVLGMLNLILDSSLN---------EKQHHQvsiaLNSANSLLniiNDILDFSKVDAGKLELEELEF 643
Cdd:NF040691  274 FVSDVSHELRTPLTTIRMAADVIHDSRDDfdpatarsaELLHTE----LDRFESLL---SDLLEISRFDAGAAELDVEPV 346
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  644 NLCNMLDDFIETIAIHAHSKNIPLMLDIEHlEYAFVIGDAGRLKQILTNLVNNALKFTHKGEVQVIakltpINNNQMRFN 723
Cdd:NF040691  347 DLRPLVRRVVDALRQLAERAGVELRVDAPG-TPVVAEVDPRRVERVLRNLVVNAIEHGEGKPVVVT-----VAQDDTAVA 420
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 503229768  724 CQVIDSGIGISAAQQAKLFKSFSQVDSSTTRKYGGTGLGLAIVKKLCHLMEGDIQVQSKENKGSNF 789
Cdd:NF040691  421 VTVRDHGVGLKPGEVALVFDRFWRADPARARTTGGTGLGLAIALEDARLHGGWLEAWGRPGQGSQF 486
PAC smart00086
Motif C-terminal to PAS motifs (likely to contribute to PAS structural domain); PAC motif ...
508-549 1.12e-08

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


Pssm-ID: 197509  Cd Length: 43  Bit Score: 51.80  E-value: 1.12e-08
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|..
gi 503229768    508 IEILNYKKDGTEFWNSLQISPVFNEQQQLTAYVGIQQDITEQ 549
Cdd:smart00086    2 VEYRLRRKDGSYIWVLVSASPIRDEDGEVEGILGVVRDITER 43
 
Name Accession Description Interval E-value
PRK11107 PRK11107
hybrid sensory histidine kinase BarA; Provisional
559-1094 3.45e-112

hybrid sensory histidine kinase BarA; Provisional


Pssm-ID: 236848 [Multi-domain]  Cd Length: 919  Bit Score: 370.72  E-value: 3.45e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  559 AKAAAEQANIAKSEFLAAMSHEIRTPMNGVLGMLNLILDSSLNEKQHHQVSIALNSANSLLNIINDILDFSKVDAGKLEL 638
Cdd:PRK11107  282 AKKRAQEAARIKSEFLANMSHELRTPLNGVIGFTRQTLKTPLTPTQRDYLQTIERSANNLLAIINDILDFSKLEAGKLVL 361
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  639 EELEFNLCNMLDDFIETIAIHAHSKNIPLMLDIEHLEYAFVIGDAGRLKQILTNLVNNALKFTHKGEVQVIAKLTPINNN 718
Cdd:PRK11107  362 ENIPFSLRETLDEVVTLLAHSAHEKGLELTLNIDPDVPDNVIGDPLRLQQIITNLVGNAIKFTESGNIDILVELRALSNT 441
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  719 QMRFNCQVIDSGIGISAAQQAKLFKSFSQVDSSTTRKYGGTGLGLAIVKKLCHLMEGDIQVQSKENKGSNFSFNVVLKRS 798
Cdd:PRK11107  442 KVQLEVQIRDTGIGISERQQSQLFQAFRQADASISRRHGGTGLGLVITQKLVNEMGGDISFHSQPNRGSTFWFHLPLDLN 521
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  799 KNPqkVLPPVDMSSL---NILIVCSNQTQSSILHKQFTKWGATAVISPSAKQAVQIcqqyiekqnlCFDLIMIDMQLSDG 875
Cdd:PRK11107  522 PNP--IIDGLPTDCLagkRLLYVEPNSAAAQATLDILSETPLEVTYSPTLSQLPEA----------HYDILLLGLPVTFR 589
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  876 DALTLSKTLDKEVDLMAAHVVLMttgeLNKQRDLYQAS--RFSAIV--TKPIITQNLFKMLStcfSDKQHSNSSLITEDL 951
Cdd:PRK11107  590 EPLTMLHERLAKAKSMTDFLILA----LPCHEQVLAEQlkQDGADAclSKPLSHTRLLPALL---EPCHHKQPPLLPPTD 662
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  952 SDTQPLSsddivwdknirILLVEDNNINqivasttLKKIG------INSIDIAENGQHALEYLKQttshNPYSLILMDCQ 1025
Cdd:PRK11107  663 ESRLPLT-----------VMAVDDNPAN-------LKLIGalleeqVEHVVLCDSGHQAVEQAKQ----RPFDLILMDIQ 720
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 503229768 1026 MPVMDGYQATTHIRVNEAGSKNPpitIIAMTANAMVGDKAKCLQVGMNDYISKPIAQDILFKKLLKWLP 1094
Cdd:PRK11107  721 MPGMDGIRACELIRQLPHNQNTP---IIAVTAHAMAGERERLLSAGMDDYLAKPIDEAMLKQVLLRYKP 786
TMAO_torS TIGR02956
TMAO reductase sytem sensor TorS; This protein, TorS, is part of a regulatory system for the ...
559-971 1.22e-75

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: 269.73  E-value: 1.22e-75
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768   559 AKAAAEQANIAKSEFLAAMSHEIRTPMNGVLGMLNLILDSSLNEKQHHQVSIALNSANSLLNIINDILDFSKVDAGKLEL 638
Cdd:TIGR02956  453 ARAEAEEANRAKSAFLATMSHEIRTPLNGILGTLELLGDTGLTSQQQQYLQVINRSGESLLDILNDILDYSKIEAGHLSI 532
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768   639 EELEFNLCNMLDDFIETIAIHAHSKNIPLMLDIEHLEYAFVIGDAGRLKQILTNLVNNALKFTHKGEVQVIAKLTPinNN 718
Cdd:TIGR02956  533 SPRPFDLNALLDDVHHLMVSRAQLKGIQLRLNIPEQLPNWWQGDGPRIRQVLINLVGNAIKFTDRGSVVLRVSLND--DS 610
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768   719 QMRFncQVIDSGIGISAAQQAKLFKSFSQVDSSttRKYGGTGLGLAIVKKLCHLMEGDIQVQSKENKGSNFSFNVVLKRS 798
Cdd:TIGR02956  611 SLLF--EVEDTGCGIAEEEQATLFDAFTQADGR--RRSGGTGLGLAISQRLVEAMDGELGVESELGVGSCFWFTLPLTRG 686
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768   799 KNPQKV--LPPVDMSSLNILIVCSNQTQSSILHKQFTKWGATAVISPSAKQAVQICQQYiekqnlCFDLIMIDMQLSDGD 876
Cdd:TIGR02956  687 KPAEDSatLTVIDLPPQRVLLVEDNEVNQMVAQGFLTRLGHKVTLAESGQSALECFHQH------AFDLALLDINLPDGD 760
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768   877 ALTLSKTL------DKEVDLMA--AHVvlmttgeLNKQRDLYQASRFSAIVTKPIITQNLFKMLSTCFSDK--------- 939
Cdd:TIGR02956  761 GVTLLQQLraiygaKNEVKFIAfsAHV-------FNEDVAQYLAAGFDGFLAKPVVEEQLTAMIAVILAGGksnteapvl 833
                          410       420       430
                   ....*....|....*....|....*....|....*.
gi 503229768   940 ----QHSNSSLITEDLSDTQPLSSDDIVWDKNIRIL 971
Cdd:TIGR02956  834 saspSFDSASVIENAQADDIPESNQASEFLLDEEQL 869
BaeS COG0642
Signal transduction histidine kinase [Signal transduction mechanisms];
536-791 3.59e-71

Signal transduction histidine kinase [Signal transduction mechanisms];


Pssm-ID: 440407 [Multi-domain]  Cd Length: 328  Bit Score: 240.58  E-value: 3.59e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  536 LTAYVGIQQDITEQKAANQLLIEAKAAAEQANIAKSEFLAAMSHEIRTPMNGVLGMLNLILDSsLNEKQHHQVSIALNSA 615
Cdd:COG0642    76 LLLLLLLLLLLLLLLLLLLLLLALLLLLEEANEAKSRFLANVSHELRTPLTAIRGYLELLLEE-LDEEQREYLETILRSA 154
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  616 NSLLNIINDILDFSKVDAGKLELEELEFNLCNMLDDFIETIAIHAHSKNIPLMLDIEHlEYAFVIGDAGRLKQILTNLVN 695
Cdd:COG0642   155 DRLLRLINDLLDLSRLEAGKLELEPEPVDLAELLEEVVELFRPLAEEKGIELELDLPD-DLPTVRGDPDRLRQVLLNLLS 233
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  696 NALKFTHKG-EVQVIAKltpINNNQMRFncQVIDSGIGISAAQQAKLFKSFSQVDSSttRKYGGTGLGLAIVKKLCHLME 774
Cdd:COG0642   234 NAIKYTPEGgTVTVSVR---REGDRVRI--SVEDTGPGIPPEDLERIFEPFFRTDPS--RRGGGTGLGLAIVKRIVELHG 306
                         250
                  ....*....|....*..
gi 503229768  775 GDIQVQSKENKGSNFSF 791
Cdd:COG0642   307 GTIEVESEPGKGTTFTV 323
PRK15347 PRK15347
two component system sensor kinase;
525-1080 1.25e-68

two component system sensor kinase;


Pssm-ID: 237951 [Multi-domain]  Cd Length: 921  Bit Score: 248.79  E-value: 1.25e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  525 QISPVFNeqqQLTAYVGIQQDITEQKAA--NQLLIEAKAAAEQANIAKSEFLAAMSHEIRTPMNGVLGMLNLILDSSLNE 602
Cdd:PRK15347  354 SIAKAYN---QLLDTLNEQYDTLENKVAerTQALAEAKQRAEQANKRKSEHLTTISHEIRTPLNGVLGALELLQNTPLTA 430
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  603 KQHHQVSIALNSANSLLNIINDILDFSKVDAGKLELEELEFNLCNMLDDFIETIAIHAHSK----------NIPLMLDIe 672
Cdd:PRK15347  431 EQMDLADTARQCTLSLLAIINNLLDFSRIESGQMTLSLEETALLPLLDQAMLTIQGPAQSKsltlrtfvgaHVPLYLHL- 509
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  673 hleyafvigDAGRLKQILTNLVNNALKFTHKGEVQVIAKltpINNNQMRFNcqVIDSGIGISAAQQAKLFKSFSQVDSST 752
Cdd:PRK15347  510 ---------DSLRLRQILVNLLGNAVKFTETGGIRLRVK---RHEQQLCFT--VEDTGCGIDIQQQQQIFTPFYQADTHS 575
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  753 trkyGGTGLGLAIVKKLCHLMEGDIQVQSKENKGSNFSFNVVLkrsknpQKVLPPVDMSSLNILIVCsnqtqssiLHKQF 832
Cdd:PRK15347  576 ----QGTGLGLTIASSLAKMMGGELTLFSTPGVGSCFSLVLPL------NEYAPPEPLKGELSAPLA--------LHRQL 637
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  833 TKWGATavispsakqavqiCQQYIEKQNLCfdlimidmqlsdgdaltlsktlDKEVdlmaahvvlmttgelnkqrdLYQA 912
Cdd:PRK15347  638 SAWGIT-------------CQPGHQNPALL----------------------DPEL--------------------AYLP 662
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  913 SRFSAIVtkpiitqnlfkmlstcfsDKQHSNSSLITEDLSDTQPlssddivWdkNIRILLVEDNNINQIVASTTLKKIGi 992
Cdd:PRK15347  663 GRLYDLL------------------QQIIQGAPNEPVINLPLQP-------W--QLQILLVDDVETNRDIIGMMLVELG- 714
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  993 NSIDIAENGQHALEYLKQTTshnpYSLILMDCQMPVMDGYQATTHIRVNEAGsKNPPITIIAMTANAMVGDKAKCLQVGM 1072
Cdd:PRK15347  715 QQVTTAASGTEALELGRQHR----FDLVLMDIRMPGLDGLETTQLWRDDPNN-LDPDCMIVALTANAAPEEIHRCKKAGM 789

                  ....*...
gi 503229768 1073 NDYISKPI 1080
Cdd:PRK15347  790 NHYLTKPV 797
KinE COG5809
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome ...
291-791 1.12e-65

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: 230.25  E-value: 1.12e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  291 EAIKQSEARYELAVKGSNDGIWDWDIVTNEVYFSPRISVLLGYDENDknalpHCADALYKLLHPDDITKHKKQIANHLIS 370
Cdd:COG5809     8 LQLRKSEQRFRSLFENAPDAILILDLEGKILKVNPAAERIFGYTEDE-----LLGTNILDFLHPDDEKELREILKLLKEG 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  371 NIPFNYDYRLKTKSGAYRYFTVKGMALRNEHNKAIRMAGSVTDITEQKRSQKALKQAKEQNDLLAQAIEScnvGISIADA 450
Cdd:COG5809    83 ESRDELEFELRHKNGKRLEFSSKLSPIFDQNGDIEGMLAISRDITERKRMEEALRESEEKFRLIFNHSPD---GIIVTDL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  451 SVQgfpLVFLNSEFEKITGYSKEEMLGINCSLLQGPNTDKNAIDIITNAIKTLKTQRIEILNYKKDGTEFWNSLQISPVF 530
Cdd:COG5809   160 DGR---IIYANPAACKLLGISIEELIGKSILELIHSDDQENVAAFISQLLKDGGIAQGEVRFWTKDGRWRLLEASGAPIK 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  531 -NEQQQltAYVGIQQDITEQKAanqlLIEAKAAAEQANIAkSEFLAAMSHEIRTPMNGVLGMLNLILDSSLNEKQHHqVS 609
Cdd:COG5809   237 kNGEVD--GIVIIFRDITERKK----LEELLRKSEKLSVV-GELAAGIAHEIRNPLTSLKGFIQLLKDTIDEEQKTY-LD 308
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  610 IALNSANSLLNIINDILDFSKVDAGKLELeeleFNLCNMLDDFIETIAIHAHSKNIPLMLDIEHLEYaFVIGDAGRLKQI 689
Cdd:COG5809   309 IMLSELDRIESIISEFLVLAKPQAIKYEP----KDLNTLIEEVIPLLQPQALLKNVQIELELEDDIP-DILGDENQLKQV 383
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  690 LTNLVNNALKFTHK-GEVQViaKLTPINNNQMRFncQVIDSGIGISAAQQAKLFKSFSqvdsstTRKYGGTGLGLAIVKK 768
Cdd:COG5809   384 FINLLKNAIEAMPEgGNITI--ETKAEDDDKVVI--SVTDEGCGIPEERLKKLGEPFY------TTKEKGTGLGLMVSYK 453
                         490       500
                  ....*....|....*....|...
gi 503229768  769 LCHLMEGDIQVQSKENKGSNFSF 791
Cdd:COG5809   454 IIEEHGGKITVESEVGKGTTFSI 476
PRK10841 PRK10841
two-component system sensor histidine kinase RcsC;
522-1085 3.88e-64

two-component system sensor histidine kinase RcsC;


Pssm-ID: 182772 [Multi-domain]  Cd Length: 924  Bit Score: 235.25  E-value: 3.88e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  522 NSLQISPVF----NEQQQLTAYVgiqqDITEQKAANQLLIEAKAAAEQANIAKSEFLAAMSHEIRTPMNGVLGMLNLILD 597
Cdd:PRK10841  399 TNLQISFVHsryrNENVAICVLV----DVSARVKMEESLQEMAQAAEQASQSKSMFLATVSHELRTPLYGIIGNLDLLQT 474
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  598 SSLNEKQHHQVSIALNSANSLLNIINDILDFSKVDAGKLELEELEFNlCNmlddfiETIAiHAHSKNIPLMLDIEHLEYA 677
Cdd:PRK10841  475 KELPKGVDRLVTAMNNSSSLLLKIISDILDFSKIESEQLKIEPREFS-PR------EVIN-HITANYLPLVVKKRLGLYC 546
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  678 F--------VIGDAGRLKQILTNLVNNALKFTHKG----EVQViakltpiNNNQMRFncQVIDSGIGISAAQQAKLFKSF 745
Cdd:PRK10841  547 FiepdvpvaLNGDPMRLQQVISNLLSNAIKFTDTGcivlHVRV-------DGDYLSF--RVRDTGVGIPAKEVVRLFDPF 617
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  746 SQVDSSTTRKYGGTGLGLAIVKKLCHLMEGDIQVQSKENKGSNFSFNVVLKRSKNPQKVLPPvDMSSLNILIVCSNQTQS 825
Cdd:PRK10841  618 FQVGTGVQRNFQGTGLGLAICEKLINMMDGDISVDSEPGMGSQFTIRIPLYGAQYPQKKGVE-GLQGKRCWLAVRNASLE 696
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  826 SILHKQFTKWGATavispsakqavqiCQQYiEKQNLCFDLIMIdmqlSDgDALTLSKTLDKEVDLMAAHVvlmttGELNK 905
Cdd:PRK10841  697 QFLETLLQRSGIQ-------------VQRY-EGQEPTPEDVLI----TD-DPVQKKWQGRAVITFCRRHI-----GIPLE 752
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  906 QRdlyqASRFSAIVTKPiitQNLFKMLSTCFSDKQHSnsslitEDLSDTQPLSSDDIVWDKNIRILLVEDNNINQIVAST 985
Cdd:PRK10841  753 IA----PGEWVHSTATP---HELPALLARIYRIELES------DDSANALPSTDKAVSDNDDMMILVVDDHPINRRLLAD 819
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  986 TLKKIGINSIdIAENGQHALEYLKQttshNPYSLILMDCQMPVMDGYQATTHIRvnEAGSKNPpitIIAMTANAMVGDKA 1065
Cdd:PRK10841  820 QLGSLGYQCK-TANDGVDALNVLSK----NHIDIVLTDVNMPNMDGYRLTQRLR--QLGLTLP---VIGVTANALAEEKQ 889
                         570       580
                  ....*....|....*....|
gi 503229768 1066 KCLQVGMNDYISKPIAQDIL 1085
Cdd:PRK10841  890 RCLEAGMDSCLSKPVTLDVL 909
KdpD COG2205
K+-sensing histidine kinase KdpD [Signal transduction mechanisms];
556-791 1.21e-62

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


Pssm-ID: 441807 [Multi-domain]  Cd Length: 239  Bit Score: 212.84  E-value: 1.21e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  556 LIEAKAAAEQANIAKSEFLAAMSHEIRTPMNGVLGMLNLILDSS--LNEKQHHQVSIALNSANSLLNIINDILDFSKVDA 633
Cdd:COG2205     2 LEEALEELEELERLKSEFLANVSHELRTPLTSILGAAELLLDEEdlSPEERRELLEIIRESAERLLRLIEDLLDLSRLES 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  634 GKLELEELEFNLCNMLDDFIETIAIHAHSKNIPLMLDIEHLEyAFVIGDAGRLKQILTNLVNNALKFTHKG-EVQVIAKl 712
Cdd:COG2205    82 GKLSLELEPVDLAELLEEAVEELRPLAEEKGIRLELDLPPEL-PLVYADPELLEQVLANLLDNAIKYSPPGgTITISAR- 159
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 503229768  713 tpINNNQMRFncQVIDSGIGISAAQQAKLFKSFSQVDSstTRKYGGTGLGLAIVKKLCHLMEGDIQVQSKENKGSNFSF 791
Cdd:COG2205   160 --REGDGVRI--SVSDNGPGIPEEELERIFERFYRGDN--SRGEGGTGLGLAIVKRIVEAHGGTIWVESEPGGGTTFTV 232
WalK COG5002
Sensor histidine kinase WalK [Signal transduction mechanisms];
506-791 1.51e-62

Sensor histidine kinase WalK [Signal transduction mechanisms];


Pssm-ID: 444026 [Multi-domain]  Cd Length: 390  Bit Score: 218.27  E-value: 1.51e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  506 QRIEILNYKKDGTEFWNSLQISPVFNEQQQLTAYVGIQQDITEQKAANQLlieakaaaeqaniaKSEFLAAMSHEIRTPM 585
Cdd:COG5002   115 AALLLLLSELLLLLLLLGRLSLRLSALLLGLLLLAAVERDITELERLEQM--------------RREFVANVSHELRTPL 180
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  586 NGVLGMLNLILDS--SLNEKQHHQVSIALNSANSLLNIINDILDFSKVDAGKLELEELEFNLCNMLDDFIETIAIHAHSK 663
Cdd:COG5002   181 TSIRGYLELLLDGaaDDPEERREYLEIILEEAERLSRLVNDLLDLSRLESGELKLEKEPVDLAELLEEVVEELRPLAEEK 260
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  664 NIPLMLDIEHlEYAFVIGDAGRLKQILTNLVNNALKFTHKG-EVQVIAKltpINNNQMRFncQVIDSGIGISAAQQAKLF 742
Cdd:COG5002   261 GIELELDLPE-DPLLVLGDPDRLEQVLTNLLDNAIKYTPEGgTITVSLR---EEDDQVRI--SVRDTGIGIPEEDLPRIF 334
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 503229768  743 KSFSQVDSSTTRKYGGTGLGLAIVKKLCHLMEGDIQVQSKENKGSNFSF 791
Cdd:COG5002   335 ERFYRVDKSRSRETGGTGLGLAIVKHIVEAHGGRIWVESEPGKGTTFTI 383
PRK11091 PRK11091
aerobic respiration control sensor protein ArcB; Provisional
416-1081 4.51e-54

aerobic respiration control sensor protein ArcB; Provisional


Pssm-ID: 236842 [Multi-domain]  Cd Length: 779  Bit Score: 202.86  E-value: 4.51e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  416 EQKRSQKALKQAKEQNDLLAqaiescnvgiSIADASvqgfP-LVF---LNSEF-------EKITGYSKEEMLGINCSLLQ 484
Cdd:PRK11091  139 EIKEREETQIELEQQSSLLR----------SFLDAS----PdLVYyrnEDGEFsgcnramELLTGKSEKQLIGLTPKDVY 204
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  485 GPNTDKNAIDIITNAIKTLKTQRIEI-LNYKkDGTEFWNSLQISPVFNEQQQLTAYVGIQQDITEQKaanqlliEAKAAA 563
Cdd:PRK11091  205 SPEAAEKVIETDEKVFRHNVSLTYEQwLDYP-DGRKACFELRKVPFYDRVGKRHGLMGFGRDITERK-------RYQDAL 276
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  564 EQANIAKSEFLAAMSHEIRTPMNGVLGMLNLILDSSLNEKQHHQVSIALNSANSLLNIINDILDFSKVDAGKLELEELEF 643
Cdd:PRK11091  277 EKASRDKTTFISTISHELRTPLNGIVGLSRILLDTELTAEQRKYLKTIHVSAITLGNIFNDIIDMDKMERRKLQLDNQPI 356
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  644 NLCNMLDDFIETIAIHAHSKNIPLMLDIEHLEYAFVIGDAGRLKQILTNLVNNALKFTHKGEV--QVIAKltpiNNNQMR 721
Cdd:PRK11091  357 DFTDFLADLENLSGLQAEQKGLRFDLEPLLPLPHKVITDGTRLRQILWNLISNAVKFTQQGGVtvRVRYE----EGDMLT 432
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  722 FncQVIDSGIGISAAQQAKLFKSFSQV-DSSTTRKYGGTGLGLAIVKKLCHLMEGDIQVQSKENKGSnfsfnvvlkrskn 800
Cdd:PRK11091  433 F--EVEDSGIGIPEDELDKIFAMYYQVkDSHGGKPATGTGIGLAVSKRLAQAMGGDITVTSEEGKGS------------- 497
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  801 pqkvlppvdmsslnilivcsnqtqssilhkqftkwgatavispsakqavqicqqyiekqnlCFdlimidmqlsdgdalTL 880
Cdd:PRK11091  498 -------------------------------------------------------------CF---------------TL 501
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  881 SktldkevdlmaahvvlmttgelnkqrdlyqasrfsaiVTKPIItqnlfkmlstcfsdKQHSNSSLITEDLsdtqPLSSd 960
Cdd:PRK11091  502 T-------------------------------------IHAPAV--------------AEEVEDAFDEDDM----PLPA- 525
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  961 divwdknIRILLVEDNNINQIVASTTLKKIGiNSIDIAENGQHALEYLKQttshNPYSLILMDCQMPVMDGYQATTHIRV 1040
Cdd:PRK11091  526 -------LNILLVEDIELNVIVARSVLEKLG-NSVDVAMTGKEALEMFDP----DEYDLVLLDIQLPDMTGLDIARELRE 593
                         650       660       670       680
                  ....*....|....*....|....*....|....*....|.
gi 503229768 1041 NEAGSKNPPitIIAMTANAMvGDKAKCLQVGMNDYISKPIA 1081
Cdd:PRK11091  594 RYPREDLPP--LVALTANVL-KDKKEYLDAGMDDVLSKPLS 631
HATPase_EvgS-ArcB-TorS-like cd16922
Histidine kinase-like ATPase domain of two-component sensor histidine kinases, many are hybrid ...
686-791 5.09e-52

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: 177.68  E-value: 5.09e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  686 LKQILTNLVNNALKFTHKGEVQVIAKLTPINNNQMRFNCQVIDSGIGISAAQQAKLFKSFSQVDSSTTRKYGGTGLGLAI 765
Cdd:cd16922     1 LRQILLNLLGNAIKFTEEGEVTLRVSLEEEEEDGVQLRFSVEDTGIGIPEEQQARLFEPFSQADSSTTRKYGGTGLGLAI 80
                          90       100
                  ....*....|....*....|....*.
gi 503229768  766 VKKLCHLMEGDIQVQSKENKGSNFSF 791
Cdd:cd16922    81 SKKLVELMGGDISVESEPGQGSTFTF 106
PRK11466 PRK11466
hybrid sensory histidine kinase TorS; Provisional
558-953 1.12e-51

hybrid sensory histidine kinase TorS; Provisional


Pssm-ID: 236914 [Multi-domain]  Cd Length: 914  Bit Score: 197.44  E-value: 1.12e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  558 EAKAAAEQANIAKSEFLAAMSHEIRTPMNGVLGMLNLILDSSLNEKQHHQVSIALNSANSLLNIINDILDFSKVDAGKLE 637
Cdd:PRK11466  432 QARAEAEKASQAKSAFLAAMSHEIRTPLYGILGTAQLLADNPALNAQRDDLRAITDSGESLLTILNDILDYSAIEAGGKN 511
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  638 LEELE--FNLCNMLDDFIETIAIHAHSKNIPLMLDIEHLEYAFVIGDAGRLKQILTNLVNNALKFTHKGEVQVIAKLtpi 715
Cdd:PRK11466  512 VSVSDepFEPRPLLESTLQLMSGRVKGRPIRLATDIADDLPTALMGDPRRIRQVITNLLSNALRFTDEGSIVLRSRT--- 588
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  716 nnNQMRFNCQVIDSGIGISAAQQAKLFKSFSQVdsstTRKYGGTGLGLAIVKKLCHLMEGDIQVQSKENKGSNFSFNVVL 795
Cdd:PRK11466  589 --DGEQWLVEVEDSGCGIDPAKLAEIFQPFVQV----SGKRGGTGLGLTISSRLAQAMGGELSATSTPEVGSCFCLRLPL 662
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  796 KRSKNPQKVLP--PVDMSSLNILIVCSNQTQSSILHKQFTKWGATAVISPSAKQAVQICQqyiekQNLCFDLIMIDMQLS 873
Cdd:PRK11466  663 RVATAPVPKTVnqAVRLDGLRLLLIEDNPLTQRITAEMLNTSGAQVVAVGNAAQALETLQ-----NSEPFAAALVDFDLP 737
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  874 DGDALTLSKTLDKEVDLM-----AAHVVlmttGELNKQRdlyQASRFSAIVTKPIITQNLFKMLSTCFSDKQHSNSSLIT 948
Cdd:PRK11466  738 DYDGITLARQLAQQYPSLvligfSAHVI----DETLRQR---TSSLFRGIIPKPVPREVLGQLLAHYLQLQVNNDQPLDV 810

