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Conserved domains on  [gi|2737555188|ref|WP_347786950|]
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MULTISPECIES: ATP-binding protein [Bacteroidales]

Protein Classification

hybrid sensor histidine kinase/response regulator( domain architecture ID 12788210)

two-component hybrid sensor histidine kinase/response regulator

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
BaeS COG0642
Signal transduction histidine kinase [Signal transduction mechanisms];
185-515 1.37e-57

Signal transduction histidine kinase [Signal transduction mechanisms];


:

Pssm-ID: 440407 [Multi-domain]  Cd Length: 328  Bit Score: 199.36  E-value: 1.37e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188 185 LNEQLIALQAERIRNMENYTDSLRIRNRELNRKLFALLGNISDHAQAAFRDREEQIAQAHQRSTSIITGLIIAAILLLVF 264
Cdd:COG0642     1 LLLLLLLLVLLLLLLLLLLLALLLLLLLLLLLALLLLLALLLLLLLLLLLLLLLALALLALLLLLLLLLLLLLLLLLLLL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188 265 SYLIIQKHLKRDSLLRKKMEGVIDRNNELletRKNVILTISHDIRGPLNIIYGYVELAKDTRDRKRRnHHLENIETECKH 344
Cdd:COG0642    81 LLLLLLLLLLLLLLLLLALLLLLEEANEA---KSRFLANVSHELRTPLTAIRGYLELLLEELDEEQR-EYLETILRSADR 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188 345 ILHLLNNLLDVYRLNESKETCNNVPFNLNDLLERIVTGFSHIANNKGIIFHHDSQNTDVVLCGDMDRISQIIDNLLTNAV 424
Cdd:COG0642   157 LLRLINDLLDLSRLEAGKLELEPEPVDLAELLEEVVELFRPLAEEKGIELELDLPDDLPTVRGDPDRLRQVLLNLLSNAI 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188 425 KFTNAG-MIQFNVRYENGMLYIEIKDTGIGMDQDTVSRIFRPFERLSSEANAEGFGLGLPITKGLVKLLGGSIDVESKIG 503
Cdd:COG0642   237 KYTPEGgTVTVSVRREGDRVRISVEDTGPGIPPEDLERIFEPFFRTDPSRRGGGTGLGLAIVKRIVELHGGTIEVESEPG 316
                         330
                  ....*....|..
gi 2737555188 504 HGSTFRVSLPLA 515
Cdd:COG0642   317 KGTTFTVTLPLA 328
PRK09959 super family cl32441
acid-sensing system histidine kinase EvgS;
287-766 2.70e-33

acid-sensing system histidine kinase EvgS;


The actual alignment was detected with superfamily member PRK09959:

Pssm-ID: 182169 [Multi-domain]  Cd Length: 1197  Bit Score: 138.33  E-value: 2.70e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188  287 IDRNNELLET--RKNVILTISHDIRGPLNIIYGYVELAKDT-RDRKRRNHHLENIETECKHILHLLNNLLDVYRLNESKE 363
Cdd:PRK09959   700 VERNKAINATvaKSQFLATMSHEIRTPISSIMGFLELLSGSgLSKEQRVEAISLAYATGQSLLGLIGEILDVDKIESGNY 779
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188  364 TCNNVPFNLNDLLERIVTGFSHIANNKGIIFHHDSQNTDVVLCG-DMDRISQIIDNLLTNAVKFTNAGMIQF-----NVR 437
Cdd:PRK09959   780 QLQPQWVDIPTLVQNTCHSFGAIAASKSIALSCSSTFPDHYLVKiDPQAFKQVLSNLLSNALKFTTEGAVKIttslgHID 859
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188  438 YENGMLYIEIKDTGIGMDQDTVSRIFRPFERLSSEANAEGFGLGLPITKGLVKLLGGSIDVESKIGHGSTFRVSLPLAVS 517
Cdd:PRK09959   860 DNHAVIKMTIMDSGSGLSQEEQQQLFKRYSQTSAGRQQTGSGLGLMICKELIKNMQGDLSLESHPGIGTTFTITIPVEIS 939
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188  518 NEKINSEASAVPQDRLPLPQRVLVIDNDTLQLEIAKEMLERNGVSCTTCSNAKELVNEMRRQDYDLLLSDIQMPETNGFE 597
Cdd:PRK09959   940 QQVATVEAKAEQPITLPEKLSILIADDHPTNRLLLKRQLNLLGYDVDEATDGVQALHKVSMQHYDLLITDVNMPNMDGFE 1019
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188  598 ILALLRKssigNSHTIPIVAMTARGEG-EKEAFIKGGFTDSIHKPFSmrelLDMVSSVVSRDVEESH-TPDFATFTADVL 675
Cdd:PRK09959  1020 LTRKLRE----QNSSLPIWGLTANAQAnEREKGLSCGMNLCLFKPLT----LDVLKTHLSQLHQVAHiAPQYRHLDIEAL 1091
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188  676 DK---------RELLRTFIIQSEQNMADLQSAIKTGDIEKLHDIAHEIKPSLELLRADApLVKLRTTLNDSACDMNTVNE 746
Cdd:PRK09959  1092 KNntandlqlmQEILMTFQHETHKDLPAAFHALEAGDNRTFHQCIHRIHGAANILNLQK-LINISHQLEITPVSDDSKPE 1170
                          490       500
                   ....*....|....*....|
gi 2737555188  747 QVKLLiGHISGLITEAEKEI 766
Cdd:PRK09959  1171 ILQLL-NSVKEHIAELDQEI 1189
 
Name Accession Description Interval E-value
BaeS COG0642
Signal transduction histidine kinase [Signal transduction mechanisms];
185-515 1.37e-57

Signal transduction histidine kinase [Signal transduction mechanisms];


Pssm-ID: 440407 [Multi-domain]  Cd Length: 328  Bit Score: 199.36  E-value: 1.37e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188 185 LNEQLIALQAERIRNMENYTDSLRIRNRELNRKLFALLGNISDHAQAAFRDREEQIAQAHQRSTSIITGLIIAAILLLVF 264
Cdd:COG0642     1 LLLLLLLLVLLLLLLLLLLLALLLLLLLLLLLALLLLLALLLLLLLLLLLLLLLALALLALLLLLLLLLLLLLLLLLLLL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188 265 SYLIIQKHLKRDSLLRKKMEGVIDRNNELletRKNVILTISHDIRGPLNIIYGYVELAKDTRDRKRRnHHLENIETECKH 344
Cdd:COG0642    81 LLLLLLLLLLLLLLLLLALLLLLEEANEA---KSRFLANVSHELRTPLTAIRGYLELLLEELDEEQR-EYLETILRSADR 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188 345 ILHLLNNLLDVYRLNESKETCNNVPFNLNDLLERIVTGFSHIANNKGIIFHHDSQNTDVVLCGDMDRISQIIDNLLTNAV 424
Cdd:COG0642   157 LLRLINDLLDLSRLEAGKLELEPEPVDLAELLEEVVELFRPLAEEKGIELELDLPDDLPTVRGDPDRLRQVLLNLLSNAI 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188 425 KFTNAG-MIQFNVRYENGMLYIEIKDTGIGMDQDTVSRIFRPFERLSSEANAEGFGLGLPITKGLVKLLGGSIDVESKIG 503
Cdd:COG0642   237 KYTPEGgTVTVSVRREGDRVRISVEDTGPGIPPEDLERIFEPFFRTDPSRRGGGTGLGLAIVKRIVELHGGTIEVESEPG 316
                         330
                  ....*....|..
gi 2737555188 504 HGSTFRVSLPLA 515
Cdd:COG0642   317 KGTTFTVTLPLA 328
PRK11091 PRK11091
aerobic respiration control sensor protein ArcB; Provisional
301-715 1.64e-48

aerobic respiration control sensor protein ArcB; Provisional


Pssm-ID: 236842 [Multi-domain]  Cd Length: 779  Bit Score: 183.99  E-value: 1.64e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188 301 ILTISHDIRGPLNIIYGYVELAKDTRDRKRRNHHLENIETECKHILHLLNNLLDVYRLNESKETCNNVPFNLNDLLERIV 380
Cdd:PRK11091  287 ISTISHELRTPLNGIVGLSRILLDTELTAEQRKYLKTIHVSAITLGNIFNDIIDMDKMERRKLQLDNQPIDFTDFLADLE 366
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188 381 TGFSHIANNKGIIFHHDSQNT-DVVLCGDMDRISQIIDNLLTNAVKFTNAGMIQFNVRYENG-MLYIEIKDTGIGMDQDT 458
Cdd:PRK11091  367 NLSGLQAEQKGLRFDLEPLLPlPHKVITDGTRLRQILWNLISNAVKFTQQGGVTVRVRYEEGdMLTFEVEDSGIGIPEDE 446
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188 459 VSRIFRPFERLSSEAN---AEGFGLGLPITKGLVKLLGGSIDVESKIGHGSTFRVSLPLAVSNEKINSEasaVPQDRLPL 535
Cdd:PRK11091  447 LDKIFAMYYQVKDSHGgkpATGTGIGLAVSKRLAQAMGGDITVTSEEGKGSCFTLTIHAPAVAEEVEDA---FDEDDMPL 523
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188 536 PQ-RVLVIDNDTLQLEIAKEMLERNGVSCTTCSNAKELVNEMRRQDYDLLLSDIQMPETNGFEILALLRKSSiGNSHTIP 614
Cdd:PRK11091  524 PAlNILLVEDIELNVIVARSVLEKLGNSVDVAMTGKEALEMFDPDEYDLVLLDIQLPDMTGLDIARELRERY-PREDLPP 602
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188 615 IVAMTARGEGEKEAFIKGGFTDSIHKPFSMRELLDMVSSVVSRDVEESHTP---DFATFTADVLDKrELLRTF------- 684
Cdd:PRK11091  603 LVALTANVLKDKKEYLDAGMDDVLSKPLSVPALTAMIKKFWDTQDDEESTVtteESSKANEALLDI-PMLEQYvelvgpk 681
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|
gi 2737555188 685 -IIQS----EQNM----ADLQSAIKTGDIEKLHDIAHEIK 715
Cdd:PRK11091  682 lITDSlavfEKMMpgylSVLDSNLTARDQKGIVEEAHKIK 721
PRK09959 PRK09959
acid-sensing system histidine kinase EvgS;
287-766 2.70e-33

acid-sensing system histidine kinase EvgS;


Pssm-ID: 182169 [Multi-domain]  Cd Length: 1197  Bit Score: 138.33  E-value: 2.70e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188  287 IDRNNELLET--RKNVILTISHDIRGPLNIIYGYVELAKDT-RDRKRRNHHLENIETECKHILHLLNNLLDVYRLNESKE 363
Cdd:PRK09959   700 VERNKAINATvaKSQFLATMSHEIRTPISSIMGFLELLSGSgLSKEQRVEAISLAYATGQSLLGLIGEILDVDKIESGNY 779
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188  364 TCNNVPFNLNDLLERIVTGFSHIANNKGIIFHHDSQNTDVVLCG-DMDRISQIIDNLLTNAVKFTNAGMIQF-----NVR 437
Cdd:PRK09959   780 QLQPQWVDIPTLVQNTCHSFGAIAASKSIALSCSSTFPDHYLVKiDPQAFKQVLSNLLSNALKFTTEGAVKIttslgHID 859
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188  438 YENGMLYIEIKDTGIGMDQDTVSRIFRPFERLSSEANAEGFGLGLPITKGLVKLLGGSIDVESKIGHGSTFRVSLPLAVS 517
Cdd:PRK09959   860 DNHAVIKMTIMDSGSGLSQEEQQQLFKRYSQTSAGRQQTGSGLGLMICKELIKNMQGDLSLESHPGIGTTFTITIPVEIS 939
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188  518 NEKINSEASAVPQDRLPLPQRVLVIDNDTLQLEIAKEMLERNGVSCTTCSNAKELVNEMRRQDYDLLLSDIQMPETNGFE 597
Cdd:PRK09959   940 QQVATVEAKAEQPITLPEKLSILIADDHPTNRLLLKRQLNLLGYDVDEATDGVQALHKVSMQHYDLLITDVNMPNMDGFE 1019
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188  598 ILALLRKssigNSHTIPIVAMTARGEG-EKEAFIKGGFTDSIHKPFSmrelLDMVSSVVSRDVEESH-TPDFATFTADVL 675
Cdd:PRK09959  1020 LTRKLRE----QNSSLPIWGLTANAQAnEREKGLSCGMNLCLFKPLT----LDVLKTHLSQLHQVAHiAPQYRHLDIEAL 1091
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188  676 DK---------RELLRTFIIQSEQNMADLQSAIKTGDIEKLHDIAHEIKPSLELLRADApLVKLRTTLNDSACDMNTVNE 746
Cdd:PRK09959  1092 KNntandlqlmQEILMTFQHETHKDLPAAFHALEAGDNRTFHQCIHRIHGAANILNLQK-LINISHQLEITPVSDDSKPE 1170
                          490       500
                   ....*....|....*....|
gi 2737555188  747 QVKLLiGHISGLITEAEKEI 766
Cdd:PRK09959  1171 ILQLL-NSVKEHIAELDQEI 1189
HATPase_EvgS-ArcB-TorS-like cd16922
Histidine kinase-like ATPase domain of two-component sensor histidine kinases, many are hybrid ...
414-514 9.69e-33

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: 122.22  E-value: 9.69e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188 414 QIIDNLLTNAVKFTNAGMIQFNVRYEN-----GMLYIEIKDTGIGMDQDTVSRIFRPFERLSSEA--NAEGFGLGLPITK 486
Cdd:cd16922     3 QILLNLLGNAIKFTEEGEVTLRVSLEEeeedgVQLRFSVEDTGIGIPEEQQARLFEPFSQADSSTtrKYGGTGLGLAISK 82
                          90       100
                  ....*....|....*....|....*...
gi 2737555188 487 GLVKLLGGSIDVESKIGHGSTFRVSLPL 514
Cdd:cd16922    83 KLVELMGGDISVESEPGQGSTFTFTLPL 110
HATPase_c smart00387
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.
407-515 5.53e-32

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


Pssm-ID: 214643 [Multi-domain]  Cd Length: 111  Bit Score: 120.06  E-value: 5.53e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188  407 GDMDRISQIIDNLLTNAVKFTNA-GMIQFNVRYENGMLYIEIKDTGIGMDQDTVSRIFRPFERLSSEA-NAEGFGLGLPI 484
Cdd:smart00387   1 GDPDRLRQVLSNLLDNAIKYTPEgGRITVTLERDGDHVEITVEDNGPGIPPEDLEKIFEPFFRTDKRSrKIGGTGLGLSI 80
                           90       100       110
                   ....*....|....*....|....*....|.
gi 2737555188  485 TKGLVKLLGGSIDVESKIGHGSTFRVSLPLA 515
Cdd:smart00387  81 VKKLVELHGGEISVESEPGGGTTFTITLPLE 111
CheY COG0784
CheY-like REC (receiver) domain, includes chemotaxis protein CheY and sporulation regulator ...
538-658 2.42e-29

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: 113.02  E-value: 2.42e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188 538 RVLVIDNDTLQLEIAKEMLERNGVSCTTCSNAKELVNEMRRQDYDLLLSDIQMPETNGFEILALLRKSSIGnsHTIPIVA 617
Cdd:COG0784     7 RILVVDDNPDNRELLRRLLERLGYEVTTAEDGAEALELLRAGPPDLILLDINMPGMDGLELLRRIRALPRL--PDIPIIA 84
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 2737555188 618 MTARG-EGEKEAFIKGGFTDSIHKPFSMRELLDMVSSVVSRD 658
Cdd:COG0784    85 LTAYAdEEDRERALEAGADDYLTKPVDPEELLEALRRLLARA 126
REC_hyHK_CKI1_RcsC-like cd17546
phosphoacceptor receiver (REC) domain of hybrid sensor histidine kinases/response regulators ...
539-651 5.01e-27

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: 106.01  E-value: 5.01e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188 539 VLVIDNDTLQLEIAKEMLERNGVSCTTCSNAKELVNEMRRQDYDLLLSDIQMPETNGFEILALLRKSSIGNSHTiPIVAM 618
Cdd:cd17546     1 VLVVDDNPVNRKVLKKLLEKLGYEVDVAENGQEALELLKEEPFDLVLMDLQMPVMDGLEATRRIRELEGGGRRT-PIIAL 79
                          90       100       110
                  ....*....|....*....|....*....|....
gi 2737555188 619 TARG-EGEKEAFIKGGFTDSIHKPFSMRELLDMV 651
Cdd:cd17546    80 TANAlEEDREKCLEAGMDDYLSKPVKLDQLKEVL 113
HATPase_c pfam02518
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the ...
407-515 5.77e-27

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


Pssm-ID: 460579 [Multi-domain]  Cd Length: 109  Bit Score: 105.53  E-value: 5.77e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188 407 GDMDRISQIIDNLLTNAVKFT-NAGMIQFNVRyENGMLYIEIKDTGIGMDQDTVSRIFRPFERLSSEaNAEGFGLGLPIT 485
Cdd:pfam02518   1 GDELRLRQVLSNLLDNALKHAaKAGEITVTLS-EGGELTLTVEDNGIGIPPEDLPRIFEPFSTADKR-GGGGTGLGLSIV 78
                          90       100       110
                  ....*....|....*....|....*....|
gi 2737555188 486 KGLVKLLGGSIDVESKIGHGSTFRVSLPLA 515
Cdd:pfam02518  79 RKLVELLGGTITVESEPGGGTTVTLTLPLA 108
Response_reg pfam00072
Response regulator receiver domain; This domain receives the signal from the sensor partner in ...
539-651 8.04e-22

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: 91.06  E-value: 8.04e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188 539 VLVIDNDTLQLEIAKEMLERNGVSCTTCSNAKELVNEMRRQDYDLLLSDIQMPETNGFEILALLRKssigNSHTIPIVAM 618
Cdd:pfam00072   1 VLIVDDDPLIRELLRQLLEKEGYVVAEADDGKEALELLKEERPDLILLDINMPGMDGLELLKRIRR----RDPTTPVIIL 76
                          90       100       110
                  ....*....|....*....|....*....|....
gi 2737555188 619 TARGEGE-KEAFIKGGFTDSIHKPFSMRELLDMV 651
Cdd:pfam00072  77 TAHGDEDdAVEALEAGADDFLSKPFDPDELLAAI 110
REC smart00448
cheY-homologous receiver domain; CheY regulates the clockwise rotation of E. coli flagellar ...
538-591 8.59e-10

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


Pssm-ID: 214668 [Multi-domain]  Cd Length: 55  Bit Score: 54.88  E-value: 8.59e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2737555188  538 RVLVIDNDTLQLEIAKEMLERNGVSCTTCSNAKELVNEMRRQDYDLLLSDIQMP 591
Cdd:smart00448   2 RILVVDDDPLLRELLKALLEKEGYEVDEATDGEEALELLKEEKPDLILLDIMMP 55
 
Name Accession Description Interval E-value
BaeS COG0642
Signal transduction histidine kinase [Signal transduction mechanisms];
185-515 1.37e-57

Signal transduction histidine kinase [Signal transduction mechanisms];


Pssm-ID: 440407 [Multi-domain]  Cd Length: 328  Bit Score: 199.36  E-value: 1.37e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188 185 LNEQLIALQAERIRNMENYTDSLRIRNRELNRKLFALLGNISDHAQAAFRDREEQIAQAHQRSTSIITGLIIAAILLLVF 264
Cdd:COG0642     1 LLLLLLLLVLLLLLLLLLLLALLLLLLLLLLLALLLLLALLLLLLLLLLLLLLLALALLALLLLLLLLLLLLLLLLLLLL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188 265 SYLIIQKHLKRDSLLRKKMEGVIDRNNELletRKNVILTISHDIRGPLNIIYGYVELAKDTRDRKRRnHHLENIETECKH 344
Cdd:COG0642    81 LLLLLLLLLLLLLLLLLALLLLLEEANEA---KSRFLANVSHELRTPLTAIRGYLELLLEELDEEQR-EYLETILRSADR 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188 345 ILHLLNNLLDVYRLNESKETCNNVPFNLNDLLERIVTGFSHIANNKGIIFHHDSQNTDVVLCGDMDRISQIIDNLLTNAV 424
Cdd:COG0642   157 LLRLINDLLDLSRLEAGKLELEPEPVDLAELLEEVVELFRPLAEEKGIELELDLPDDLPTVRGDPDRLRQVLLNLLSNAI 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188 425 KFTNAG-MIQFNVRYENGMLYIEIKDTGIGMDQDTVSRIFRPFERLSSEANAEGFGLGLPITKGLVKLLGGSIDVESKIG 503
Cdd:COG0642   237 KYTPEGgTVTVSVRREGDRVRISVEDTGPGIPPEDLERIFEPFFRTDPSRRGGGTGLGLAIVKRIVELHGGTIEVESEPG 316
                         330
                  ....*....|..
gi 2737555188 504 HGSTFRVSLPLA 515
Cdd:COG0642   317 KGTTFTVTLPLA 328
KdpD COG2205
K+-sensing histidine kinase KdpD [Signal transduction mechanisms];
292-517 9.58e-54

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


Pssm-ID: 441807 [Multi-domain]  Cd Length: 239  Bit Score: 185.88  E-value: 9.58e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188 292 ELLETRKNVILTISHDIRGPLNIIYGYVELAKD--TRDRKRRNHHLENIETECKHILHLLNNLLDVYRLNESKETCNNVP 369
Cdd:COG2205    11 ELERLKSEFLANVSHELRTPLTSILGAAELLLDeeDLSPEERRELLEIIRESAERLLRLIEDLLDLSRLESGKLSLELEP 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188 370 FNLNDLLERIVTGFSHIANNKGIIFHHDSQNTDVVLCGDMDRISQIIDNLLTNAVKFTNAG-MIQFNVRYENGMLYIEIK 448
Cdd:COG2205    91 VDLAELLEEAVEELRPLAEEKGIRLELDLPPELPLVYADPELLEQVLANLLDNAIKYSPPGgTITISARREGDGVRISVS 170
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2737555188 449 DTGIGMDQDTVSRIFRPFERLSSEANAEGFGLGLPITKGLVKLLGGSIDVESKIGHGSTFRVSLPLAVS 517
Cdd:COG2205   171 DNGPGIPEEELERIFERFYRGDNSRGEGGTGLGLAIVKRIVEAHGGTIWVESEPGGGTTFTVTLPLAES 239
WalK COG5002
Sensor histidine kinase WalK [Signal transduction mechanisms];
172-515 1.36e-50

Sensor histidine kinase WalK [Signal transduction mechanisms];


Pssm-ID: 444026 [Multi-domain]  Cd Length: 390  Bit Score: 182.06  E-value: 1.36e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188 172 TVQVPASSDKLRSLNEQLIALQAERIRNMENYTDSLRIRNRELNRKLFALLGNISDHAQAAFRDREEQIAQAHQRSTSII 251
Cdd:COG5002    40 LLLLLLLLLLLLLALLLLLLLLLLLLLALLLLLLLLLLLLALALLLLALLLLLLLLLLLLALLILLLLLALLILLAALLL 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188 252 TGLIIAAILLLVFSYLIIQKHLKRDSLLRKKMEGVIDRNNELLETRKNVILTISHDIRGPLNIIYGYVELAKD--TRDRK 329
Cdd:COG5002   120 LLSELLLLLLLLGRLSLRLSALLLGLLLLAAVERDITELERLEQMRREFVANVSHELRTPLTSIRGYLELLLDgaADDPE 199
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188 330 RRNHHLENIETECKHILHLLNNLLDVYRLNESKETCNNVPFNLNDLLERIVTGFSHIANNKGIIFHHDSQNTDVVLCGDM 409
Cdd:COG5002   200 ERREYLEIILEEAERLSRLVNDLLDLSRLESGELKLEKEPVDLAELLEEVVEELRPLAEEKGIELELDLPEDPLLVLGDP 279
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188 410 DRISQIIDNLLTNAVKFTNAG-MIQFNVRYENGMLYIEIKDTGIGMDQDTVSRIFRPFERLSSEANAE--GFGLGLPITK 486
Cdd:COG5002   280 DRLEQVLTNLLDNAIKYTPEGgTITVSLREEDDQVRISVRDTGIGIPEEDLPRIFERFYRVDKSRSREtgGTGLGLAIVK 359
                         330       340
                  ....*....|....*....|....*....
gi 2737555188 487 GLVKLLGGSIDVESKIGHGSTFRVSLPLA 515
Cdd:COG5002   360 HIVEAHGGRIWVESEPGKGTTFTITLPLA 388
PRK11091 PRK11091
aerobic respiration control sensor protein ArcB; Provisional
301-715 1.64e-48

aerobic respiration control sensor protein ArcB; Provisional


Pssm-ID: 236842 [Multi-domain]  Cd Length: 779  Bit Score: 183.99  E-value: 1.64e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188 301 ILTISHDIRGPLNIIYGYVELAKDTRDRKRRNHHLENIETECKHILHLLNNLLDVYRLNESKETCNNVPFNLNDLLERIV 380
Cdd:PRK11091  287 ISTISHELRTPLNGIVGLSRILLDTELTAEQRKYLKTIHVSAITLGNIFNDIIDMDKMERRKLQLDNQPIDFTDFLADLE 366
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188 381 TGFSHIANNKGIIFHHDSQNT-DVVLCGDMDRISQIIDNLLTNAVKFTNAGMIQFNVRYENG-MLYIEIKDTGIGMDQDT 458
Cdd:PRK11091  367 NLSGLQAEQKGLRFDLEPLLPlPHKVITDGTRLRQILWNLISNAVKFTQQGGVTVRVRYEEGdMLTFEVEDSGIGIPEDE 446
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188 459 VSRIFRPFERLSSEAN---AEGFGLGLPITKGLVKLLGGSIDVESKIGHGSTFRVSLPLAVSNEKINSEasaVPQDRLPL 535
Cdd:PRK11091  447 LDKIFAMYYQVKDSHGgkpATGTGIGLAVSKRLAQAMGGDITVTSEEGKGSCFTLTIHAPAVAEEVEDA---FDEDDMPL 523
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188 536 PQ-RVLVIDNDTLQLEIAKEMLERNGVSCTTCSNAKELVNEMRRQDYDLLLSDIQMPETNGFEILALLRKSSiGNSHTIP 614
Cdd:PRK11091  524 PAlNILLVEDIELNVIVARSVLEKLGNSVDVAMTGKEALEMFDPDEYDLVLLDIQLPDMTGLDIARELRERY-PREDLPP 602
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188 615 IVAMTARGEGEKEAFIKGGFTDSIHKPFSMRELLDMVSSVVSRDVEESHTP---DFATFTADVLDKrELLRTF------- 684
Cdd:PRK11091  603 LVALTANVLKDKKEYLDAGMDDVLSKPLSVPALTAMIKKFWDTQDDEESTVtteESSKANEALLDI-PMLEQYvelvgpk 681
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|
gi 2737555188 685 -IIQS----EQNM----ADLQSAIKTGDIEKLHDIAHEIK 715
Cdd:PRK11091  682 lITDSlavfEKMMpgylSVLDSNLTARDQKGIVEEAHKIK 721
PRK15347 PRK15347
two component system sensor kinase;
292-715 4.27e-40

two component system sensor kinase;


