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Conserved domains on  [gi|1027852989|ref|NP_001311596|]
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protein EIN4-like precursor [Nicotiana tabacum]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
REC_ETR-like cd19933
phosphoacceptor receiver (REC) domain of plant ethylene receptors ETR1, ETR2, and EIN4, and ...
 634-749 8.57e-50

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: 170.27  E-value: 8.57e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027852989 634 LQVLLADDDDVNRMVTKKLLEKLGCQVIAVSTGFQCLSAMGHSKTSIQVVILDLHMPEMDGFEVAIRVRK-FHSHGWPLI 712
Cdd:cd19933     1 LKVLLVDDNAVNRMVTKGLLEKLGCEVTTVSSGEECLNLLASAEHSFQLVLLDLCMPEMDGFEVALRIRKlFGRRERPLI 80

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1027852989 713 IALSATSEELVWDRCLQVGINGLIRKPVLLQGMAEEL 749
Cdd:cd19933    81 VALTANTDDSTREKCLSLGMNGVITKPVSLHALGDEL 117
HATPase_ETR2_ERS2-EIN4-like cd16938
Histidine kinase-like ATPase domain of Arabidopsis thaliana ETR2, ERS2, and EIN4, and related ...
 474-603 2.17e-35

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: 130.66  E-value: 2.17e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027852989 474 LPNLVMGDEMRTFQVLLHMVGHLLNISFGSGSVVFRV----GTEDGNDKIWGARRHSIVDEYVTIKFETKINLESSQRNS 549
Cdd:cd16938     1 LPDVVVGDERRVFQVLLHMLGNLLKMRNGGGNITFRVflegGSEDRSDRDWGPWRPSMSDESVEIRFEVEINDSGSPSIE 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1027852989 550 SMSSIHFGGRRYNSKELKEGLSFRMCKKLVQMMQGNVYMSSNSeGRAQGMTLIL 603
Cdd:cd16938    81 SASMRNSLNRRYNLSELGEHLSFSICKQLVQLMGGNIWIVPGS-GLGTTMSLLL 133
BaeS COG0642
Signal transduction histidine kinase [Signal transduction mechanisms];
299-605 1.13e-12

Signal transduction histidine kinase [Signal transduction mechanisms];


:

Pssm-ID: 440407 [Multi-domain]  Cd Length: 328  Bit Score: 69.94  E-value: 1.13e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027852989 299 AILVLVLPSGDFDWSSNEMEIVEVVADQVAVALSHATVLEESQLMREKLEIRNGLLQQAKENAVKATQARNSFQKVMNNG 378
Cdd:COG0642    41 LLLLLLLLLLLLLLALALLALLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLALLLLLEEANEAKSRFLANVSHE 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027852989 379 MRQPMHSVLGLLSILQDEnfTSSNQRIIIDTMMRTSTVLSTLTNDAMDISEKDEGRIPVEMMPFQLHSLIREASCLVKCL 458
Cdd:COG0642   121 LRTPLTAIRGYLELLLEE--LDEEQREYLETILRSADRLLRLINDLLDLSRLEAGKLELEPEPVDLAELLEEVVELFRPL 198

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027852989 459 CIYKGFGFSTDFPNSLPnLVMGDEMRTFQVLLHMVGhllN-ISFGS--GSVVFRVGTEDGNDKIW----G-----ARRHS 526
Cdd:COG0642   199 AEEKGIELELDLPDDLP-TVRGDPDRLRQVLLNLLS---NaIKYTPegGTVTVSVRREGDRVRISvedtGpgippEDLER 274

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1027852989 527 IVDEYVTIKfetkinlessqrnssmssihfGGRRYNSKELkeGLSfrMCKKLVQMMQGNVYMSSNSEgraQGMTLILRF 605
Cdd:COG0642   275 IFEPFFRTD---------------------PSRRGGGTGL--GLA--IVKRIVELHGGTIEVESEPG---KGTTFTVTL 325
GAF pfam01590
GAF domain; This domain is present in cGMP-specific phosphodiesterases, adenylyl and guanylyl ...
 183-331 7.39e-10

GAF domain; This domain is present in cGMP-specific phosphodiesterases, adenylyl and guanylyl cyclases, phytochromes, FhlA and NifA. Adenylyl and guanylyl cyclases catalyze ATP and GTP to the second messengers cAMP and cGMP, respectively, these products up-regulating catalytic activity by binding to the regulatory GAF domain(s). The opposite hydrolysis reaction is catalyzed by phosphodiesterase. cGMP-dependent 3',5'-cyclic phosphodiesterase catalyzes the conversion of guanosine 3',5'-cyclic phosphate to guanosine 5'-phosphate. Here too, cGMP regulates catalytic activity by GAF-domain binding. Phytochromes are regulatory photoreceptors in plants and bacteria which exist in two thermally-stable states that are reversibly inter-convertible by light: the Pr state absorbs maximally in the red region of the spectrum, while the Pfr state absorbs maximally in the far-red region. This domain is also found in FhlA (formate hydrogen lyase transcriptional activator) and NifA, a transcriptional activator which is required for activation of most Nif operons which are directly involved in nitrogen fixation. NifA interacts with sigma-54. This domain can bind biliverdine and phycocyanobilin (Matilla et al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).


:

Pssm-ID: 460259 [Multi-domain]  Cd Length: 133  Bit Score: 57.49  E-value: 7.39e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027852989 183 DKHNILYTTLVELSKTLNLHNCAVWMPNENRsvmnlTHGLSPGSAVEYHRSLPIDDPDvleitkdkGVRILRQDSVLAAA 262
Cdd:pfam01590   1 DLEEILQTILEELRELLGADRCALYLPDADG-----LEYLPPGARWLKAAGLEIPPGT--------GVTVLRTGRPLVVP 67

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1027852989 263 SSggPGEPCTVAaiRMPLLRASDFKG--GTPVLVDTR-YAILVLVLPSGDfdWSSNEMEIVEVVADQVAVAL 331
Cdd:pfam01590  68 DA--AGDPRFLD--PLLLLRNFGIRSllAVPIIDDGElLGVLVLHHPRPP--FTEEELELLEVLADQVAIAL 133
 
Name Accession Description Interval E-value
REC_ETR-like cd19933
phosphoacceptor receiver (REC) domain of plant ethylene receptors ETR1, ETR2, and EIN4, and ...
 634-749 8.57e-50

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: 170.27  E-value: 8.57e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027852989 634 LQVLLADDDDVNRMVTKKLLEKLGCQVIAVSTGFQCLSAMGHSKTSIQVVILDLHMPEMDGFEVAIRVRK-FHSHGWPLI 712
Cdd:cd19933     1 LKVLLVDDNAVNRMVTKGLLEKLGCEVTTVSSGEECLNLLASAEHSFQLVLLDLCMPEMDGFEVALRIRKlFGRRERPLI 80

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1027852989 713 IALSATSEELVWDRCLQVGINGLIRKPVLLQGMAEEL 749
Cdd:cd19933    81 VALTANTDDSTREKCLSLGMNGVITKPVSLHALGDEL 117
HATPase_ETR2_ERS2-EIN4-like cd16938
Histidine kinase-like ATPase domain of Arabidopsis thaliana ETR2, ERS2, and EIN4, and related ...
 474-603 2.17e-35

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: 130.66  E-value: 2.17e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027852989 474 LPNLVMGDEMRTFQVLLHMVGHLLNISFGSGSVVFRV----GTEDGNDKIWGARRHSIVDEYVTIKFETKINLESSQRNS 549
Cdd:cd16938     1 LPDVVVGDERRVFQVLLHMLGNLLKMRNGGGNITFRVflegGSEDRSDRDWGPWRPSMSDESVEIRFEVEINDSGSPSIE 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1027852989 550 SMSSIHFGGRRYNSKELKEGLSFRMCKKLVQMMQGNVYMSSNSeGRAQGMTLIL 603
Cdd:cd16938    81 SASMRNSLNRRYNLSELGEHLSFSICKQLVQLMGGNIWIVPGS-GLGTTMSLLL 133
CheY COG0784
CheY-like REC (receiver) domain, includes chemotaxis protein CheY and sporulation regulator ...
 632-756 1.20e-31

