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Conserved domains on  [gi|1539062979|ref|WP_125890072|]
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ATP-binding protein [Pseudomonas luteola]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PRK13557 super family cl36263
histidine kinase; Provisional
9-495 5.57e-122

histidine kinase; Provisional


The actual alignment was detected with superfamily member PRK13557:

Pssm-ID: 237425 [Multi-domain]  Cd Length: 540  Bit Score: 367.46  E-value: 5.57e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539062979   9 AVLEALPIPVIVKDLN---HRIVFVNQAasgyfqdpidtLVGKTDYDcfpaehaatywqmEEKVISTQCpceneETIIGP 85
Cdd:PRK13557   34 AAVETTRMPMIVTDPNqpdNPIVFANRA-----------FLEMTGYA-------------AEEIIGNNC-----RFLQGP 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539062979  86 EGKPQIIITTKTLVT----VANESL------------------------LVAYF---INVTAQRQFEEQLRQAQKMEAVG 134
Cdd:PRK13557   85 ETDRATVAEVRDAIAerreIATEILnyrkdgssfwnalfvspvyndagdLVYFFgsqLDVSRRRDAEDALRQAQKMEALG 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539062979 135 QLTGGIAHDFNNHLGGIIGSLGIMQKRIAKGTC-VG-LERYTDNAMASAQRAASLTHRLLAFSRRQSLNPKPLKLNDLFD 212
Cdd:PRK13557  165 QLTGGIAHDFNNLLQVMSGYLDVIQAALSHPDAdRGrMARSVENIRAAAERAATLTQQLLAFARKQRLEGRVLNLNGLVS 244
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539062979 213 EFQSFINQSLGPEYRFEVHYEGDLWTTFCDHHQLENAVLNLAINARDAMPNGGIIICQITNS-------ASVPGLFEGEC 285
Cdd:PRK13557  245 GMGELAERTLGDAVTIETDLAPDLWNCRIDPTQAEVALLNVLINARDAMPEGGRVTIRTRNVeiededlAMYHGLPPGRY 324
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539062979 286 VCISIVDTGTGIAPEIMDRVIEPFFTTKPIGEGTGLGLSMVYGFVKQSNGHFTIESTQAKGTTVSLYLPRYIGETCQHTS 365
Cdd:PRK13557  325 VSIAVTDTGSGMPPEILARVMDPFFTTKEEGKGTGLGLSMVYGFAKQSGGAVRIYSEVGEGTTVRLYFPASDQAENPEQE 404
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539062979 366 STDEPLKEGLQQTVMLVEDDEVLREIIIEVLEDLDYHVLSTGNGQHALELIVTAAkPVDLLLTDIGLPG-INGRDLAAHV 444
Cdd:PRK13557  405 PKARAIDRGGTETILIVDDRPDVAELARMILEDFGYRTLVASNGREALEILDSHP-EVDLLFTDLIMPGgMNGVMLAREA 483
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1539062979 445 LDRFPKLKIMFITGYDKTvtlpkSLFRHDV-----EVMTKPFTISELASRVQRLLE 495
Cdd:PRK13557  484 RRRQPKIKVLLTTGYAEA-----SIERTDAggsefDILNKPYRRAELARRVRMVLD 534
 
Name Accession Description Interval E-value
PRK13557 PRK13557
histidine kinase; Provisional
9-495 5.57e-122

histidine kinase; Provisional


Pssm-ID: 237425 [Multi-domain]  Cd Length: 540  Bit Score: 367.46  E-value: 5.57e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539062979   9 AVLEALPIPVIVKDLN---HRIVFVNQAasgyfqdpidtLVGKTDYDcfpaehaatywqmEEKVISTQCpceneETIIGP 85
Cdd:PRK13557   34 AAVETTRMPMIVTDPNqpdNPIVFANRA-----------FLEMTGYA-------------AEEIIGNNC-----RFLQGP 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539062979  86 EGKPQIIITTKTLVT----VANESL------------------------LVAYF---INVTAQRQFEEQLRQAQKMEAVG 134
Cdd:PRK13557   85 ETDRATVAEVRDAIAerreIATEILnyrkdgssfwnalfvspvyndagdLVYFFgsqLDVSRRRDAEDALRQAQKMEALG 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539062979 135 QLTGGIAHDFNNHLGGIIGSLGIMQKRIAKGTC-VG-LERYTDNAMASAQRAASLTHRLLAFSRRQSLNPKPLKLNDLFD 212
Cdd:PRK13557  165 QLTGGIAHDFNNLLQVMSGYLDVIQAALSHPDAdRGrMARSVENIRAAAERAATLTQQLLAFARKQRLEGRVLNLNGLVS 244
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539062979 213 EFQSFINQSLGPEYRFEVHYEGDLWTTFCDHHQLENAVLNLAINARDAMPNGGIIICQITNS-------ASVPGLFEGEC 285
Cdd:PRK13557  245 GMGELAERTLGDAVTIETDLAPDLWNCRIDPTQAEVALLNVLINARDAMPEGGRVTIRTRNVeiededlAMYHGLPPGRY 324
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539062979 286 VCISIVDTGTGIAPEIMDRVIEPFFTTKPIGEGTGLGLSMVYGFVKQSNGHFTIESTQAKGTTVSLYLPRYIGETCQHTS 365
Cdd:PRK13557  325 VSIAVTDTGSGMPPEILARVMDPFFTTKEEGKGTGLGLSMVYGFAKQSGGAVRIYSEVGEGTTVRLYFPASDQAENPEQE 404
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539062979 366 STDEPLKEGLQQTVMLVEDDEVLREIIIEVLEDLDYHVLSTGNGQHALELIVTAAkPVDLLLTDIGLPG-INGRDLAAHV 444
Cdd:PRK13557  405 PKARAIDRGGTETILIVDDRPDVAELARMILEDFGYRTLVASNGREALEILDSHP-EVDLLFTDLIMPGgMNGVMLAREA 483
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1539062979 445 LDRFPKLKIMFITGYDKTvtlpkSLFRHDV-----EVMTKPFTISELASRVQRLLE 495
Cdd:PRK13557  484 RRRQPKIKVLLTTGYAEA-----SIERTDAggsefDILNKPYRRAELARRVRMVLD 534
NtrB COG3852
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms];
9-356 8.18e-96

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


Pssm-ID: 443061 [Multi-domain]  Cd Length: 361  Bit Score: 294.06  E-value: 8.18e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539062979   9 AVLEALPIPVIVKDLNHRIVFVNQAASGYFQDPIDTLVGKTDYDCFPaeHAATYWQMEEKVISTQCPCENEE-TIIGPEG 87
Cdd:COG3852    11 AILDSLPDAVIVLDADGRITYVNPAAERLLGLSAEELLGRPLAELFP--EDSPLRELLERALAEGQPVTEREvTLRRKDG 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539062979  88 KPQII-ITTKTLVTVANESLLVAYFINVTAQRQFEEQLRQAQKMEAVGQLTGGIAHDFNNHLGGIIGSLGIMQKRIAKGt 166
Cdd:COG3852    89 EERPVdVSVSPLRDAEGEGGVLLVLRDITERKRLERELRRAEKLAAVGELAAGLAHEIRNPLTGIRGAAQLLERELPDD- 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539062979 167 cvGLERYTDNAMASAQRAASLTHRLLAFSRRQSLNPKPLKLNDLFDEFQSFINQSLGPEYRFEVHYEGDLWTTFCDHHQL 246
Cdd:COG3852   168 --ELREYTQLIIEEADRLNNLVDRLLSFSRPRPPEREPVNLHEVLERVLELLRAEAPKNIRIVRDYDPSLPEVLGDPDQL 245
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539062979 247 ENAVLNLAINARDAMPNGGIIICQITNSASV--PGLFEGECVCISIVDTGTGIAPEIMDRVIEPFFTTKPigEGTGLGLS 324
Cdd:COG3852   246 IQVLLNLVRNAAEAMPEGGTITIRTRVERQVtlGGLRPRLYVRIEVIDNGPGIPEEILDRIFEPFFTTKE--KGTGLGLA 323
                         330       340       350
                  ....*....|....*....|....*....|..
gi 1539062979 325 MVYGFVKQSNGHFTIESTQAKGTTVSLYLPRY 356
Cdd:COG3852   324 IVQKIVEQHGGTIEVESEPGKGTTFRIYLPLE 355
HATPase_CckA-like cd16919
Histidine kinase-like ATPase domain of two-component sensor hybrid histidine kinases, similar ...
246-354 3.56e-50

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: 167.17  E-value: 3.56e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539062979 246 LENAVLNLAINARDAMPNGGIIICQITN-------SASVPGLFEGECVCISIVDTGTGIAPEIMDRVIEPFFTTKPIGEG 318
Cdd:cd16919     1 LELAILNLAVNARDAMPEGGRLTIETSNqrvdadyALNYRDLIPGNYVCLEVSDTGSGMPAEVLRRAFEPFFTTKEVGKG 80
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1539062979 319 TGLGLSMVYGFVKQSNGHFTIESTQAKGTTVSLYLP 354
Cdd:cd16919    81 TGLGLSMVYGFVKQSGGHLRIYSEPGVGTTVRIYLP 116
HATPase_c smart00387
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.
242-354 2.71e-24

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


Pssm-ID: 214643 [Multi-domain]  Cd Length: 111  Bit Score: 97.33  E-value: 2.71e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539062979  242 DHHQLENAVLNLAINARDAMPNGGIIICQITnsasvpglFEGECVCISIVDTGTGIAPEIMDRVIEPFFTTKPI---GEG 318
Cdd:smart00387   2 DPDRLRQVLSNLLDNAIKYTPEGGRITVTLE--------RDGDHVEITVEDNGPGIPPEDLEKIFEPFFRTDKRsrkIGG 73
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1539062979  319 TGLGLSMVYGFVKQSNGHFTIESTQAKGTTVSLYLP 354
Cdd:smart00387  74 TGLGLSIVKKLVELHGGEISVESEPGGGTTFTITLP 109
HATPase_c pfam02518
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the ...
242-357 1.13e-21

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: 89.73  E-value: 1.13e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539062979 242 DHHQLENAVLNLAINARDAMPNGGIIICQITnsasvpglfEGECVCISIVDTGTGIAPEIMDRVIEPFFTTKPI-GEGTG 320
Cdd:pfam02518   2 DELRLRQVLSNLLDNALKHAAKAGEITVTLS---------EGGELTLTVEDNGIGIPPEDLPRIFEPFSTADKRgGGGTG 72
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1539062979 321 LGLSMVYGFVKQSNGHFTIESTQAKGTTVSLYLPRYI 357
Cdd:pfam02518  73 LGLSIVRKLVELLGGTITVESEPGGGTTVTLTLPLAQ 109
 
Name Accession Description Interval E-value
PRK13557 PRK13557
histidine kinase; Provisional
9-495 5.57e-122

histidine kinase; Provisional


Pssm-ID: 237425 [Multi-domain]  Cd Length: 540  Bit Score: 367.46  E-value: 5.57e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539062979   9 AVLEALPIPVIVKDLN---HRIVFVNQAasgyfqdpidtLVGKTDYDcfpaehaatywqmEEKVISTQCpceneETIIGP 85
Cdd:PRK13557   34 AAVETTRMPMIVTDPNqpdNPIVFANRA-----------FLEMTGYA-------------AEEIIGNNC-----RFLQGP 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539062979  86 EGKPQIIITTKTLVT----VANESL------------------------LVAYF---INVTAQRQFEEQLRQAQKMEAVG 134
Cdd:PRK13557   85 ETDRATVAEVRDAIAerreIATEILnyrkdgssfwnalfvspvyndagdLVYFFgsqLDVSRRRDAEDALRQAQKMEALG 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539062979 135 QLTGGIAHDFNNHLGGIIGSLGIMQKRIAKGTC-VG-LERYTDNAMASAQRAASLTHRLLAFSRRQSLNPKPLKLNDLFD 212
Cdd:PRK13557  165 QLTGGIAHDFNNLLQVMSGYLDVIQAALSHPDAdRGrMARSVENIRAAAERAATLTQQLLAFARKQRLEGRVLNLNGLVS 244
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539062979 213 EFQSFINQSLGPEYRFEVHYEGDLWTTFCDHHQLENAVLNLAINARDAMPNGGIIICQITNS-------ASVPGLFEGEC 285
Cdd:PRK13557  245 GMGELAERTLGDAVTIETDLAPDLWNCRIDPTQAEVALLNVLINARDAMPEGGRVTIRTRNVeiededlAMYHGLPPGRY 324
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539062979 286 VCISIVDTGTGIAPEIMDRVIEPFFTTKPIGEGTGLGLSMVYGFVKQSNGHFTIESTQAKGTTVSLYLPRYIGETCQHTS 365
Cdd:PRK13557  325 VSIAVTDTGSGMPPEILARVMDPFFTTKEEGKGTGLGLSMVYGFAKQSGGAVRIYSEVGEGTTVRLYFPASDQAENPEQE 404
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539062979 366 STDEPLKEGLQQTVMLVEDDEVLREIIIEVLEDLDYHVLSTGNGQHALELIVTAAkPVDLLLTDIGLPG-INGRDLAAHV 444
Cdd:PRK13557  405 PKARAIDRGGTETILIVDDRPDVAELARMILEDFGYRTLVASNGREALEILDSHP-EVDLLFTDLIMPGgMNGVMLAREA 483
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1539062979 445 LDRFPKLKIMFITGYDKTvtlpkSLFRHDV-----EVMTKPFTISELASRVQRLLE 495
Cdd:PRK13557  484 RRRQPKIKVLLTTGYAEA-----SIERTDAggsefDILNKPYRRAELARRVRMVLD 534
NtrB COG3852
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms];
9-356 8.18e-96

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


Pssm-ID: 443061 [Multi-domain]  Cd Length: 361  Bit Score: 294.06  E-value: 8.18e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539062979   9 AVLEALPIPVIVKDLNHRIVFVNQAASGYFQDPIDTLVGKTDYDCFPaeHAATYWQMEEKVISTQCPCENEE-TIIGPEG 87
Cdd:COG3852    11 AILDSLPDAVIVLDADGRITYVNPAAERLLGLSAEELLGRPLAELFP--EDSPLRELLERALAEGQPVTEREvTLRRKDG 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539062979  88 KPQII-ITTKTLVTVANESLLVAYFINVTAQRQFEEQLRQAQKMEAVGQLTGGIAHDFNNHLGGIIGSLGIMQKRIAKGt 166
Cdd:COG3852    89 EERPVdVSVSPLRDAEGEGGVLLVLRDITERKRLERELRRAEKLAAVGELAAGLAHEIRNPLTGIRGAAQLLERELPDD- 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539062979 167 cvGLERYTDNAMASAQRAASLTHRLLAFSRRQSLNPKPLKLNDLFDEFQSFINQSLGPEYRFEVHYEGDLWTTFCDHHQL 246
Cdd:COG3852   168 --ELREYTQLIIEEADRLNNLVDRLLSFSRPRPPEREPVNLHEVLERVLELLRAEAPKNIRIVRDYDPSLPEVLGDPDQL 245
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539062979 247 ENAVLNLAINARDAMPNGGIIICQITNSASV--PGLFEGECVCISIVDTGTGIAPEIMDRVIEPFFTTKPigEGTGLGLS 324
Cdd:COG3852   246 IQVLLNLVRNAAEAMPEGGTITIRTRVERQVtlGGLRPRLYVRIEVIDNGPGIPEEILDRIFEPFFTTKE--KGTGLGLA 323
                         330       340       350
                  ....*....|....*....|....*....|..
gi 1539062979 325 MVYGFVKQSNGHFTIESTQAKGTTVSLYLPRY 356
Cdd:COG3852   324 IVQKIVEQHGGTIEVESEPGKGTTFRIYLPLE 355
COG4191 COG4191
Signal transduction histidine kinase regulating C4-dicarboxylate transport system [Signal ...
114-355 4.16e-82

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


Pssm-ID: 443345 [Multi-domain]  Cd Length: 361  Bit Score: 258.96  E-value: 4.16e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539062979 114 VTAQRQFEEQLRQAQKMEAVGQLTGGIAHDFNNHLGGIIGSLGIMQKRIA-KGTCVGLERYTDNAMASAQRAASLTHRLL 192
Cdd:COG4191   123 EEELRELQEQLVQSEKLAALGELAAGIAHEINNPLAAILGNAELLRRRLEdEPDPEELREALERILEGAERAAEIVRSLR 202
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539062979 193 AFSRRQSLNPKPLKLNDLFDEFQSFINQSLGP-EYRFEVHYEGDLWTTFCDHHQLENAVLNLAINARDAMPNG--Giiic 269
Cdd:COG4191   203 AFSRRDEEEREPVDLNELIDEALELLRPRLKArGIEVELDLPPDLPPVLGDPGQLEQVLLNLLINAIDAMEEGegG---- 278
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539062979 270 QITNSASVpglfEGECVCISIVDTGTGIAPEIMDRVIEPFFTTKPIGEGTGLGLSMVYGFVKQSNGHFTIESTQAKGTTV 349
Cdd:COG4191   279 RITISTRR----EGDYVVISVRDNGPGIPPEVLERIFEPFFTTKPVGKGTGLGLSISYGIVEKHGGRIEVESEPGGGTTF 354

                  ....*.
gi 1539062979 350 SLYLPR 355
Cdd:COG4191   355 TITLPL 360
NtrY COG5000
Signal transduction histidine kinase NtrY involved in nitrogen fixation and metabolism ...
9-355 2.20e-69

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: 227.54  E-value: 2.20e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539062979   9 AVLEALPIPVIVKDLNHRIVFVNQAASGYFQDPIDTLVGKTDYDCFPAehaatyWQMEEKVISTQCPCENEETIIGPEGK 88
Cdd:COG5000    94 TILENLPAGVIVLDADGRITLANPAAERLLGIPLEELIGKPLEELLPE------LDLAELLREALERGWQEEIELTRDGR 167
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539062979  89 PQIIITTKTLVTVAneslLVAYFINVTaqrqfeeQLRQAQKMEAVGQLTGGIAHDFNNHLGGIIGSLGIMQKRIAKGTCV 168
Cdd:COG5000   168 RTLLVRASPLRDDG----YVIVFDDIT-------ELLRAERLAAWGELARRIAHEIKNPLTPIQLSAERLRRKLADKLEE 236
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539062979 169 G---LERYTDNAMASAQRAASLTHRLLAFSRRQSLNPKPLKLNDLFDEFQSFINQSL-GPEYRFEVHYEGDLWTTFCDHH 244
Cdd:COG5000   237 DredLERALDTIIRQVDRLKRIVDEFLDFARLPEPQLEPVDLNELLREVLALYEPALkEKDIRLELDLDPDLPEVLADRD 316
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539062979 245 QLENAVLNLAINARDAMPNGGIIICQITnsasvpglFEGECVCISIVDTGTGIAPEIMDRVIEPFFTTKPigEGTGLGLS 324
Cdd:COG5000   317 QLEQVLINLLKNAIEAIEEGGEIEVSTR--------REDGRVRIEVSDNGPGIPEEVLERIFEPFFTTKP--KGTGLGLA 386
                         330       340       350
                  ....*....|....*....|....*....|.
gi 1539062979 325 MVYGFVKQSNGHFTIESTQAKGTTVSLYLPR 355
Cdd:COG5000   387 IVKKIVEEHGGTIELESRPGGGTTFTIRLPL 417
PRK13837 PRK13837
two-component system VirA-like sensor kinase;
121-494 1.66e-57

two-component system VirA-like sensor kinase;


Pssm-ID: 237526 [Multi-domain]  Cd Length: 828  Bit Score: 204.53  E-value: 1.66e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539062979 121 EEQLRQAQKMEAVGQLTGGIAHDFNNHLGGIIGSLGIMQKRIAKGTcvGLERYTDNAMASAQRAASLTHRLLAFSRRQSL 200
Cdd:PRK13837  438 ERRLEHARRLEAVGTLASGIAHNFNNILGAILGYAEMALNKLARHS--RAARYIDEIISAGARARLIIDQILAFGRKGER 515
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539062979 201 NPKPLKLNDLFDEFQSFINQSLGPEYRFEVHYEGDLWTTFCDHHQLENAVLNLAINARDAMPNGGIIICQItNSASVPG- 279
Cdd:PRK13837  516 NTKPFDLSELVTEIAPLLRVSLPPGVELDFDQDQEPAVVEGNPAELQQVLMNLCSNAAQAMDGAGRVDISL-SRAKLRAp 594
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539062979 280 -------LFEGECVCISIVDTGTGIAPEIMDRVIEPFFTTKPigEGTGLGLSMVYGFVKQSNGHFTIESTQAKGTTVSLY 352
Cdd:PRK13837  595 kvlshgvLPPGRYVLLRVSDTGAGIDEAVLPHIFEPFFTTRA--GGTGLGLATVHGIVSAHAGYIDVQSTVGRGTRFDVY 672
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539062979 353 LPRYIGETCQHTSST-DEPLKEGLQQTVMLVEDDEVLREIIIEVLEDLDYHVLSTGNGQHALELIVTAAKPVDLLLTDIG 431
Cdd:PRK13837  673 LPPSSKVPVAPQAFFgPGPLPRGRGETVLLVEPDDATLERYEEKLAALGYEPVGFSTLAAAIAWISKGPERFDLVLVDDR 752
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1539062979 432 LPGINgrDLAAHVLDRFPKLKIMFITGyDKTVTLPKSLFRHDVEVMTKPFTISELASRVQRLL 494
Cdd:PRK13837  753 LLDEE--QAAAALHAAAPTLPIILGGN-SKTMALSPDLLASVAEILAKPISSRTLAYALRTAL 812
KinE COG5809
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome ...
10-359 8.03e-56

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: 193.65  E-value: 8.03e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539062979  10 VLEALPIPVIVKDLNHRIVFVNQAASGYFQDPIDTLVGKTDYDCFPAEHAATYWQMEEKVISTQCPCENEETIIGPEGKp 89
Cdd:COG5809   146 IFNHSPDGIIVTDLDGRIIYANPAACKLLGISIEELIGKSILELIHSDDQENVAAFISQLLKDGGIAQGEVRFWTKDGR- 224
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539062979  90 QIIITTKTLVTVANESLLVAYFI--NVTAQRQFEEQLRQAQKMEAVGQLTGGIAHDFNNHLGGIIGSLGIMQKRIAKGTc 167
Cdd:COG5809   225 WRLLEASGAPIKKNGEVDGIVIIfrDITERKKLEELLRKSEKLSVVGELAAGIAHEIRNPLTSLKGFIQLLKDTIDEEQ- 303
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539062979 168 vglERYTDNAMASAQRAASLTHRLLAFSRRQSLNPKPLKLNDLFDEFQSFIN-QSLGPEYRFEVHYEGDLWTTFCDHHQL 246
Cdd:COG5809   304 ---KTYLDIMLSELDRIESIISEFLVLAKPQAIKYEPKDLNTLIEEVIPLLQpQALLKNVQIELELEDDIPDILGDENQL 380
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539062979 247 ENAVLNLAINARDAMPNGGIIICQITnsasvpgLFEGECVCISIVDTGTGIAPEIMDRVIEPFFTTKPigEGTGLGLSMV 326
Cdd:COG5809   381 KQVFINLLKNAIEAMPEGGNITIETK-------AEDDDKVVISVTDEGCGIPEERLKKLGEPFYTTKE--KGTGLGLMVS 451
                         330       340       350
                  ....*....|....*....|....*....|...
gi 1539062979 327 YGFVKQSNGHFTIESTQAKGTTVSLYLPRYIGE 359
Cdd:COG5809   452 YKIIEEHGGKITVESEVGKGTTFSITLPIKLSE 484
KinC COG5807
Sporulation sensor histidine kinase C [Cell cycle control, cell division, chromosome ...
11-356 1.05e-55