Pssm-ID: 237951 [Multi-domain]  Cd Length: 921  Bit Score: 159.04  E-value: 4.27e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188 292 ELLETRKNVILT-ISHDIRGPLNIIYGYVELakdtrdrkrrnhhLENIETECKHIlhllnnlldvyRLNESKETC-NNVP 369
Cdd:PRK15347  392 EQANKRKSEHLTtISHEIRTPLNGVLGALEL-------------LQNTPLTAEQM-----------DLADTARQCtLSLL 447
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188 370 FNLNDLLErivtgFSHI----------------------------ANNKGIIFHhDSQNTDVVLCGDMD--RISQIIDNL 419
Cdd:PRK15347  448 AIINNLLD-----FSRIesgqmtlsleetallplldqamltiqgpAQSKSLTLR-TFVGAHVPLYLHLDslRLRQILVNL 521
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188 420 LTNAVKFTNAGMIQFNVRYENGMLYIEIKDTGIGMDQDTVSRIFRPFerLSSEANAEGFGLGLPITKGLVKLLGGSIDVE 499
Cdd:PRK15347  522 LGNAVKFTETGGIRLRVKRHEQQLCFTVEDTGCGIDIQQQQQIFTPF--YQADTHSQGTGLGLTIASSLAKMMGGELTLF 599
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188 500 SKIGHGSTFRVSLPLA--------------------------------------VSNE-------------KINSEASAV 528
Cdd:PRK15347  600 STPGVGSCFSLVLPLNeyappeplkgelsaplalhrqlsawgitcqpghqnpalLDPElaylpgrlydllqQIIQGAPNE 679
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188 529 PQDRLPLPQ---RVLVIDNDTLQLEIAKEMLERNGVSCTTCSNAKELVNEMRRQDYDLLLSDIQMPETNGFEILALLRKS 605
Cdd:PRK15347  680 PVINLPLQPwqlQILLVDDVETNRDIIGMMLVELGQQVTTAASGTEALELGRQHRFDLVLMDIRMPGLDGLETTQLWRDD 759
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188 606 SIGNSHTIPIVAMTARGE-GEKEAFIKGGFTDSIHKPFSMRELLDMVSSVVS----RDVE-----ESHTPDFATFTADVL 675
Cdd:PRK15347  760 PNNLDPDCMIVALTANAApEEIHRCKKAGMNHYLTKPVTLAQLARALELAAEyqllRGIElspqdSSCSPLLDTDDMALN 839
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|.
gi 2737555188 676 DK-RELLRTFIIQSEQNMADLqsaiktgdiEKLHDIAHEIK 715
Cdd:PRK15347  840 SKlYQSLLLLLAQIEQAVENQ---------EVLSQLLHTLK 871
COG4251 COG4251
Bacteriophytochrome (light-regulated signal transduction histidine kinase) [Signal ...
26-515 2.16e-35

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


Pssm-ID: 443393 [Multi-domain]  Cd Length: 503  Bit Score: 141.08  E-value: 2.16e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188  26 AAILFHEHARLRKIEADTYEIRQARRDISEIHRNITVLASLGESVIAWEDEDYHAYQTRRLRVDSLLQMLQTNHSYIFGL 105
Cdd:COG4251     8 LLLLLLLLLLLLLLLLLLLVLLLALALLLLLALLVLLLLLIRLLLLLLLSLLALLLLLLLLLLLLLVLAALALLLLLLLL 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188 106 SQIDTLQQLLADKETHLHQIMQVFHRQDKADSLLVNHLPEAARQATQTRTVVQKKKGIAGWFGGKETVQVPASSDKLRSL 185
Cdd:COG4251    88 ELALVLLALLLVLLLLLALLLLLALLLLLELLLLLLALLLLLLLLALLLLEELALLRLALALLLLLLLLLLLLLLLLALI 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188 186 NEQLIALQAERIRNMENYTDSLRIRNRELNRKLFALLGNISDHAQAAFRDREEQIAQAHQRSTSIITGLIIAAILLLVFS 265
Cdd:COG4251   168 LALLLAALAELELLLLLLLVLLLLLLLLLLLLLLLLRLLLELLLLLEAELLLSLGGGLGLLLLLLLLLVLLLLLILLLLL 247
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188 266 YLIIQKHLKRDSLLRKKMEGVIDRNNELleTRKNVIL-----TISHDIRGPLNIIYGYVE-LAKDTRDR--KRRNHHLEN 337
Cdd:COG4251   248 LILVLELLELRLELEELEEELEERTAEL--ERSNEELeqfayVASHDLREPLRKISGFSQlLEEDYGDKldEEGREYLER 325
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188 338 IETECKhilhllnnlldvyRLNE-----------SKETCNNVPFNLNDLLERIVTGFSHIANNKGIIFHHDSqntDVVLC 406
Cdd:COG4251   326 IRDAAE-------------RMQAliddllaysrvGRQELEFEPVDLNELLEEVLEDLEPRIEERGAEIEVGP---LPTVR 389
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188 407 GDMDRISQIIDNLLTNAVKFTNAGM---IQFNVRYENGMLYIEIKDTGIGMDQDTVSRIFRPFERLSSEANAEGFGLGLP 483
Cdd:COG4251   390 GDPTLLRQVFQNLISNAIKYSRPGEpprIEIGAEREGGEWVFSVRDNGIGIDPEYAEKIFEIFQRLHSRDEYEGTGIGLA 469
                         490       500       510
                  ....*....|....*....|....*....|..
gi 2737555188 484 ITKGLVKLLGGSIDVESKIGHGSTFRVSLPLA 515
Cdd:COG4251   470 IVKKIVERHGGRIWVESEPGEGATFYFTLPKA 501
COG4191 COG4191
Signal transduction histidine kinase regulating C4-dicarboxylate transport system [Signal ...
182-515 1.19e-33

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


Pssm-ID: 443345 [Multi-domain]  Cd Length: 361  Bit Score: 133.00  E-value: 1.19e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188 182 LRSLNEQLIALQAERIRNMENYTDSLRIRNRELNRKLFALLGNISDHAQAAFRDREEQIAQAHQRSTSIITGLIIAAILL 261
Cdd:COG4191    15 LRALALALALLLLLLLLLLALLLLLLALLLALLALLLLLLLLLLLLLLELLLLLLALLGGLLRLLLLLGLLLLLLLEALL 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188 262 LVFSYLIIQKHLKRDSLLRKKMEGVIDRNNELLETRKNVILT------------ISHDIRGPLNIIYGYVELAK----DT 325
Cdd:COG4191    95 LLLLAALDAEENAELEELERDITELERAEEELRELQEQLVQSeklaalgelaagIAHEINNPLAAILGNAELLRrrleDE 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188 326 RDRKRRNHHLENIETECKHILHLLNNLLDVYRLNESKETcnnvPFNLNDLLERIVTGFSHIANNKGIIFHHDSQNTDVVL 405
Cdd:COG4191   175 PDPEELREALERILEGAERAAEIVRSLRAFSRRDEEERE----PVDLNELIDEALELLRPRLKARGIEVELDLPPDLPPV 250
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188 406 CGDMDRISQIIDNLLTN---AVKFTNAGMIQFNVRYENGMLYIEIKDTGIGMDQDTVSRIFRPFerLSSEANAEGFGLGL 482
Cdd:COG4191   251 LGDPGQLEQVLLNLLINaidAMEEGEGGRITISTRREGDYVVISVRDNGPGIPPEVLERIFEPF--FTTKPVGKGTGLGL 328
                         330       340       350
                  ....*....|....*....|....*....|...
gi 2737555188 483 PITKGLVKLLGGSIDVESKIGHGSTFRVSLPLA 515
Cdd:COG4191   329 SISYGIVEKHGGRIEVESEPGGGTTFTITLPLA 361
PRK09959 PRK09959
acid-sensing system histidine kinase EvgS;
287-766 2.70e-33

acid-sensing system histidine kinase EvgS;


Pssm-ID: 182169 [Multi-domain]  Cd Length: 1197  Bit Score: 138.33  E-value: 2.70e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188  287 IDRNNELLET--RKNVILTISHDIRGPLNIIYGYVELAKDT-RDRKRRNHHLENIETECKHILHLLNNLLDVYRLNESKE 363
Cdd:PRK09959   700 VERNKAINATvaKSQFLATMSHEIRTPISSIMGFLELLSGSgLSKEQRVEAISLAYATGQSLLGLIGEILDVDKIESGNY 779
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188  364 TCNNVPFNLNDLLERIVTGFSHIANNKGIIFHHDSQNTDVVLCG-DMDRISQIIDNLLTNAVKFTNAGMIQF-----NVR 437
Cdd:PRK09959   780 QLQPQWVDIPTLVQNTCHSFGAIAASKSIALSCSSTFPDHYLVKiDPQAFKQVLSNLLSNALKFTTEGAVKIttslgHID 859
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188  438 YENGMLYIEIKDTGIGMDQDTVSRIFRPFERLSSEANAEGFGLGLPITKGLVKLLGGSIDVESKIGHGSTFRVSLPLAVS 517
Cdd:PRK09959   860 DNHAVIKMTIMDSGSGLSQEEQQQLFKRYSQTSAGRQQTGSGLGLMICKELIKNMQGDLSLESHPGIGTTFTITIPVEIS 939
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188  518 NEKINSEASAVPQDRLPLPQRVLVIDNDTLQLEIAKEMLERNGVSCTTCSNAKELVNEMRRQDYDLLLSDIQMPETNGFE 597
Cdd:PRK09959   940 QQVATVEAKAEQPITLPEKLSILIADDHPTNRLLLKRQLNLLGYDVDEATDGVQALHKVSMQHYDLLITDVNMPNMDGFE 1019
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188  598 ILALLRKssigNSHTIPIVAMTARGEG-EKEAFIKGGFTDSIHKPFSmrelLDMVSSVVSRDVEESH-TPDFATFTADVL 675
Cdd:PRK09959  1020 LTRKLRE----QNSSLPIWGLTANAQAnEREKGLSCGMNLCLFKPLT----LDVLKTHLSQLHQVAHiAPQYRHLDIEAL 1091
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188  676 DK---------RELLRTFIIQSEQNMADLQSAIKTGDIEKLHDIAHEIKPSLELLRADApLVKLRTTLNDSACDMNTVNE 746
Cdd:PRK09959  1092 KNntandlqlmQEILMTFQHETHKDLPAAFHALEAGDNRTFHQCIHRIHGAANILNLQK-LINISHQLEITPVSDDSKPE 1170
                          490       500
                   ....*....|....*....|
gi 2737555188  747 QVKLLiGHISGLITEAEKEI 766
Cdd:PRK09959  1171 ILQLL-NSVKEHIAELDQEI 1189
HATPase_EvgS-ArcB-TorS-like cd16922
Histidine kinase-like ATPase domain of two-component sensor histidine kinases, many are hybrid ...
414-514 9.69e-33

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: 122.22  E-value: 9.69e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188 414 QIIDNLLTNAVKFTNAGMIQFNVRYEN-----GMLYIEIKDTGIGMDQDTVSRIFRPFERLSSEA--NAEGFGLGLPITK 486
Cdd:cd16922     3 QILLNLLGNAIKFTEEGEVTLRVSLEEeeedgVQLRFSVEDTGIGIPEEQQARLFEPFSQADSSTtrKYGGTGLGLAISK 82
                          90       100
                  ....*....|....*....|....*...
gi 2737555188 487 GLVKLLGGSIDVESKIGHGSTFRVSLPL 514
Cdd:cd16922    83 KLVELMGGDISVESEPGQGSTFTFTLPL 110
HATPase_c smart00387
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.
407-515 5.53e-32

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


Pssm-ID: 214643 [Multi-domain]  Cd Length: 111  Bit Score: 120.06  E-value: 5.53e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188  407 GDMDRISQIIDNLLTNAVKFTNA-GMIQFNVRYENGMLYIEIKDTGIGMDQDTVSRIFRPFERLSSEA-NAEGFGLGLPI 484
Cdd:smart00387   1 GDPDRLRQVLSNLLDNAIKYTPEgGRITVTLERDGDHVEITVEDNGPGIPPEDLEKIFEPFFRTDKRSrKIGGTGLGLSI 80
                           90       100       110
                   ....*....|....*....|....*....|.
gi 2737555188  485 TKGLVKLLGGSIDVESKIGHGSTFRVSLPLA 515
Cdd:smart00387  81 VKKLVELHGGEISVESEPGGGTTFTITLPLE 111
PRK11107 PRK11107
hybrid sensory histidine kinase BarA; Provisional
367-648 1.34e-31

hybrid sensory histidine kinase BarA; Provisional


Pssm-ID: 236848 [Multi-domain]  Cd Length: 919  Bit Score: 132.67  E-value: 1.34e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188 367 NVPFNLNDLLERIVTGFSHIANNKGIIFHHDSQNtDV--VLCGDMDRISQIIDNLLTNAVKFTNAGMIQFNV-----RYE 439
Cdd:PRK11107  363 NIPFSLRETLDEVVTLLAHSAHEKGLELTLNIDP-DVpdNVIGDPLRLQQIITNLVGNAIKFTESGNIDILVelralSNT 441
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188 440 NGMLYIEIKDTGIGMDQDTVSRIFRPFerlsSEANAE------GFGLGLPITKGLVKLLGGSIDVESKIGHGSTFRVSLP 513
Cdd:PRK11107  442 KVQLEVQIRDTGIGISERQQSQLFQAF----RQADASisrrhgGTGLGLVITQKLVNEMGGDISFHSQPNRGSTFWFHLP 517
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188 514 LAVSNEKINSEAsavPQDRLpLPQRVLVIDNDTLQLEIAKEMLERNGVSCTTCSNAKELvnEMRRQDYDLLLsdIQMPET 593
Cdd:PRK11107  518 LDLNPNPIIDGL---PTDCL-AGKRLLYVEPNSAAAQATLDILSETPLEVTYSPTLSQL--PEAHYDILLLG--LPVTFR 589
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2737555188 594 NGFEILALLRKSSIGNSHTIpIVAMTARGEGEKEAFIKGGFTDSIHKPFSMRELL 648
Cdd:PRK11107  590 EPLTMLHERLAKAKSMTDFL-ILALPCHEQVLAEQLKQDGADACLSKPLSHTRLL 643
NtrY COG5000
Signal transduction histidine kinase NtrY involved in nitrogen fixation and metabolism ...
207-519 2.70e-30

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: 124.30  E-value: 2.70e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188 207 LRIRNRELNRKLFALLGNISDHAQAAFRDREEQIAQAHQRSTSIITGLIIAAILLLVFSYLIiqkhlkrdsllrkkmegV 286
Cdd:COG5000   123 LGIPLEELIGKPLEELLPELDLAELLREALERGWQEEIELTRDGRRTLLVRASPLRDDGYVI-----------------V 185
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188 287 IDRNNELLETRKN-----VILTISHDIRGPLNIIYGYVEL------AKDTRDRKRRNHHLENIETECKHILHLLNNLLDV 355
Cdd:COG5000   186 FDDITELLRAERLaawgeLARRIAHEIKNPLTPIQLSAERlrrklaDKLEEDREDLERALDTIIRQVDRLKRIVDEFLDF 265
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188 356 YRLNESKetcnNVPFNLNDLLERIVTGFSHIANNKGIIFHHDSQNTDVVLCGDMDRISQIIDNLLTNAVKFT-NAGMIQF 434
Cdd:COG5000   266 ARLPEPQ----LEPVDLNELLREVLALYEPALKEKDIRLELDLDPDLPEVLADRDQLEQVLINLLKNAIEAIeEGGEIEV 341
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188 435 NVRYENGMLYIEIKDTGIGMDQDTVSRIFRPFErlSSeaNAEGFGLGLPITKGLVKLLGGSIDVESKIGHGSTFRVSLPL 514
Cdd:COG5000   342 STRREDGRVRIEVSDNGPGIPEEVLERIFEPFF--TT--KPKGTGLGLAIVKKIVEEHGGTIELESRPGGGTTFTIRLPL 417

                  ....*
gi 2737555188 515 AVSNE 519
Cdd:COG5000   418 AEEAE 422
NtrB COG3852
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms];
260-519 4.23e-30

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


Pssm-ID: 443061 [Multi-domain]  Cd Length: 361  Bit Score: 122.65  E-value: 4.23e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188 260 LLLVFSYLIIQKHLKRDSLLRKKMEGVIdrnnELLETrknviltISHDIRGPLNIIYGYVELAKDTRDRKRRNHHLENIE 339
Cdd:COG3852   109 VLLVLRDITERKRLERELRRAEKLAAVG----ELAAG-------LAHEIRNPLTGIRGAAQLLERELPDDELREYTQLII 177
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188 340 TECKhilhllnnlldvyRLNE--------SKETCNNV-PFNLNDLLERIVTGFSH-IANNKGIIFHHDSQNTDVvlCGDM 409
Cdd:COG3852   178 EEAD-------------RLNNlvdrllsfSRPRPPERePVNLHEVLERVLELLRAeAPKNIRIVRDYDPSLPEV--LGDP 242
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188 410 DRISQIIDNLLTNAVK-FTNAGMIQFNVRYENG----------MLYIEIKDTGIGMDQDTVSRIFRPFerLSSEANaeGF 478
Cdd:COG3852   243 DQLIQVLLNLVRNAAEaMPEGGTITIRTRVERQvtlgglrprlYVRIEVIDNGPGIPEEILDRIFEPF--FTTKEK--GT 318
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 2737555188 479 GLGLPITKGLVKLLGGSIDVESKIGHGSTFRVSLPLAVSNE 519
Cdd:COG3852   319 GLGLAIVQKIVEQHGGTIEVESEPGKGTTFRIYLPLEQAEE 359
CheY COG0784
CheY-like REC (receiver) domain, includes chemotaxis protein CheY and sporulation regulator ...
538-658 2.42e-29

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: 113.02  E-value: 2.42e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188 538 RVLVIDNDTLQLEIAKEMLERNGVSCTTCSNAKELVNEMRRQDYDLLLSDIQMPETNGFEILALLRKSSIGnsHTIPIVA 617
Cdd:COG0784     7 RILVVDDNPDNRELLRRLLERLGYEVTTAEDGAEALELLRAGPPDLILLDINMPGMDGLELLRRIRALPRL--PDIPIIA 84
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 2737555188 618 MTARG-EGEKEAFIKGGFTDSIHKPFSMRELLDMVSSVVSRD 658
Cdd:COG0784    85 LTAYAdEEDRERALEAGADDYLTKPVDPEELLEALRRLLARA 126
PRK11466 PRK11466
hybrid sensory histidine kinase TorS; Provisional
304-717 3.66e-29

hybrid sensory histidine kinase TorS; Provisional


Pssm-ID: 236914 [Multi-domain]  Cd Length: 914  Bit Score: 124.63  E-value: 3.66e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188 304 ISHDIRGPLNIIYGYVELAKDTRDRKRRNHHLENIETECKHILHLLNNLLDvYRLNESKET---CNNVPFNLNDLLERIV 380
Cdd:PRK11466  451 MSHEIRTPLYGILGTAQLLADNPALNAQRDDLRAITDSGESLLTILNDILD-YSAIEAGGKnvsVSDEPFEPRPLLESTL 529
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188 381 TGFSHIANNKGIIFHHD-SQNTDVVLCGDMDRISQIIDNLLTNAVKFTNAGMIQFNVRYENGMLYIEIKDTGIGMDQDTV 459
Cdd:PRK11466  530 QLMSGRVKGRPIRLATDiADDLPTALMGDPRRIRQVITNLLSNALRFTDEGSIVLRSRTDGEQWLVEVEDSGCGIDPAKL 609
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188 460 SRIFRPFERLSseANAEGFGLGLPITKGLVKLLGGSIDVESKIGHGSTFRVSLPLAVSNEKI-NSEASAVPQDRLplpqR 538
Cdd:PRK11466  610 AEIFQPFVQVS--GKRGGTGLGLTISSRLAQAMGGELSATSTPEVGSCFCLRLPLRVATAPVpKTVNQAVRLDGL----R 683
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188 539 VLVIDNDTLQLEIAKEMLERNGVSCTTCSNAKELVNEMRRQD-YDLLLSDIQMPETNGFEILALLRKS-----SIGNSHT 612
Cdd:PRK11466  684 LLLIEDNPLTQRITAEMLNTSGAQVVAVGNAAQALETLQNSEpFAAALVDFDLPDYDGITLARQLAQQypslvLIGFSAH 763
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188 613 IPIVAMTARgegekeafIKGGFTDSIHKPFSMRELLDMVSSVVsRDVEESHTP--------DFATFTADVLdkRELLRTF 684
Cdd:PRK11466  764 VIDETLRQR--------TSSLFRGIIPKPVPREVLGQLLAHYL-QLQVNNDQPldvsqlneDAALMGTEKI--HEWLALF 832
                         410       420       430
                  ....*....|....*....|....*....|...
gi 2737555188 685 IIQSEQNMADLQSAIKTGDIEKLHDIAHEIKPS 717
Cdd:PRK11466  833 KQHALPLLDEIDIARASQDSEKIKRAAHQLKSS 865
REC_hyHK_CKI1_RcsC-like cd17546
phosphoacceptor receiver (REC) domain of hybrid sensor histidine kinases/response regulators ...
539-651 5.01e-27

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: 106.01  E-value: 5.01e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188 539 VLVIDNDTLQLEIAKEMLERNGVSCTTCSNAKELVNEMRRQDYDLLLSDIQMPETNGFEILALLRKSSIGNSHTiPIVAM 618
Cdd:cd17546     1 VLVVDDNPVNRKVLKKLLEKLGYEVDVAENGQEALELLKEEPFDLVLMDLQMPVMDGLEATRRIRELEGGGRRT-PIIAL 79
                          90       100       110
                  ....*....|....*....|....*....|....
gi 2737555188 619 TARG-EGEKEAFIKGGFTDSIHKPFSMRELLDMV 651
Cdd:cd17546    80 TANAlEEDREKCLEAGMDDYLSKPVKLDQLKEVL 113
HATPase_c pfam02518
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the ...
407-515 5.77e-27

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


Pssm-ID: 460579 [Multi-domain]  Cd Length: 109  Bit Score: 105.53  E-value: 5.77e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188 407 GDMDRISQIIDNLLTNAVKFT-NAGMIQFNVRyENGMLYIEIKDTGIGMDQDTVSRIFRPFERLSSEaNAEGFGLGLPIT 485
Cdd:pfam02518   1 GDELRLRQVLSNLLDNALKHAaKAGEITVTLS-EGGELTLTVEDNGIGIPPEDLPRIFEPFSTADKR-GGGGTGLGLSIV 78
                          90       100       110
                  ....*....|....*....|....*....|
gi 2737555188 486 KGLVKLLGGSIDVESKIGHGSTFRVSLPLA 515
Cdd:pfam02518  79 RKLVELLGGTITVESEPGGGTTVTLTLPLA 108
OmpR COG0745
DNA-binding response regulator, OmpR family, contains REC and winged-helix (wHTH) domain ...
536-657 2.09e-24

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


Pssm-ID: 440508 [Multi-domain]  Cd Length: 204  Bit Score: 101.57  E-value: 2.09e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188 536 PQRVLVIDNDTLQLEIAKEMLERNGVSCTTCSNAKELVNEMRRQDYDLLLSDIQMPETNGFEILALLRKssigNSHTIPI 615
Cdd:COG0745     1 MPRILVVEDDPDIRELLADALEREGYEVDTAADGEEALELLEEERPDLILLDLMLPGMDGLEVCRRLRA----RPSDIPI 76
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 2737555188 616 VAMTARG-EGEKEAFIKGGFTDSIHKPFSMRELLDMVSSVVSR 657
Cdd:COG0745    77 IMLTARDdEEDRVRGLEAGADDYLTKPFDPEELLARIRALLRR 119
REC_typeB_ARR-like cd17584
phosphoacceptor receiver (REC) domain of type B Arabidopsis response regulators (ARRs) and ...
539-650 4.78e-24