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: 119.57  E-value: 1.20e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027852989 632 KGLQVLLADDDDVNRMVTKKLLEKLGCQVIAVSTGFQCLSAMghSKTSIQVVILDLHMPEMDGFEVAIRVRKFHSHGWPL 711
Cdd:COG0784     4 GGKRILVVDDNPDNRELLRRLLERLGYEVTTAEDGAEALELL--RAGPPDLILLDINMPGMDGLELLRRIRALPRLPDIP 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1027852989 712 IIALSATSEELVWDRCLQVGINGLIRKPVLLQGMAEELQRVLQRA 756
Cdd:COG0784    82 IIALTAYADEEDRERALEAGADDYLTKPVDPEELLEALRRLLARA 126
PRK09959 PRK09959
acid-sensing system histidine kinase EvgS;
354-756 1.52e-18

acid-sensing system histidine kinase EvgS;


Pssm-ID: 182169 [Multi-domain]  Cd Length: 1197  Bit Score: 90.95  E-value: 1.52e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027852989  354 LQQAKENAVKATQARNSFQKVMNNGMRQPMHSVLGLLSILQDENFTSSNQRIIIDTMMRTSTVLSTLTNDAMDISEKDEG 433
Cdd:PRK09959   698 LEVERNKAINATVAKSQFLATMSHEIRTPISSIMGFLELLSGSGLSKEQRVEAISLAYATGQSLLGLIGEILDVDKIESG 777

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027852989  434 RIPVEMMPFQLHSLIREASCLVKCLCIYKGFGFS--TDFPNSLpnLVMGDEMRTFQVLLHMVGHLLNIsfgsgsvvfrvg 511
Cdd:PRK09959   778 NYQLQPQWVDIPTLVQNTCHSFGAIAASKSIALScsSTFPDHY--LVKIDPQAFKQVLSNLLSNALKF------------ 843

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027852989  512 TEDGNDKIWGARRHsIVDEYVTIKFE-----TKINLESSQRNSSMSSIHFGGRrynsKELKEGLSFRMCKKLVQMMQGNV 586
Cdd:PRK09959   844 TTEGAVKITTSLGH-IDDNHAVIKMTimdsgSGLSQEEQQQLFKRYSQTSAGR----QQTGSGLGLMICKELIKNMQGDL 918

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027852989  587 YMSSNSE-GRAQGMTLILRFLKQSSfrkhmfDLGNPLEQAISssMFKGLQVLLADDDDVNRMVTKKLLEKLGCQVIAVST 665
Cdd:PRK09959   919 SLESHPGiGTTFTITIPVEISQQVA------TVEAKAEQPIT--LPEKLSILIADDHPTNRLLLKRQLNLLGYDVDEATD 990

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027852989  666 GFQCLSAMghSKTSIQVVILDLHMPEMDGFEVAIRVRKFHShGWPlIIALSATSEELVWDRCLQVGINGLIRKPVLLQGM 745
Cdd:PRK09959   991 GVQALHKV--SMQHYDLLITDVNMPNMDGFELTRKLREQNS-SLP-IWGLTANAQANEREKGLSCGMNLCLFKPLTLDVL 1066

                          410
                   ....*....|.
gi 1027852989  746 AEELQRVLQRA 756
Cdd:PRK09959  1067 KTHLSQLHQVA 1077
Response_reg pfam00072
Response regulator receiver domain; This domain receives the signal from the sensor partner in ...
 636-740 1.36e-17

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: 79.12  E-value: 1.36e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027852989 636 VLLADDDDVNRMVTKKLLEKLGCQVIAVSTGFQCLSAMGHSKtsIQVVILDLHMPEMDGFEVAIRVRKFHSHgwPLIIAL 715
Cdd:pfam00072   1 VLIVDDDPLIRELLRQLLEKEGYVVAEADDGKEALELLKEER--PDLILLDINMPGMDGLELLKRIRRRDPT--TPVIIL 76

                          90       100
                  ....*....|....*....|....*
gi 1027852989 716 SATSEELVWDRCLQVGINGLIRKPV 740
Cdd:pfam00072  77 TAHGDEDDAVEALEAGADDFLSKPF 101
BaeS COG0642
Signal transduction histidine kinase [Signal transduction mechanisms];
299-605 1.13e-12

Signal transduction histidine kinase [Signal transduction mechanisms];


Pssm-ID: 440407 [Multi-domain]  Cd Length: 328  Bit Score: 69.94  E-value: 1.13e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027852989 299 AILVLVLPSGDFDWSSNEMEIVEVVADQVAVALSHATVLEESQLMREKLEIRNGLLQQAKENAVKATQARNSFQKVMNNG 378
Cdd:COG0642    41 LLLLLLLLLLLLLLALALLALLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLALLLLLEEANEAKSRFLANVSHE 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027852989 379 MRQPMHSVLGLLSILQDEnfTSSNQRIIIDTMMRTSTVLSTLTNDAMDISEKDEGRIPVEMMPFQLHSLIREASCLVKCL 458
Cdd:COG0642   121 LRTPLTAIRGYLELLLEE--LDEEQREYLETILRSADRLLRLINDLLDLSRLEAGKLELEPEPVDLAELLEEVVELFRPL 198

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027852989 459 CIYKGFGFSTDFPNSLPnLVMGDEMRTFQVLLHMVGhllN-ISFGS--GSVVFRVGTEDGNDKIW----G-----ARRHS 526
Cdd:COG0642   199 AEEKGIELELDLPDDLP-TVRGDPDRLRQVLLNLLS---NaIKYTPegGTVTVSVRREGDRVRISvedtGpgippEDLER 274

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1027852989 527 IVDEYVTIKfetkinlessqrnssmssihfGGRRYNSKELkeGLSfrMCKKLVQMMQGNVYMSSNSEgraQGMTLILRF 605
Cdd:COG0642   275 IFEPFFRTD---------------------PSRRGGGTGL--GLA--IVKRIVELHGGTIEVESEPG---KGTTFTVTL 325
PRK15347 PRK15347
two component system sensor kinase;
354-749 2.29e-12

two component system sensor kinase;


Pssm-ID: 237951 [Multi-domain]  Cd Length: 921  Bit Score: 70.83  E-value: 2.29e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027852989 354 LQQAKENAVKATQARNSFQKVMNNGMRQPMHSVLGLLSILQDENFTSSnQRIIIDTMMRTSTVLSTLTNDAMDISEKDEG 433
Cdd:PRK15347  384 LAEAKQRAEQANKRKSEHLTTISHEIRTPLNGVLGALELLQNTPLTAE-QMDLADTARQCTLSLLAIINNLLDFSRIESG 462

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027852989 434 RIPVEMMPFQLHSLIREASCLVKCLCIYKGFGFSTDFPNSLPNLVMGDEMRTFQVLLHMVGHllnisfgsgSVVFrvgTE 513
Cdd:PRK15347  463 QMTLSLEETALLPLLDQAMLTIQGPAQSKSLTLRTFVGAHVPLYLHLDSLRLRQILVNLLGN---------AVKF---TE 530

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027852989 514 DGNDKIWGARRH-----SIVD--EYVTIKFETKInlessQRNSSMSSIHFGGrrynskelkEGLSFRMCKKLVQMMQGNV 586
Cdd:PRK15347  531 TGGIRLRVKRHEqqlcfTVEDtgCGIDIQQQQQI-----FTPFYQADTHSQG---------TGLGLTIASSLAKMMGGEL 596

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027852989 587 YMSSNS-EG--------------------------------RAQGMTLI------------LRFLKQSSFR---KHMFDL 618
Cdd:PRK15347  597 TLFSTPgVGscfslvlplneyappeplkgelsaplalhrqlSAWGITCQpghqnpalldpeLAYLPGRLYDllqQIIQGA 676

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027852989 619 GNPLEQAISSSMFKgLQVLLADDDDVNRMVTKKLLEKLGCQVIAVSTGFQCLsAMGHSKTsIQVVILDLHMPEMDGFEVA 698
Cdd:PRK15347  677 PNEPVINLPLQPWQ-LQILLVDDVETNRDIIGMMLVELGQQVTTAASGTEAL-ELGRQHR-FDLVLMDIRMPGLDGLETT 753