                  ....*
gi 503229768  949 EDLSD 953
Cdd:PRK11466  811 SQLNE 815
REC_hyHK_CKI1_RcsC-like cd17546
phosphoacceptor receiver (REC) domain of hybrid sensor histidine kinases/response regulators ...
970-1089 2.25e-47

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: 164.56  E-value: 2.25e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  970 ILLVEDNNINQIVASTTLKKIGINsIDIAENGQHALEYLKQttshNPYSLILMDCQMPVMDGYQATTHIRVNEAGSKNPP 1049
Cdd:cd17546     1 VLVVDDNPVNRKVLKKLLEKLGYE-VDVAENGQEALELLKE----EPFDLVLMDLQMPVMDGLEATRRIRELEGGGRRTP 75
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 503229768 1050 ItiIAMTANAMVGDKAKCLQVGMNDYISKPIAQDILFKKL 1089
Cdd:cd17546    76 I--IALTANALEEDREKCLEAGMDDYLSKPVKLDQLKEVL 113
NtrB COG3852
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms];
426-790 4.31e-45

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


Pssm-ID: 443061 [Multi-domain]  Cd Length: 361  Bit Score: 166.95  E-value: 4.31e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  426 QAKEQNDLLAQAIESCNVGISIADAsvQGFpLVFLNSEFEKITGYSKEEMLGINCSLLQGPntDKNAIDIITNAIKTLKT 505
Cdd:COG3852     1 ALRESEELLRAILDSLPDAVIVLDA--DGR-ITYVNPAAERLLGLSAEELLGRPLAELFPE--DSPLRELLERALAEGQP 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  506 QRI-EILNYKKDGTEFWNSLQISPVFNEQQQlTAYVGIQQDITEQKAANQLLIEAkaaaEQANIAKsEFLAAMSHEIRTP 584
Cdd:COG3852    76 VTErEVTLRRKDGEERPVDVSVSPLRDAEGE-GGVLLVLRDITERKRLERELRRA----EKLAAVG-ELAAGLAHEIRNP 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  585 MNGVLGMLNLILDSSLNEKQHHQVSIALNSANSLLNIINDILDFSKVDAGKLELeeleFNLCNMLDDFIETIAiHAHSKN 664
Cdd:COG3852   150 LTGIRGAAQLLERELPDDELREYTQLIIEEADRLNNLVDRLLSFSRPRPPEREP----VNLHEVLERVLELLR-AEAPKN 224
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  665 IplmlDIEhLEYA----FVIGDAGRLKQILTNLVNNALK-FTHKGEVQV---IAKLTPINNNQMRFNCQ--VIDSGIGIS 734
Cdd:COG3852   225 I----RIV-RDYDpslpEVLGDPDQLIQVLLNLVRNAAEaMPEGGTITIrtrVERQVTLGGLRPRLYVRieVIDNGPGIP 299
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 503229768  735 AAQQAKLFKSFsqVdssTTRKyGGTGLGLAIVKKLCHLMEGDIQVQSKENKGSNFS 790
Cdd:COG3852   300 EEILDRIFEPF--F---TTKE-KGTGLGLAIVQKIVEQHGGTIEVESEPGKGTTFR 349
PRK09959 PRK09959
acid-sensing system histidine kinase EvgS;
461-887 2.07e-42

acid-sensing system histidine kinase EvgS;


Pssm-ID: 182169 [Multi-domain]  Cd Length: 1197  Bit Score: 169.14  E-value: 2.07e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  461 NSEFEK--ITGYSKEEMLGINCSllQGPNTD----KNAIDIITNAIKTLKTQRIEILN-YKKDGTEFWNSLQISPVfneq 533
Cdd:PRK09959  602 NSAFEHyfTADYYKNAMLPLENS--DSPFKDvfsnAHEVTAETKENRTIYTQVFEIDNgIEKRCINHWHTLCNLPA---- 675
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  534 QQLTAYVGIQQDITEQKAANQLLIEAKAAAEQANIAKSEFLAAMSHEIRTPMNGVLGMLNLILDSSLNEKQH-HQVSIAL 612
Cdd:PRK09959  676 SDHAVYICGWQDITETRDLIHALEVERNKAINATVAKSQFLATMSHEIRTPISSIMGFLELLSGSGLSKEQRvEAISLAY 755
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  613 NSANSLLNIINDILDFSKVDAGKLELEELEFNLCNMLDDFIETIAIHAHSKNIPLMLDIEHLEYAFVIGDAGRLKQILTN 692
Cdd:PRK09959  756 ATGQSLLGLIGEILDVDKIESGNYQLQPQWVDIPTLVQNTCHSFGAIAASKSIALSCSSTFPDHYLVKIDPQAFKQVLSN 835
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  693 LVNNALKFTHKGEVQVIAKLTPINNNQMRFNCQVIDSGIGISAAQQAKLFKSFSQvdSSTTRKYGGTGLGLAIVKKLCHL 772
Cdd:PRK09959  836 LLSNALKFTTEGAVKITTSLGHIDDNHAVIKMTIMDSGSGLSQEEQQQLFKRYSQ--TSAGRQQTGSGLGLMICKELIKN 913
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  773 MEGDIQVQSKENKGSNFSFNVVLK--------RSKNPQKVLPPvdmSSLNILIVCSNQTQSSILHKQFTKWGATAVISPS 844
Cdd:PRK09959  914 MQGDLSLESHPGIGTTFTITIPVEisqqvatvEAKAEQPITLP---EKLSILIADDHPTNRLLLKRQLNLLGYDVDEATD 990
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....
gi 503229768  845 AKQAV-QICQQYiekqnlcFDLIMIDMQLSDGDALTLSKTLDKE 887
Cdd:PRK09959  991 GVQALhKVSMQH-------YDLLITDVNMPNMDGFELTRKLREQ 1027
COG4251 COG4251
Bacteriophytochrome (light-regulated signal transduction histidine kinase) [Signal ...
411-791 2.42e-42

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


Pssm-ID: 443393 [Multi-domain]  Cd Length: 503  Bit Score: 162.65  E-value: 2.42e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  411 VTDITEQKRSQKALKQAKEQNDLLAQAIESCNVGISIADASVQGFPLVFLNSEFEKITGYSKEEMLGINCSLLQGPNTDK 490
Cdd:COG4251   123 LALLLLLLLLALLLLEELALLRLALALLLLLLLLLLLLLLLLALILALLLAALAELELLLLLLLVLLLLLLLLLLLLLLL 202
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  491 NAIDIITNAIKTLKTQRIEILNYKKDGTEFWNSLQISPVFNEQQQLTAYVGIQQDITEQKAANQLLIEAKAAAEQANIAK 570
Cdd:COG4251   203 LRLLLELLLLLEAELLLSLGGGLGLLLLLLLLLVLLLLLILLLLLLILVLELLELRLELEELEEELEERTAELERSNEEL 282
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  571 SEFLAAMSHEIRTPMNGVLGMLNLILD---SSLNEKQHHQVSIALNSANSLLNIINDILDFSKVdaGKLELEELEFNLCN 647
Cdd:COG4251   283 EQFAYVASHDLREPLRKISGFSQLLEEdygDKLDEEGREYLERIRDAAERMQALIDDLLAYSRV--GRQELEFEPVDLNE 360
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  648 MLDDFIETIAIHAHSKNIplmlDIEHLEYAFVIGDAGRLKQILTNLVNNALKFTHKGEVQVI---AKltpINNNQMRFnc 724
Cdd:COG4251   361 LLEEVLEDLEPRIEERGA----EIEVGPLPTVRGDPTLLRQVFQNLISNAIKYSRPGEPPRIeigAE---REGGEWVF-- 431
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 503229768  725 QVIDSGIGISAAQQAKLFKSFSQVDSSttRKYGGTGLGLAIVKKLCHLMEGDIQVQSKENKGSNFSF 791
Cdd:COG4251   432 SVRDNGIGIDPEYAEKIFEIFQRLHSR--DEYEGTGIGLAIVKKIVERHGGRIWVESEPGEGATFYF 496
CheY COG0784
CheY-like REC (receiver) domain, includes chemotaxis protein CheY and sporulation regulator ...
966-1094 5.71e-41

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: 146.92  E-value: 5.71e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  966 KNIRILLVEDNNINQIVASTTLKKIGINsIDIAENGQHALEYLKQttshNPYSLILMDCQMPVMDGYQATTHIRvneAGS 1045
Cdd:COG0784     4 GGKRILVVDDNPDNRELLRRLLERLGYE-VTTAEDGAEALELLRA----GPPDLILLDINMPGMDGLELLRRIR---ALP 75
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 503229768 1046 KNPPITIIAMTANAMVGDKAKCLQVGMNDYISKPIAQDILFKKLLKWLP 1094
Cdd:COG0784    76 RLPDIPIIALTAYADEEDRERALEAGADDYLTKPVDPEELLEALRRLLA 124
PAS COG2202
PAS domain [Signal transduction mechanisms];
290-556 2.42e-36

PAS domain [Signal transduction mechanisms];


Pssm-ID: 441804 [Multi-domain]  Cd Length: 258  Bit Score: 138.23  E-value: 2.42e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  290 REAIKQSEARYELAVKGSNDGIWDWDIVTNEVYFSPRISVLLGYDENDKNALPHcadalYKLLHPDDITKHKKQIANHLI 369
Cdd:COG2202     3 EEALEESERRLRALVESSPDAIIITDLDGRILYVNPAFERLTGYSAEELLGKTL-----RDLLPPEDDDEFLELLRAALA 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  370 SNIPFNYDYRLKTKSGAYRYFTVKGMALRNEHNKAIRMAGSVTDITEQKRSQKALKQAKEQndlLAQAIESCNVGISIAD 449
Cdd:COG2202    78 GGGVWRGELRNRRKDGSLFWVELSISPVRDEDGEITGFVGIARDITERKRAEEALRESEER---LRLLVENAPDGIFVLD 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  450 ASVQgfpLVFLNSEFEKITGYSKEEMLGINCSLLQGPNTDKNAIDIITNAIKTlKTQRIEILNYKKDGTEFWNSLQISPV 529
Cdd:COG2202   155 LDGR---ILYVNPAAEELLGYSPEELLGKSLLDLLHPEDRERLLELLRRLLEG-GRESYELELRLKDGDGRWVWVEASAV 230
                         250       260
                  ....*....|....*....|....*...
gi 503229768  530 FNE-QQQLTAYVGIQQDITEQKAANQLL 556
Cdd:COG2202   231 PLRdGGEVIGVLGIVRDITERKRAEEAL 258
KinA COG5805
Sporulation sensor histidine kinase A (Stage II sporulation protein SpoIIF/SpoIIJ) [Cell cycle ...
290-790 3.74e-36

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: 144.10  E-value: 3.74e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  290 REAIKQSEaRYELAVKGSNDGIWDWDIVTNEVYFSPRISVLLGYDENDKNALPHCaDALYKLLHPDDITKHKKQIANHLI 369
Cdd:COG5805    27 RMAIEITE-ELETILENLPDAIIAVNREGKVIYINPAMEKLLGYTSEEIIGKTIF-DFLEKEYHYRVKTRIERLQKGYDV 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  370 SNIPFNYdyrlkTKSGAYRYFTVKGMALRNEHNKAIRMAgsVTDITEQKRSQKALKQAKEQNDLLaqaIESCNVGISIAD 449
Cdd:COG5805   105 VMIEQIY-----CKDGELIYVEVKLFPIYNQNGQAAILA--LRDITKKKKIEEILQEQEERLQTL---IENSPDLICVID 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  450 ASVQgfpLVFLNSEFEKITGYSKEEMLGINcSLLQGPNTDKNAIDIITNAIKTLKTQRIEILN-YKKDGTEFWNSLQISP 528
Cdd:COG5805   175 TDGR---ILFINESIERLFGAPREELIGKN-LLELLHPCDKEEFKERIESITEVWQEFIIEREiITKDGRIRYFEAVIVP 250
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  529 VFNEQQQLTAYVGIQQDITEQKAANQLLIEakaaAEQANIAkSEFLAAMSHEIRTPMNGVLGMLNLILDSSlnEKQHHQV 608
Cdd:COG5805   251 LIDTDGSVKGILVILRDITEKKEAEELMAR----SEKLSIA-GQLAAGIAHEIRNPLTSIKGFLQLLQPGI--EDKEEYF 323
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  609 SIALNSANSLLNIINDILDFSKVDAgkleLEELEFNLCNMLDD---FIETIAIhAHSKNIPLmldiEHLEY-AFVIGDAG 684
Cdd:COG5805   324 DIMLSELDRIESIISEFLALAKPQA----VNKEKENINELIQDvvtLLETEAI-LHNIQIRL----ELLDEdPFIYCDEN 394
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  685 RLKQILTNLVNNALKFTHKGEVQVIAklTPINNNQMRFncQVIDSGIGISAAQQAKLFKSFsqvdssTTRKYGGTGLGLA 764
Cdd:COG5805   395 QIKQVFINLIKNAIEAMPNGGTITIH--TEEEDNSVII--RVIDEGIGIPEERLKKLGEPF------FTTKEKGTGLGLM 464
                         490       500
                  ....*....|....*....|....*.
gi 503229768  765 IVKKLCHLMEGDIQVQSKENKGSNFS 790
Cdd:COG5805   465 VSYKIIENHNGTIDIDSKVGKGTTFT 490
NtrY COG5000
Signal transduction histidine kinase NtrY involved in nitrogen fixation and metabolism ...
406-790 4.99e-36

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: 142.02  E-value: 4.99e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  406 RMAGSVTDITEQKRSQKAlkQAKEQNDLLAQAIESCNVGISIADASvqgFPLVFLNSEFEKITGYSKEEMLGincSLLQG 485
Cdd:COG5000    66 ELARAFNRMTDQLKEQRE--ELEERRRYLETILENLPAGVIVLDAD---GRITLANPAAERLLGIPLEELIG---KPLEE 137
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  486 PNTDKNAIDIITNAIKTLKTQRIEILNykkdGTEFWNSLQISPVFNEqqqltAYVGIQQDITEqkaanqLLIEAKAAAEQ 565
Cdd:COG5000   138 LLPELDLAELLREALERGWQEEIELTR----DGRRTLLVRASPLRDD-----GYVIVFDDITE------LLRAERLAAWG 202
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  566 aniaksEFLAAMSHEIR---TPMNGVLGMLNLILDSSL---NEKQHHQVSIALNSANSLLNIINDILDFSKVDAGKLELe 639
Cdd:COG5000   203 ------ELARRIAHEIKnplTPIQLSAERLRRKLADKLeedREDLERALDTIIRQVDRLKRIVDEFLDFARLPEPQLEP- 275
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  640 eleFNLCNMLDDFIETIAIHAHSKNIPLMLDIEHlEYAFVIGDAGRLKQILTNLVNNALKFT-HKGEVQVIAKLtpiNNN 718
Cdd:COG5000   276 ---VDLNELLREVLALYEPALKEKDIRLELDLDP-DLPEVLADRDQLEQVLINLLKNAIEAIeEGGEIEVSTRR---EDG 348
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 503229768  719 QMRFncQVIDSGIGISAAQQAKLFKSFSqvdssTTRKyGGTGLGLAIVKKLCHLMEGDIQVQSKENKGSNFS 790
Cdd:COG5000   349 RVRI--EVSDNGPGIPEEVLERIFEPFF-----TTKP-KGTGLGLAIVKKIVEEHGGTIELESRPGGGTTFT 412
PRK13558 PRK13558
bacterio-opsin activator; Provisional
427-566 1.45e-35

bacterio-opsin activator; Provisional


Pssm-ID: 237426 [Multi-domain]  Cd Length: 665  Bit Score: 144.98  E-value: 1.45e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  427 AKEQNDLLAQAIESCNVGISIADASVQGFPLVFLNSEFEKITGYSKEEMLGINCSLLQGPNTDKNAIDIITNAIKTLKTQ 506
Cdd:PRK13558  143 VESDRRLKERALDEAPVGITIADATLPDEPLIYINDAFERITGYSPDEVLGRNCRFLQGEDTNEERVAELREAIDEERPT 222
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  507 RIEILNYKKDGTEFWNSLQISPVFNEQQQLTAYVGIQQDITEQKAAnqlliEAKAAAEQA 566
Cdd:PRK13558  223 SVELRNYRKDGSTFWNQVDIAPIRDEDGTVTHYVGFQTDVTERKEA-----ELALQRERR 277
phoR_proteo TIGR02966
phosphate regulon sensor kinase PhoR; Members of this protein family are the regulatory ...
523-791 2.09e-34

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: 135.03  E-value: 2.09e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768   523 SLQISPVFNEQQQLTAyvgiqQDITEQKaanQLlieakaaaEQAniaKSEFLAAMSHEIRTPMNGVLGMLNLILDSSLNE 602
Cdd:TIGR02966   86 EIRIAPYGEEQKLLVA-----RDVTRLR---RL--------EQM---RRDFVANVSHELRTPLTVLRGYLETLADGPDED 146
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768   603 KQHHQVSIALNSANS--LLNIINDILDFSKVDAGKLELEELEFNLCNMLDDFIETIAIHAHSKNIPLMLDIEHLeyAFVI 680
Cdd:TIGR02966  147 PEEWNRALEIMLEQSqrMQSLVEDLLTLSRLESAASPLEDEPVDMPALLDHLRDEAEALSQGKNHQITFEIDGG--VDVL 224
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768   681 GDAGRLKQILTNLVNNALKFTHKG-EVQVIAKLTPinnNQMRFNcqVIDSGIGISAAQQAKLFKSFSQVDSSTTRKYGGT 759
Cdd:TIGR02966  225 GDEDELRSAFSNLVSNAIKYTPEGgTITVRWRRDG---GGAEFS--VTDTGIGIAPEHLPRLTERFYRVDKSRSRDTGGT 299
                          250       260       270
                   ....*....|....*....|....*....|..
gi 503229768   760 GLGLAIVKKLCHLMEGDIQVQSKENKGSNFSF 791
Cdd:TIGR02966  300 GLGLAIVKHVLSRHHARLEIESELGKGSTFSF 331
PleD COG3706
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate ...
967-1089 6.23e-33

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: 125.79  E-value: 6.23e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  967 NIRILLVEDNNINQIVASTTLKKIGINsIDIAENGQHALEYLKQttshNPYSLILMDCQMPVMDGYQATTHIRvNEAGSK 1046
Cdd:COG3706     1 PARILVVDDDPTNRKLLRRLLEAAGYE-VVEAADGEEALELLQE----HRPDLILLDLEMPDMDGLELCRRLR-ADPRTA 74
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 503229768 1047 NPPItiIAMTANAMVGDKAKCLQVGMNDYISKPIAQDILFKKL 1089
Cdd:COG3706    75 DIPI--IFLTALDDEEDRARALEAGADDYLTKPFDPEELLARV 115
PAS COG2202
PAS domain [Signal transduction mechanisms];
422-583 5.48e-32

PAS domain [Signal transduction mechanisms];


Pssm-ID: 441804 [Multi-domain]  Cd Length: 258  Bit Score: 125.91  E-value: 5.48e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  422 KALKQAKEQNDLLAQAIESCNVGISIADASvqgFPLVFLNSEFEKITGYSKEEMLGINCSLLQGPNTDKNAIDIITNAIK 501
Cdd:COG2202     1 TAEEALEESERRLRALVESSPDAIIITDLD---GRILYVNPAFERLTGYSAEELLGKTLRDLLPPEDDDEFLELLRAALA 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  502 TLKTQRIEILNYKKDGTEFWNSLQISPVFNEQQQLTAYVGIQQDITEQKAANQLLIEAKAAAEQANIAKSEFLAAMSHEI 581
Cdd:COG2202    78 GGGVWRGELRNRRKDGSLFWVELSISPVRDEDGEITGFVGIARDITERKRAEEALRESEERLRLLVENAPDGIFVLDLDG 157

                  ..
gi 503229768  582 RT 583
Cdd:COG2202   158 RI 159
HATPase_c smart00387
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.
681-791 1.57e-30

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


Pssm-ID: 214643 [Multi-domain]  Cd Length: 111  Bit Score: 116.21  E-value: 1.57e-30
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768    681 GDAGRLKQILTNLVNNALKFTHK-GEVQVIAKLTPinnnqMRFNCQVIDSGIGISAAQQAKLFKSFSQVDSsTTRKYGGT 759
Cdd:smart00387    1 GDPDRLRQVLSNLLDNAIKYTPEgGRITVTLERDG-----DHVEITVEDNGPGIPPEDLEKIFEPFFRTDK-RSRKIGGT 74
                            90       100       110
                    ....*....|....*....|....*....|..
gi 503229768    760 GLGLAIVKKLCHLMEGDIQVQSKENKGSNFSF 791
Cdd:smart00387   75 GLGLSIVKKLVELHGGEISVESEPGGGTTFTI 106
COG4191 COG4191
Signal transduction histidine kinase regulating C4-dicarboxylate transport system [Signal ...
542-791 3.96e-30

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


Pssm-ID: 443345 [Multi-domain]  Cd Length: 361  Bit Score: 123.37  E-value: 3.96e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  542 IQQDITEQKAANQLLIEAKAAAEQAniAKsefLAAM-------SHEIRTPMNGVLGMLNLILDSSLNEKQHHQVSIALNS 614
Cdd:COG4191   112 LERDITELERAEEELRELQEQLVQS--EK---LAALgelaagiAHEINNPLAAILGNAELLRRRLEDEPDPEELREALER 186
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  615 ANSLLN----IINDILDFSKVDAGKLELeeleFNLCNMLDDFIETIAIHAHSKNIPLMLDIEHlEYAFVIGDAGRLKQIL 690
Cdd:COG4191   187 ILEGAEraaeIVRSLRAFSRRDEEEREP----VDLNELIDEALELLRPRLKARGIEVELDLPP-DLPPVLGDPGQLEQVL 261
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  691 TNLVNN---ALKFTHKGEVQVIAKLTpinNNQMRFncQVIDSGIGISAAQQAKLFKSFSqvdssTTRKYG-GTGLGLAIV 766
Cdd:COG4191   262 LNLLINaidAMEEGEGGRITISTRRE---GDYVVI--SVRDNGPGIPPEVLERIFEPFF-----TTKPVGkGTGLGLSIS 331
                         250       260
                  ....*....|....*....|....*
gi 503229768  767 KKLCHLMEGDIQVQSKENKGSNFSF 791
Cdd:COG4191   332 YGIVEKHGGRIEVESEPGGGTTFTI 356
PRK13557 PRK13557
histidine kinase; Provisional
427-867 4.26e-30

histidine kinase; Provisional


Pssm-ID: 237425 [Multi-domain]  Cd Length: 540  Bit Score: 126.32  E-value: 4.26e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  427 AKEQNDLLAQAIESCNVGISIADASVQGFPLVFLNSEFEKITGYSKEEMLGINCSLLQGPNTDKNAIDIITNAIKTLKTQ 506
Cdd:PRK13557   25 SDHRSDIFFAAVETTRMPMIVTDPNQPDNPIVFANRAFLEMTGYAAEEIIGNNCRFLQGPETDRATVAEVRDAIAERREI 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  507 RIEILNYKKDGTEFWNSLQISPVFNEQQQLTAYVGIQQDITEQKAANQLLIEAkaaaeQANIAKSEFLAAMSHE---IRT 583
Cdd:PRK13557  105 ATEILNYRKDGSSFWNALFVSPVYNDAGDLVYFFGSQLDVSRRRDAEDALRQA-----QKMEALGQLTGGIAHDfnnLLQ 179
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  584 PMNGVLGMLNLILDSSLNEKQHHQVSI-----ALNSANSLlniINDILDFSKvdagKLELEELEFNLCNMLDDFIEtIAI 658
Cdd:PRK13557  180 VMSGYLDVIQAALSHPDADRGRMARSVeniraAAERAATL---TQQLLAFAR----KQRLEGRVLNLNGLVSGMGE-LAE 251
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  659 HAHSKNIPLMLDIEHLEYAFVIgDAGRLKQILTNLVNNALK-FTHKGEVQV------IAKLTPINNNQMRFNC----QVI 727
Cdd:PRK13557  252 RTLGDAVTIETDLAPDLWNCRI-DPTQAEVALLNVLINARDaMPEGGRVTIrtrnveIEDEDLAMYHGLPPGRyvsiAVT 330
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  728 DSGIGISAAQQAKLFKSFsqvdsSTTRKYG-GTGLGLAIVKKLCHLMEGDIQVQSKENKGSN--FSFNVVLKRSKNPQKV 804
Cdd:PRK13557  331 DTGSGMPPEILARVMDPF-----FTTKEEGkGTGLGLSMVYGFAKQSGGAVRIYSEVGEGTTvrLYFPASDQAENPEQEP 405
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 503229768  805 -LPPVDM-SSLNILIVcSNQTQSSILHKQFTK-WGATAVISPSAKQAVQICQQYIEKQNLCFDLIM 867
Cdd:PRK13557  406 kARAIDRgGTETILIV-DDRPDVAELARMILEdFGYRTLVASNGREALEILDSHPEVDLLFTDLIM 470
PRK13559 PRK13559
hypothetical protein; Provisional
395-613 3.25e-28

hypothetical protein; Provisional


Pssm-ID: 237427 [Multi-domain]  Cd Length: 361  Bit Score: 117.61  E-value: 3.25e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  395 MALRNEHNKAIRMAGSvTDITEQKRSQKALKQAKEQNDLLAQAIESCNVGISIADASVQGFPLVFLNSEFEKITGYSKEE 474
Cdd:PRK13559    7 EPLHGDLPAASSKAFS-ADRKELAAIHDPRDFRGASGRLFEQAMEQTRMAMCITDPHQPDLPIVLANQAFLDLTGYAAEE 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  475 MLGINCSLLQGPNTDKNAIDIITNAIKTLKTQRIEILNYKKDGTEFWNSLQISPVFNEQQQLTAYVGIQQDITEQKAanq 554
Cdd:PRK13559   86 VVGRNCRFLQGAATDPIAVAKIRAAIAAEREIVVELLNYRKDGEPFWNALHLGPVYGEDGRLLYFFGSQWDVTDIRA--- 162
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 503229768  555 llIEAKAAAEQaniakseflaAMSHEIRTPMNGVLGMLNLILDSSLNEKQHHQVSIALN 613
Cdd:PRK13559  163 --VRALEAHER----------RLAREVDHRSKNVFAVVDSIVRLTGRADDPSLYAAAIQ 209
HATPase cd00075
Histidine kinase-like ATPase domain; This superfamily includes the histidine kinase-like ...
686-791 1.60e-26

Histidine kinase-like ATPase domain; This superfamily includes the histidine kinase-like ATPase (HATPase) domains of several ATP-binding proteins such as histidine kinase, DNA gyrase B, topoisomerases, heat shock protein 90 (HSP90), phytochrome-like ATPases and DNA mismatch repair proteins. Domains belonging to this superfamily are also referred to as GHKL (gyrase, heat-shock protein 90, histidine kinase, MutL) ATPase domains.