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


Pssm-ID: 444509 [Multi-domain]  Cd Length: 358  Bit Score: 190.00  E-value: 1.05e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539062979  11 LEALPIPVIVKDLNHRIVFVNQAASGYFQDPIDTLVGKTdydcFPAEHA-ATYWQMEEKVISTqcpcENEETIIGPEGKP 89
Cdd:COG5807    33 FDSILEFVFFIDSKGEILECNDFAEDLYGLSQNEYIGKT----FVEEKCiLKDEQLYNKEAFD----RIEISYLTKNGEF 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539062979  90 QIIITtKTLVTVANESLLVAYFINVTAQRQFEEQLRQAQKMEAVGQLTGGIAHDFNNHLGGIIGSLGIMQKRIakgTCVG 169
Cdd:COG5807   105 DEIIY-PIYYKDGVILGLITVYRDITKRKEAEDKLLRSEKLSVAGELAAGIAHEIRNPLTSIKGFLQLLQESR---EDSE 180
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539062979 170 LERYTDNAMASAQRAASLTHRLLAFSRRQSLNPKPLKLNDLFDEFQSFIN-QSLGPEYRFEVHYEGDLWTTFCDHHQLEN 248
Cdd:COG5807   181 REEYFNIIISEIDRINTIITELLVLSKPKKFNFKKLNLNDVLEDVIALLStEAILKNISIKYDLADDEPVINGDKNQLKQ 260
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539062979 249 AVLNLAINARDAMPNGGIIICqitnSASVpglfEGECVCISIVDTGTGIAPEIMDRVIEPFFTTKpiGEGTGLGLSMVYG 328
Cdd:COG5807   261 VFINLIKNAIEAMETGGNITI----KTYV----EGDFVVISVKDEGIGIPEEVLEKIGEPFFTTK--EEGTGLGLSICKK 330
                         330       340
                  ....*....|....*....|....*...
gi 1539062979 329 FVKQSNGHFTIESTQAKGTTVSLYLPRY 356
Cdd:COG5807   331 IIEEHNGTIEVESKPGKGTTFTIYLPLY 358
HATPase_CckA-like cd16919
Histidine kinase-like ATPase domain of two-component sensor hybrid histidine kinases, similar ...
246-354 3.56e-50

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: 167.17  E-value: 3.56e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539062979 246 LENAVLNLAINARDAMPNGGIIICQITN-------SASVPGLFEGECVCISIVDTGTGIAPEIMDRVIEPFFTTKPIGEG 318
Cdd:cd16919     1 LELAILNLAVNARDAMPEGGRLTIETSNqrvdadyALNYRDLIPGNYVCLEVSDTGSGMPAEVLRRAFEPFFTTKEVGKG 80
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1539062979 319 TGLGLSMVYGFVKQSNGHFTIESTQAKGTTVSLYLP 354
Cdd:cd16919    81 TGLGLSMVYGFVKQSGGHLRIYSEPGVGTTVRIYLP 116
BaeS COG0642
Signal transduction histidine kinase [Signal transduction mechanisms];
98-355 7.55e-49

Signal transduction histidine kinase [Signal transduction mechanisms];


Pssm-ID: 440407 [Multi-domain]  Cd Length: 328  Bit Score: 170.86  E-value: 7.55e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539062979  98 LVTVANESLLVAYFINVTAQRQFEEQLRQAQKMEAVGQLTGGIAHDFNNHLGGIIGSLGIMQKRIAKGtcvgLERYTDNA 177
Cdd:COG0642    75 LLLLLLLLLLLLLLLLLLLLLLLALLLLLEEANEAKSRFLANVSHELRTPLTAIRGYLELLLEELDEE----QREYLETI 150
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539062979 178 MASAQRAASLTHRLLAFSR----RQSLNPKPLKLNDLFDE-FQSFINQSLGPEYRFEVHYEGDLWTTFCDHHQLENAVLN 252
Cdd:COG0642   151 LRSADRLLRLINDLLDLSRleagKLELEPEPVDLAELLEEvVELFRPLAEEKGIELELDLPDDLPTVRGDPDRLRQVLLN 230
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539062979 253 LAINARDAMPNGGIIICQITNsasvpglfEGECVCISIVDTGTGIAPEIMDRVIEPFFTTKP--IGEGTGLGLSMVYGFV 330
Cdd:COG0642   231 LLSNAIKYTPEGGTVTVSVRR--------EGDRVRISVEDTGPGIPPEDLERIFEPFFRTDPsrRGGGTGLGLAIVKRIV 302
                         250       260
                  ....*....|....*....|....*
gi 1539062979 331 KQSNGHFTIESTQAKGTTVSLYLPR 355
Cdd:COG0642   303 ELHGGTIEVESEPGKGTTFTVTLPL 327
KinA COG5805
Sporulation sensor histidine kinase A (Stage II sporulation protein SpoIIF/SpoIIJ) [Cell cycle ...
9-354 2.53e-48

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: 173.76  E-value: 2.53e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539062979   9 AVLEALPIPVIVKDLNHRIVFVNQAASGYFQDPIDTLVGKTDYDCFPAEHAATYWQMEEKVISTQCPCENEETIIGPEGK 88
Cdd:COG5805   161 TLIENSPDLICVIDTDGRILFINESIERLFGAPREELIGKNLLELLHPCDKEEFKERIESITEVWQEFIIEREIITKDGR 240
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539062979  89 PQIIITTKTLVTVANESLLVAYFI--NVTAQRQFEEQLRQAQKMEAVGQLTGGIAHDFNNHLGGIIGSLGIMQkriakgt 166
Cdd:COG5805   241 IRYFEAVIVPLIDTDGSVKGILVIlrDITEKKEAEELMARSEKLSIAGQLAAGIAHEIRNPLTSIKGFLQLLQ------- 313
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539062979 167 cVGLERYTD--NAMASA-QRAASLTHRLLAFSRRQSLNPKPLKLNDLFDEFQSFIN-QSLGPEYRFEVHYEGDLWTTFCD 242
Cdd:COG5805   314 -PGIEDKEEyfDIMLSElDRIESIISEFLALAKPQAVNKEKENINELIQDVVTLLEtEAILHNIQIRLELLDEDPFIYCD 392
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539062979 243 HHQLENAVLNLAINARDAMPNGGIIICQITNsasvpglfEGECVCISIVDTGTGIAPEIMDRVIEPFFTTKPigEGTGLG 322
Cdd:COG5805   393 ENQIKQVFINLIKNAIEAMPNGGTITIHTEE--------EDNSVIIRVIDEGIGIPEERLKKLGEPFFTTKE--KGTGLG 462
                         330       340       350
                  ....*....|....*....|....*....|..
gi 1539062979 323 LSMVYGFVKQSNGHFTIESTQAKGTTVSLYLP 354
Cdd:COG5805   463 LMVSYKIIENHNGTIDIDSKVGKGTTFTITLP 494
PRK11360 PRK11360
two-component system sensor histidine kinase AtoS;
18-360 3.72e-47

two-component system sensor histidine kinase AtoS;


Pssm-ID: 236901 [Multi-domain]  Cd Length: 607  Bit Score: 172.46  E-value: 3.72e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539062979  18 VIVKDLNHRIVFVNQAASGYFQDPIDTLVGKTDYDCFP-AEHAATY----WQMEEKVISTQCPCENeetiigPEGKPQII 92
Cdd:PRK11360  275 VIAIDRQGKITTMNPAAEVITGLQRHELVGKPYSELFPpNTPFASPlldtLEHGTEHVDLEISFPG------RDRTIELS 348
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539062979  93 ITTKTLVTVANESL-LVAYFINVTAQRQFEEQLRQAQKMEAVGQLTGGIAHDFNNHLGGIIGSLGIMQKRIAKgtcVGLE 171
Cdd:PRK11360  349 VSTSLLHNTHGEMIgALVIFSDLTERKRLQRRVARQERLAALGELVAGVAHEIRNPLTAIRGYVQIWRQQTSD---PPSQ 425
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539062979 172 RYTDNAMASAQRAASLTHRLLAFSRRQSLNPKPLKLNDLFDEFQSFINQSLGPE-YRFEVHYEGDLWTTFCDHHQLENAV 250
Cdd:PRK11360  426 EYLSVVLREVDRLNKVIDQLLEFSRPRESQWQPVSLNALVEEVLQLFQTAGVQArVDFETELDNELPPIWADPELLKQVL 505
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539062979 251 LNLAINARDAMPNGGIIicQITNSASVPGLfegecVCISIVDTGTGIAPEIMDRVIEPFFTTKPigEGTGLGLSMVYGFV 330
Cdd:PRK11360  506 LNILINAVQAISARGKI--RIRTWQYSDGQ-----VAVSIEDNGCGIDPELLKKIFDPFFTTKA--KGTGLGLALSQRII 576
                         330       340       350
                  ....*....|....*....|....*....|
gi 1539062979 331 KQSNGHFTIESTQAKGTTVSLYLPRYIGET 360
Cdd:PRK11360  577 NAHGGDIEVESEPGVGTTFTLYLPINPQGN 606
KdpD COG2205
K+-sensing histidine kinase KdpD [Signal transduction mechanisms];
119-355 3.15e-39

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


Pssm-ID: 441807 [Multi-domain]  Cd Length: 239  Bit Score: 142.35  E-value: 3.15e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539062979 119 QFEEQLRQAQKMEAV-GQLTGGIAHDFNNHLGGIIGSLGIMQKRIAKGTcVGLERYTDNAMASAQRAASLTHRLLAFSRR 197
Cdd:COG2205     1 ELEEALEELEELERLkSEFLANVSHELRTPLTSILGAAELLLDEEDLSP-EERRELLEIIRESAERLLRLIEDLLDLSRL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539062979 198 QS----LNPKPLKLNDLFDE-FQSFINQSLGPEYRFEVHYEGDLWTTFCDHHQLENAVLNLAINARDAMPNGGIIICQIT 272
Cdd:COG2205    80 ESgklsLELEPVDLAELLEEaVEELRPLAEEKGIRLELDLPPELPLVYADPELLEQVLANLLDNAIKYSPPGGTITISAR 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539062979 273 NsasvpglfEGECVCISIVDTGTGIAPEIMDRVIEPFFTTKPIG--EGTGLGLSMVYGFVKQSNGHFTIESTQAKGTTVS 350
Cdd:COG2205   160 R--------EGDGVRISVSDNGPGIPEEELERIFERFYRGDNSRgeGGTGLGLAIVKRIVEAHGGTIWVESEPGGGTTFT 231

                  ....*
gi 1539062979 351 LYLPR 355
Cdd:COG2205   232 VTLPL 236
PRK10364 PRK10364
two-component system sensor histidine kinase ZraS;
116-354 2.57e-34

two-component system sensor histidine kinase ZraS;


Pssm-ID: 236674 [Multi-domain]  Cd Length: 457  Bit Score: 134.14  E-value: 2.57e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539062979 116 AQRQFEEQLRQAQKMEAVGQLTGGIAHDFNNHLGGIIGSLGIMQKRIAKGtcvGLERYTDNAMAS-AQRAASLTHRLLAF 194
Cdd:PRK10364  220 SRQLLQDEMKRKEKLVALGHLAAGVAHEIRNPLSSIKGLAKYFAERAPAG---GEAHQLAQVMAKeADRLNRVVSELLEL 296
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539062979 195 SRRQSLNPKPLKLNDLFDEFQSFINQ---SLGPEYRFEVHYEgdLWTTFCDHHQLENAVLNLAINARDAMPNGGIIICQI 271
Cdd:PRK10364  297 VKPTHLALQAVDLNDLINHSLQLVSQdanSREIQLRFTANDT--LPEIQADPDRLTQVLLNLYLNAIQAIGQHGVISVTA 374
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539062979 272 TNSasvpglfeGECVCISIVDTGTGIAPEIMDRVIEPFFTTKpiGEGTGLGLSMVYGFVKQSNGHFTIESTQAKGTTVSL 351
Cdd:PRK10364  375 SES--------GAGVKISVTDSGKGIAADQLEAIFTPYFTTK--AEGTGLGLAVVHNIVEQHGGTIQVASQEGKGATFTL 444

                  ...
gi 1539062979 352 YLP 354
Cdd:PRK10364  445 WLP 447
WalK COG5002
Sensor histidine kinase WalK [Signal transduction mechanisms];
98-355 1.49e-31

Sensor histidine kinase WalK [Signal transduction mechanisms];


Pssm-ID: 444026 [Multi-domain]  Cd Length: 390  Bit Score: 125.44  E-value: 1.49e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539062979  98 LVTVANESLLVAYFINVTAQRQFEEQLRQaqkmeavgqLTGGIAHDFNNHLGGIIGSLGIMQKRiAKGTCVGLERYTDNA 177
Cdd:COG5002   139 SALLLGLLLLAAVERDITELERLEQMRRE---------FVANVSHELRTPLTSIRGYLELLLDG-AADDPEERREYLEII 208
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539062979 178 MASAQRAASLTHRLLAFSR----RQSLNPKPLKLNDLFDE-FQSFINQSLGPEYRFEVHYEGDLWTTFCDHHQLENAVLN 252
Cdd:COG5002   209 LEEAERLSRLVNDLLDLSRlesgELKLEKEPVDLAELLEEvVEELRPLAEEKGIELELDLPEDPLLVLGDPDRLEQVLTN 288
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539062979 253 LAINARDAMPNGGIIICQITNsasvpglfEGECVCISIVDTGTGIAPEIMDRVIEPFFTTKP-----IGeGTGLGLSMVY 327
Cdd:COG5002   289 LLDNAIKYTPEGGTITVSLRE--------EDDQVRISVRDTGIGIPEEDLPRIFERFYRVDKsrsreTG-GTGLGLAIVK 359
                         250       260
                  ....*....|....*....|....*...
gi 1539062979 328 GFVKQSNGHFTIESTQAKGTTVSLYLPR 355
Cdd:COG5002   360 HIVEAHGGRIWVESEPGKGTTFTITLPL 387
CheY COG0784
CheY-like REC (receiver) domain, includes chemotaxis protein CheY and sporulation regulator ...
378-497 4.19e-27

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


Pssm-ID: 440547 [Multi-domain]  Cd Length: 128  Bit Score: 105.70  E-value: 4.19e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539062979 378 TVMLVEDDEVLREIIIEVLEDLDYHVLSTGNGQHALELIvtAAKPVDLLLTDIGLPGINGRDLAAHV--LDRFPKLKIMF 455
Cdd:COG0784     7 RILVVDDNPDNRELLRRLLERLGYEVTTAEDGAEALELL--RAGPPDLILLDINMPGMDGLELLRRIraLPRLPDIPIIA 84
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1539062979 456 ITGYDKTVTLPKSLFRHDVEVMTKPFTISELASRVQRLLEQD 497
Cdd:COG0784    85 LTAYADEEDRERALEAGADDYLTKPVDPEELLEALRRLLARA 126
HATPase_AtoS-like cd16943
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
245-355 5.78e-26

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


Pssm-ID: 340419 [Multi-domain]  Cd Length: 105  Bit Score: 101.73  E-value: 5.78e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539062979 245 QLENAVLNLAINARDAMPNGGIIIcqITNSASVPGLFegecvcISIVDTGTGIAPEIMDRVIEPFFTTKPIGEGTGLGLS 324
Cdd:cd16943     3 QLNQVLLNLLVNAAQAMEGRGRIT--IRTWAHVDQVL------IEVEDTGSGIDPEILGRIFDPFFTTKPVGEGTGLGLS 74
                          90       100       110
                  ....*....|....*....|....*....|.
gi 1539062979 325 MVYGFVKQSNGHFTIESTQAKGTTVSLYLPR 355
Cdd:cd16943    75 LSYRIIQKHGGTIRVASVPGGGTRFTIILPI 105
KinB COG5806
Sporulation sensor histidine kinase B [Cell cycle control, cell division, chromosome ...
106-356 7.76e-26

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


Pssm-ID: 444508 [Multi-domain]  Cd Length: 412  Bit Score: 109.19  E-value: 7.76e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539062979 106 LLVAYFIN--VTAQRQFEEqLRQAQKMEAVGQLTGGIAHDFNNHLGGIIGSLGIMQKRiaKGTCVGLERYTDNAMASAQR 183
Cdd:COG5806   173 LIAVYLIEnlIENILLRKE-LQRAEKLEVVSELAASIAHEVRNPLTVVRGFIQLLQEP--ELSDEKRKQYIRIALEELDR 249
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539062979 184 AASLTHRLLAFSRRQSLNPKPLklnDLFDEFQSFIN--QSLGPEYRFEVH--YEGDLwTTFCDHHQLENAVLNLAINARD 259
Cdd:COG5806   250 AEAIITDYLTFAKPQPEKLEKI---DVSEELEHVIDvlSPYANMNNVEIQteLEPGL-YIEGDRQKLQQCLINIIKNGIE 325
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539062979 260 AMPNGGIIicQITNSAsvpglfEGECVCISIVDTGTGIAPEIMDRVIEPFFTTKpiGEGTGLGLSMVYGFVKQSNGHFTI 339
Cdd:COG5806   326 AMPNGGTL--TIDVSI------DKNKVIISIKDTGVGMTKEQLERLGEPYFSTK--EKGTGLGTMVSYRIIEAMNGTIRV 395
                         250
                  ....*....|....*..
gi 1539062979 340 ESTQAKGTTVSLYLPRY 356
Cdd:COG5806   396 ESEVGKGTTFTITLPLA 412
AtoC COG2204
DNA-binding transcriptional response regulator, NtrC family, contains REC, AAA-type ATPase, ...
376-496 1.42e-24

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


Pssm-ID: 441806 [Multi-domain]  Cd Length: 418  Bit Score: 105.82  E-value: 1.42e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539062979 376 QQTVMLVEDDEVLREIIIEVLEDLDYHVLSTGNGQHALELIvtAAKPVDLLLTDIGLPGINGRDLAAHVLDRFPKLKIMF 455
Cdd:COG2204     2 MARILVVDDDPDIRRLLKELLERAGYEVETAASGEEALALL--REEPPDLVLLDLRMPGMDGLELLRELRALDPDLPVIL 79
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1539062979 456 ITGYDKTVTLPKSLFRHDVEVMTKPFTISELASRVQRLLEQ 496
Cdd:COG2204    80 LTGYGDVETAVEAIKAGAFDYLTKPFDLEELLAAVERALER 120
HATPase_c smart00387
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.
242-354 2.71e-24

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


Pssm-ID: 214643 [Multi-domain]  Cd Length: 111  Bit Score: 97.33  E-value: 2.71e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539062979  242 DHHQLENAVLNLAINARDAMPNGGIIICQITnsasvpglFEGECVCISIVDTGTGIAPEIMDRVIEPFFTTKPI---GEG 318
Cdd:smart00387   2 DPDRLRQVLSNLLDNAIKYTPEGGRITVTLE--------RDGDHVEITVEDNGPGIPPEDLEKIFEPFFRTDKRsrkIGG 73
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1539062979  319 TGLGLSMVYGFVKQSNGHFTIESTQAKGTTVSLYLP 354
Cdd:smart00387  74 TGLGLSIVKKLVELHGGEISVESEPGGGTTFTITLP 109
REC_hyHK_blue-like cd18161
phosphoacceptor receiver (REC) domain of hybrid sensor histidine kinase/response regulators ...
379-481 1.40e-23

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


Pssm-ID: 381145 [Multi-domain]  Cd Length: 102  Bit Score: 95.11  E-value: 1.40e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539062979 379 VMLVEDDEVLREIIIEVLEDLDYHVLSTGNGQHALELIvTAAKPVDLLLTDIGLPG-INGRDLAAHVLDRFPKLKIMFIT 457
Cdd:cd18161     1 VLVVEDDPDVRRLTAEVLEDLGYTVLEAASGDEALDLL-ESGPDIDLLVTDVIMPGgMNGSQLAEEARRRRPDLKVLLTS 79
                          90       100
                  ....*....|....*....|....*.
gi 1539062979 458 GYDKTVTLPKslfRHD--VEVMTKPF 481
Cdd:cd18161    80 GYAENAIEGG---DLApgVDVLSKPF 102
CitA COG3290
Sensor histidine kinase DipB regulating citrate/malate metabolism [Signal transduction ...
9-355 5.61e-23

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


Pssm-ID: 442519 [Multi-domain]  Cd Length: 389  Bit Score: 100.69  E-value: 5.61e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539062979   9 AVLEALPIPVIVKDLNHRIVFVNQAASGYF-QDPIDTLVGKTDYDCFPAEHAATYWQMEEKV-ISTQCPCENEETIIGpe 86
Cdd:COG3290    88 AVLESIREGVIAVDRDGRITLINDAARRLLgLDAIGRPIDEVLAEVLETGERDEEILLNGRVlVVNRVPIRDDGRVVG-- 165
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539062979  87 gkpqiiittktlvtvaneslLVAYFINVTAQRQFEEQLRQAQKMEavgQLTGGIAHDFNNHLGGIigsLGIMQkriakgt 166
Cdd:COG3290   166 --------------------AVATFRDRTELERLEEELEGVKELA---EALRAQRHDFRNHLHTI---SGLLQ------- 212
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539062979 167 cvgLERYtDNAMASAQRAASLTHRLLAFSRRQSLNPKplkLNDLFdefQSFINQ--SLGPEyrFEVHYEGDLWTTFCDHH 244
Cdd:COG3290   213 ---LGEY-DEALEYIDEISEELQELIDSLLSRIGNPV---LAALL---LGKAARarERGID--LTIDIDSDLPDLPLSDT 280
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539062979 245 QLENAVLNLAINARDAMPNGGIIICQITNSASVpglfEGECVCISIVDTGTGIAPEIMDRVIEPFFTTKPiGEGTGLGLS 324
Cdd:COG3290   281 DLVTILGNLLDNAIEAVEKLPEEERRVELSIRD----DGDELVIEVEDSGPGIPEELLEKIFERGFSTKL-GEGRGLGLA 355
                         330       340       350
                  ....*....|....*....|....*....|.
gi 1539062979 325 MVYGFVKQSNGHFTIESTQAKGTTVSLYLPR 355
Cdd:COG3290   356 LVKQIVEKYGGTIEVESEEGEGTVFTVRLPK 386
RpfG COG3437
Response regulator c-di-GMP phosphodiesterase, RpfG family, contains REC and HD-GYP domains ...
371-496 9.21e-22

Response regulator c-di-GMP phosphodiesterase, RpfG family, contains REC and HD-GYP domains [Signal transduction mechanisms];


Pssm-ID: 442663 [Multi-domain]  Cd Length: 224  Bit Score: 93.69  E-value: 9.21e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539062979 371 LKEGLQQTVMLVEDDEVLREIIIEVLEDLDYHVLSTGNGQHALELIvtAAKPVDLLLTDIGLPGINGRDLAAHV--LDRF 448
Cdd:COG3437     1 MRTGQAPTVLIVDDDPENLELLRQLLRTLGYDVVTAESGEEALELL--LEAPPDLILLDVRMPGMDGFELLRLLraDPST 78
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1539062979 449 PKLKIMFITGYDKTVTLPKSLFRHDVEVMTKPFTISELASRVQRLLEQ 496
Cdd:COG3437    79 RDIPVIFLTALADPEDRERALEAGADDYLTKPFDPEELLARVRNALEL 126
HATPase_c pfam02518
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the ...
242-357 1.13e-21