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1027852989 699 IRVRkfHS----HGWPLIIALSAT--SEELvwDRCLQVGINGLIRKPVLLQGMAEEL 749
Cdd:PRK15347  754 QLWR--DDpnnlDPDCMIVALTANaaPEEI--HRCKKAGMNHYLTKPVTLAQLARAL 806
GAF pfam01590
GAF domain; This domain is present in cGMP-specific phosphodiesterases, adenylyl and guanylyl ...
 183-331 7.39e-10

GAF domain; This domain is present in cGMP-specific phosphodiesterases, adenylyl and guanylyl cyclases, phytochromes, FhlA and NifA. Adenylyl and guanylyl cyclases catalyze ATP and GTP to the second messengers cAMP and cGMP, respectively, these products up-regulating catalytic activity by binding to the regulatory GAF domain(s). The opposite hydrolysis reaction is catalyzed by phosphodiesterase. cGMP-dependent 3',5'-cyclic phosphodiesterase catalyzes the conversion of guanosine 3',5'-cyclic phosphate to guanosine 5'-phosphate. Here too, cGMP regulates catalytic activity by GAF-domain binding. Phytochromes are regulatory photoreceptors in plants and bacteria which exist in two thermally-stable states that are reversibly inter-convertible by light: the Pr state absorbs maximally in the red region of the spectrum, while the Pfr state absorbs maximally in the far-red region. This domain is also found in FhlA (formate hydrogen lyase transcriptional activator) and NifA, a transcriptional activator which is required for activation of most Nif operons which are directly involved in nitrogen fixation. NifA interacts with sigma-54. This domain can bind biliverdine and phycocyanobilin (Matilla et al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).


Pssm-ID: 460259 [Multi-domain]  Cd Length: 133  Bit Score: 57.49  E-value: 7.39e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027852989 183 DKHNILYTTLVELSKTLNLHNCAVWMPNENRsvmnlTHGLSPGSAVEYHRSLPIDDPDvleitkdkGVRILRQDSVLAAA 262
Cdd:pfam01590   1 DLEEILQTILEELRELLGADRCALYLPDADG-----LEYLPPGARWLKAAGLEIPPGT--------GVTVLRTGRPLVVP 67

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1027852989 263 SSggPGEPCTVAaiRMPLLRASDFKG--GTPVLVDTR-YAILVLVLPSGDfdWSSNEMEIVEVVADQVAVAL 331
Cdd:pfam01590  68 DA--AGDPRFLD--PLLLLRNFGIRSllAVPIIDDGElLGVLVLHHPRPP--FTEEELELLEVLADQVAIAL 133
REC smart00448
cheY-homologous receiver domain; CheY regulates the clockwise rotation of E. coli flagellar ...
 636-690 8.96e-08

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


Pssm-ID: 214668 [Multi-domain]  Cd Length: 55  Bit Score: 49.10  E-value: 8.96e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1027852989  636 VLLADDDDVNRMVTKKLLEKLGCQVIAVSTGFQCLSAMghSKTSIQVVILDLHMP 690
Cdd:smart00448   3 ILVVDDDPLLRELLKALLEKEGYEVDEATDGEEALELL--KEEKPDLILLDIMMP 55
GAF COG2203
GAF domain [Signal transduction mechanisms];
174-398 3.34e-07

GAF domain [Signal transduction mechanisms];


Pssm-ID: 441805 [Multi-domain]  Cd Length: 712  Bit Score: 54.04  E-value: 3.34e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027852989 174 LTREIRKSIDKHNILYTTLVELSKTLNLHNCAVWMPNENRSVMNLTHglSPGSAVEYHRSLPIDDPDVLE-ITKDKGVRI 252
Cdd:COG2203   198 ISQALRSALDLEELLQRILELAGELLGADRGAILLVDEDGGELELVA--APGLPEEELGRLPLGEGLAGRaLRTGEPVVV 275

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027852989 253 --LRQDSVLAAASSGGPGEPCTVAAIRMPLLRAsdfkggtpvlvDTRYAILVLVLPSGDfDWSSNEMEIVEVVADQVAVA 330
Cdd:COG2203   276 ndASTDPRFAPSLRELLLALGIRSLLCVPLLVD-----------GRLIGVLALYSKEPR-AFTEEDLELLEALADQAAIA 343

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1027852989 331 LSHATVLEESQLMREKLEIRNGLLQQAKENAVKATQARNSFQKVMNNGMRQPMHSVLGLLSILQDENF 398
Cdd:COG2203   344 IERARLYEALEAALAALLQELALLRLLLDLELTLLRLRQLLLELLLALLLLLSLLGAELLLLLLDAAD 411
GAF smart00065
Domain present in phytochromes and cGMP-specific phosphodiesterases; Mutations within these ...
 185-341 4.47e-06

Domain present in phytochromes and cGMP-specific phosphodiesterases; Mutations within these domains in PDE6B result in autosomal recessive inheritance of retinitis pigmentosa.


Pssm-ID: 214500 [Multi-domain]  Cd Length: 149  Bit Score: 46.99  E-value: 4.47e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027852989  185 HNILYTTLVELSKTLNLHNCAVWMPNENRS---VMNLTHGLSPGSaveYHRSLPIDDPDVLEITKDKGVRILR--QDSVL 259
Cdd:smart00065   3 EELLQTILEELRQLLGADRVLIYLVDENDRgelVLVAADGLTLPT---LGIRFPLDEGLAGRVAETGRPLNIPdvEADPL 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027852989  260 AAASSGGPgEPCTVAAIRMPLLRasdfkGGTPVlvdtryAILVLVLPSGDFDWSSNEMEIVEVVADQVAVALSHATVLEE 339
Cdd:smart00065  80 FAEDLLGR-YQGVRSFLAVPLVA-----DGELV------GVLALHNKKSPRPFTEEDEELLQALANQLAIALANAQLYEE 147


                   ..
gi 1027852989  340 SQ 341
Cdd:smart00065 148 LR 149
HisKA pfam00512
His Kinase A (phospho-acceptor) domain; dimerization and phospho-acceptor domain of histidine ...
 367-433 1.04e-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: 41.04  E-value: 1.04e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1027852989 367 ARNSFQKVMNNGMRQPMHSVLGLLSILQDENfTSSNQRIIIDTMMRTSTVLSTLTNDAMDISEKDEG 433
Cdd:pfam00512   1 AKSEFLANLSHELRTPLTAIRGYLELLRDEK-LDEEQREYLETILRSAERLLRLINDLLDLSRIEAG 66
 
Name Accession Description Interval E-value
REC_ETR-like cd19933
phosphoacceptor receiver (REC) domain of plant ethylene receptors ETR1, ETR2, and EIN4, and ...
 634-749 8.57e-50

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: 170.27  E-value: 8.57e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027852989 634 LQVLLADDDDVNRMVTKKLLEKLGCQVIAVSTGFQCLSAMGHSKTSIQVVILDLHMPEMDGFEVAIRVRK-FHSHGWPLI 712
Cdd:cd19933     1 LKVLLVDDNAVNRMVTKGLLEKLGCEVTTVSSGEECLNLLASAEHSFQLVLLDLCMPEMDGFEVALRIRKlFGRRERPLI 80

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1027852989 713 IALSATSEELVWDRCLQVGINGLIRKPVLLQGMAEEL 749
Cdd:cd19933    81 VALTANTDDSTREKCLSLGMNGVITKPVSLHALGDEL 117
HATPase_ETR2_ERS2-EIN4-like cd16938
Histidine kinase-like ATPase domain of Arabidopsis thaliana ETR2, ERS2, and EIN4, and related ...
 474-603 2.17e-35