Pssm-ID: 340391 [Multi-domain]  Cd Length: 102  Bit Score: 104.61  E-value: 1.60e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  686 LKQILTNLVNNALKFTHK-GEVQVIAKLTPinnNQMRFncQVIDSGIGISAAQQAKLFKSFSQVDSSttRKYGGTGLGLA 764
Cdd:cd00075     1 LEQVLSNLLDNALKYSPPgGTIEISLRQEG---DGVVL--EVEDNGPGIPEEDLERIFERFYRGDKS--REGGGTGLGLA 73
                          90       100
                  ....*....|....*....|....*..
gi 503229768  765 IVKKLCHLMEGDIQVQSKENKGSNFSF 791
Cdd:cd00075    74 IVRRIVEAHGGRITVESEPGGGTTFTV 100
HATPase_c pfam02518
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the ...
681-791 3.72e-26

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


Pssm-ID: 460579 [Multi-domain]  Cd Length: 109  Bit Score: 103.99  E-value: 3.72e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768   681 GDAGRLKQILTNLVNNALKFTHK-GEVQViaKLTPINNNQMRfncqVIDSGIGISAAQQAKLFKSFSQVDSsttRKYGGT 759
Cdd:pfam02518    1 GDELRLRQVLSNLLDNALKHAAKaGEITV--TLSEGGELTLT----VEDNGIGIPPEDLPRIFEPFSTADK---RGGGGT 71
                           90       100       110
                   ....*....|....*....|....*....|..
gi 503229768   760 GLGLAIVKKLCHLMEGDIQVQSKENKGSNFSF 791
Cdd:pfam02518   72 GLGLSIVRKLVELLGGTITVESEPGGGTTVTL 103
PRK11360 PRK11360
two-component system sensor histidine kinase AtoS;
422-791 7.70e-26

two-component system sensor histidine kinase AtoS;


Pssm-ID: 236901 [Multi-domain]  Cd Length: 607  Bit Score: 113.91  E-value: 7.70e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  422 KALKQAKEQNDLLaqaIESCNVGISIADASVQgfpLVFLNSEFEKITGYSKEEMLGINCSLLQGPNTDknAIDIITNAIK 501
Cdd:PRK11360  255 QALRETRSLNELI---LESIADGVIAIDRQGK---ITTMNPAAEVITGLQRHELVGKPYSELFPPNTP--FASPLLDTLE 326
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  502 TLKTQRIEILNYKKDGTEFWNSLQISPVFNEQQQLTAYVGIQQDITEQKAANQLLIEAKAAAeqaniAKSEFLAAMSHEI 581
Cdd:PRK11360  327 HGTEHVDLEISFPGRDRTIELSVSTSLLHNTHGEMIGALVIFSDLTERKRLQRRVARQERLA-----ALGELVAGVAHEI 401
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  582 RTPMNGVLGMLNLILDSSLNEKQHHQVSIALNSANSLLNIINDILDFSKVDAGKLELEElefnlcnmLDDFIETIAI--- 658
Cdd:PRK11360  402 RNPLTAIRGYVQIWRQQTSDPPSQEYLSVVLREVDRLNKVIDQLLEFSRPRESQWQPVS--------LNALVEEVLQlfq 473
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  659 HAHSKN-IPLMLDIEHlEYAFVIGDAGRLKQILTNLVNNALK-FTHKGEVQVIAKLTPiNNNQMrfnCQVIDSGIGISAA 736
Cdd:PRK11360  474 TAGVQArVDFETELDN-ELPPIWADPELLKQVLLNILINAVQaISARGKIRIRTWQYS-DGQVA---VSIEDNGCGIDPE 548
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 503229768  737 QQAKLFKSFsqvdssTTRKYGGTGLGLAIVKKLCHLMEGDIQVQSKENKGSNFSF 791
Cdd:PRK11360  549 LLKKIFDPF------FTTKAKGTGLGLALSQRIINAHGGDIEVESEPGVGTTFTL 597
REC_DivK-like cd17548
phosphoacceptor receiver (REC) domain of DivK and similar proteins; Caulobacter crescentus ...
969-1080 1.53e-25

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: 102.23  E-value: 1.53e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  969 RILLVEDNNINQIVASTTLKKIGINSIDiAENGQHALEYLKQttsHNPySLILMDCQMPVMDGYQATTHIRVNEAGSKnp 1048
Cdd:cd17548     1 KILIVEDNPLNMKLARDLLESAGYEVLE-AADGEEALEIARK---EKP-DLILMDIQLPGMDGLEATRLLKEDPATRD-- 73
                          90       100       110
                  ....*....|....*....|....*....|..
gi 503229768 1049 pITIIAMTANAMVGDKAKCLQVGMNDYISKPI 1080
Cdd:cd17548    74 -IPVIALTAYAMKGDREKILEAGCDGYISKPI 104
phoR PRK11006
phosphate regulon sensor histidine kinase PhoR;
569-791 1.30e-24

phosphate regulon sensor histidine kinase PhoR;


Pssm-ID: 182895 [Multi-domain]  Cd Length: 430  Bit Score: 108.17  E-value: 1.30e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  569 AKSEFLAAMSHEIRTPM---NGVLGMLN-LILDSSLNEKQHHQVSIALNSANSLlniINDILDFSKVDAGKLELEELEFN 644
Cdd:PRK11006  203 ARRNFFANVSHELRTPLtvlQGYLEMMQdQPLEGALREKALHTMREQTQRMEGL---VKQLLTLSKIEAAPTIDLNEKVD 279
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  645 LCNMLDdFIETIAIHAHSKNIPLMLDI-EHLEyafVIGDAGRLKQILTNLVNNALKFTHKG-EVQVIAKLTPinnNQMRF 722
Cdd:PRK11006  280 VPMMLR-VLEREAQTLSQGKHTITFEVdNSLK---VFGNEDQLRSAISNLVYNAVNHTPEGtHITVRWQRVP---QGAEF 352
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 503229768  723 ncQVIDSGIGISAAQQAKLFKSFSQVDSSTTRKYGGTGLGLAIVKKLCHLMEGDIQVQSKENKGSNFSF 791
Cdd:PRK11006  353 --SVEDNGPGIAPEHIPRLTERFYRVDKARSRQTGGSGLGLAIVKHALSHHDSRLEIESEVGKGTRFSF 419
Response_reg pfam00072
Response regulator receiver domain; This domain receives the signal from the sensor partner in ...
970-1089 4.28e-24

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: 97.99  E-value: 4.28e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768   970 ILLVEDNNINQIVASTTLKKIGINsIDIAENGQHALEYLKQttshNPYSLILMDCQMPVMDGYQATTHIRvneagSKNPP 1049
Cdd:pfam00072    1 VLIVDDDPLIRELLRQLLEKEGYV-VAEADDGKEALELLKE----ERPDLILLDINMPGMDGLELLKRIR-----RRDPT 70
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 503229768  1050 ITIIAMTANAMVGDKAKCLQVGMNDYISKPIAQDILFKKL 1089
Cdd:pfam00072   71 TPVIILTAHGDEDDAVEALEAGADDFLSKPFDPDELLAAI 110
RpfG COG3437
Response regulator c-di-GMP phosphodiesterase, RpfG family, contains REC and HD-GYP domains ...
965-1093 1.70e-23

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: 100.24  E-value: 1.70e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  965 DKNIRILLVEDNNINQIVASTTLKKIGINsIDIAENGQHALEYLKQttshNPYSLILMDCQMPVMDGYQATTHIRVNEAG 1044
Cdd:COG3437     4 GQAPTVLIVDDDPENLELLRQLLRTLGYD-VVTAESGEEALELLLE----APPDLILLDVRMPGMDGFELLRLLRADPST 78
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 503229768 1045 SKnppITIIAMTANAMVGDKAKCLQVGMNDYISKPIAQDILFKKLLKWL 1093
Cdd:COG3437    79 RD---IPVIFLTALADPEDRERALEAGADDYLTKPFDPEELLARVRNAL 124
OmpR COG0745
DNA-binding response regulator, OmpR family, contains REC and winged-helix (wHTH) domain ...
969-1085 3.65e-23

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: 98.49  E-value: 3.65e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  969 RILLVEDN-NINQIVASTtLKKIGInSIDIAENGQHALEYLKQttshNPYSLILMDCQMPVMDGYQATTHIRvneagSKN 1047
Cdd:COG0745     3 RILVVEDDpDIRELLADA-LEREGY-EVDTAADGEEALELLEE----ERPDLILLDLMLPGMDGLEVCRRLR-----ARP 71
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 503229768 1048 PPITIIAMTANAMVGDKAKCLQVGMNDYISKPIAQDIL 1085
Cdd:COG0745    72 SDIPIIMLTARDDEEDRVRGLEAGADDYLTKPFDPEEL 109
BaeS_SmeS NF012163
sensor histidine kinase efflux regulator BaeS;
553-777 4.34e-21

sensor histidine kinase efflux regulator BaeS;


Pssm-ID: 411086 [Multi-domain]  Cd Length: 457  Bit Score: 97.98  E-value: 4.34e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  553 NQLlieaKAAAEQANIAKSEFLAAMSHEIRTPMNGVLGMLNLILDSSLNEKQHHQVSIaLNSANSLLNIINDILDFSKVD 632
Cdd:NF012163  227 NQL----ASTLEKNEQMRRDFMADISHELRTPLAVLRAELEAIQDGIRKFTPESLDSL-QAEVGTLTKLVDDLHDLSMSD 301
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  633 AGKLELEELEFNLCNMLDDFIETIAIHAHSKNIPLMLDIEhlEYAFVIGDAGRLKQILTNLVNNALKFTHK-GEVQVIAK 711
Cdd:NF012163  302 EGALAYQKASVDLVPLLEVEGGAFRERFASAGLELEVSLP--DSSLVFGDRDRLMQLFNNLLENSLRYTDSgGSLHISAS 379
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 503229768  712 LTPinnnQMRFnCQVIDSGIGISAAQQAKLFKSFSQVDSSTTRKYGGTGLGLAIVKKLCHLMEGDI 777
Cdd:NF012163  380 QRP----KEVT-LTVADSAPGVSDEQLARLFERFYRVEVSRNRASGGSGLGLAISLNIVQAHGGTL 440
REC cd00156
phosphoacceptor receiver (REC) domain of response regulators (RRs) and pseudo response ...
971-1079 7.35e-20

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: 85.36  E-value: 7.35e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  971 LLVEDNNINQIVASTTLKKIGINsIDIAENGQHALEYLKQttshNPYSLILMDCQMPVMDGYQATTHIRvneagSKNPPI 1050
Cdd:cd00156     1 LIVDDDPAIRELLKSLLEREGYE-VDTAADGEEALELLRE----ERPDLVLLDLMMPGMDGLELLRKLR-----ELPPDI 70
                          90       100
                  ....*....|....*....|....*....
gi 503229768 1051 TIIAMTANAMVGDKAKCLQVGMNDYISKP 1079
Cdd:cd00156    71 PVIVLTAKADEEDAVRALELGADDYLVKP 99
REC_OmpR cd17574
phosphoacceptor receiver (REC) domain of OmpR family response regulators; OmpR-like proteins ...
971-1079 9.43e-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: 85.15  E-value: 9.43e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  971 LLVEDN-NINQIVaSTTLKKIGINsIDIAENGQHALEYLKQttshNPYSLILMDCQMPVMDGYQATTHIRvneagSKNPP 1049
Cdd:cd17574     1 LVVEDDeEIAELL-SDYLEKEGYE-VDTAADGEEALELARE----EQPDLIILDVMLPGMDGFEVCRRLR-----EKGSD 69
                          90       100       110
                  ....*....|....*....|....*....|
gi 503229768 1050 ITIIAMTANAMVGDKAKCLQVGMNDYISKP 1079
Cdd:cd17574    70 IPIIMLTAKDEEEDKVLGLELGADDYITKP 99
REC_ETR-like cd19933
phosphoacceptor receiver (REC) domain of plant ethylene receptors ETR1, ETR2, and EIN4, and ...
968-1089 2.14e-19

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


Pssm-ID: 381160 [Multi-domain]  Cd Length: 117  Bit Score: 84.76  E-value: 2.14e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  968 IRILLVEDNNINQIVASTTLKKIGINsIDIAENGQHALEYLKQTTShnPYSLILMDCQMPVMDGYQATTHIRvNEAGSKN 1047
Cdd:cd19933     1 LKVLLVDDNAVNRMVTKGLLEKLGCE-VTTVSSGEECLNLLASAEH--SFQLVLLDLCMPEMDGFEVALRIR-KLFGRRE 76
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 503229768 1048 PPItIIAMTANAMVGDKAKCLQVGMNDYISKPIAQDILFKKL 1089
Cdd:cd19933    77 RPL-IVALTANTDDSTREKCLSLGMNGVITKPVSLHALGDEL 117
HisKA pfam00512
His Kinase A (phospho-acceptor) domain; dimerization and phospho-acceptor domain of histidine ...
569-634 2.35e-19

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


Pssm-ID: 459839 [Multi-domain]  Cd Length: 66  Bit Score: 83.03  E-value: 2.35e-19
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 503229768   569 AKSEFLAAMSHEIRTPMNGVLGMLNLILDSSLNEKQHHQVSIALNSANSLLNIINDILDFSKVDAG 634
Cdd:pfam00512    1 AKSEFLANLSHELRTPLTAIRGYLELLRDEKLDEEQREYLETILRSAERLLRLINDLLDLSRIEAG 66
HisKA smart00388
His Kinase A (phosphoacceptor) domain; Dimerisation and phosphoacceptor domain of histidine ...
569-634 3.76e-19

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


Pssm-ID: 214644 [Multi-domain]  Cd Length: 66  Bit Score: 82.23  E-value: 3.76e-19
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 503229768    569 AKSEFLAAMSHEIRTPMNGVLGMLNLILDSSLNEKQHHQVSIALNSANSLLNIINDILDFSKVDAG 634
Cdd:smart00388    1 AKREFLANLSHELRTPLTAIRGYLELLLDTELSEEQREYLETILREAERLLRLINDLLDLSRIEAG 66
CitB COG4565
DNA-binding response regulator DpiB of citrate/malate metabolism [Transcription, Signal ...
966-1095 5.90e-19

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


Pssm-ID: 443622 [Multi-domain]  Cd Length: 138  Bit Score: 84.25  E-value: 5.90e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  966 KNIRILLVEDNNINQIVASTTLKKI-GINSIDIAENGQHALEYLKQttshNPYSLILMDCQMPVMDGYQATTHIRvneag 1044
Cdd:COG4565     2 KMIRVLIVEDDPMVAELLRRYLERLpGFEVVGVASSGEEALALLAE----HRPDLILLDIYLPDGDGLELLRELR----- 72
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 503229768 1045 SKNPPITIIAMTANAMVGDKAKCLQVGMNDYISKPIAQDILFKKLLKWLPY 1095
Cdd:COG4565    73 ARGPDVDVIVITAARDPETVREALRAGVVDYLIKPFTFERLREALERYLEY 123
YesN COG4753
Two-component response regulator, YesN/AraC family, consists of REC and AraC-type DNA-binding ...
969-1079 1.38e-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: 82.13  E-value: 1.38e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  969 RILLVEDNNINQIVASTTLKKI-GINSIDIAENGQHALEYLKQttshNPYSLILMDCQMPVMDGYQATTHIRvneagSKN 1047
Cdd:COG4753     1 KVLIVDDEPLIREGLKRILEWEaGFEVVGEAENGEEALELLEE----HKPDLVITDINMPGMDGLELLEAIR-----ELD 71
                          90       100       110
                  ....*....|....*....|....*....|..
gi 503229768 1048 PPITIIAMTANAMVGDKAKCLQVGMNDYISKP 1079
Cdd:COG4753    72 PDTKIIILSGYSDFEYAQEAIKLGADDYLLKP 103
PRK10549 PRK10549
two-component system sensor histidine kinase BaeS;
573-765 8.26e-18

two-component system sensor histidine kinase BaeS;


Pssm-ID: 182539 [Multi-domain]  Cd Length: 466  Bit Score: 87.77  E-value: 8.26e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  573 FLAAMSHEIRTPMNGVLGMLNLILD-------SSLNEKQHhQVSIalnsansLLNIINDILDFSKVDAGKLELEELEFNL 645
Cdd:PRK10549  243 FMADISHELRTPLAVLRGELEAIQDgvrkftpESVASLQA-EVGT-------LTKLVDDLHQLSLSDEGALAYRKTPVDL 314
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  646 CNMLDdfietIAIHA-----HSKNIPLMLDIEhlEYAFVIGDAGRLKQILTNLVNNALKFTHK-GEVQVIAKLTPiNNNQ 719
Cdd:PRK10549  315 VPLLE-----VAGGAfrerfASRGLTLQLSLP--DSATVFGDPDRLMQLFNNLLENSLRYTDSgGSLHISAEQRD-KTLR 386
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 503229768  720 MRFncqvIDSGIGISAAQQAKLFKSFSQVDSSTTRKYGGTGLGLAI 765
Cdd:PRK10549  387 LTF----ADSAPGVSDEQLQKLFERFYRTEGSRNRASGGSGLGLAI 428
HATPase_FilI-like cd16921
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
686-791 8.85e-18

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: 79.68  E-value: 8.85e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  686 LKQILTNLVNNALKFTHKGEVQVIAKLTPINNNQMRFncQVIDSGIGISAAQQAKLFKSFSQVDSSTtrKYGGTGLGLAI 765
Cdd:cd16921     1 LGQVLTNLLGNAIKFRRPRRPPRIEVGAEDVGEEWTF--YVRDNGIGIDPEYAEKVFGIFQRLHSRE--EYEGTGVGLAI 76
                          90       100
                  ....*....|....*....|....*.
gi 503229768  766 VKKLCHLMEGDIQVQSKENKGSNFSF 791
Cdd:cd16921    77 VRKIIERHGGRIWLESEPGEGTTFYF 102
HATPase_TutC-TodS-like cd16925
Histidine kinase-like ATPase domain of hybrid sensor histidine kinases similar to Pseudomonas ...
682-789 1.03e-17

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: 79.84  E-value: 1.03e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  682 DAGRLKQILTNLVNNALKFT-HKGEVQVIAKLTPINnnqmRFNCQVIDSGIGISAAQQAKLFKSFSQVDSSTTRKYGGTG 760
Cdd:cd16925     1 DAEKYERVVLNLLSNAFKFTpDGGRIRCILEKFRLN----RFLLTVSDSGPGIPPNLREEIFERFRQGDGSSTRAHGGTG 76
                          90       100
                  ....*....|....*....|....*....
gi 503229768  761 LGLAIVKKLCHLMEGDIQVQSKENKGSNF 789
Cdd:cd16925    77 LGLSIVKEFVELHGGTVTVSDAPGGGALF 105
HATPase_BaeS-like cd16946
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
682-777 1.33e-17

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: 79.43  E-value: 1.33e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  682 DAGRLKQILTNLVNNALKFTHKG-EVQVIAKLTPinnNQMRFNcqVIDSGIGISAAQQAKLFKSFSQVDSSTTRKYGGTG 760
Cdd:cd16946     1 DRDRLQQLFVNLLENSLRYTDTGgKLRIRAAQTP---QEVRLD--VEDSAPGVSDDQLARLFERFYRVESSRNRASGGSG 75
                          90
                  ....*....|....*..
gi 503229768  761 LGLAIVKKLCHLMEGDI 777
Cdd:cd16946    76 LGLAICHNIALAHGGTI 92
PRK10604 PRK10604
sensor protein RstB; Provisional
565-792 1.75e-17

sensor protein RstB; Provisional


Pssm-ID: 236724 [Multi-domain]  Cd Length: 433  Bit Score: 86.58  E-value: 1.75e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  565 QANIA-KSEFLAAMSHEIRTPmngvLGMLNLILDSSLNEKQHHQVsiALNSANSLLN-IINDILDFSKVDAGKLELEELE 642
Cdd:PRK10604  206 NALIAsKKQLIDGIAHELRTP----LVRLRYRLEMSDNLSAAESQ--ALNRDIGQLEaLIEELLTYARLDRPQNELHLSE 279
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  643 FNLCNMLDDFIETIAIHAHSKNIplMLDIEHLEyAFVIGDAGRLKQILTNLVNNALKFTHkGEVQVIAKLtpinnNQMRF 722
Cdd:PRK10604  280 PDLPAWLSTHLADIQAVTPEKTV--RLDTPHQG-DYGALDMRLMERVLDNLLNNALRYAH-SRVRVSLLL-----DGNQA 350
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  723 NCQVIDSGIGISAAQQAKLFKSFSQVDSSTTRKYGGTGLGLAIVKKLCHLMEGDIQVQSKENKGSNFSFN 792
Cdd:PRK10604  351 CLIVEDDGPGIPPEERERVFEPFVRLDPSRDRATGGCGLGLAIVHSIALAMGGSVNCDESELGGARFSFS 420
REC_PA4781-like cd19920
phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase PA4781 and similar ...
970-1080 8.08e-17

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: 76.78  E-value: 8.08e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  970 ILLVEDNNINQIVASTTLKKIGInSIDIAENGQHALEYLKQttshNPYSLILMDCQMPVMDGYQATTHIRVNEAGSKnpp 1049
Cdd:cd19920     1 ILIVDDVPDNLRLLSELLRAAGY-RVLVATDGQQALQRAQA----EPPDLILLDVMMPGMDGFEVCRRLKADPATRH--- 72
                          90       100       110
                  ....*....|....*....|....*....|.
gi 503229768 1050 ITIIAMTANAMVGDKAKCLQVGMNDYISKPI 1080
Cdd:cd19920    73 IPVIFLTALTDTEDKVKGFELGAVDYITKPF 103
PRK11100 PRK11100
sensory histidine kinase CreC; Provisional
576-786 9.35e-17

sensory histidine kinase CreC; Provisional


Pssm-ID: 236846 [Multi-domain]  Cd Length: 475  Bit Score: 84.51  E-value: 9.35e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  576 AMSHEIRTPMNGVLGMLNLILDSSLNEKQHHQVSIALNSANSLLNIINDILDFSKVDAGKLELEELEFNLCNMLDDFIET 655
Cdd:PRK11100  262 TLTHELKSPLAAIRGAAELLQEDPPPEDRARFTGNILTQSARLQQLIDRLLELARLEQRQELEVLEPVALAALLEELVEA 341
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  656 IAIHAHSKNIPLMLDIEHLEyafVIGDAGRLKQILTNLVNNALKFTH-KGEVQVIAKLTpinNNQMRFncQVIDSGIGIS 734
Cdd:PRK11100  342 REAQAAAKGITLRLRPDDAR---VLGDPFLLRQALGNLLDNAIDFSPeGGTITLSAEVD---GEQVAL--SVEDQGPGIP 413
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 503229768  735 AAQQAKLF-KSFSQVDSSTTRKygGTGLGLAIVKKLCHLMEGDIQVQSKENKG 786
Cdd:PRK11100  414 DYALPRIFeRFYSLPRPANGRK--STGLGLAFVREVARLHGGEVTLRNRPEGG 464
PAS_9 pfam13426
PAS domain; This domain is found in many signalling proteins in which it functions as a sensor ...
455-548 1.15e-16

PAS domain; This domain is found in many signalling proteins in which it functions as a sensor domain. It recognizes FMN, Zn(II), FAD and riboflavin (MAtilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).