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: 89.73  E-value: 1.13e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539062979 242 DHHQLENAVLNLAINARDAMPNGGIIICQITnsasvpglfEGECVCISIVDTGTGIAPEIMDRVIEPFFTTKPI-GEGTG 320
Cdd:pfam02518   2 DELRLRQVLSNLLDNALKHAAKAGEITVTLS---------EGGELTLTVEDNGIGIPPEDLPRIFEPFSTADKRgGGGTG 72
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1539062979 321 LGLSMVYGFVKQSNGHFTIESTQAKGTTVSLYLPRYI 357
Cdd:pfam02518  73 LGLSIVRKLVELLGGTITVESEPGGGTTVTLTLPLAQ 109
OmpR COG0745
DNA-binding response regulator, OmpR family, contains REC and winged-helix (wHTH) domain ...
376-494 1.50e-21

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: 92.33  E-value: 1.50e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539062979 376 QQTVMLVEDDEVLREIIIEVLEDLDYHVLSTGNGQHALELIvtAAKPVDLLLTDIGLPGINGRDLAAHVLDRFPKLKIMF 455
Cdd:COG0745     1 MPRILVVEDDPDIRELLADALEREGYEVDTAADGEEALELL--EEERPDLILLDLMLPGMDGLEVCRRLRARPSDIPIIM 78
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1539062979 456 ITGYDKTVTLPKSLfrhDV---EVMTKPFTISELASRVQRLL 494
Cdd:COG0745    79 LTARDDEEDRVRGL---EAgadDYLTKPFDPEELLARIRALL 117
PleD COG3706
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate ...
378-490 3.45e-21

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


Pssm-ID: 442920 [Multi-domain]  Cd Length: 179  Bit Score: 90.74  E-value: 3.45e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539062979 378 TVMLVEDDEVLREIIIEVLEDLDYHVLSTGNGQHALELIvtAAKPVDLLLTDIGLPGINGRDLAAHV--LDRFPKLKIMF 455
Cdd:COG3706     3 RILVVDDDPTNRKLLRRLLEAAGYEVVEAADGEEALELL--QEHRPDLILLDLEMPDMDGLELCRRLraDPRTADIPIIF 80
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1539062979 456 ITGYDKTVTLPKSLFRHDVEVMTKPFTISELASRV 490
Cdd:COG3706    81 LTALDDEEDRARALEAGADDYLTKPFDPEELLARV 115
CitB COG4565
DNA-binding response regulator DpiB of citrate/malate metabolism [Transcription, Signal ...
378-495 7.41e-21

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


Pssm-ID: 443622 [Multi-domain]  Cd Length: 138  Bit Score: 88.49  E-value: 7.41e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539062979 378 TVMLVEDDEVLREIIIEVLEDLDYH--VLSTGNGQHALELIvtAAKPVDLLLTDIGLPGINGRDLAAHVLDRFPKLKIMF 455
Cdd:COG4565     5 RVLIVEDDPMVAELLRRYLERLPGFevVGVASSGEEALALL--AEHRPDLILLDIYLPDGDGLELLRELRARGPDVDVIV 82
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1539062979 456 ITGYDKTVTLPKSLFRHDVEVMTKPFTISELASRVQRLLE 495
Cdd:COG4565    83 ITAARDPETVREALRAGVVDYLIKPFTFERLREALERYLE 122
COG4251 COG4251
Bacteriophytochrome (light-regulated signal transduction histidine kinase) [Signal ...
2-355 9.63e-21

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


Pssm-ID: 443393 [Multi-domain]  Cd Length: 503  Bit Score: 95.24  E-value: 9.63e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539062979   2 LDKEAALAVLEALPIPVIVKDLNHRIVFVNQAASGYFQDPIDTLVGKTDYDCFPAEHAATYWQMEEKVISTQCPCENEET 81
Cdd:COG4251   137 LEELALLRLALALLLLLLLLLLLLLLLLALILALLLAALAELELLLLLLLVLLLLLLLLLLLLLLLLRLLLELLLLLEAE 216
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539062979  82 IIGPEGKPQIIITTKTLVTVANESLLVAYFINVTAQRQFEEQLRQAQKMEAVGQLTG--------------GIAHDFNNH 147
Cdd:COG4251   217 LLLSLGGGLGLLLLLLLLLVLLLLLILLLLLLILVLELLELRLELEELEEELEERTAelersneeleqfayVASHDLREP 296
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539062979 148 LGGIIGSLGIMQKRIAKGTCVGLERYTDNAMASAQRAASLTHRLLAFSR--RQSLNPKPLKLNDLFDEFQSFINQSLgPE 225
Cdd:COG4251   297 LRKISGFSQLLEEDYGDKLDEEGREYLERIRDAAERMQALIDDLLAYSRvgRQELEFEPVDLNELLEEVLEDLEPRI-EE 375
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539062979 226 YRFEVHYEgDLWTTFCDHHQLENAVLNL---AINARDAMPNGgiiicQITNSASVpglfEGECVCISIVDTGTGIAPEIM 302
Cdd:COG4251   376 RGAEIEVG-PLPTVRGDPTLLRQVFQNLisnAIKYSRPGEPP-----RIEIGAER----EGGEWVFSVRDNGIGIDPEYA 445
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1539062979 303 DRVIEPFFT--TKPIGEGTGLGLSMVYGFVKQSNGHFTIESTQAKGTTVSLYLPR 355
Cdd:COG4251   446 EKIFEIFQRlhSRDEYEGTGIGLAIVKKIVERHGGRIWVESEPGEGATFYFTLPK 500
Response_reg pfam00072
Response regulator receiver domain; This domain receives the signal from the sensor partner in ...
379-491 6.65e-20

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: 84.90  E-value: 6.65e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539062979 379 VMLVEDDEVLREIIIEVLEDLDYHVLSTGNGQHALELIvtAAKPVDLLLTDIGLPGINGRDLAAHVLDRFPKLKIMFITG 458
Cdd:pfam00072   1 VLIVDDDPLIRELLRQLLEKEGYVVAEADDGKEALELL--KEERPDLILLDINMPGMDGLELLKRIRRRDPTTPVIILTA 78
                          90       100       110
                  ....*....|....*....|....*....|...
gi 1539062979 459 YDKTVTLPKSLFRHDVEVMTKPFTISELASRVQ 491
Cdd:pfam00072  79 HGDEDDAVEALEAGADDFLSKPFDPDELLAAIR 111
REC cd00156
phosphoacceptor receiver (REC) domain of response regulators (RRs) and pseudo response ...
380-480 3.03e-19

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: 82.66  E-value: 3.03e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539062979 380 MLVEDDEVLREIIIEVLEDLDYHVLSTGNGQHALELIvtAAKPVDLLLTDIGLPGINGRDLAAHVLDRFPKLKIMFITGY 459
Cdd:cd00156     1 LIVDDDPAIRELLKSLLEREGYEVDTAADGEEALELL--REERPDLVLLDLMMPGMDGLELLRKLRELPPDIPVIVLTAK 78
                          90       100
                  ....*....|....*....|.
gi 1539062979 460 DKTVTLPKSLFRHDVEVMTKP 480
Cdd:cd00156    79 ADEEDAVRALELGADDYLVKP 99
YesN COG4753
Two-component response regulator, YesN/AraC family, consists of REC and AraC-type DNA-binding ...
378-460 2.71e-18

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


Pssm-ID: 443786 [Multi-domain]  Cd Length: 103  Bit Score: 80.20  E-value: 2.71e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539062979 378 TVMLVEDDEVLREIIIEVLEDLD--YHVLSTGNGQHALELIvtAAKPVDLLLTDIGLPGINGRDLAAHVLDRFPKLKIMF 455
Cdd:COG4753     1 KVLIVDDEPLIREGLKRILEWEAgfEVVGEAENGEEALELL--EEHKPDLVITDINMPGMDGLELLEAIRELDPDTKIII 78

                  ....*
gi 1539062979 456 ITGYD 460
Cdd:COG4753    79 LSGYS 83
COG4192 COG4192
Signal transduction histidine kinase regulating phosphoglycerate transport system [Signal ...
118-354 3.25e-18

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


Pssm-ID: 443346 [Multi-domain]  Cd Length: 640  Bit Score: 87.82  E-value: 3.25e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539062979 118 RQFEEQLRQAQKMEAVGQLTGGIAHDFNNHLGGIIGSLGIMQKRIAKGTCVGLERYTDNAMASAQRAASLTHRLLAFSRR 197
Cdd:COG4192   418 RQTQDELIQAAKMAVVGQTMTSLAHELNQPLNAMSMYLFSAKKALEQENYAQLPTSLDKIEGLIERMDKIIKSLRQFSRK 497
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539062979 198 QSLNPKPLKLNDLFDEFQSFINQSLGPEyRFEVHYEGDLWtTFCDHHQLENAVLNLAINARDAMPNGGIIicqitnsaSV 277
Cdd:COG4192   498 SDTPLQPVDLRQVIEQAWELVESRAKPQ-QITLHIPDDLM-VQGDQVLLEQVLVNLLVNALDAVATQPQI--------SV 567
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1539062979 278 PGLFEGECVCISIVDTGTGIApeIMDRVIEPFFTTKPIgeGTGLGLSMVYGFVKQSNGHFTIESTQAKGTTVSLYLP 354
Cdd:COG4192   568 DLLSNAENLRVAISDNGNGWP--LVDKLFTPFTTTKEV--GLGLGLSICRSIMQQFGGDLYLASTLERGAMVILEFN 640
REC_TrrA-like cd17554
phosphoacceptor receiver (REC) domain of Thermotoga maritima response regulator TrrA and ...
378-493 1.09e-16

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: 75.72  E-value: 1.09e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539062979 378 TVMLVEDDEVLREIIIEVLEDLDYHVLSTGNGQHALELIvtAAKPVDLLLTDIGLPGINGRDLAAHVLDRFPKLKIMFIT 457
Cdd:cd17554     2 KILVVDDEENIRELYKEELEDEGYEVVTAGNGEEALEKL--ESEDPDLVILDIKMPGMDGLETLRKIREKKPDLPVIICT 79
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1539062979 458 GYdktvtlpkSLFRHDVE--------VMTKPFTisELASRVQRL 493
Cdd:cd17554    80 AY--------SEYKSDFSswaadayvVKSSDLT--ELKETIKRL 113
HATPase_HupT_MifS-like cd16976
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
246-353 1.63e-16

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


Pssm-ID: 340435 [Multi-domain]  Cd Length: 102  Bit Score: 75.19  E-value: 1.63e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539062979 246 LENAVLNLAINARDAM---PNGGIiicqitnsaSVPGLFEGECVCISIVDTGTGIAPEIMDRVIEPFFTTKPIGEGTGLG 322
Cdd:cd16976     1 IQQVLMNLLQNALDAMgkvENPRI---------RIAARRLGGRLVLVVRDNGPGIAEEHLSRVFDPFFTTKPVGKGTGLG 71
                          90       100       110
                  ....*....|....*....|....*....|.
gi 1539062979 323 LSMVYGFVKQSNGHFTIESTQAKGTTVSLYL 353
Cdd:cd16976    72 LSISYGIVEEHGGRLSVANEEGAGARFTFDL 102
REC_YesN-like cd17536
phosphoacceptor receiver (REC) domain of YesN and related helix-turn-helix containing response ...
379-496 2.33e-16

phosphoacceptor receiver (REC) domain of YesN and related helix-turn-helix containing response regulators; This family is composed of uncharacterized response regulators that contain a REC domain and a AraC family helix-turn-helix (HTH) DNA-binding output domain, including Bacillus subtilis uncharacterized transcriptional regulatory protein YesN and Staphylococcus aureus uncharacterized response regulatory protein SAR0214. YesN is a member of the two-component regulatory system YesM/YesN and SAR0214 is a member of the probable two-component regulatory system SAR0215/SAR0214. Also included in this family is the AlgR-like group of LytTR/AlgR family response, which includes Pseudomonas aeruginosa positive alginate biosynthesis regulatory protein AlgR and Bacillus subtilis sensory transduction protein LytT, among others. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381091 [Multi-domain]  Cd Length: 121  Bit Score: 75.07  E-value: 2.33e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539062979 379 VMLVEDDEVLREIIIEVL--EDLDYHVLST-GNGQHALELIvtAAKPVDLLLTDIGLPGINGRDLAAHVLDRFPKLKIMF 455
Cdd:cd17536     1 VLIVDDEPLIREGLKKLIdwEELGFEVVGEaENGEEALELI--EEHKPDIVITDIRMPGMDGLELIEKIRELYPDIKIII 78
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1539062979 456 ITGYDKtvtlpkslF-------RHDV-EVMTKPFTISELASRVQRLLEQ 496
Cdd:cd17536    79 LSGYDD--------FeyaqkaiRLGVvDYLLKPVDEEELEEALEKAKEE 119
glnL PRK11073
nitrogen regulation protein NR(II);
1-354 3.51e-16

nitrogen regulation protein NR(II);


Pssm-ID: 182947 [Multi-domain]  Cd Length: 348  Bit Score: 79.74  E-value: 3.51e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539062979   1 MLDKEAALAVLEALPIPVIVKDLNHRIVFVNQAASGYFQDPIDTLVGKtdydcfPAEHAATYWQ-----MEEKVISTQCP 75
Cdd:PRK11073    3 TGTLPDAGQILNSLINSILLLDDDLAIHYANPAAQQLLAQSSRKLFGT------PLPELLSYFSlnielMRESLQAGQGF 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539062979  76 CENEETIIgPEGKPQIIITTKTLVTvanESLLVAYFINVTAQRQF-EEQLRQAQKMeAVGQLTGGIAHDFNNHLGGIIGS 154
Cdd:PRK11073   77 TDNEVTLV-IDGRSHILSLTAQRLP---EGMILLEMAPMDNQRRLsQEQLQHAQQV-AARDLVRGLAHEIKNPLGGLRGA 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539062979 155 LGIMQKRIAKGTcvgLERYTDNAMASAQRAASLTHRLLAFSR---RQSLNpkplkLNDLFDEFQSFINQSLGPEYRFEVH 231
Cdd:PRK11073  152 AQLLSKALPDPA---LTEYTKVIIEQADRLRNLVDRLLGPQRpgtHVTES-----IHKVAERVVQLVSLELPDNVRLIRD 223
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539062979 232 YEGDLWTTFCDHHQLENAVLNLAINARDAM-PNGGIIIC------QITnsasvpglFEGE----CVCISIVDTGTGIAPE 300
Cdd:PRK11073  224 YDPSLPELAHDPDQIEQVLLNIVRNALQALgPEGGTITLrtrtafQLT--------LHGEryrlAARIDIEDNGPGIPPH 295
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1539062979 301 IMDRVIEPFFTTKPigEGTGLGLSMVYGFVKQSNGHftIESTQAKG-TTVSLYLP 354
Cdd:PRK11073  296 LQDTLFYPMVSGRE--GGTGLGLSIARNLIDQHSGK--IEFTSWPGhTEFSVYLP 346
HATPase_Glnl-NtrB-like cd16918
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
246-354 1.72e-15

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: 72.43  E-value: 1.72e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539062979 246 LENAVLNLAINARDAMPNGG--IIICQITNSASVPGLFEGECVC-ISIVDTGTGIAPEIMDRVIEPFFTTKPigEGTGLG 322
Cdd:cd16918     1 LIQVFLNLVRNAAQALAGSGgeIILRTRTQRQVTLGHPRHRLALrVSVIDNGPGIPPDLQDTIFYPMVSGRE--NGTGLG 78
                          90       100       110
                  ....*....|....*....|....*....|...
gi 1539062979 323 LSMVYGFVKQSNGhfTIESTQAKGTTV-SLYLP 354
Cdd:cd16918    79 LAIAQNIVSQHGG--VIECDSQPGHTVfSVSLP 109
HATPase_TmoS-FixL-DctS-like cd16920
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
246-354 2.30e-15

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: 71.66  E-value: 2.30e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539062979 246 LENAVLNLAINARDAMPNGGII--ICQITNSASVPGLfegecVCISIVDTGTGIAPEIMDRVIEPFFTTKPigEGTGLGL 323
Cdd:cd16920     1 IQQVLINLVRNGIEAMSEGGCErrELTIRTSPADDRA-----VTISVKDTGPGIAEEVAGQLFDPFYTTKS--EGLGMGL 73
                          90       100       110
                  ....*....|....*....|....*....|.
gi 1539062979 324 SMVYGFVKQSNGHFTIESTQAKGTTVSLYLP 354
Cdd:cd16920    74 SICRSIIEAHGGRLSVESPAGGGATFQFTLP 104
REC_CpdR_CckA-like cd18160
phosphoacceptor receiver (REC) domain of Brucella abortus CpdR and CckA, and similar domains; ...
378-481 9.60e-15

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: 69.84  E-value: 9.60e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539062979 378 TVMLVEDDEVLREIIIEVLEDLDYHVLSTGNGQHALElIVTAAKPVDLLLTDIGLPGINGRDLAAHVLDRFPKLKIMFIT 457
Cdd:cd18160     1 TILLADDEPSVRKFIVTTLKKAGYAVTEAESGAEALE-KLQQGKDIDIVVTDIVMPEMDGIELAREARKIDPDVKILFIS 79
                          90       100
                  ....*....|....*....|....
gi 1539062979 458 GYDKTVTLPKSLFRHDVEVMTKPF 481
Cdd:cd18160    80 GGAAAAPELLSDAVGDNATLKKPF 103
REC_OmpR cd17574
phosphoacceptor receiver (REC) domain of OmpR family response regulators; OmpR-like proteins ...
380-457 4.99e-14

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: 67.82  E-value: 4.99e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1539062979 380 MLVEDDEVLREIIIEVLEDLDYHVLSTGNGQHALELIvtAAKPVDLLLTDIGLPGINGRDLAAHVLDRFPKLKIMFIT 457
Cdd:cd17574     1 LVVEDDEEIAELLSDYLEKEGYEVDTAADGEEALELA--REEQPDLIILDVMLPGMDGFEVCRRLREKGSDIPIIMLT 76
PRK15347 PRK15347
two component system sensor kinase;
113-437 5.35e-14

two component system sensor kinase;


Pssm-ID: 237951 [Multi-domain]  Cd Length: 921  Bit Score: 74.68  E-value: 5.35e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539062979 113 NVTAQR--QFEEQLRQAQKMEA--VGQLTGgIAHDFNNHLGGIIGSLGIMQKriakgTCVGLE--RYTDNAMASAQRAAS 186
Cdd:PRK15347  375 NKVAERtqALAEAKQRAEQANKrkSEHLTT-ISHEIRTPLNGVLGALELLQN-----TPLTAEqmDLADTARQCTLSLLA 448
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539062979 187 LTHRLLAFSRRQS----LNPKPLKLNDLFDE----FQS-----------FINQSLgPEYrfevhyegdLWTtfcDHHQLE 247
Cdd:PRK15347  449 IINNLLDFSRIESgqmtLSLEETALLPLLDQamltIQGpaqsksltlrtFVGAHV-PLY---------LHL---DSLRLR 515
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539062979 248 NAVLNLAINARDAMPNGGIiicqitnsaSVPGLFEGECVCISIVDTGTGIAPEIMDRVIEPFFTTKPIGEGTGLGLSMVY 327
Cdd:PRK15347  516 QILVNLLGNAVKFTETGGI---------RLRVKRHEQQLCFTVEDTGCGIDIQQQQQIFTPFYQADTHSQGTGLGLTIAS 586
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539062979 328 GFVKQSNGHFTIESTQAKGTTVSLYLP------------------------RYIGETCQhtSSTDEP------------- 370
Cdd:PRK15347  587 SLAKMMGGELTLFSTPGVGSCFSLVLPlneyappeplkgelsaplalhrqlSAWGITCQ--PGHQNPalldpelaylpgr 664
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539062979 371 ----LKEGLQQT----------------VMLVEDDEVLREIIIEVLEDLDYHVLSTGNGQHALELivTAAKPVDLLLTDI 430
Cdd:PRK15347  665 lydlLQQIIQGApnepvinlplqpwqlqILLVDDVETNRDIIGMMLVELGQQVTTAASGTEALEL--GRQHRFDLVLMDI 742

                  ....*..
gi 1539062979 431 GLPGING 437
Cdd:PRK15347  743 RMPGLDG 749
PAS COG2202
PAS domain [Signal transduction mechanisms];
5-152 8.95e-14

PAS domain [Signal transduction mechanisms];


Pssm-ID: 441804 [Multi-domain]  Cd Length: 258  Bit Score: 71.21  E-value: 8.95e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539062979   5 EAALAVLEALPIPVIVKDLNHRIVFVNQAASGYFQDPIDTLVGKTDYDCFPAEHAATYWQMEEKVISTQCPCENEETIIG 84
Cdd:COG2202    11 RRLRALVESSPDAIIITDLDGRILYVNPAFERLTGYSAEELLGKTLRDLLPPEDDDEFLELLRAALAGGGVWRGELRNRR 90
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539062979  85 PEGKPQIIITTKTLVTVANESL--LVAYFINVTAQRQFEEQLRQAQKMEAVGQLTGGIAHDFNNHLGGII 152
Cdd:COG2202    91 KDGSLFWVELSISPVRDEDGEItgFVGIARDITERKRAEEALRESEERLRLLVENAPDGIFVLDLDGRIL 160
PRK11091 PRK11091
aerobic respiration control sensor protein ArcB; Provisional
196-450 1.78e-13

aerobic respiration control sensor protein ArcB; Provisional


Pssm-ID: 236842 [Multi-domain]  Cd Length: 779  Bit Score: 73.05  E-value: 1.78e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539062979 196 RRQSLNPKPLKLNDLFDEFQSFINQSLGPE-YRFEVHYEGDLWTTFC-DHHQLENAVLNLAINARDAMPNGGIIIcqiTN 273
Cdd:PRK11091  347 RKLQLDNQPIDFTDFLADLENLSGLQAEQKgLRFDLEPLLPLPHKVItDGTRLRQILWNLISNAVKFTQQGGVTV---RV 423
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539062979 274 SASvpglfEGECVCISIVDTGTGIAPEIMDRVIEPFFTTKPIGE-----GTGLGLSMVYGFVKQSNGHFTIESTQAKGT- 347
Cdd:PRK11091  424 RYE-----EGDMLTFEVEDSGIGIPEDELDKIFAMYYQVKDSHGgkpatGTGIGLAVSKRLAQAMGGDITVTSEEGKGSc 498
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539062979 348 -TVSLYLPRyIGETCQHTSSTDEPLKEGLQqtVMLVEDDEVLREIIIEVLEDLDYHVLSTGNGQHALELIvtAAKPVDLL 426
Cdd:PRK11091  499 fTLTIHAPA-VAEEVEDAFDEDDMPLPALN--ILLVEDIELNVIVARSVLEKLGNSVDVAMTGKEALEMF--DPDEYDLV 573
                         250       260
                  ....*....|....*....|....
gi 1539062979 427 LTDIGLPGINGRDLAAHVLDRFPK 450
Cdd:PRK11091  574 LLDIQLPDMTGLDIARELRERYPR 597
PRK11100 PRK11100
sensory histidine kinase CreC; Provisional
171-355 3.62e-13

sensory histidine kinase CreC; Provisional


Pssm-ID: 236846 [Multi-domain]  Cd Length: 475  Bit Score: 71.41  E-value: 3.62e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539062979 171 ERYTDNAMASAQRAASLTHRLLAFSR---RQSL-NPKPLKLNDLFDEF-----QSFINQSLGPEYRFE---VHYEGDLwt 238
Cdd:PRK11100  291 ARFTGNILTQSARLQQLIDRLLELARleqRQELeVLEPVALAALLEELveareAQAAAKGITLRLRPDdarVLGDPFL-- 368
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539062979 239 tfcdhhqLENAVLNLAINARDAMPNGGiiicQITNSASVpglfEGECVCISIVDTGTGIAPEIMDRVIEPFFTT-KPIGE 317
Cdd:PRK11100  369 -------LRQALGNLLDNAIDFSPEGG----TITLSAEV----DGEQVALSVEDQGPGIPDYALPRIFERFYSLpRPANG 433
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1539062979 318 --GTGLGLSMVYGFVKQSNGHFTIESTQAKGTTVSLYLPR 355
Cdd:PRK11100  434 rkSTGLGLAFVREVARLHGGEVTLRNRPEGGVLATLTLPR 473
PRK11466 PRK11466
hybrid sensory histidine kinase TorS; Provisional
114-452 7.78e-13

hybrid sensory histidine kinase TorS; Provisional


Pssm-ID: 236914 [Multi-domain]  Cd Length: 914  Bit Score: 71.09  E-value: 7.78e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539062979 114 VTAQRQFEEQLRQAQkmEAVGQLTGGIAHDFNNHLGGIIGSLGIMQKRIAKGTCVG-LERYTDnamaSAQRAASLTHRLL 192
Cdd:PRK11466  427 VIEHRQARAEAEKAS--QAKSAFLAAMSHEIRTPLYGILGTAQLLADNPALNAQRDdLRAITD----SGESLLTILNDIL 500
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539062979 193 AFS------RRQSLNPKPLKLNDLFDEFQSFINQSL-GPEYRFEVHYEGDLWTTFC-DHHQLENAVLNLAINARDAMPNG 264
Cdd:PRK11466  501 DYSaieaggKNVSVSDEPFEPRPLLESTLQLMSGRVkGRPIRLATDIADDLPTALMgDPRRIRQVITNLLSNALRFTDEG 580
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539062979 265 GIIICQITnsasvpglfEGECVCISIVDTGTGIAPEIMDRVIEPFFTTKPIGEGTGLGLSMVYGFVKQSNGHFTIESTQA 344
Cdd:PRK11466  581 SIVLRSRT---------DGEQWLVEVEDSGCGIDPAKLAEIFQPFVQVSGKRGGTGLGLTISSRLAQAMGGELSATSTPE 651
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539062979 345 KGTTVSLYLPRYIGETcqhtsstdePLKEGLQQTV-------MLVEDDEVLREIIIEVLEDLDYHVLSTGNGQHALELIV 417
Cdd:PRK11466  652 VGSCFCLRLPLRVATA---------PVPKTVNQAVrldglrlLLIEDNPLTQRITAEMLNTSGAQVVAVGNAAQALETLQ 722
                         330       340       350
                  ....*....|....*....|....*....|....*
gi 1539062979 418 TaAKPVDLLLTDIGLPGINGRDLAAHVLDRFPKLK 452
Cdd:PRK11466  723 N-SEPFAAALVDFDLPDYDGITLARQLAQQYPSLV 756
REC_typeB_ARR-like cd17584
phosphoacceptor receiver (REC) domain of type B Arabidopsis response regulators (ARRs) and ...
379-494 2.61e-12