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: 97.70  E-value: 4.78e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188 539 VLVIDNDTLQLEIAKEMLERNGVSCTTCSNAKELVNEMR--RQDYDLLLSDIQMPETNGFEILALLRKSSignshTIPIV 616
Cdd:cd17584     1 VLVVDDDPTCLAILKRMLLRCGYQVTTCTDAEEALSMLRenKDEFDLVITDVHMPDMDGFEFLELIRLEM-----DLPVI 75
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2737555188 617 AMTARGEGEK-EAFIKGGFTDSIHKPFSMRELLDM 650
Cdd:cd17584    76 MMSADGSTSTvMKGLAHGACDYLLKPVSIEDLKNI 110
KinE COG5809
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome ...
259-519 5.99e-24

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: 106.21  E-value: 5.99e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188 259 ILLLVFSYLIIQKHLKRDSLL--------RKKMEgvidrnnELLET--RKNVI----LTISHDIRGPLNIIYGYVELAKD 324
Cdd:COG5809   225 WRLLEASGAPIKKNGEVDGIViifrditeRKKLE-------ELLRKseKLSVVgelaAGIAHEIRNPLTSLKGFIQLLKD 297
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188 325 TRDRKRRnHHLENIETECKhilhllnnlldvyRLNE--------SK-ETCNNVPFNLNDLLERIVTGFSHIANNKGIIFH 395
Cdd:COG5809   298 TIDEEQK-TYLDIMLSELD-------------RIESiiseflvlAKpQAIKYEPKDLNTLIEEVIPLLQPQALLKNVQIE 363
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188 396 HDSQNTDVVLCGDMDRISQIIDNLLTNAVKFT-NAGMIQFNVRY-ENGMLYIEIKDTGIGMDQDTVSRIFRPFERLSSEa 473
Cdd:COG5809   364 LELEDDIPDILGDENQLKQVFINLLKNAIEAMpEGGNITIETKAeDDDKVVISVTDEGCGIPEERLKKLGEPFYTTKEK- 442
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 2737555188 474 naeGFGLGLPITKGLVKLLGGSIDVESKIGHGSTFRVSLPLAVSNE 519
Cdd:COG5809   443 ---GTGLGLMVSYKIIEEHGGKITVESEVGKGTTFSITLPIKLSEQ 485
PleD COG3706
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate ...
536-655 1.19e-23

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: 98.44  E-value: 1.19e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188 536 PQRVLVIDNDTLQLEIAKEMLERNGVSCTTCSNAKELVNEMRRQDYDLLLSDIQMPETNGFEILALLRKSSigNSHTIPI 615
Cdd:COG3706     1 PARILVVDDDPTNRKLLRRLLEAAGYEVVEAADGEEALELLQEHRPDLILLDLEMPDMDGLELCRRLRADP--RTADIPI 78
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 2737555188 616 VAMTARGEGE-KEAFIKGGFTDSIHKPFSMRELLDMVSSVV 655
Cdd:COG3706    79 IFLTALDDEEdRARALEAGADDYLTKPFDPEELLARVDLVA 119
PRK10841 PRK10841
two-component system sensor histidine kinase RcsC;
403-583 6.37e-23

two-component system sensor histidine kinase RcsC;


Pssm-ID: 182772 [Multi-domain]  Cd Length: 924  Bit Score: 104.67  E-value: 6.37e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188 403 VVLCGDMDRISQIIDNLLTNAVKFTNAGMIQFNVRYENGMLYIEIKDTGIGMDQDTVSRIFRPFERLSS--EANAEGFGL 480
Cdd:PRK10841  554 VALNGDPMRLQQVISNLLSNAIKFTDTGCIVLHVRVDGDYLSFRVRDTGVGIPAKEVVRLFDPFFQVGTgvQRNFQGTGL 633
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188 481 GLPITKGLVKLLGGSIDVESKIGHGSTFRVSLPLAVSnekinSEASAVPQDRLPLPQRVLVIDNDTLQlEIAKEMLERNG 560
Cdd:PRK10841  634 GLAICEKLINMMDGDISVDSEPGMGSQFTIRIPLYGA-----QYPQKKGVEGLQGKRCWLAVRNASLE-QFLETLLQRSG 707
                         170       180
                  ....*....|....*....|...
gi 2737555188 561 VSCTTCSNAKELVNEMRRQDYDL 583
Cdd:PRK10841  708 IQVQRYEGQEPTPEDVLITDDPV 730
KinB COG5806
Sporulation sensor histidine kinase B [Cell cycle control, cell division, chromosome ...
250-515 2.33e-22

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: 100.33  E-value: 2.33e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188 250 IITGLIIAAILLLVFSYLIiqKHLKRDSLLRKKMegvidRNNELLETRKNVILTISHDIRGPLNIIYGYVELAK--DTRD 327
Cdd:COG5806   161 ILYFIIIQLLAMLIAVYLI--ENLIENILLRKEL-----QRAEKLEVVSELAASIAHEVRNPLTVVRGFIQLLQepELSD 233
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188 328 RKRRNHH---------LENIETEckhilhllnnlldvYrLNESKETCNN-VPFNLNDLLERIVTGFSHIANNKGIIFHHD 397
Cdd:COG5806   234 EKRKQYIrialeeldrAEAIITD--------------Y-LTFAKPQPEKlEKIDVSEELEHVIDVLSPYANMNNVEIQTE 298
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188 398 SQNTdVVLCGDMDRISQIIDNLLTNAVK-FTNAGMIQFNVRYENGMLYIEIKDTGIGMDQDTVSRIFRPFerLSSEanAE 476
Cdd:COG5806   299 LEPG-LYIEGDRQKLQQCLINIIKNGIEaMPNGGTLTIDVSIDKNKVIISIKDTGVGMTKEQLERLGEPY--FSTK--EK 373
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 2737555188 477 GFGLGLPITKGLVKLLGGSIDVESKIGHGSTFRVSLPLA 515
Cdd:COG5806   374 GTGLGTMVSYRIIEAMNGTIRVESEVGKGTTFTITLPLA 412
AtoC COG2204
DNA-binding transcriptional response regulator, NtrC family, contains REC, AAA-type ATPase, ...
536-657 2.44e-22

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: 100.42  E-value: 2.44e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188 536 PQRVLVIDNDTLQLEIAKEMLERNGVSCTTCSNAKELVNEMRRQDYDLLLSDIQMPETNGFEILALLRKssigNSHTIPI 615
Cdd:COG2204     2 MARILVVDDDPDIRRLLKELLERAGYEVETAASGEEALALLREEPPDLVLLDLRMPGMDGLELLRELRA----LDPDLPV 77
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 2737555188 616 VAMTARGEGEK-EAFIKGGFTDSIHKPFSMRELLDMVSSVVSR 657
Cdd:COG2204    78 ILLTGYGDVETaVEAIKAGAFDYLTKPFDLEELLAAVERALER 120
Response_reg pfam00072
Response regulator receiver domain; This domain receives the signal from the sensor partner in ...
539-651 8.04e-22

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: 91.06  E-value: 8.04e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188 539 VLVIDNDTLQLEIAKEMLERNGVSCTTCSNAKELVNEMRRQDYDLLLSDIQMPETNGFEILALLRKssigNSHTIPIVAM 618
Cdd:pfam00072   1 VLIVDDDPLIRELLRQLLEKEGYVVAEADDGKEALELLKEERPDLILLDINMPGMDGLELLKRIRR----RDPTTPVIIL 76
                          90       100       110
                  ....*....|....*....|....*....|....
gi 2737555188 619 TARGEGE-KEAFIKGGFTDSIHKPFSMRELLDMV 651
Cdd:pfam00072  77 TAHGDEDdAVEALEAGADDFLSKPFDPDELLAAI 110
RpfG COG3437
Response regulator c-di-GMP phosphodiesterase, RpfG family, contains REC and HD-GYP domains ...
532-657 4.54e-21

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: 92.54  E-value: 4.54e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188 532 RLPLPQRVLVIDNDTLQLEIAKEMLERNGVSCTTCSNAKELVNEMRRQDYDLLLSDIQMPETNGFEILALLRKSSigNSH 611
Cdd:COG3437     2 RTGQAPTVLIVDDDPENLELLRQLLRTLGYDVVTAESGEEALELLLEAPPDLILLDVRMPGMDGFELLRLLRADP--STR 79
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 2737555188 612 TIPIVAMTARGEGE-KEAFIKGGFTDSIHKPFSMRELLDMVSSVVSR 657
Cdd:COG3437    80 DIPVIFLTALADPEdRERALEAGADDYLTKPFDPEELLARVRNALEL 126
PRK13837 PRK13837
two-component system VirA-like sensor kinase;
304-647 5.44e-21

two-component system VirA-like sensor kinase;


Pssm-ID: 237526 [Multi-domain]  Cd Length: 828  Bit Score: 98.60  E-value: 5.44e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188 304 ISHDIRGPLNIIYGYVELAKDT-RDRKRRNHHLENIETECKHILHLLNNLLDVYRLNESketcNNVPFNLNDLLERIVTG 382
Cdd:PRK13837  457 IAHNFNNILGAILGYAEMALNKlARHSRAARYIDEIISAGARARLIIDQILAFGRKGER----NTKPFDLSELVTEIAPL 532
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188 383 FS-HIANNKGIIFHHDSQntDVVLCGDMDRISQIIDNLLTNAVK-FTNAGMIQFNVR---------YENGML----YIEI 447
Cdd:PRK13837  533 LRvSLPPGVELDFDQDQE--PAVVEGNPAELQQVLMNLCSNAAQaMDGAGRVDISLSraklrapkvLSHGVLppgrYVLL 610
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188 448 K--DTGIGMDQDTVSRIFRPF--ERlsseanAEGFGLGLPITKGLVKLLGGSIDVESKIGHGSTFRVSLPLAvSNEKINS 523
Cdd:PRK13837  611 RvsDTGAGIDEAVLPHIFEPFftTR------AGGTGLGLATVHGIVSAHAGYIDVQSTVGRGTRFDVYLPPS-SKVPVAP 683
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188 524 EASAVPQdRLPLP--QRVLVIDNDTLQLEIAKEMLERNG---VSCTTCSNAKELVNEmRRQDYDLLLsdIQMPETNGFEI 598
Cdd:PRK13837  684 QAFFGPG-PLPRGrgETVLLVEPDDATLERYEEKLAALGyepVGFSTLAAAIAWISK-GPERFDLVL--VDDRLLDEEQA 759
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*....
gi 2737555188 599 LALLRKSSIgnshTIPIVAMTARGEGEKEAFIKGGFTDSIHKPFSMREL 647
Cdd:PRK13837  760 AAALHAAAP----TLPIILGGNSKTMALSPDLLASVAEILAKPISSRTL 804
KinA COG5805
Sporulation sensor histidine kinase A (Stage II sporulation protein SpoIIF/SpoIIJ) [Cell cycle ...
303-514 3.68e-20

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: 94.41  E-value: 3.68e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188 303 TISHDIRGPLNIIYGYVELAKDTRDRKRrnHHLENIETECKHILHLLNNLldvyrLNESK-ETCNNVPFNLNDLLERIVT 381
Cdd:COG5805   293 GIAHEIRNPLTSIKGFLQLLQPGIEDKE--EYFDIMLSELDRIESIISEF-----LALAKpQAVNKEKENINELIQDVVT 365
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188 382 GFSHIANNKGIIFHHDSQNTDVVLCGDMDRISQIIDNLLTNAVK-FTNAGMIQFNVRYENGMLYIEIKDTGIGMDQDTVS 460
Cdd:COG5805   366 LLETEAILHNIQIRLELLDEDPFIYCDENQIKQVFINLIKNAIEaMPNGGTITIHTEEEDNSVIIRVIDEGIGIPEERLK 445
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2737555188 461 RIFRPFERLSSEanaeGFGLGLPITKGLVKLLGGSIDVESKIGHGSTFRVSLPL 514
Cdd:COG5805   446 KLGEPFFTTKEK----GTGLGLMVSYKIIENHNGTIDIDSKVGKGTTFTITLPL 495
PRK11360 PRK11360
two-component system sensor histidine kinase AtoS;
234-514 5.40e-20

two-component system sensor histidine kinase AtoS;


Pssm-ID: 236901 [Multi-domain]  Cd Length: 607  Bit Score: 94.65  E-value: 5.40e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188 234 RDREEQIAQahqrSTSII---TGLIIAAILLLvfsyliiqkhlkRDSLLRKKMEGVIDRNnELLETRKNVILTISHDIRG 310
Cdd:PRK11360  341 RDRTIELSV----STSLLhntHGEMIGALVIF------------SDLTERKRLQRRVARQ-ERLAALGELVAGVAHEIRN 403
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188 311 PLNIIYGYVELAKDTRDRKRRNHHLENIETECKHILHLLNNLLDVYRLNESKetcnNVPFNLNDLLERIVTGFSHIANNK 390
Cdd:PRK11360  404 PLTAIRGYVQIWRQQTSDPPSQEYLSVVLREVDRLNKVIDQLLEFSRPRESQ----WQPVSLNALVEEVLQLFQTAGVQA 479
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188 391 GIIFHHDSQNTDVVLCGDMDRISQIIDNLLTNAVKFTNA-GMIQFNVRYE-NGMLYIEIKDTGIGMDQDTVSRIFRPFer 468
Cdd:PRK11360  480 RVDFETELDNELPPIWADPELLKQVLLNILINAVQAISArGKIRIRTWQYsDGQVAVSIEDNGCGIDPELLKKIFDPF-- 557
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 2737555188 469 lsSEANAEGFGLGLPITKGLVKLLGGSIDVESKIGHGSTFRVSLPL 514
Cdd:PRK11360  558 --FTTKAKGTGLGLALSQRIINAHGGDIEVESEPGVGTTFTLYLPI 601
HATPase_AtoS-like cd16943
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
412-514 1.62e-19

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: 84.40  E-value: 1.62e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188 412 ISQIIDNLLTNAVKFTNA-GMIQFNVRYENGMLYIEIKDTGIGMDQDTVSRIFRPFerLSSEANAEGFGLGLPITKGLVK 490
Cdd:cd16943     4 LNQVLLNLLVNAAQAMEGrGRITIRTWAHVDQVLIEVEDTGSGIDPEILGRIFDPF--FTTKPVGEGTGLGLSLSYRIIQ 81
                          90       100
                  ....*....|....*....|....
gi 2737555188 491 LLGGSIDVESKIGHGSTFRVSLPL 514
Cdd:cd16943    82 KHGGTIRVASVPGGGTRFTIILPI 105
REC cd00156
phosphoacceptor receiver (REC) domain of response regulators (RRs) and pseudo response ...
540-641 3.09e-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: 83.43  E-value: 3.09e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188 540 LVIDNDTLQLEIAKEMLERNGVSCTTCSNAKELVNEMRRQDYDLLLSDIQMPETNGFEILALLRKssigNSHTIPIVAMT 619
Cdd:cd00156     1 LIVDDDPAIRELLKSLLEREGYEVDTAADGEEALELLREERPDLVLLDLMMPGMDGLELLRKLRE----LPPDIPVIVLT 76
                          90       100
                  ....*....|....*....|...
gi 2737555188 620 ARGEGE-KEAFIKGGFTDSIHKP 641
Cdd:cd00156    77 AKADEEdAVRALELGADDYLVKP 99
PRK13557 PRK13557
histidine kinase; Provisional
445-654 1.02e-18

histidine kinase; Provisional


Pssm-ID: 237425 [Multi-domain]  Cd Length: 540  Bit Score: 90.50  E-value: 1.02e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188 445 IEIKDTGIGMDQDTVSRIFRPFerLSSEANAEGFGLGLPITKGLVKLLGGSIDVESKIGHGSTFRVSLPLAVSNEKINSE 524
Cdd:PRK13557  327 IAVTDTGSGMPPEILARVMDPF--FTTKEEGKGTGLGLSMVYGFAKQSGGAVRIYSEVGEGTTVRLYFPASDQAENPEQE 404
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188 525 ASAVPQDRlPLPQRVLVIDNDTLQLEIAKEMLERNGVSCTTCSNAKE---LVNEMRRqdYDLLLSDIQMP-ETNGFEILA 600
Cdd:PRK13557  405 PKARAIDR-GGTETILIVDDRPDVAELARMILEDFGYRTLVASNGREaleILDSHPE--VDLLFTDLIMPgGMNGVMLAR 481
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2737555188 601 LLRKSsignSHTIPIVAMTARGEGEKE-AFIKGGFTDSIHKPFSMRELLDMVSSV 654
Cdd:PRK13557  482 EARRR----QPKIKVLLTTGYAEASIErTDAGGSEFDILNKPYRRAELARRVRMV 532
HATPase_FilI-like cd16921
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
412-513 9.22e-18

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


Pssm-ID: 340398 [Multi-domain]  Cd Length: 105  Bit Score: 79.29  E-value: 9.22e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188 412 ISQIIDNLLTNAVKFTNAG---MIQFNVRYENGMLYIEIKDTGIGMDQDTVSRIFRPFERLSSEANAEGFGLGLPITKGL 488
Cdd:cd16921     1 LGQVLTNLLGNAIKFRRPRrppRIEVGAEDVGEEWTFYVRDNGIGIDPEYAEKVFGIFQRLHSREEYEGTGVGLAIVRKI 80
                          90       100
                  ....*....|....*....|....*
gi 2737555188 489 VKLLGGSIDVESKIGHGSTFRVSLP 513
Cdd:cd16921    81 IERHGGRIWLESEPGEGTTFYFTLP 105
HATPase_CpxA-like cd16949
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
412-514 3.21e-17

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: 77.75  E-value: 3.21e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188 412 ISQIIDNLLTNAVKFTNaGMIQFNVRYENGMLYIEIKDTGIGMDQDTVSRIFRPFERLSSEANAE--GFGLGLPITKGLV 489
Cdd:cd16949     1 LARALENVLRNALRYSP-SKILLDISQDGDQWTITITDDGPGVPEDQLEQIFLPFYRVDSARDREsgGTGLGLAIAERAI 79
                          90       100
                  ....*....|....*....|....*
gi 2737555188 490 KLLGGSIDVESKIGHGSTFRVSLPL 514
Cdd:cd16949    80 EQHGGKIKASNRKPGGLRVRIWLPA 104
REC_DivK-like cd17548
phosphoacceptor receiver (REC) domain of DivK and similar proteins; Caulobacter crescentus ...
538-653 7.73e-17

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: 76.81  E-value: 7.73e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188 538 RVLVIDNDTLQLEIAKEMLERNGVSCTTCSNAKELVNEMRRQDYDLLLSDIQMPETNGFEILALLRKSSigNSHTIPIVA 617
Cdd:cd17548     1 KILIVEDNPLNMKLARDLLESAGYEVLEAADGEEALEIARKEKPDLILMDIQLPGMDGLEATRLLKEDP--ATRDIPVIA 78
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2737555188 618 MTARG-EGEKEAFIKGGFTDSIHKPFSMRELLDMVSS 653
Cdd:cd17548    79 LTAYAmKGDREKILEAGCDGYISKPIDTREFLETVAK 115
CitB COG4565
DNA-binding response regulator DpiB of citrate/malate metabolism [Transcription, Signal ...
538-657 1.12e-16

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


Pssm-ID: 443622 [Multi-domain]  Cd Length: 138  Bit Score: 77.32  E-value: 1.12e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188 538 RVLVIDNDTLQLEIAKEMLERNG--VSCTTCSNAKELVNEMRRQDYDLLLSDIQMPETNGFEILALLRKssigNSHTIPI 615
Cdd:COG4565     5 RVLIVEDDPMVAELLRRYLERLPgfEVVGVASSGEEALALLAEHRPDLILLDIYLPDGDGLELLRELRA----RGPDVDV 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 2737555188 616 VAMTARGEGEK-EAFIKGGFTDSIHKPFSMRELLDMVSSVVSR 657
Cdd:COG4565    81 IVITAARDPETvREALRAGVVDYLIKPFTFERLREALERYLEY 123
REC_2_DhkD-like cd17580
second phosphoacceptor receiver (REC) domain of Dictyostelium discoideum hybrid signal ...
539-651 1.16e-16

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


Pssm-ID: 381118 [Multi-domain]  Cd Length: 112  Bit Score: 76.34  E-value: 1.16e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188 539 VLVIDNDTLQLEIAKEMLERNGVSCTTCSNAKELVNEMRRQDYDLLLSDIQMPETNGFEILALLRKssIGNSHTIPIVAM 618
Cdd:cd17580     1 ILVVDDNEDAAEMLALLLELEGAEVTTAHSGEEALEAAQRFRPDVILSDIGMPGMDGYELARRLRE--LPWLANTPAIAL 78
                          90       100       110
                  ....*....|....*....|....*....|....
gi 2737555188 619 TARGEGE-KEAFIKGGFTDSIHKPFSMRELLDMV 651
Cdd:cd17580    79 TGYGQPEdRERALEAGFDAHLVKPVDPDELIELI 112
PRK10364 PRK10364
two-component system sensor histidine kinase ZraS;
232-520 1.51e-16

two-component system sensor histidine kinase ZraS;


Pssm-ID: 236674 [Multi-domain]  Cd Length: 457  Bit Score: 82.91  E-value: 1.51e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188 232 AFRDREEQIAQAH-QRSTSIITGLIIAAILLLVFSYLIIQKHLKRDSLLRKKMegvidRNNELLETRKNVILTISHDIRG 310
Cdd:PRK10364  176 AFDASNLVSAQAReQRNTLIILFALATVLLASLLAFFWYRRYLRSRQLLQDEM-----KRKEKLVALGHLAAGVAHEIRN 250
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188 311 PLNIIYGYVELAKDTRDRKRRNHHLENIETecKHILHLLNNLLDVYRLNESKETCNNvPFNLNDLLERIVTGFSHIANNK 390
Cdd:PRK10364  251 PLSSIKGLAKYFAERAPAGGEAHQLAQVMA--KEADRLNRVVSELLELVKPTHLALQ-AVDLNDLINHSLQLVSQDANSR 327
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188 391 GIIFHHDSQNTDVVLCGDMDRISQIIDNLLTNAVK-FTNAGMIQFNVRYENGMLYIEIKDTGIGMDQDTVSRIFRPFerl 469
Cdd:PRK10364  328 EIQLRFTANDTLPEIQADPDRLTQVLLNLYLNAIQaIGQHGVISVTASESGAGVKISVTDSGKGIAADQLEAIFTPY--- 404
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2737555188 470 sSEANAEGFGLGLPITKGLVKLLGGSIDVESKIGHGSTFRVSLPLAVSNEK 520
Cdd:PRK10364  405 -FTTKAEGTGLGLAVVHNIVEQHGGTIQVASQEGKGATFTLWLPVNITRRD 454
REC_OmpR cd17574
phosphoacceptor receiver (REC) domain of OmpR family response regulators; OmpR-like proteins ...
540-623 6.01e-16

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: 73.98  E-value: 6.01e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188 540 LVIDNDTLQLEIAKEMLERNGVSCTTCSNAKELVNEMRRQDYDLLLSDIQMPETNGFEILALLRKssigNSHTIPIVAMT 619
Cdd:cd17574     1 LVVEDDEEIAELLSDYLEKEGYEVDTAADGEEALELAREEQPDLIILDVMLPGMDGFEVCRRLRE----KGSDIPIIMLT 76

                  ....
gi 2737555188 620 ARGE 623
Cdd:cd17574    77 AKDE 80
REC_RpfG-like cd17551
phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase response regulator ...
538-648 1.53e-15

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: 73.24  E-value: 1.53e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188 538 RVLVIDNDTLQLEIAKEMLER-NGVSCTTCSNAKELVNEMRRQDYDLLLSDIQMPETNGFEILALLRKSSiGNSHtIPIV 616
Cdd:cd17551     2 RILIVDDNPTNLLLLEALLRSaGYLEVVSFTDPREALAWCRENPPDLILLDYMMPGMDGLEFIRRLRALP-GLED-VPIV 79
                          90       100       110
                  ....*....|....*....|....*....|...
gi 2737555188 617 AMTARGEGE-KEAFIKGGFTDSIHKPFSMRELL 648
Cdd:cd17551    80 MITADTDREvRLRALEAGATDFLTKPFDPVELL 112
HATPase_BceS-YxdK-YvcQ-like cd16948
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
415-513 3.62e-15

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: 71.93  E-value: 3.62e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188 415 IIDNLLTNAVKFTN-AGMIQFNVRYENGMLYIEIKDTGIGMDQDTVSRIFRPF-----ERLSSEANaegfGLGLPITKGL 488
Cdd:cd16948     9 IIGQIVSNALKYSKqGGKIEIYSETNEQGVVLSIKDFGIGIPEEDLPRVFDKGftgenGRNFQEST----GMGLYLVKKL 84
                          90       100
                  ....*....|....*....|....*
gi 2737555188 489 VKLLGGSIDVESKIGHGSTFRVSLP 513
Cdd:cd16948    85 CDKLGHKIDVESEVGEGTTFTITFP 109
CitA COG3290
Sensor histidine kinase DipB regulating citrate/malate metabolism [Signal transduction ...
304-515 6.45e-15