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: 130.66  E-value: 2.17e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027852989 474 LPNLVMGDEMRTFQVLLHMVGHLLNISFGSGSVVFRV----GTEDGNDKIWGARRHSIVDEYVTIKFETKINLESSQRNS 549
Cdd:cd16938     1 LPDVVVGDERRVFQVLLHMLGNLLKMRNGGGNITFRVflegGSEDRSDRDWGPWRPSMSDESVEIRFEVEINDSGSPSIE 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1027852989 550 SMSSIHFGGRRYNSKELKEGLSFRMCKKLVQMMQGNVYMSSNSeGRAQGMTLIL 603
Cdd:cd16938    81 SASMRNSLNRRYNLSELGEHLSFSICKQLVQLMGGNIWIVPGS-GLGTTMSLLL 133
CheY COG0784
CheY-like REC (receiver) domain, includes chemotaxis protein CheY and sporulation regulator ...
 632-756 1.20e-31

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: 119.57  E-value: 1.20e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027852989 632 KGLQVLLADDDDVNRMVTKKLLEKLGCQVIAVSTGFQCLSAMghSKTSIQVVILDLHMPEMDGFEVAIRVRKFHSHGWPL 711
Cdd:COG0784     4 GGKRILVVDDNPDNRELLRRLLERLGYEVTTAEDGAEALELL--RAGPPDLILLDINMPGMDGLELLRRIRALPRLPDIP 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1027852989 712 IIALSATSEELVWDRCLQVGINGLIRKPVLLQGMAEELQRVLQRA 756
Cdd:COG0784    82 IIALTAYADEEDRERALEAGADDYLTKPVDPEELLEALRRLLARA 126
REC_hyHK_CKI1_RcsC-like cd17546
phosphoacceptor receiver (REC) domain of hybrid sensor histidine kinases/response regulators ...
 636-753 2.35e-31

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: 118.34  E-value: 2.35e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027852989 636 VLLADDDDVNRMVTKKLLEKLGCQVIAVSTGFQCLSAMghSKTSIQVVILDLHMPEMDGFEVAIRVRKFHSHGWPL-IIA 714
Cdd:cd17546     1 VLVVDDNPVNRKVLKKLLEKLGYEVDVAENGQEALELL--KEEPFDLVLMDLQMPVMDGLEATRRIRELEGGGRRTpIIA 78

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1027852989 715 LSATSEELVWDRCLQVGINGLIRKPVLLqgmaEELQRVL 753
Cdd:cd17546    79 LTANALEEDREKCLEAGMDDYLSKPVKL----DQLKEVL 113
PleD COG3706
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate ...
 636-740 2.36e-24

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: 100.75  E-value: 2.36e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027852989 636 VLLADDDDVNRMVTKKLLEKLGCQVIAVSTGFQCLSAMghSKTSIQVVILDLHMPEMDGFEVAIRVRKFHSHGWPLIIAL 715
Cdd:COG3706     4 ILVVDDDPTNRKLLRRLLEAAGYEVVEAADGEEALELL--QEHRPDLILLDLEMPDMDGLELCRRLRADPRTADIPIIFL 81

                          90       100
                  ....*....|....*....|....*
gi 1027852989 716 SATSEELVWDRCLQVGINGLIRKPV 740
Cdd:COG3706    82 TALDDEEDRARALEAGADDYLTKPF 106
REC cd00156
phosphoacceptor receiver (REC) domain of response regulators (RRs) and pseudo response ...
 637-739 2.56e-22

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: 91.91  E-value: 2.56e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027852989 637 LLADDDDVNRMVTKKLLEKLGCQVIAVSTGFQCLSAMghSKTSIQVVILDLHMPEMDGFEVAIRVRKFHSHgwPLIIALS 716
Cdd:cd00156     1 LIVDDDPAIRELLKSLLEREGYEVDTAADGEEALELL--REERPDLVLLDLMMPGMDGLELLRKLRELPPD--IPVIVLT 76

                          90       100
                  ....*....|....*....|...
gi 1027852989 717 ATSEELVWDRCLQVGINGLIRKP 739
Cdd:cd00156    77 AKADEEDAVRALELGADDYLVKP 99
RpfG COG3437
Response regulator c-di-GMP phosphodiesterase, RpfG family, contains REC and HD-GYP domains ...
 636-758 2.17e-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: 93.31  E-value: 2.17e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027852989 636 VLLADDDDVNRMVTKKLLEKLGCQVIAVSTGFQCLSAMghSKTSIQVVILDLHMPEMDGFEVAIRVRKFHSHGWPLIIAL 715
Cdd:COG3437     9 VLIVDDDPENLELLRQLLRTLGYDVVTAESGEEALELL--LEAPPDLILLDVRMPGMDGFELLRLLRADPSTRDIPVIFL 86

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1027852989 716 SATSEELVWDRCLQVGINGLIRKPVllqgMAEELQRVLQRAGE 758
Cdd:COG3437    87 TALADPEDRERALEAGADDYLTKPF----DPEELLARVRNALE 125
OmpR COG0745
DNA-binding response regulator, OmpR family, contains REC and winged-helix (wHTH) domain ...
 634-757 4.54e-21

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


Pssm-ID: 440508 [Multi-domain]  Cd Length: 204  Bit Score: 91.94  E-value: 4.54e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027852989 634 LQVLLADDDDVNRMVTKKLLEKLGCQVIAVSTGFQCLSAMghSKTSIQVVILDLHMPEMDGFEVAIRVRKFHSHGwPlII 713
Cdd:COG0745     2 PRILVVEDDPDIRELLADALEREGYEVDTAADGEEALELL--EEERPDLILLDLMLPGMDGLEVCRRLRARPSDI-P-II 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1027852989 714 ALSATSEELVWDRCLQVGINGLIRKPVLLQGMAEELQRVLQRAG 757
Cdd:COG0745    78 MLTARDDEEDRVRGLEAGADDYLTKPFDPEELLARIRALLRRRA 121
PRK09959 PRK09959
acid-sensing system histidine kinase EvgS;
354-756 1.52e-18

acid-sensing system histidine kinase EvgS;


Pssm-ID: 182169 [Multi-domain]  Cd Length: 1197  Bit Score: 90.95  E-value: 1.52e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027852989  354 LQQAKENAVKATQARNSFQKVMNNGMRQPMHSVLGLLSILQDENFTSSNQRIIIDTMMRTSTVLSTLTNDAMDISEKDEG 433
Cdd:PRK09959   698 LEVERNKAINATVAKSQFLATMSHEIRTPISSIMGFLELLSGSGLSKEQRVEAISLAYATGQSLLGLIGEILDVDKIESG 777

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027852989  434 RIPVEMMPFQLHSLIREASCLVKCLCIYKGFGFS--TDFPNSLpnLVMGDEMRTFQVLLHMVGHLLNIsfgsgsvvfrvg 511
Cdd:PRK09959   778 NYQLQPQWVDIPTLVQNTCHSFGAIAASKSIALScsSTFPDHY--LVKIDPQAFKQVLSNLLSNALKF------------ 843

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027852989  512 TEDGNDKIWGARRHsIVDEYVTIKFE-----TKINLESSQRNSSMSSIHFGGRrynsKELKEGLSFRMCKKLVQMMQGNV 586
Cdd:PRK09959   844 TTEGAVKITTSLGH-IDDNHAVIKMTimdsgSGLSQEEQQQLFKRYSQTSAGR----QQTGSGLGLMICKELIKNMQGDL 918

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027852989  587 YMSSNSE-GRAQGMTLILRFLKQSSfrkhmfDLGNPLEQAISssMFKGLQVLLADDDDVNRMVTKKLLEKLGCQVIAVST 665
Cdd:PRK09959   919 SLESHPGiGTTFTITIPVEISQQVA------TVEAKAEQPIT--LPEKLSILIADDHPTNRLLLKRQLNLLGYDVDEATD 990

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027852989  666 GFQCLSAMghSKTSIQVVILDLHMPEMDGFEVAIRVRKFHShGWPlIIALSATSEELVWDRCLQVGINGLIRKPVLLQGM 745
Cdd:PRK09959   991 GVQALHKV--SMQHYDLLITDVNMPNMDGFELTRKLREQNS-SLP-IWGLTANAQANEREKGLSCGMNLCLFKPLTLDVL 1066

                          410
                   ....*....|.
gi 1027852989  746 AEELQRVLQRA 756
Cdd:PRK09959  1067 KTHLSQLHQVA 1077
CitB COG4565
DNA-binding response regulator DpiB of citrate/malate metabolism [Transcription, Signal ...
 632-756 4.06e-18