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: 63.42  E-value: 2.61e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539062979 379 VMLVEDDEVLREIIIEVLEDLDYHVLSTGNGQHALELIVTAAKPVDLLLTDIGLPGINGRDLAAHVLDRFpKLKIMFITG 458
Cdd:cd17584     1 VLVVDDDPTCLAILKRMLLRCGYQVTTCTDAEEALSMLRENKDEFDLVITDVHMPDMDGFEFLELIRLEM-DLPVIMMSA 79
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1539062979 459 YDKTVTLPKSLFRHDVEVMTKPFTISELASRVQRLL 494
Cdd:cd17584    80 DGSTSTVMKGLAHGACDYLLKPVSIEDLKNIWQHVV 115
REC_RssB-like cd17555
phosphoacceptor receiver (REC) domain of Pseudomonas aeruginosa RssB and similar domains; ...
378-458 3.80e-12

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: 62.99  E-value: 3.80e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539062979 378 TVMLVEDDEVLREIIIEVLEDLDYHVLSTGNGQHALELIvtAAKPVDLLLTDIGLPGINGRDLAAHVLDRFPKLKIMFIT 457
Cdd:cd17555     2 TILVIDDDEVVRESIAAYLEDSGFQVLQAADGRQGLELF--RSEQPDLVLCDLRMPEMDGLEVLKQITKESPDTPVIVVS 79

                  .
gi 1539062979 458 G 458
Cdd:cd17555    80 G 80
REC_hyHK_CKI1_RcsC-like cd17546
phosphoacceptor receiver (REC) domain of hybrid sensor histidine kinases/response regulators ...
379-486 5.86e-12

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: 62.49  E-value: 5.86e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539062979 379 VMLVEDDEVLREIIIEVLEDLDYHVLSTGNGQHALELIvtAAKPVDLLLTDIGLPGINGRDLAAHV---LDRFPKLKIMF 455
Cdd:cd17546     1 VLVVDDNPVNRKVLKKLLEKLGYEVDVAENGQEALELL--KEEPFDLVLMDLQMPVMDGLEATRRIrelEGGGRRTPIIA 78
                          90       100       110
                  ....*....|....*....|....*....|....
gi 1539062979 456 ITGYDKTVTLPKSLfrhDV---EVMTKPFTISEL 486
Cdd:cd17546    79 LTANALEEDREKCL---EAgmdDYLSKPVKLDQL 109
REC_NarL-like cd17535
phosphoacceptor receiver (REC) domain of NarL (Nitrate/Nitrite response regulator L) family ...
379-460 5.99e-12

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: 62.53  E-value: 5.99e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539062979 379 VMLVEDDEVLRE---IIIEVLEDLDYhVLSTGNGQHALELIvtAAKPVDLLLTDIGLPGINGRDLAAHVLDRFPKLKIMF 455
Cdd:cd17535     1 VLIVDDHPLVREglrRLLESEPDIEV-VGEAADGEEALALL--RELRPDVVLMDLSMPGMDGIEALRRLRRRYPDLKVIV 77

                  ....*
gi 1539062979 456 ITGYD 460
Cdd:cd17535    78 LTAHD 82
REC_OmpR_PmrA-like cd17624
phosphoacceptor receiver (REC) domain of PmrA-like OmpR family response regulators; This ...
379-494 6.59e-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: 62.12  E-value: 6.59e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539062979 379 VMLVEDDEVLREIIIEVLEDLDYHVLSTGNGQHALELIvtAAKPVDLLLTDIGLPGINGRDLAAHVLDRFPKLKIMFITG 458
Cdd:cd17624     1 ILLVEDDALLGDGLKTGLRKAGYAVDWVRTGAEAEAAL--ASGPYDLVILDLGLPDGDGLDLLRRWRRQGQSLPVLILTA 78
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1539062979 459 YDKTVTLPKSLfrhDV---EVMTKPFTISELASRVQRLL 494
Cdd:cd17624    79 RDGVDDRVAGL---DAgadDYLVKPFALEELLARLRALL 114
LytT COG3279
DNA-binding response regulator, LytR/AlgR family [Transcription, Signal transduction ...
378-496 8.69e-12

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


Pssm-ID: 442510 [Multi-domain]  Cd Length: 235  Bit Score: 64.84  E-value: 8.69e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539062979 378 TVMLVEDDEVLREIIIEVLEDLDYH--VLSTGNGQHALELIvtAAKPVDLLLTDIGLPGINGRDLAAHVLDRFPKLKIMF 455
Cdd:COG3279     3 KILIVDDEPLARERLERLLEKYPDLevVGEASNGEEALELL--EEHKPDLVFLDIQMPGLDGFELARQLRELDPPPPIIF 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1539062979 456 ITGYDKTVtlPKSlFRHD-VEVMTKPFTISELASRVQRLLEQ 496
Cdd:COG3279    81 TTAYDEYA--LEA-FEVNaVDYLLKPIDEERLAKALEKAKER 119
REC_OmpR_PhoB cd17618
phosphoacceptor receiver (REC) domain of PhoB response regulator from the OmpR family; The ...
378-494 2.49e-11

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: 60.73  E-value: 2.49e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539062979 378 TVMLVEDDEVLREIIIEVLEDLDYHVLSTGNGQHALELIVTaaKPVDLLLTDIGLPGINGRDLAAHvLDRFPKLK---IM 454
Cdd:cd17618     2 TILIVEDEPAIREMIAFNLERAGFDVVEAEDAESAVNLIVE--PRPDLILLDWMLPGGSGIQFIRR-LKRDEMTRdipII 78
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1539062979 455 FITG----YDKTVTLpkslfrhDV---EVMTKPFTISELASRVQRLL 494
Cdd:cd17618    79 MLTArgeeEDKVRGL-------EAgadDYITKPFSPRELVARIKAVL 118
HATPase_EvgS-ArcB-TorS-like cd16922
Histidine kinase-like ATPase domain of two-component sensor histidine kinases, many are hybrid ...
250-354 3.23e-11

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: 60.20  E-value: 3.23e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539062979 250 VLNLAINARDAMPNGGIIIcqitnSASVPGLFEGECV-CISIVDTGTGIAPEIMDRVIEPFF-----TTKPIGeGTGLGL 323
Cdd:cd16922     5 LLNLLGNAIKFTEEGEVTL-----RVSLEEEEEDGVQlRFSVEDTGIGIPEEQQARLFEPFSqadssTTRKYG-GTGLGL 78
                          90       100       110
                  ....*....|....*....|....*....|.
gi 1539062979 324 SMVYGFVKQSNGHFTIESTQAKGTTVSLYLP 354
Cdd:cd16922    79 AISKKLVELMGGDISVESEPGQGSTFTFTLP 109
HATPase_DpiB-CitA-like cd16915
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
252-354 3.98e-11

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: 59.61  E-value: 3.98e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539062979 252 NLAINARDAMPNGGIIICQITNSASvpglFEGECVCISIVDTGTGIAPEIMDRVIEPFFTTKPIGEgTGLGLSMVYGFVK 331
Cdd:cd16915     7 NLIDNALDALAATGAPNKQVEVFLR----DEGDDLVIEVRDTGPGIAPELRDKVFERGVSTKGQGE-RGIGLALVRQSVE 81
                          90       100
                  ....*....|....*....|...
gi 1539062979 332 QSNGHFTIESTQAKGTTVSLYLP 354
Cdd:cd16915    82 RLGGSITVESEPGGGTTFSIRIP 104
REC_citrate_TCS cd19925
phosphoacceptor receiver (REC) domain of citrate family two-component system response ...
378-492 4.06e-11

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


Pssm-ID: 381152 [Multi-domain]  Cd Length: 118  Bit Score: 59.95  E-value: 4.06e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539062979 378 TVMLVEDDEVLREIIIEVLEDLDY-HVLST-GNGQHALELIvtAAKPVDLLLTDIGLPGINGRDLAAHVLDRFPKLKIMF 455
Cdd:cd19925     2 NVLIVEDDPMVAEIHRAYVEQVPGfTVIGTaGTGEEALKLL--KERQPDLILLDIYLPDGNGLDLLRELRAAGHDVDVIV 79
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1539062979 456 ITGYDKTVTLPKSLFRHDVEVMTKPFTISELASRVQR 492
Cdd:cd19925    80 VTAANDVETVREALRLGVVDYLIKPFTFERLRQRLER 116
REC_DC-like cd17534
phosphoacceptor receiver (REC) domain of modulated diguanylate cyclase and similar domains; ...
378-486 4.81e-11

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: 59.73  E-value: 4.81e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539062979 378 TVMLVEDDEVLREIIIEVLEDLDYHVLST-GNGQHALELIvtAAKPVDLLLTDIGLPG-INGRDLAAHVLDRFPkLKIMF 455
Cdd:cd17534     2 KILIVEDEAIIALDLKEILESLGYEVVGIaDSGEEAIELA--EENKPDLILMDINLKGdMDGIEAAREIREKFD-IPVIF 78
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1539062979 456 ITGYDKTVTLPKSLfrhdvEV-----MTKPFTISEL 486
Cdd:cd17534    79 LTAYSDEETLERAK-----ETnpygyLVKPFNEREL 109
REC_DctD-like cd17549
phosphoacceptor receiver (REC) domain of C4-dicarboxylic acid transport protein D (DctD) and ...
379-496 5.01e-11

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


Pssm-ID: 381101 [Multi-domain]  Cd Length: 130  Bit Score: 60.20  E-value: 5.01e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539062979 379 VMLVEDDEVLREIIIEVLEDLDYHVLSTGNGQHALELIvtAAKPVDLLLTDIGLPGINGRDLAAHVLDRFPKLKIMFITG 458
Cdd:cd17549     1 VLLVDDDADVREALQQTLELAGFRVRAFADAEEALAAL--SPDFPGVVISDIRMPGMDGLELLAQIRELDPDLPVILITG 78
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1539062979 459 Y-DktVTLPkslfrhdVEVM--------TKPFTISELASRVQRLLEQ 496
Cdd:cd17549    79 HgD--VPMA-------VEAMragaydflEKPFDPERLLDVVRRALEK 116
REC smart00448
cheY-homologous receiver domain; CheY regulates the clockwise rotation of E. coli flagellar ...
378-433 5.12e-11

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: 57.96  E-value: 5.12e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1539062979  378 TVMLVEDDEVLREIIIEVLEDLDYHVLSTGNGQHALELIvtAAKPVDLLLTDIGLP 433
Cdd:smart00448   2 RILVVDDDPLLRELLKALLEKEGYEVDEATDGEEALELL--KEEKPDLILLDIMMP 55
REC_2_DhkD-like cd17580
second phosphoacceptor receiver (REC) domain of Dictyostelium discoideum hybrid signal ...
379-459 5.82e-11

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: 59.39  E-value: 5.82e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539062979 379 VMLVEDDEVLREIIIEVLEDLDYHVLSTGNGQHALELIvtAAKPVDLLLTDIGLPGINGRDLAAHVLDRFPKLKIMFI-- 456
Cdd:cd17580     1 ILVVDDNEDAAEMLALLLELEGAEVTTAHSGEEALEAA--QRFRPDVILSDIGMPGMDGYELARRLRELPWLANTPAIal 78

                  ...
gi 1539062979 457 TGY 459
Cdd:cd17580    79 TGY 81
REC_OmpR_ArcA_TorR-like cd17619
phosphoacceptor receiver (REC) domain of ArcA- and TorR-like OmpR family response regulators; ...
379-491 6.23e-11

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


Pssm-ID: 381134 [Multi-domain]  Cd Length: 113  Bit Score: 59.32  E-value: 6.23e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539062979 379 VMLVEDDEVLREIIIEVLEDLDYHVLSTGNGQHALELIvtAAKPVDLLLTDIGLPGINGRDLAAHvLDRFPKLKIMFITG 458
Cdd:cd17619     3 ILIVEDEPVTRATLKSYFEQEGYDVSEAGDGEEMRQIL--ARQDIDLVLLDINLPGKDGLSLTRE-LREQSEVGIILVTG 79
                          90       100       110
                  ....*....|....*....|....*....|...
gi 1539062979 459 YDKTVTLPKSLFRHDVEVMTKPFTISELASRVQ 491
Cdd:cd17619    80 RDDEVDRIVGLEIGADDYVTKPFNPRELLVRAK 112
HATPase_NtrY-like cd16944
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
242-354 7.32e-11

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: 59.09  E-value: 7.32e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539062979 242 DHHQLENAVLNLAINARDAMPNGGIIICQITnsASVPGLFEGECVcISIVDTGTGIAPEIMDRVIEPFFTTKPigEGTGL 321
Cdd:cd16944     1 DTTQISQVLTNILKNAAEAIEGRPSDVGEVR--IRVEADQDGRIV-LIVCDNGKGFPREMRHRATEPYVTTRP--KGTGL 75
                          90       100       110
                  ....*....|....*....|....*....|...
gi 1539062979 322 GLSMVYGFVKQSNGHFTIESTQAKGTTVSLYLP 354
Cdd:cd16944    76 GLAIVKKIMEEHGGRISLSNREAGGACIRIILP 108
HATPase_TutC-TodS-like cd16925
Histidine kinase-like ATPase domain of hybrid sensor histidine kinases similar to Pseudomonas ...
242-354 8.17e-11

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


Pssm-ID: 340402 [Multi-domain]  Cd Length: 110  Bit Score: 59.04  E-value: 8.17e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539062979 242 DHHQLENAVLNLAINARDAMPNGGIIICQITnsasvpgLFEGECVCISIVDTGTGIAPEIMDRVIEPFFTTKPIGE---- 317
Cdd:cd16925     1 DAEKYERVVLNLLSNAFKFTPDGGRIRCILE-------KFRLNRFLLTVSDSGPGIPPNLREEIFERFRQGDGSSTrahg 73
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1539062979 318 GTGLGLSMVYGFVKQSNGHFTIESTQAKGTTVSLYLP 354
Cdd:cd16925    74 GTGLGLSIVKEFVELHGGTVTVSDAPGGGALFQVELP 110
REC_RegA-like cd17563
phosphoacceptor receiver (REC) domain of photosynthetic apparatus regulatory protein RegA; ...
377-459 9.75e-11

phosphoacceptor receiver (REC) domain of photosynthetic apparatus regulatory protein RegA; Rhodobacter sphaeroides RegA, also called response regulator PrrA, is the DNA binding regulatory protein of a redox-responsive two-component regulatory system RegB/RegA that is involved in transactivating anaerobic expression of the photosynthetic apparatus. It contains a REC domain and a DNA-binding helix-turn-helix output domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381111 [Multi-domain]  Cd Length: 112  Bit Score: 58.99  E-value: 9.75e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539062979 377 QTVMLVEDDEVLREIIIEVLEDLDYHVLSTGNGQHALELIvtAAKPVDLLLTDIGLPGINGRDLAAHVLDRFPKLKIMFI 456
Cdd:cd17563     1 KSLLLVDDDEVFAERLARALERRGFEVETAHSVEEALALA--REEKPDYAVLDLRLGGDSGLDLIPPLRALQPDARIVVL 78

                  ...
gi 1539062979 457 TGY 459
Cdd:cd17563    79 TGY 81
phoR PRK11006
phosphate regulon sensor histidine kinase PhoR;
181-354 1.48e-10

phosphate regulon sensor histidine kinase PhoR;


Pssm-ID: 182895 [Multi-domain]  Cd Length: 430  Bit Score: 63.11  E-value: 1.48e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539062979 181 AQRAASLTHRLLAFSRRQS-----LNPK---PLKLNDLFDEFQSFINQslgpeyRFEVHYEGD-LWTTFCDHHQLENAVL 251
Cdd:PRK11006  250 TQRMEGLVKQLLTLSKIEAaptidLNEKvdvPMMLRVLEREAQTLSQG------KHTITFEVDnSLKVFGNEDQLRSAIS 323
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539062979 252 NLAINARDAMPNGG-IIICQITNSASVpglfegecvCISIVDTGTGIAPEIMDRVIEPFFT-----TKPIGeGTGLGLSM 325
Cdd:PRK11006  324 NLVYNAVNHTPEGThITVRWQRVPQGA---------EFSVEDNGPGIAPEHIPRLTERFYRvdkarSRQTG-GSGLGLAI 393
                         170       180
                  ....*....|....*....|....*....
gi 1539062979 326 VYGFVKQSNGHFTIESTQAKGTTVSLYLP 354
Cdd:PRK11006  394 VKHALSHHDSRLEIESEVGKGTRFSFVLP 422
PRK09959 PRK09959
acid-sensing system histidine kinase EvgS;
238-493 1.66e-10

acid-sensing system histidine kinase EvgS;


Pssm-ID: 182169 [Multi-domain]  Cd Length: 1197  Bit Score: 63.60  E-value: 1.66e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539062979  238 TTFCDHH-------QLENAVLNLAINARDAMPNGGIIIcqitnSASVPGLFEGECVC-ISIVDTGTGIAPEIMDRVIEPF 309
Cdd:PRK09959   814 STFPDHYlvkidpqAFKQVLSNLLSNALKFTTEGAVKI-----TTSLGHIDDNHAVIkMTIMDSGSGLSQEEQQQLFKRY 888
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539062979  310 FTTKPIGE--GTGLGLSMVYGFVKQSNGHFTIESTQAKGTTVSLYLP-RYIGETCQHTSSTDEPLKEGLQQTVMLVEDDE 386
Cdd:PRK09959   889 SQTSAGRQqtGSGLGLMICKELIKNMQGDLSLESHPGIGTTFTITIPvEISQQVATVEAKAEQPITLPEKLSILIADDHP 968
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539062979  387 VLREIIIEVLEDLDYHVLSTGNGQHALELIvtAAKPVDLLLTDIGLPGINGRDLAAHVLDRFPKLKIMFITGYDKTVTLP 466
Cdd:PRK09959   969 TNRLLLKRQLNLLGYDVDEATDGVQALHKV--SMQHYDLLITDVNMPNMDGFELTRKLREQNSSLPIWGLTANAQANERE 1046
                          250       260
                   ....*....|....*....|....*..
gi 1539062979  467 KSLFRHDVEVMTKPFTISELASRVQRL 493
Cdd:PRK09959  1047 KGLSCGMNLCLFKPLTLDVLKTHLSQL 1073
REC_OmpR_DrrD-like cd17625
phosphoacceptor receiver (REC) domain of DrrD-like OmpR family response regulators; DrrD is a ...
380-494 1.85e-10

phosphoacceptor receiver (REC) domain of DrrD-like OmpR family response regulators; DrrD is a OmpR/PhoB homolog from Thermotoga maritima whose function is not yet known. This subfamily also includes Streptococcus agalactiae transcriptional regulatory protein DltR, part of the DltS/DltR two-component system (TCS), and Pseudomonas aeruginosa transcriptional activator protein PfeR, part of the PfeR/PfeS TCS, which activates expression of the ferric enterobactin receptor. The DltS/DltR TCS regulates the expression of the dlt operon, which comprises four genes (dltA, dltB, dltC, and dltD) that catalyze the incorporation of D-alanine residues into the lipoteichoic acids. Members of this subfamily belong to the OmpR/PhoB family, which comprises of two domains, an N-terminal receiver domain and a C-terminal DNA-binding winged helix-turn-helix effector domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381140 [Multi-domain]  Cd Length: 115  Bit Score: 58.00  E-value: 1.85e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539062979 380 MLVEDDEVLREIIIEVLEDLDYHVLSTGNGQHALELIvtAAKPVDLLLTDIGLPGINGRDLAAHVLDRFPKLKIMFITGY 459
Cdd:cd17625     1 LVVEDEKDLSEAITKHLKKEGYTVDVCFDGEEGLEYA--LSGIYDLIILDIMLPGMDGLEVLKSLREEGIETPVLLLTAL 78
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1539062979 460 DKTVTLPKSLFRHDVEVMTKPFTISELASRVQRLL 494
Cdd:cd17625    79 DAVEDRVKGLDLGADDYLPKPFSLAELLARIRALL 113
PRK11361 PRK11361
acetoacetate metabolism transcriptional regulator AtoC;
377-495 2.79e-10

acetoacetate metabolism transcriptional regulator AtoC;


Pssm-ID: 183099 [Multi-domain]  Cd Length: 457  Bit Score: 62.17  E-value: 2.79e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539062979 377 QTVMLVEDDEVLREIIIEVLEDLDYHVLSTGNGQHALELIvtAAKPVDLLLTDIGLPGINGRDLAAHVLDRFPKLKIMFI 456
Cdd:PRK11361    5 NRILIVDDEDNVRRMLSTAFALQGFETHCANNGRTALHLF--ADIHPDVVLMDIRMPEMDGIKALKEMRSHETRTPVILM 82
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1539062979 457 TGYDKTVTLPKSLFRHDVEVMTKPFTISELASRVQRLLE 495
Cdd:PRK11361   83 TAYAEVETAVEALRCGAFDYVIKPFDLDELNLIVQRALQ 121
REC_HupR-like cd17569
phosphoacceptor receiver (REC) domain of hydrogen uptake protein regulator (HupR) and similar ...
378-459 4.30e-10