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


Pssm-ID: 442519 [Multi-domain]  Cd Length: 389  Bit Score: 77.58  E-value: 6.45e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188 304 ISHDIRGPLNIIYGYVELAKDTRDRKrrnhHLENIETECKHILHLLNNLLDVYRLNEsketcnnvpfnlndllerIVTGF 383
Cdd:COG3290   196 QRHDFRNHLHTISGLLQLGEYDEALE----YIDEISEELQELIDSLLSRIGNPVLAA------------------LLLGK 253
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188 384 SHIANNKGIIFHHDSQNTDVVLCGDMDRISQIIDNLLTNAV-----KFTNAGMIQFNVRYENGMLYIEIKDTGIGMDQDT 458
Cdd:COG3290   254 AARARERGIDLTIDIDSDLPDLPLSDTDLVTILGNLLDNAIeavekLPEEERRVELSIRDDGDELVIEVEDSGPGIPEEL 333
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2737555188 459 VSRIFrpfERLSSEANAEGFGLGLPITKGLVKLLGGSIDVESKIGHGSTFRVSLPLA 515
Cdd:COG3290   334 LEKIF---ERGFSTKLGEGRGLGLALVKQIVEKYGGTIEVESEEGEGTVFTVRLPKE 387
REC_OmpR_PhoB cd17618
phosphoacceptor receiver (REC) domain of PhoB response regulator from the OmpR family; The ...
538-648 6.91e-15

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: 71.51  E-value: 6.91e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188 538 RVLVIDNDTLQLEIAKEMLERNGVSCTTCSNAKELVNEMRRQDYDLLLSDIQMPETNGFEILALLRKSSIGNshTIPIVA 617
Cdd:cd17618     2 TILIVEDEPAIREMIAFNLERAGFDVVEAEDAESAVNLIVEPRPDLILLDWMLPGGSGIQFIRRLKRDEMTR--DIPIIM 79
                          90       100       110
                  ....*....|....*....|....*....|..
gi 2737555188 618 MTARG-EGEKEAFIKGGFTDSIHKPFSMRELL 648
Cdd:cd17618    80 LTARGeEEDKVRGLEAGADDYITKPFSPRELV 111
REC_OmpR_CpxR cd17623
phosphoacceptor receiver (REC) domain of CpxR-like OmpR family response regulators; CpxR is ...
539-657 8.87e-15

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: 71.18  E-value: 8.87e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188 539 VLVIDNDTLQLEIAKEMLERNGVSCTTCSNAKELVNEMRRQDYDLLLSDIQMPETNGFEILALLRKSSignshTIPIVAM 618
Cdd:cd17623     1 ILLIDDDRELTELLTEYLEMEGFNVRAAHDGEQGLAALLEGSPDLVVLDVMLPKMNGLDVLKELRKTS-----QVPVLML 75
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 2737555188 619 TARGEGEKEafIKG---GFTDSIHKPFSMRELLDMVSSVVSR 657
Cdd:cd17623    76 TARGDDIDR--ILGlelGADDYLPKPFNPRELVARIRAILRR 115
HATPase_TmoS-FixL-DctS-like cd16920
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
412-513 1.33e-14

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: 70.12  E-value: 1.33e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188 412 ISQIIDNLLTNAVKFTNAG-------MIQFNvRYENGMLYIEIKDTGIGMDQDTVSRIFRPFerlsSEANAEGFGLGLPI 484
Cdd:cd16920     1 IQQVLINLVRNGIEAMSEGgcerrelTIRTS-PADDRAVTISVKDTGPGIAEEVAGQLFDPF----YTTKSEGLGMGLSI 75
                          90       100
                  ....*....|....*....|....*....
gi 2737555188 485 TKGLVKLLGGSIDVESKIGHGSTFRVSLP 513
Cdd:cd16920    76 CRSIIEAHGGRLSVESPAGGGATFQFTLP 104
REC_OmpR_BsPhoP-like cd19937
phosphoacceptor receiver (REC) domain of BsPhoP-like OmpR family response regulators; Bacillus ...
540-654 1.82e-14

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: 70.38  E-value: 1.82e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188 540 LVIDNDTLQLEIAKEMLERNGVSCTTCSNAKELVNEMRRQDYDLLLSDIQMPETNGFEILALLRksSIGNSHTIPIVAMT 619
Cdd:cd19937     1 LVVDDEEDIVELLKYNLEKEGYEVVTAYDGEEALKRAKDEKPDLIILDLMLPGIDGLEVCRILR--SDPKTSSIPIIMLT 78
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2737555188 620 ARG-EGEKEAFIKGGFTDSIHKPFSMRELLDMVSSV 654
Cdd:cd19937    79 AKGeEFDKVLGLELGADDYITKPFSPRELLARVKAV 114
HATPase_CckA-like cd16919
Histidine kinase-like ATPase domain of two-component sensor hybrid histidine kinases, similar ...
445-513 3.68e-14

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: 69.33  E-value: 3.68e-14
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2737555188 445 IEIKDTGIGMDQDTVSRIFRPFerLSSEANAEGFGLGLPITKGLVKLLGGSIDVESKIGHGSTFRVSLP 513
Cdd:cd16919    50 LEVSDTGSGMPAEVLRRAFEPF--FTTKEVGKGTGLGLSMVYGFVKQSGGHLRIYSEPGVGTTVRIYLP 116
PRK09303 PRK09303
histidine kinase;
407-513 4.77e-14

histidine kinase;


Pssm-ID: 236462 [Multi-domain]  Cd Length: 380  Bit Score: 74.60  E-value: 4.77e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188 407 GDMDRISQIIDNLLTNAVKFTNA-GMIQFNvryengMLY-------IEIKDTGIGMDQDTVSRIFRPFERLSSEANAEGF 478
Cdd:PRK09303  268 ADQERIRQVLLNLLDNAIKYTPEgGTITLS------MLHrttqkvqVSICDTGPGIPEEEQERIFEDRVRLPRDEGTEGY 341
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2737555188 479 GLGLPITKGLVKLLGGSIDVESKIGHGSTFRVSLP 513
Cdd:PRK09303  342 GIGLSVCRRIVRVHYGQIWVDSEPGQGSCFHFTLP 376
YesN COG4753
Two-component response regulator, YesN/AraC family, consists of REC and AraC-type DNA-binding ...
538-641 8.11e-14

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: 67.88  E-value: 8.11e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188 538 RVLVIDNDTLQLEIAKEMLERNG--VSCTTCSNAKELVNEMRRQDYDLLLSDIQMPETNGFEILALLRKssigNSHTIPI 615
Cdd:COG4753     1 KVLIVDDEPLIREGLKRILEWEAgfEVVGEAENGEEALELLEEHKPDLVITDINMPGMDGLELLEAIRE----LDPDTKI 76
                          90       100
                  ....*....|....*....|....*...
gi 2737555188 616 VAMTARGEGE--KEAfIKGGFTDSIHKP 641
Cdd:COG4753    77 IILSGYSDFEyaQEA-IKLGADDYLLKP 103
REC_OmpR_DrrD-like cd17625
phosphoacceptor receiver (REC) domain of DrrD-like OmpR family response regulators; DrrD is a ...
540-657 1.10e-13

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


Pssm-ID: 381140 [Multi-domain]  Cd Length: 115  Bit Score: 68.02  E-value: 1.10e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188 540 LVIDNDTLQLEIAKEMLERNGVSCTTCSNAKELVNEMRRQDYDLLLSDIQMPETNGFEILALLRKSSIgnshTIPIVAMT 619
Cdd:cd17625     1 LVVEDEKDLSEAITKHLKKEGYTVDVCFDGEEGLEYALSGIYDLIILDIMLPGMDGLEVLKSLREEGI----ETPVLLLT 76
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 2737555188 620 ARGEGEKEafIKG---GFTDSIHKPFSMRELLDMVSSVVSR 657
Cdd:cd17625    77 ALDAVEDR--VKGldlGADDYLPKPFSLAELLARIRALLRR 115
HATPase_TutC-TodS-like cd16925
Histidine kinase-like ATPase domain of hybrid sensor histidine kinases similar to Pseudomonas ...
408-513 1.47e-13

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: 67.52  E-value: 1.47e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188 408 DMDRISQIIDNLLTNAVKFT-NAGMIQFNV-RYENGMLYIEIKDTGIGMDQDTVSRIFRPFERLSSEANAE--GFGLGLP 483
Cdd:cd16925     1 DAEKYERVVLNLLSNAFKFTpDGGRIRCILeKFRLNRFLLTVSDSGPGIPPNLREEIFERFRQGDGSSTRAhgGTGLGLS 80
                          90       100       110
                  ....*....|....*....|....*....|
gi 2737555188 484 ITKGLVKLLGGSIDVESKIGHGSTFRVSLP 513
Cdd:cd16925    81 IVKEFVELHGGTVTVSDAPGGGALFQVELP 110
PRK11100 PRK11100
sensory histidine kinase CreC; Provisional
303-515 2.74e-13

sensory histidine kinase CreC; Provisional


Pssm-ID: 236846 [Multi-domain]  Cd Length: 475  Bit Score: 72.95  E-value: 2.74e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188 303 TISHDIRGPLNIIYGYVELAKDTRDRKRRNHHLENIETECKHILHLLNNLLDVYRLNESKETCNNVPFNLNDLLERIVTG 382
Cdd:PRK11100  262 TLTHELKSPLAAIRGAAELLQEDPPPEDRARFTGNILTQSARLQQLIDRLLELARLEQRQELEVLEPVALAALLEELVEA 341
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188 383 FSHIANNKGIIFHHDSQNTDVVlcGDMDRISQIIDNLLTNAVKFTNAG-MIQFNVRYENGMLYIEIKDTGIGMDQDTVSR 461
Cdd:PRK11100  342 REAQAAAKGITLRLRPDDARVL--GDPFLLRQALGNLLDNAIDFSPEGgTITLSAEVDGEQVALSVEDQGPGIPDYALPR 419
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2737555188 462 IFRPFERLSSEANAE-GFGLGLPITKGLVKLLGGSIDVESKIGHGSTFRVSLPLA 515
Cdd:PRK11100  420 IFERFYSLPRPANGRkSTGLGLAFVREVARLHGGEVTLRNRPEGGVLATLTLPRH 474
PRK10549 PRK10549
two-component system sensor histidine kinase BaeS;
297-514 2.83e-13

two-component system sensor histidine kinase BaeS;


Pssm-ID: 182539 [Multi-domain]  Cd Length: 466  Bit Score: 72.74  E-value: 2.83e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188 297 RKNVILTISHDIRGPLNIIYGYVELAKDTRdRKRRNHHLENIETEckhILHLLNNLLDVYRLNESKE---TCNNVPFNLN 373
Cdd:PRK10549  240 RRDFMADISHELRTPLAVLRGELEAIQDGV-RKFTPESVASLQAE---VGTLTKLVDDLHQLSLSDEgalAYRKTPVDLV 315
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188 374 DLLERIVTGFSHIANNKGIIFH---HDSqntdVVLCGDMDRISQIIDNLLTNAVKFTNA-GMIQFNVRYENGMLYIEIKD 449
Cdd:PRK10549  316 PLLEVAGGAFRERFASRGLTLQlslPDS----ATVFGDPDRLMQLFNNLLENSLRYTDSgGSLHISAEQRDKTLRLTFAD 391
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2737555188 450 TGIGMDQDTVSRIFRPFERLSSEAN--AEGFGLGLPITKGLVKLLGGSIDVE-SKIGhGSTFRVSLPL 514
Cdd:PRK10549  392 SAPGVSDEQLQKLFERFYRTEGSRNraSGGSGLGLAICLNIVEAHNGRIIAAhSPFG-GVSITVELPL 458
LytT COG3279
DNA-binding response regulator, LytR/AlgR family [Transcription, Signal transduction ...
538-657 4.16e-13

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


Pssm-ID: 442510 [Multi-domain]  Cd Length: 235  Bit Score: 69.46  E-value: 4.16e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188 538 RVLVIDNDTLQLEIAKEMLER-NGVSC-TTCSNAKELVNEMRRQDYDLLLSDIQMPETNGFEILALLRKssigNSHTIPI 615
Cdd:COG3279     3 KILIVDDEPLARERLERLLEKyPDLEVvGEASNGEEALELLEEHKPDLVFLDIQMPGLDGFELARQLRE----LDPPPPI 78
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 2737555188 616 VAMTARGEGEKEAFiKGGFTDSIHKPFSMRELLDMVSSVVSR 657
Cdd:COG3279    79 IFTTAYDEYALEAF-EVNAVDYLLKPIDEERLAKALEKAKER 119
HATPase_YcbM-like cd16947
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
407-512 6.42e-13

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: 66.00  E-value: 6.42e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188 407 GDMDRISQIIDNLLTNAVKFTNAG-MIQFNVRYENGMLYIEIKDTGIGMDQDTVSRIFRPFERLSSEANA--EGFGLGLP 483
Cdd:cd16947    16 ANTEALQRILKNLISNAIKYGSDGkFLGMTLREDEKHVYIDIWDKGKGISETEKDHVFERLYTLEDSRNSakQGNGLGLT 95
                          90       100
                  ....*....|....*....|....*....
gi 2737555188 484 ITKGLVKLLGGSIDVESKIGHGSTFRVSL 512
Cdd:cd16947    96 ITKRLAESMGGSIYVNSKPYEKTVFTVTL 124
PRK11086 PRK11086
sensory histidine kinase DcuS; Provisional
415-513 1.17e-12

sensory histidine kinase DcuS; Provisional


Pssm-ID: 236839 [Multi-domain]  Cd Length: 542  Bit Score: 71.10  E-value: 1.17e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188 415 IIDNLLTN---AVKFTNAGMIQFNVRYENGMLYIEIKDTGIGMDQDTVSRIFRpfERLSSEANAEGFGLGLpiTKGLVKL 491
Cdd:PRK11086  437 ILGNLIENaleAVGGEEGGEISVSLHYRNGWLHCEVSDDGPGIAPDEIDAIFD--KGYSTKGSNRGVGLYL--VKQSVEN 512
                          90       100
                  ....*....|....*....|..
gi 2737555188 492 LGGSIDVESKIGHGSTFRVSLP 513
Cdd:PRK11086  513 LGGSIAVESEPGVGTQFFVQIP 534
HATPase_VanS-like cd16923
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
415-513 1.44e-12

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: 64.33  E-value: 1.44e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188 415 IIDNLLTNAVKFT--NAgMIQFNVRYENGMLYIEIKDTGIGMDQDTVSRIFRPFERLSSEANAEGFGLGLPITKGLVKLL 492
Cdd:cd16923     4 VFSNLLSNAIKYSpeNT-RIYITSFLTDDVVNIMFKNPSSHPLDFKLEKLFERFYRGDNSRNTEGAGLGLSIAKAIIELH 82
                          90       100
                  ....*....|....*....|.
gi 2737555188 493 GGSIDVESKiGHGSTFRVSLP 513
Cdd:cd16923    83 GGSASAEYD-DNHDLFKVRLP 102
FixJ COG4566
DNA-binding response regulator, FixJ family, consists of REC and HTH domains [Signal ...
539-660 1.48e-12

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: 67.05  E-value: 1.48e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188 539 VLVIDNDTLQLEIAKEMLERNGVSCTTCSNAKELVNEMRRQDYDLLLSDIQMPETNGFEILALLRKSSIgnshTIPIVAM 618
Cdd:COG4566     2 VYIVDDDEAVRDSLAFLLESAGLRVETFASAEAFLAALDPDRPGCLLLDVRMPGMSGLELQEELAARGS----PLPVIFL 77
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 2737555188 619 TARGEGE--KEAFIKGGFtDSIHKPFSMRELLDMVSSVVSRDVE 660
Cdd:COG4566    78 TGHGDVPmaVRAMKAGAV-DFLEKPFDDQALLDAVRRALARDRA 120
HATPase_BasS-like cd16940
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
402-512 1.72e-12

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: 64.35  E-value: 1.72e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188 402 DVVLCGDMDRISQIIDNLLTNAVKFTNAGMiQFNVRYENGML-YIEIKDTGIGMDQDTVSRIFRPFERLSSEaNAEGFGL 480
Cdd:cd16940     4 DIQVQGDALLLFLLLRNLVDNAVRYSPQGS-RVEIKLSADDGaVIRVEDNGPGIDEEELEALFERFYRSDGQ-NYGGSGL 81
                          90       100       110
                  ....*....|....*....|....*....|..
gi 2737555188 481 GLPITKGLVKLLGGSIDVESKIGHGSTFRVSL 512
Cdd:cd16940    82 GLSIVKRIVELHGGQIFLGNAQGGGLEAWVRL 113
HATPase_DpiB-CitA-like cd16915
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
415-513 1.97e-12

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: 63.85  E-value: 1.97e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188 415 IIDNLLTNAVKFTNA-----GMIQFNVRYENGMLYIEIKDTGIGMDQDTVSRIFrpfERLSSEANAEGFGLGLPITKGLV 489
Cdd:cd16915     4 IVGNLIDNALDALAAtgapnKQVEVFLRDEGDDLVIEVRDTGPGIAPELRDKVF---ERGVSTKGQGERGIGLALVRQSV 80
                          90       100
                  ....*....|....*....|....
gi 2737555188 490 KLLGGSIDVESKIGHGSTFRVSLP 513
Cdd:cd16915    81 ERLGGSITVESEPGGGTTFSIRIP 104
PRK10490 PRK10490
sensor protein KdpD; Provisional
418-514 2.28e-12

sensor protein KdpD; Provisional


Pssm-ID: 236701 [Multi-domain]  Cd Length: 895  Bit Score: 70.84  E-value: 2.28e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188 418 NLLTNAVKFTNAGM-IQFNVRYENGMLYIEIKDTGIGMDQDTVSRIFRPFERLSSEANAEGFGLGLPITKGLVKLLGGSI 496
Cdd:PRK10490  785 NLLENAVKYAGAQAeIGIDAHVEGERLQLDVWDNGPGIPPGQEQLIFDKFARGNKESAIPGVGLGLAICRAIVEVHGGTI 864
                          90
                  ....*....|....*...
gi 2737555188 497 DVESKIGHGSTFRVSLPL 514
Cdd:PRK10490  865 WAENRPEGGACFRVTLPL 882
PRK10618 PRK10618
phosphotransfer intermediate protein in two-component regulatory system with RcsBC; Provisional
366-587 3.69e-12

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


Pssm-ID: 236726 [Multi-domain]  Cd Length: 894  Bit Score: 69.96  E-value: 3.69e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188 366 NNVPFNLNDLLERIVTGFSHIANNKGI-IFHHDSQNTDVVLCGDMDRISQIIDNLLTNAVKFTNAGMIQFNVRYEN---G 441
Cdd:PRK10618  519 EQELFSLQDLIDEVLPEVLPAIKRKGLqLLIHNHLKAEQLRIGDRDALRKILLLLLNYAITTTAYGKITLEVDQDEsspD 598
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188 442 MLYIEIKDTGIGMDQDTVSRIFRPFerlSSEANAEGFGLGLPIT----KGLVKLLGGSIDVESKIGHGSTFRVSLPLAVS 517
Cdd:PRK10618  599 RLTIRILDTGAGVSIKELDNLHFPF---LNQTQGDRYGKASGLTfflcNQLCRKLGGHLTIKSREGLGTRYSIHLKMLAA 675
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2737555188 518 NEKINSEasavpQDRLplpqrvlvIDNDTLQLEIAKE--------MLERNGVSCTTCSnaKELVNemrrQDYDLLLSD 587
Cdd:PRK10618  676 DPEVEEE-----EEKL--------LDGVTVLLDITSEevrkivtrQLENWGATCITPD--ERLIS----QEYDIFLTD 734
HATPase_EnvZ-like cd16950
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
412-513 3.80e-12

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: 63.24  E-value: 3.80e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188 412 ISQIIDNLLTNAVKFTNaGMIQFNVRYENGMLYIEIKDTGIGMDQDTVSRIFRPFERLSSEANAEGFGLGLPITKGLVKL 491
Cdd:cd16950     1 LKRVLSNLVDNALRYGG-GWVEVSSDGEGNRTRIQVLDNGPGIAPEEVDELFQPFYRGDNARGTSGTGLGLAIVQRISDA 79
                          90       100
                  ....*....|....*....|..
gi 2737555188 492 LGGSIDVESKIGHGSTFRVSLP 513
Cdd:cd16950    80 HGGSLTLANRAGGGLCARIELP 101
HATPase_SpaK_NisK-like cd16975
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
408-510 4.29e-12

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: 63.25  E-value: 4.29e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188 408 DMDRISQIIDNLLTNAVKFT-NAGMIQFNVRYENGMLYIEIKDTGIGMDQDTVSRIFRPFERLSSEANAEG-FGLGLPIT 485
Cdd:cd16975     1 DTLLLSRALINIISNACQYApEGGTVSISIYDEEEYLYFEIWDNGHGFSEQDLKKALELFYRDDTSRRSGGhYGMGLYIA 80
                          90       100
                  ....*....|....*....|....*
gi 2737555188 486 KGLVKLLGGSIDVESKIGHGSTFRV 510
Cdd:cd16975    81 KNLVEKHGGSLIIENSQKGGAEVTV 105
HATPase_BaeS-like cd16946
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
408-513 4.65e-12

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Escherichia coli BasS; This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component sensor histidine kinase (HKs) similar to Escherichia coli BaeS HK of the BaeS/BaeR two-component regulatory system (TCS), which responds to envelope stress. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA), and a HAMP sensory domain.


Pssm-ID: 340422 [Multi-domain]  Cd Length: 109  Bit Score: 63.25  E-value: 4.65e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188 408 DMDRISQIIDNLLTNAVKFTNA-GMIQFNVRYENGMLYIEIKDTGIGMDQDTVSRIFRPFERLSSEAN--AEGFGLGLPI 484
Cdd:cd16946     1 DRDRLQQLFVNLLENSLRYTDTgGKLRIRAAQTPQEVRLDVEDSAPGVSDDQLARLFERFYRVESSRNraSGGSGLGLAI 80
                          90       100       110
                  ....*....|....*....|....*....|
gi 2737555188 485 TKGLVKLLGGSIDVE-SKIGhGSTFRVSLP 513
Cdd:cd16946    81 CHNIALAHGGTISAEhSPLG-GLRLVLTLP 109
REC_Ycf29 cd19927
phosphoacceptor receiver (REC) domain of probable transcriptional regulator Ycf29; Ycf29 is a ...
539-622 1.54e-11

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


Pssm-ID: 381154 [Multi-domain]  Cd Length: 102  Bit Score: 61.62  E-value: 1.54e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188 539 VLVIDNDTLQLEIAKEMLERNGVSCTTCSNAKELVNEMRRQDYDLLLSDIQMPETNGFEILALLRKssIGNSHTIPIVAM 618
Cdd:cd19927     1 ILLVDDDPGIRLAVKDYLEDQGFTVIAASNGLEALDLLNQYIPDLIISDIIMPGVDGYSLLGKLRK--NADFDTIPVIFL 78

                  ....
gi 2737555188 619 TARG 622
Cdd:cd19927    79 TAKG 82
REC_OmpR_PmrA-like cd17624
phosphoacceptor receiver (REC) domain of PmrA-like OmpR family response regulators; This ...
539-648 1.60e-11

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


Pssm-ID: 381139 [Multi-domain]  Cd Length: 115  Bit Score: 61.73  E-value: 1.60e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188 539 VLVIDNDTLQLEIAKEMLERNGVSCTTCSNAKELVNEMRRQDYDLLLSDIQMPETNGFEILALLRKSSIgnshTIPIVAM 618
Cdd:cd17624     1 ILLVEDDALLGDGLKTGLRKAGYAVDWVRTGAEAEAALASGPYDLVILDLGLPDGDGLDLLRRWRRQGQ----SLPVLIL 76
                          90       100       110
                  ....*....|....*....|....*....|...
gi 2737555188 619 TARGEGEKEafIKG---GFTDSIHKPFSMRELL 648
Cdd:cd17624    77 TARDGVDDR--VAGldaGADDYLVKPFALEELL 107
PRK10604 PRK10604
sensor protein RstB; Provisional
277-514 1.97e-11

sensor protein RstB; Provisional


Pssm-ID: 236724 [Multi-domain]  Cd Length: 433  Bit Score: 66.94  E-value: 1.97e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188 277 SLLR--KKMEGVIDRNNELLETRKNVILTISHDIRGPLNIIYGYVELAKDTRDRKRR--NHHLENIETECKHILHLLnnl 352
Cdd:PRK10604  190 SLERlgVAFNQMADNINALIASKKQLIDGIAHELRTPLVRLRYRLEMSDNLSAAESQalNRDIGQLEALIEELLTYA--- 266
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188 353 ldvyRLNESKETCNNVPFNLNDLLERIVTGFSHIanNKGIIFHHDSQNTDVVLCGDMDRISQIIDNLLTNAVKFTNaGMI 432
Cdd:PRK10604  267 ----RLDRPQNELHLSEPDLPAWLSTHLADIQAV--TPEKTVRLDTPHQGDYGALDMRLMERVLDNLLNNALRYAH-SRV 339
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188 433 QFNVRYENGMLYIEIKDTGIGMDQDTVSRIFRPFERL--SSEANAEGFGLGLPITKGLVKLLGGSIDVESKIGHGSTFRV 510
Cdd:PRK10604  340 RVSLLLDGNQACLIVEDDGPGIPPEERERVFEPFVRLdpSRDRATGGCGLGLAIVHSIALAMGGSVNCDESELGGARFSF 419