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


Pssm-ID: 443622 [Multi-domain]  Cd Length: 138  Bit Score: 81.55  E-value: 4.06e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027852989 632 KGLQVLLADDDDVNRMVTKKLLEKL-GCQVIAV-STGFQCLSAMGHSKtsIQVVILDLHMPEMDGFEVAIRVRKFHSHgw 709
Cdd:COG4565     2 KMIRVLIVEDDPMVAELLRRYLERLpGFEVVGVaSSGEEALALLAEHR--PDLILLDIYLPDGDGLELLRELRARGPD-- 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1027852989 710 PLIIALSATSEELVWDRCLQVGINGLIRKPVllqgMAEELQRVLQRA 756
Cdd:COG4565    78 VDVIVITAARDPETVREALRAGVVDYLIKPF----TFERLREALERY 120
PRK11466 PRK11466
hybrid sensory histidine kinase TorS; Provisional
 321-756 1.15e-17

hybrid sensory histidine kinase TorS; Provisional


Pssm-ID: 236914 [Multi-domain]  Cd Length: 914  Bit Score: 87.65  E-value: 1.15e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027852989 321 EVVADQVAV--ALSHATVLEEsqlmrekleirngllQQAKENAVKATQARNSFQKVMNNGMRQPMHSVLGLLSILQDeNF 398
Cdd:PRK11466  410 EQLAAQVKArtAELQELVIEH---------------RQARAEAEKASQAKSAFLAAMSHEIRTPLYGILGTAQLLAD-NP 473

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027852989 399 TSSNQRIIIDTMMRTSTVLSTLTNDAMDISEKDEGRIPVEMM--PFQ----LHSLIREASCLVKCLCIykgfGFSTDFPN 472
Cdd:PRK11466  474 ALNAQRDDLRAITDSGESLLTILNDILDYSAIEAGGKNVSVSdePFEprplLESTLQLMSGRVKGRPI----RLATDIAD 549

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027852989 473 SLPNLVMGDEMRTFQVLLHMVGHLLNISfGSGSVVFRVGT---------EDGNDKIWGARRHSIVDEYVTIKfetkinle 543
Cdd:PRK11466  550 DLPTALMGDPRRIRQVITNLLSNALRFT-DEGSIVLRSRTdgeqwlvevEDSGCGIDPAKLAEIFQPFVQVS-------- 620

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027852989 544 ssqrnssmssihfgGRRYNSkelkeGLSFRMCKKLVQMMQGNVYMSSNSEGRAqgmtlilRFLKQSSFRKHMFDLGNPLE 623
Cdd:PRK11466  621 --------------GKRGGT-----GLGLTISSRLAQAMGGELSATSTPEVGS-------CFCLRLPLRVATAPVPKTVN 674

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027852989 624 QAISssmFKGLQVLLADDDDVNRMVTKKLLEKLGCQVIAVSTGFQCLSAMGHSkTSIQVVILDLHMPEMDGFEVAIRVrk 703
Cdd:PRK11466  675 QAVR---LDGLRLLLIEDNPLTQRITAEMLNTSGAQVVAVGNAAQALETLQNS-EPFAAALVDFDLPDYDGITLARQL-- 748

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1027852989 704 fhSHGWPLI--IALSATseelVWDRCLQVGIN----GLIRKPV----LLQGMAEELQRVLQRA 756
Cdd:PRK11466  749 --AQQYPSLvlIGFSAH----VIDETLRQRTSslfrGIIPKPVprevLGQLLAHYLQLQVNND 805
Response_reg pfam00072
Response regulator receiver domain; This domain receives the signal from the sensor partner in ...
 636-740 1.36e-17

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: 79.12  E-value: 1.36e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027852989 636 VLLADDDDVNRMVTKKLLEKLGCQVIAVSTGFQCLSAMGHSKtsIQVVILDLHMPEMDGFEVAIRVRKFHSHgwPLIIAL 715
Cdd:pfam00072   1 VLIVDDDPLIRELLRQLLEKEGYVVAEADDGKEALELLKEER--PDLILLDINMPGMDGLELLKRIRRRDPT--TPVIIL 76

                          90       100
                  ....*....|....*....|....*
gi 1027852989 716 SATSEELVWDRCLQVGINGLIRKPV 740
Cdd:pfam00072  77 TAHGDEDDAVEALEAGADDFLSKPF 101
REC_2_GGDEF cd17544
second phosphoacceptor receiver (REC) domain of uncharacterized GGDEF domain proteins; This ...
 636-754 7.25e-16

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: 74.48  E-value: 7.25e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027852989 636 VLLADDDDVNRMVTKKLLEKLGCQVIAVSTGFQCLSAMGhSKTSIQVVILDLHMPEMDGFEVAIRVRKFHSHGWPLIIAL 715
Cdd:cd17544     3 VLVVDDSATSRNHLRALLRRHNFQVLEAANGQEALEVLE-QHPDIKLVITDYNMPEMDGFELVREIRKKYSRDQLAIIGI 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1027852989 716 SATSEELVWDRCLQVGINGLIRKPVLlqgmAEELQ-RVLQ 754
Cdd:cd17544    82 SASGDNALSARFIKAGANDFLTKPFL----PEEFYcRVTQ 117
AtoC COG2204
DNA-binding transcriptional response regulator, NtrC family, contains REC, AAA-type ATPase, ...
 636-758 1.30e-15

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: 79.62  E-value: 1.30e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027852989 636 VLLADDDDVNRMVTKKLLEKLGCQVIAVSTGFQCLSAMghSKTSIQVVILDLHMPEMDGFEVAIRVRKFHSHgwPLIIAL 715
Cdd:COG2204     5 ILVVDDDPDIRRLLKELLERAGYEVETAASGEEALALL--REEPPDLVLLDLRMPGMDGLELLRELRALDPD--LPVILL 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1027852989 716 SATSEELVWDRCLQVGINGLIRKPVLLqgmaEELQRVLQRAGE 758
Cdd:COG2204    81 TGYGDVETAVEAIKAGAFDYLTKPFDL----EELLAAVERALE 119
PRK11091 PRK11091
aerobic respiration control sensor protein ArcB; Provisional
 356-740 3.93e-15

aerobic respiration control sensor protein ArcB; Provisional


Pssm-ID: 236842 [Multi-domain]  Cd Length: 779  Bit Score: 79.60  E-value: 3.93e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027852989 356 QAKENAVKATQARNSFQKVMNNGMRQPMHSVLGLLSILQDENFTSSnQRIIIDTMMRTSTVLSTLTNDAMDISEKDEGRI 435
Cdd:PRK11091  271 RYQDALEKASRDKTTFISTISHELRTPLNGIVGLSRILLDTELTAE-QRKYLKTIHVSAITLGNIFNDIIDMDKMERRKL 349

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027852989 436 PVEMMPFQLHSLIREASCLVKCLCIYKGFGFSTDFPNSLPNLVMGDEMRTFQVLLHMVGHLLNISfGSGSVVFRVGTEDG 515
Cdd:PRK11091  350 QLDNQPIDFTDFLADLENLSGLQAEQKGLRFDLEPLLPLPHKVITDGTRLRQILWNLISNAVKFT-QQGGVTVRVRYEEG 428

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027852989 516 NDkiwgaRRHSIVDEYVTIKFE--TKInlessqrnssmssihFGgRRYNSKELKEGLS-------FRMCKKLVQMMQGNV 586
Cdd:PRK11091  429 DM-----LTFEVEDSGIGIPEDelDKI---------------FA-MYYQVKDSHGGKPatgtgigLAVSKRLAQAMGGDI 487

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027852989 587 YMSSnSEGraQGMTLILRFLKQSSFRKHmfdlgnpLEQAISSSM-FKGLQVLLADDDDVNRMVTKKLLEKLGCQVIAVST 665
Cdd:PRK11091  488 TVTS-EEG--KGSCFTLTIHAPAVAEEV-------EDAFDEDDMpLPALNILLVEDIELNVIVARSVLEKLGNSVDVAMT 557