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: 57.03  E-value: 4.30e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539062979 378 TVMLVEDDEVLREIIIEVLEDLDYHVLSTGNGQHALELIvtAAKPVDLLLTDIGLPGINGRDLAAHVLDRFPK-LKIMfI 456
Cdd:cd17569     2 TILLVDDEPNILKALKRLLRREGYEVLTATSGEEALEIL--KQEPVDVVISDQRMPGMDGAELLKRVRERYPDtVRIL-L 78

                  ...
gi 1539062979 457 TGY 459
Cdd:cd17569    79 TGY 81
REC_OmpR_BsPhoP-like cd19937
phosphoacceptor receiver (REC) domain of BsPhoP-like OmpR family response regulators; Bacillus ...
380-494 5.80e-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: 56.90  E-value: 5.80e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539062979 380 MLVEDDEVLREIIIEVLEDLDYHVLSTGNGQHALELIvtAAKPVDLLLTDIGLPGINGRDLAaHVLDRFPKLK---IMFI 456
Cdd:cd19937     1 LVVDDEEDIVELLKYNLEKEGYEVVTAYDGEEALKRA--KDEKPDLIILDLMLPGIDGLEVC-RILRSDPKTSsipIIML 77
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1539062979 457 TG----YDKTVTLpkSLFRHDVevMTKPFTISELASRVQRLL 494
Cdd:cd19937    78 TAkgeeFDKVLGL--ELGADDY--ITKPFSPRELLARVKAVL 115
PAS_4 pfam08448
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
11-119 8.98e-10

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


Pssm-ID: 312075 [Multi-domain]  Cd Length: 110  Bit Score: 55.88  E-value: 8.98e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539062979  11 LEALPIPVIVKDLNHRIVFVNQAASGYFQDPIDTLVGKTDYDCFPAEHAATYWQMEEKVISTQCPCENEEtIIGPEGKPQ 90
Cdd:pfam08448   1 LDSLPDALAVLDPDGRVRYANAAAAELFGLPPEELLGKTLAELLPPEDAARLERALRRALEGEEPIDFLE-ELLLNGEER 79
                          90       100       110
                  ....*....|....*....|....*....|.
gi 1539062979  91 IIITTKTLVTVAN--ESLLVAYFINVTAQRQ 119
Cdd:pfam08448  80 HYELRLTPLRDPDgeVIGVLVISRDITERRR 110
REC_NtrC cd19919
phosphoacceptor receiver (REC) domain of DNA-binding transcriptional regulator NtrC; ...
377-492 9.52e-10

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: 56.13  E-value: 9.52e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539062979 377 QTVMLVEDDEVLREIIIEVLEDLDYHVLSTGNGQHALELIVTAaKPvDLLLTDIGLPGINGRDLAAHVLDRFPKLKIMFI 456
Cdd:cd19919     1 KTVWIVDDDSSIRWVLERALAGAGLTVTSFENAQEALAALASS-QP-DVLISDIRMPGMDGLALLAQIKQRHPDLPVIIM 78
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1539062979 457 TGYDKTVTLPKSLFRHDVEVMTKPFTISELASRVQR 492
Cdd:cd19919    79 TAHSDLDSAVSAYQGGAFEYLPKPFDIDEAVALVER 114
PRK11083 PRK11083
DNA-binding response regulator CreB; Provisional
376-494 1.59e-09

DNA-binding response regulator CreB; Provisional


Pssm-ID: 236838 [Multi-domain]  Cd Length: 228  Bit Score: 58.05  E-value: 1.59e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539062979 376 QQTVMLVEDDEVLREIIIEVLEDLDYHVLSTGNGQHALELIvtAAKPVDLLLTDIGLPGINGRDLAAHVLDRFPKLKIMF 455
Cdd:PRK11083    3 QPTILLVEDEQAIADTLVYALQSEGFTVEWFERGLPALDKL--RQQPPDLVILDVGLPDISGFELCRQLLAFHPALPVIF 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1539062979 456 ITGydktvtlpkslfRHDvEV-------------MTKPFTISELASRVQRLL 494
Cdd:PRK11083   81 LTA------------RSD-EVdrlvgleigaddyVAKPFSPREVAARVRTIL 119
FixJ COG4566
DNA-binding response regulator, FixJ family, consists of REC and HTH domains [Signal ...
378-497 1.99e-09

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


Pssm-ID: 443623 [Multi-domain]  Cd Length: 196  Bit Score: 57.03  E-value: 1.99e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539062979 378 TVMLVEDDEVLREIIIEVLEDLDYHVLSTGNGQHALElivtAAKP--VDLLLTDIGLPGINGRDLAAHVLDRFPKLKIMF 455
Cdd:COG4566     1 TVYIVDDDEAVRDSLAFLLESAGLRVETFASAEAFLA----ALDPdrPGCLLLDVRMPGMSGLELQEELAARGSPLPVIF 76
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1539062979 456 ITGYDkTVTLPKSLFRHD-VEVMTKPFTISELASRVQRLLEQD 497
Cdd:COG4566    77 LTGHG-DVPMAVRAMKAGaVDFLEKPFDDQALLDAVRRALARD 118
PRK10604 PRK10604
sensor protein RstB; Provisional
135-356 2.24e-09

sensor protein RstB; Provisional


Pssm-ID: 236724 [Multi-domain]  Cd Length: 433  Bit Score: 59.23  E-value: 2.24e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539062979 135 QLTGGIAHDFNNHLggiigslgimqkriakgtcVGLeRY----TDNAMASAQRA--------ASLTHRLLAFSR--RQ-- 198
Cdd:PRK10604  214 QLIDGIAHELRTPL-------------------VRL-RYrlemSDNLSAAESQAlnrdigqlEALIEELLTYARldRPqn 273
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539062979 199 SLNPKPLKL----NDLFDEFQSfinqsLGPEYRFEVH--YEGDLWTTfcDHHQLENAVLNLAINA-RDAmpnggiiicqi 271
Cdd:PRK10604  274 ELHLSEPDLpawlSTHLADIQA-----VTPEKTVRLDtpHQGDYGAL--DMRLMERVLDNLLNNAlRYA----------- 335
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539062979 272 TNSASVPGLFEGECVCISIVDTGTGIAPEIMDRVIEPFFTTKPIGE----GTGLGLSMVYGFVKQSNGHFTIESTQAKGT 347
Cdd:PRK10604  336 HSRVRVSLLLDGNQACLIVEDDGPGIPPEERERVFEPFVRLDPSRDratgGCGLGLAIVHSIALAMGGSVNCDESELGGA 415

                  ....*....
gi 1539062979 348 TVSLYLPRY 356
Cdd:PRK10604  416 RFSFSWPVW 424
REC_Ycf29 cd19927
phosphoacceptor receiver (REC) domain of probable transcriptional regulator Ycf29; Ycf29 is a ...
379-457 3.13e-09

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


Pssm-ID: 381154 [Multi-domain]  Cd Length: 102  Bit Score: 54.31  E-value: 3.13e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539062979 379 VMLVEDDEVLREIIIEVLEDLDYHVLSTGNGQHALELIVTaaKPVDLLLTDIGLPGINGRDLAAHV--LDRFPKLKIMFI 456
Cdd:cd19927     1 ILLVDDDPGIRLAVKDYLEDQGFTVIAASNGLEALDLLNQ--YIPDLIISDIIMPGVDGYSLLGKLrkNADFDTIPVIFL 78

                  .
gi 1539062979 457 T 457
Cdd:cd19927    79 T 79
COG4567 COG4567
DNA-binding response regulator, ActR/RegA family, consists of REC and Fis-type HTH domains ...
376-459 3.22e-09

DNA-binding response regulator, ActR/RegA family, consists of REC and Fis-type HTH domains [Signal transduction mechanisms, Transcription];


Pssm-ID: 443624 [Multi-domain]  Cd Length: 177  Bit Score: 56.08  E-value: 3.22e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539062979 376 QQTVMLVEDDEVLREIIIEVLEDLDYHVLSTGNGQHALELIVTAakPVDLLLTDIGLPGINGRDLAAHVLDRFPKLKIMF 455
Cdd:COG4567     4 DRSLLLVDDDEAFARVLARALERRGFEVTTAASVEEALALLEQA--PPDYAVLDLRLGDGSGLDLIEALRERDPDARIVV 81

                  ....
gi 1539062979 456 ITGY 459
Cdd:COG4567    82 LTGY 85
PRK11086 PRK11086
sensory histidine kinase DcuS; Provisional
244-354 3.59e-09

sensory histidine kinase DcuS; Provisional


Pssm-ID: 236839 [Multi-domain]  Cd Length: 542  Bit Score: 59.16  E-value: 3.59e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539062979 244 HQLENAVLNLAINARDAM---PNGGIiicqitnsaSVPGLFEGECVCISIVDTGTGIAPEIMDRVIEPFFTTKpiGEGTG 320
Cdd:PRK11086  432 HELITILGNLIENALEAVggeEGGEI---------SVSLHYRNGWLHCEVSDDGPGIAPDEIDAIFDKGYSTK--GSNRG 500
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1539062979 321 LGLSmvygFVKQS----NGHFTIESTQAKGTTVSLYLP 354
Cdd:PRK11086  501 VGLY----LVKQSvenlGGSIAVESEPGVGTQFFVQIP 534
REC_CheV-like cd19924
phosphoacceptor receiver (REC) domain of chemotaxis protein CheV and similar proteins; This ...
379-457 5.22e-09

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: 53.92  E-value: 5.22e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539062979 379 VMLVEDDEVLREIIIEVLEDLDYHVLSTGNGQHALELIVTAA-------KPVDLLLTDIGLPGINGRDLAAHVLD--RFP 449
Cdd:cd19924     1 ILVVDDSPTARKQLRDLLKNLGFEIAEAVDGEEALNKLENLAkegndlsKELDLIITDIEMPKMDGYELTFELRDdpRLA 80

                  ....*...
gi 1539062979 450 KLKIMFIT 457
Cdd:cd19924    81 NIPVILNS 88
REC_LytTR_AlgR-like cd17532
phosphoacceptor receiver (REC) domain of LytTR/AlgR family response regulators similar to AlgR; ...
379-496 8.32e-09

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: 53.31  E-value: 8.32e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539062979 379 VMLVEDDEVLREIIIEVLEDLDYHVL--STGNGQHALELIVTAAkpVDLLLTDIGLPGINGRDLAAhVLDRFPKL-KIMF 455
Cdd:cd17532     1 ALIVDDEPLAREELRYLLEEHPDIEIvgEAENGEEALEAIEELK--PDVVFLDIQMPGLDGLELAK-KLSKLAKPpLIVF 77
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1539062979 456 ITGYD----KTVTLpkslfrHDVEVMTKPFTISELASRVQRLLEQ 496
Cdd:cd17532    78 VTAYDeyavEAFEL------NAVDYLLKPFSEERLAEALAKLRKR 116
HATPase_BasS-like cd16940
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
246-353 9.16e-09

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: 53.18  E-value: 9.16e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539062979 246 LENAVLNLAINARDAMPNGGIIicQITNSASVPGLfegecvcISIVDTGTGIAPEIMDRVIEPFFTTKPI-GEGTGLGLS 324
Cdd:cd16940    14 LFLLLRNLVDNAVRYSPQGSRV--EIKLSADDGAV-------IRVEDNGPGIDEEELEALFERFYRSDGQnYGGSGLGLS 84
                          90       100
                  ....*....|....*....|....*....
gi 1539062979 325 MVYGFVKQSNGHFTIESTQAKGTTVSLYL 353
Cdd:cd16940    85 IVKRIVELHGGQIFLGNAQGGGLEAWVRL 113
REC_Spo0F-like cd17553
phosphoacceptor receiver (REC) domain of Spo0F and similar domains; Spo0F, a stand-alone ...
379-494 1.05e-08

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: 53.33  E-value: 1.05e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539062979 379 VMLVEDDEVLREIIIEVLEDLDYHVLSTGNGQHALElIVTAAKPvDLLLTDIGLPGINGRDLAAHVLDRFPKLKIMFITG 458
Cdd:cd17553     3 ILIVDDQYGIRILLNEVFNKEGYQTFQAANGLQALD-IVTKERP-DLVLLDMKIPGMDGIEILKRMKVIDENIRVIIMTA 80
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1539062979 459 YDKTVTLPKSLFRHDVEVMTKPFTISELASRVQRLL 494
Cdd:cd17553    81 YGELDMIQESKELGALTHFAKPFDIDEIRDAVKKYL 116
REC_DivK-like cd17548
phosphoacceptor receiver (REC) domain of DivK and similar proteins; Caulobacter crescentus ...
378-437 1.11e-08

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: 52.93  E-value: 1.11e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539062979 378 TVMLVEDDEVLREIIIEVLEDLDYHVLSTGNGQHALElIVTAAKPvDLLLTDIGLPGING 437
Cdd:cd17548     1 KILIVEDNPLNMKLARDLLESAGYEVLEAADGEEALE-IARKEKP-DLILMDIQLPGMDG 58
REC_2_GGDEF cd17544
second phosphoacceptor receiver (REC) domain of uncharacterized GGDEF domain proteins; This ...
379-496 1.39e-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: 52.91  E-value: 1.39e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539062979 379 VMLVEDDEVLREIIIEVLEDLDYHVLSTGNGQHALELIvtAAKP-VDLLLTDIGLPGINGRDLAAHVLDRFPK--LKIMF 455
Cdd:cd17544     3 VLVVDDSATSRNHLRALLRRHNFQVLEAANGQEALEVL--EQHPdIKLVITDYNMPEMDGFELVREIRKKYSRdqLAIIG 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1539062979 456 ITGYDKTVTLPKSL------FrhdvevMTKPFTISELASRVQRLLEQ 496
Cdd:cd17544    81 ISASGDNALSARFIkagandF------LTKPFLPEEFYCRVTQNLET 121
REC_OmpR_NsrR-like cd18159
phosphoacceptor receiver (REC) domain of Streptococcus agalactiae NsrR-like OmpR family ...
379-494 1.53e-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: 52.67  E-value: 1.53e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539062979 379 VMLVEDDEVLREIIIEVLEDLDYHVLSTGNGQHALELIVtAAKPvDLLLTDIGLPGING----RDLAAHVldrfpKLKIM 454
Cdd:cd18159     1 ILIVEDDETIASLLKKHLEKWGYEVVLIEDFEDVLEEFL-QFKP-DLVLLDINLPYFDGfywcREIRQIS-----NVPII 73
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1539062979 455 FITGYDKTVTLPKSLFRHDVEVMTKPFTISELASRVQRLL 494
Cdd:cd18159    74 FISSRDDNMDQVMAINMGGDDYITKPFDLDVLLAKIKAIL 113
REC_OmpR_BaeR-like cd19938
phosphoacceptor receiver (REC) domain of BaeR-like OmpR family response regulators; BaeR is ...
378-494 1.90e-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: 1.90e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539062979 378 TVMLVEDDEVLREIIIEVLEDLDYHVLSTGNGQHALELIvtAAKPVDLLLTDIGLPGINGRDLAAHvLDRFPKLKIMFIT 457
Cdd:cd19938     1 RILIVEDEPKLAQLLIDYLRAAGYAPTLLAHGDQVLPYV--RHTPPDLILLDLMLPGTDGLTLCRE-IRRFSDVPIIMVT 77
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1539062979 458 GYDKTVTLPKSLFRHDVEVMTKPFTISELASRVQRLL 494
Cdd:cd19938    78 ARVEEIDRLLGLELGADDYICKPYSPREVVARVKAIL 114
HATPase_CreC-like cd16945
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
246-343 2.54e-08

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: 51.69  E-value: 2.54e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539062979 246 LENAVLNLAINARDAMPNGGIIICQITnsasvpglFEGECVCISIVDTGTGIAPEIMDRVIEPFFTTKPIGEG---TGLG 322
Cdd:cd16945     5 LRQAINNLLDNAIDFSPEGGLIALQLE--------ADTEGIELLVFDEGSGIPDYALNRVFERFYSLPRPHSGqksTGLG 76
                          90       100
                  ....*....|....*....|.
gi 1539062979 323 LSMVYGFVKQSNGHFTIESTQ 343
Cdd:cd16945    77 LAFVQEVAQLHGGRITLRNRP 97
HATPase_EnvZ-like cd16950
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
246-354 2.63e-08

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: 51.68  E-value: 2.63e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539062979 246 LENAVLNLAINARDampNGGIIIcqitnsaSVPGLFEGECVCISIVDTGTGIAPEIMDRVIEPFFTTKPI--GEGTGLGL 323
Cdd:cd16950     1 LKRVLSNLVDNALR---YGGGWV-------EVSSDGEGNRTRIQVLDNGPGIAPEEVDELFQPFYRGDNArgTSGTGLGL 70
                          90       100       110
                  ....*....|....*....|....*....|.
gi 1539062979 324 SMVYGFVKQSNGHFTIESTQAKGTTVSLYLP 354
Cdd:cd16950    71 AIVQRISDAHGGSLTLANRAGGGLCARIELP 101
REC_NtrC1-like cd17572
phosphoacceptor receiver (REC) domain of nitrogen regulatory protein C 1 (NtrC1) from Aquifex ...
379-496 2.71e-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: 52.20  E-value: 2.71e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539062979 379 VMLVEDDEVLREIIIEVLEDLDYHVLSTGNGQHALELIvtAAKPVDLLLTDIGLPGINGRDLAAHVLDRFPKLKIMFITG 458
Cdd:cd17572     1 VLLVEDSPSLAALYQEYLSDEGYKVTHVETGKEALAFL--SDQPPDVVLLDLKLPDMSGMEILKWIQERSLPTSVIVITA 78
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1539062979 459 YDkTVTLPKSLFR---HDveVMTKPFTISELASRVQRLLEQ 496
Cdd:cd17572    79 HG-SVDIAVEAMRlgaYD--FLEKPFDADRLRVTVRNALKH 116
CitB COG2197
DNA-binding response regulator, NarL/FixJ family, contains REC and HTH domains [Signal ...
378-445 3.07e-08

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: 52.20  E-value: 3.07e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539062979 378 TVMLVEDDEVLREIIIEVLEDL-DYHVLST-GNGQHALELIvtAAKPVDLLLTDIGLPGINGRDLAAHVL 445
Cdd:COG2197     3 RVLIVDDHPLVREGLRALLEAEpDIEVVGEaADGEEALELL--EELRPDVVLLDIRMPGMDGLEALRRLL 70
REC_NtrX-like cd17550
phosphoacceptor receiver (REC) domain of nitrogen assimilation regulatory protein NtrX and ...
380-495 5.25e-08

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: 50.96  E-value: 5.25e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539062979 380 MLVEDDEV-LREIIIEVLEDLDYHVLSTGNGQHALELIvtAAKPVDLLLTDIGLPGINGRDLAAHVLDRFPKLKIMFITG 458
Cdd:cd17550     1 ILIVDDEEdIRESLSGILEDEGYEVDTAADGEEALKLI--KERRPDLVLLDIWLPDMDGLELLKEIKEKYPDLPVIMISG 78
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1539062979 459 YDKTVTLPKSLFRHDVEVMTKPFTISELASRVQRLLE 495
Cdd:cd17550    79 HGTIETAVKATKLGAYDFIEKPLSLDRLLLTIERALE 115
AmiR COG3707
Two-component response regulator, AmiR/NasT family, consists of REC and RNA-binding ...
378-496 5.63e-08

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: 53.04  E-value: 5.63e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539062979 378 TVMLVEDDEVLREIIIEVLEDLDYHVLST-GNGQHALELIVtAAKPvDLLLTDIGLPGINGRDLAAHVLDRFPKLKIMFi 456
Cdd:COG3707     5 RVLVVDDEPLRRADLREGLREAGYEVVAEaADGEDAVELVR-ELKP-DLVIVDIDMPDRDGLEAARQISEERPAPVILL- 81
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1539062979 457 TGYDKTVTLPKSLfrhDVEVM---TKPFTISELASRVQRLLEQ 496
Cdd:COG3707    82 TAYSDPELIERAL---EAGVSaylVKPLDPEDLLPALELALAR 121
HATPase_SpaK_NisK-like cd16975
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
242-351 9.95e-08

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: 50.15  E-value: 9.95e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539062979 242 DHHQLENAVLNLAINARDAMPNGGIIICQITNsasvpglfEGECVCISIVDTGTGIAPEIMDRVIEPFFTTKPI---GEG 318
Cdd:cd16975     1 DTLLLSRALINIISNACQYAPEGGTVSISIYD--------EEEYLYFEIWDNGHGFSEQDLKKALELFYRDDTSrrsGGH 72
                          90       100       110
                  ....*....|....*....|....*....|...
gi 1539062979 319 TGLGLSMVYGFVKQSNGHFTIESTQAKGTTVSL 351
Cdd:cd16975    73 YGMGLYIAKNLVEKHGGSLIIENSQKGGAEVTV 105
HATPase_EcPhoR-like cd16952
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
246-354 1.06e-07

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: 50.28  E-value: 1.06e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539062979 246 LENAVLNLAINARDAMPNGGIIICQITNSASVPGLfegecvciSIVDTGTGIAPEIMDRVIEPFFTTKPIGE----GTGL 321
Cdd:cd16952     1 LRSAFSNLVSNAVKYTPPSDTITVRWSQEESGARL--------SVEDTGPGIPPEHIPRLTERFYRVDIERCrntgGTGL 72
                          90       100       110
                  ....*....|....*....|....*....|...
gi 1539062979 322 GLSMVYGFVKQSNGHFTIESTQAKGTTVSLYLP 354
Cdd:cd16952    73 GLAIVKHVMSRHDARLLIASELGKGSRFTCLFP 105
PAS COG2202
PAS domain [Signal transduction mechanisms];
9-124 1.23e-07

PAS domain [Signal transduction mechanisms];


Pssm-ID: 441804 [Multi-domain]  Cd Length: 258  Bit Score: 52.72  E-value: 1.23e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539062979   9 AVLEALPIPVIVKDLNHRIVFVNQAASGYFQDPIDTLVGKTDYDCFPAEHAATYWQMEEKVISTQC-PCENEETIIGPEG 87
Cdd:COG2202   141 LLVENAPDGIFVLDLDGRILYVNPAAEELLGYSPEELLGKSLLDLLHPEDRERLLELLRRLLEGGReSYELELRLKDGDG 220
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1539062979  88 KPQII-ITTKTLVTVANESLLVAYFINVTAQRQFEEQL 124
Cdd:COG2202   221 RWVWVeASAVPLRDGGEVIGVLGIVRDITERKRAEEAL 258
REC_OmpR_BfmR-like cd19939
phosphoacceptor receiver (REC) domain of BfmR-like OmpR family response regulators; ...
379-494 1.29e-07