Pssm-ID: 463873 [Multi-domain]  Cd Length: 93  Bit Score: 76.35  E-value: 1.15e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768   455 FPLVFLNSEFEKITGYSKEEMLGINCSLLQGpntDKNAIDIITNAIKTLKTQR-IEILNYKKDGTEFWNSLQISPVFNEQ 533
Cdd:pfam13426    2 GRIIYVNDAALRLLGYTREELLGKSITDLFA---EPEDSERLREALREGKAVReFEVVLYRKDGEPFPVLVSLAPIRDDG 78
                           90
                   ....*....|....*
gi 503229768   534 QQLTAYVGIQQDITE 548
Cdd:pfam13426   79 GELVGIIAILRDITE 93
REC_CheY_CheY3 cd19923
phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY3 and similar CheY ...
968-1091 1.63e-16

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: 76.61  E-value: 1.63e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  968 IRILLVEDNNINQIVASTTLKKIGINSIDIAENGQHALEYLKqttsHNPYSLILMDCQMPVMDGYQATTHIRVNEAGSKN 1047
Cdd:cd19923     1 MKVLVVDDFSTMRRIIKNLLKELGFNNVEEAEDGVDALEKLK----AGGFDFVITDWNMPNMDGLELLKTIRADGALSHL 76
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 503229768 1048 PpitIIAMTANAMVGDKAKCLQVGMNDYISKPIAQDILFKKLLK 1091
Cdd:cd19923    77 P---VLMVTAEAKKENVIAAAQAGVNNYIVKPFTAATLKEKLEK 117
PRK09776 PRK09776
putative diguanylate cyclase; Provisional
280-478 1.85e-16

putative diguanylate cyclase; Provisional


Pssm-ID: 182070 [Multi-domain]  Cd Length: 1092  Bit Score: 85.11  E-value: 1.85e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  280 LNPFKLLESSREaiKQSEaRYELAVKGSNDGIWDWDIVTNEVYFSPRISVLLGYDENDKNALphcaDALYKLLHPDDITK 359
Cdd:PRK09776  395 INELKRTEQVNE--RLME-RITLANEAGGIGIWEWDLKPNIISWDKRMFELYEIPPHIKPTW----QVWYACLHPEDRQR 467
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  360 HKKQIANHLISNIPFNYDYRLKTKSGAyRYFTVKGMALRNEHNKAIRMAGSVTDITEQKRSQKALKQAKEQNDLLAQaie 439
Cdd:PRK09776  468 VEKEIRDALQGRSPFKLEFRIVVKDGV-RHIRALANRVLNKDGEVERLLGINMDMTEVRQLNEALFQEKERLHITLD--- 543
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 503229768  440 scnvgiSIADASV---QGFPLVFLNSEFEKITGYSKEEMLGI 478
Cdd:PRK09776  544 ------SIGEAVVctdMAMKVTFMNPVAEKMTGWTQEEALGV 579
REC_2_DhkD-like cd17580
second phosphoacceptor receiver (REC) domain of Dictyostelium discoideum hybrid signal ...
970-1089 3.15e-16

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: 75.57  E-value: 3.15e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  970 ILLVEDNNINQIVASTTLKKIGiNSIDIAENGQHALEYLKqttsHNPYSLILMDCQMPVMDGYQATTHIRVNEAGSKnpp 1049
Cdd:cd17580     1 ILVVDDNEDAAEMLALLLELEG-AEVTTAHSGEEALEAAQ----RFRPDVILSDIGMPGMDGYELARRLRELPWLAN--- 72
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 503229768 1050 ITIIAMTANAMVGDKAKCLQVGMNDYISKPIAQDILFKKL 1089
Cdd:cd17580    73 TPAIALTGYGQPEDRERALEAGFDAHLVKPVDPDELIELI 112
AtoC COG2204
DNA-binding transcriptional response regulator, NtrC family, contains REC, AAA-type ATPase, ...
966-1089 7.11e-16

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: 81.16  E-value: 7.11e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  966 KNIRILLVEDNNINQIVASTTLKKIGINsIDIAENGQHALEYLKQttshNPYSLILMDCQMPVMDGYQATTHIRvneagS 1045
Cdd:COG2204     1 SMARILVVDDDPDIRRLLKELLERAGYE-VETAASGEEALALLRE----EPPDLVLLDLRMPGMDGLELLRELR-----A 70
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 503229768 1046 KNPPITIIAMTANAMVGDKAKCLQVGMNDYISKPIAQDILFKKL 1089
Cdd:COG2204    71 LDPDLPVILLTGYGDVETAVEAIKAGAFDYLTKPFDLEELLAAV 114
REC_Rcp-like cd17557
phosphoacceptor receiver (REC) domain of cyanobacterial phytochrome response regulator Rcp and ...
969-1080 7.40e-16

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: 75.15  E-value: 7.40e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  969 RILLVEDNNINQIVASTTLKKIGI-NSIDIAENGQHALEYLKQTTSHNPYS---LILMDCQMPVMDGYQATTHIRVNEAG 1044
Cdd:cd17557     1 TILLVEDNPGDAELIQEAFKEAGVpNELHVVRDGEEALDFLRGEGEYADAPrpdLILLDLNMPRMDGFEVLREIKADPDL 80
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 503229768 1045 SKnppITIIAMTANAMVGDKAKCLQVGMNDYISKPI 1080
Cdd:cd17557    81 RR---IPVVVLTTSDAEEDIERAYELGANSYIVKPV 113
cztS_silS_copS TIGR01386
heavy metal sensor kinase; Members of this family contain a sensor histidine kinase domain ...
564-781 8.79e-16

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: 81.28  E-value: 8.79e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768   564 EQANIAKSEFLAAMSHEIRTPMNGVLGMLNLILdSSLNEKQHHQVSIA--LNSANSLLNIINDILDFSKVDAGKLELEEL 641
Cdd:TIGR01386  235 EDAFQRLSQFSADLAHELRTPLTNLLGQTQVAL-SQPRTGEEYREVLEsnLEELERLSRMVSDMLFLARADNGQLALERV 313
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768   642 EFNLCNMLDDFIETIAIHAHSKNIPLMLDIEhleyAFVIGDAGRLKQILTNLVNNALKFTHKGEVQVIAkltpINNNQMR 721
Cdd:TIGR01386  314 RLDLAAELAKVAEYFEPLAEERGVRIRVEGE----GLVRGDPQMFRRAISNLLSNALRHTPDGGTITVR----IERRSDE 385
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768   722 FNCQVIDSGIGISAAQQAKLFKSFSQVDSSTTRKYGGTGLGLAIVKKLCHLMEGDIQVQS 781
Cdd:TIGR01386  386 VRVSVSNPGPGIPPEHLSRLFDRFYRVDPARSNSGEGTGLGLAIVRSIMEAHGGRASAES 445
HATPase_RstB-like cd16939
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
686-791 1.44e-15

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: 73.62  E-value: 1.44e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  686 LKQILTNLVNNALKFTHKgEVQVIAKLtpiNNNQMRFncQVIDSGIGISAAQQAKLFKSFSQVDSSTTRKYGGTGLGLAI 765
Cdd:cd16939     1 MARALDNLLRNALRYAHR-TVRIALLV---SGGRLTL--IVEDDGPGIPAAARERVFEPFVRLDPSRDRATGGFGLGLAI 74
                          90       100
                  ....*....|....*....|....*.
gi 503229768  766 VKKLCHLMEGDIQVQSKENKGSNFSF 791
Cdd:cd16939    75 VHRVALWHGGHVECDDSELGGACFRL 100
PRK09835 PRK09835
Cu(+)/Ag(+) sensor histidine kinase;
570-781 2.07e-15

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


Pssm-ID: 182101 [Multi-domain]  Cd Length: 482  Bit Score: 80.20  E-value: 2.07e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  570 KSEFLAAMSHEIRTPMNGVLGMLNLILDSSLNEKQHHQVSIA-LNSANSLLNIINDILDFSKVDAGKLELEELEFNLCNM 648
Cdd:PRK09835  262 QSNFSADIAHEIRTPITNLITQTEIALSQSRSQKELEDVLYSnLEELTRMAKMVSDMLFLAQADNNQLIPEKKMLDLADE 341
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  649 LDDFIETIAIHAHSKNIPLMLDIEHleyAFVIGDAGRLKQILTNLVNNALKFTHKGEvQVIAKLTPINNNqmrfnCQVI- 727
Cdd:PRK09835  342 VGKVFDFFEAWAEERGVELRFVGDP---CQVAGDPLMLRRAISNLLSNALRYTPAGE-AITVRCQEVDHQ-----VQLVv 412
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 503229768  728 -DSGIGISAAQQAKLFKSFSQVDSSTTRKYGGTGLGLAIVKKLCHLMEGDIQVQS 781
Cdd:PRK09835  413 eNPGTPIAPEHLPRLFDRFYRVDPSRQRKGEGSGIGLAIVKSIVVAHKGTVAVTS 467
REC_D1_PleD-like cd17538
first (D1) phosphoacceptor receiver (REC) domain of response regulator PleD and similar ...
969-1080 2.81e-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: 72.53  E-value: 2.81e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  969 RILLVEDNNINQIVASTTLKKIGINSIdIAENGQHALEYLKQttsHNPySLILMDCQMPVMDGYQATTHIRVNEAgskNP 1048
Cdd:cd17538     1 KILVVDDEPANRELLEALLSAEGYEVL-TADSGQEALALAEE---ELP-DLILLDVMMPGMDGFEVCRRLKEDPE---TR 72
                          90       100       110
                  ....*....|....*....|....*....|..
gi 503229768 1049 PITIIAMTANAMVGDKAKCLQVGMNDYISKPI 1080
Cdd:cd17538    73 HIPVIMITALDDREDRIRGLEAGADDFLSKPI 104
PRK10490 PRK10490
sensor protein KdpD; Provisional
532-796 1.09e-14

sensor protein KdpD; Provisional


Pssm-ID: 236701 [Multi-domain]  Cd Length: 895  Bit Score: 78.92  E-value: 1.09e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  532 EQQQL-TAYVGIQQDITEQKAANQLLIEAKAAAEQANIAKSeFLAAMSHEIRTPMNGVLG-----MLNLILDSSLNEKQH 605
Cdd:PRK10490  626 EQQRLlETFTLLIANALERLTLTASEEQARLASEREQLRNA-LLAALSHDLRTPLTVLFGqaeilTLDLASEGSPHARQA 704
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  606 HQVSIALNSANSLlniINDILDFSKVDAGKleleeleFNL---CNMLDDFIET------IAIHAHskniPLMLDIEHlEY 676
Cdd:PRK10490  705 SEIRQQVLNTTRL---VNNLLDMARIQSGG-------FNLrkeWLTLEEVVGSalqmlePGLSGH----PINLSLPE-PL 769
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  677 AFVIGDAGRLKQILTNLVNNALKFThkGEVQVIAKLTPINNNQMRFncQVIDSGIGISAAQQAKLFKSFSQVDSSTTrkY 756
Cdd:PRK10490  770 TLIHVDGPLFERVLINLLENAVKYA--GAQAEIGIDAHVEGERLQL--DVWDNGPGIPPGQEQLIFDKFARGNKESA--I 843
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 503229768  757 GGTGLGLAIVKKLCHLMEGDIQVQSKENKGSNFSFNVVLK 796
Cdd:PRK10490  844 PGVGLGLAICRAIVEVHGGTIWAENRPEGGACFRVTLPLE 883
HisKA cd00082
Histidine Kinase A (dimerization/phosphoacceptor) domain; Histidine Kinase A dimers are formed ...
569-630 1.17e-14

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: 69.55  E-value: 1.17e-14
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 503229768  569 AKSEFLAAMSHEIRTPMNGVLGMLNLILDSSL-NEKQHHQVSIALNSANSLLNIINDILDFSK 630
Cdd:cd00082     3 AKGEFLANVSHELRTPLTAIRGALELLEEELLdDEEQREYLERIREEAERLLRLINDLLDLSR 65
sensory_box TIGR00229
PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain ...
432-556 1.43e-14

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


Pssm-ID: 272971 [Multi-domain]  Cd Length: 124  Bit Score: 71.17  E-value: 1.43e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768   432 DLLAQAIESCNVGISIADasVQGFpLVFLNSEFEKITGYSKEEMLGINCS-LLQGPNTDKNAIDIITNAIKTLKTQRIEI 510
Cdd:TIGR00229    3 ERYRAIFESSPDAIIVID--LEGN-ILYVNPAFEEIFGYSAEELIGRNVLeLIPEEDREEVRERIERRLEGEPEPVSEER 79
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 503229768   511 LNYKKDGTEFWNSLQISPVFnEQQQLTAYVGIQQDITEQKAANQLL 556
Cdd:TIGR00229   80 RVRRKDGSEIWVEVSVSPIR-TNGGELGVVGIVRDITERKEAEEAL 124
HATPase_EnvZ-like cd16950
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
686-786 2.03e-14

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: 70.17  E-value: 2.03e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  686 LKQILTNLVNNALKFThKGEVQViakLTPINNNQMRFncQVIDSGIGISAAQQAKLFKSFSQVDSSttRKYGGTGLGLAI 765
Cdd:cd16950     1 LKRVLSNLVDNALRYG-GGWVEV---SSDGEGNRTRI--QVLDNGPGIAPEEVDELFQPFYRGDNA--RGTSGTGLGLAI 72
                          90       100
                  ....*....|....*....|.
gi 503229768  766 VKKLCHLMEGDIQVQSKENKG 786
Cdd:cd16950    73 VQRISDAHGGSLTLANRAGGG 93
REC_RpfG-like cd17551
phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase response regulator ...
969-1080 2.15e-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: 70.55  E-value: 2.15e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  969 RILLVEDNNINQIVASTTLKKIGINSIDIAENGQHALEYLKqttsHNPYSLILMDCQMPVMDGYQATTHIRVNEAGSkNP 1048
Cdd:cd17551     2 RILIVDDNPTNLLLLEALLRSAGYLEVVSFTDPREALAWCR----ENPPDLILLDYMMPGMDGLEFIRRLRALPGLE-DV 76
                          90       100       110
                  ....*....|....*....|....*....|..
gi 503229768 1049 PITIIamTANAMVGDKAKCLQVGMNDYISKPI 1080
Cdd:cd17551    77 PIVMI--TADTDREVRLRALEAGATDFLTKPF 106
PAS_3 pfam08447
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
320-411 3.85e-14

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


Pssm-ID: 430001 [Multi-domain]  Cd Length: 89  Bit Score: 68.90  E-value: 3.85e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768   320 EVYFSPRISVLLGYDENDknaLPHCADALYKLLHPDDITKHKKQIANHLISNIPFNYDYRLKTKSGAYRYFTVKGMALRN 399
Cdd:pfam08447    1 IIYWSPRFEEILGYTPEE---LLGKGESWLDLVHPDDRERVREALWEALKGGEPYSGEYRIRRKDGEYRWVEARARPIRD 77
                           90
                   ....*....|..
gi 503229768   400 EHNKAIRMAGSV 411
Cdd:pfam08447   78 ENGKPVRVIGVA 89
REC_CheV-like cd19924
phosphoacceptor receiver (REC) domain of chemotaxis protein CheV and similar proteins; This ...
970-1079 3.91e-14

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: 69.71  E-value: 3.91e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  970 ILLVEDNNINQIVASTTLKKIGINsIDIAENGQHALEYLKQTTS-----HNPYSLILMDCQMPVMDGYQATTHIRVNEAG 1044
Cdd:cd19924     1 ILVVDDSPTARKQLRDLLKNLGFE-IAEAVDGEEALNKLENLAKegndlSKELDLIITDIEMPKMDGYELTFELRDDPRL 79
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 503229768 1045 SKNPpitIIAMTANAMVGDKAKCLQVGMNDYISKP 1079
Cdd:cd19924    80 ANIP---VILNSSLSGEFSRARGKKVGADAYLAKF 111
Spo0F COG5803
Stage 0 sporulation initiation response regulator Spo0F [Cell cycle control, cell division, ...
962-1079 1.06e-13

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: 68.67  E-value: 1.06e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  962 IVWD-KNIRILLVEdnninqivastTLKKIGINsIDIAENGQHALEYLKQttshNPYSLILMDCQMPVMDGYQATTHIRv 1040
Cdd:COG5803     7 IVDDqAGIRMLLKE-----------VLKKEGYE-VFQAANGKEALEKVKE----LKPDLVLLDMKMPGMDGIEILKEIK- 69
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 503229768 1041 neagSKNPPITIIAMTA---NAMVgDKAKCLqvGMNDYISKP 1079
Cdd:COG5803    70 ----EIDPDIPVIMMTAygeLDMV-EEAKEL--GAKGYFTKP 104
REC_OmpR_DrrD-like cd17625
phosphoacceptor receiver (REC) domain of DrrD-like OmpR family response regulators; DrrD is a ...
971-1079 1.64e-13

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: 68.02  E-value: 1.64e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  971 LLVEDN-NINQIVASTtLKKIGInSIDIAENGQHALEYLKQttshNPYSLILMDCQMPVMDGYQATTHIRvnEAGSKNPp 1049
Cdd:cd17625     1 LVVEDEkDLSEAITKH-LKKEGY-TVDVCFDGEEGLEYALS----GIYDLIILDIMLPGMDGLEVLKSLR--EEGIETP- 71
                          90       100       110
                  ....*....|....*....|....*....|
gi 503229768 1050 itIIAMTANAMVGDKAKCLQVGMNDYISKP 1079
Cdd:cd17625    72 --VLLLTALDAVEDRVKGLDLGADDYLPKP 99
HATPase_BasS-like cd16940
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
673-786 1.69e-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 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: 67.82  E-value: 1.69e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  673 HLEYAFVIGDAGRLKQILTNLVNNALKFTHKGEvQVIAKLTPINNNQMRfncqVIDSGIGISAAQQAKLFKSFSQVDSST 752
Cdd:cd16940     1 SAADIQVQGDALLLFLLLRNLVDNAVRYSPQGS-RVEIKLSADDGAVIR----VEDNGPGIDEEELEALFERFYRSDGQN 75
                          90       100       110
                  ....*....|....*....|....*....|....
gi 503229768  753 trkYGGTGLGLAIVKKLCHLMEGDIQVQSKENKG 786
Cdd:cd16940    76 ---YGGSGLGLSIVKRIVELHGGQIFLGNAQGGG 106
CitA COG3290
Sensor histidine kinase DipB regulating citrate/malate metabolism [Signal transduction ...
480-790 4.99e-13

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


Pssm-ID: 442519 [Multi-domain]  Cd Length: 389  Bit Score: 72.19  E-value: 4.99e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  480 CSLLQGPNTDKNAIDIITNAIKTLKTQRIEILNykkdgtEFWNSLQISPVFNEQQQLTAyVGIQQDITEQKAANQLLIEA 559
Cdd:COG3290   114 RRLLGLDAIGRPIDEVLAEVLETGERDEEILLN------GRVLVVNRVPIRDDGRVVGA-VATFRDRTELERLEEELEGV 186
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  560 KAAAEQaniaksefLAAMSHEIRTPMNGVLGMLNLildsslneKQHHQvsiALNSANSLLNIINDILDFSKVdagklele 639
Cdd:COG3290   187 KELAEA--------LRAQRHDFRNHLHTISGLLQL--------GEYDE---ALEYIDEISEELQELIDSLLS-------- 239
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  640 elefNLCN-MLDDFIETIAIHAHSKNIPLMLDIE-HLEYAFVIGDAgrLKQILTNLVNNAL---KFTHKGEVQVIAKLTP 714
Cdd:COG3290   240 ----RIGNpVLAALLLGKAARARERGIDLTIDIDsDLPDLPLSDTD--LVTILGNLLDNAIeavEKLPEEERRVELSIRD 313
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 503229768  715 INNnqmRFNCQVIDSGIGISAAQQAKLFKS-FSqvdsstTRKYGGTGLGLAIVKKLCHLMEGDIQVQSKENKGSNFS 790
Cdd:COG3290   314 DGD---ELVIEVEDSGPGIPEELLEKIFERgFS------TKLGEGRGLGLALVKQIVEKYGGTIEVESEEGEGTVFT 381
REC_OmpR_PmrA-like cd17624
phosphoacceptor receiver (REC) domain of PmrA-like OmpR family response regulators; This ...
970-1081 2.18e-12

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: 64.81  E-value: 2.18e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  970 ILLVEDNNINQIVASTTLKKIGInSIDIAENGQHALEYLKQTtshnPYSLILMDCQMPVMDGYQATTHIRvnEAGSKNPp 1049
Cdd:cd17624     1 ILLVEDDALLGDGLKTGLRKAGY-AVDWVRTGAEAEAALASG----PYDLVILDLGLPDGDGLDLLRRWR--RQGQSLP- 72
                          90       100       110
                  ....*....|....*....|....*....|..
gi 503229768 1050 itIIAMTANAMVGDKAKCLQVGMNDYISKPIA 1081
Cdd:cd17624    73 --VLILTARDGVDDRVAGLDAGADDYLVKPFA 102
PRK10755 PRK10755
two-component system sensor histidine kinase PmrB;
526-786 2.48e-12

two-component system sensor histidine kinase PmrB;


Pssm-ID: 236751 [Multi-domain]  Cd Length: 356  Bit Score: 69.61  E-value: 2.48e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  526 ISPVFNEQQQLTAY-------VGIQQDITEQKAA----NQLLIEAKAAAEQANIakseFLAAMSHEIRTPMNGVlgMLNL 594
Cdd:PRK10755   86 TRPLAELQKELEARtadnltpIAIHSSTLEIEAVtsalNQLVSRLTSTLDQERL----FTADVAHELRTPLAGI--RLHL 159
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  595 ildsSLNEKQHH-QVSIALNSANSLLNIINDILDFSKVDAGKLELEELEFNLCN-----MLDDFIETIAIHAHSKNIPlm 668
Cdd:PRK10755  160 ----ELLEKQHHiDVAPLIARLDQMMHTVEQLLQLARAGQSFSSGHYQTVKLLEdvilpSQDELSEMLEQRQQTLLLP-- 233
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  669 ldiEHLEYAFVIGDAGRLKQILTNLVNNALKFTHKGEVQVIAkltpINNNQMRFNCQVIDSGIGISAAQQAKLFKSFSQV 748
Cdd:PRK10755  234 ---ESAADITVQGDATLLRLLLRNLVENAHRYSPEGSTITIK----LSQEDGGAVLAVEDEGPGIDESKCGELSKAFVRM 306
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 503229768  749 DSsttrKYGGTGLGLAIVKKLCHLMEGDIQVQSKENKG 786
Cdd:PRK10755  307 DS----RYGGIGLGLSIVSRITQLHHGQFFLQNRQERS 340
HATPase_EcPhoR-like cd16952
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
686-791 2.98e-12

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: 64.15  E-value: 2.98e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  686 LKQILTNLVNNALKFT-HKGEVQVIAKLTPinnNQMRFNCQviDSGIGISAAQQAKLFKSFSQVDSSTTRKYGGTGLGLA 764
Cdd:cd16952     1 LRSAFSNLVSNAVKYTpPSDTITVRWSQEE---SGARLSVE--DTGPGIPPEHIPRLTERFYRVDIERCRNTGGTGLGLA 75
                          90       100
                  ....*....|....*....|....*..
gi 503229768  765 IVKKLCHLMEGDIQVQSKENKGSNFSF 791
Cdd:cd16952    76 IVKHVMSRHDARLLIASELGKGSRFTC 102
PRK10618 PRK10618
phosphotransfer intermediate protein in two-component regulatory system with RcsBC; Provisional
553-871 3.44e-12

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


Pssm-ID: 236726 [Multi-domain]  Cd Length: 894  Bit Score: 70.73  E-value: 3.44e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  553 NQLLIEAKAAAEQANIAKSEFLAAMSHEIRTPMNGVLGMLNLILDSSLNEKQHHQVSIALNSANSLLNIINDILDFSKVD 632
Cdd:PRK10618  433 NKKLQQAQREYEKNQQARKAFLQNIGDELKQPLQSLAQLAAQLRQTSDEEQQQPELDQLAEQSDVLVRLVDNIQLLNMLE 512
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  633 AGKLELEELEFNLCNMLDDFIETIAIHAHSKNIPLM----LDIEHLeyafVIGDAGRLKQILTNLVNNALKFTHKGEVQV 708
Cdd:PRK10618  513 TQDWKPEQELFSLQDLIDEVLPEVLPAIKRKGLQLLihnhLKAEQL----RIGDRDALRKILLLLLNYAITTTAYGKITL 588
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  709 IAKLTPINNNQMRFncQVIDSGIGISAAQQAKL---FKSFSQVDssttrKYG-GTGLGLAIVKKLCHLMEGDIQVQSKEN 784
Cdd:PRK10618  589 EVDQDESSPDRLTI--RILDTGAGVSIKELDNLhfpFLNQTQGD-----RYGkASGLTFFLCNQLCRKLGGHLTIKSREG 661
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  785 KGSNFSFNVVLKRSKNPQKVLPPVDMSSLNILIVCSNQTQSSILHKQFTKWGATaVISPSAKqavQICQQYiekqnlcfD 864
Cdd:PRK10618  662 LGTRYSIHLKMLAADPEVEEEEEKLLDGVTVLLDITSEEVRKIVTRQLENWGAT-CITPDER---LISQEY--------D 729

                  ....*..
gi 503229768  865 LIMIDMQ 871
Cdd:PRK10618  730 IFLTDNP 736
PAS cd00130
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
307-414 3.62e-12

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


Pssm-ID: 238075 [Multi-domain]  Cd Length: 103  Bit Score: 63.81  E-value: 3.62e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  307 SNDGIWDWDIVTNEVYFSPRISVLLGYDENDKNALPhcadaLYKLLHPDDITKHKKQIANHLISNIPFNYDYRLKTKSGA 386
Cdd:cd00130     1 LPDGVIVLDLDGRILYANPAAEQLLGYSPEELIGKS-----LLDLIHPEDREELRERLENLLSGGEPVTLEVRLRRKDGS 75
                          90       100
                  ....*....|....*....|....*...
gi 503229768  387 YRYFTVKGMALRNEHNKAIRMAGSVTDI 414
Cdd:cd00130    76 VIWVLVSLTPIRDEGGEVIGLLGVVRDI 103
REC_CheB-like cd17541
phosphoacceptor receiver (REC) domain of chemotaxis response regulator protein-glutamate ...
968-1079 3.67e-12

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: 64.34  E-value: 3.67e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  968 IRILLVEDNninqIVASTTLKKIgINS------IDIAENGQHALEYLKQttsHNPySLILMDCQMPVMDGYQATTHIRvn 1041
Cdd:cd17541     1 IRVLIVDDS----AVMRKLLSRI-LESdpdievVGTARDGEEALEKIKE---LKP-DVITLDIEMPVMDGLEALRRIM-- 69
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 503229768 1042 eagsKNPPITIIAMTANAMVGDKA--KCLQVGMNDYISKP 1079
Cdd:cd17541    70 ----AERPTPVVMVSSLTEEGAEItlEALELGAVDFIAKP 105
PRK13837 PRK13837
two-component system VirA-like sensor kinase;
621-789 5.38e-12

two-component system VirA-like sensor kinase;


Pssm-ID: 237526 [Multi-domain]  Cd Length: 828  Bit Score: 70.09  E-value: 5.38e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  621 IINDILDFSKvdagKLELEELEFNLCNMLDDFIETIAIhAHSKNIPLMLDiEHLEYAFVIGDAGRLKQILTNLVNNALK- 699
Cdd:PRK13837  502 IIDQILAFGR----KGERNTKPFDLSELVTEIAPLLRV-SLPPGVELDFD-QDQEPAVVEGNPAELQQVLMNLCSNAAQa 575
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  700 FTHKGEVQVIAK--------------LTPINNNQMRfncqVIDSGIGISAAQQAKLFKSFSqvdssTTRKyGGTGLGLAI 765
Cdd:PRK13837  576 MDGAGRVDISLSraklrapkvlshgvLPPGRYVLLR----VSDTGAGIDEAVLPHIFEPFF-----TTRA-GGTGLGLAT 645
                         170       180
                  ....*....|....*....|....
gi 503229768  766 VKKLCHLMEGDIQVQSKENKGSNF 789
Cdd:PRK13837  646 VHGIVSAHAGYIDVQSTVGRGTRF 669
HATPase_YcbM-like cd16947
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
664-796 7.29e-12

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: 63.69  E-value: 7.29e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  664 NIPlmldiEHLEYAFVIGDAgrLKQILTNLVNNALKFTHKGEVQVIAkltpINNNQMRFNCQVIDSGIGISAAQQAKLFK 743
Cdd:cd16947     6 NIP-----DRPIYANANTEA--LQRILKNLISNAIKYGSDGKFLGMT----LREDEKHVYIDIWDKGKGISETEKDHVFE 74
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 503229768  744 SFSQVDSSTTRKYGGTGLGLAIVKKLCHLMEGDIQVQSKENKGSnfSFNVVLK 796
Cdd:cd16947    75 RLYTLEDSRNSAKQGNGLGLTITKRLAESMGGSIYVNSKPYEKT--VFTVTLK 125
MtrAB_MtrB NF040691
MtrAB system histidine kinase MtrB;
573-789 2.03e-11

MtrAB system histidine kinase MtrB;


Pssm-ID: 468655 [Multi-domain]  Cd Length: 507  Bit Score: 67.74  E-value: 2.03e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  573 FLAAMSHEIRTPMNGVLGMLNLILDSSLN---------EKQHHQvsiaLNSANSLLniiNDILDFSKVDAGKLELEELEF 643
Cdd:NF040691  274 FVSDVSHELRTPLTTIRMAADVIHDSRDDfdpatarsaELLHTE----LDRFESLL---SDLLEISRFDAGAAELDVEPV 346
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  644 NLCNMLDDFIETIAIHAHSKNIPLMLDIEHlEYAFVIGDAGRLKQILTNLVNNALKFTHKGEVQVIakltpINNNQMRFN 723
Cdd:NF040691  347 DLRPLVRRVVDALRQLAERAGVELRVDAPG-TPVVAEVDPRRVERVLRNLVVNAIEHGEGKPVVVT-----VAQDDTAVA 420
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 503229768  724 CQVIDSGIGISAAQQAKLFKSFSQVDSSTTRKYGGTGLGLAIVKKLCHLMEGDIQVQSKENKGSNF 789
Cdd:NF040691  421 VTVRDHGVGLKPGEVALVFDRFWRADPARARTTGGTGLGLAIALEDARLHGGWLEAWGRPGQGSQF 486
PRK10610 PRK10610
chemotaxis protein CheY;
965-1091 2.30e-11

chemotaxis protein CheY;