                  ....
gi 2737555188 511 SLPL 514
Cdd:PRK10604  420 SWPV 423
HATPase_HupT_MifS-like cd16976
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
412-512 2.66e-11

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: 60.93  E-value: 2.66e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188 412 ISQIIDNLLTNAV----KFTNaGMIQFNVRYENGMLYIEIKDTGIGMDQDTVSRIFRPFerLSSEANAEGFGLGLPITKG 487
Cdd:cd16976     1 IQQVLMNLLQNALdamgKVEN-PRIRIAARRLGGRLVLVVRDNGPGIAEEHLSRVFDPF--FTTKPVGKGTGLGLSISYG 77
                          90       100
                  ....*....|....*....|....*
gi 2737555188 488 LVKLLGGSIDVESKIGHGSTFRVSL 512
Cdd:cd16976    78 IVEEHGGRLSVANEEGAGARFTFDL 102
REC_OmpR_YycF-like cd17614
phosphoacceptor receiver (REC) domain of YrcF-like OmpR family response regulators; YycF ...
539-657 3.57e-11

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: 60.90  E-value: 3.57e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188 539 VLVIDNDTLQLEIAKEMLERNGVSCTTCSNAKELVNEMRRQDYDLLLSDIQMPETNGFEILALLRKSSignshTIPIVAM 618
Cdd:cd17614     1 ILVVDDEKPISDILKFNLTKEGYEVVTAYDGREALEKVEEEQPDLILLDLMLPEKDGLEVCREVRKTS-----NVPIIML 75
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2737555188 619 TAR-GEGEKEAFIKGGFTDSIHKPFSMRELLDMVSSVVSR 657
Cdd:cd17614    76 TAKdSEVDKVLGLELGADDYVTKPFSNRELLARVKANLRR 115
HATPase_RstB-like cd16939
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
412-514 4.79e-11

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: 60.14  E-value: 4.79e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188 412 ISQIIDNLLTNAVKFTnAGMIQFNVRYENGMLYIEIKDTGIGMDQDTVSRIFRPFERL--SSEANAEGFGLGLPITKGLV 489
Cdd:cd16939     1 MARALDNLLRNALRYA-HRTVRIALLVSGGRLTLIVEDDGPGIPAAARERVFEPFVRLdpSRDRATGGFGLGLAIVHRVA 79
                          90       100
                  ....*....|....*....|....*.
gi 2737555188 490 KLLGGSIDV-ESKIGhGSTFRVSLPL 514
Cdd:cd16939    80 LWHGGHVECdDSELG-GACFRLTWPR 104
phoR PRK11006
phosphate regulon sensor histidine kinase PhoR;
275-519 6.01e-11

phosphate regulon sensor histidine kinase PhoR;


Pssm-ID: 182895 [Multi-domain]  Cd Length: 430  Bit Score: 65.42  E-value: 6.01e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188 275 RDSLLRKKMEGvidrnnelleTRKNVILTISHDIRGPLNIIYGYVELAKD------TRDR---------KRRNH------ 333
Cdd:PRK11006  192 RDVTQMHQLEG----------ARRNFFANVSHELRTPLTVLQGYLEMMQDqplegaLREKalhtmreqtQRMEGlvkqll 261
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188 334 HLENIETeckhilhllnnlLDVYRLNESKetcnNVPFNLnDLLERIVTGFSHiaNNKGIIFHHDSQntdVVLCGDMDRIS 413
Cdd:PRK11006  262 TLSKIEA------------APTIDLNEKV----DVPMML-RVLEREAQTLSQ--GKHTITFEVDNS---LKVFGNEDQLR 319
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188 414 QIIDNLLTNAVKFTNAGMiQFNVRYE---NGMLYiEIKDTGIGMDQDTVSRIFRPFERLSSEANAE--GFGLGLPITKGL 488
Cdd:PRK11006  320 SAISNLVYNAVNHTPEGT-HITVRWQrvpQGAEF-SVEDNGPGIAPEHIPRLTERFYRVDKARSRQtgGSGLGLAIVKHA 397
                         250       260       270
                  ....*....|....*....|....*....|...
gi 2737555188 489 VKLLGGSIDVESKIGHGSTFRVSLP--LAVSNE 519
Cdd:PRK11006  398 LSHHDSRLEIESEVGKGTRFSFVLPerLIAKNS 430
REC_CheY_CheY3 cd19923
phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY3 and similar CheY ...
538-651 6.80e-11

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: 60.04  E-value: 6.80e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188 538 RVLVIDNDTLQLEIAKEMLERNGVSCTT-CSNAKELVNEMRRQDYDLLLSDIQMPETNGFEILALLRKSSigNSHTIPIV 616
Cdd:cd19923     2 KVLVVDDFSTMRRIIKNLLKELGFNNVEeAEDGVDALEKLKAGGFDFVITDWNMPNMDGLELLKTIRADG--ALSHLPVL 79
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 2737555188 617 AMTArgEGEKEAFI---KGGFTDSIHKPFS---MRELLDMV 651
Cdd:cd19923    80 MVTA--EAKKENVIaaaQAGVNNYIVKPFTaatLKEKLEKI 118
HATPase_Glnl-NtrB-like cd16918
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
412-513 7.24e-11

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: 59.72  E-value: 7.24e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188 412 ISQIIDNLLTNAVKFT--NAGMIQFNVRYENGM----------LYIEIKDTGIGMDQDTVSRIFRPFerLSSEANaeGFG 479
Cdd:cd16918     1 LIQVFLNLVRNAAQALagSGGEIILRTRTQRQVtlghprhrlaLRVSVIDNGPGIPPDLQDTIFYPM--VSGREN--GTG 76
                          90       100       110
                  ....*....|....*....|....*....|....
gi 2737555188 480 LGLPITKGLVKLLGGSIDVESKIGHgSTFRVSLP 513
Cdd:cd16918    77 LGLAIAQNIVSQHGGVIECDSQPGH-TVFSVSLP 109
REC_PA4781-like cd19920
phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase PA4781 and similar ...
539-642 9.85e-11

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


Pssm-ID: 381147 [Multi-domain]  Cd Length: 103  Bit Score: 59.06  E-value: 9.85e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188 539 VLVIDNDTLQLEIAKEMLERNGVSCTTCSNAKELVNEMRRQDYDLLLSDIQMPETNGFEILALLRKssigNSHT--IPIV 616
Cdd:cd19920     1 ILIVDDVPDNLRLLSELLRAAGYRVLVATDGQQALQRAQAEPPDLILLDVMMPGMDGFEVCRRLKA----DPATrhIPVI 76
                          90       100
                  ....*....|....*....|....*...
gi 2737555188 617 AMTARGEGEKE--AFIKGGfTDSIHKPF 642
Cdd:cd19920    77 FLTALTDTEDKvkGFELGA-VDYITKPF 103
glnG PRK10923
nitrogen regulation protein NR(I); Provisional
536-675 1.02e-10

nitrogen regulation protein NR(I); Provisional


Pssm-ID: 182842 [Multi-domain]  Cd Length: 469  Bit Score: 64.89  E-value: 1.02e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188 536 PQRVLVIDNDTLQLEIAKEMLERNGVSCTTCSNAKELVNEMRRQDYDLLLSDIQMPETNGfeiLALLRKssIGNSH-TIP 614
Cdd:PRK10923    3 RGIVWVVDDDSSIRWVLERALAGAGLTCTTFENGNEVLEALASKTPDVLLSDIRMPGMDG---LALLKQ--IKQRHpMLP 77
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2737555188 615 IVAMTARGEGEK--EAFIKGGFtDSIHKPFSMRELLDMVSSVVS--RDVEESHTPDFATFTADVL 675
Cdd:PRK10923   78 VIIMTAHSDLDAavSAYQQGAF-DYLPKPFDIDEAVALVERAIShyQEQQQPRNIQVNGPTTDII 141
PRK10161 PRK10161
phosphate response regulator transcription factor PhoB;
535-657 1.29e-10

phosphate response regulator transcription factor PhoB;


Pssm-ID: 182277 [Multi-domain]  Cd Length: 229  Bit Score: 62.04  E-value: 1.29e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188 535 LPQRVLVIDNDTLQLEIAKEMLERNGVSCTTCSNAKELVNEMRRQDYDLLLSDIQMPETNGFEILALLRKSSIgnSHTIP 614
Cdd:PRK10161    1 MARRILVVEDEAPIREMVCFVLEQNGFQPVEAEDYDSAVNQLNEPWPDLILLDWMLPGGSGIQFIKHLKRESM--TRDIP 78
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 2737555188 615 IVAMTARGEGEKEAF-IKGGFTDSIHKPFSMRELLDMVSSVVSR 657
Cdd:PRK10161   79 VVMLTARGEEEDRVRgLETGADDYITKPFSPKELVARIKAVMRR 122
REC_NtrC cd19919
phosphoacceptor receiver (REC) domain of DNA-binding transcriptional regulator NtrC; ...
537-651 1.52e-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: 59.21  E-value: 1.52e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188 537 QRVLVIDNDT---LQLEIAkemLERNGVSCTTCSNAKELVNEMRRQDYDLLLSDIQMPETNGFEILALLRKssignSHT- 612
Cdd:cd19919     1 KTVWIVDDDSsirWVLERA---LAGAGLTVTSFENAQEALAALASSQPDVLISDIRMPGMDGLALLAQIKQ-----RHPd 72
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 2737555188 613 IPIVAMTARGEGEK--EAFIKGGFtDSIHKPFSMRELLDMV 651
Cdd:cd19919    73 LPVIIMTAHSDLDSavSAYQGGAF-EYLPKPFDIDEAVALV 112
REC_OmpR_PrrA-like cd17627
phosphoacceptor receiver (REC) domain of PrrA-like OmpR family response regulators; The ...
539-657 1.80e-10

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


Pssm-ID: 381142 [Multi-domain]  Cd Length: 116  Bit Score: 58.93  E-value: 1.80e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188 539 VLVIDNDTLQLEIAKEMLERNGVSCTTCSNAKELVNEMRRQDYDLLLSDIQMPETNGFEILALLRKSsiGNShtIPIVAM 618
Cdd:cd17627     1 ILVVDDDRAVRESLRRSLRFEGYEVETAVDGAEALRVISGNRPDAVVLDVMMPRLDGLEVCRRLRAA--GND--LPILVL 76
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2737555188 619 TARGE-GEKEAFIKGGFTDSIHKPFSMRELLDMVSSVVSR 657
Cdd:cd17627    77 TARDSvSDRVAGLDAGADDYLVKPFALEELLARVRALLRR 116
REC_ETR-like cd19933
phosphoacceptor receiver (REC) domain of plant ethylene receptors ETR1, ETR2, and EIN4, and ...
538-647 1.86e-10

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


Pssm-ID: 381160 [Multi-domain]  Cd Length: 117  Bit Score: 58.95  E-value: 1.86e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188 538 RVLVIDNDTLQLEIAKEMLERNGVSCTTCSNAKELVNEMRR--QDYDLLLSDIQMPETNGFEILALLRKsSIGNSHTIPI 615
Cdd:cd19933     2 KVLLVDDNAVNRMVTKGLLEKLGCEVTTVSSGEECLNLLASaeHSFQLVLLDLCMPEMDGFEVALRIRK-LFGRRERPLI 80
                          90       100       110
                  ....*....|....*....|....*....|...
gi 2737555188 616 VAMTARGEGE-KEAFIKGGFTDSIHKPFSMREL 647
Cdd:cd19933    81 VALTANTDDStREKCLSLGMNGVITKPVSLHAL 113
REC_D1_PleD-like cd17538
first (D1) phosphoacceptor receiver (REC) domain of response regulator PleD and similar ...
538-642 2.47e-10

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: 57.89  E-value: 2.47e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188 538 RVLVIDNDTLQLEIAKEMLERNGVSCTTCSNAKELVNEMRRQDYDLLLSDIQMPETNGFEILALLRKssigNSHT--IPI 615
Cdd:cd17538     1 KILVVDDEPANRELLEALLSAEGYEVLTADSGQEALALAEEELPDLILLDVMMPGMDGFEVCRRLKE----DPETrhIPV 76
                          90       100       110
                  ....*....|....*....|....*....|
gi 2737555188 616 VAMTARgeGEKEAFIKG---GFTDSIHKPF 642
Cdd:cd17538    77 IMITAL--DDREDRIRGleaGADDFLSKPI 104
PRK10955 PRK10955
envelope stress response regulator transcription factor CpxR;
538-657 4.12e-10

envelope stress response regulator transcription factor CpxR;


Pssm-ID: 182864 [Multi-domain]  Cd Length: 232  Bit Score: 60.59  E-value: 4.12e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188 538 RVLVIDNDTLQLEIAKEMLERNGVSCTTCSNAKELVNEMRrQDYDLLLSDIQMPETNGFEILALLRKssignSHTIPIVA 617
Cdd:PRK10955    3 KILLVDDDRELTSLLKELLEMEGFNVIVAHDGEQALDLLD-DSIDLLLLDVMMPKKNGIDTLKELRQ-----THQTPVIM 76
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 2737555188 618 MTARG-EGEKEAFIKGGFTDSIHKPFSMRELLDMVSSVVSR 657
Cdd:PRK10955   77 LTARGsELDRVLGLELGADDYLPKPFNDRELVARIRAILRR 117
ComP COG4585
Signal transduction histidine kinase ComP [Signal transduction mechanisms];
419-515 4.70e-10

Signal transduction histidine kinase ComP [Signal transduction mechanisms];


Pssm-ID: 443642 [Multi-domain]  Cd Length: 252  Bit Score: 60.79  E-value: 4.70e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188 419 LLTNAVKFTNAGMIQFNVRYENGMLYIEIKDTGIGMDQDTVSRifrpferlsseanaEGFGL-GLpitKGLVKLLGGSID 497
Cdd:COG4585   170 ALTNALKHAGATRVTVTLEVDDGELTLTVRDDGVGFDPEAAPG--------------GGLGLrGM---RERAEALGGTLT 232
                          90
                  ....*....|....*...
gi 2737555188 498 VESKIGHGSTFRVSLPLA 515
Cdd:COG4585   233 IGSAPGGGTRVRATLPLA 250
REC_DctD-like cd17549
phosphoacceptor receiver (REC) domain of C4-dicarboxylic acid transport protein D (DctD) and ...
539-682 5.13e-10

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: 57.88  E-value: 5.13e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188 539 VLVIDNDTLQLEIAKEMLERNGVSCTTCSNAKELVNEMRRQDYDLLLSDIQMPETNGFEILALLRKssigNSHTIPIVAM 618
Cdd:cd17549     1 VLLVDDDADVREALQQTLELAGFRVRAFADAEEALAALSPDFPGVVISDIRMPGMDGLELLAQIRE----LDPDLPVILI 76
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2737555188 619 TARGEGEK--EAfIKGGFTDSIHKPFSMRELLDmvssVVSRDVEESHTpdfatftadVLDKRELLR 682
Cdd:cd17549    77 TGHGDVPMavEA-MRAGAYDFLEKPFDPERLLD----VVRRALEKRRL---------VLENRRLRQ 128
REC_Rcp-like cd17557
phosphoacceptor receiver (REC) domain of cyanobacterial phytochrome response regulator Rcp and ...
538-656 8.46e-10

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


Pssm-ID: 381108 [Multi-domain]  Cd Length: 129  Bit Score: 57.43  E-value: 8.46e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188 538 RVLVIDNDTLQLEIAKEMLERNGVSC--TTCSNAKELVNEMRRQD-Y------DLLLSDIQMPETNGFEILALLRKSSig 608
Cdd:cd17557     1 TILLVEDNPGDAELIQEAFKEAGVPNelHVVRDGEEALDFLRGEGeYadaprpDLILLDLNMPRMDGFEVLREIKADP-- 78
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2737555188 609 NSHTIPIVAMTARGEGE--KEAFIKG--GFtdsIHKPFSMRELLDMVSSVVS 656
Cdd:cd17557    79 DLRRIPVVVLTTSDAEEdiERAYELGanSY---IVKPVDFEEFVEAIRSLGE 127
REC smart00448
cheY-homologous receiver domain; CheY regulates the clockwise rotation of E. coli flagellar ...
538-591 8.59e-10

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


Pssm-ID: 214668 [Multi-domain]  Cd Length: 55  Bit Score: 54.88  E-value: 8.59e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2737555188  538 RVLVIDNDTLQLEIAKEMLERNGVSCTTCSNAKELVNEMRRQDYDLLLSDIQMP 591
Cdd:smart00448   2 RILVVDDDPLLRELLKALLEKEGYEVDEATDGEEALELLKEEKPDLILLDIMMP 55
ompR PRK09468
osmolarity response regulator; Provisional
538-682 9.73e-10

osmolarity response regulator; Provisional


Pssm-ID: 181883 [Multi-domain]  Cd Length: 239  Bit Score: 59.60  E-value: 9.73e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188 538 RVLVIDNDTLQLEIAKEMLERNGVSCTTCSNAKELVNEMRRQDYDLLLSDIQMPETNGFEILALLRkssiGNSHTIPIVA 617
Cdd:PRK09468    7 KILVVDDDMRLRALLERYLTEQGFQVRSAANAEQMDRLLTRESFHLMVLDLMLPGEDGLSICRRLR----SQNNPTPIIM 82
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2737555188 618 MTARGEGEKEafIKG---GFTDSIHKPFSMRELLDMVSSVVSRDVEE-----SHTPDFATFTADVLD--KRELLR 682
Cdd:PRK09468   83 LTAKGEEVDR--IVGleiGADDYLPKPFNPRELLARIRAVLRRQAPElpgapSQEEEVIAFGKFKLNlgTRELFR 155
REC_OmpR_ArcA_TorR-like cd17619
phosphoacceptor receiver (REC) domain of ArcA- and TorR-like OmpR family response regulators; ...
538-648 2.43e-09

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: 55.47  E-value: 2.43e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188 538 RVLVIDNDTLQLEIAKEMLERNGVSCTTCSNAKELVNEMRRQDYDLLLSDIQMPETNGFEILALLRKSSignshTIPIVA 617
Cdd:cd17619     2 HILIVEDEPVTRATLKSYFEQEGYDVSEAGDGEEMRQILARQDIDLVLLDINLPGKDGLSLTRELREQS-----EVGIIL 76
                          90       100       110
                  ....*....|....*....|....*....|..
gi 2737555188 618 MTARGEG-EKEAFIKGGFTDSIHKPFSMRELL 648
Cdd:cd17619    77 VTGRDDEvDRIVGLEIGADDYVTKPFNPRELL 108
orf27 CHL00148
Ycf27; Reviewed
537-657 2.88e-09

Ycf27; Reviewed


Pssm-ID: 214376 [Multi-domain]  Cd Length: 240  Bit Score: 58.19  E-value: 2.88e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188 537 QRVLVIDNDTLQLEIAKEMLERNGVSCTTCSNAKELVNEMRRQDYDLLLSDIQMPETNGFEILALLRKSSignshTIPIV 616
Cdd:CHL00148    7 EKILVVDDEAYIRKILETRLSIIGYEVITASDGEEALKLFRKEQPDLVILDVMMPKLDGYGVCQEIRKES-----DVPII 81
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 2737555188 617 AMTARGEGEKEafIKG---GFTDSIHKPFSMRELLDMVSSVVSR 657
Cdd:CHL00148   82 MLTALGDVSDR--ITGlelGADDYVVKPFSPKELEARIRSVLRR 123
AmiR COG3707
Two-component response regulator, AmiR/NasT family, consists of REC and RNA-binding ...
538-657 3.03e-09

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


Pssm-ID: 442921 [Multi-domain]  Cd Length: 194  Bit Score: 57.27  E-value: 3.03e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188 538 RVLVIDNDTLQLEIAKEMLERNGVS-CTTCSNAKELVNEMRRQDYDLLLSDIQMPETNGFEILALLRKSSIgnshtIPIV 616
Cdd:COG3707     5 RVLVVDDEPLRRADLREGLREAGYEvVAEAADGEDAVELVRELKPDLVIVDIDMPDRDGLEAARQISEERP-----APVI 79
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 2737555188 617 AMTARGEGEK-EAFIKGGFTDSIHKPFSMRELLDMVSSVVSR 657
Cdd:COG3707    80 LLTAYSDPELiERALEAGVSAYLVKPLDPEDLLPALELALAR 121
REC_OmpR_BaeR-like cd19938
phosphoacceptor receiver (REC) domain of BaeR-like OmpR family response regulators; BaeR is ...
538-655 3.32e-09

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: 55.08  E-value: 3.32e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188 538 RVLVIDNDTLQLEIAKEMLERNGVSCTTCSNAKELVNEMRRQDYDLLLSDIQMPETNGFEILALLRKSSignshTIPIVA 617
Cdd:cd19938     1 RILIVEDEPKLAQLLIDYLRAAGYAPTLLAHGDQVLPYVRHTPPDLILLDLMLPGTDGLTLCREIRRFS-----DVPIIM 75
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2737555188 618 MTAR-GEGEKEAFIKGGFTDSIHKPFSMRELLDMVSSVV 655
Cdd:cd19938    76 VTARvEEIDRLLGLELGADDYICKPYSPREVVARVKAIL 114
HATPase_CheA-like cd16916
Histidine kinase-like ATPase domain of the chemotaxis protein histidine kinase CheA, and some ...
430-513 3.67e-09

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: 56.82  E-value: 3.67e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188 430 GMIQFNVRYENGMLYIEIKDTGIGMDQDTVSR------------------------IFRP-FERLSSEANAEGFGLGLPI 484
Cdd:cd16916    70 GTITLRAEHQGNQVVIEVSDDGRGIDREKIREkaierglitadeaatlsddevlnlIFAPgFSTAEQVTDVSGRGVGMDV 149
                          90       100
                  ....*....|....*....|....*....
gi 2737555188 485 TKGLVKLLGGSIDVESKIGHGSTFRVSLP 513
Cdd:cd16916   150 VKRSIESLGGTIEVESEPGQGTTFTIRLP 178
REC_OmpR_MtrA-like cd17626
phosphoacceptor receiver (REC) domain of MtrA-like OmpR family response regulators; MtrA is ...
537-648 3.72e-09

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: 55.17  E-value: 3.72e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188 537 QRVLVIDNDTLQLEIAKEMLERNGVSCTTCSNAKELVNEMRRQDYDLLLSDIQMPETNGFEILALLRKSSignshTIPIV 616
Cdd:cd17626     1 ARILVVDDDAALAEMIGIVLRGEGFDPAFCGDGTQALAAFREVRPDLVLLDLMLPGIDGIEVCRQIRAES-----GVPIV 75
                          90       100       110
                  ....*....|....*....|....*....|...
gi 2737555188 617 AMTARGEG-EKEAFIKGGFTDSIHKPFSMRELL 648
Cdd:cd17626    76 MLTAKSDTvDVVLGLESGADDYVAKPFKPKELV 108
envZ PRK09467
osmolarity sensor protein; Provisional
412-515 4.06e-09

osmolarity sensor protein; Provisional


Pssm-ID: 236531 [Multi-domain]  Cd Length: 435  Bit Score: 59.54  E-value: 4.06e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188 412 ISQIIDNLLTNAVKFTNaGMIQFNVRYENGMLYIEIKDTGIGMDQDTVSRIFRPFERLSSEANAEGFGLGLPITKGLVKL 491
Cdd:PRK09467  332 IKRALANLVVNAARYGN-GWIKVSSGTEGKRAWFQVEDDGPGIPPEQLKHLFQPFTRGDSARGSSGTGLGLAIVKRIVDQ 410
                          90       100
                  ....*....|....*....|....
gi 2737555188 492 LGGSIDVESKIGHGSTFRVSLPLA 515
Cdd:PRK09467  411 HNGKVELGNSEEGGLSARAWLPLT 434
REC_OmpR_BfmR-like cd19939
phosphoacceptor receiver (REC) domain of BfmR-like OmpR family response regulators; ...
538-657 4.37e-09

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: 55.07  E-value: 4.37e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188 538 RVLVIDNDTLQLEIAKEMLERNGVSCTTCSNAKELVNEMRRQDYDLLLSDIQMPETNGFEILALLRKSSignshTIPIVA 617
Cdd:cd19939     1 RILIVEDELELARLTRDYLIKAGLEVSVFTDGQRAVRRIIDEQPSLVVLDIMLPGMDGLTVCREVREHS-----HVPILM 75
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 2737555188 618 MTARGEGEKEAF-IKGGFTDSIHKPFSMRELLDMVSSVVSR 657
Cdd:cd19939    76 LTARTEEMDRVLgLEMGADDYLCKPFSPRELLARVRALLRR 116
REC_FixJ cd17537
phosphoacceptor receiver (REC) domain of FixJ family response regulators; FixJ family response ...
539-653 4.40e-09

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: 54.91  E-value: 4.40e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188 539 VLVIDNDTLQLEIAKEMLERNGVSCTTCSNAKELVNEMRRQDYDLLLSDIQMPETNGFEILALLRKSSIgnshTIPIVAM 618
Cdd:cd17537     3 VYVVDDDEAVRDSLAFLLRSVGLAVKTFTSASAFLAAAPPDQPGCLVLDVRMPGMSGLELQDELLARGS----NIPIIFI 78
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2737555188 619 TARGEGEK--EAFIKGGFtDSIHKPFSMRELLDMVSS 653
Cdd:cd17537    79 TGHGDVPMavEAMKAGAV-DFLEKPFRDQVLLDAIEQ 114
REC_OmpR_MtPhoP-like cd17615
phosphoacceptor receiver (REC) domain of MtPhoP-like OmpR family response regulators; ...
538-657 5.17e-09