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027852989 666 GFQCLSAMghSKTSIQVVILDLHMPEMDGFEVAIRVR-KFHSHGWPLIIALSAT----SEELvwdrcLQVGINGLIRKPV 740
Cdd:PRK11091  558 GKEALEMF--DPDEYDLVLLDIQLPDMTGLDIARELReRYPREDLPPLVALTANvlkdKKEY-----LDAGMDDVLSKPL 630
YesN COG4753
Two-component response regulator, YesN/AraC family, consists of REC and AraC-type DNA-binding ...
 636-739 4.36e-15

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: 71.34  E-value: 4.36e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027852989 636 VLLADDDDVNRMVTKKLLEKL-GCQVIAV-STGFQCLSAMghSKTSIQVVILDLHMPEMDGFEVAIRVRKFHSHGWplII 713
Cdd:COG4753     2 VLIVDDEPLIREGLKRILEWEaGFEVVGEaENGEEALELL--EEHKPDLVITDINMPGMDGLELLEAIRELDPDTK--II 77

                          90       100
                  ....*....|....*....|....*.
gi 1027852989 714 ALSATSEELVWDRCLQVGINGLIRKP 739
Cdd:COG4753    78 ILSGYSDFEYAQEAIKLGADDYLLKP 103
REC_OmpR cd17574
phosphoacceptor receiver (REC) domain of OmpR family response regulators; OmpR-like proteins ...
 637-739 8.03e-15

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: 70.51  E-value: 8.03e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027852989 637 LLADDDDVNRMVTKKLLEKLGCQVIAVSTGFQCLSAmgHSKTSIQVVILDLHMPEMDGFEVAIRVRKFHSHgWPlIIALS 716
Cdd:cd17574     1 LVVEDDEEIAELLSDYLEKEGYEVDTAADGEEALEL--AREEQPDLIILDVMLPGMDGFEVCRRLREKGSD-IP-IIMLT 76

                          90       100
                  ....*....|....*....|....*
gi 1027852989 717 ATSEElvWDR--CLQVGINGLIRKP 739
Cdd:cd17574    77 AKDEE--EDKvlGLELGADDYITKP 99
REC_2_DhkD-like cd17580
second phosphoacceptor receiver (REC) domain of Dictyostelium discoideum hybrid signal ...
 636-753 3.41e-14

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: 69.41  E-value: 3.41e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027852989 636 VLLADDDDVNRMVTKKLLEKLGCQVIAVSTGFQCLSAMGHSKTsiQVVILDLHMPEMDGFEVAIRVRKFHSHGWPLIIAL 715
Cdd:cd17580     1 ILVVDDNEDAAEMLALLLELEGAEVTTAHSGEEALEAAQRFRP--DVILSDIGMPGMDGYELARRLRELPWLANTPAIAL 78

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1027852989 716 SATSEELVWDRCLQVGINGLIRKPVLLqgmaEELQRVL 753
Cdd:cd17580    79 TGYGQPEDRERALEAGFDAHLVKPVDP----DELIELI 112
REC_RpfG-like cd17551
phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase response regulator ...
 635-740 1.24e-13

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: 67.85  E-value: 1.24e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027852989 635 QVLLADDDDVNRMVTKKLLEKLG-CQVIAVSTGFQCLSAmgHSKTSIQVVILDLHMPEMDGFEVAIRVRKFHSHGWPLII 713
Cdd:cd17551     2 RILIVDDNPTNLLLLEALLRSAGyLEVVSFTDPREALAW--CRENPPDLILLDYMMPGMDGLEFIRRLRALPGLEDVPIV 79

                          90       100
                  ....*....|....*....|....*..
gi 1027852989 714 ALSATSEELVWDRCLQVGINGLIRKPV 740
Cdd:cd17551    80 MITADTDREVRLRALEAGATDFLTKPF 106
REC_CheC-like cd17593
phosphoacceptor receiver (REC) domain of uncharacterized response regulators containing a CheC ...
 634-757 3.16e-13

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: 66.79  E-value: 3.16e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027852989 634 LQVLLADDDDVNR-MVTKKLLEKLGCQVIAVSTGFQCLSAMGHSKtsIQVVILDLHMPEMDGFEV--AIRVRKFHshgwP 710
Cdd:cd17593     1 MKVLICDDSSMARkQLARALPADWDVEITFAENGEEALEILREGR--IDVLFLDLTMPVMDGYEVleALPVEQLE----T 74

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1027852989 711 LIIALSATSEELVWDRCLQVGINGLIRKPVllqgMAEELQRVLQRAG 757
Cdd:cd17593    75 KVIVVSGDVQPEAKERVLELGALAFLKKPF----DPEKLAQLLEELG 117
REC_NarL-like cd17535
phosphoacceptor receiver (REC) domain of NarL (Nitrate/Nitrite response regulator L) family ...
 636-753 4.51e-13

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: 66.38  E-value: 4.51e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027852989 636 VLLADDDDVNRMVTKKLLEK-LGCQVIA-VSTGFQCLSAMghSKTSIQVVILDLHMPEMDGFEVAIRVRKFHSHgwPLII 713
Cdd:cd17535     1 VLIVDDHPLVREGLRRLLESePDIEVVGeAADGEEALALL--RELRPDVVLMDLSMPGMDGIEALRRLRRRYPD--LKVI 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1027852989 714 ALSATSEELVWDRCLQVGINGLIRKPVLLQGMAEELQRVL 753
Cdd:cd17535    77 VLTAHDDPEYVLRALKAGAAGYLLKDSSPEELIEAIRAVA 116
AmiR COG3707
Two-component response regulator, AmiR/NasT family, consists of REC and RNA-binding ...
 632-758 5.94e-13

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: 68.06  E-value: 5.94e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027852989 632 KGLQVLLADDDDVNRMVTKKLLEKLGCQVIA-VSTGFQCLSAMghSKTSIQVVILDLHMPEMDGFEVAIRVRKFHSHGwp 710
Cdd:COG3707     2 RGLRVLVVDDEPLRRADLREGLREAGYEVVAeAADGEDAVELV--RELKPDLVIVDIDMPDRDGLEAARQISEERPAP-- 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1027852989 711 lIIALSATSEELVWDRCLQVGINGLIRKPVLLQGMAEELQRVLQRAGE 758
Cdd:COG3707    78 -VILLTAYSDPELIERALEAGVSAYLVKPLDPEDLLPALELALARFRE 124
BaeS COG0642
Signal transduction histidine kinase [Signal transduction mechanisms];
299-605 1.13e-12

Signal transduction histidine kinase [Signal transduction mechanisms];


Pssm-ID: 440407 [Multi-domain]  Cd Length: 328  Bit Score: 69.94  E-value: 1.13e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027852989 299 AILVLVLPSGDFDWSSNEMEIVEVVADQVAVALSHATVLEESQLMREKLEIRNGLLQQAKENAVKATQARNSFQKVMNNG 378
Cdd:COG0642    41 LLLLLLLLLLLLLLALALLALLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLALLLLLEEANEAKSRFLANVSHE 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027852989 379 MRQPMHSVLGLLSILQDEnfTSSNQRIIIDTMMRTSTVLSTLTNDAMDISEKDEGRIPVEMMPFQLHSLIREASCLVKCL 458
Cdd:COG0642   121 LRTPLTAIRGYLELLLEE--LDEEQREYLETILRSADRLLRLINDLLDLSRLEAGKLELEPEPVDLAELLEEVVELFRPL 198

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027852989 459 CIYKGFGFSTDFPNSLPnLVMGDEMRTFQVLLHMVGhllN-ISFGS--GSVVFRVGTEDGNDKIW----G-----ARRHS 526
Cdd:COG0642   199 AEEKGIELELDLPDDLP-TVRGDPDRLRQVLLNLLS---NaIKYTPegGTVTVSVRREGDRVRISvedtGpgippEDLER 274

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1027852989 527 IVDEYVTIKfetkinlessqrnssmssihfGGRRYNSKELkeGLSfrMCKKLVQMMQGNVYMSSNSEgraQGMTLILRF 605
Cdd:COG0642   275 IFEPFFRTD---------------------PSRRGGGTGL--GLA--IVKRIVELHGGTIEVESEPG---KGTTFTVTL 325
PRK15347 PRK15347
two component system sensor kinase;
354-749 2.29e-12

two component system sensor kinase;