Pssm-ID: 170568 [Multi-domain]  Cd Length: 129  Bit Score: 62.30  E-value: 2.30e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  965 DKNIRILLVEDNNINQIVASTTLKKIGINSIDIAENGQHALEYLKQTTshnpYSLILMDCQMPVMDGYQATTHIRVNEAG 1044
Cdd:PRK10610    3 DKELKFLVVDDFSTMRRIVRNLLKELGFNNVEEAEDGVDALNKLQAGG----FGFVISDWNMPNMDGLELLKTIRADGAM 78
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 503229768 1045 SKNPpitIIAMTANAMVGDKAKCLQVGMNDYISKPIAQDILFKKLLK 1091
Cdd:PRK10610   79 SALP---VLMVTAEAKKENIIAAAQAGASGYVVKPFTAATLEEKLNK 122
PRK10364 PRK10364
two-component system sensor histidine kinase ZraS;
565-803 2.37e-11

two-component system sensor histidine kinase ZraS;


Pssm-ID: 236674 [Multi-domain]  Cd Length: 457  Bit Score: 67.50  E-value: 2.37e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  565 QANIAKSEFLAAM-------SHEIRTPMNGVLGMLNLILDSSLNEKQHHQVS-IALNSANSLLNIINDILDFSKvdagKL 636
Cdd:PRK10364  225 QDEMKRKEKLVALghlaagvAHEIRNPLSSIKGLAKYFAERAPAGGEAHQLAqVMAKEADRLNRVVSELLELVK----PT 300
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  637 ELEELEFNLCNMLDDFIETIAIHAHSKNIPLMLDI-EHLEYAFVigDAGRLKQILTNLVNNALK-FTHKGEVQVIAKltp 714
Cdd:PRK10364  301 HLALQAVDLNDLINHSLQLVSQDANSREIQLRFTAnDTLPEIQA--DPDRLTQVLLNLYLNAIQaIGQHGVISVTAS--- 375
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  715 inNNQMRFNCQVIDSGIGISAAQQAKLFksfsqvDSSTTRKYGGTGLGLAIVKKLCHLMEGDIQVQSKENKGSNFSFNVV 794
Cdd:PRK10364  376 --ESGAGVKISVTDSGKGIAADQLEAIF------TPYFTTKAEGTGLGLAVVHNIVEQHGGTIQVASQEGKGATFTLWLP 447
                         250
                  ....*....|
gi 503229768  795 LK-RSKNPQK 803
Cdd:PRK10364  448 VNiTRRDPQG 457
REC_OmpR_CusR-like cd19935
phosphoacceptor receiver (REC) domain of CusR-like OmpR family response regulators; ...
970-1079 3.67e-11

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: 60.53  E-value: 3.67e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  970 ILLVEDNninqIVASTTLKKiGIN----SIDIAENGQHALEYLkqttSHNPYSLILMDCQMPVMDGYQATTHIRvnEAGS 1045
Cdd:cd19935     1 ILVVEDE----KKLAEYLKK-GLTeegyAVDVAYDGEDGLHLA----LTNEYDLIILDVMLPGLDGLEVLRRLR--AAGK 69
                          90       100       110
                  ....*....|....*....|....*....|....
gi 503229768 1046 KNPpitIIAMTANAMVGDKAKCLQVGMNDYISKP 1079
Cdd:cd19935    70 QTP---VLMLTARDSVEDRVKGLDLGADDYLVKP 100
REC_CheC-like cd17593
phosphoacceptor receiver (REC) domain of uncharacterized response regulators containing a CheC ...
998-1091 3.67e-11

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: 61.40  E-value: 3.67e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  998 AENGQHALEYLKQttshNPYSLILMDCQMPVMDGYQATTHIRVNEAgsknpPITIIAMTANamVGDKAK--CLQVGMNDY 1075
Cdd:cd17593    31 AENGEEALEILRE----GRIDVLFLDLTMPVMDGYEVLEALPVEQL-----ETKVIVVSGD--VQPEAKerVLELGALAF 99
                          90
                  ....*....|....*.
gi 503229768 1076 ISKPIAQDILFKKLLK 1091
Cdd:cd17593   100 LKKPFDPEKLAQLLEE 115
envZ PRK09467
osmolarity sensor protein; Provisional
686-786 4.22e-11

osmolarity sensor protein; Provisional


Pssm-ID: 236531 [Multi-domain]  Cd Length: 435  Bit Score: 66.47  E-value: 4.22e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  686 LKQILTNLVNNALKFTHkGEVQVIAKLtpinnNQMRFNCQVIDSGIGISAAQQAKLFKSFSQVDssTTRKYGGTGLGLAI 765
Cdd:PRK09467  332 IKRALANLVVNAARYGN-GWIKVSSGT-----EGKRAWFQVEDDGPGIPPEQLKHLFQPFTRGD--SARGSSGTGLGLAI 403
                          90       100
                  ....*....|....*....|.
gi 503229768  766 VKKLCHLMEGDIQVQSKENKG 786
Cdd:PRK09467  404 VKRIVDQHNGKVELGNSEEGG 424
REC_RR468-like cd17552
phosphoacceptor receiver (REC) domain of Thermotoga maritima response regulator RR468 and ...
969-1079 4.80e-11

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: 61.03  E-value: 4.80e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  969 RILLVEDNNINQIVASTTLKKIGINSIDIAENGQHALEylkQTTSHNPySLILMDCQMPVMDGYQATTHIRVNeagSKNP 1048
Cdd:cd17552     3 RILVIDDEEDIREVVQACLEKLAGWEVLTASSGQEGLE---KAATEQP-DAILLDVMMPDMDGLATLKKLQAN---PETQ 75
                          90       100       110
                  ....*....|....*....|....*....|.
gi 503229768 1049 PITIIAMTANAMVGDKAKCLQVGMNDYISKP 1079
Cdd:cd17552    76 SIPVILLTAKAQPSDRQRFASLGVAGVIAKP 106
REC_Ycf29 cd19927
phosphoacceptor receiver (REC) domain of probable transcriptional regulator Ycf29; Ycf29 is a ...
970-1079 7.07e-11

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: 60.08  E-value: 7.07e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  970 ILLVEDNNINQIVASTTLKKIGINsIDIAENGQHALEYLKQTTSHnpysLILMDCQMPVMDGYQATTHIRVNEAGSKNPp 1049
Cdd:cd19927     1 ILLVDDDPGIRLAVKDYLEDQGFT-VIAASNGLEALDLLNQYIPD----LIISDIIMPGVDGYSLLGKLRKNADFDTIP- 74
                          90       100       110
                  ....*....|....*....|....*....|
gi 503229768 1050 itIIAMTANAMVGDKAKCLQVGMNDYISKP 1079
Cdd:cd19927    75 --VIFLTAKGMTSDRIKGYNAGCDGYLSKP 102
PRK09303 PRK09303
histidine kinase;
533-793 7.81e-11

histidine kinase;


Pssm-ID: 236462 [Multi-domain]  Cd Length: 380  Bit Score: 65.36  E-value: 7.81e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  533 QQQLTAYVGIQQDITEQKAAN---------------QLLIEAKAAAEQANiAKSEFLAAMSHEIRTPMNG---VLGMLNL 594
Cdd:PRK09303  100 QQEGATYSGLGENLQPSEIDSgrysqellqlsdelfVLRQENETLLEQLK-FKDRVLAMLAHDLRTPLTAaslALETLEL 178
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  595 ILDSSLNEKQHHQVSIALNSANSLLNIIN----DILDFSKVDAGKLELEELEFNLCNMLDDFIETIAIHAHSKNIPLMLD 670
Cdd:PRK09303  179 GQIDEDTELKPALIEQLQDQARRQLEEIErlitDLLEVGRTRWEALRFNPQKLDLGSLCQEVILELEKRWLAKSLEIQTD 258
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  671 I-EHLEYAFviGDAGRLKQILTNLVNNALKFTHK-GEVQVIAkltpINNNQMRFNCQVIDSGIGISAAQQAKLFK-SFS- 746
Cdd:PRK09303  259 IpSDLPSVY--ADQERIRQVLLNLLDNAIKYTPEgGTITLSM----LHRTTQKVQVSICDTGPGIPEEEQERIFEdRVRl 332
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 503229768  747 QVDSSTTrkygGTGLGLAIVKKLCHLMEGDIQVQSKENKGSNFSFNV 793
Cdd:PRK09303  333 PRDEGTE----GYGIGLSVCRRIVRVHYGQIWVDSEPGQGSCFHFTL 375
CheY COG0784
CheY-like REC (receiver) domain, includes chemotaxis protein CheY and sporulation regulator ...
808-940 9.70e-11

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


Pssm-ID: 440547 [Multi-domain]  Cd Length: 128  Bit Score: 60.25  E-value: 9.70e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  808 VDMSSLNILIVCSNQTQSSILHKQFTKWGATAVISPSAKQAVQICQQYiekqnlCFDLIMIDMQLSDGDALTLSKTLDKE 887
Cdd:COG0784     1 PPLGGKRILVVDDNPDNRELLRRLLERLGYEVTTAEDGAEALELLRAG------PPDLILLDINMPGMDGLELLRRIRAL 74
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 503229768  888 VDLMAAHVVLMTTGELNKQRDLYQASRFSAIVTKPIITQNLFKMLSTCFSDKQ 940
Cdd:COG0784    75 PRLPDIPIIALTAYADEEDRERALEAGADDYLTKPVDPEELLEALRRLLARAS 127
cpxA PRK09470
envelope stress sensor histidine kinase CpxA;
574-766 1.28e-10

envelope stress sensor histidine kinase CpxA;


Pssm-ID: 236532 [Multi-domain]  Cd Length: 461  Bit Score: 64.95  E-value: 1.28e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  574 LAAMSHEIRTPMNgvlgmlNLILDSSLNEKQHHQvSIAL----NSANSLLNIINDILDFSKVDAgKLELEELEFNLCNML 649
Cdd:PRK09470  247 LSDISHELRTPLT------RLQLATALLRRRQGE-SKELerieTEAQRLDSMINDLLVLSRNQQ-KNHLERETFKANSLW 318
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  650 DDFIETIAIHAHSKNIPLMLdIEHLEYAFVIGDAGRLKQILTNLVNNALKFTHkgevQVIAKLTPINNNQMRFNcqVIDS 729
Cdd:PRK09470  319 SEVLEDAKFEAEQMGKSLTV-SAPPGPWPINGNPNALASALENIVRNALRYSH----TKIEVAFSVDKDGLTIT--VDDD 391
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 503229768  730 GIGISAAQQAKLFKSFSQVDSSTTRKYGGTGLGLAIV 766
Cdd:PRK09470  392 GPGVPEEEREQIFRPFYRVDEARDRESGGTGLGLAIV 428
REC_YesN-like cd17536
phosphoacceptor receiver (REC) domain of YesN and related helix-turn-helix containing response ...
970-1091 1.83e-10

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: 59.27  E-value: 1.83e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  970 ILLVEDNNInqIVASttLKKI------GINSIDIAENGQHALEYLKQttsHNPySLILMDCQMPVMDGYQATTHIRvnea 1043
Cdd:cd17536     1 VLIVDDEPL--IREG--LKKLidweelGFEVVGEAENGEEALELIEE---HKP-DIVITDIRMPGMDGLELIEKIR---- 68
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 503229768 1044 gSKNPPITIIAMTANAmvgDKA---KCLQVGMNDYISKPIAQDILFKKLLK 1091
Cdd:cd17536    69 -ELYPDIKIIILSGYD---DFEyaqKAIRLGVVDYLLKPVDEEELEEALEK 115
PRK11517 PRK11517
DNA-binding response regulator HprR;
968-1100 2.25e-10

DNA-binding response regulator HprR;


Pssm-ID: 183172 [Multi-domain]  Cd Length: 223  Bit Score: 61.84  E-value: 2.25e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  968 IRILLVEDNNINQIVASTTLKKIGInSIDIAENGQHALEYLKQttshNPYSLILMDCQMPVMDGYQATTHIRVneagSKN 1047
Cdd:PRK11517    1 MKILLIEDNQRTQEWVTQGLSEAGY-VIDAVSDGRDGLYLALK----DDYALIILDIMLPGMDGWQILQTLRT----AKQ 71
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 503229768 1048 PPItiIAMTANAMVGDKAKCLQVGMNDYISKPIAqdilFKKLLKWLPYELKNN 1100
Cdd:PRK11517   72 TPV--ICLTARDSVDDRVRGLDSGANDYLVKPFS----FSELLARVRAQLRQH 118
COG4192 COG4192
Signal transduction histidine kinase regulating phosphoglycerate transport system [Signal ...
531-786 2.44e-10

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


Pssm-ID: 443346 [Multi-domain]  Cd Length: 640  Bit Score: 64.71  E-value: 2.44e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  531 NEQQQLtayvgIQQDITEQKAANQLLI----EAKAAAEQANIAKSefLAAMSHEIRTPMNgVLGMLNLILDSSLNEKQHH 606
Cdd:COG4192   397 IEKTQE-----LETEIEERKRIEKNLRqtqdELIQAAKMAVVGQT--MTSLAHELNQPLN-AMSMYLFSAKKALEQENYA 468
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  607 QVSIALNSANSLL----NIINDILDFSKvdagKLELEELEFNLCNMLDDFIETIAIHAHSKNIPLMLDIEHleyaFVIGD 682
Cdd:COG4192   469 QLPTSLDKIEGLIermdKIIKSLRQFSR----KSDTPLQPVDLRQVIEQAWELVESRAKPQQITLHIPDDL----MVQGD 540
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  683 AGRLKQILTNLVNNALK-FTHKGEVQVIAKLTPINNNQMrfncqVIDSGIGISAAQqaKLFKSFsqvdssTTRKYGGTGL 761
Cdd:COG4192   541 QVLLEQVLVNLLVNALDaVATQPQISVDLLSNAENLRVA-----ISDNGNGWPLVD--KLFTPF------TTTKEVGLGL 607
                         250       260
                  ....*....|....*....|....*
gi 503229768  762 GLAIVKKLCHLMEGDIQVQSKENKG 786
Cdd:COG4192   608 GLSICRSIMQQFGGDLYLASTLERG 632
orf27 CHL00148
Ycf27; Reviewed
969-1079 2.49e-10

Ycf27; Reviewed


Pssm-ID: 214376 [Multi-domain]  Cd Length: 240  Bit Score: 62.04  E-value: 2.49e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  969 RILLVED-NNINQIVaSTTLKKIGINSIDiAENGQHALeylKQTTSHNPySLILMDCQMPVMDGYQATTHIRvneagsKN 1047
Cdd:CHL00148    8 KILVVDDeAYIRKIL-ETRLSIIGYEVIT-ASDGEEAL---KLFRKEQP-DLVILDVMMPKLDGYGVCQEIR------KE 75
                          90       100       110
                  ....*....|....*....|....*....|..
gi 503229768 1048 PPITIIAMTANAMVGDKAKCLQVGMNDYISKP 1079
Cdd:CHL00148   76 SDVPIIMLTALGDVSDRITGLELGADDYVVKP 107
REC_OmpR_PhoB cd17618
phosphoacceptor receiver (REC) domain of PhoB response regulator from the OmpR family; The ...
969-1079 2.70e-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: 58.80  E-value: 2.70e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  969 RILLVEDNN-INQIVAsTTLKKIGINSIDiAENGQHALEYLKQTTSHnpysLILMDCQMPVMDGYQATTHIRVNEAGSKN 1047
Cdd:cd17618     2 TILIVEDEPaIREMIA-FNLERAGFDVVE-AEDAESAVNLIVEPRPD----LILLDWMLPGGSGIQFIRRLKRDEMTRDI 75
                          90       100       110
                  ....*....|....*....|....*....|..
gi 503229768 1048 PpitIIAMTANAMVGDKAKCLQVGMNDYISKP 1079
Cdd:cd17618    76 P---IIMLTARGEEEDKVRGLEAGADDYITKP 104
REC_CheY cd17542
phosphoacceptor receiver (REC) domain of chemotaxis protein CheY; The chemotaxis response ...
968-1083 2.87e-10

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: 58.83  E-value: 2.87e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  968 IRILLVED-----NNINQIvasttLKKIGINSIDIAENGQHALEYLKQttsHNPySLILMDCQMPVMDGYQATTHIRVNE 1042
Cdd:cd17542     1 KKVLIVDDaafmrMMLKDI-----LTKAGYEVVGEAANGEEAVEKYKE---LKP-DLVTMDITMPEMDGIEALKEIKKID 71
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 503229768 1043 AGSKnpPITIIAMTANAMVgdkAKCLQVGMNDYISKPIAQD 1083
Cdd:cd17542    72 PNAK--VIMCSAMGQEEMV---KEAIKAGAKDFIVKPFQPE 107
HATPase_AtoS-like cd16943
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
686-789 3.23e-10

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: 58.20  E-value: 3.23e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  686 LKQILTNLVNNALK-FTHKGEVQVIAKLTpinnnQMRFNCQVIDSGIGISAAQQAKLFKSFSqvdssTTRKYG-GTGLGL 763
Cdd:cd16943     4 LNQVLLNLLVNAAQaMEGRGRITIRTWAH-----VDQVLIEVEDTGSGIDPEILGRIFDPFF-----TTKPVGeGTGLGL 73
                          90       100
                  ....*....|....*....|....*.
gi 503229768  764 AIVKKLCHLMEGDIQVQSKENKGSNF 789
Cdd:cd16943    74 SLSYRIIQKHGGTIRVASVPGGGTRF 99
REC_OmpR_BsPhoP-like cd19937
phosphoacceptor receiver (REC) domain of BsPhoP-like OmpR family response regulators; Bacillus ...
971-1080 3.51e-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: 58.44  E-value: 3.51e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  971 LLVEDN-NINQIVaSTTLKKIGiNSIDIAENGQHALEYLKQttshNPYSLILMDCQMPVMDGYQATTHIRVNEAGSKNPp 1049
Cdd:cd19937     1 LVVDDEeDIVELL-KYNLEKEG-YEVVTAYDGEEALKRAKD----EKPDLIILDLMLPGIDGLEVCRILRSDPKTSSIP- 73
                          90       100       110
                  ....*....|....*....|....*....|.
gi 503229768 1050 itIIAMTANAMVGDKAKCLQVGMNDYISKPI 1080
Cdd:cd19937    74 --IIMLTAKGEEFDKVLGLELGADDYITKPF 102
HATPase_CpxA-like cd16949
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
686-786 5.01e-10

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: 57.72  E-value: 5.01e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  686 LKQILTNLVNNALKFTHkGEVQVIAKLTpINNNQMRFNcqviDSGIGISAAQQAKLFKSFSQVDSSTTRKYGGTGLGLAI 765
Cdd:cd16949     1 LARALENVLRNALRYSP-SKILLDISQD-GDQWTITIT----DDGPGVPEDQLEQIFLPFYRVDSARDRESGGTGLGLAI 74
                          90       100
                  ....*....|....*....|.
gi 503229768  766 VKKLCHLMEGDIQVQSKENKG 786
Cdd:cd16949    75 AERAIEQHGGKIKASNRKPGG 95
REC smart00448
cheY-homologous receiver domain; CheY regulates the clockwise rotation of E. coli flagellar ...
968-1027 5.01e-10

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


Pssm-ID: 214668 [Multi-domain]  Cd Length: 55  Bit Score: 56.04  E-value: 5.01e-10
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768    968 IRILLVEDNNINQIVASTTLKKIGInSIDIAENGQHALEYLKQttshNPYSLILMDCQMP 1027
Cdd:smart00448    1 MRILVVDDDPLLRELLKALLEKEGY-EVDEATDGEEALELLKE----EKPDLILLDIMMP 55
REC_OmpR_PrrA-like cd17627
phosphoacceptor receiver (REC) domain of PrrA-like OmpR family response regulators; The ...
994-1089 5.95e-10

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: 57.78  E-value: 5.95e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  994 SIDIAENGQHALEYLkqttSHNPYSLILMDCQMPVMDGYQATTHIRvnEAGSKNPpitIIAMTANAMVGDKAKCLQVGMN 1073
Cdd:cd17627    24 EVETAVDGAEALRVI----SGNRPDAVVLDVMMPRLDGLEVCRRLR--AAGNDLP---ILVLTARDSVSDRVAGLDAGAD 94
                          90
                  ....*....|....*.
gi 503229768 1074 DYISKPIAQDILFKKL 1089
Cdd:cd17627    95 DYLVKPFALEELLARV 110
PRK11361 PRK11361
acetoacetate metabolism transcriptional regulator AtoC;
969-1079 8.38e-10

acetoacetate metabolism transcriptional regulator AtoC;


Pssm-ID: 183099 [Multi-domain]  Cd Length: 457  Bit Score: 62.56  E-value: 8.38e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  969 RILLVED-NNINQIVaSTTLKKIGINSIDiAENGQHALEYLKQTtshnPYSLILMDCQMPVMDGYQATTHIRvneagSKN 1047
Cdd:PRK11361    6 RILIVDDeDNVRRML-STAFALQGFETHC-ANNGRTALHLFADI----HPDVVLMDIRMPEMDGIKALKEMR-----SHE 74
                          90       100       110
                  ....*....|....*....|....*....|..
gi 503229768 1048 PPITIIAMTANAMVGDKAKCLQVGMNDYISKP 1079
Cdd:PRK11361   75 TRTPVILMTAYAEVETAVEALRCGAFDYVIKP 106
REC_DC-like cd17534
phosphoacceptor receiver (REC) domain of modulated diguanylate cyclase and similar domains; ...
968-1085 1.55e-09

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


Pssm-ID: 381089 [Multi-domain]  Cd Length: 117  Bit Score: 56.65  E-value: 1.55e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  968 IRILLVEDNNINQIVASTTLKKIGINSIDIAENGQHALEYLKQttsHNPySLILMDCQMP-VMDGYQATTHIRvneagsK 1046
Cdd:cd17534     1 KKILIVEDEAIIALDLKEILESLGYEVVGIADSGEEAIELAEE---NKP-DLILMDINLKgDMDGIEAAREIR------E 70
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 503229768 1047 NPPITIIAMTANA---MVgDKAKclQVGMNDYISKPIAQDIL 1085
Cdd:cd17534    71 KFDIPVIFLTAYSdeeTL-ERAK--ETNPYGYLVKPFNEREL 109
PRK10365 PRK10365
sigma-54-dependent response regulator transcription factor ZraR;
967-1095 1.82e-09

sigma-54-dependent response regulator transcription factor ZraR;


Pssm-ID: 182412 [Multi-domain]  Cd Length: 441  Bit Score: 61.20  E-value: 1.82e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  967 NIRILLVEDNNINQIVASTTLKKIGINsIDIAENGQHALEylkqTTSHNPYSLILMDCQMPVMDGYQATTHIRvneagSK 1046
Cdd:PRK10365    5 NIDILVVDDDISHCTILQALLRGWGYN-VALANSGRQALE----QVREQVFDLVLCDVRMAEMDGIATLKEIK-----AL 74
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 503229768 1047 NPPITIIAMTANAMVGDKAKCLQVGMNDYISKPIAQDILFKKLLKWLPY 1095
Cdd:PRK10365   75 NPAIPVLIMTAYSSVETAVEALKTGALDYLIKPLDFDNLQATLEKALAH 123
REC_PdtaR-like cd19932
phosphoacceptor receiver (REC) domain of PdtaR and similar proteins; This subfamily includes ...
968-1086 1.98e-09

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: 56.27  E-value: 1.98e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  968 IRILLVEDNNINQIVASTTLKKIGINSIDIAENGQHALEYLKQttsHNPySLILMDCQMPVMDGYQATTHIRVNEAGskn 1047
Cdd:cd19932     1 VRVLIAEDEALIRMDLREMLEEAGYEVVGEASDGEEAVELAKK---HKP-DLVIMDVKMPRLDGIEAAKIITSENIA--- 73
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 503229768 1048 pPITIIAMTANAMVGDKAKclQVGMNDYISKPIAQDILF 1086
Cdd:cd19932    74 -PIVLLTAYSQQDLVERAK--EAGAMAYLVKPFSESDLI 109
sensory_box TIGR00229
PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain ...
296-424 3.09e-09

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


Pssm-ID: 272971 [Multi-domain]  Cd Length: 124  Bit Score: 56.15  E-value: 3.09e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768   296 SEARYELAVKGSNDGIWDWDIVTNEVYFSPRISVLLGYDEND---KNALphcadalyKLLHPDDITKHKKQIANHLISNI 372
Cdd:TIGR00229    1 SEERYRAIFESSPDAIIVIDLEGNILYVNPAFEEIFGYSAEEligRNVL--------ELIPEEDREEVRERIERRLEGEP 72
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 503229768   373 PFNYD-YRLKTKSGAYRYFTVKGMALRnEHNKAIRMAGSVTDITEQKRSQKAL 424
Cdd:TIGR00229   73 EPVSEeRRVRRKDGSEIWVEVSVSPIR-TNGGELGVVGIVRDITERKEAEEAL 124
AmiR COG3707
Two-component response regulator, AmiR/NasT family, consists of REC and RNA-binding ...
966-1086 4.69e-09

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: 57.27  E-value: 4.69e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  966 KNIRILLVEDNNINQIVASTTLKKIGINSIDIAENGQHALEylkQTTSHNPySLILMDCQMPVMDGYQATTHIrvneagS 1045
Cdd:COG3707     2 RGLRVLVVDDEPLRRADLREGLREAGYEVVAEAADGEDAVE---LVRELKP-DLVIVDIDMPDRDGLEAARQI------S 71
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 503229768 1046 KNPPITIIAMTANAMVGDKAKCLQVGMNDYISKPIAQDILF 1086
Cdd:COG3707    72 EERPAPVILLTAYSDPELIERALEAGVSAYLVKPLDPEDLL 112
HATPase_HupT_MifS-like cd16976
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
686-791 8.13e-09

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: 54.00  E-value: 8.13e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  686 LKQILTNLVNNALKFTHKGEVQVIAKLTPINNNqmRFNCQVIDSGIGISAAQQAKLFKSFSqvdssTTRKYG-GTGLGLA 764
Cdd:cd16976     1 IQQVLMNLLQNALDAMGKVENPRIRIAARRLGG--RLVLVVRDNGPGIAEEHLSRVFDPFF-----TTKPVGkGTGLGLS 73
                          90       100
                  ....*....|....*....|....*..
gi 503229768  765 IVKKLCHLMEGDIQVQSKENKGSNFSF 791
Cdd:cd16976    74 ISYGIVEEHGGRLSVANEEGAGARFTF 100
REC_CpdR_CckA-like cd18160
phosphoacceptor receiver (REC) domain of Brucella abortus CpdR and CckA, and similar domains; ...
969-1079 9.73e-09