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: 50.06  E-value: 1.29e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539062979 379 VMLVEDDEVLREIIIEVLEDLDYHVLSTGNGQHALELIVTaaKPVDLLLTDIGLPGINGRDLAAHVLDRFpKLKIMFITG 458
Cdd:cd19939     2 ILIVEDELELARLTRDYLIKAGLEVSVFTDGQRAVRRIID--EQPSLVVLDIMLPGMDGLTVCREVREHS-HVPILMLTA 78
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1539062979 459 YDKTVTLPKSLFRHDVEVMTKPFTISELASRVQRLL 494
Cdd:cd19939    79 RTEEMDRVLGLEMGADDYLCKPFSPRELLARVRALL 114
REC_OmpR_MtPhoP-like cd17615
phosphoacceptor receiver (REC) domain of MtPhoP-like OmpR family response regulators; ...
378-494 1.74e-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: 49.66  E-value: 1.74e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539062979 378 TVMLVEDDEVLREIIIEVLEDLDYHVLSTGNGQHALelivTAAKPV--DLLLTDIGLPGINGRDLAAHVLDRFPKLKIMF 455
Cdd:cd17615     1 RVLVVDDEPNITELLSMALRYEGWDVETAADGAEAL----AAAREFrpDAVVLDIMLPDMDGLEVLRRLRADGPDVPVLF 76
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1539062979 456 ITGYDKTVTLPKSLFRHDVEVMTKPFTISELASRVQRLL 494
Cdd:cd17615    77 LTAKDSVEDRIAGLTAGGDDYVTKPFSLEEVVARLRALL 115
PRK11173 PRK11173
two-component response regulator; Provisional
377-494 1.88e-07

two-component response regulator; Provisional


Pssm-ID: 183013 [Multi-domain]  Cd Length: 237  Bit Score: 51.94  E-value: 1.88e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539062979 377 QT--VMLVEDDEVLREIIIEVLEDLDYHVLSTGNG---QHALelivtAAKPVDLLLTDIGLPGINGRDLAAHVLDRfPKL 451
Cdd:PRK11173    2 QTphILIVEDELVTRNTLKSIFEAEGYDVFEATDGaemHQIL-----SENDINLVIMDINLPGKNGLLLARELREQ-ANV 75
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1539062979 452 KIMFITGYDKTVTlpKSLfrhDVEV-----MTKPFTISELASRVQRLL 494
Cdd:PRK11173   76 ALMFLTGRDNEVD--KIL---GLEIgaddyITKPFNPRELTIRARNLL 118
PRK10766 PRK10766
two-component system response regulator TorR;
378-494 1.95e-07

two-component system response regulator TorR;


Pssm-ID: 182711 [Multi-domain]  Cd Length: 221  Bit Score: 51.96  E-value: 1.95e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539062979 378 TVMLVEDDEVLREIIIEVLEDLDYHVLSTGNGQHALELIvtAAKPVDLLLTDIGLPGINGRDLAAHVLDRfPKLKIMFIT 457
Cdd:PRK10766    4 HILVVEDEPVTRARLQGYFEQEGYTVSEAASGAGMREIM--QNQHVDLILLDINLPGEDGLMLTRELRSR-STVGIILVT 80
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1539062979 458 GYDKTVTLPKSLFRHDVEVMTKPFTISELASRVQRLL 494
Cdd:PRK10766   81 GRTDSIDRIVGLEMGADDYVTKPLELRELLVRVKNLL 117
REC_Rcp-like cd17557
phosphoacceptor receiver (REC) domain of cyanobacterial phytochrome response regulator Rcp and ...
378-495 2.15e-07

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: 49.72  E-value: 2.15e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539062979 378 TVMLVEDDEVLREIIIEVLED--LDYHVLSTGNGQHALELI------VTAAKPvDLLLTDIGLPGINGRDlaahVLDRF- 448
Cdd:cd17557     1 TILLVEDNPGDAELIQEAFKEagVPNELHVVRDGEEALDFLrgegeyADAPRP-DLILLDLNMPRMDGFE----VLREIk 75
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1539062979 449 --PKLK----IMFITGYDKTvtlpkslfrhDVEV---------MTKPFTISELASRVQRLLE 495
Cdd:cd17557    76 adPDLRripvVVLTTSDAEE----------DIERayelgansyIVKPVDFEEFVEAIRSLGE 127
REC_OmpR_EcPhoP-like cd19934
phosphoacceptor receiver (REC) domain of EcPhoP-like OmpR family response regulators; ...
379-494 2.44e-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: 49.20  E-value: 2.44e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539062979 379 VMLVEDDEVLREIIIEVLEDLDYHVLSTGNGQHALELIVTaaKPVDLLLTDIGLPGINGRDLAAHVLDRFPKLKIMFITG 458
Cdd:cd19934     1 LLLVEDDALLAAQLKEQLSDAGYVVDVAEDGEEALFQGEE--EPYDLVVLDLGLPGMDGLSVLRRWRSEGRATPVLILTA 78
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1539062979 459 YDKtvtlpkslFRHDVEVM--------TKPFTISELASRVQRLL 494
Cdd:cd19934    79 RDS--------WQDKVEGLdagaddylTKPFHIEELLARLRALI 114
HATPase_BceS-YxdK-YvcQ-like cd16948
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
283-354 2.59e-07

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: 48.82  E-value: 2.59e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1539062979 283 GECVCISIVDTGTGIAPEIMDRVIEPFFTTK---PIGEGTGLGLSMVYGFVKQSNGHFTIESTQAKGTTVSLYLP 354
Cdd:cd16948    35 EQGVVLSIKDFGIGIPEEDLPRVFDKGFTGEngrNFQESTGMGLYLVKKLCDKLGHKIDVESEVGEGTTFTITFP 109
REC_OmpR_KdpE-like cd17620
phosphoacceptor receiver (REC) domain of KdpE-like OmpR family response regulators; KdpE is a ...
379-440 2.78e-07

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: 48.70  E-value: 2.78e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1539062979 379 VMLVEDDEVLREIIIEVLEDLDYHVLSTGNGQHALELIVTaAKPvDLLLTDIGLPGINGRDL 440
Cdd:cd17620     1 ILVIEDEPQIRRFLRTALEAHGYRVFEAETGQEGLLEAAT-RKP-DLIILDLGLPDMDGLEV 60
HATPase_VanS-like cd16923
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
252-354 3.43e-07

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: 48.54  E-value: 3.43e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539062979 252 NLAINA-RDAMPNGGIIIcqitnsasvPGLFEGECVCISIVDTGTGIAPEIMDRVIEPFF--TTKPIGEGTGLGLSMVYG 328
Cdd:cd16923     7 NLLSNAiKYSPENTRIYI---------TSFLTDDVVNIMFKNPSSHPLDFKLEKLFERFYrgDNSRNTEGAGLGLSIAKA 77
                          90       100
                  ....*....|....*....|....*.
gi 1539062979 329 FVKQSNGHFTIEStQAKGTTVSLYLP 354
Cdd:cd16923    78 IIELHGGSASAEY-DDNHDLFKVRLP 102
YesM COG2972
Sensor histidine kinase YesM [Signal transduction mechanisms];
246-355 4.41e-07

Sensor histidine kinase YesM [Signal transduction mechanisms];


Pssm-ID: 442211 [Multi-domain]  Cd Length: 445  Bit Score: 52.33  E-value: 4.41e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539062979 246 LENAVlnlaINARDAMPNGGIIICQITNsasvpglfEGECVCISIVDTGTGIAPEIMDRVIEPFFTTkpiGEGTGLGLSM 325
Cdd:COG2972   345 VENAI----EHGIEPKEGGGTIRISIRK--------EGDRLVITVEDNGVGMPEEKLEKLLEELSSK---GEGRGIGLRN 409
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1539062979 326 V-------YGfvkqSNGHFTIESTQAKGTTVSLYLPR 355
Cdd:COG2972   410 VrerlklyYG----EEYGLEIESEPGEGTTVTIRIPL 442
REC_RR468-like cd17552
phosphoacceptor receiver (REC) domain of Thermotoga maritima response regulator RR468 and ...
377-494 5.12e-07

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: 48.32  E-value: 5.12e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539062979 377 QTVMLVEDDEVLREIIIEVLEDL-DYHVLSTGNGQHALELIVTAaKPvDLLLTDIGLPGINGRDLAAHvLDRFPKLK--- 452
Cdd:cd17552     2 KRILVIDDEEDIREVVQACLEKLaGWEVLTASSGQEGLEKAATE-QP-DAILLDVMMPDMDGLATLKK-LQANPETQsip 78
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1539062979 453 IMFITGydKTVTLPKSLFRH-DVE-VMTKPFTISELASRVQRLL 494
Cdd:cd17552    79 VILLTA--KAQPSDRQRFASlGVAgVIAKPFDPLTLAEQIAKLL 120
HATPase_FilI-like cd16921
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
288-354 7.22e-07

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: 47.71  E-value: 7.22e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1539062979 288 ISIVDTGTGIAPEIMDRVIEPF--FTTKPIGEGTGLGLSMVYGFVKQSNGHFTIESTQAKGTTVSLYLP 354
Cdd:cd16921    37 FYVRDNGIGIDPEYAEKVFGIFqrLHSREEYEGTGVGLAIVRKIIERHGGRIWLESEPGEGTTFYFTLP 105
REC_RpfG-like cd17551
phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase response regulator ...
378-493 7.40e-07

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: 47.82  E-value: 7.40e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539062979 378 TVMLVEDDEVLREIIIEVLEDLDY-HVLSTGNGQHALELIvtAAKPVDLLLTDIGLPGINGRDlaahVLDRFPKLK---- 452
Cdd:cd17551     2 RILIVDDNPTNLLLLEALLRSAGYlEVVSFTDPREALAWC--RENPPDLILLDYMMPGMDGLE----FIRRLRALPgled 75
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1539062979 453 --IMFITGYDKTVTLPKSLFRHDVEVMTKPFTISELASRVQRL 493
Cdd:cd17551    76 vpIVMITADTDREVRLRALEAGATDFLTKPFDPVELLARVRNL 118
HATPase_SpoIIAB-like cd16942
Histidine kinase-like ATPase domain of SpoIIAB, an anti sigma-F factor and serine-protein ...
249-351 1.07e-06

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


Pssm-ID: 340418 [Multi-domain]  Cd Length: 135  Bit Score: 47.92  E-value: 1.07e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539062979 249 AVLNLAINARDAMPNGGIIIcqitnSASVpglfEGECVCISIVDTGTGIapEIMDRVIEPFFTTKPIGEGTGLGLSMVYG 328
Cdd:cd16942    46 AVTNAIIHGYNNDPNGIVSI-----SVII----EDGVVHLTVRDEGVGI--PDIEEARQPLFTTKPELERSGMGFTIMEN 114
                          90       100
                  ....*....|....*....|...
gi 1539062979 329 FVKQsnghFTIESTQAKGTTVSL 351
Cdd:cd16942   115 FMDE----VIVESEVNKGTTVYL 133
REC_OmpR_kpRstA-like cd17622
phosphoacceptor receiver (REC) domain of kpRstA-like OmpR family response regulators; ...
379-455 1.22e-06

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: 47.37  E-value: 1.22e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1539062979 379 VMLVEDDEVLREIIIEVLEDLDYHVLSTGNGQHALELIVTaAKPvDLLLTDIGLPGINGRDLAAHVLDRFPKLKIMF 455
Cdd:cd17622     3 ILLVEDDPKLARLIADFLESHGFNVVVEHRGDRALEVIAR-EKP-DAVLLDIMLPGIDGLTLCRDLRPKYQGPILLL 77
REC_DesR-like cd19930
phosphoacceptor receiver (REC) domain of DesR and similar proteins; This group is composed of ...
379-495 1.55e-06

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


Pssm-ID: 381157 [Multi-domain]  Cd Length: 117  Bit Score: 46.88  E-value: 1.55e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539062979 379 VMLVEDDEVLREIIIEVLE---DLDYhVLSTGNGQHALELIVTAAkpVDLLLTDIGLPGINGRDLAAHVLDRFPKLKIMF 455
Cdd:cd19930     1 VLIAEDQEMVRGALAALLEledDLEV-VAQASNGQEALRLVLKHS--PDVAILDIEMPGRTGLEVAAELREELPDTKVLI 77
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1539062979 456 ITGYDKTVTLPKSLFRHDVEVMTKPFTISELASRVQRLLE 495
Cdd:cd19930    78 VTTFGRPGYFRRALAAGVDGYVLKDRPIEELADAIRTVHA 117
COG3920 COG3920
Two-component sensor histidine kinase, HisKA and HATPase domains [Signal transduction ...
112-354 1.60e-06

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


Pssm-ID: 443125 [Multi-domain]  Cd Length: 495  Bit Score: 50.67  E-value: 1.60e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539062979 112 INVTAQRQFEEQLRQAQKMEAVgqLTGGIAHDFNNHLGgIIGSLGIMQKRIAKGTCVglerytDNAMASAQ---RAASLT 188
Cdd:COG3920   276 LVITERKRAEEELEASLEEKEL--LLRELHHRVKNNLQ-VVSSLLRLQARRADDPEA------REALEESQnriQALALV 346
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539062979 189 HRLLAfsrrQSLNPKPLKLNDLFDEFQSFINQSLGPEyRFEVHYEGDlwttfcdhhqlenavlNLAINARDAMPnGGIII 268
Cdd:COG3920   347 HELLY----QSEDWEGVDLRDYLRELLEPLRDSYGGR-GIRIELDGP----------------DVELPADAAVP-LGLIL 404
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539062979 269 CQ-ITNSA-----SVPG-------LFEGECVCISIVDTGTGIAPEImdrviepffttkPIGEGTGLGLSMVYGFVKQSNG 335
Cdd:COG3920   405 NElVTNALkhaflSGEGgrirvswRREDGRLRLTVSDNGVGLPEDV------------DPPARKGLGLRLIRALVRQLGG 472
                         250
                  ....*....|....*....
gi 1539062979 336 HFTIEStqAKGTTVSLYLP 354
Cdd:COG3920   473 TLELDR--PEGTRVRITFP 489
HATPase_RstB-like cd16939
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
246-355 1.69e-06

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: 46.65  E-value: 1.69e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539062979 246 LENAVLNLAINA-RDAmpnggiiicqiTNSASVPGLFEGECVCISIVDTGTGIAPEIMDRVIEPFFTTKPIGE----GTG 320
Cdd:cd16939     1 MARALDNLLRNAlRYA-----------HRTVRIALLVSGGRLTLIVEDDGPGIPAAARERVFEPFVRLDPSRDratgGFG 69
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1539062979 321 LGLSMVYGFVKQSNGHFTIESTQAKGTTVSLYLPR 355
Cdd:cd16939    70 LGLAIVHRVALWHGGHVECDDSELGGACFRLTWPR 104
HATPase_YpdA-YehU-LytS-like cd16924
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
265-354 1.75e-06

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


Pssm-ID: 340401 [Multi-domain]  Cd Length: 103  Bit Score: 46.67  E-value: 1.75e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539062979 265 GIIICQITNSASVPGLFEGECVCISIVDTGTGIAPEIMDRViepfftTKPIGEGTGLGLSMVYGFVKQSNG---HFTIES 341
Cdd:cd16924    17 GLSPLTDKGVVTISALKEDNHVMIEVEDNGRGIDPKVLNIL------GKKPKEGNGIGLYNVHQRLILLFGedyGIHIAS 90
                          90
                  ....*....|...
gi 1539062979 342 TQAKGTTVSLYLP 354
Cdd:cd16924    91 EPDKGTRITFTIP 103
HisKA cd00082
Histidine Kinase A (dimerization/phosphoacceptor) domain; Histidine Kinase A dimers are formed ...
130-196 1.77e-06

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: 45.28  E-value: 1.77e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1539062979 130 MEAVGQLTGGIAHDFNNHLGGIIGSLGIMQKRIAKGTcvGLERYTDNAMASAQRAASLTHRLLAFSR 196
Cdd:cd00082     1 LQAKGEFLANVSHELRTPLTAIRGALELLEEELLDDE--EQREYLERIREEAERLLRLINDLLDLSR 65
dpiB PRK15053
sensor histidine kinase DpiB; Provisional
282-355 1.97e-06

sensor histidine kinase DpiB; Provisional


Pssm-ID: 185013 [Multi-domain]  Cd Length: 545  Bit Score: 50.22  E-value: 1.97e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1539062979 282 EGECVCISIVDTGTGIAPEIMDRVIEPFFTTKPIGEGT-GLGLSMVYGFVKQSNGHFTIESTQAKGTTVSLYLPR 355
Cdd:PRK15053  465 EGDDVVIEVADQGCGVPESLRDKIFEQGVSTRADEPGEhGIGLYLIASYVTRCGGVITLEDNDPCGTLFSIFIPK 539
PAS pfam00989
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
9-100 2.09e-06

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: 46.64  E-value: 2.09e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539062979   9 AVLEALPIPVIVKDLNHRIVFVNQAASGYFQDPIDTLVGKTDYDCFPAE-HAATYWQMEEKVISTQCPCENEETIIGPEG 87
Cdd:pfam00989   5 AILESLPDGIFVVDEDGRILYVNAAAEELLGLSREEVIGKSLLDLIPEEdDAEVAELLRQALLQGEESRGFEVSFRVPDG 84
                          90
                  ....*....|...
gi 1539062979  88 KPQIIITTKTLVT 100
Cdd:pfam00989  85 RPRHVEVRASPVR 97
PAS cd00130
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
14-100 2.14e-06

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: 46.09  E-value: 2.14e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539062979  14 LPIPVIVKDLNHRIVFVNQAASGYFQDPIDTLVGKTDYDCFPAEHAATYWQMEEKVISTQCPCENEETIIGPEGKPQIII 93
Cdd:cd00130     1 LPDGVIVLDLDGRILYANPAAEQLLGYSPEELIGKSLLDLIHPEDREELRERLENLLSGGEPVTLEVRLRRKDGSVIWVL 80

                  ....*..
gi 1539062979  94 TTKTLVT 100
Cdd:cd00130    81 VSLTPIR 87
psREC_PRR cd17582
pseudo receiver domain of pseudo-response regulators; In Arabidopsis, five pseudo-response ...
379-480 2.18e-06

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


Pssm-ID: 381120 [Multi-domain]  Cd Length: 104  Bit Score: 46.24  E-value: 2.18e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539062979 379 VMLVEDDEVLREIIIEVLEDLDYHVLSTGNGQHALELIVTAAKPVDLLLTDIGLPGINGRDLAAHV-----LDRFPklkI 453
Cdd:cd17582     1 VLLVENDDSTRQIVTALLRKCSYEVTAASDGLQAWDVLEDEQNEIDLILTEVDLPVSSGFKLLSYImrhkiCKNIP---V 77
                          90       100
                  ....*....|....*....|....*..
gi 1539062979 454 MFITGYDKTVTLPKSLFRHDVEVMTKP 480
Cdd:cd17582    78 IMMSSQDSVGVVFKCLSKGAADYLVKP 104
RocR COG3829
RocR-type transcriptional regulator, contains PAS, AAA-type ATPase, and DNA-binding Fis ...
9-164 2.28e-06

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: 49.77  E-value: 2.28e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539062979   9 AVLEALPIPVIVKDLNHRIVFVNQAASGYFQDPIDTLVGKTDYDCFPAEHAAtywqmeeKVISTQCPCENEetIIGPEGK 88
Cdd:COG3829    15 AILDSLDDGIIVVDADGRITYVNRAAERILGLPREEVIGKNVTELIPNSPLL-------EVLKTGKPVTGV--IQKTGGK 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539062979  89 PQIIITTKTLVTVANESLL-VAYFINVTAQRQFEEQLRQAQKMEAVGQltggiahdfNNHLGGIIGSLGIMQ------KR 161
Cdd:COG3829    86 GKTVIVTAIPIFEDGEVIGaVETFRDITELKRLERKLREEELERGLSA---------KYTFDDIIGKSPAMKellelaKR 156

                  ...
gi 1539062979 162 IAK 164
Cdd:COG3829   157 VAK 159
cpxA PRK09470
envelope stress sensor histidine kinase CpxA;
181-357 2.29e-06

envelope stress sensor histidine kinase CpxA;


Pssm-ID: 236532 [Multi-domain]  Cd Length: 461  Bit Score: 49.93  E-value: 2.29e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539062979 181 AQRAASLTHRLLAFSRRQ---SLNPKPLKLNDLFDEF---QSFINQSLGPEYRFEVHYEGdlWTTFCDHHQLENAVLNLA 254
Cdd:PRK09470  285 AQRLDSMINDLLVLSRNQqknHLERETFKANSLWSEVledAKFEAEQMGKSLTVSAPPGP--WPINGNPNALASALENIV 362
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539062979 255 inaRDAMPNGGIIIcQITNSASVPGLFegecvcISIVDTGTGIAPEIMDRVIEPFFTTkpiGE-------GTGLGLSMVY 327
Cdd:PRK09470  363 ---RNALRYSHTKI-EVAFSVDKDGLT------ITVDDDGPGVPEEEREQIFRPFYRV---DEardresgGTGLGLAIVE 429
                         170       180       190
                  ....*....|....*....|....*....|
gi 1539062979 328 GFVKQSNGHFTIESTQAKGTTVSLYLPRYI 357
Cdd:PRK09470  430 NAIQQHRGWVKAEDSPLGGLRLTIWLPLYK 459
REC_OmpR_YycF-like cd17614
phosphoacceptor receiver (REC) domain of YrcF-like OmpR family response regulators; YycF ...
379-494 2.32e-06

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


Pssm-ID: 381130 [Multi-domain]  Cd Length: 115  Bit Score: 46.65  E-value: 2.32e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539062979 379 VMLVEDDEVLREIIIEVLEDLDYHVLSTGNGQHALELiVTAAKPvDLLLTDIGLPGINGRDLAAHVLDRFpKLKIMFITG 458
Cdd:cd17614     1 ILVVDDEKPISDILKFNLTKEGYEVVTAYDGREALEK-VEEEQP-DLILLDLMLPEKDGLEVCREVRKTS-NVPIIMLTA 77
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1539062979 459 YDKTVTLPKSLFRHDVEVMTKPFTISELASRVQRLL 494
Cdd:cd17614    78 KDSEVDKVLGLELGADDYVTKPFSNRELLARVKANL 113
REC_OmpR_VirG cd17594
phosphoacceptor receiver (REC) domain of VirG-like OmpR family response regulators; VirG is ...
378-491 2.37e-06

phosphoacceptor receiver (REC) domain of VirG-like OmpR family response regulators; VirG is part of the VirA/VirG two-component system that regulates the expression of virulence (vir) genes. The histidine kinase VirA senses a phenolic wound response signal, undergoes autophosphorylation, and phosphorelays to the VirG response regulator, which induces transcription of the vir regulon. VirG belongs to the OmpR family of DNA-binding response regulators that contain N-terminal receiver (REC) and C-terminal DNA-binding winged helix-turn-helix effector domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381125 [Multi-domain]  Cd Length: 113  Bit Score: 46.29  E-value: 2.37e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539062979 378 TVMLVEDDEVLREIIIEVLEDLDYHVLSTGNGQHALELIVTaaKPVDLLLTDIGLPGINGRDLaAHVLDRFPKLKIMFIT 457
Cdd:cd17594     1 HVLVVDDDAAMRHLLILYLRERGFDVTAAADGAEEARLMLH--RRVDLVLLDLRLGQESGLDL-LRTIRARSDVPIIIIS 77
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1539062979 458 GY-----DKTVTLPKSLfrhdVEVMTKPFTISELASRVQ 491
Cdd:cd17594    78 GDrrdeiDRVVGLELGA----DDYLAKPFGLRELLARVR 112
orf27 CHL00148
Ycf27; Reviewed
372-494 2.38e-06

Ycf27; Reviewed


Pssm-ID: 214376 [Multi-domain]  Cd Length: 240  Bit Score: 48.94  E-value: 2.38e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539062979 372 KEGLQQTVMLVEDDEVLREIIIEVLEDLDYHVLSTGNGQHALELIvTAAKPvDLLLTDIGLPGINGRDLAAHvLDRFPKL 451
Cdd:CHL00148    2 MENSKEKILVVDDEAYIRKILETRLSIIGYEVITASDGEEALKLF-RKEQP-DLVILDVMMPKLDGYGVCQE-IRKESDV 78
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1539062979 452 KIMFITGYDKTVTLPKSL-FRHDVEVMtKPFTISELASRVQRLL 494
Cdd:CHL00148   79 PIIMLTALGDVSDRITGLeLGADDYVV-KPFSPKELEARIRSVL 121
PAS smart00091
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
9-71 2.45e-06