Pssm-ID: 237951 [Multi-domain]  Cd Length: 921  Bit Score: 70.83  E-value: 2.29e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027852989 354 LQQAKENAVKATQARNSFQKVMNNGMRQPMHSVLGLLSILQDENFTSSnQRIIIDTMMRTSTVLSTLTNDAMDISEKDEG 433
Cdd:PRK15347  384 LAEAKQRAEQANKRKSEHLTTISHEIRTPLNGVLGALELLQNTPLTAE-QMDLADTARQCTLSLLAIINNLLDFSRIESG 462

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027852989 434 RIPVEMMPFQLHSLIREASCLVKCLCIYKGFGFSTDFPNSLPNLVMGDEMRTFQVLLHMVGHllnisfgsgSVVFrvgTE 513
Cdd:PRK15347  463 QMTLSLEETALLPLLDQAMLTIQGPAQSKSLTLRTFVGAHVPLYLHLDSLRLRQILVNLLGN---------AVKF---TE 530

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027852989 514 DGNDKIWGARRH-----SIVD--EYVTIKFETKInlessQRNSSMSSIHFGGrrynskelkEGLSFRMCKKLVQMMQGNV 586
Cdd:PRK15347  531 TGGIRLRVKRHEqqlcfTVEDtgCGIDIQQQQQI-----FTPFYQADTHSQG---------TGLGLTIASSLAKMMGGEL 596

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027852989 587 YMSSNS-EG--------------------------------RAQGMTLI------------LRFLKQSSFR---KHMFDL 618
Cdd:PRK15347  597 TLFSTPgVGscfslvlplneyappeplkgelsaplalhrqlSAWGITCQpghqnpalldpeLAYLPGRLYDllqQIIQGA 676

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027852989 619 GNPLEQAISSSMFKgLQVLLADDDDVNRMVTKKLLEKLGCQVIAVSTGFQCLsAMGHSKTsIQVVILDLHMPEMDGFEVA 698
Cdd:PRK15347  677 PNEPVINLPLQPWQ-LQILLVDDVETNRDIIGMMLVELGQQVTTAASGTEAL-ELGRQHR-FDLVLMDIRMPGLDGLETT 753

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1027852989 699 IRVRkfHS----HGWPLIIALSAT--SEELvwDRCLQVGINGLIRKPVLLQGMAEEL 749
Cdd:PRK15347  754 QLWR--DDpnnlDPDCMIVALTANaaPEEI--HRCKKAGMNHYLTKPVTLAQLARAL 806
REC_typeB_ARR-like cd17584
phosphoacceptor receiver (REC) domain of type B Arabidopsis response regulators (ARRs) and ...
 636-756 7.28e-12

phosphoacceptor receiver (REC) domain of type B Arabidopsis response regulators (ARRs) and similar domains; Type-B ARRs (Arabidopsis response regulators) are a class of MYB-type transcription factors that act as major players in the transcriptional activation of cytokinin-responsive genes. They directly regulate the expression of type-A ARR genes and other downstream target genes. Cytokinin is a plant hormone implicated in many growth and development processes including shoot organogenesis, leaf senescence, sink/source relationships, vascular development, lateral bud release, and photomorphogenic development. Cytokinin signaling involves a phosphorelay cascade by histidine kinase receptors (AHKs), histidine phosphotransfer proteins (AHPs) and downstream ARRs. ARRs are divided into two groups, type-A and -B, according to their sequence and domain structure. Type-B ARRs contain a receiver (REC) domain and a large C-terminal extension that has characteristics of an effector or output domain, with a Myb-like DNA binding domain referred to as the GARP domain. The GARP domain is a motif specific to plant transcription factors. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381121 [Multi-domain]  Cd Length: 115  Bit Score: 62.65  E-value: 7.28e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027852989 636 VLLADDDDVNRMVTKKLLEKLGCQVIAVSTGFQCLSAMGHSKTSIQVVILDLHMPEMDGFEVAIRVRKfhSHGWPLIIAL 715
Cdd:cd17584     1 VLVVDDDPTCLAILKRMLLRCGYQVTTCTDAEEALSMLRENKDEFDLVITDVHMPDMDGFEFLELIRL--EMDLPVIMMS 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1027852989 716 SATSEELVWdRCLQVGINGLIRKPVllqgMAEELQRVLQRA 756
Cdd:cd17584    79 ADGSTSTVM-KGLAHGACDYLLKPV----SIEDLKNIWQHV 114
REC_D1_PleD-like cd17538
first (D1) phosphoacceptor receiver (REC) domain of response regulator PleD and similar ...
 636-740 2.45e-11

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: 60.97  E-value: 2.45e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027852989 636 VLLADDDDVNRMVTKKLLEKLGCQVIAVSTGFQCLSAMghSKTSIQVVILDLHMPEMDGFEVAIRVRKFHSHGWPLIIAL 715
Cdd:cd17538     2 ILVVDDEPANRELLEALLSAEGYEVLTADSGQEALALA--EEELPDLILLDVMMPGMDGFEVCRRLKEDPETRHIPVIMI 79

                          90       100
                  ....*....|....*....|....*
gi 1027852989 716 SATSEELVWDRCLQVGINGLIRKPV 740
Cdd:cd17538    80 TALDDREDRIRGLEAGADDFLSKPI 104
REC_Rcp-like cd17557
phosphoacceptor receiver (REC) domain of cyanobacterial phytochrome response regulator Rcp and ...
 635-758 5.18e-11

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: 60.89  E-value: 5.18e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027852989 635 QVLLADDDDVNRMVTKKLLEKLG--CQVIAVSTGFQCLSAMGHSKTSIQ-----VVILDLHMPEMDGFEV--AIR----V 701
Cdd:cd17557     1 TILLVEDNPGDAELIQEAFKEAGvpNELHVVRDGEEALDFLRGEGEYADaprpdLILLDLNMPRMDGFEVlrEIKadpdL 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1027852989 702 RKFhshgwPLIIaLSATSEElvWD--RCLQVGINGLIRKPVLLqgmaEELQRVLQRAGE 758
Cdd:cd17557    81 RRI-----PVVV-LTTSDAE--EDieRAYELGANSYIVKPVDF----EEFVEAIRSLGE 127
REC_CpdR_CckA-like cd18160
phosphoacceptor receiver (REC) domain of Brucella abortus CpdR and CckA, and similar domains; ...
 636-739 5.42e-11

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: 59.82  E-value: 5.42e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027852989 636 VLLADDDDVNRMVTKKLLEKLGCQVIAVSTGFQCLSAMgHSKTSIQVVILDLHMPEMDGFEVAIRVRKFHSHgwPLIIAL 715
Cdd:cd18160     2 ILLADDEPSVRKFIVTTLKKAGYAVTEAESGAEALEKL-QQGKDIDIVVTDIVMPEMDGIELAREARKIDPD--VKILFI 78

                          90       100
                  ....*....|....*....|....*
gi 1027852989 716 SATSeELVWDRCLQ-VGINGLIRKP 739
Cdd:cd18160    79 SGGA-AAAPELLSDaVGDNATLKKP 102
LytT COG3279
DNA-binding response regulator, LytR/AlgR family [Transcription, Signal transduction ...
 634-756 1.28e-10

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


Pssm-ID: 442510 [Multi-domain]  Cd Length: 235  Bit Score: 62.14  E-value: 1.28e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027852989 634 LQVLLADDDDVNRMVTKKLLEKL-GCQVIAV-STGFQCLSAMghSKTSIQVVILDLHMPEMDGFEVAIRVRKFHSHgwPL 711
Cdd:COG3279     2 MKILIVDDEPLARERLERLLEKYpDLEVVGEaSNGEEALELL--EEHKPDLVFLDIQMPGLDGFELARQLRELDPP--PP 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1027852989 712 IIALSATSEELVwdRCLQVGINGLIRKPVLlqgmAEELQRVLQRA 756
Cdd:COG3279    78 IIFTTAYDEYAL--EAFEVNAVDYLLKPID----EERLAKALEKA 116
REC_YesN-like cd17536
phosphoacceptor receiver (REC) domain of YesN and related helix-turn-helix containing response ...
 636-758 3.72e-10