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: 54.05  E-value: 9.73e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  969 RILLVEDNNINQIVASTTLKKIGInSIDIAENGQHALEYLKQttsHNPYSLILMDCQMPVMDGYQAtthirVNEAGSKNP 1048
Cdd:cd18160     1 TILLADDEPSVRKFIVTTLKKAGY-AVTEAESGAEALEKLQQ---GKDIDIVVTDIVMPEMDGIEL-----AREARKIDP 71
                          90       100       110
                  ....*....|....*....|....*....|.
gi 503229768 1049 PITIIAMTANAMVGDKAKCLQVGMNDYISKP 1079
Cdd:cd18160    72 DVKILFISGGAAAAPELLSDAVGDNATLKKP 102
PAC smart00086
Motif C-terminal to PAS motifs (likely to contribute to PAS structural domain); PAC motif ...
508-549 1.12e-08

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


Pssm-ID: 197509  Cd Length: 43  Bit Score: 51.80  E-value: 1.12e-08
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|..
gi 503229768    508 IEILNYKKDGTEFWNSLQISPVFNEQQQLTAYVGIQQDITEQ 549
Cdd:smart00086    2 VEYRLRRKDGSYIWVLVSASPIRDEDGEVEGILGVVRDITER 43
RocR COG3829
RocR-type transcriptional regulator, contains PAS, AAA-type ATPase, and DNA-binding Fis ...
428-573 1.40e-08

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


Pssm-ID: 443041 [Multi-domain]  Cd Length: 448  Bit Score: 58.63  E-value: 1.40e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  428 KEQNDLLAQAIESCNVGISIADAsvQGFpLVFLNSEFEKITGYSKEEMLGINCSLLQgPNTdknaidIITNAIKTLKTQR 507
Cdd:COG3829     7 KELEEELEAILDSLDDGIIVVDA--DGR-ITYVNRAAERILGLPREEVIGKNVTELI-PNS------PLLEVLKTGKPVT 76
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 503229768  508 IEILNYKKDGTEFWNSlqISPVFnEQQQLTAYVGIQQDITEQKAANQLLIEAKaaAEQANIAKSEF 573
Cdd:COG3829    77 GVIQKTGGKGKTVIVT--AIPIF-EDGEVIGAVETFRDITELKRLERKLREEE--LERGLSAKYTF 137
REC_NtrC1-like cd17572
phosphoacceptor receiver (REC) domain of nitrogen regulatory protein C 1 (NtrC1) from Aquifex ...
970-1080 1.62e-08

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: 53.74  E-value: 1.62e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  970 ILLVEDNNINQIVASTTLKKIGINsIDIAENGQHALEYLKQttshNPYSLILMDCQMPVMDGYQATTHIRVNEagsknPP 1049
Cdd:cd17572     1 VLLVEDSPSLAALYQEYLSDEGYK-VTHVETGKEALAFLSD----QPPDVVLLDLKLPDMSGMEILKWIQERS-----LP 70
                          90       100       110
                  ....*....|....*....|....*....|.
gi 503229768 1050 ITIIAMTANAMVGDKAKCLQVGMNDYISKPI 1080
Cdd:cd17572    71 TSVIVITAHGSVDIAVEAMRLGAYDFLEKPF 101
REC_NarL-like cd17535
phosphoacceptor receiver (REC) domain of NarL (Nitrate/Nitrite response regulator L) family ...
991-1087 1.62e-08

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: 53.67  E-value: 1.62e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  991 GINSIDIAENGQHALEYLKQTtshnPYSLILMDCQMPVMDGYQATTHIRvneagSKNPPITIIAMTANAMVGDKAKCLQV 1070
Cdd:cd17535    23 DIEVVGEAADGEEALALLREL----RPDVVLMDLSMPGMDGIEALRRLR-----RRYPDLKVIVLTAHDDPEYVLRALKA 93
                          90
                  ....*....|....*..
gi 503229768 1071 GMNDYISKPIAQDILFK 1087
Cdd:cd17535    94 GAAGYLLKDSSPEELIE 110
REC_CheY4-like cd17562
phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY4 and similar CheY ...
969-1090 1.94e-08

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: 53.46  E-value: 1.94e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  969 RILLVEDNN-INQIVaSTTLKKIGINSIDiAENGQHALEYLKQTTshnpYSLILMDCQMPVMDGYQATTHIRVNeAGSKN 1047
Cdd:cd17562     2 KILAVDDSAsIRQMV-SFTLRGAGYEVVE-AADGRDALSKAQSKK----FDLIITDQNMPNMDGIELIKELRKL-PAYKF 74
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 503229768 1048 PPitIIAMTANAMVGDKAKCLQVGMNDYISKPIAQDILF---KKLL 1090
Cdd:cd17562    75 TP--ILMLTTESSDEKKQEGKAAGATGWLVKPFDPEQLLevvKKVL 118
REC_TPR cd17589
phosphoacceptor receiver (REC) domain of uncharacterized tetratricopeptide repeat (TPR) ...
970-1089 2.14e-08

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: 53.42  E-value: 2.14e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  970 ILLVEDNNINQIVASTTLKKIGINSIDIAENGQHALEYLKqttsHNPYSLILMDCQMPV-MDGYQATTHIRVNEAgskNP 1048
Cdd:cd17589     1 FLIVDDQPTFRSMLKSMLRSLGVTRIDTASSGEEALRMCE----NKTYDIVLCDYNLGKgKNGQQLLEELRHKKL---IS 73
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 503229768 1049 PITIIAM----TANAMVgdkAKCLQVGMNDYISKPIAQDILFKKL 1089
Cdd:cd17589    74 PSTVFIMvtgeSSRAMV---LSALELEPDDYLLKPFTVSELRERL 115
REC_OmpR_NsrR-like cd18159
phosphoacceptor receiver (REC) domain of Streptococcus agalactiae NsrR-like OmpR family ...
970-1089 2.46e-08

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: 53.05  E-value: 2.46e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  970 ILLVEDNNINQIVASTTLKKIGINSIdIAENGQHALEYLKQttsHNPySLILMDCQMPVMDGYQATTHIRvneAGSKNPP 1049
Cdd:cd18159     1 ILIVEDDETIASLLKKHLEKWGYEVV-LIEDFEDVLEEFLQ---FKP-DLVLLDINLPYFDGFYWCREIR---QISNVPI 72
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 503229768 1050 ITIIAMTANAmvgDKAKCLQVGMNDYISKPIAQDILFKKL 1089
Cdd:cd18159    73 IFISSRDDNM---DQVMAINMGGDDYITKPFDLDVLLAKI 109
PAS pfam00989
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
433-546 2.57e-08

PAS fold; The PAS fold corresponds to the structural domain that has previously been defined as PAS and PAC motifs. The PAS fold appears in archaea, eubacteria and eukarya. This domain can bind gases (O2, CO and NO), FAD, 4-hydroxycinnamic acid and NAD+ (Matilla et.al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).


Pssm-ID: 395786 [Multi-domain]  Cd Length: 113  Bit Score: 53.19  E-value: 2.57e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768   433 LLAQAIESCNVGISIADAsvQGFpLVFLNSEFEKITGYSKEEMLGINCSLLQGPNTDKNAIDIITNAIKTLKTQRI-EIL 511
Cdd:pfam00989    2 DLRAILESLPDGIFVVDE--DGR-ILYVNAAAEELLGLSREEVIGKSLLDLIPEEDDAEVAELLRQALLQGEESRGfEVS 78
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 503229768   512 NYKKDGTEFWNSLQISPVFNEQQQLTAYVGIQQDI 546
Cdd:pfam00989   79 FRVPDGRPRHVEVRASPVRDAGGEILGFLGVLRDI 113
HATPase_BceS-YxdK-YvcQ-like cd16948
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
682-791 2.73e-08

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: 52.67  E-value: 2.73e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  682 DAGRLKQILTNLVNNALKFTHKGEVQVIAKLTpiNNNQMRFncQVIDSGIGISAAQQAKLF-KSFSQVDSSTTRKygGTG 760
Cdd:cd16948     2 DAKWLSFIIGQIVSNALKYSKQGGKIEIYSET--NEQGVVL--SIKDFGIGIPEEDLPRVFdKGFTGENGRNFQE--STG 75
                          90       100       110
                  ....*....|....*....|....*....|.
gi 503229768  761 LGLAIVKKLCHLMEGDIQVQSKENKGSNFSF 791
Cdd:cd16948    76 MGLYLVKKLCDKLGHKIDVESEVGEGTTFTI 106
REC_2_GGDEF cd17544
second phosphoacceptor receiver (REC) domain of uncharacterized GGDEF domain proteins; This ...
968-1086 2.77e-08

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: 53.29  E-value: 2.77e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  968 IRILLVEDNNINQIVASTTLKKIGINSIDiAENGQHALEYLKQttsHNPYSLILMDCQMPVMDGYQATTHIRvnEAGSKN 1047
Cdd:cd17544     1 IKVLVVDDSATSRNHLRALLRRHNFQVLE-AANGQEALEVLEQ---HPDIKLVITDYNMPEMDGFELVREIR--KKYSRD 74
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 503229768 1048 pPITIIAMTANAMVGDKAKCLQVGMNDYISKPIAQDILF 1086
Cdd:cd17544    75 -QLAIIGISASGDNALSARFIKAGANDFLTKPFLPEEFY 112
PAS cd00130
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
458-546 3.68e-08

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


Pssm-ID: 238075 [Multi-domain]  Cd Length: 103  Bit Score: 52.25  E-value: 3.68e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  458 VFLNSEFEKITGYSKEEMLGINCSLLQGPNTDKNAIDIITNAIKTLKTQRIEILNYKKDGTEFWNSLQISPVFNEQQQLT 537
Cdd:cd00130    15 LYANPAAEQLLGYSPEELIGKSLLDLIHPEDREELRERLENLLSGGEPVTLEVRLRRKDGSVIWVLVSLTPIRDEGGEVI 94

                  ....*....
gi 503229768  538 AYVGIQQDI 546
Cdd:cd00130    95 GLLGVVRDI 103
REC_OmpR_BaeR-like cd19938
phosphoacceptor receiver (REC) domain of BaeR-like OmpR family response regulators; BaeR is ...
969-1079 4.19e-08

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


Pssm-ID: 381165 [Multi-domain]  Cd Length: 114  Bit Score: 52.38  E-value: 4.19e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  969 RILLVEDN-NINQIVASTtLKKIGInSIDIAENGQHALEYLKqttsHNPYSLILMDCQMPVMDGYQATTHIRvneagsKN 1047
Cdd:cd19938     1 RILIVEDEpKLAQLLIDY-LRAAGY-APTLLAHGDQVLPYVR----HTPPDLILLDLMLPGTDGLTLCREIR------RF 68
                          90       100       110
                  ....*....|....*....|....*....|..
gi 503229768 1048 PPITIIAMTANAMVGDKAKCLQVGMNDYISKP 1079
Cdd:cd19938    69 SDVPIIMVTARVEEIDRLLGLELGADDYICKP 100
LytT COG3279
DNA-binding response regulator, LytR/AlgR family [Transcription, Signal transduction ...
968-1091 6.15e-08

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


Pssm-ID: 442510 [Multi-domain]  Cd Length: 235  Bit Score: 54.82  E-value: 6.15e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  968 IRILLVEDNNINQIVASTTLKKI-GINSIDIAENGQHALEYLKQttshNPYSLILMDCQMPVMDGYQATTHIRvneagSK 1046
Cdd:COG3279     2 MKILIVDDEPLARERLERLLEKYpDLEVVGEASNGEEALELLEE----HKPDLVFLDIQMPGLDGFELARQLR-----EL 72
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 503229768 1047 NPPITIIAMTANAmvgDKA-KCLQVGMNDYISKPIAQDILFKKLLK 1091
Cdd:COG3279    73 DPPPPIIFTTAYD---EYAlEAFEVNAVDYLLKPIDEERLAKALEK 115
REC_OmpR_KdpE-like cd17620
phosphoacceptor receiver (REC) domain of KdpE-like OmpR family response regulators; KdpE is a ...
970-1079 6.53e-08

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


Pssm-ID: 381135 [Multi-domain]  Cd Length: 99  Bit Score: 51.40  E-value: 6.53e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  970 ILLVEDNNinQI--VASTTLKKIGInSIDIAENGQHALeylKQTTSHNPySLILMDCQMPVMDGYQATTHIRVNeagSKN 1047
Cdd:cd17620     1 ILVIEDEP--QIrrFLRTALEAHGY-RVFEAETGQEGL---LEAATRKP-DLIILDLGLPDMDGLEVIRRLREW---SAV 70
                          90       100       110
                  ....*....|....*....|....*....|..
gi 503229768 1048 PpitIIAMTANAMVGDKAKCLQVGMNDYISKP 1079
Cdd:cd17620    71 P---VIVLSARDEESDKIAALDAGADDYLTKP 99
HATPase_DpiB-CitA-like cd16915
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
689-790 1.04e-07

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


Pssm-ID: 340392 [Multi-domain]  Cd Length: 104  Bit Score: 51.13  E-value: 1.04e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  689 ILTNLVNNALKF---THKGEVQVIAKLTPINNNqmrFNCQVIDSGIGISAAQQAKLF-KSFSqvdsstTRKYGGTGLGLA 764
Cdd:cd16915     4 IVGNLIDNALDAlaaTGAPNKQVEVFLRDEGDD---LVIEVRDTGPGIAPELRDKVFeRGVS------TKGQGERGIGLA 74
                          90       100
                  ....*....|....*....|....*.
gi 503229768  765 IVKKLCHLMEGDIQVQSKENKGSNFS 790
Cdd:cd16915    75 LVRQSVERLGGSITVESEPGGGTTFS 100
REC_OmpR_YycF-like cd17614
phosphoacceptor receiver (REC) domain of YrcF-like OmpR family response regulators; YycF ...
970-1079 1.21e-07

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


Pssm-ID: 381130 [Multi-domain]  Cd Length: 115  Bit Score: 51.27  E-value: 1.21e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  970 ILLVEDN-NINQIVaSTTLKKIGINsIDIAENGQHALEYLKQttsHNPySLILMDCQMPVMDGYQATTHIRvneaGSKNP 1048
Cdd:cd17614     1 ILVVDDEkPISDIL-KFNLTKEGYE-VVTAYDGREALEKVEE---EQP-DLILLDLMLPEKDGLEVCREVR----KTSNV 70
                          90       100       110
                  ....*....|....*....|....*....|.
gi 503229768 1049 PItiIAMTANAMVGDKAKCLQVGMNDYISKP 1079
Cdd:cd17614    71 PI--IMLTAKDSEVDKVLGLELGADDYVTKP 99
REC_OmpR_MtPhoP-like cd17615
phosphoacceptor receiver (REC) domain of MtPhoP-like OmpR family response regulators; ...
969-1079 1.24e-07

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: 51.20  E-value: 1.24e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  969 RILLVEDN-NINQIVaSTTLKKIGINsIDIAENGQHALEYLKQttsHNPYSLILmDCQMPVMDGYQATTHIRvneagSKN 1047
Cdd:cd17615     1 RVLVVDDEpNITELL-SMALRYEGWD-VETAADGAEALAAARE---FRPDAVVL-DIMLPDMDGLEVLRRLR-----ADG 69
                          90       100       110
                  ....*....|....*....|....*....|..
gi 503229768 1048 PPITIIAMTANAMVGDKAKCLQVGMNDYISKP 1079
Cdd:cd17615    70 PDVPVLFLTAKDSVEDRIAGLTAGGDDYVTKP 101
HATPase_TmoS-FixL-DctS-like cd16920
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
686-791 1.39e-07

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: 50.86  E-value: 1.39e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  686 LKQILTNLVNNALKFTHKGEV---QVIAKLTPINNNQMRFncQVIDSGIGISAAQQAKLFKSFsqvdssTTRKYGGTGLG 762
Cdd:cd16920     1 IQQVLINLVRNGIEAMSEGGCerrELTIRTSPADDRAVTI--SVKDTGPGIAEEVAGQLFDPF------YTTKSEGLGMG 72
                          90       100
                  ....*....|....*....|....*....
gi 503229768  763 LAIVKKLCHLMEGDIQVQSKENKGSNFSF 791
Cdd:cd16920    73 LSICRSIIEAHGGRLSVESPAGGGATFQF 101
REC_OmpR_EcPhoP-like cd19934
phosphoacceptor receiver (REC) domain of EcPhoP-like OmpR family response regulators; ...
970-1079 1.43e-07

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


Pssm-ID: 381161 [Multi-domain]  Cd Length: 117  Bit Score: 51.13  E-value: 1.43e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  970 ILLVEDNNINQIVASTTLKKIGiNSIDIAENGQHALEYLKQttshNPYSLILMDCQMPVMDGYQATTHIRvnEAGSKNPp 1049
Cdd:cd19934     1 LLLVEDDALLAAQLKEQLSDAG-YVVDVAEDGEEALFQGEE----EPYDLVVLDLGLPGMDGLSVLRRWR--SEGRATP- 72
                          90       100       110
                  ....*....|....*....|....*....|
gi 503229768 1050 itIIAMTANAMVGDKAKCLQVGMNDYISKP 1079
Cdd:cd19934    73 --VLILTARDSWQDKVEGLDAGADDYLTKP 100
REC_citrate_TCS cd19925
phosphoacceptor receiver (REC) domain of citrate family two-component system response ...
968-1092 2.23e-07

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


Pssm-ID: 381152 [Multi-domain]  Cd Length: 118  Bit Score: 50.32  E-value: 2.23e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  968 IRILLVEDNNINQIVASTTLKKI-GINSIDIAENGQHALEYLKQTtshnPYSLILMDCQMPVMDGYQATTHIRvneagSK 1046
Cdd:cd19925     1 INVLIVEDDPMVAEIHRAYVEQVpGFTVIGTAGTGEEALKLLKER----QPDLILLDIYLPDGNGLDLLRELR-----AA 71
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 503229768 1047 NPPITIIAMTANAMVGDKAKCLQVGMNDYISKPIAQDILFKKLLKW 1092
Cdd:cd19925    72 GHDVDVIVVTAANDVETVREALRLGVVDYLIKPFTFERLRQRLERY 117
psREC_PRR cd17582
pseudo receiver domain of pseudo-response regulators; In Arabidopsis, five pseudo-response ...
970-1079 2.34e-07

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: 50.09  E-value: 2.34e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  970 ILLVEDNNINQIVASTTLKKIGINSIDiAENGQHALEYLKQTTSHnpYSLILMDCQMPVMDGYQATTHIRVNEAgSKNpp 1049
Cdd:cd17582     1 VLLVENDDSTRQIVTALLRKCSYEVTA-ASDGLQAWDVLEDEQNE--IDLILTEVDLPVSSGFKLLSYIMRHKI-CKN-- 74
                          90       100       110
                  ....*....|....*....|....*....|
gi 503229768 1050 ITIIAMTANAMVGDKAKCLQVGMNDYISKP 1079
Cdd:cd17582    75 IPVIMMSSQDSVGVVFKCLSKGAADYLVKP 104
HATPase_CreC-like cd16945
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
682-780 3.01e-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: 49.77  E-value: 3.01e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  682 DAGRLKQILTNLVNNALKFTHKGevQVIAKLTPINNNQMRFncQVIDSGIGISAAQQAKLFKSFSqvdsSTTRKYGG--- 758
Cdd:cd16945     1 DPFLLRQAINNLLDNAIDFSPEG--GLIALQLEADTEGIEL--LVFDEGSGIPDYALNRVFERFY----SLPRPHSGqks 72
                          90       100
                  ....*....|....*....|..
gi 503229768  759 TGLGLAIVKKLCHLMEGDIQVQ 780
Cdd:cd16945    73 TGLGLAFVQEVAQLHGGRITLR 94
REC_hyHK cd17598
phosphoacceptor receiver (REC) domain of uncharacterized hybrid sensor histidine kinase ...
970-1079 3.84e-07

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


Pssm-ID: 381128 [Multi-domain]  Cd Length: 118  Bit Score: 50.02  E-value: 3.84e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  970 ILLVEDNNINQIVASTTLKKIGInSIDIAENGQHALEYLKQttsHNPySLILMDCQMPVMDGYQATTHIRVNEaGSKNPP 1049
Cdd:cd17598     1 ILIVEDSPTQAEQLKHILEEQGY-KVQVARNGREALAMLAE---HRP-TLVISDIVMPEMDGYELCRKIKSDP-DLKDIP 74
                          90       100       110
                  ....*....|....*....|....*....|
gi 503229768 1050 itIIAMTANAMVGDKAKCLQVGMNDYISKP 1079
Cdd:cd17598    75 --VILLTTLSDPRDVIRGLECGADNFITKP 102
REC_OmpR_kpRstA-like cd17622
phosphoacceptor receiver (REC) domain of kpRstA-like OmpR family response regulators; ...
969-1089 5.37e-07

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


Pssm-ID: 381137 [Multi-domain]  Cd Length: 116  Bit Score: 49.30  E-value: 5.37e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  969 RILLVEDN-NINQIVASTtLKKIGINsIDIAENGQHALEYLKQttsHNPySLILMDCQMPVMDGYQATTHIRVNEAGSkn 1047
Cdd:cd17622     2 RILLVEDDpKLARLIADF-LESHGFN-VVVEHRGDRALEVIAR---EKP-DAVLLDIMLPGIDGLTLCRDLRPKYQGP-- 73
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 503229768 1048 ppitIIAMTANAMVGDKAKCLQVGMNDYISKPIAQDILFKKL 1089
Cdd:cd17622    74 ----ILLLTALDSDIDHILGLELGADDYVVKPVEPAVLLARL 111
PRK15479 PRK15479
transcriptional regulator TctD;
968-1079 5.82e-07

transcriptional regulator TctD;


Pssm-ID: 185376 [Multi-domain]  Cd Length: 221  Bit Score: 51.65  E-value: 5.82e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  968 IRILLVEDNNinqiVASTTLKKIGINS---IDIAENGQHAlEYLKQTTShnpYSLILMDCQMPVMDGYQATTHIRvnEAG 1044
Cdd:PRK15479    1 MRLLLAEDNR----ELAHWLEKALVQNgfaVDCVFDGLAA-DHLLQSEM---YALAVLDINMPGMDGLEVLQRLR--KRG 70
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 503229768 1045 SKNPpitIIAMTANAMVGDKAKCLQVGMNDYISKP 1079
Cdd:PRK15479   71 QTLP---VLLLTARSAVADRVKGLNVGADDYLPKP 102
PAS pfam00989
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
298-414 6.26e-07

PAS fold; The PAS fold corresponds to the structural domain that has previously been defined as PAS and PAC motifs. The PAS fold appears in archaea, eubacteria and eukarya. This domain can bind gases (O2, CO and NO), FAD, 4-hydroxycinnamic acid and NAD+ (Matilla et.al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).