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: 45.08  E-value: 2.45e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1539062979    9 AVLEALPIPVIVKDLNHRIVFVNQAASGYFQDPIDTLVGKTDYDCFPAEHAATYWQMEEKVIS 71
Cdd:smart00091   5 AILESLPDGIFVLDLDGRILYANPAAEELLGYSPEELIGKSLLELIHPEDRERVQEALQRLLS 67
HisKA pfam00512
His Kinase A (phospho-acceptor) domain; dimerization and phospho-acceptor domain of histidine ...
132-199 2.47e-06

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


Pssm-ID: 459839 [Multi-domain]  Cd Length: 66  Bit Score: 44.89  E-value: 2.47e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1539062979 132 AVGQLTGGIAHDFNNHLGGIIGSLGIMQKRIAKGTcvgLERYTDNAMASAQRAASLTHRLLAFSRRQS 199
Cdd:pfam00512   1 AKSEFLANLSHELRTPLTAIRGYLELLRDEKLDEE---QREYLETILRSAERLLRLINDLLDLSRIEA 65
REC_HupR cd17596
phosphoacceptor receiver (REC) domain of hydrogen uptake protein regulator (HupR); Members of ...
377-459 2.65e-06

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


Pssm-ID: 381127 [Multi-domain]  Cd Length: 133  Bit Score: 46.59  E-value: 2.65e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539062979 377 QTVMLVEDDEVLREIIIEVLEDlDYHVLSTGNGQHALELIvtAAKPVDLLLTDIGLPGINGRDLAAHVLDRFPKLKIMFI 456
Cdd:cd17596     1 PTILVVDDEVRSLEALRRTLEE-DFDVLTAASAEEALAIL--EEEWVQVILCDQRMPGTTGVEFLKEVRERWPEVVRIII 77

                  ...
gi 1539062979 457 TGY 459
Cdd:cd17596    78 SGY 80
REC_PilR cd19926
phosphoacceptor receiver (REC) domain of type 4 fimbriae expression regulatory protein PilR ...
379-480 4.47e-06

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


Pssm-ID: 381153 [Multi-domain]  Cd Length: 100  Bit Score: 45.22  E-value: 4.47e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539062979 379 VMLVEDDEVLREIIIEVLEDLDYHVLSTGNGQHALELIvtAAKPVDLLLTDIGLPGINGRDLAAHVLDRFPKLKIMFITG 458
Cdd:cd19926     1 VLVVDDEPDIRELLEITLGRMGLDVRSARNVKEARELL--ASEPYDLCLTDMRLPDGSGLELVQHIQQRLPQTPVAVITA 78
                          90       100
                  ....*....|....*....|..
gi 1539062979 459 YDKTVTLPKSLFRHDVEVMTKP 480
Cdd:cd19926    79 YGSLDTAIEALKAGAFDFLTKP 100
REC_TrxB cd17595
phosphoacceptor receiver (REC) domain a fused response regulator with a thioredoxin reductase ...
379-462 4.64e-06

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


Pssm-ID: 381126 [Multi-domain]  Cd Length: 135  Bit Score: 46.18  E-value: 4.64e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539062979 379 VMLVEDD-EVLREiiieVLEDL------DYHVLSTGNGQHALELIVTAAK---PVDLLLTDIGLPGINGRDLAAHVLDRF 448
Cdd:cd17595     3 ILTVDDDpQVLRA----VARDLrrqygkDYRVLRADSGAEALDALKELKLrgeAVALFLVDQRMPEMDGVEFLEKAMELF 78
                          90
                  ....*....|....
gi 1539062979 449 PKLKIMFITGYDKT 462
Cdd:cd17595    79 PEAKRVLLTAYADT 92
PRK09835 PRK09835
Cu(+)/Ag(+) sensor histidine kinase;
192-355 4.74e-06

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


Pssm-ID: 182101 [Multi-domain]  Cd Length: 482  Bit Score: 49.00  E-value: 4.74e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539062979 192 LAFSRRQSLNP--KPLKLND----LFDEFQSfinqsLGPEYRFEVHYEGDLWTTFCDHHQLENAVLNLAINARDAMPNGG 265
Cdd:PRK09835  321 LAQADNNQLIPekKMLDLADevgkVFDFFEA-----WAEERGVELRFVGDPCQVAGDPLMLRRAISNLLSNALRYTPAGE 395
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539062979 266 IIICQITNSASVpglfegecVCISIVDTGTGIAPEIMDRVIEPFFTTKPI----GEGTGLGLSMVYGFVKQSNGHFTIES 341
Cdd:PRK09835  396 AITVRCQEVDHQ--------VQLVVENPGTPIAPEHLPRLFDRFYRVDPSrqrkGEGSGIGLAIVKSIVVAHKGTVAVTS 467
                         170
                  ....*....|....
gi 1539062979 342 tQAKGTTVSLYLPR 355
Cdd:PRK09835  468 -DARGTRFVISLPR 480
PRK10955 PRK10955
envelope stress response regulator transcription factor CpxR;
379-494 5.00e-06

envelope stress response regulator transcription factor CpxR;


Pssm-ID: 182864 [Multi-domain]  Cd Length: 232  Bit Score: 47.88  E-value: 5.00e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539062979 379 VMLVEDDEVLREIIIEVLEDLDYHVLSTGNGQHALELIVTAakpVDLLLTDIGLPGINGRDLAAHVLDRFPKLKIMFIT- 457
Cdd:PRK10955    4 ILLVDDDRELTSLLKELLEMEGFNVIVAHDGEQALDLLDDS---IDLLLLDVMMPKKNGIDTLKELRQTHQTPVIMLTAr 80
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1539062979 458 GYDKTVTLPKSLFRHDveVMTKPFTISELASRVQRLL 494
Cdd:PRK10955   81 GSELDRVLGLELGADD--YLPKPFNDRELVARIRAIL 115
REC_OmpR_MtrA-like cd17626
phosphoacceptor receiver (REC) domain of MtrA-like OmpR family response regulators; MtrA is ...
377-491 1.07e-05

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: 44.38  E-value: 1.07e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539062979 377 QTVMLVEDDEVLREIIIEVLEDLDYHVLSTGNGQHALElIVTAAKPvDLLLTDIGLPGINGRDLAAHVLDRfPKLKIMFI 456
Cdd:cd17626     1 ARILVVDDDAALAEMIGIVLRGEGFDPAFCGDGTQALA-AFREVRP-DLVLLDLMLPGIDGIEVCRQIRAE-SGVPIVML 77
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1539062979 457 TGYDKTVTLPKSLFRHDVEVMTKPFTISELASRVQ 491
Cdd:cd17626    78 TAKSDTVDVVLGLESGADDYVAKPFKPKELVARIR 112
PRK15369 PRK15369
two component system response regulator;
374-460 1.09e-05

two component system response regulator;


Pssm-ID: 185267 [Multi-domain]  Cd Length: 211  Bit Score: 46.61  E-value: 1.09e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539062979 374 GLQQTVMLVEDDEVLREIIIEVLEDL-DYHVL-STGNGQHALELIVtAAKPvDLLLTDIGLPGINGRDLAAHVLDRFPKL 451
Cdd:PRK15369    1 MKNYKILLVDDHELIINGIKNMLAPYpRYKIVgQVDNGLEVYNACR-QLEP-DIVILDLGLPGMNGLDVIPQLHQRWPAM 78

                  ....*....
gi 1539062979 452 KIMFITGYD 460
Cdd:PRK15369   79 NILVLTARQ 87
REC_CheY4-like cd17562
phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY4 and similar CheY ...
378-457 1.19e-05

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: 44.60  E-value: 1.19e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539062979 378 TVMLVEDDEVLREIIIEVLEDLDYHVLSTGNGQHALELIvtAAKPVDLLLTDIGLPGINGRDLAAHV--LDRFPKLKIMF 455
Cdd:cd17562     2 KILAVDDSASIRQMVSFTLRGAGYEVVEAADGRDALSKA--QSKKFDLIITDQNMPNMDGIELIKELrkLPAYKFTPILM 79

                  ..
gi 1539062979 456 IT 457
Cdd:cd17562    80 LT 81
REC_D1_PleD-like cd17538
first (D1) phosphoacceptor receiver (REC) domain of response regulator PleD and similar ...
378-437 1.38e-05

first (D1) phosphoacceptor receiver (REC) domain of response regulator PleD and similar domains; PleD contains a REC domain (D1) with the phosphorylatable aspartate, a REC-like adaptor domain (D2), and the enzymatic diguanylate cyclase (DGC) domain, also called the GGDEF domain according to a conserved sequence motif, as its output domain. The GGDEF-containing PleD response regulators are global regulators of cell metabolism in some important human pathogens. This model describes D1 of PleD and similar domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381093 [Multi-domain]  Cd Length: 104  Bit Score: 44.03  E-value: 1.38e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539062979 378 TVMLVEDDEVLREIIIEVLEDLDYHVLSTGNGQHALELIvtAAKPVDLLLTDIGLPGING 437
Cdd:cd17538     1 KILVVDDEPANRELLEALLSAEGYEVLTADSGQEALALA--EEELPDLILLDVMMPGMDG 58
REC_CheY cd17542
phosphoacceptor receiver (REC) domain of chemotaxis protein CheY; The chemotaxis response ...
378-494 1.53e-05

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: 44.19  E-value: 1.53e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539062979 378 TVMLVEDDEVLREIIIEVLEDLDYHVLST-GNGQHALElIVTAAKPvDLLLTDIGLPGINGRDLAAHVLDRFPKLKIMFI 456
Cdd:cd17542     2 KVLIVDDAAFMRMMLKDILTKAGYEVVGEaANGEEAVE-KYKELKP-DLVTMDITMPEMDGIEALKEIKKIDPNAKVIMC 79
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1539062979 457 TGYDKTVTLPKSLFRHDVEVMTKPFTISELASRVQRLL 494
Cdd:cd17542    80 SAMGQEEMVKEAIKAGAKDFIVKPFQPERVLEAVEKVL 117
HATPase_LytS-like cd16957
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
247-354 1.58e-05

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


Pssm-ID: 340433 [Multi-domain]  Cd Length: 106  Bit Score: 43.95  E-value: 1.58e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539062979 247 ENAVlnlainaRDAMPNGGIIiCQITnsasVPGLFEGECVCISIVDTGTGIAPEIMDRVIEPFFTTKPiGEGTGL----- 321
Cdd:cd16957    11 ENAI-------RHAFPKRKEN-NEVR----VVVKKDQHKVHVSVSDNGQGIPEERLDLLGKTTVTSEK-GTGTALenlnr 77
                          90       100       110
                  ....*....|....*....|....*....|...
gi 1539062979 322 GLSMVYGfvkqSNGHFTIESTQAKGTTVSLYLP 354
Cdd:cd16957    78 RLIGLFG----SEACLHIESEVHGGTEVWFVIP 106
REC_RcNtrC-like cd19928
phosphoacceptor receiver (REC) domain of Rhodobacter capsulatus nitrogen regulatory protein C ...
379-480 1.69e-05

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


Pssm-ID: 381155 [Multi-domain]  Cd Length: 100  Bit Score: 43.65  E-value: 1.69e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539062979 379 VMLVEDDEVLREIIIEVLEDLDYHVLSTGNGQHALELIvtAAKPVDLLLTDIGLPGINGRDLAAHVLDRFPKLKIMFITG 458
Cdd:cd19928     1 ILVADDDRAIRTVLTQALGRAGYEVRTTGNAATLWRWV--EEGEGDLVITDVVMPDENGLDLIPRIKKARPDLPIIVMSA 78
                          90       100
                  ....*....|....*....|..
gi 1539062979 459 YDKTVTLPKSLFRHDVEVMTKP 480
Cdd:cd19928    79 QNTLMTAVKAAERGAFEYLPKP 100
HATPase_BvrS-ChvG-like cd16953
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
246-354 2.07e-05

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


Pssm-ID: 340429 [Multi-domain]  Cd Length: 110  Bit Score: 43.72  E-value: 2.07e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539062979 246 LENAVLNLAINARDAMPNGgiiicqiTNSASVPGLFEGECVCISIVDTGTGIAPEIMDRVIEPFFTTKPIGEG----TGL 321
Cdd:cd16953     1 LGQVLRNLIGNAISFSPPD-------TGRITVSAMPTGKMVTISVEDEGPGIPQEKLESIFDRFYTERPANEAfgqhSGL 73
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1539062979 322 GLSMVYGFVKQSNGHFTIES----TQAKGTTVSLYLP 354
Cdd:cd16953    74 GLSISRQIIEAHGGISVAENhnqpGQVIGARFTVQLP 110
PRK10618 PRK10618
phosphotransfer intermediate protein in two-component regulatory system with RcsBC; Provisional
284-397 2.08e-05

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


Pssm-ID: 236726 [Multi-domain]  Cd Length: 894  Bit Score: 47.23  E-value: 2.08e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539062979 284 ECVCISIVDTGTGIAPEIMDRVIEPFFtTKPI----GEGTGLGLSMVYGFVKQSNGHFTIESTQAKGTTVSLYLPRYIGE 359
Cdd:PRK10618  598 DRLTIRILDTGAGVSIKELDNLHFPFL-NQTQgdryGKASGLTFFLCNQLCRKLGGHLTIKSREGLGTRYSIHLKMLAAD 676
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1539062979 360 tcQHTSSTDEPLKEGLqqTVML-VEDDEVlREIIIEVLE 397
Cdd:PRK10618  677 --PEVEEEEEKLLDGV--TVLLdITSEEV-RKIVTRQLE 710
glnG PRK10923
nitrogen regulation protein NR(I); Provisional
379-494 2.86e-05

nitrogen regulation protein NR(I); Provisional


Pssm-ID: 182842 [Multi-domain]  Cd Length: 469  Bit Score: 46.40  E-value: 2.86e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539062979 379 VMLVEDDEVLREIIIEVLEDLDYHVLSTGNGQHALELIvtAAKPVDLLLTDIGLPGINGRDLAAHVLDRFPKLKIMFITG 458
Cdd:PRK10923    6 VWVVDDDSSIRWVLERALAGAGLTCTTFENGNEVLEAL--ASKTPDVLLSDIRMPGMDGLALLKQIKQRHPMLPVIIMTA 83
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1539062979 459 Y---DKTVtlpkSLFRHDV-EVMTKPFTISELASRVQRLL 494
Cdd:PRK10923   84 HsdlDAAV----SAYQQGAfDYLPKPFDIDEAVALVERAI 119
REC_OmpR_CusR-like cd19935
phosphoacceptor receiver (REC) domain of CusR-like OmpR family response regulators; ...
379-460 3.68e-05

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: 42.43  E-value: 3.68e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539062979 379 VMLVEDDEVLREIIIEVLEDLDYHVLSTGNGQHALELIVTAakPVDLLLTDIGLPGINGRDLAAHVLDRFPKLKIMFITG 458
Cdd:cd19935     1 ILVVEDEKKLAEYLKKGLTEEGYAVDVAYDGEDGLHLALTN--EYDLIILDVMLPGLDGLEVLRRLRAAGKQTPVLMLTA 78

                  ..
gi 1539062979 459 YD 460
Cdd:cd19935    79 RD 80
REC_FixJ cd17537
phosphoacceptor receiver (REC) domain of FixJ family response regulators; FixJ family response ...
378-492 3.84e-05

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


Pssm-ID: 381092 [Multi-domain]  Cd Length: 116  Bit Score: 42.97  E-value: 3.84e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539062979 378 TVMLVEDDEVLREIIIEVLEDLDYHVLSTGNGQHALelivtAAKPVDL---LLTDIGLPGINGRDLAAHVLDRFPKLKIM 454
Cdd:cd17537     2 TVYVVDDDEAVRDSLAFLLRSVGLAVKTFTSASAFL-----AAAPPDQpgcLVLDVRMPGMSGLELQDELLARGSNIPII 76
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1539062979 455 FITGYDktvTLP---KSLFRHDVEVMTKPFTISELASRVQR 492
Cdd:cd17537    77 FITGHG---DVPmavEAMKAGAVDFLEKPFRDQVLLDAIEQ 114
PRK10337 PRK10337
sensor protein QseC; Provisional
183-326 3.97e-05

sensor protein QseC; Provisional


Pssm-ID: 182388 [Multi-domain]  Cd Length: 449  Bit Score: 46.18  E-value: 3.97e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539062979 183 RAASLTHRLLAFSRRQSLNP----KPLKLNDLFDefQSFIN-----QSLGPEYRFEVHYEGDLWTTfcdhHQLENAVL-- 251
Cdd:PRK10337  285 RATRLVDQLLTLSRLDSLDNlqdvAEIPLEDLLQ--SAVMDiyhtaQQAGIDVRLTLNAHPVIRTG----QPLLLSLLvr 358
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1539062979 252 NLAINARDAMPNGGIIicQITNSASvpglfegecvCISIVDTGTGIAPEIMDRVIEPFFttKPIGE---GTGLGLSMV 326
Cdd:PRK10337  359 NLLDNAIRYSPQGSVV--DVTLNAR----------NFTVRDNGPGVTPEALARIGERFY--RPPGQeatGSGLGLSIV 422
PRK10336 PRK10336
two-component system response regulator QseB;
379-496 4.16e-05

two-component system response regulator QseB;


Pssm-ID: 182387 [Multi-domain]  Cd Length: 219  Bit Score: 44.89  E-value: 4.16e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539062979 379 VMLVEDDEVLREIIIEVLEDLDYHVLSTGNGQHALELIVTAakPVDLLLTDIGLPGINGRDLAAHVLDRFPKLKIMFITG 458
Cdd:PRK10336    3 ILLIEDDMLIGDGIKTGLSKMGFSVDWFTQGRQGKEALYSA--PYDAVILDLTLPGMDGRDILREWREKGQREPVLILTA 80
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1539062979 459 YDKTVTLPKSLFRHDVEVMTKPFTISELASRVQRLLEQ 496
Cdd:PRK10336   81 RDALAERVEGLRLGADDYLCKPFALIEVAARLEALMRR 118
REC_OmpR_CtrA cd17616
phosphoacceptor receiver (REC) domain of CtrA-like OmpR family response regulators; CtrA is ...
379-491 5.36e-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: 42.40  E-value: 5.36e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539062979 379 VMLVEDDEVLREIIIEVLEDLDYHVLSTGNGQHALELivtaAK--PVDLLLTDIGLPGINGRDlaahVLDRFPKLK---- 452
Cdd:cd17616     1 VLLIEDDSATAQSIELMLKSEGFNVYTTDLGEEGLDL----GKlyDYDIILLDLNLPDMSGYE----VLRTLRLAKvktp 72
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1539062979 453 IMFITGYDKTVTLPKSL-FRHDvEVMTKPFTISELASRVQ 491
Cdd:cd17616    73 ILILSGLADIEDKVKGLgFGAD-DYMTKPFHKDELVARIH 111
HisKA smart00388
His Kinase A (phosphoacceptor) domain; Dimerisation and phosphoacceptor domain of histidine ...
132-199 5.99e-05

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


Pssm-ID: 214644 [Multi-domain]  Cd Length: 66  Bit Score: 41.01  E-value: 5.99e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1539062979  132 AVGQLTGGIAHDFNNHLGGIIGSLGIMQKRIAKGtcvGLERYTDNAMASAQRAASLTHRLLAFSRRQS 199
Cdd:smart00388   1 AKREFLANLSHELRTPLTAIRGYLELLLDTELSE---EQREYLETILREAERLLRLINDLLDLSRIEA 65
REC_PA4781-like cd19920
phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase PA4781 and similar ...
379-481 7.99e-05

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


Pssm-ID: 381147 [Multi-domain]  Cd Length: 103  Bit Score: 41.73  E-value: 7.99e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539062979 379 VMLVEDDEVLREIIIEVLEDLDYHVLSTGNGQHALElIVTAAKPvDLLLTDIGLPGING----RDLAAHvldrfPKLK-- 452
Cdd:cd19920     1 ILIVDDVPDNLRLLSELLRAAGYRVLVATDGQQALQ-RAQAEPP-DLILLDVMMPGMDGfevcRRLKAD-----PATRhi 73
                          90       100       110
                  ....*....|....*....|....*....|
gi 1539062979 453 -IMFITGYDKTVTLPKSLFRHDVEVMTKPF 481
Cdd:cd19920    74 pVIFLTALTDTEDKVKGFELGAVDYITKPF 103
REC_OmpR_ChvI-like cd19936
phosphoacceptor receiver (REC) domain of ChvI-like OmpR family response regulators; ...
379-463 9.36e-05

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


Pssm-ID: 381163 [Multi-domain]  Cd Length: 99  Bit Score: 41.28  E-value: 9.36e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539062979 379 VMLVEDDEVLREIIIEVLEDLDYHVLSTGNGQHALELIvtAAKPVDLLLTDIGLPGINGRDLAAHvLDRFPKLKIMFITG 458
Cdd:cd19936     1 IALVDDDRNILTSVSMALEAEGFSVETYTDGASALDGL--NARPPDLAILDIKMPRMDGMELLQR-LRQKSTLPVIFLTS 77

                  ....*
gi 1539062979 459 YDKTV 463
Cdd:cd19936    78 KDDEI 82
PRK09836 PRK09836
DNA-binding transcriptional activator CusR; Provisional
379-496 9.77e-05

DNA-binding transcriptional activator CusR; Provisional


Pssm-ID: 182102 [Multi-domain]  Cd Length: 227  Bit Score: 43.76  E-value: 9.77e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539062979 379 VMLVEDDEVLREIIIEVLEDLDYHVLSTGNGQHALELIVTAAkpVDLLLTDIGLPGINGRDLAAHVLDRFPKLKIMFITG 458
Cdd:PRK09836    3 LLIVEDEKKTGEYLTKGLTEAGFVVDLADNGLNGYHLAMTGD--YDLIILDIMLPDVNGWDIVRMLRSANKGMPILLLTA 80
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1539062979 459 YDKTVTLPKSLFRHDVEVMTKPFTISELASRVQRLLEQ 496
Cdd:PRK09836   81 LGTIEHRVKGLELGADDYLVKPFAFAELLARVRTLLRR 118
envZ PRK09467
osmolarity sensor protein; Provisional
281-354 1.18e-04

osmolarity sensor protein; Provisional


Pssm-ID: 236531 [Multi-domain]  Cd Length: 435  Bit Score: 44.52  E-value: 1.18e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1539062979 281 FEGECVCISIVDTGTGIAPEIMDRVIEPFFT--TKPIGEGTGLGLSMVYGFVKQSNGHFTIESTQAKGTTVSLYLP 354
Cdd:PRK09467  357 TEGKRAWFQVEDDGPGIPPEQLKHLFQPFTRgdSARGSSGTGLGLAIVKRIVDQHNGKVELGNSEEGGLSARAWLP 432
REC_hyHK cd17598
phosphoacceptor receiver (REC) domain of uncharacterized hybrid sensor histidine kinase ...
379-494 1.26e-04

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


Pssm-ID: 381128 [Multi-domain]  Cd Length: 118  Bit Score: 41.54  E-value: 1.26e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539062979 379 VMLVEDDEVLREIIIEVLEDLDYHVLSTGNGQHALELIvTAAKPvDLLLTDIGLPGINGRDLAAHVLDRfPKLKimfitg 458
Cdd:cd17598     1 ILIVEDSPTQAEQLKHILEEQGYKVQVARNGREALAML-AEHRP-TLVISDIVMPEMDGYELCRKIKSD-PDLK------ 71
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1539062979 459 yDKTVTLPKSLFR-HDV---------EVMTKPFTISELASRVQRLL 494
Cdd:cd17598    72 -DIPVILLTTLSDpRDVirglecgadNFITKPYDEKYLLSRIKYIL 116
PAS_8 pfam13188
PAS domain; PAS domains are involved in many signalling proteins where they are used as a ...
9-58 1.52e-04

PAS domain; PAS domains are involved in many signalling proteins where they are used as a signal sensor domain. PAS domains appear in archaea, bacteria and eukaryotes. Several PAS-domain proteins are known to detect their signal by way of an associated cofactor. Heme, flavin, and a 4-hydroxycinnamyl chromophore are used in different proteins. This domain recognizes oxygen and CO (Matilla et al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).