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: 54.67  E-value: 5.17e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188 538 RVLVIDNDTLQLEIAKEMLERNGVSCTTCSNAKELVNEMRRQDYDLLLSDIQMPETNGFEILALLRKSSIGnshtIPIVA 617
Cdd:cd17615     1 RVLVVDDEPNITELLSMALRYEGWDVETAADGAEALAAAREFRPDAVVLDIMLPDMDGLEVLRRLRADGPD----VPVLF 76
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 2737555188 618 MTARGEGE-KEAFIKGGFTDSIHKPFSMRELLDMVSSVVSR 657
Cdd:cd17615    77 LTAKDSVEdRIAGLTAGGDDYVTKPFSLEEVVARLRALLRR 117
REC_TrrA-like cd17554
phosphoacceptor receiver (REC) domain of Thermotoga maritima response regulator TrrA and ...
538-620 5.92e-09

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: 54.53  E-value: 5.92e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188 538 RVLVIDNDTLQLEIAKEMLERNGVSCTTCSNAKELVNEMRRQDYDLLLSDIQMPETNGFEILALLRKSsignSHTIPIVA 617
Cdd:cd17554     2 KILVVDDEENIRELYKEELEDEGYEVVTAGNGEEALEKLESEDPDLVILDIKMPGMDGLETLRKIREK----KPDLPVII 77

                  ...
gi 2737555188 618 MTA 620
Cdd:cd17554    78 CTA 80
REC_OmpR_VirG cd17594
phosphoacceptor receiver (REC) domain of VirG-like OmpR family response regulators; VirG is ...
539-651 7.11e-09

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: 54.37  E-value: 7.11e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188 539 VLVIDNDTLQLEIAKEMLERNGVSCTTCSNAKELVNEMRRQDYDLLLSDIQMPETNGFEILALLRKSSignshTIPIVAM 618
Cdd:cd17594     2 VLVVDDDAAMRHLLILYLRERGFDVTAAADGAEEARLMLHRRVDLVLLDLRLGQESGLDLLRTIRARS-----DVPIIII 76
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2737555188 619 TA--RGEGEKEAFIKGGFTDSIHKPFSMRELLDMV 651
Cdd:cd17594    77 SGdrRDEIDRVVGLELGADDYLAKPFGLRELLARV 111
COG3920 COG3920
Two-component sensor histidine kinase, HisKA and HATPase domains [Signal transduction ...
371-515 8.67e-09

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


Pssm-ID: 443125 [Multi-domain]  Cd Length: 495  Bit Score: 58.76  E-value: 8.67e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188 371 NLNDLLERIVTGFSHIANNKGIIFHHDSQNTDVvlcgDMDR---ISQIIDNLLTNAVKF----TNAGMIQFNVRYENGML 443
Cdd:COG3920   360 DLRDYLRELLEPLRDSYGGRGIRIELDGPDVEL----PADAavpLGLILNELVTNALKHaflsGEGGRIRVSWRREDGRL 435
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2737555188 444 YIEIKDTGIGMDQDTvsrifrpferlsSEANAEGFGLGLpiTKGLVKLLGGSIDVESkiGHGSTFRVSLPLA 515
Cdd:COG3920   436 RLTVSDNGVGLPEDV------------DPPARKGLGLRL--IRALVRQLGGTLELDR--PEGTRVRITFPLA 491
HATPase_EcPhoR-like cd16952
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
416-513 1.03e-08

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


Pssm-ID: 340428 [Multi-domain]  Cd Length: 108  Bit Score: 53.75  E-value: 1.03e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188 416 IDNLLTNAVKFTNAGMiQFNVRY---ENGMlYIEIKDTGIGMDQDTVSRIFRPFERLSSE--ANAEGFGLGLPITKGLVK 490
Cdd:cd16952     5 FSNLVSNAVKYTPPSD-TITVRWsqeESGA-RLSVEDTGPGIPPEHIPRLTERFYRVDIErcRNTGGTGLGLAIVKHVMS 82
                          90       100
                  ....*....|....*....|...
gi 2737555188 491 LLGGSIDVESKIGHGSTFRVSLP 513
Cdd:cd16952    83 RHDARLLIASELGKGSRFTCLFP 105
PRK11361 PRK11361
acetoacetate metabolism transcriptional regulator AtoC;
537-647 1.19e-08

acetoacetate metabolism transcriptional regulator AtoC;


Pssm-ID: 183099 [Multi-domain]  Cd Length: 457  Bit Score: 58.32  E-value: 1.19e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188 537 QRVLVIDNDTLQLEIAKEMLERNGVSCTTCSNAKELVNEMRRQDYDLLLSDIQMPETNGFEILALLRKSSIGnshtIPIV 616
Cdd:PRK11361    5 NRILIVDDEDNVRRMLSTAFALQGFETHCANNGRTALHLFADIHPDVVLMDIRMPEMDGIKALKEMRSHETR----TPVI 80
                          90       100       110
                  ....*....|....*....|....*....|...
gi 2737555188 617 AMTARGEGEK--EAFIKGGFtDSIHKPFSMREL 647
Cdd:PRK11361   81 LMTAYAEVETavEALRCGAF-DYVIKPFDLDEL 112
REC_NtrX-like cd17550
phosphoacceptor receiver (REC) domain of nitrogen assimilation regulatory protein NtrX and ...
539-651 1.22e-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: 53.65  E-value: 1.22e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188 539 VLVIDNDTLQLEIAKEMLERNGVSCTTCSNAKELVNEMRRQDYDLLLSDIQMPETNGFEILALLRKssigNSHTIPIVAM 618
Cdd:cd17550     1 ILIVDDEEDIRESLSGILEDEGYEVDTAADGEEALKLIKERRPDLVLLDIWLPDMDGLELLKEIKE----KYPDLPVIMI 76
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2737555188 619 TARGEGEK--EAfIKGGFTDSIHKPFSMRELLDMV 651
Cdd:cd17550    77 SGHGTIETavKA-TKLGAYDFIEKPLSLDRLLLTI 110
COG4567 COG4567
DNA-binding response regulator, ActR/RegA family, consists of REC and Fis-type HTH domains ...
536-665 1.33e-08

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


Pssm-ID: 443624 [Multi-domain]  Cd Length: 177  Bit Score: 54.92  E-value: 1.33e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188 536 PQRVLVIDNDTLQLEIAKEMLERNGVSCTTCSNAKELVNEMRRQDYDLLLSDIQMPETNGFEILALLRKSsignSHTIPI 615
Cdd:COG4567     4 DRSLLLVDDDEAFARVLARALERRGFEVTTAASVEEALALLEQAPPDYAVLDLRLGDGSGLDLIEALRER----DPDARI 79
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2737555188 616 VAMTarGEG----EKEAfIKGGFTDSIHKPFSMRELLDMVSSVVSRDVEESHTP 665
Cdd:COG4567    80 VVLT--GYAsiatAVEA-IKLGADDYLAKPADADDLLAALERAEGDAPAPPENP 130
REC_OmpR_CtrA cd17616
phosphoacceptor receiver (REC) domain of CtrA-like OmpR family response regulators; CtrA is ...
539-655 1.83e-08

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


Pssm-ID: 381132 [Multi-domain]  Cd Length: 114  Bit Score: 53.18  E-value: 1.83e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188 539 VLVIDNDTLQLEIAKEMLERNGVSCTTCSNAKELVNEMRRQDYDLLLSDIQMPETNGFEILALLRKSSIgnshTIPIVAM 618
Cdd:cd17616     1 VLLIEDDSATAQSIELMLKSEGFNVYTTDLGEEGLDLGKLYDYDIILLDLNLPDMSGYEVLRTLRLAKV----KTPILIL 76
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2737555188 619 TarGEGEKEAFIKG---GFTDSIHKPFSMRELLDMVSSVV 655
Cdd:cd17616    77 S--GLADIEDKVKGlgfGADDYMTKPFHKDELVARIHAIV 114
HATPase_BvrS-ChvG-like cd16953
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
414-513 2.65e-08

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: 52.57  E-value: 2.65e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188 414 QIIDNLLTNAVKFT--NAGMIQFNVRYENGMLYIEIKDTGIGMDQDTVSRIFRPF--ERLSSEANAEGFGLGLPITKGLV 489
Cdd:cd16953     3 QVLRNLIGNAISFSppDTGRITVSAMPTGKMVTISVEDEGPGIPQEKLESIFDRFytERPANEAFGQHSGLGLSISRQII 82
                          90       100
                  ....*....|....*....|....*...
gi 2737555188 490 KLLGGSIDVESK----IGHGSTFRVSLP 513
Cdd:cd16953    83 EAHGGISVAENHnqpgQVIGARFTVQLP 110
REC_YesN-like cd17536
phosphoacceptor receiver (REC) domain of YesN and related helix-turn-helix containing response ...
539-657 3.46e-08

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: 52.34  E-value: 3.46e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188 539 VLVIDNDTLQLEIAKEMLERNGVSCT---TCSNAKELVNEMRRQDYDLLLSDIQMPETNGFEILALLRKSSIGnshtIPI 615
Cdd:cd17536     1 VLIVDDEPLIREGLKKLIDWEELGFEvvgEAENGEEALELIEEHKPDIVITDIRMPGMDGLELIEKIRELYPD----IKI 76
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 2737555188 616 VAMTARGEGE--KEAfIKGGFTDSIHKPFSMRELLDMVSSVVSR 657
Cdd:cd17536    77 IILSGYDDFEyaQKA-IRLGVVDYLLKPVDEEELEEALEKAKEE 119
REC_CheY cd17542
phosphoacceptor receiver (REC) domain of chemotaxis protein CheY; The chemotaxis response ...
538-655 4.41e-08

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


Pssm-ID: 381097 [Multi-domain]  Cd Length: 117  Bit Score: 51.90  E-value: 4.41e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188 538 RVLVIDNDTLQLEIAKEMLERNGVSCT-TCSNAKELVNEMRRQDYDLLLSDIQMPETNGFEILALLRKSSIGnshtIPIV 616
Cdd:cd17542     2 KVLIVDDAAFMRMMLKDILTKAGYEVVgEAANGEEAVEKYKELKPDLVTMDITMPEMDGIEALKEIKKIDPN----AKVI 77
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 2737555188 617 AMTARGEGE--KEAfIKGGFTDSIHKPFSMRELLDMVSSVV 655
Cdd:cd17542    78 MCSAMGQEEmvKEA-IKAGAKDFIVKPFQPERVLEAVEKVL 117
REC_LytTR_AlgR-like cd17532
phosphoacceptor receiver (REC) domain of LytTR/AlgR family response regulators similar to AlgR; ...
539-654 6.52e-08

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: 51.38  E-value: 6.52e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188 539 VLVIDNDTLQLEIAKEMLERNG--VSCTTCSNAKELVNEMRRQDYDLLLSDIQMPETNGFEILALLRKSsignSHTIPIV 616
Cdd:cd17532     1 ALIVDDEPLAREELRYLLEEHPdiEIVGEAENGEEALEAIEELKPDVVFLDIQMPGLDGLELAKKLSKL----AKPPLIV 76
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2737555188 617 AMTARGEGEKEAFIKGGFtDSIHKPFSMRELLDMVSSV 654
Cdd:cd17532    77 FVTAYDEYAVEAFELNAV-DYLLKPFSEERLAEALAKL 113
COG4192 COG4192
Signal transduction histidine kinase regulating phosphoglycerate transport system [Signal ...
177-505 1.12e-07

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


Pssm-ID: 443346 [Multi-domain]  Cd Length: 640  Bit Score: 55.46  E-value: 1.12e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188 177 ASSDKLRSLNEQLIALqaerIRNmENYTDSLRIRNRELNRKLFALLGNIsDHAQAAFRDR--------EEQIAQAHQRST 248
Cdd:COG4192   245 PSTITLRQLIDELLAI----GSG-EGGLPSLRRDELAAQATLEALAEEN-NSILEQLRTQisglvgnsREQLVALNQETA 318
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188 249 SIIT--GLIIAAILLL------VFSYLIIQKHL-KRDSLLRKKMEGV----------IDRNNE-------LLETRKNVI- 301
Cdd:COG4192   319 QLVQqsGILLLAIALLslllavLINYFYVRRRLvKRLNALSDAMAAIaagdldvpipVDGNDEigriarlLRVFRDQAIe 398
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188 302 ---------------------------------------LTISHDIRGPLNIIYGYVELAKDTRDRKRRN---HHLENIE 339
Cdd:COG4192   399 ktqeleteieerkrieknlrqtqdeliqaakmavvgqtmTSLAHELNQPLNAMSMYLFSAKKALEQENYAqlpTSLDKIE 478
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188 340 TECKHILHLLNNLLDVYRLNESKETcnnvPFNLNDLLERIVTGFSHIANNKGIIFHhdsQNTDVVLCGDMDRISQIIDNL 419
Cdd:COG4192   479 GLIERMDKIIKSLRQFSRKSDTPLQ----PVDLRQVIEQAWELVESRAKPQQITLH---IPDDLMVQGDQVLLEQVLVNL 551
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188 420 LTNAVK-FTNAGMIQFNVRYENGMLYIEIKDTGIGMdqDTVSRIFRPFerlsSEANAEGFGLGLPITKGLVKLLGGSIDV 498
Cdd:COG4192   552 LVNALDaVATQPQISVDLLSNAENLRVAISDNGNGW--PLVDKLFTPF----TTTKEVGLGLGLSICRSIMQQFGGDLYL 625

                  ....*..
gi 2737555188 499 ESKIGHG 505
Cdd:COG4192   626 ASTLERG 632
PRK09836 PRK09836
DNA-binding transcriptional activator CusR; Provisional
580-657 1.43e-07

DNA-binding transcriptional activator CusR; Provisional


Pssm-ID: 182102 [Multi-domain]  Cd Length: 227  Bit Score: 53.00  E-value: 1.43e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188 580 DYDLLLSDIQMPETNGFEILALLRKSSIGnshtIPIVAMTARGEGEKEafIKG---GFTDSIHKPFSMRELLDMVSSVVS 656
Cdd:PRK09836   44 DYDLIILDIMLPDVNGWDIVRMLRSANKG----MPILLLTALGTIEHR--VKGlelGADDYLVKPFAFAELLARVRTLLR 117

                  .
gi 2737555188 657 R 657
Cdd:PRK09836  118 R 118
HATPase_NtrY-like cd16944
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
408-513 1.63e-07

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


Pssm-ID: 340420 [Multi-domain]  Cd Length: 108  Bit Score: 50.23  E-value: 1.63e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188 408 DMDRISQIIDNLLTNAVKFTNA---GMIQFNVRYENGM---LYIEIKDTGIGMDQDTVSRIFRPFERLSSEanaeGFGLG 481
Cdd:cd16944     1 DTTQISQVLTNILKNAAEAIEGrpsDVGEVRIRVEADQdgrIVLIVCDNGKGFPREMRHRATEPYVTTRPK----GTGLG 76
                          90       100       110
                  ....*....|....*....|....*....|..
gi 2737555188 482 LPITKGLVKLLGGSIDVESKIGHGSTFRVSLP 513
Cdd:cd16944    77 LAIVKKIMEEHGGRISLSNREAGGACIRIILP 108
REC_RR468-like cd17552
phosphoacceptor receiver (REC) domain of Thermotoga maritima response regulator RR468 and ...
536-642 1.83e-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: 50.24  E-value: 1.83e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188 536 PQRVLVIDNDTLQLEIAKEMLERNG---VSctTCSNAKELVNEMRRQDYDLLLSDIQMPETNGFEILALLRKSSigNSHT 612
Cdd:cd17552     1 SKRILVIDDEEDIREVVQACLEKLAgweVL--TASSGQEGLEKAATEQPDAILLDVMMPDMDGLATLKKLQANP--ETQS 76
                          90       100       110
                  ....*....|....*....|....*....|.
gi 2737555188 613 IPIVAMTARG-EGEKEAFIKGGFTDSIHKPF 642
Cdd:cd17552    77 IPVILLTAKAqPSDRQRFASLGVAGVIAKPF 107
REC_OmpR_EcPhoP-like cd19934
phosphoacceptor receiver (REC) domain of EcPhoP-like OmpR family response regulators; ...
539-657 1.99e-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: 49.97  E-value: 1.99e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188 539 VLVIDNDTLQLEIAKEMLERNGVSCTTCSNAKELVNEMRRQDYDLLLSDIQMPETNGFEILALLRKssigNSHTIPIVAM 618
Cdd:cd19934     1 LLLVEDDALLAAQLKEQLSDAGYVVDVAEDGEEALFQGEEEPYDLVVLDLGLPGMDGLSVLRRWRS----EGRATPVLIL 76
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2737555188 619 TARG-EGEKEAFIKGGFTDSIHKPFSMRELLDMVSSVVSR 657
Cdd:cd19934    77 TARDsWQDKVEGLDAGADDYLTKPFHIEELLARLRALIRR 116
REC_PilR cd19926
phosphoacceptor receiver (REC) domain of type 4 fimbriae expression regulatory protein PilR ...
539-641 3.98e-07

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: 48.69  E-value: 3.98e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188 539 VLVIDNDTLQLEIAKEMLERNGVSCTTCSNAKELVNEMRRQDYDLLLSDIQMPETNGFEILALLRKSSIGnshtIPIVAM 618
Cdd:cd19926     1 VLVVDDEPDIRELLEITLGRMGLDVRSARNVKEARELLASEPYDLCLTDMRLPDGSGLELVQHIQQRLPQ----TPVAVI 76
                          90       100
                  ....*....|....*....|....
gi 2737555188 619 TARGEGEK-EAFIKGGFTDSIHKP 641
Cdd:cd19926    77 TAYGSLDTaIEALKAGAFDFLTKP 100
PRK10610 PRK10610
chemotaxis protein CheY;
538-657 6.83e-07

chemotaxis protein CheY;


Pssm-ID: 170568 [Multi-domain]  Cd Length: 129  Bit Score: 49.20  E-value: 6.83e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188 538 RVLVIDNDTLQLEIAKEMLERNGV-SCTTCSNAKELVNEMRRQDYDLLLSDIQMPETNGFEILALLRKSsiGNSHTIPIV 616
Cdd:PRK10610    7 KFLVVDDFSTMRRIVRNLLKELGFnNVEEAEDGVDALNKLQAGGFGFVISDWNMPNMDGLELLKTIRAD--GAMSALPVL 84
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 2737555188 617 AMTArgEGEKEAFI---KGGFTDSIHKPFSMRELLDMVSSVVSR 657
Cdd:PRK10610   85 MVTA--EAKKENIIaaaQAGASGYVVKPFTAATLEEKLNKIFEK 126
REC_hyHK_blue-like cd18161
phosphoacceptor receiver (REC) domain of hybrid sensor histidine kinase/response regulators ...
539-603 1.13e-06

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: 47.73  E-value: 1.13e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2737555188 539 VLVIDNDTLQLEIAKEMLERNGVSCTTCSNAKELVNEMRRQ-DYDLLLSDIQMP-ETNGFEILALLR 603
Cdd:cd18161     1 VLVVEDDPDVRRLTAEVLEDLGYTVLEAASGDEALDLLESGpDIDLLVTDVIMPgGMNGSQLAEEAR 67
PRK11517 PRK11517
DNA-binding response regulator HprR;
538-676 1.25e-06

DNA-binding response regulator HprR;


Pssm-ID: 183172 [Multi-domain]  Cd Length: 223  Bit Score: 50.28  E-value: 1.25e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188 538 RVLVIDNDTLQLEIAKEMLERNGVSCTTCSNAKELVNEMRRQDYDLLLSDIQMPETNGFEILALLRkssigNSHTIPIVA 617
Cdd:PRK11517    2 KILLIEDNQRTQEWVTQGLSEAGYVIDAVSDGRDGLYLALKDDYALIILDIMLPGMDGWQILQTLR-----TAKQTPVIC 76
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2737555188 618 MTARGEGEKEafIKG---GFTDSIHKPFSMRELLDMVSSVVSRdveesHTPDFATFTADVLD 676
Cdd:PRK11517   77 LTARDSVDDR--VRGldsGANDYLVKPFSFSELLARVRAQLRQ-----HHALNSTLEISGLR 131
HATPase_UhpB-NarQ-NarX-like cd16917
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
412-513 1.32e-06

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


Pssm-ID: 340394 [Multi-domain]  Cd Length: 87  Bit Score: 46.78  E-value: 1.32e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188 412 ISQIIDNLLTNAVKFTNAGMIQFNVRYENGMLYIEIKDTGIGMDQDTVSRifrpferlsseanaeGFGLGLPITKGLVKL 491
Cdd:cd16917     1 LYRIVQEALTNALKHAGASRVRVTLSYTADELTLTVVDDGVGFDGPAPPG---------------GGGFGLLGMRERAEL 65
                          90       100
                  ....*....|....*....|..
gi 2737555188 492 LGGSIDVESKIGHGSTFRVSLP 513
Cdd:cd16917    66 LGGTLTIGSRPGGGTRVTARLP 87
REC_OmpR_CusR-like cd19935
phosphoacceptor receiver (REC) domain of CusR-like OmpR family response regulators; ...
539-622 1.35e-06

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: 47.43  E-value: 1.35e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188 539 VLVIDNDTLQLEIAKEMLERNGVSCTTCSNAKELVNEMRRQDYDLLLSDIQMPETNGFEILALLRKSSIgnshTIPIVAM 618
Cdd:cd19935     1 ILVVEDEKKLAEYLKKGLTEEGYAVDVAYDGEDGLHLALTNEYDLIILDVMLPGLDGLEVLRRLRAAGK----QTPVLML 76

                  ....
gi 2737555188 619 TARG 622
Cdd:cd19935    77 TARD 80
PRK10766 PRK10766
two-component system response regulator TorR;
535-682 1.45e-06

two-component system response regulator TorR;


Pssm-ID: 182711 [Multi-domain]  Cd Length: 221  Bit Score: 50.04  E-value: 1.45e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188 535 LPQRVLVIDNDTLQLEIAKEMLERNGVSCTTCSNAKELVNEMRRQDYDLLLSDIQMPETNGFEILALLRKSSignshTIP 614
Cdd:PRK10766    1 MSYHILVVEDEPVTRARLQGYFEQEGYTVSEAASGAGMREIMQNQHVDLILLDINLPGEDGLMLTRELRSRS-----TVG 75
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2737555188 615 IVAMTARGEG-EKEAFIKGGFTDSIHKPFSMRELL----------DMVSSVVSRDVEESHTPDFATFTADVlDKRELLR 682
Cdd:PRK10766   76 IILVTGRTDSiDRIVGLEMGADDYVTKPLELRELLvrvknllwriSLARQAQPHAQEEDNCYRFAGYCLNV-SRRTLER 153
REC_NtrC1-like cd17572
phosphoacceptor receiver (REC) domain of nitrogen regulatory protein C 1 (NtrC1) from Aquifex ...
539-647 1.66e-06

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: 47.58  E-value: 1.66e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188 539 VLVIDnDTLQLEIA-KEMLERNGVSCTTCSNAKELVNEMRRQDYDLLLSDIQMPETNGFEILALLRKSSIgnshTIPIVA 617
Cdd:cd17572     1 VLLVE-DSPSLAALyQEYLSDEGYKVTHVETGKEALAFLSDQPPDVVLLDLKLPDMSGMEILKWIQERSL----PTSVIV 75
                          90       100       110
                  ....*....|....*....|....*....|..
gi 2737555188 618 MTARGEGEK--EAfIKGGFTDSIHKPFSMREL 647
Cdd:cd17572    76 ITAHGSVDIavEA-MRLGAYDFLEKPFDADRL 106
HATPase_CreC-like cd16945
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
414-508 1.70e-06

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: 47.07  E-value: 1.70e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188 414 QIIDNLLTNAVKFTNA-GMIQFNVRYENGMLYIEIKDTGIGMDQDTVSRIFRPFERLSSEANAE-GFGLGLPITKGLVKL 491
Cdd:cd16945     7 QAINNLLDNAIDFSPEgGLIALQLEADTEGIELLVFDEGSGIPDYALNRVFERFYSLPRPHSGQkSTGLGLAFVQEVAQL 86
                          90
                  ....*....|....*..
gi 2737555188 492 LGGSIDVESKIGHGSTF 508
Cdd:cd16945    87 HGGRITLRNRPDGVLAF 103
REC_2_GGDEF cd17544
second phosphoacceptor receiver (REC) domain of uncharacterized GGDEF domain proteins; This ...
538-647 2.19e-06

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: 47.13  E-value: 2.19e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188 538 RVLVIDNDTLQLEIAKEMLERNGVSCTTCSNAKELVNEMRRQ-DYDLLLSDIQMPETNGFEILALLRKSSigNSHTIPIV 616
Cdd:cd17544     2 KVLVVDDSATSRNHLRALLRRHNFQVLEAANGQEALEVLEQHpDIKLVITDYNMPEMDGFELVREIRKKY--SRDQLAII 79
                          90       100       110
                  ....*....|....*....|....*....|..
gi 2737555188 617 AMTARGEGEKEA-FIKGGFTDSIHKPFSMREL 647
Cdd:cd17544    80 GISASGDNALSArFIKAGANDFLTKPFLPEEF 111
REC_RcNtrC-like cd19928
phosphoacceptor receiver (REC) domain of Rhodobacter capsulatus nitrogen regulatory protein C ...
539-621 2.35e-06