Pssm-ID: 395786 [Multi-domain]  Cd Length: 113  Bit Score: 48.95  E-value: 6.26e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768   298 ARYELAVKGSNDGIWDWDIVTNEVYFSPRISVLLGYDEND---KNalphcadaLYKLLHPDDITKHKKQIANHLIS-NIP 373
Cdd:pfam00989    1 EDLRAILESLPDGIFVVDEDGRILYVNAAAEELLGLSREEvigKS--------LLDLIPEEDDAEVAELLRQALLQgEES 72
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 503229768   374 FNYDYRLKTKSGAYRYFTVKGMALRNEHNKAIRMAGSVTDI 414
Cdd:pfam00989   73 RGFEVSFRVPDGRPRHVEVRASPVRDAGGEILGFLGVLRDI 113
REC_RssB-like cd17555
phosphoacceptor receiver (REC) domain of Pseudomonas aeruginosa RssB and similar domains; ...
998-1081 9.48e-07

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: 48.74  E-value: 9.48e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  998 AENGQHALEYLKQttsHNPySLILMDCQMPVMDGYQATTHIRvneagSKNPPITIIAMTANAMVGDKAKCLQVGMNDYIS 1077
Cdd:cd17555    30 AADGRQGLELFRS---EQP-DLVLCDLRMPEMDGLEVLKQIT-----KESPDTPVIVVSGAGVMSDAVEALRLGAWDYLT 100

                  ....
gi 503229768 1078 KPIA 1081
Cdd:cd17555   101 KPIE 104
PRK10336 PRK10336
two-component system response regulator QseB;
968-1081 1.40e-06

two-component system response regulator QseB;


Pssm-ID: 182387 [Multi-domain]  Cd Length: 219  Bit Score: 50.66  E-value: 1.40e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  968 IRILLVEDNNINQIVASTTLKKIGInSIDIAENGQHALEYLKQTtshnPYSLILMDCQMPVMDGYQATTHIRvnEAGSKN 1047
Cdd:PRK10336    1 MRILLIEDDMLIGDGIKTGLSKMGF-SVDWFTQGRQGKEALYSA----PYDAVILDLTLPGMDGRDILREWR--EKGQRE 73
                          90       100       110
                  ....*....|....*....|....*....|....
gi 503229768 1048 PpitIIAMTANAMVGDKAKCLQVGMNDYISKPIA 1081
Cdd:PRK10336   74 P---VLILTARDALAERVEGLRLGADDYLCKPFA 104
HATPase_Glnl-NtrB-like cd16918
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
686-781 1.41e-06

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: 48.17  E-value: 1.41e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  686 LKQILTNLVNNA---LKFTHkGEV----QVIAKLTpINNNQMRFNCQ--VIDSGIGISAAQQAKLFKSFsqvdssTTRKY 756
Cdd:cd16918     1 LIQVFLNLVRNAaqaLAGSG-GEIilrtRTQRQVT-LGHPRHRLALRvsVIDNGPGIPPDLQDTIFYPM------VSGRE 72
                          90       100
                  ....*....|....*....|....*
gi 503229768  757 GGTGLGLAIVKKLCHLMEGDIQVQS 781
Cdd:cd16918    73 NGTGLGLAIAQNIVSQHGGVIECDS 97
REC_PatA-like cd17602
phosphoacceptor receiver (REC) domain of PatA and similar domains; Nostoc sp. (or Anabaena sp.) ...
970-1079 1.73e-06

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: 47.36  E-value: 1.73e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  970 ILLVEDNNINQIVASTTLKKIGINSIDIaengQHALEYLKQTTSHNPySLILMDCQMPVMDGYQATTHIRVNEAgSKNPP 1049
Cdd:cd17602     1 VACVDDRPSIQKMIEYFLEKQGFRVVVI----DDPLRALTTLLNSKP-DLILIDIDMPDLDGYELCSLLRKSSA-LKDTP 74
                          90       100       110
                  ....*....|....*....|....*....|
gi 503229768 1050 itIIAMTANAMVGDKAKCLQVGMNDYISKP 1079
Cdd:cd17602    75 --IIMLTGKDGLVDRIRAKMAGASGYLTKP 102
HATPase_Phy-like cd16932
Histidine kinase-like ATPase domain of plant phytochromes similar to Arabidopsis thaliana ...
681-778 2.00e-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: 47.65  E-value: 2.00e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  681 GDAGRLKQILTNLVNNALKFT--HKG--EVQVIAKLTPI--NNNQMRFNCQVIDSGIGISAAQQAKLFKSfsqvDSSTTR 754
Cdd:cd16932     2 GDQIRLQQVLADFLLNAVRFTpsPGGwvEIKVSPTKKQIgdGVHVIHLEFRITHPGQGLPEELVQEMFEE----NQWTTQ 77
                          90       100
                  ....*....|....*....|....
gi 503229768  755 KyggtGLGLAIVKKLCHLMEGDIQ 778
Cdd:cd16932    78 E----GLGLSISRKLVKLMNGDVR 97
HATPase_NtrY-like cd16944
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
682-787 3.18e-06

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: 47.15  E-value: 3.18e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  682 DAGRLKQILTNLVNNALKFTH-----KGEVQVIAKltpiNNNQMRFNCQVIDSGIGISAAQQAKLFKSFsqvdssTTRKY 756
Cdd:cd16944     1 DTTQISQVLTNILKNAAEAIEgrpsdVGEVRIRVE----ADQDGRIVLIVCDNGKGFPREMRHRATEPY------VTTRP 70
                          90       100       110
                  ....*....|....*....|....*....|.
gi 503229768  757 GGTGLGLAIVKKLCHLMEGDIQVQSKENKGS 787
Cdd:cd16944    71 KGTGLGLAIVKKIMEEHGGRISLSNREAGGA 101
PRK10693 PRK10693
two-component system response regulator RssB;
998-1081 3.23e-06

two-component system response regulator RssB;


Pssm-ID: 182652 [Multi-domain]  Cd Length: 303  Bit Score: 50.37  E-value: 3.23e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  998 AENGQHALEYLKQTTShnpySLILMDCQMPVMDGYQATTHIRVNeaGSKNpPITIIAMTANamVGDKAKCLQVGMNDYIS 1077
Cdd:PRK10693    3 AANGVDALELLGGFTP----DLIICDLAMPRMNGIEFVEHLRNR--GDQT-PVLVISATEN--MADIAKALRLGVQDVLL 73

                  ....
gi 503229768 1078 KPIA 1081
Cdd:PRK10693   74 KPVK 77
HATPase_PhoQ-like cd16954
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
644-790 3.43e-06

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: 47.63  E-value: 3.43e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  644 NLCNMLDdfietiAIHAhSKNIPLMLDIEHlEYAFViGDAGRLKQILTNLVNNALKFTHKgEVQVIAKLTPinnNQMRFn 723
Cdd:cd16954     5 SLCSALN------KVYQ-RKGVSISLDISP-ELRFP-GERNDLMELLGNLLDNACKWCLE-FVEVTARQTD---GGLHL- 70
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 503229768  724 cQVIDSGIGISAAQQAKLFKSFSQVDSSTTrkygGTGLGLAIVKKLCHLMEGDIQVQSKENKGSNFS 790
Cdd:cd16954    71 -IVDDDGPGVPESQRSKIFQRGQRLDEQRP----GQGLGLAIAKEIVEQYGGELSLSDSPLGGARFE 132
CitB COG2197
DNA-binding response regulator, NarL/FixJ family, contains REC and HTH domains [Signal ...
968-1038 4.07e-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: 47.19  E-value: 4.07e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 503229768  968 IRILLVEDNNI-NQIVASTTLKKIGINSIDIAENGQHALEYLKQttsHNPySLILMDCQMPVMDGYQATTHI 1038
Cdd:COG2197     2 IRVLIVDDHPLvREGLRALLEAEPDIEVVGEAADGEEALELLEE---LRP-DVVLLDIRMPGMDGLEALRRL 69
REC_TrrA-like cd17554
phosphoacceptor receiver (REC) domain of Thermotoga maritima response regulator TrrA and ...
969-1057 7.51e-06

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


Pssm-ID: 381106 [Multi-domain]  Cd Length: 113  Bit Score: 46.06  E-value: 7.51e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  969 RILLVEDN-NINQIVASTtLKKIGINsIDIAENGQHALEYLKQttshNPYSLILMDCQMPVMDGYQATTHIRvneagSKN 1047
Cdd:cd17554     2 KILVVDDEeNIRELYKEE-LEDEGYE-VVTAGNGEEALEKLES----EDPDLVILDIKMPGMDGLETLRKIR-----EKK 70
                          90
                  ....*....|
gi 503229768 1048 PPITIIAMTA 1057
Cdd:cd17554    71 PDLPVIICTA 80
PRK11086 PRK11086
sensory histidine kinase DcuS; Provisional
689-793 1.17e-05

sensory histidine kinase DcuS; Provisional


Pssm-ID: 236839 [Multi-domain]  Cd Length: 542  Bit Score: 49.14  E-value: 1.17e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  689 ILTNLVNNAL---KFTHKGEVQViakLTPINNNQMrfNCQVIDSGIGISAAQQAKLF-KSFSQvdssttrKYGGTGLGLA 764
Cdd:PRK11086  437 ILGNLIENALeavGGEEGGEISV---SLHYRNGWL--HCEVSDDGPGIAPDEIDAIFdKGYST-------KGSNRGVGLY 504
                          90       100
                  ....*....|....*....|....*....
gi 503229768  765 IVKKLCHLMEGDIQVQSKENKGSNFSFNV 793
Cdd:PRK11086  505 LVKQSVENLGGSIAVESEPGVGTQFFVQI 533
PRK10161 PRK10161
phosphate response regulator transcription factor PhoB;
969-1089 1.68e-05

phosphate response regulator transcription factor PhoB;


Pssm-ID: 182277 [Multi-domain]  Cd Length: 229  Bit Score: 47.41  E-value: 1.68e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  969 RILLVEDNNINQIVASTTLKKIGINSIDiAENGQHALEYLKQttshnPY-SLILMDCQMPVMDGYQATTHIRvNEAGSKN 1047
Cdd:PRK10161    4 RILVVEDEAPIREMVCFVLEQNGFQPVE-AEDYDSAVNQLNE-----PWpDLILLDWMLPGGSGIQFIKHLK-RESMTRD 76
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 503229768 1048 PPItiIAMTANAMVGDKAKCLQVGMNDYISKPIAQDILFKKL 1089
Cdd:PRK10161   77 IPV--VMLTARGEEEDRVRGLETGADDYITKPFSPKELVARI 116
REC_NtrC cd19919
phosphoacceptor receiver (REC) domain of DNA-binding transcriptional regulator NtrC; ...
999-1079 1.77e-05

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: 44.96  E-value: 1.77e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  999 ENGQHALEYLKqttSHNPySLILMDCQMPVMDGYQATTHIRvneagSKNPPITIIAMTANAMVGDKAKCLQVGMNDYISK 1078
Cdd:cd19919    31 ENAQEALAALA---SSQP-DVLISDIRMPGMDGLALLAQIK-----QRHPDLPVIIMTAHSDLDSAVSAYQGGAFEYLPK 101

                  .
gi 503229768 1079 P 1079
Cdd:cd19919   102 P 102
PRK00742 PRK00742
chemotaxis-specific protein-glutamate methyltransferase CheB;
968-1090 1.96e-05

chemotaxis-specific protein-glutamate methyltransferase CheB;


Pssm-ID: 234828 [Multi-domain]  Cd Length: 354  Bit Score: 48.22  E-value: 1.96e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  968 IRILLVEDNN-----INQIVASTTlkkiGINSIDIAENGQHALEYLKQttsHNPySLILMDCQMPVMDGYQATTHIRvne 1042
Cdd:PRK00742    4 IRVLVVDDSAfmrrlISEILNSDP----DIEVVGTAPDGLEAREKIKK---LNP-DVITLDVEMPVMDGLDALEKIM--- 72
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 503229768 1043 agSKNP-PITII-AMTANamvGDKA--KCLQVGMNDYISKP---IAQDIL-FKKLL 1090
Cdd:PRK00742   73 --RLRPtPVVMVsSLTER---GAEItlRALELGAVDFVTKPflgISLGMDeYKEEL 123
REC_OmpR_CtrA cd17616
phosphoacceptor receiver (REC) domain of CtrA-like OmpR family response regulators; CtrA is ...
970-1085 2.60e-05

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: 44.32  E-value: 2.60e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  970 ILLVEDNNINQIVASTTLKKIGINsIDIAENGQHALEYLKQTTshnpYSLILMDCQMPVMDGYQATTHIRVneAGSKNPp 1049
Cdd:cd17616     1 VLLIEDDSATAQSIELMLKSEGFN-VYTTDLGEEGLDLGKLYD----YDIILLDLNLPDMSGYEVLRTLRL--AKVKTP- 72
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 503229768 1050 itIIAMTANAMVGDKAKCLQVGMNDYISKPIAQDIL 1085
Cdd:cd17616    73 --ILILSGLADIEDKVKGLGFGADDYMTKPFHKDEL 106
PRK15115 PRK15115
response regulator GlrR; Provisional
966-1087 2.95e-05

response regulator GlrR; Provisional


Pssm-ID: 185070 [Multi-domain]  Cd Length: 444  Bit Score: 47.91  E-value: 2.95e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  966 KNIRILLVEDNninqivaSTTLKKIGIN------SIDIAENGQHALEYLKQttshNPYSLILMDCQMPVMDGYQATTHIR 1039
Cdd:PRK15115    4 KPAHLLLVDDD-------PGLLKLLGMRltsegySVVTAESGQEALRVLNR----EKVDLVISDLRMDEMDGMQLFAEIQ 72
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 503229768 1040 VNEAGsknppITIIAMTANAMVGDKAKCLQVGMNDYISKPIAQDILFK 1087
Cdd:PRK15115   73 KVQPG-----MPVIILTAHGSIPDAVAATQQGVFSFLTKPVDRDALYK 115
PRK10955 PRK10955
envelope stress response regulator transcription factor CpxR;
969-1079 3.25e-05

envelope stress response regulator transcription factor CpxR;


Pssm-ID: 182864 [Multi-domain]  Cd Length: 232  Bit Score: 46.72  E-value: 3.25e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  969 RILLVEDNNINQIVASTTLKKIGINsIDIAENGQHALEYLKQTTShnpysLILMDCQMPVMDGYQATTHIRvneagsKNP 1048
Cdd:PRK10955    3 KILLVDDDRELTSLLKELLEMEGFN-VIVAHDGEQALDLLDDSID-----LLLLDVMMPKKNGIDTLKELR------QTH 70
                          90       100       110
                  ....*....|....*....|....*....|.
gi 503229768 1049 PITIIAMTANAMVGDKAKCLQVGMNDYISKP 1079
Cdd:PRK10955   71 QTPVIMLTARGSELDRVLGLELGADDYLPKP 101
REC_OmpR_BfmR-like cd19939
phosphoacceptor receiver (REC) domain of BfmR-like OmpR family response regulators; ...
969-1079 4.06e-05

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: 43.90  E-value: 4.06e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  969 RILLVEDN-NINQIVASTtLKKIGINsIDIAENGQHALEYLKQTtshnPYSLILMDCQMPVMDGYQATTHIRVNeagSKN 1047
Cdd:cd19939     1 RILIVEDElELARLTRDY-LIKAGLE-VSVFTDGQRAVRRIIDE----QPSLVVLDIMLPGMDGLTVCREVREH---SHV 71
                          90       100       110
                  ....*....|....*....|....*....|..
gi 503229768 1048 PpitIIAMTANAMVGDKAKCLQVGMNDYISKP 1079
Cdd:cd19939    72 P---ILMLTARTEEMDRVLGLEMGADDYLCKP 100
PAS smart00091
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
298-368 4.40e-05

PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising identification of a PAS domain was that in EAG-like K+-channels.


Pssm-ID: 214512  Cd Length: 67  Bit Score: 42.39  E-value: 4.40e-05
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 503229768    298 ARYELAVKGSNDGIWDWDIVTNEVYFSPRISVLLGYDENDKNALPhcadaLYKLLHPDDITKHKKQIANHL 368
Cdd:smart00091    1 ERLRAILESLPDGIFVLDLDGRILYANPAAEELLGYSPEELIGKS-----LLELIHPEDRERVQEALQRLL 66
marine_sort_HK TIGR03785
proteobacterial dedicated sortase system histidine kinase; This histidine kinase protein is ...
573-779 4.49e-05

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: 47.43  E-value: 4.49e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768   573 FLAAMSHEIRTPMNGVLGMLNLiLDSSLNEKQHHQ-VSIALNSANSLLNIINDILDFSKVDAGKLELEELEFNLCNMLDD 651
Cdd:TIGR03785  488 MSSRLSHELRTPVAVVRSSLEN-LELQALEQEKQKyLERAREGTERLSMILNNMSEATRLEQAIQSAEVEDFDLSEVLSG 566
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768   652 FIE----TIAIHAHSKNIP---LMLDiehleyafviGDAGRLKQILTNLVNNALKFTHKGEVQVIaKLTPINNNQMRFnc 724
Cdd:TIGR03785  567 CMQgyqmTYPPQRFELNIPetpLVMR----------GSPELIAQMLDKLVDNAREFSPEDGLIEV-GLSQNKSHALLT-- 633
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 503229768   725 qVIDSGIGISAAQQAKLFKSFSQVDSSTTRKYGGTGLGLAIVKKLCHLMEGDIQV 779
Cdd:TIGR03785  634 -VSNEGPPLPEDMGEQLFDSMVSVRDQGAQDQPHLGLGLYIVRLIADFHQGRIQA 687
HATPase_ETR2_ERS2-EIN4-like cd16938
Histidine kinase-like ATPase domain of Arabidopsis thaliana ETR2, ERS2, and EIN4, and related ...
678-795 5.83e-05

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: 43.99  E-value: 5.83e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  678 FVIGDAGRLKQILTNLVNNALKFTHKG---EVQVIAKLTPINNNQMRF--------NCQV-IDSGIGISAAQQAKLFKSF 745
Cdd:cd16938     4 VVVGDERRVFQVLLHMLGNLLKMRNGGgniTFRVFLEGGSEDRSDRDWgpwrpsmsDESVeIRFEVEINDSGSPSIESAS 83
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 503229768  746 SQvdSSTTRKYG----GTGLGLAIVKKLCHLMEGDIQVQSkeNKGSNFSFNVVL 795
Cdd:cd16938    84 MR--NSLNRRYNlselGEHLSFSICKQLVQLMGGNIWIVP--GSGLGTTMSLLL 133
pleD PRK09581
response regulator PleD; Reviewed
998-1098 7.06e-05

response regulator PleD; Reviewed


Pssm-ID: 236577 [Multi-domain]  Cd Length: 457  Bit Score: 46.82  E-value: 7.06e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  998 AENGQHALEYLKQTtshnPYSLILMDCQMPVMDGY---------QATTHIrvneagsknpPITIIamTANAMVGDKAKCL 1068
Cdd:PRK09581   32 ASSGAEAIAICERE----QPDIILLDVMMPGMDGFevcrrlksdPATTHI----------PVVMV--TALDDPEDRVRGL 95
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 503229768 1069 QVGMNDYISKPIAQDILF---KKL--LKWLPYELK 1098
Cdd:PRK09581   96 EAGADDFLTKPINDVALFarvKSLtrLKMVIDELR 130
PRK09836 PRK09836
DNA-binding transcriptional activator CusR; Provisional
968-1090 8.53e-05

DNA-binding transcriptional activator CusR; Provisional


Pssm-ID: 182102 [Multi-domain]  Cd Length: 227  Bit Score: 45.30  E-value: 8.53e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  968 IRILLVEDNNINQIVASTTLKKIGInSIDIAENGQHALeYLKQTTShnpYSLILMDCQMPVMDGYQATTHIRvneagSKN 1047
Cdd:PRK09836    1 MKLLIVEDEKKTGEYLTKGLTEAGF-VVDLADNGLNGY-HLAMTGD---YDLIILDIMLPDVNGWDIVRMLR-----SAN 70
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 503229768 1048 PPITIIAMTANAMVGDKAKCLQVGMNDYISKPIAqdilFKKLL 1090
Cdd:PRK09836   71 KGMPILLLTALGTIEHRVKGLELGADDYLVKPFA----FAELL 109
REC_OmpR_RegX3-like cd17621
phosphoacceptor receiver (REC) domain of RegX3-like OmpR family response regulators; RegX3 is ...
970-1079 9.39e-05

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


Pssm-ID: 381136 [Multi-domain]  Cd Length: 99  Bit Score: 42.57  E-value: 9.39e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  970 ILLVEDNNINQIVASTTLKKIGInSIDIAENGQHALEYLKQttshNPYSLILMDCQMPVMDGYQATTHIRvneaGSKNPP 1049
Cdd:cd17621     1 VLVVEDEESFSDPLAYLLRKEGF-EVTVATDGPAALAEFDR----AGADIVLLDLMLPGLSGTEVCRQLR----ARSNVP 71
                          90       100       110
                  ....*....|....*....|....*....|
gi 503229768 1050 ItiIAMTANAMVGDKAKCLQVGMNDYISKP 1079
Cdd:cd17621    72 V--IMVTAKDSEIDKVVGLELGADDYVTKP 99
PleD COG3706
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate ...
812-932 9.44e-05

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: 44.51  E-value: 9.44e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  812 SLNILIVCSNQTQSSILHKQFTKWGATAVISPSAKQAVQICQQYIekqnlcFDLIMIDMQLSDGDALTLSKTLDKEVDLM 891
Cdd:COG3706     1 PARILVVDDDPTNRKLLRRLLEAAGYEVVEAADGEEALELLQEHR------PDLILLDLEMPDMDGLELCRRLRADPRTA 74
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 503229768  892 AAHVVLMTTGELNKQRDLYQASRFSAIVTKPIITQNLFKML 932
Cdd:COG3706    75 DIPIIFLTALDDEEDRARALEAGADDYLTKPFDPEELLARV 115
REC_Spo0F-like cd17553
phosphoacceptor receiver (REC) domain of Spo0F and similar domains; Spo0F, a stand-alone ...
969-1094 1.46e-04

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


Pssm-ID: 381105 [Multi-domain]  Cd Length: 117  Bit Score: 42.54  E-value: 1.46e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  969 RILLVEDNNINQIVASTTLKKIGINSIDiAENGQHALEYLKQttshNPYSLILMDCQMPVMDGYQATTHIRVneagsKNP 1048
Cdd:cd17553     2 KILIVDDQYGIRILLNEVFNKEGYQTFQ-AANGLQALDIVTK----ERPDLVLLDMKIPGMDGIEILKRMKV-----IDE 71
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 503229768 1049 PITIIAMTANAMVGDKAKCLQVGMNDYISKPIAQDILFKKLLKWLP 1094
Cdd:cd17553    72 NIRVIIMTAYGELDMIQESKELGALTHFAKPFDIDEIRDAVKKYLP 117
COG3920 COG3920
Two-component sensor histidine kinase, HisKA and HATPase domains [Signal transduction ...
290-783 1.48e-04

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


Pssm-ID: 443125 [Multi-domain]  Cd Length: 495  Bit Score: 45.67  E-value: 1.48e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  290 REAIKQSEARYELAVKGSNDGIWDWDIVTNEVYFSPRISVLLGYDENDKNALPHCADALYKLLHPDDITKHKKQIANHLI 369
Cdd:COG3920    26 AAALLLALLALLLLALLLLALLLASALLALLALSAAALAAALAVALAAAVGAAAALLALLVLLLLLLLAAAALALALLLA 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  370 SNIPFNYDYRLKTKSGAYRYFTVKGMALRNEHNKAIRMAGSVTDITEQKRSQKALKQAKEQNDLLAQAIEScnvgISIAD 449
Cdd:COG3920   106 ALAGLLLLAALLLLRLVALLAALALLALLLLLLLLLAILALAELAVALAELAAALLLLAEELAALRLAAAA----LLLLL 181
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  450 ASVQGFPLVFLNSEFEKITGYSKEEMLGINCSLLQGPNTDKNAIDIITNAIKTLKTQRIEILNYKKDGTEFWNSLQISPV 529
Cdd:COG3920   182 AALLDLGLALAALAAAALLALLLALELLLALLLLLLLLLALLLVLLAALLRLRAAVLEELERRRRARGLGRLLLLLLLLL 261
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  530 FNEQQQLTAYVGIQQDITEQKAANQlliEAKAAAEQANIAKSEflaaMSHEIRTPMNGVLGMLNLILDSSLNEkqhhQVS 609
Cdd:COG3920   262 LLLRALLLLAAGIRLVITERKRAEE---ELEASLEEKELLLRE----LHHRVKNNLQVVSSLLRLQARRADDP----EAR 330
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  610 IALNSANS---LLNIINDIL----DFSKVDagkleleelefnLCNMLDDFIETIAIHAHSKNIPLMLDIEHL----EYAF 678
Cdd:COG3920   331 EALEESQNriqALALVHELLyqseDWEGVD------------LRDYLRELLEPLRDSYGGRGIRIELDGPDVelpaDAAV 398
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  679 VIGdagrLkqILTNLVNNALKF----THKGEVQVIAKLtpiNNNQMRFncQVIDSGIGISAaqqaklfksfsQVDSSTTR 754
Cdd:COG3920   399 PLG----L--ILNELVTNALKHaflsGEGGRIRVSWRR---EDGRLRL--TVSDNGVGLPE-----------DVDPPARK 456
                         490       500
                  ....*....|....*....|....*....
gi 503229768  755 kyggtGLGLAIVKKLCHLMEGDIQVQSKE 783
Cdd:COG3920   457 -----GLGLRLIRALVRQLGGTLELDRPE 480
PRK13560 PRK13560
hypothetical protein; Provisional
351-438 1.55e-04

hypothetical protein; Provisional


Pssm-ID: 106506 [Multi-domain]  Cd Length: 807  Bit Score: 45.82  E-value: 1.55e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  351 LLHPDDITKHKKQIANHLISNIP-FNYDYRLKTKSGAYRYFTVKGMALRNEHNKAIRMAGSVTDITEQKRSQKALKQAKE 429
Cdd:PRK13560  524 IIHPADLEQVAAEVAEFAAQGVDrFEQEYRILGKGGAVCWIDDQSAAERDEEGQISHFEGIVIDISERKHAEEKIKAALT 603

                  ....*....
gi 503229768  430 QNDLLAQAI 438
Cdd:PRK13560  604 EKEVLLKEI 612
REC_HP-RR-like cd17573
phosphoacceptor receiver (REC) domain of orphan response regulator HP-RR and similar proteins; ...
970-1085 1.73e-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: 42.03  E-value: 1.73e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  970 ILLVEDNNINQIVASTTLKKIGINSiDIAENGQHAlEYLKQTTShnpYSLILMDCQMPVMDGYQATTHIRvneagSKNPP 1049
Cdd:cd17573     1 ILLIEDDSTLGKEISKGLNEKGYQA-DVAESLKDG-EYYIDIRN---YDLVLVSDKLPDGNGLSIVSRIK-----EKHPS 70
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 503229768 1050 ITIIAMTANAMVGDKAKCLQVGMNDYISKPIAQDIL 1085
Cdd:cd17573    71 IVVIVLSDNPKTEQEIEAFKEGADDYIAKPFDFKVL 106
PRK10643 PRK10643
two-component system response regulator PmrA;
968-1081 1.92e-04

two-component system response regulator PmrA;


Pssm-ID: 182612 [Multi-domain]  Cd Length: 222  Bit Score: 44.26  E-value: 1.92e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  968 IRILLVEDNNINQIVASTTLKKIGInSIDIAENGQHALEYLkqTTSHnpYSLILMDCQMPVMDGYQATTHIRVNEAGSkn 1047
Cdd:PRK10643    1 MKILIVEDDTLLLQGLILALQTEGY-ACDCASTAREAEALL--ESGH--YSLVVLDLGLPDEDGLHLLRRWRQKKYTL-- 73
                          90       100       110
                  ....*....|....*....|....*....|....
gi 503229768 1048 pPITIiaMTANAMVGDKAKCLQVGMNDYISKPIA 1081
Cdd:PRK10643   74 -PVLI--LTARDTLEDRVAGLDVGADDYLVKPFA 104
PRK10816 PRK10816
two-component system response regulator PhoP;
968-1079 1.93e-04

two-component system response regulator PhoP;


Pssm-ID: 182755 [Multi-domain]  Cd Length: 223  Bit Score: 43.96  E-value: 1.93e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  968 IRILLVEDNNINQIVASTTLKKIGiNSIDIAENGQHALEYLKQttsHNPySLILMDCQMPVMDGyqaTTHIRVNEAGSKN 1047
Cdd:PRK10816    1 MRVLVVEDNALLRHHLKVQLQDAG-HQVDAAEDAKEADYYLNE---HLP-DIAIVDLGLPDEDG---LSLIRRWRSNDVS 72
                          90       100       110
                  ....*....|....*....|....*....|..
gi 503229768 1048 PPITIiaMTANAMVGDKAKCLQVGMNDYISKP 1079
Cdd:PRK10816   73 LPILV--LTARESWQDKVEVLSAGADDYVTKP 102
PRK13560 PRK13560
hypothetical protein; Provisional
376-566 1.95e-04

hypothetical protein; Provisional


Pssm-ID: 106506 [Multi-domain]  Cd Length: 807  Bit Score: 45.43  E-value: 1.95e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  376 YDYRLKTKSGAYRYFTVK--GMALRNEHNKAIRMAGSVTDITEQKRSQKALKqakEQNDLLAQAIESCNVGISIADASvq 453
Cdd:PRK13560  277 IEAEFQNKDGRTRPVDVIfnHAEFDDKENHCAGLVGAITDISGRRAAERELL---EKEDMLRAIIEAAPIAAIGLDAD-- 351
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  454 GFPLVFLNSEFEKITGYSKEEMLG-------------INCSLLQ--GPNTDKNAIDIITNAiKTLKTQRI----EILNYK 514
Cdd:PRK13560  352 GNICFVNNNAAERMLGWSAAEVMGkplpgmdpelneeFWCGDFQewYPDGRPMAFDACPMA-KTIKGGKIfdgqEVLIER 430
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 503229768  515 KDGTEFWNSLQISPVFNEQQQLTAYVGIQQDITEQKAANQLLIEAKAAAEQA 566
Cdd:PRK13560  431 EDDGPADCSAYAEPLHDADGNIIGAIALLVDITERKQVEEQLLLANLIVENS 482
PAC smart00086
Motif C-terminal to PAS motifs (likely to contribute to PAS structural domain); PAC motif ...
375-417 1.99e-04