Pssm-ID: 463802 [Multi-domain]  Cd Length: 65  Bit Score: 39.84  E-value: 1.52e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1539062979   9 AVLEALPIPVIVKDLNHRIVFVNQAASGYFQDPIDTLVGKTDYDCFPAEH 58
Cdd:pfam13188   5 ALFESSPDGILVLDEGGRIIYVNPAALELLGYELLGELLGELLDLLDPLL 54
REC_GlnL-like cd17565
phosphoacceptor receiver (REC) domain of transcriptional regulatory protein GlnL and similar ...
380-456 2.74e-04

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


Pssm-ID: 381112 [Multi-domain]  Cd Length: 103  Bit Score: 40.33  E-value: 2.74e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539062979 380 MLVEDDEVLREI---IIEVlEDLDYHVLSTGNGQHALELIVTAAkpVDLLLTDIGLPGINGRDLAAHVLDRFPKLKIMFI 456
Cdd:cd17565     2 YIVDDDKNIIKIlsdIIED-DDLGEVVGEADNGAQAYDEILFLQ--PDIVLIDLLMPGMDGIQLVRKLKDTGSNGKFIMI 78
REC_RitR-like cd19922
receiver (REC) domain of orphan response regulator RitR and similar domains; Streptococcus ...
379-490 2.75e-04

receiver (REC) domain of orphan response regulator RitR and similar domains; Streptococcus pneumoniae RitR (Repressor of iron transport Regulator, formerly RR489) is an orphan two-component signal transduction response regulator that is required for lung pathogenicity. It acts to repress iron uptake via binding the pneumococcal iron uptake (Piu) transporter promoter. 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. However, members of this family do not contain the phosphorylatable aspartic acid residue and are phosphorylation-independent.


Pssm-ID: 381149 [Multi-domain]  Cd Length: 110  Bit Score: 40.54  E-value: 2.75e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539062979 379 VMLVEDDEVLREIIIEVLEDLDYHVLSTGNGQHALELIvtAAKPVDLLLTDIGLPGINGRDLAAHVLDRFPKLKIMFITG 458
Cdd:cd19922     1 ILLLEKERNLAHFLSLELQKEGYRVDLVETGQEALSLA--LETDYDLILLNVNLSDMSAQDFAEKLSRIKPASVIIVLDH 78
                          90       100       110
                  ....*....|....*....|....*....|..
gi 1539062979 459 YDKTVTLPKSLFRHDVEVMTKPFTISELASRV 490
Cdd:cd19922    79 WEDLQEELEEVQRFAVSYVVKPVLISNLVDKI 110
ComP COG4585
Signal transduction histidine kinase ComP [Signal transduction mechanisms];
281-355 2.78e-04

Signal transduction histidine kinase ComP [Signal transduction mechanisms];


Pssm-ID: 443642 [Multi-domain]  Cd Length: 252  Bit Score: 42.68  E-value: 2.78e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1539062979 281 FEGECVCISIVDTGTGIAPEIMdrviepffttkpigEGTGLGLSMVYGFVKQSNGHFTIESTQAKGTTVSLYLPR 355
Cdd:COG4585   189 VDDGELTLTVRDDGVGFDPEAA--------------PGGGLGLRGMRERAEALGGTLTIGSAPGGGTRVRATLPL 249
REC_CheY_CheY3 cd19923
phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY3 and similar CheY ...
379-457 3.66e-04

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: 40.40  E-value: 3.66e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539062979 379 VMLVEDDEVLREIIIEVLEDLDY-HVLSTGNGQHALELIvtAAKPVDLLLTDIGLPGINGRDLAAHVL--DRFPKLKIMF 455
Cdd:cd19923     3 VLVVDDFSTMRRIIKNLLKELGFnNVEEAEDGVDALEKL--KAGGFDFVITDWNMPNMDGLELLKTIRadGALSHLPVLM 80

                  ..
gi 1539062979 456 IT 457
Cdd:cd19923    81 VT 82
REC_OmpR_CpxR cd17623
phosphoacceptor receiver (REC) domain of CpxR-like OmpR family response regulators; CpxR is ...
379-494 4.00e-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: 39.98  E-value: 4.00e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539062979 379 VMLVEDDEVLREIIIEVLEDLDYHVLSTGNGQHALELIvtAAKPVDLLLTDIGLPGINGRDLAAHVLDRfPKLKIMFITG 458
Cdd:cd17623     1 ILLIDDDRELTELLTEYLEMEGFNVRAAHDGEQGLAAL--LEGSPDLVVLDVMLPKMNGLDVLKELRKT-SQVPVLMLTA 77
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1539062979 459 ----YDKTVTLpkSLFRHDveVMTKPFTISELASRVQRLL 494
Cdd:cd17623    78 rgddIDRILGL--ELGADD--YLPKPFNPRELVARIRAIL 113
HATPase_CpxA-like cd16949
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
282-354 4.06e-04

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: 39.62  E-value: 4.06e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1539062979 282 EGECVCISIVDTGTGIAPEIMDRVIEPFFTTKPI----GEGTGLGLSMVYGFVKQSNGHFTIESTQAKGTTVSLYLP 354
Cdd:cd16949    27 DGDQWTITITDDGPGVPEDQLEQIFLPFYRVDSArdreSGGTGLGLAIAERAIEQHGGKIKASNRKPGGLRVRIWLP 103
REC_LytTR_AgrA-like cd17533
phosphoacceptor receiver (REC) domain of LytTR/AlgR family response regulators similar to AgrA; ...
379-495 4.12e-04

phosphoacceptor receiver (REC) domain of LytTR/AlgR family response regulators similar to AgrA; 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 AgrA-like group of LytTR/AlgR family response regulators are Staphylococcus aureus accessory gene regulator protein A (AgrA) and Streptococcus pneumoniae response regulator ComE, which are members of two-component regulatory systems. AgrA is a global regulator that controls the synthesis of virulence factors and other exoproteins. ComE is part of the ComD-ComE system that is part of a quorum-sensing signaling pathway that controls the development of competence, a physiological state required for genetic transformation. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381088 [Multi-domain]  Cd Length: 131  Bit Score: 40.30  E-value: 4.12e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539062979 379 VMLVEDDEVLREIIIEVLE------DLDYHVLSTGNGQHALELIVTAAK-PVDLLLTDIGLPGINGRDLAAHVLDRFPKL 451
Cdd:cd17533     3 IFILEDDKIQRVRLEEIIEnilkieNIEYVIELTGKTEELLEKIKERGKnGIYFLDIDIKMEEKNGLEVAQKIRKYDPYA 82
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1539062979 452 KIMFITGYDKTVTLpksLFRHDVEVM---TKPFTISELASRVQRLLE 495
Cdd:cd17533    83 IIIFVTTHSEFAPL---TFEYKVAALdfiLKPLKLEEFKKRIEECIK 126
PRK10710 PRK10710
DNA-binding transcriptional regulator BaeR; Provisional
367-494 5.72e-04

DNA-binding transcriptional regulator BaeR; Provisional


Pssm-ID: 182665 [Multi-domain]  Cd Length: 240  Bit Score: 41.59  E-value: 5.72e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539062979 367 TDEPLKEGLQQTVMLVEDDEVLREIIIEVLEDLDYHVLSTGNGQHALELIvtAAKPVDLLLTDIGLPGINGRDLAAHvLD 446
Cdd:PRK10710    1 MTELPIDENTPRILIVEDEPKLGQLLIDYLQAASYATTLLSHGDEVLPYV--RQTPPDLILLDLMLPGTDGLTLCRE-IR 77
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1539062979 447 RFPKLKIMFITGydKTVTLPKSLfrhDVEV-----MTKPFTISELASRVQRLL 494
Cdd:PRK10710   78 RFSDIPIVMVTA--KIEEIDRLL---GLEIgaddyICKPYSPREVVARVKTIL 125
PRK10529 PRK10529
DNA-binding transcriptional activator KdpE; Provisional
376-491 8.24e-04

DNA-binding transcriptional activator KdpE; Provisional


Pssm-ID: 182522 [Multi-domain]  Cd Length: 225  Bit Score: 40.94  E-value: 8.24e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539062979 376 QQTVMLVEDDEVLREIIIEVLEDLDYHVLSTGNGQHALelIVTAAKPVDLLLTDIGLPGINGRDLAAHvLDRFPKLKIMF 455
Cdd:PRK10529    1 MTNVLIVEDEQAIRRFLRTALEGDGMRVFEAETLQRGL--LEAATRKPDLIILDLGLPDGDGIEFIRD-LRQWSAIPVIV 77
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1539062979 456 ITGYDKTVTLPKSLFRHDVEVMTKPFTISELASRVQ 491
Cdd:PRK10529   78 LSARSEESDKIAALDAGADDYLSKPFGIGELQARLR 113
HATPase_CheA-like cd16916
Histidine kinase-like ATPase domain of the chemotaxis protein histidine kinase CheA, and some ...
270-354 8.74e-04

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


Pssm-ID: 340393 [Multi-domain]  Cd Length: 178  Bit Score: 40.26  E-value: 8.74e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539062979 270 QITNSASVpglfEGECVCISIVDTGTGIAP------------------------EIMDRVIEPFFTTK-PIGE--GTGLG 322
Cdd:cd16916    71 TITLRAEH----QGNQVVIEVSDDGRGIDRekirekaierglitadeaatlsddEVLNLIFAPGFSTAeQVTDvsGRGVG 146
                          90       100       110
                  ....*....|....*....|....*....|..
gi 1539062979 323 LSMVYGFVKQSNGHFTIESTQAKGTTVSLYLP 354
Cdd:cd16916   147 MDVVKRSIESLGGTIEVESEPGQGTTFTIRLP 178
PRK10643 PRK10643
two-component system response regulator PmrA;
379-494 1.10e-03

two-component system response regulator PmrA;


Pssm-ID: 182612 [Multi-domain]  Cd Length: 222  Bit Score: 40.40  E-value: 1.10e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539062979 379 VMLVEDDEVLREIIIEVLEDLDYHVLSTGNGQHALELIVTAAkpVDLLLTDIGLPGINGrdlaAHVLDRFPK----LKIM 454
Cdd:PRK10643    3 ILIVEDDTLLLQGLILALQTEGYACDCASTAREAEALLESGH--YSLVVLDLGLPDEDG----LHLLRRWRQkkytLPVL 76
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1539062979 455 FITGYDktvTLPKSLFRHDV---EVMTKPFTISELASRVQRLL 494
Cdd:PRK10643   77 ILTARD---TLEDRVAGLDVgadDYLVKPFALEELHARIRALI 116
REC_RocR cd17530
phosphoacceptor receiver (REC) domain of response regulator RocR; The response regulator RocR ...
378-486 1.24e-03

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


Pssm-ID: 381086 [Multi-domain]  Cd Length: 123  Bit Score: 38.96  E-value: 1.24e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539062979 378 TVMLVEDDEVLREIIIEVLEDLDY-HVLSTGNGQHALELIVTAAkpVDLLLTDIGLPGINGRDLAAHVLDRFPKLKIMFI 456
Cdd:cd17530     2 RVLVLDDDPFQCMMAATILEDLGPgNVDEADDGREALVILLCNA--PDIIICDLKMPDMDGIEFLRHLAESHSNAAVILM 79
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1539062979 457 TGYD-----KTVTLPKSLFRHDVEVMTKPFTISEL 486
Cdd:cd17530    80 SGLDggileSAETLAGANGLNLLGTLSKPFSPEEL 114
PRK10841 PRK10841
two-component system sensor histidine kinase RcsC;
287-378 1.38e-03

two-component system sensor histidine kinase RcsC;


Pssm-ID: 182772 [Multi-domain]  Cd Length: 924  Bit Score: 41.50  E-value: 1.38e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539062979 287 CISIVDTGTGIAPEIMDRVIEPFFTtkpIG-------EGTGLGLSMVYGFVKQSNGHFTIESTQAKGTTVSLYLPRYige 359
Cdd:PRK10841  595 SFRVRDTGVGIPAKEVVRLFDPFFQ---VGtgvqrnfQGTGLGLAICEKLINMMDGDISVDSEPGMGSQFTIRIPLY--- 668
                          90
                  ....*....|....*....
gi 1539062979 360 tcqHTSSTDEPLKEGLQQT 378
Cdd:PRK10841  669 ---GAQYPQKKGVEGLQGK 684
TyrR COG3283
Transcriptional regulator TyrR of aromatic amino acids metabolism [Transcription, Amino acid ...
9-49 2.16e-03

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


Pssm-ID: 442513 [Multi-domain]  Cd Length: 514  Bit Score: 40.56  E-value: 2.16e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1539062979   9 AVLEALPIPVIVKDLNHRIVFVNQAASGYFQDPIDTLVGKT 49
Cdd:COG3283    84 ALLEALPDPVFSIDLKGKIELANPAALSLLGLSEEELIGQP 124
REC_CheB-like cd17541
phosphoacceptor receiver (REC) domain of chemotaxis response regulator protein-glutamate ...
379-437 2.52e-03

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


Pssm-ID: 381096 [Multi-domain]  Cd Length: 125  Bit Score: 37.76  E-value: 2.52e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1539062979 379 VMLVEDDEVLREIIIEVLE-DLDYHVLST-GNGQHALELIVtAAKPvDLLLTDIGLPGING 437
Cdd:cd17541     3 VLIVDDSAVMRKLLSRILEsDPDIEVVGTaRDGEEALEKIK-ELKP-DVITLDIEMPVMDG 61
HATPase_PDK-like cd16929
Histidine kinase-like ATPase domain of pyruvate dehydrogenase kinase, branched-chain ...
284-354 2.57e-03

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


Pssm-ID: 340406 [Multi-domain]  Cd Length: 169  Bit Score: 38.86  E-value: 2.57e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539062979 284 ECVCISIVDTGTGIAPEIMDRVIEPFFTTKP---------IGEGT--------GLGLSMVYGFVKQSNGHFTIESTQAKG 346
Cdd:cd16929    82 EDLTIKISDRGGGIPREDLARLFSYMYSTAPqpslddfsdLISGTqpsplagfGYGLPMSRLYAEYFGGDLDLQSMEGYG 161

                  ....*...
gi 1539062979 347 TTVSLYLP 354
Cdd:cd16929   162 TDVYIYLK 169
PAS_9 pfam13426
PAS domain; This domain is found in many signalling proteins in which it functions as a sensor ...
24-116 2.66e-03

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: 37.06  E-value: 2.66e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539062979  24 NHRIVFVNQAASGYFQDPIDTLVGKTDYDCFPAEHAAtywQMEEKVISTQCPCENEETI-IGPEGKPQIIITTKTLVTVA 102
Cdd:pfam13426   1 DGRIIYVNDAALRLLGYTREELLGKSITDLFAEPEDS---ERLREALREGKAVREFEVVlYRKDGEPFPVLVSLAPIRDD 77
                          90
                  ....*....|....*.
gi 1539062979 103 NESL--LVAYFINVTA 116
Cdd:pfam13426  78 GGELvgIIAILRDITE 93
REC_PFxFATGY cd17586
phosphoacceptor receiver (REC) domain of PFxFATGY motif single-domain (stand-alone) response ...
379-494 4.06e-03

phosphoacceptor receiver (REC) domain of PFxFATGY motif single-domain (stand-alone) response regulators; This subfamily is composed of stand-alone response regulators (RRs) containing the PFxFATG[G/Y] motif; RRs with such a motif are also called ''FAT GUY'' response regulators. Included in this subfamily are Sphingomonas melonis SdrG, Sinorhizobium meliloti Sma0114, and Erythrobacter litoralis EL_LovR. SdrG is involved in the control of the general stress response. Sma0114 is part of the Sma0113/Sma0114 two-component system (TCS) that is involved in catabolite repression and polyhydroxy butyrate synthesis. EL_LovR is involved in a light-regulated TCS. PFxFATG[G/Y] RRs are typically associated with histidine-tryptophan-glutamate (HWE) histidine kinases that constitute a subclass of the larger histidine kinase superfamily characterized by an altered ATP binding site, which lacks the F-box that is normally an integral component of the ATP lid. The PFxFATG[G/Y] motif is involved in conformational changes after phosphorylation that results in the activation of the RR. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381122 [Multi-domain]  Cd Length: 111  Bit Score: 37.06  E-value: 4.06e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539062979 379 VMLVEDDEVLREIIIEVLEDLDYHVLSTGNG-QHALELIvtAAKPVDLLLTDIGLpginGRDLAAHVLDRFPKLKIMFI- 456
Cdd:cd17586     1 VLVLEDEPLIAMNLEDALEDLGGKEVVTAATcAEALRSL--ADGPIDIAILDVNL----GGETSIPVADALKRRAIPFIf 74
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1539062979 457 -TGYDKTVTLPKSLfrHDVEVMTKPFTISELASRVQRLL 494
Cdd:cd17586    75 aTGYGDSHGIDSRL--IDVPVLRKPFDADSALAALAMLL 111
PRK10755 PRK10755
two-component system sensor histidine kinase PmrB;
248-355 4.29e-03

two-component system sensor histidine kinase PmrB;


Pssm-ID: 236751 [Multi-domain]  Cd Length: 356  Bit Score: 39.18  E-value: 4.29e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539062979 248 NAVL------NLAINARDAMPNGGIIICQITNSasvpglfEGECVcISIVDTGTGIAPEIMDRVIEPFFTTKPIGEGTGL 321
Cdd:PRK10755  244 DATLlrlllrNLVENAHRYSPEGSTITIKLSQE-------DGGAV-LAVEDEGPGIDESKCGELSKAFVRMDSRYGGIGL 315
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1539062979 322 GLSMVYGFVKQSNGHFTIES-TQAKGTTVSLYLPR 355
Cdd:PRK10755  316 GLSIVSRITQLHHGQFFLQNrQERSGTRAWVWLPK 350
REC_PhyR cd17540
phosphoacceptor receiver (REC) domain of response regulator PhyR and similar proteins; PhyR is ...
377-491 4.36e-03

phosphoacceptor receiver (REC) domain of response regulator PhyR and similar proteins; PhyR is a hybrid stress regulator that contains an N-terminal sigma-like (SL) domain and a C-terminal REC domain. Phosphorylation of the REC domain is known to promote binding of the SL domain to an anti-sigma factor. PhyR thus functions as an anti-anti-sigma factor in its phosphorylated state. It is involved in the general stress response. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381095 [Multi-domain]  Cd Length: 117  Bit Score: 37.23  E-value: 4.36e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539062979 377 QTVMLVEDDEVLREIIIEVLEDLDYHVLSTGNGQH-ALELiVTAAKPvDLLLTDIGLP-GINGRDLAAHVLDRFPKLKIm 454
Cdd:cd17540     1 TRVLIIEDEPLIAMDLEQIVEDLGHQVVGIARTRDeAVAL-ARRERP-DLILADIQLAdGSSGIDAVNEILTTHDVPVI- 77
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1539062979 455 FITGYdktvtlPKSLFRHD----VEVMTKPFTISELASRVQ 491
Cdd:cd17540    78 FVTAY------PERLLTGErpepTFLITKPFDPEMVKAAIS 112
HATPase_YcbM-like cd16947
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
286-351 4.38e-03

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: 37.49  E-value: 4.38e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1539062979 286 VCISIVDTGTGIAPEIMDRVIEPFFTTKPIG----EGTGLGLSMVYGFVKQSNGHFTIESTQAKGT--TVSL 351
Cdd:cd16947    53 VYIDIWDKGKGISETEKDHVFERLYTLEDSRnsakQGNGLGLTITKRLAESMGGSIYVNSKPYEKTvfTVTL 124
HATPase_YpdA-like cd16955
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
288-354 5.24e-03

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Escherichia coli YpdA; This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component sensor histidine kinase (HKs) such as Escherichia coli YpdA, a HK of the two-component system (TCS) YpdA-YpdB which is involved in a nutrient sensing regulatory network with YehU-YehT. Proteins having this HATPase domain also contain a histidine kinase domain (His-kinase), and some have a GAF sensor domain; some contain a DUF3816 domain; some are hybrid sensor histidine kinases as they also contain a REC signal receiver domain.


Pssm-ID: 340431 [Multi-domain]  Cd Length: 102  Bit Score: 36.67  E-value: 5.24e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1539062979 288 ISIVDTGTGIAPEIMDRVIEPFFttkpigEGTGLGLSMVYGFVKQSNGH-FTIESTQAKGTTVSLYLP 354
Cdd:cd16955    41 IAVEDNGIGISPKVIERVEQDEM------PGNKIGLLNVHQRLKLGYGEgLHIRSRPDPGTLIAFYIP 102
PRK11517 PRK11517
DNA-binding response regulator HprR;
379-496 6.87e-03

DNA-binding response regulator HprR;


Pssm-ID: 183172 [Multi-domain]  Cd Length: 223  Bit Score: 37.96  E-value: 6.87e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539062979 379 VMLVEDDEVLREIIIEVLEDLDYHVLSTGNGQHALELIVTaaKPVDLLLTDIGLPGINGRDLAaHVLDRFPKLKIMFITG 458
Cdd:PRK11517    3 ILLIEDNQRTQEWVTQGLSEAGYVIDAVSDGRDGLYLALK--DDYALIILDIMLPGMDGWQIL-QTLRTAKQTPVICLTA 79
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1539062979 459 YDKTVTLPKSLFRHDVEVMTKPFTISELASRVQRLLEQ 496
Cdd:PRK11517   80 RDSVDDRVRGLDSGANDYLVKPFSFSELLARVRAQLRQ 117
REC_PatA-like cd17602
phosphoacceptor receiver (REC) domain of PatA and similar domains; Nostoc sp. (or Anabaena sp.) ...
379-440 7.93e-03

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: 36.19  E-value: 7.93e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1539062979 379 VMLVEDDEVLREIIIEVLEDLDYHVLSTGNGQHALELIVTaAKPvDLLLTDIGLPGINGRDL 440
Cdd:cd17602     1 VACVDDRPSIQKMIEYFLEKQGFRVVVIDDPLRALTTLLN-SKP-DLILIDIDMPDLDGYEL 60
PRK10651 PRK10651
transcriptional regulator NarL; Provisional
366-447 8.91e-03

transcriptional regulator NarL; Provisional


Pssm-ID: 182619 [Multi-domain]  Cd Length: 216  Bit Score: 37.70  E-value: 8.91e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539062979 366 STDEPlkeglqQTVMLVEDDEVLREIIIEVLE---DLDYhVLSTGNGQHALELIVtAAKPvDLLLTDIGLPGINGRDLAA 442
Cdd:PRK10651    2 SNQEP------ATILLIDDHPMLRTGVKQLISmapDITV-VGEASNGEQGIELAE-SLDP-DLILLDLNMPGMNGLETLD 72

                  ....*
gi 1539062979 443 HVLDR 447
Cdd:PRK10651   73 KLREK 77
 
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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