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: 46.73  E-value: 2.35e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188 539 VLVIDNDTLQLEIAKEMLERNGVSCTTCSNAKELVNEMRRQDYDLLLSDIQMPETNGFEILALLRKSSIGnshtIPIVAM 618
Cdd:cd19928     1 ILVADDDRAIRTVLTQALGRAGYEVRTTGNAATLWRWVEEGEGDLVITDVVMPDENGLDLIPRIKKARPD----LPIIVM 76

                  ...
gi 2737555188 619 TAR 621
Cdd:cd19928    77 SAQ 79
PRK10643 PRK10643
two-component system response regulator PmrA;
538-662 2.56e-06

two-component system response regulator PmrA;


Pssm-ID: 182612 [Multi-domain]  Cd Length: 222  Bit Score: 49.26  E-value: 2.56e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188 538 RVLVIDNDTLQLEIAKEMLERNGVSCTTCSNAKELVNEMRRQDYDLLLSDIQMPETNGFEILALLRKssigNSHTIPIVA 617
Cdd:PRK10643    2 KILIVEDDTLLLQGLILALQTEGYACDCASTAREAEALLESGHYSLVVLDLGLPDEDGLHLLRRWRQ----KKYTLPVLI 77
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 2737555188 618 MTARGEGEKEafIKG---GFTDSIHKPFSMRELLDMVSSVVSRDVEES 662
Cdd:PRK10643   78 LTARDTLEDR--VAGldvGADDYLVKPFALEELHARIRALIRRHQGQG 123
HATPase_PhoQ-like cd16954
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
374-512 2.66e-06

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


Pssm-ID: 340430 [Multi-domain]  Cd Length: 135  Bit Score: 47.24  E-value: 2.66e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188 374 DLLERIVTGFSHIANNKGIIFHHDSqNTDVVLCGDMDRISQIIDNLLTNAVKFTNaGMIQFNVRYENGMLYIEIKDTGIG 453
Cdd:cd16954     1 PLLDSLCSALNKVYQRKGVSISLDI-SPELRFPGERNDLMELLGNLLDNACKWCL-EFVEVTARQTDGGLHLIVDDDGPG 78
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188 454 MDQDTVSRIFRPFERLSSEanAEGFGLGLPITKGLVKLLGGSIDVE-SKIGhGSTFRVSL 512
Cdd:cd16954    79 VPESQRSKIFQRGQRLDEQ--RPGQGLGLAIAKEIVEQYGGELSLSdSPLG-GARFEVVF 135
PRK09835 PRK09835
Cu(+)/Ag(+) sensor histidine kinase;
368-513 3.12e-06

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


Pssm-ID: 182101 [Multi-domain]  Cd Length: 482  Bit Score: 50.54  E-value: 3.12e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188 368 VPFNLNDLLERIVTGFSHIANNKGIIFHHDSQNTDVVlcGDMDRISQIIDNLLTNAVKFTNAG-MIQFNVRYENGMLYIE 446
Cdd:PRK09835  334 KMLDLADEVGKVFDFFEAWAEERGVELRFVGDPCQVA--GDPLMLRRAISNLLSNALRYTPAGeAITVRCQEVDHQVQLV 411
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2737555188 447 IKDTGIGMDQDTVSRIFRPFERL--SSEANAEGFGLGLPITKGLVKLLGGSIDVESKIgHGSTFRVSLP 513
Cdd:PRK09835  412 VENPGTPIAPEHLPRLFDRFYRVdpSRQRKGEGSGIGLAIVKSIVVAHKGTVAVTSDA-RGTRFVISLP 479
REC_OmpR_NsrR-like cd18159
phosphoacceptor receiver (REC) domain of Streptococcus agalactiae NsrR-like OmpR family ...
540-654 3.75e-06

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: 46.51  E-value: 3.75e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188 540 LVIDNDTLQLEIAKeMLERNGVSCTTCSNAKELVNEMRRQDYDLLLSDIQMPETNGFEILALLRKSSignshTIPIVAMT 619
Cdd:cd18159     3 IVEDDETIASLLKK-HLEKWGYEVVLIEDFEDVLEEFLQFKPDLVLLDINLPYFDGFYWCREIRQIS-----NVPIIFIS 76
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2737555188 620 AR-GEGEKEAFIKGGFTDSIHKPFSMRELLDMVSSV 654
Cdd:cd18159    77 SRdDNMDQVMAINMGGDDYITKPFDLDVLLAKIKAI 112
CitB COG2197
DNA-binding response regulator, NarL/FixJ family, contains REC and HTH domains [Signal ...
538-602 3.80e-06

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


Pssm-ID: 441799 [Multi-domain]  Cd Length: 131  Bit Score: 46.81  E-value: 3.80e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2737555188 538 RVLVIDNDTLQLEIAKEMLERNG--VSCTTCSNAKELVNEMRRQDYDLLLSDIQMPETNGFEILALL 602
Cdd:COG2197     3 RVLIVDDHPLVREGLRALLEAEPdiEVVGEAADGEEALELLEELRPDVVLLDIRMPGMDGLEALRRL 69
REC_RocR cd17530
phosphoacceptor receiver (REC) domain of response regulator RocR; The response regulator RocR ...
538-653 3.81e-06

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: 46.67  E-value: 3.81e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188 538 RVLVIDNDTLQLEIAKEMLERNGV-SCTTCSNAKELVNEMRRQDYDLLLSDIQMPETNGFEIlalLRKssIGNSHT-IPI 615
Cdd:cd17530     2 RVLVLDDDPFQCMMAATILEDLGPgNVDEADDGREALVILLCNAPDIIICDLKMPDMDGIEF---LRH--LAESHSnAAV 76
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 2737555188 616 VAMTARGEGEKEAFIKGG------FTDSIHKPFSMRELLDMVSS 653
Cdd:cd17530    77 ILMSGLDGGILESAETLAganglnLLGTLSKPFSPEELTELLTK 120
CheA COG0643
Chemotaxis protein histidine kinase CheA [Signal transduction mechanisms];
429-514 4.11e-06

Chemotaxis protein histidine kinase CheA [Signal transduction mechanisms];


Pssm-ID: 440408 [Multi-domain]  Cd Length: 563  Bit Score: 50.18  E-value: 4.11e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188 429 AGMIQFNVRYENGMLYIEIKDTGIGMD------------------------QDTVSRIFRPferlsseanaeGF------ 478
Cdd:COG0643   308 TGTITLSAYHEGGRVVIEVSDDGRGLDlekirakaiekglitaeeaaalsdEELLELIFAP-----------GFstaeev 376
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 2737555188 479 ------GLGLPITKGLVKLLGGSIDVESKIGHGSTFRVSLPL 514
Cdd:COG0643   377 tdlsgrGVGMDVVKTNIEALGGTIEIESEPGKGTTFTLRLPL 418
REC_HupR-like cd17569
phosphoacceptor receiver (REC) domain of hydrogen uptake protein regulator (HupR) and similar ...
538-604 4.85e-06

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


Pssm-ID: 381113 [Multi-domain]  Cd Length: 118  Bit Score: 46.24  E-value: 4.85e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2737555188 538 RVLVIDNDTLQLEIAKEMLERNGVSCTTCSNAKELVNEMRRQDYDLLLSDIQMPETNGFEILALLRK 604
Cdd:cd17569     2 TILLVDDEPNILKALKRLLRREGYEVLTATSGEEALEILKQEPVDVVISDQRMPGMDGAELLKRVRE 68
PRK10365 PRK10365
sigma-54-dependent response regulator transcription factor ZraR;
539-764 6.29e-06

sigma-54-dependent response regulator transcription factor ZraR;


Pssm-ID: 182412 [Multi-domain]  Cd Length: 441  Bit Score: 49.26  E-value: 6.29e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188 539 VLVIDNDTLQLEIAKEMLERNGVSCTTCSNAKELVNEMRRQDYDLLLSDIQMPETNGFEILALLRkssiGNSHTIPIVAM 618
Cdd:PRK10365    8 ILVVDDDISHCTILQALLRGWGYNVALANSGRQALEQVREQVFDLVLCDVRMAEMDGIATLKEIK----ALNPAIPVLIM 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188 619 TARGEGEK--EAfIKGGFTDSIHKPFSMRELLD-MVSSVVSRDVEESHTPDFATFTADVLDKRELLRTFIiqSEQNMADL 695
Cdd:PRK10365   84 TAYSSVETavEA-LKTGALDYLIKPLDFDNLQAtLEKALAHTHSIDAETPAVTASQFGMVGKSPAMQHLL--SEIALVAP 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2737555188 696 QSAI-----KTGDIEKLhdIAHEIKPSLEllRADAPLVklrtTLNDSACDMNTVNEQvklLIGHISGLITEAEK 764
Cdd:PRK10365  161 SEATvlihgDSGTGKEL--VARAIHASSA--RSEKPLV----TLNCAALNESLLESE---LFGHEKGAFTGADK 223
YesM COG2972
Sensor histidine kinase YesM [Signal transduction mechanisms];
430-514 7.09e-06

Sensor histidine kinase YesM [Signal transduction mechanisms];


Pssm-ID: 442211 [Multi-domain]  Cd Length: 445  Bit Score: 49.25  E-value: 7.09e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188 430 GMIQFNVRYENGMLYIEIKDTGIGMDQDTVSRIFRPFERlsseaNAEGFGLGLPITKGLVKLL---GGSIDVESKIGHGS 506
Cdd:COG2972   360 GTIRISIRKEGDRLVITVEDNGVGMPEEKLEKLLEELSS-----KGEGRGIGLRNVRERLKLYygeEYGLEIESEPGEGT 434

                  ....*...
gi 2737555188 507 TFRVSLPL 514
Cdd:COG2972   435 TVTIRIPL 442
HATPase_PDK-like cd16929
Histidine kinase-like ATPase domain of pyruvate dehydrogenase kinase, branched-chain ...
432-513 8.52e-06

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: 46.56  E-value: 8.52e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188 432 IQFNVRYENGMLYIEIKDTGIGMDQDTVSRIF---------------RPFERLSSEANAEGFGLGLPITKGLVKLLGGSI 496
Cdd:cd16929    73 IKVTVAKGDEDLTIKISDRGGGIPREDLARLFsymystapqpslddfSDLISGTQPSPLAGFGYGLPMSRLYAEYFGGDL 152
                          90
                  ....*....|....*..
gi 2737555188 497 DVESKIGHGSTFRVSLP 513
Cdd:cd16929   153 DLQSMEGYGTDVYIYLK 169
REC_CheV-like cd19924
phosphoacceptor receiver (REC) domain of chemotaxis protein CheV and similar proteins; This ...
539-604 9.39e-06

phosphoacceptor receiver (REC) domain of chemotaxis protein CheV and similar proteins; This subfamily includes the REC domains of Bacillus subtilis chemotaxis protein CheV, Myxococcus xanthus gliding motility regulatory protein FrzE, and similar proteins. CheV is a hybrid protein with an N-terminal CheW-like domain and a C-terminal CheY-like REC domain. The CheV pathway is one of three systems employed by B. subtilis for sensory adaptation that contribute to chemotaxis. It is involved in the transmission of sensory signals from chemoreceptors to flagellar motors. Together with CheW, it is involved in the coupling of methyl-accepting chemoreceptors to the central two-component histidine kinase CheA. FrzE is a hybrid sensor histidine kinase/response regulator that is part of the Frz pathway that controls cell reversal frequency to support directional motility during swarming and fruiting body formation. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381151 [Multi-domain]  Cd Length: 111  Bit Score: 45.06  E-value: 9.39e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2737555188 539 VLVIDNDTLQLEIAKEMLERNGVSCTTCSNAKELVNEM---------RRQDYDLLLSDIQMPETNGFEILALLRK 604
Cdd:cd19924     1 ILVVDDSPTARKQLRDLLKNLGFEIAEAVDGEEALNKLenlakegndLSKELDLIITDIEMPKMDGYELTFELRD 75
HATPase_ETR2_ERS2-EIN4-like cd16938
Histidine kinase-like ATPase domain of Arabidopsis thaliana ETR2, ERS2, and EIN4, and related ...
404-512 9.73e-06

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


Pssm-ID: 340415 [Multi-domain]  Cd Length: 133  Bit Score: 45.91  E-value: 9.73e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188 404 VLCGDMDRISQIIDNLLTNAVKFTN-AGMIQFNVRYENGMLYIEIKDTGIG---MDQDTV-------------SRIFRPF 466
Cdd:cd16938     4 VVVGDERRVFQVLLHMLGNLLKMRNgGGNITFRVFLEGGSEDRSDRDWGPWrpsMSDESVeirfeveindsgsPSIESAS 83
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 2737555188 467 ERLS----SEANAEGFGLGLPITKGLVKLLGGSIDVESKIGHGSTFRVSL 512
Cdd:cd16938    84 MRNSlnrrYNLSELGEHLSFSICKQLVQLMGGNIWIVPGSGLGTTMSLLL 133
PRK11083 PRK11083
DNA-binding response regulator CreB; Provisional
538-657 9.76e-06

DNA-binding response regulator CreB; Provisional


Pssm-ID: 236838 [Multi-domain]  Cd Length: 228  Bit Score: 47.65  E-value: 9.76e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188 538 RVLVIDN-----DTLQLeiakeMLERNGVSCTTCSNAKELVNEMRRQDYDLLLSDIQMPETNGFEIL-ALLRKSSignsh 611
Cdd:PRK11083    5 TILLVEDeqaiaDTLVY-----ALQSEGFTVEWFERGLPALDKLRQQPPDLVILDVGLPDISGFELCrQLLAFHP----- 74
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 2737555188 612 TIPIVAMTAR-GEGEKEAFIKGGFTDSIHKPFSMRELLDMVSSVVSR 657
Cdd:PRK11083   75 ALPVIFLTARsDEVDRLVGLEIGADDYVAKPFSPREVAARVRTILRR 121
REC_OmpR_ChvI-like cd19936
phosphoacceptor receiver (REC) domain of ChvI-like OmpR family response regulators; ...
539-641 1.02e-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: 44.74  E-value: 1.02e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188 539 VLVIDNDTLQLEIAKEMLERNGVSCTTCSNAKELVNEMRRQDYDLLLSDIQMPETNGFEILALLRKSSignshTIPIVAM 618
Cdd:cd19936     1 IALVDDDRNILTSVSMALEAEGFSVETYTDGASALDGLNARPPDLAILDIKMPRMDGMELLQRLRQKS-----TLPVIFL 75
                          90       100
                  ....*....|....*....|....
gi 2737555188 619 TARGEGEKEAF-IKGGFTDSIHKP 641
Cdd:cd19936    76 TSKDDEIDEVFgLRMGADDYITKP 99
REC_PatA-like cd17602
phosphoacceptor receiver (REC) domain of PatA and similar domains; Nostoc sp. (or Anabaena sp.) ...
539-641 1.20e-05

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: 44.67  E-value: 1.20e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188 539 VLVIDNDTLQLEIAKEMLERNGVSCTTCSNAKELVNEMRRQDYDLLLSDIQMPETNGFEILALLRKSSIGNShtIPIVAM 618
Cdd:cd17602     1 VACVDDRPSIQKMIEYFLEKQGFRVVVIDDPLRALTTLLNSKPDLILIDIDMPDLDGYELCSLLRKSSALKD--TPIIML 78
                          90       100
                  ....*....|....*....|....*....
gi 2737555188 619 TargegEKEAFIKG------GFTDSIHKP 641
Cdd:cd17602    79 T-----GKDGLVDRirakmaGASGYLTKP 102
PRK11644 PRK11644
signal transduction histidine-protein kinase/phosphatase UhpB;
389-514 1.53e-05

signal transduction histidine-protein kinase/phosphatase UhpB;


Pssm-ID: 236945 [Multi-domain]  Cd Length: 495  Bit Score: 48.44  E-value: 1.53e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188 389 NKGIIFHHDSQNTDVVLcGDMDRIS--QIIDNLLTNAVKFTNAGMIQFNVRYENGMLYIEIKDTGIGMDQDTVSRifrpf 466
Cdd:PRK11644  387 DRGIVSHLDWRIDESAL-SETQRVTlfRVCQEGLNNIVKHADASAVTLQGWQQDERLMLVIEDDGSGLPPGSGQQ----- 460
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2737555188 467 erlsseanaeGFGLglpitKGL---VKLLGGSIDVESKigHGSTFRVSLPL 514
Cdd:PRK11644  461 ----------GFGL-----RGMrerVTALGGTLTISCT--HGTRLSVSLPQ 494
PRK10337 PRK10337
sensor protein QseC; Provisional
369-493 1.89e-05

sensor protein QseC; Provisional


Pssm-ID: 182388 [Multi-domain]  Cd Length: 449  Bit Score: 47.72  E-value: 1.89e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188 369 PFNLNDLLERIVTGFSHIANNKGIIFHHDSQNTDVVLCGDMDRISQIIDNLLTNAVKFTNAGMiQFNVRYENGmlYIEIK 448
Cdd:PRK10337  310 EIPLEDLLQSAVMDIYHTAQQAGIDVRLTLNAHPVIRTGQPLLLSLLVRNLLDNAIRYSPQGS-VVDVTLNAR--NFTVR 386
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 2737555188 449 DTGIGMDQDTVSRIFRPFERLSSEaNAEGFGLGLPITKGLVKLLG 493
Cdd:PRK10337  387 DNGPGVTPEALARIGERFYRPPGQ-EATGSGLGLSIVRRIAKLHG 430
REC_citrate_TCS cd19925
phosphoacceptor receiver (REC) domain of citrate family two-component system response ...
538-647 2.23e-05

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


Pssm-ID: 381152 [Multi-domain]  Cd Length: 118  Bit Score: 44.16  E-value: 2.23e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188 538 RVLVIDNDTLQLEIAKEMLER-NGVS-CTTCSNAKELVNEMRRQDYDLLLSDIQMPETNGFEILALLRKSsignSHTIPI 615
Cdd:cd19925     2 NVLIVEDDPMVAEIHRAYVEQvPGFTvIGTAGTGEEALKLLKERQPDLILLDIYLPDGNGLDLLRELRAA----GHDVDV 77
                          90       100       110
                  ....*....|....*....|....*....|....
gi 2737555188 616 VAMTARGEGE--KEAfIKGGFTDSIHKPFSMREL 647
Cdd:cd19925    78 IVVTAANDVEtvREA-LRLGVVDYLIKPFTFERL 110
REC_RegA-like cd17563
phosphoacceptor receiver (REC) domain of photosynthetic apparatus regulatory protein RegA; ...
537-604 2.71e-05

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


Pssm-ID: 381111 [Multi-domain]  Cd Length: 112  Bit Score: 43.97  E-value: 2.71e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2737555188 537 QRVLVIDNDTLQLEIAKEMLERNGVSCTTCSNAKELVNEMRRQDYDLLLSDIQMPETNGFEILALLRK 604
Cdd:cd17563     1 KSLLLVDDDEVFAERLARALERRGFEVETAHSVEEALALAREEKPDYAVLDLRLGGDSGLDLIPPLRA 68
HPtr COG2198
HPt (histidine-containing phosphotransfer) domain [Signal transduction mechanisms];
3-725 2.79e-05

HPt (histidine-containing phosphotransfer) domain [Signal transduction mechanisms];


Pssm-ID: 441800 [Multi-domain]  Cd Length: 871  Bit Score: 47.73  E-value: 2.79e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188   3 RNIPLQAKILFGYMMLMAVIISMAAILFHEHARLRKIEADTYEIRQARRDISEIHRNITVLASLGESVIAWEDEDYHAYQ 82
Cdd:COG2198    94 LLLLLLLLLALLLLLLLLLALLLLLLLLLLLLLLLLLLLALLLLLLLLLALLLLLLLLLVLAALLLLLLLALLLALLLLV 173
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188  83 TRRLRVDSLLQMLQTNHSYIFGLSQIDTLQQLLADKETHLHQIMQVFHRQDKADSLLVNHLPEAARQATQTRTVVQKKKG 162
Cdd:COG2198   174 LLVLLLLLLLLLLLLLLLLLLLLLLLLALTLAALLELLAAELALEALLAELAAEAAAALAAELALAELAALLLLLLLLLL 253
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188 163 IAGWFGGKETVQVPASSDKLRSLNEQLIALQAERIRNMENYTDSLRIRNRELNRKLFALLGNISDHAQAAFRDREEQIAQ 242
Cdd:COG2198   254 LLILLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLELLLLLLLALLLLLLLLLLLLLLLLLLLLLLLLL 333
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188 243 AHQRSTSIITGLIIAAILLLVFSYLIIQKHLKRDSLLRKKMEGVIDRNNELLETRKNVILTISHDIRGPLNIIYGYVELA 322
Cdd:COG2198   334 LLLLLLLLLLLLLLLLALLLLALLLALLLAAAAALAAALEALLTELALILLLLLLLLLLLILLGLLLLLLLSLLLSLLLL 413
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188 323 KDTRDRKRRNHHLENIETECKHILHLLNNLLDVYRLNESKETCNNVPFNLNDLLERIVTGFSHIANNKGIIFHHDSQNTD 402
Cdd:COG2198   414 LLLLLLLLLLLLLLLLLLLLLLLLLLLGLLLLLLLLLGLLLLLLLGLLLLALLLLLLLLLLLLLLLLLLLLLLLLLLLLL 493
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188 403 VVLCGDMDRISQIIDNLLTNAVKFTNAGMIQFNVRYENGMLYIEIKDTGIGMDQDTVSRIFRPFERLSSEANAEGFGLGL 482
Cdd:COG2198   494 LLLLLLLLLLLLLVAAALAALALLLLLALLLLLLLDLLILGLLLILLLLLLGLLALGLAALLLLLALLLGLGLLLGLLLG 573
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188 483 PITKGLVKLLGGSIDVESKIGHGSTFRVSLPLAVSNEKINSEASAVPQDRLPLPQRVLVIDNDTLQLEIAKEMLERNGVS 562
Cdd:COG2198   574 GLLLLLLLLLLLLLLLLLLLLLLLLLLALLLALLAAAAALLLLLLLLALLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLA 653
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188 563 CTTCSNAKELVNEMRRQDYDLLLSDIQMPETNGFEILALLRKSSIGNSHTIPIVAMTARGEGEKEAFIKGGFTDSIHKPF 642
Cdd:COG2198   654 VLLAAAAAAAALAALDLLLDLDDMMMMLDDMMAEAARARALAARAAAIAAAAAAAAAAAAAAAAAAAALLAALLLLLLLL 733
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188 643 SMRELLDMVSSVVSRDVEESHTPDFATFTADVLDKR----------ELLRTFIIQSEQNMADLQSAIKTGDIEKLHDIAH 712
Cdd:COG2198   734 LLLLLLLLLLLLAAAAAAAASPAAPALPVLDLEALRrlggdpellrELLELFLEELPELLAELRQALAAGDLEALARLAH 813
                         730
                  ....*....|...
gi 2737555188 713 EIKPSLELLRADA 725
Cdd:COG2198   814 KLKGSAGNLGAPR 826
cpxA PRK09470
envelope stress sensor histidine kinase CpxA;
416-514 3.27e-05

envelope stress sensor histidine kinase CpxA;


Pssm-ID: 236532 [Multi-domain]  Cd Length: 461  Bit Score: 47.23  E-value: 3.27e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188 416 IDNLLTNAVKFTNAgMIQFNVRYENGMLYIEIKDTGIGMDQDTVSRIFRPFERLsSEANAE---GFGLGLPITKGLVKLL 492
Cdd:PRK09470  358 LENIVRNALRYSHT-KIEVAFSVDKDGLTITVDDDGPGVPEEEREQIFRPFYRV-DEARDResgGTGLGLAIVENAIQQH 435
                          90       100
                  ....*....|....*....|...
gi 2737555188 493 GGSIDVE-SKIGhGSTFRVSLPL 514
Cdd:PRK09470  436 RGWVKAEdSPLG-GLRLTIWLPL 457
fixJ PRK09390
response regulator FixJ; Provisional
539-662 4.01e-05

response regulator FixJ; Provisional


Pssm-ID: 181815 [Multi-domain]  Cd Length: 202  Bit Score: 45.38  E-value: 4.01e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188 539 VLVIDNDTLQLEIAKEMLERNGVSCTTCSNAKELVNEMRRQDYDLLLSDIQMPETNGFEILALLRKssigNSHTIPIVAM 618
Cdd:PRK09390    6 VHVVDDDEAMRDSLAFLLDSAGFEVRLFESAQAFLDALPGLRFGCVVTDVRMPGIDGIELLRRLKA----RGSPLPVIVM 81
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 2737555188 619 TarGEGE----KEAfIKGGFTDSIHKPFSMRELLDMVSSVVSRDVEES 662
Cdd:PRK09390   82 T--GHGDvplaVEA-MKLGAVDFIEKPFEDERLIGAIERALAQAPEAA 126
PRK15115 PRK15115
response regulator GlrR; Provisional
536-622 4.50e-05

response regulator GlrR; Provisional


Pssm-ID: 185070 [Multi-domain]  Cd Length: 444  Bit Score: 46.75  E-value: 4.50e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188 536 PQRVLVIDNDTLQLEIAKEMLERNGVSCTTCSNAKELVNEMRRQDYDLLLSDIQMPETNGFEILALLRKSSIGnshtIPI 615
Cdd:PRK15115    5 PAHLLLVDDDPGLLKLLGMRLTSEGYSVVTAESGQEALRVLNREKVDLVISDLRMDEMDGMQLFAEIQKVQPG----MPV 80