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


Pssm-ID: 197509  Cd Length: 43  Bit Score: 39.86  E-value: 1.99e-04
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|...
gi 503229768    375 NYDYRLKTKSGAYRYFTVKGMALRNEHNKAIRMAGSVTDITEQ 417
Cdd:smart00086    1 TVEYRLRRKDGSYIWVLVSASPIRDEDGEVEGILGVVRDITER 43
PRK09483 PRK09483
response regulator; Provisional
968-1083 2.02e-04

response regulator; Provisional


Pssm-ID: 236538 [Multi-domain]  Cd Length: 217  Bit Score: 43.94  E-value: 2.02e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  968 IRILLVEDNNInqivASTTLKKI-----GINSIDIAENGQHALEYLKQttshNPYSLILMDCQMPVMDGYQATTHI-RVn 1041
Cdd:PRK09483    2 INVLLVDDHEL----VRAGIRRIledikGIKVVGEACCGEDAVKWCRT----NAVDVVLMDMNMPGIGGLEATRKIlRY- 72
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 503229768 1042 eagskNPPITIIAMTANAMVGDKAKCLQVGMNDYISKPIAQD 1083
Cdd:PRK09483   73 -----TPDVKIIMLTVHTENPLPAKVMQAGAAGYLSKGAAPQ 109
PRK11359 PRK11359
cyclic-di-GMP phosphodiesterase; Provisional
427-555 2.10e-04

cyclic-di-GMP phosphodiesterase; Provisional


Pssm-ID: 183097 [Multi-domain]  Cd Length: 799  Bit Score: 45.53  E-value: 2.10e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  427 AKEQNDLLAQAIESCNVGISIADASVQgfpLVFLNSEFEKITGYSKEEMLGINC-SLLQGPNT-DKNAIDIITNAIKTLK 504
Cdd:PRK11359  131 QKEQTRQLIIAVDHLDRPVIVLDPERR---IVQCNRAFTEMFGYCISEASGMQPdTLLNIPEFpADNRIRLQQLLWKTAR 207
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 503229768  505 TQRiEILNYKKDGTEFWNSLQISPVFNEQQQLTAYVGIQQDITEQKAANQL 555
Cdd:PRK11359  208 DQD-EFLLLTRTGEKIWIKASISPVYDVLAHLQNLVMTFSDITEERQIRQL 257
REC_typeA_ARR cd17581
phosphoacceptor receiver (REC) domain of type A Arabidopsis response regulators (ARRs) and ...
970-1080 2.18e-04

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: 41.97  E-value: 2.18e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  970 ILLVEDNNINQIVASTTLKkigINSIDI--AENGQHALEYL-----KQTTSHNPY--SLILMDCQMPVMDGYQATTHIRv 1040
Cdd:cd17581     1 VLAVDDSLVDRKVIERLLR---ISSCRVtaVDSGKRALEFLgledeEDSSNFNEPkvNMIITDYCMPGMTGYDLLKKVK- 76
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 503229768 1041 neAGSKNPPITIIAMTANAMVGDKAKCLQVGMNDYISKPI 1080
Cdd:cd17581    77 --ESSALKEIPVVIMSSENIPTRISRCLEEGAEDFLLKPV 114
REC_RocR cd17530
phosphoacceptor receiver (REC) domain of response regulator RocR; The response regulator RocR ...
969-1053 2.79e-04

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: 41.66  E-value: 2.79e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  969 RILLVEDNNINQIVASTTLKKIGINSIDIAENGQHALEYLKQttshNPYSLILMDCQMPVMDGYQATTHIrvneAGSKNP 1048
Cdd:cd17530     2 RVLVLDDDPFQCMMAATILEDLGPGNVDEADDGREALVILLC----NAPDIIICDLKMPDMDGIEFLRHL----AESHSN 73

                  ....*
gi 503229768 1049 PITII 1053
Cdd:cd17530    74 AAVIL 78
PRK10710 PRK10710
DNA-binding transcriptional regulator BaeR; Provisional
1000-1079 3.13e-04

DNA-binding transcriptional regulator BaeR; Provisional


Pssm-ID: 182665 [Multi-domain]  Cd Length: 240  Bit Score: 43.52  E-value: 3.13e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768 1000 NGQHALEYLKQTtshnPYSLILMDCQMPVMDGYQATTHIRvneagsKNPPITIIAMTANAMVGDKAKCLQVGMNDYISKP 1079
Cdd:PRK10710   42 HGDEVLPYVRQT----PPDLILLDLMLPGTDGLTLCREIR------RFSDIPIVMVTAKIEEIDRLLGLEIGADDYICKP 111
AmiR COG3707
Two-component response regulator, AmiR/NasT family, consists of REC and RNA-binding ...
810-923 3.39e-04

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: 43.02  E-value: 3.39e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  810 MSSLNILIVCSNQTQSSILHKQFTKWGATAV-ISPSAKQAVQICQQyiekqnLCFDLIMIDMQLSDGDALTLSKTLDKEv 888
Cdd:COG3707     1 MRGLRVLVVDDEPLRRADLREGLREAGYEVVaEAADGEDAVELVRE------LKPDLVIVDIDMPDRDGLEAARQISEE- 73
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 503229768  889 dlMAAHVVLMTTGElnkQRDLYQASR---FSAIVTKPI 923
Cdd:COG3707    74 --RPAPVILLTAYS---DPELIERALeagVSAYLVKPL 106
PAS_3 pfam08447
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
458-542 3.76e-04

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


Pssm-ID: 430001 [Multi-domain]  Cd Length: 89  Bit Score: 40.40  E-value: 3.76e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768   458 VFLNSEFEKITGYSKEEMLGINCSLLQG--PNTDKNAIDIITNAIKTLKTQRIEILNYKKDGTEFWNSLQISPVFNEQQQ 535
Cdd:pfam08447    2 IYWSPRFEEILGYTPEELLGKGESWLDLvhPDDRERVREALWEALKGGEPYSGEYRIRRKDGEYRWVEARARPIRDENGK 81

                   ....*..
gi 503229768   536 LTAYVGI 542
Cdd:pfam08447   82 PVRVIGV 88
REC_OmpR_MtrA-like cd17626
phosphoacceptor receiver (REC) domain of MtrA-like OmpR family response regulators; MtrA is ...
969-1079 4.22e-04

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


Pssm-ID: 381141 [Multi-domain]  Cd Length: 115  Bit Score: 40.92  E-value: 4.22e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  969 RILLVEDNNINQIVASTTLKKIGINSIdIAENGQHALEYLKQTtshNPySLILMDCQMPVMDGYQATTHIRvneAGSKNP 1048
Cdd:cd17626     2 RILVVDDDAALAEMIGIVLRGEGFDPA-FCGDGTQALAAFREV---RP-DLVLLDLMLPGIDGIEVCRQIR---AESGVP 73
                          90       100       110
                  ....*....|....*....|....*....|.
gi 503229768 1049 pitIIAMTANAMVGDKAKCLQVGMNDYISKP 1079
Cdd:cd17626    74 ---IVMLTAKSDTVDVVLGLESGADDYVAKP 101
HATPase_VanS-like cd16923
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
686-790 4.34e-04

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: 40.83  E-value: 4.34e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  686 LKQILTNLVNNALKFTHKGEVQVIAKLTPINNNQMRFncqvIDSGIGISAAQQAKLFKSFSQVDSSttRKYGGTGLGLAI 765
Cdd:cd16923     1 LQRVFSNLLSNAIKYSPENTRIYITSFLTDDVVNIMF----KNPSSHPLDFKLEKLFERFYRGDNS--RNTEGAGLGLSI 74
                          90       100
                  ....*....|....*....|....*
gi 503229768  766 VKKLCHLMEGDIQVQSkENKGSNFS 790
Cdd:cd16923    75 AKAIIELHGGSASAEY-DDNHDLFK 98
PRK12555 PRK12555
chemotaxis-specific protein-glutamate methyltransferase CheB;
968-1038 4.34e-04

chemotaxis-specific protein-glutamate methyltransferase CheB;


Pssm-ID: 237135 [Multi-domain]  Cd Length: 337  Bit Score: 43.72  E-value: 4.34e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 503229768  968 IRILLVEDnninQIVASTTLKKI-----GINSIDIAENGQHALEYLKQttsHNPySLILMDCQMPVMDGYQATTHI 1038
Cdd:PRK12555    1 MRIGIVND----SPLAVEALRRAlardpDHEVVWVATDGAQAVERCAA---QPP-DVILMDLEMPRMDGVEATRRI 68
REC_typeB_ARR-like cd17584
phosphoacceptor receiver (REC) domain of type B Arabidopsis response regulators (ARRs) and ...
1004-1080 6.41e-04

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: 40.69  E-value: 6.41e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 503229768 1004 ALEYLKQttSHNPYSLILMDCQMPVMDGYQATTHIRvneagsKNPPITIIAMTANAMVGDKAKCLQVGMNDYISKPI 1080
Cdd:cd17584    34 ALSMLRE--NKDEFDLVITDVHMPDMDGFEFLELIR------LEMDLPVIMMSADGSTSTVMKGLAHGACDYLLKPV 102
REC_OmpR_CpxR cd17623
phosphoacceptor receiver (REC) domain of CpxR-like OmpR family response regulators; CpxR is ...
970-1079 6.70e-04

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


Pssm-ID: 381138 [Multi-domain]  Cd Length: 115  Bit Score: 40.37  E-value: 6.70e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  970 ILLVEDNNINQIVASTTLKKIGINsIDIAENGQHALEYLkqttSHNPYSLILMDCQMPVMDGYQATTHIRvneagsKNPP 1049
Cdd:cd17623     1 ILLIDDDRELTELLTEYLEMEGFN-VRAAHDGEQGLAAL----LEGSPDLVVLDVMLPKMNGLDVLKELR------KTSQ 69
                          90       100       110
                  ....*....|....*....|....*....|
gi 503229768 1050 ITIIAMTANAMVGDKAKCLQVGMNDYISKP 1079
Cdd:cd17623    70 VPVLMLTARGDDIDRILGLELGADDYLPKP 99
REC_Spo0A cd17561
phosphoacceptor receiver (REC) domain of Spo0A; Spo0A is a response regulator of the ...
967-1079 6.74e-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: 40.28  E-value: 6.74e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  967 NIRILLVEDN-NINQIVASTTLKKIGINSIDIAENGQHALEYLKQttsHNPySLILMDCQMPVMDGYQATTHIRVNEAGS 1045
Cdd:cd17561     1 KIKVLIADDNrEFVQLLEEYLNSQPDMEVVGVAHNGQEALELIEE---KEP-DVLLLDIIMPHLDGIGVLEKLRRMRLEK 76
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 503229768 1046 KnppITIIAMTAnamVGDKA---KCLQVGMNDYISKP 1079
Cdd:cd17561    77 R---PKIIMLTA---FGQEDitqRAVELGASYYILKP 107
PRK09776 PRK09776
putative diguanylate cyclase; Provisional
290-560 6.92e-04

putative diguanylate cyclase; Provisional


Pssm-ID: 182070 [Multi-domain]  Cd Length: 1092  Bit Score: 43.89  E-value: 6.92e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  290 REAIKQSEARYELAVKGSN--------DGIWdwdIVTNEVyfsprISVLLGYDENDKNALPhcadaLYKLLHPDDITKHK 361
Cdd:PRK09776  275 RKHISESETRFRNAMEYSAigmalvgtEGQW---LQVNKA-----LCQFLGYSQEELRGLT-----FQQLTWPEDLNKDL 341
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  362 KQIANHLISNIpfnYDYRLK----TKSGAYRYFTVKGMALRNEHNKAIRMAGSVTDITEQKRSQKALKQAKEQNDLlaqA 437
Cdd:PRK09776  342 QQVEKLLSGEI---NSYSMEkryyRRDGEVVWALLAVSLVRDTDGTPLYFIAQIEDINELKRTEQVNERLMERITL---A 415
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  438 IESCNVGISIADASVQGFPLVFLNSEFEKITGYSK-EEMLGINCSLlqgPNTDKNAIDIITNAIKTLKTQRIEILNYKKD 516
Cdd:PRK09776  416 NEAGGIGIWEWDLKPNIISWDKRMFELYEIPPHIKpTWQVWYACLH---PEDRQRVEKEIRDALQGRSPFKLEFRIVVKD 492
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 503229768  517 GTEFWNSLQiSPVFNEQQQLTAYVGIQQDITEQKAANQLLIEAK 560
Cdd:PRK09776  493 GVRHIRALA-NRVLNKDGEVERLLGINMDMTEVRQLNEALFQEK 535
REC_HupR-like cd17569
phosphoacceptor receiver (REC) domain of hydrogen uptake protein regulator (HupR) and similar ...
968-1031 7.17e-04

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


Pssm-ID: 381113 [Multi-domain]  Cd Length: 118  Bit Score: 40.46  E-value: 7.17e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 503229768  968 IRILLVED--NNINQIVAstTLKKIGINsIDIAENGQHALEYLKQttshNPYSLILMDCQMPVMDG 1031
Cdd:cd17569     1 PTILLVDDepNILKALKR--LLRREGYE-VLTATSGEEALEILKQ----EPVDVVISDQRMPGMDG 59
HATPase_CckA-like cd16919
Histidine kinase-like ATPase domain of two-component sensor hybrid histidine kinases, similar ...
726-790 7.89e-04

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: 40.44  E-value: 7.89e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 503229768  726 VIDSGIGISAAQQAKLFKSFSqvdssTTRKYG-GTGLGLAIVKKLCHLMEGDIQVQSKENKGSNFS 790
Cdd:cd16919    52 VSDTGSGMPAEVLRRAFEPFF-----TTKEVGkGTGLGLSMVYGFVKQSGGHLRIYSEPGVGTTVR 112
HATPase_SpaK_NisK-like cd16975
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
682-787 9.53e-04

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: 39.75  E-value: 9.53e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  682 DAGRLKQILTNLVNNALKFT-HKGEVQVIAKltpinNNQMRFNCQVIDSGIGISAAQQAKLFKSFSQVDSSTTRKyGGTG 760
Cdd:cd16975     1 DTLLLSRALINIISNACQYApEGGTVSISIY-----DEEEYLYFEIWDNGHGFSEQDLKKALELFYRDDTSRRSG-GHYG 74
                          90       100
                  ....*....|....*....|....*..
gi 503229768  761 LGLAIVKKLCHLMEGDIQVQSKENKGS 787
Cdd:cd16975    75 MGLYIAKNLVEKHGGSLIIENSQKGGA 101
AtoC COG2204
DNA-binding transcriptional response regulator, NtrC family, contains REC, AAA-type ATPase, ...
811-899 1.14e-03

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: 42.64  E-value: 1.14e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  811 SSLNILIVCSNQTQSSILHKQFTKWGATAVISPSAKQAVQIcqqyIEKQNlcFDLIMIDMQLSDGDALTLSKTLdKEVDL 890
Cdd:COG2204     1 SMARILVVDDDPDIRRLLKELLERAGYEVETAASGEEALAL----LREEP--PDLVLLDLRMPGMDGLELLREL-RALDP 73

                  ....*....
gi 503229768  891 mAAHVVLMT 899
Cdd:COG2204    74 -DLPVILLT 81
RpfG COG3437
Response regulator c-di-GMP phosphodiesterase, RpfG family, contains REC and HD-GYP domains ...
811-941 1.19e-03

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: 41.69  E-value: 1.19e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  811 SSLNILIVCSNQTQSSILHKQFTKWGATAVISPSAKQAVQICQQYiekqnlCFDLIMIDMQLSDGDALTLSKTLDKEVDL 890
Cdd:COG3437     5 QAPTVLIVDDDPENLELLRQLLRTLGYDVVTAESGEEALELLLEA------PPDLILLDVRMPGMDGFELLRLLRADPST 78
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 503229768  891 MAAHVVLMTTGELNKQRDLYQASRFSAIVTKPIITQNLFKMLSTCFSDKQH 941
Cdd:COG3437    79 RDIPVIFLTALADPEDRERALEAGADDYLTKPFDPEELLARVRNALELRRL 129
REC_NtrX-like cd17550
phosphoacceptor receiver (REC) domain of nitrogen assimilation regulatory protein NtrX and ...
994-1090 1.33e-03

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


Pssm-ID: 381102 [Multi-domain]  Cd Length: 115  Bit Score: 39.79  E-value: 1.33e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  994 SIDIAENGQHALEYLKQttshNPYSLILMDCQMPVMDGYQATTHIRvneagSKNPPITIIAMTANAMVGDKAKCLQVGMN 1073
Cdd:cd17550    24 EVDTAADGEEALKLIKE----RRPDLVLLDIWLPDMDGLELLKEIK-----EKYPDLPVIMISGHGTIETAVKATKLGAY 94
                          90
                  ....*....|....*..
gi 503229768 1074 DYISKPIAQDilfkKLL 1090
Cdd:cd17550    95 DFIEKPLSLD----RLL 107
REC_OmpR_ChvI-like cd19936
phosphoacceptor receiver (REC) domain of ChvI-like OmpR family response regulators; ...
970-1079 1.46e-03

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: 38.97  E-value: 1.46e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  970 ILLVEDN-NINQIVaSTTLKKIGINsIDIAENGQHALEYLkqttSHNPYSLILMDCQMPVMDGYQATTHIRvneagsKNP 1048
Cdd:cd19936     1 IALVDDDrNILTSV-SMALEAEGFS-VETYTDGASALDGL----NARPPDLAILDIKMPRMDGMELLQRLR------QKS 68
                          90       100       110
                  ....*....|....*....|....*....|.
gi 503229768 1049 PITIIAMTANAMVGDKAKCLQVGMNDYISKP 1079
Cdd:cd19936    69 TLPVIFLTSKDDEIDEVFGLRMGADDYITKP 99
PRK11359 PRK11359
cyclic-di-GMP phosphodiesterase; Provisional
457-559 2.39e-03

cyclic-di-GMP phosphodiesterase; Provisional


Pssm-ID: 183097 [Multi-domain]  Cd Length: 799  Bit Score: 42.06  E-value: 2.39e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  457 LVFLNSEFEKITGYSKEEMLGINCSLLQGPNTDKNAIDII----TNAIKTLKTQRIEILNYKKDGTEFWNSLQISPVFNE 532
Cdd:PRK11359   34 VLFFNPAAEKLWGYKREEVIGNNIDMLIPRDLRPAHPEYIrhnrEGGKARVEGMSRELQLEKKDGSKIWTRFALSKVSAE 113
                          90       100       110
                  ....*....|....*....|....*....|
gi 503229768  533 QQqlTAYVGIQQDIT---EQKAANQLLIEA 559
Cdd:PRK11359  114 GK--VYYLALVRDASvemAQKEQTRQLIIA 141
REC_OmpR_ArcA_TorR-like cd17619
phosphoacceptor receiver (REC) domain of ArcA- and TorR-like OmpR family response regulators; ...
969-1079 2.62e-03

phosphoacceptor receiver (REC) domain of ArcA- and TorR-like OmpR family response regulators; This subfamily includes Escherichia coli TorR and ArcA, both OmpR family response regulators that mediate adaptation to changes in various respiratory growth conditions. The TorS-TorR two-component system (TCS) is responsible for the tight regulation of the torCAD operon, which encodes the trimethylamine N-oxide (TMAO) reductase respiratory system in response to anaerobic conditions and the presence of TMAO. The ArcA-ArcB TCS is involved in cell growth during anaerobiosis. ArcA is a global regulator that controls more than 30 operons involved in redox regulation (the Arc modulon). OmpR family DNA-binding response regulators are characterized by a REC domain and a winged helix-turn-helix (wHTH) DNA-binding output effector domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381134 [Multi-domain]  Cd Length: 113  Bit Score: 38.91  E-value: 2.62e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  969 RILLVEDNNINQIVASTTLKKIGInsiDIAENGQHalEYLKQTTSHNPYSLILMDCQMPVMDGYQATTHIRVNEAgsknp 1048
Cdd:cd17619     2 HILIVEDEPVTRATLKSYFEQEGY---DVSEAGDG--EEMRQILARQDIDLVLLDINLPGKDGLSLTRELREQSE----- 71
                          90       100       110
                  ....*....|....*....|....*....|.
gi 503229768 1049 pITIIAMTANAMVGDKAKCLQVGMNDYISKP 1079
Cdd:cd17619    72 -VGIILVTGRDDEVDRIVGLEIGADDYVTKP 101
HATPase_BvrS-ChvG-like cd16953
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
686-786 2.71e-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: 38.71  E-value: 2.71e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  686 LKQILTNLVNNALKFTHKGEVQVIAKLTPINNnqmRFNCQVIDSGIGISAAQQAKLFKSFsQVDSSTTRKYG-GTGLGLA 764
Cdd:cd16953     1 LGQVLRNLIGNAISFSPPDTGRITVSAMPTGK---MVTISVEDEGPGIPQEKLESIFDRF-YTERPANEAFGqHSGLGLS 76
                          90       100
                  ....*....|....*....|..
gi 503229768  765 IVKKLCHLMEGDIQVQSKENKG 786
Cdd:cd16953    77 ISRQIIEAHGGISVAENHNQPG 98
ompR PRK09468
osmolarity response regulator; Provisional
1017-1079 2.85e-03

osmolarity response regulator; Provisional


Pssm-ID: 181883 [Multi-domain]  Cd Length: 239  Bit Score: 40.73  E-value: 2.85e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 503229768 1017 YSLILMDCQMPVMDGYQATTHIRvneagSKNPPITIIAMTANAMVGDKAKCLQVGMNDYISKP 1079
Cdd:PRK09468   50 FHLMVLDLMLPGEDGLSICRRLR-----SQNNPTPIIMLTAKGEEVDRIVGLEIGADDYLPKP 107
glnG PRK10923
nitrogen regulation protein NR(I); Provisional
970-1083 3.06e-03

nitrogen regulation protein NR(I); Provisional


Pssm-ID: 182842 [Multi-domain]  Cd Length: 469  Bit Score: 41.39  E-value: 3.06e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  970 ILLVEDNNINQIVASTTLKKIGINSIDIaENGQHALEYLKQTTShnpySLILMDCQMPVMDGYQATTHIRVNeagskNPP 1049
Cdd:PRK10923    6 VWVVDDDSSIRWVLERALAGAGLTCTTF-ENGNEVLEALASKTP----DVLLSDIRMPGMDGLALLKQIKQR-----HPM 75
                          90       100       110
                  ....*....|....*....|....*....|....
gi 503229768 1050 ITIIAMTANAMVGDKAKCLQVGMNDYISKPIAQD 1083
Cdd:PRK10923   76 LPVIIMTAHSDLDAAVSAYQQGAFDYLPKPFDID 109
CitB COG4565
DNA-binding response regulator DpiB of citrate/malate metabolism [Transcription, Signal ...
810-940 3.79e-03

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


Pssm-ID: 443622 [Multi-domain]  Cd Length: 138  Bit Score: 38.80  E-value: 3.79e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  810 MSSLNILIVCSNQTQSSILHKQFTKWGATAVISP--SAKQAVQICQQYIekqnlcFDLIMIDMQLSDGDALTLSKTL--- 884
Cdd:COG4565     1 MKMIRVLIVEDDPMVAELLRRYLERLPGFEVVGVasSGEEALALLAEHR------PDLILLDIYLPDGDGLELLRELrar 74
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 503229768  885 DKEVDlmaahvVLMTTGELNkQRDLYQASRFSAI--VTKPIITQNLFKMLSTCFSDKQ 940
Cdd:COG4565    75 GPDVD------VIVITAARD-PETVREALRAGVVdyLIKPFTFERLREALERYLEYRR 125
REC_GlnL-like cd17565
phosphoacceptor receiver (REC) domain of transcriptional regulatory protein GlnL and similar ...
965-1080 4.36e-03

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


Pssm-ID: 381112 [Multi-domain]  Cd Length: 103  Bit Score: 38.02  E-value: 4.36e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  965 DKNIRILL---VEDNNINQIVAsttlkkiginsidIAENGQHALEYLKQTtshNPySLILMDCQMPVMDGYQAtthirVN 1041
Cdd:cd17565     7 DKNIIKILsdiIEDDDLGEVVG-------------EADNGAQAYDEILFL---QP-DIVLIDLLMPGMDGIQL-----VR 64
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 503229768 1042 EAGSKNPPITIIAMtanAMVGDK---AKCLQVGMNDYISKPI 1080
Cdd:cd17565    65 KLKDTGSNGKFIMI---SQVSDKemiGKAYQAGIEFFINKPI 103
glnL PRK11073
nitrogen regulation protein NR(II);
563-781 4.75e-03

nitrogen regulation protein NR(II);


Pssm-ID: 182947 [Multi-domain]  Cd Length: 348  Bit Score: 40.45  E-value: 4.75e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  563 AEQanIAKSEFLAAMSHEIRTPMNGVLGMLNLIL----DSSLNEkqHHQVSIAlnSANSLLNIINDILDFSKvdAGKLEL 638
Cdd:PRK11073  125 AQQ--VAARDLVRGLAHEIKNPLGGLRGAAQLLSkalpDPALTE--YTKVIIE--QADRLRNLVDRLLGPQR--PGTHVT 196
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  639 EelefNLCNMLDDFIETIAIHAhSKNI-------PLMLDIEHleyafvigDAGRLKQILTNLVNNALK-FTHKGEVQVIA 710
Cdd:PRK11073  197 E----SIHKVAERVVQLVSLEL-PDNVrlirdydPSLPELAH--------DPDQIEQVLLNIVRNALQaLGPEGGTITLR 263
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 503229768  711 KLTP--INNNQMRF----NCQVIDSGIGISAAQQAKLFksFSQVdsstTRKYGGTGLGLAIVKKLCHLMEGDIQVQS 781
Cdd:PRK11073  264 TRTAfqLTLHGERYrlaaRIDIEDNGPGIPPHLQDTLF--YPMV----SGREGGTGLGLSIARNLIDQHSGKIEFTS 334
REC_LytTR_AlgR-like cd17532
phosphoacceptor receiver (REC) domain of LytTR/AlgR family response regulators similar to AlgR; ...
992-1083 6.02e-03

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


Pssm-ID: 381087 [Multi-domain]  Cd Length: 118  Bit Score: 37.90  E-value: 6.02e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  992 INSIDI---AENGQHALEYLKQttsHNPySLILMDCQMPVMDGYQATTHIRvneaGSKNPPItIIAMTANAMVGDKAkcL 1068
Cdd:cd17532    21 HPDIEIvgeAENGEEALEAIEE---LKP-DVVFLDIQMPGLDGLELAKKLS----KLAKPPL-IVFVTAYDEYAVEA--F 89
                          90
                  ....*....|....*
gi 503229768 1069 QVGMNDYISKPIAQD 1083
Cdd:cd17532    90 ELNAVDYLLKPFSEE 104
REC_TPR cd17589
phosphoacceptor receiver (REC) domain of uncharacterized tetratricopeptide repeat (TPR) ...
815-902 8.53e-03

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: 37.24  E-value: 8.53e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503229768  815 ILIVCSNQTQSSILHKQFTKWGAT-AVISPSAKQAVQICqqyiekQNLCFDLIMIDMQLSDG-DALTLSKTLdKEVDLMA 892
Cdd:cd17589     1 FLIVDDQPTFRSMLKSMLRSLGVTrIDTASSGEEALRMC------ENKTYDIVLCDYNLGKGkNGQQLLEEL-RHKKLIS 73
                          90
                  ....*....|.
gi 503229768  893 AH-VVLMTTGE 902
Cdd:cd17589    74 PStVFIMVTGE 84
 
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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