                  ....*..
gi 2737555188 616 VAMTARG 622
Cdd:PRK15115   81 IILTAHG 87
REC_RssB-like cd17555
phosphoacceptor receiver (REC) domain of Pseudomonas aeruginosa RssB and similar domains; ...
538-622 4.74e-05

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: 43.34  E-value: 4.74e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188 538 RVLVIDNDTLQLEIAKEMLERNGVSCTTCSNAKELVNEMRRQDYDLLLSDIQMPETNGFEILALLRKSSIGnshtIPIVA 617
Cdd:cd17555     2 TILVIDDDEVVRESIAAYLEDSGFQVLQAADGRQGLELFRSEQPDLVLCDLRMPEMDGLEVLKQITKESPD----TPVIV 77

                  ....*
gi 2737555188 618 MTARG 622
Cdd:cd17555    78 VSGAG 82
REC_NarL-like cd17535
phosphoacceptor receiver (REC) domain of NarL (Nitrate/Nitrite response regulator L) family ...
539-654 5.20e-05

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: 43.27  E-value: 5.20e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188 539 VLVIDNDTLQLEIAKEMLERNG----VSctTCSNAKELVNEMRRQDYDLLLSDIQMPETNGFEILALLRKSsignSHTIP 614
Cdd:cd17535     1 VLIVDDHPLVREGLRRLLESEPdievVG--EAADGEEALALLRELRPDVVLMDLSMPGMDGIEALRRLRRR----YPDLK 74
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 2737555188 615 IVAMTARGEGE--KEAfIKGGFTDSIHKPFSMRELLDMVSSV 654
Cdd:cd17535    75 VIVLTAHDDPEyvLRA-LKAGAAGYLLKDSSPEELIEAIRAV 115
REC_hyHK cd17598
phosphoacceptor receiver (REC) domain of uncharacterized hybrid sensor histidine kinase ...
539-648 5.25e-05

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: 43.08  E-value: 5.25e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188 539 VLVIDNDTLQLEIAKEMLERNGVSCTTCSNAKELVNEMRRQDYDLLLSDIQMPETNGFEilaLLRK-SSIGNSHTIPIVA 617
Cdd:cd17598     1 ILIVEDSPTQAEQLKHILEEQGYKVQVARNGREALAMLAEHRPTLVISDIVMPEMDGYE---LCRKiKSDPDLKDIPVIL 77
                          90       100       110
                  ....*....|....*....|....*....|....
gi 2737555188 618 MTARGEGEKeaFIKG---GFTDSIHKPFSMRELL 648
Cdd:cd17598    78 LTTLSDPRD--VIRGlecGADNFITKPYDEKYLL 109
RsbW COG2172
Anti-sigma regulatory factor (Ser/Thr protein kinase) [Signal transduction mechanisms];
408-514 5.65e-05

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


Pssm-ID: 441775 [Multi-domain]  Cd Length: 127  Bit Score: 43.36  E-value: 5.65e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188 408 DMDRISQIIDNLLTNAVKFTNA----GMIQFNVRYENGMLYIEIKDTGIGMDQDTVSRIFRPFERLsseanaegfGLGLP 483
Cdd:COG2172    31 DADDLVLAVSEAVTNAVRHAYGgdpdGPVEVELELDPDGLEIEVRDEGPGFDPEDLPDPYSTLAEG---------GRGLF 101
                          90       100       110
                  ....*....|....*....|....*....|.
gi 2737555188 484 ITKGLVKllggSIDVESKIGhGSTFRVSLPL 514
Cdd:COG2172   102 LIRRLMD----EVEYESDPG-GTTVRLVKRL 127
REC_CheY4-like cd17562
phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY4 and similar CheY ...
538-655 5.82e-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: 43.06  E-value: 5.82e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188 538 RVLVIDNDTLQLEIAKEMLERNGVSCTTCSNAKELVNEMRRQDYDLLLSDIQMPETNGFEILALLRKSSigNSHTIPIVA 617
Cdd:cd17562     2 KILAVDDSASIRQMVSFTLRGAGYEVVEAADGRDALSKAQSKKFDLIITDQNMPNMDGIELIKELRKLP--AYKFTPILM 79
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2737555188 618 MTARGEGEKEAFIK-GGFTDSIHKPFSMRELLDMVSSVV 655
Cdd:cd17562    80 LTTESSDEKKQEGKaAGATGWLVKPFDPEQLLEVVKKVL 118
REC_HP-RR-like cd17573
phosphoacceptor receiver (REC) domain of orphan response regulator HP-RR and similar proteins; ...
539-648 7.28e-05

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


Pssm-ID: 381115 [Multi-domain]  Cd Length: 110  Bit Score: 42.80  E-value: 7.28e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188 539 VLVIDND-TLQLEIAKEmLERNGVSCTTCSNAKELVNEMRRQDYDLLLSDIQMPETNGFEILALLRKssigNSHTIPIVA 617
Cdd:cd17573     1 ILLIEDDsTLGKEISKG-LNEKGYQADVAESLKDGEYYIDIRNYDLVLVSDKLPDGNGLSIVSRIKE----KHPSIVVIV 75
                          90       100       110
                  ....*....|....*....|....*....|...
gi 2737555188 618 MTAR--GEGEKEAFiKGGFTDSIHKPFSMRELL 648
Cdd:cd17573    76 LSDNpkTEQEIEAF-KEGADDYIAKPFDFKVLV 107
PRK13560 PRK13560
hypothetical protein; Provisional
374-515 8.88e-05

hypothetical protein; Provisional


Pssm-ID: 106506 [Multi-domain]  Cd Length: 807  Bit Score: 46.20  E-value: 8.88e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188 374 DLLERIVTGFSHIANNKGIIFHHDSQNTDV-VLCGDMDRI---SQIIDNLLTNAVKF----TNAGMIQFNVRYE-NGMLY 444
Cdd:PRK13560  670 DFLDYIESLTAHLKNSFAIDFGRIDCKIDAdDGCLDIDKAipcGLIISELLSNALKHafpdGAAGNIKVEIREQgDGMVN 749
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2737555188 445 IEIKDTGIGMDQDtvsrifrpFERLSSEAnaegfgLGLPITKGLVKLLGGSIDVESKigHGSTFRVSLPLA 515
Cdd:PRK13560  750 LCVADDGIGLPAG--------FDFRAAET------LGLQLVCALVKQLDGEIALDSR--GGARFNIRFPMS 804
REC_PdtaR-like cd19932
phosphoacceptor receiver (REC) domain of PdtaR and similar proteins; This subfamily includes ...
538-657 9.44e-05

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


Pssm-ID: 381159 [Multi-domain]  Cd Length: 118  Bit Score: 42.40  E-value: 9.44e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188 538 RVLVIDNDTLQLEIAKEMLERNGVSCT-TCSNAKELVNEMRRQDYDLLLSDIQMPETNGFEILALLRKSSIGnshtiPIV 616
Cdd:cd19932     2 RVLIAEDEALIRMDLREMLEEAGYEVVgEASDGEEAVELAKKHKPDLVIMDVKMPRLDGIEAAKIITSENIA-----PIV 76
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 2737555188 617 AMTARGEGE--KEAFIKGGFTdSIHKPFSMRELLDMVSSVVSR 657
Cdd:cd19932    77 LLTAYSQQDlvERAKEAGAMA-YLVKPFSESDLIPAIEMAIAR 118
REC_Spo0F-like cd17553
phosphoacceptor receiver (REC) domain of Spo0F and similar domains; Spo0F, a stand-alone ...
537-653 1.20e-04

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


Pssm-ID: 381105 [Multi-domain]  Cd Length: 117  Bit Score: 42.16  E-value: 1.20e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188 537 QRVLVIDNDTLQLEIAKEMLERNGVSCTTCSNAKELVNEMRRQDYDLLLSDIQMPETNGFEILALLRKSsignSHTIPIV 616
Cdd:cd17553     1 EKILIVDDQYGIRILLNEVFNKEGYQTFQAANGLQALDIVTKERPDLVLLDMKIPGMDGIEILKRMKVI----DENIRVI 76
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2737555188 617 AMTARGEGE--KEAFIKGGFTdSIHKPFSMRELLDMVSS 653
Cdd:cd17553    77 IMTAYGELDmiQESKELGALT-HFAKPFDIDEIRDAVKK 114
PRK11697 PRK11697
two-component system response regulator BtsR;
538-629 1.79e-04

two-component system response regulator BtsR;


Pssm-ID: 236956 [Multi-domain]  Cd Length: 238  Bit Score: 43.68  E-value: 1.79e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188 538 RVLVIDNDTLQLEIAKEMLERNG--VSCTTCSNAKELVNEMRRQDYDLLLSDIQMPETNGFEILALLrkssigNSHTIP- 614
Cdd:PRK11697    3 KVLIVDDEPLAREELRELLQEEGdiEIVGECSNAIEAIGAIHRLKPDVVFLDIQMPRISGLELVGML------DPEHMPy 76
                          90
                  ....*....|....*
gi 2737555188 615 IVAMTARGEGEKEAF 629
Cdd:PRK11697   77 IVFVTAFDEYAIKAF 91
PRK13856 PRK13856
two-component response regulator VirG; Provisional
537-670 2.40e-04

two-component response regulator VirG; Provisional


Pssm-ID: 172377 [Multi-domain]  Cd Length: 241  Bit Score: 43.65  E-value: 2.40e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188 537 QRVLVIDNDTLQLEIAKEMLERNGVSCTTCSNAKELVNEMRRQDYDLLLSDIQMPETNGFEILALLRKSSignshTIPIV 616
Cdd:PRK13856    2 KHVLVIDDDVAMRHLIVEYLTIHAFKVTAVADSQQFNRVLASETVDVVVVDLNLGREDGLEIVRSLATKS-----DVPII 76
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2737555188 617 AMTAR--GEGEKEAFIKGGFTDSIHKPFSMRELLDMVSSVVSRDVEESHTPDFATF 670
Cdd:PRK13856   77 IISGDrlEEADKVVALELGATDFIAKPFGTREFLARIRVALRVRPNVVRTKDRRSF 132
UhpB COG3851
Signal transduction histidine kinase UhpB, glucose-6-phosphate specific [Signal transduction ...
419-519 2.89e-04

Signal transduction histidine kinase UhpB, glucose-6-phosphate specific [Signal transduction mechanisms];


Pssm-ID: 443060 [Multi-domain]  Cd Length: 493  Bit Score: 44.23  E-value: 2.89e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188 419 LLTNAVKFTNAGMIQFNVRYENGMLYIEIKDTGIGMDqdtvsrifrpferlsSEANAEGFGLglpitKGL---VKLLGGS 495
Cdd:COG3851   408 ALTNILKHAEASQIRISLSQDKRLLSLEIRDDGIGLP---------------PELRAKGFGL-----RGMrerVRALGGD 467
                          90       100
                  ....*....|....*....|....*
gi 2737555188 496 IDVESkIGHGSTFRVSLPL-AVSNE 519
Cdd:COG3851   468 FRLSS-APKGTRLSVLLPTpAASNE 491
PRK10529 PRK10529
DNA-binding transcriptional activator KdpE; Provisional
582-678 3.22e-04

DNA-binding transcriptional activator KdpE; Provisional


Pssm-ID: 182522 [Multi-domain]  Cd Length: 225  Bit Score: 42.87  E-value: 3.22e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188 582 DLLLSDIQMPETNGFEILALLRKSSignshTIPIVAMTARG-EGEKEAFIKGGFTDSIHKPFSMRELLDMVsSVVSRDVE 660
Cdd:PRK10529   47 DLIILDLGLPDGDGIEFIRDLRQWS-----AIPVIVLSARSeESDKIAALDAGADDYLSKPFGIGELQARL-RVALRRHS 120
                          90       100
                  ....*....|....*....|..
gi 2737555188 661 ESHTPD----FATFTADVLDKR 678
Cdd:PRK10529  121 ATPAPDplvkFSDVTVDLAARV 142
REC_DC-like cd17534
phosphoacceptor receiver (REC) domain of modulated diguanylate cyclase and similar domains; ...
538-648 3.45e-04

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: 40.85  E-value: 3.45e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188 538 RVLVIDNDTLQLEIAKEMLERNGVSCT-TCSNAKELVNEMRRQDYDLLLSDIQMP-ETNGFEILALLRKssignSHTIPI 615
Cdd:cd17534     2 KILIVEDEAIIALDLKEILESLGYEVVgIADSGEEAIELAEENKPDLILMDINLKgDMDGIEAAREIRE-----KFDIPV 76
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 2737555188 616 VAMTARGEGE-----KE----AFIKggftdsihKPFSMRELL 648
Cdd:cd17534    77 IFLTAYSDEEtleraKEtnpyGYLV--------KPFNERELK 110
REC_CheC-like cd17593
phosphoacceptor receiver (REC) domain of uncharacterized response regulators containing a CheC ...
560-607 3.90e-04

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


Pssm-ID: 381124 [Multi-domain]  Cd Length: 117  Bit Score: 40.60  E-value: 3.90e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 2737555188 560 GVSCTTCSNAKELVNEMRRQDYDLLLSDIQMPETNGFEILALLRKSSI 607
Cdd:cd17593    25 DVEITFAENGEEALEILREGRIDVLFLDLTMPVMDGYEVLEALPVEQL 72
REC_CpdR_CckA-like cd18160
phosphoacceptor receiver (REC) domain of Brucella abortus CpdR and CckA, and similar domains; ...
538-625 3.95e-04

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: 40.56  E-value: 3.95e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188 538 RVLVIDNDTLQLEIAKEMLERNGVSCTTCSNAKELVNEMRRQ-DYDLLLSDIQMPETNGFEILALLRKSsignSHTIPIV 616
Cdd:cd18160     1 TILLADDEPSVRKFIVTTLKKAGYAVTEAESGAEALEKLQQGkDIDIVVTDIVMPEMDGIELAREARKI----DPDVKIL 76

                  ....*....
gi 2737555188 617 AMTARGEGE 625
Cdd:cd18160    77 FISGGAAAA 85
PRK15479 PRK15479
transcriptional regulator TctD;
579-647 4.88e-04

transcriptional regulator TctD;


Pssm-ID: 185376 [Multi-domain]  Cd Length: 221  Bit Score: 42.40  E-value: 4.88e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2737555188 579 QDYDLLLSDIQMPETNGFEILALLRKssigNSHTIPIVAMTARGEGEKEafIKG---GFTDSIHKPFSMREL 647
Cdd:PRK15479   43 EMYALAVLDINMPGMDGLEVLQRLRK----RGQTLPVLLLTARSAVADR--VKGlnvGADDYLPKPFELEEL 108
REC_TPR cd17589
phosphoacceptor receiver (REC) domain of uncharacterized tetratricopeptide repeat (TPR) ...
539-647 5.68e-04

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


Pssm-ID: 381123 [Multi-domain]  Cd Length: 115  Bit Score: 40.32  E-value: 5.68e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188 539 VLVIDNDTLQLEIAKEMLERNGVS-CTTCSNAKELVNEMRRQDYDLLLSDIQMPE-TNGFEILALLRKSSIGNSHTIPIV 616
Cdd:cd17589     1 FLIVDDQPTFRSMLKSMLRSLGVTrIDTASSGEEALRMCENKTYDIVLCDYNLGKgKNGQQLLEELRHKKLISPSTVFIM 80
                          90       100       110
                  ....*....|....*....|....*....|..
gi 2737555188 617 aMTARGEGEK-EAFIKGGFTDSIHKPFSMREL 647
Cdd:cd17589    81 -VTGESSRAMvLSALELEPDDYLLKPFTVSEL 111
REC_CheB-like cd17541
phosphoacceptor receiver (REC) domain of chemotaxis response regulator protein-glutamate ...
538-651 6.37e-04

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: 40.45  E-value: 6.37e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188 538 RVLVIDNDTLQLEIAKEMLERNG---VsCTTCSNAKELVNEMRRQDYDLLLSDIQMPETNGFEILALLRKssignSHTIP 614
Cdd:cd17541     2 RVLIVDDSAVMRKLLSRILESDPdieV-VGTARDGEEALEKIKELKPDVITLDIEMPVMDGLEALRRIMA-----ERPTP 75
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 2737555188 615 IVAMTARGEGEKEAFIK----GGFtDSIHKPF---------SMRELLDMV 651
Cdd:cd17541    76 VVMVSSLTEEGAEITLEalelGAV-DFIAKPSggisldleeIAEELIEKI 124
HisKA pfam00512
His Kinase A (phospho-acceptor) domain; dimerization and phospho-acceptor domain of histidine ...
297-343 6.53e-04

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


Pssm-ID: 459839 [Multi-domain]  Cd Length: 66  Bit Score: 38.73  E-value: 6.53e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 2737555188 297 RKNVILTISHDIRGPLNIIYGYVELAKDTRDRKRRNHHLENIETECK 343
Cdd:pfam00512   2 KSEFLANLSHELRTPLTAIRGYLELLRDEKLDEEQREYLETILRSAE 48
PRK10430 PRK10430
two-component system response regulator DcuR;
539-642 6.75e-04

two-component system response regulator DcuR;


Pssm-ID: 182454 [Multi-domain]  Cd Length: 239  Bit Score: 42.02  E-value: 6.75e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188 539 VLVIDNDTLQLEIAKEMLER-NGVSC----TTCSNAKELVNEmRRQDYDLLLSDIQMPETNGFEILALLRKSSignSHTI 613
Cdd:PRK10430    4 VLIVDDDAMVAELNRRYVAQiPGFQCcgtaSTLEQAKEIIFN-SDTPIDLILLDIYMQQENGLDLLPVLHEAG---CKSD 79
                          90       100
                  ....*....|....*....|....*....
gi 2737555188 614 PIVAMTARGEGEKEAFIKGGFTDSIHKPF 642
Cdd:PRK10430   80 VIVISSAADAATIKDSLHYGVVDYLIKPF 108
REC_OmpR_kpRstA-like cd17622
phosphoacceptor receiver (REC) domain of kpRstA-like OmpR family response regulators; ...
538-648 7.87e-04

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


Pssm-ID: 381137 [Multi-domain]  Cd Length: 116  Bit Score: 39.67  E-value: 7.87e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188 538 RVLVIDNDTLQLEIAKEMLERNGVSCTTCSNAKELVNEMRRQDYDLLLSDIQMPETNGFEILALLRKSSIGnshtiPIVA 617
Cdd:cd17622     2 RILLVEDDPKLARLIADFLESHGFNVVVEHRGDRALEVIAREKPDAVLLDIMLPGIDGLTLCRDLRPKYQG-----PILL 76
                          90       100       110
                  ....*....|....*....|....*....|....
gi 2737555188 618 MTARGEGEKEafIKG---GFTDSIHKPFSMRELL 648
Cdd:cd17622    77 LTALDSDIDH--ILGlelGADDYVVKPVEPAVLL 108
PRK10710 PRK10710
DNA-binding transcriptional regulator BaeR; Provisional
567-657 7.92e-04

DNA-binding transcriptional regulator BaeR; Provisional


Pssm-ID: 182665 [Multi-domain]  Cd Length: 240  Bit Score: 41.98  E-value: 7.92e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188 567 SNAKELVNEMRRQDYDLLLSDIQMPETNGFEILALLRKSSignshTIPIVAMTARGEG-EKEAFIKGGFTDSIHKPFSMR 645
Cdd:PRK10710   41 SHGDEVLPYVRQTPPDLILLDLMLPGTDGLTLCREIRRFS-----DIPIVMVTAKIEEiDRLLGLEIGADDYICKPYSPR 115
                          90
                  ....*....|..
gi 2737555188 646 ELLDMVSSVVSR 657
Cdd:PRK10710  116 EVVARVKTILRR 127
REC_OmpR_KdpE-like cd17620
phosphoacceptor receiver (REC) domain of KdpE-like OmpR family response regulators; KdpE is a ...
539-641 1.27e-03

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


Pssm-ID: 381135 [Multi-domain]  Cd Length: 99  Bit Score: 38.68  E-value: 1.27e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188 539 VLVIDNDTLQLEIAKEMLERNGVSCTTCSNAKELVNEMRRQDYDLLLSDIQMPETNGFEILALLRKSSignshTIPIVAM 618
Cdd:cd17620     1 ILVIEDEPQIRRFLRTALEAHGYRVFEAETGQEGLLEAATRKPDLIILDLGLPDMDGLEVIRRLREWS-----AVPVIVL 75
                          90       100
                  ....*....|....*....|....
gi 2737555188 619 TARG-EGEKEAFIKGGFTDSIHKP 641
Cdd:cd17620    76 SARDeESDKIAALDAGADDYLTKP 99
PRK10336 PRK10336
two-component system response regulator QseB;
538-657 2.20e-03

two-component system response regulator QseB;


Pssm-ID: 182387 [Multi-domain]  Cd Length: 219  Bit Score: 40.26  E-value: 2.20e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188 538 RVLVIDNDTLQLEIAKEMLERNGVSCTTCSNAKELVNEMRRQDYDLLLSDIQMPETNGFEILALLRKSsiGNSHtiPIVA 617
Cdd:PRK10336    2 RILLIEDDMLIGDGIKTGLSKMGFSVDWFTQGRQGKEALYSAPYDAVILDLTLPGMDGRDILREWREK--GQRE--PVLI 77
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 2737555188 618 MTARGE-GEKEAFIKGGFTDSIHKPFSMRELLDMVSSVVSR 657
Cdd:PRK10336   78 LTARDAlAERVEGLRLGADDYLCKPFALIEVAARLEALMRR 118
HATPase_YehU-like cd16956
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
419-513 2.42e-03

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


Pssm-ID: 340432 [Multi-domain]  Cd Length: 101  Bit Score: 38.19  E-value: 2.42e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188 419 LLTNAVKFTNAGM-----IQFNVRYENGMLYIEIKDTGIGMDQDTVSRIFRPferlsseaNAEGFGLGLpITKGLVKLLG 493
Cdd:cd16956     9 IVENAVKHGLSGLldggrVEITARLDGQHLLLEVEDNGGGMDPDTLARILIR--------SSNGLGLNL-VDKRLRQAFG 79
                          90       100
                  ....*....|....*....|..
gi 2737555188 494 GS--IDVESKIGHGSTFRVSLP 513
Cdd:cd16956    80 NDygLDIECAPGEGTRITIRLP 101
REC_HupR cd17596
phosphoacceptor receiver (REC) domain of hydrogen uptake protein regulator (HupR); Members of ...
537-605 2.88e-03

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


Pssm-ID: 381127 [Multi-domain]  Cd Length: 133  Bit Score: 38.50  E-value: 2.88e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2737555188 537 QRVLVIDNDTLQLEIAKEMLERNgVSCTTCSNAKELVNEMRRQDYDLLLSDIQMPETNGFEILALLRKS 605
Cdd:cd17596     1 PTILVVDDEVRSLEALRRTLEED-FDVLTAASAEEALAILEEEWVQVILCDQRMPGTTGVEFLKEVRER 68
glnL PRK11073
nitrogen regulation protein NR(II);
408-514 3.45e-03

nitrogen regulation protein NR(II);


Pssm-ID: 182947 [Multi-domain]  Cd Length: 348  Bit Score: 40.45  E-value: 3.45e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188 408 DMDRISQIIDNLLTNAVKF--TNAGMIQFNVRYE-----NGMLY-----IEIKDTGIGMD---QDTvsrIFRPFerlsSE 472
Cdd:PRK11073  234 DPDQIEQVLLNIVRNALQAlgPEGGTITLRTRTAfqltlHGERYrlaarIDIEDNGPGIPphlQDT---LFYPM----VS 306
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 2737555188 473 ANAEGFGLGLPITKGLVKLLGGSIDVESKIGHgSTFRVSLPL 514
Cdd:PRK11073  307 GREGGTGLGLSIARNLIDQHSGKIEFTSWPGH-TEFSVYLPI 347
HisKA cd00082
Histidine Kinase A (dimerization/phosphoacceptor) domain; Histidine Kinase A dimers are formed ...
294-343 3.89e-03

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: 36.42  E-value: 3.89e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2737555188 294 LETRKNVILTISHDIRGPLNIIYGYVELAKDTRDRK-RRNHHLENIETECK 343
Cdd:cd00082     1 LQAKGEFLANVSHELRTPLTAIRGALELLEEELLDDeEQREYLERIREEAE 51
HATPase_Phy-like cd16932
Histidine kinase-like ATPase domain of plant phytochromes similar to Arabidopsis thaliana ...
407-494 8.79e-03

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


Pssm-ID: 340409 [Multi-domain]  Cd Length: 113  Bit Score: 36.87  E-value: 8.79e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2737555188 407 GDMDRISQIIDNLLTNAVKFTNA--GMIQFNV-----RYENGMLYIE----IKDTGIGMDQDTVSRIFRPFERLSSEana 475
Cdd:cd16932     2 GDQIRLQQVLADFLLNAVRFTPSpgGWVEIKVsptkkQIGDGVHVIHlefrITHPGQGLPEELVQEMFEENQWTTQE--- 78
                          90
                  ....*....|....*....
gi 2737555188 476 egfGLGLPITKGLVKLLGG 494
Cdd:cd16932    79 ---GLGLSISRKLVKLMNG 94
 
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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