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


Pssm-ID: 381091 [Multi-domain]  Cd Length: 121  Bit Score: 58.12  E-value: 3.72e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027852989 636 VLLADDDDVNRMVTKKLL--EKLGCQVIA-VSTGFQCLSAMGHSKtsIQVVILDLHMPEMDGFEVAIRVRKFHSHgwPLI 712
Cdd:cd17536     1 VLIVDDEPLIREGLKKLIdwEELGFEVVGeAENGEEALELIEEHK--PDIVITDIRMPGMDGLELIEKIRELYPD--IKI 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1027852989 713 IALSATSE-ELVwDRCLQVGINGLIRKPVllqgMAEELQRVLQRAGE 758
Cdd:cd17536    77 IILSGYDDfEYA-QKAIRLGVVDYLLKPV----DEEELEEALEKAKE 118
PRK10841 PRK10841
two-component system sensor histidine kinase RcsC;
634-753 5.26e-10

two-component system sensor histidine kinase RcsC;


Pssm-ID: 182772 [Multi-domain]  Cd Length: 924  Bit Score: 63.07  E-value: 5.26e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027852989 634 LQVLLADDDDVNRMVTKKLLEKLGCQVIAVSTGFQCLSAMghSKTSIQVVILDLHMPEMDGFEVAIRVRKFHsHGWPLI- 712
Cdd:PRK10841  802 MMILVVDDHPINRRLLADQLGSLGYQCKTANDGVDALNVL--SKNHIDIVLTDVNMPNMDGYRLTQRLRQLG-LTLPVIg 878

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1027852989 713 IALSATSEELvwDRCLQVGINGLIRKPVLLqgmaEELQRVL 753
Cdd:PRK10841  879 VTANALAEEK--QRCLEAGMDSCLSKPVTL----DVLKQTL 913
GAF pfam01590
GAF domain; This domain is present in cGMP-specific phosphodiesterases, adenylyl and guanylyl ...
 183-331 7.39e-10

GAF domain; This domain is present in cGMP-specific phosphodiesterases, adenylyl and guanylyl cyclases, phytochromes, FhlA and NifA. Adenylyl and guanylyl cyclases catalyze ATP and GTP to the second messengers cAMP and cGMP, respectively, these products up-regulating catalytic activity by binding to the regulatory GAF domain(s). The opposite hydrolysis reaction is catalyzed by phosphodiesterase. cGMP-dependent 3',5'-cyclic phosphodiesterase catalyzes the conversion of guanosine 3',5'-cyclic phosphate to guanosine 5'-phosphate. Here too, cGMP regulates catalytic activity by GAF-domain binding. Phytochromes are regulatory photoreceptors in plants and bacteria which exist in two thermally-stable states that are reversibly inter-convertible by light: the Pr state absorbs maximally in the red region of the spectrum, while the Pfr state absorbs maximally in the far-red region. This domain is also found in FhlA (formate hydrogen lyase transcriptional activator) and NifA, a transcriptional activator which is required for activation of most Nif operons which are directly involved in nitrogen fixation. NifA interacts with sigma-54. This domain can bind biliverdine and phycocyanobilin (Matilla et al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).


Pssm-ID: 460259 [Multi-domain]  Cd Length: 133  Bit Score: 57.49  E-value: 7.39e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027852989 183 DKHNILYTTLVELSKTLNLHNCAVWMPNENRsvmnlTHGLSPGSAVEYHRSLPIDDPDvleitkdkGVRILRQDSVLAAA 262
Cdd:pfam01590   1 DLEEILQTILEELRELLGADRCALYLPDADG-----LEYLPPGARWLKAAGLEIPPGT--------GVTVLRTGRPLVVP 67

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1027852989 263 SSggPGEPCTVAaiRMPLLRASDFKG--GTPVLVDTR-YAILVLVLPSGDfdWSSNEMEIVEVVADQVAVAL 331
Cdd:pfam01590  68 DA--AGDPRFLD--PLLLLRNFGIRSllAVPIIDDGElLGVLVLHHPRPP--FTEEELELLEVLADQVAIAL 133
REC_PdtaR-like cd19932
phosphoacceptor receiver (REC) domain of PdtaR and similar proteins; This subfamily includes ...
 634-740 8.03e-10

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: 57.04  E-value: 8.03e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027852989 634 LQVLLADDDDVNRMVTKKLLEKLGCQVIA-VSTGFQCLSAMGHSKTSiqVVILDLHMPEMDGFEVAirvRKFHSHGWPLI 712
Cdd:cd19932     1 VRVLIAEDEALIRMDLREMLEEAGYEVVGeASDGEEAVELAKKHKPD--LVIMDVKMPRLDGIEAA---KIITSENIAPI 75

                          90       100
                  ....*....|....*....|....*...
gi 1027852989 713 IALSATSEELVWDRCLQVGINGLIRKPV 740
Cdd:cd19932    76 VLLTAYSQQDLVERAKEAGAMAYLVKPF 103
PRK11107 PRK11107
hybrid sensory histidine kinase BarA; Provisional
 345-748 3.22e-09

hybrid sensory histidine kinase BarA; Provisional


Pssm-ID: 236848 [Multi-domain]  Cd Length: 919  Bit Score: 60.63  E-value: 3.22e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027852989 345 EKLEIRNGLLQQAKENAVKATQARNSFQKVMNNGMRQPMHSVLGllsilqdenFT--------SSNQRIIIDTMMRTSTV 416
Cdd:PRK11107  270 EQMEIQNVELDLAKKRAQEAARIKSEFLANMSHELRTPLNGVIG---------FTrqtlktplTPTQRDYLQTIERSANN 340

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027852989 417 LSTLTNDAMDISEKDEGRIPVEMMPFQLHSLIREASCLVKCLCIYKGFGFSTDFPNSLPNLVMGDEMRTFQVLLHMVGhl 496
Cdd:PRK11107  341 LLAIINDILDFSKLEAGKLVLENIPFSLRETLDEVVTLLAHSAHEKGLELTLNIDPDVPDNVIGDPLRLQQIITNLVG-- 418

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027852989 497 lN-ISFgsgsvvfrvgTEDGNDKIWGARRhSIVDEYVTIKFEtkinlessqrnssmssIH-----------------FG- 557
Cdd:PRK11107  419 -NaIKF----------TESGNIDILVELR-ALSNTKVQLEVQ----------------IRdtgigiserqqsqlfqaFRq 470

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027852989 558 -----GRRYNSKelkeGLSFRMCKKLVQMMQGNVYMSSNSEgraQGmtlilrflkqSSFRKHM-FDLG-NPLEQAISSSM 630
Cdd:PRK11107  471 adasiSRRHGGT----GLGLVITQKLVNEMGGDISFHSQPN---RG----------STFWFHLpLDLNpNPIIDGLPTDC 533

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027852989 631 FKGLQVLLADDDDVNRMVTKKLLEKLGCQVIAVSTgfqcLSAMGHSKTSIQVVILDLHMPEMDGfEVAIRVRKFHSHGWP 710
Cdd:PRK11107  534 LAGKRLLYVEPNSAAAQATLDILSETPLEVTYSPT----LSQLPEAHYDILLLGLPVTFREPLT-MLHERLAKAKSMTDF 608

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|..
gi 1027852989 711 LIIALSATSEELVwDRCLQVGINGLIRKPV----LLQGMAEE 748
Cdd:PRK11107  609 LILALPCHEQVLA-EQLKQDGADACLSKPLshtrLLPALLEP 649
REC_typeA_ARR cd17581
phosphoacceptor receiver (REC) domain of type A Arabidopsis response regulators (ARRs) and ...
 636-740 5.04e-09

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


Pssm-ID: 381119 [Multi-domain]  Cd Length: 122  Bit Score: 54.68  E-value: 5.04e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027852989 636 VLLADDDDVNRMVTKKLLEKLGCQVIAVSTGFQCLSAMG---------HSKTSIQVVILDLHMPEMDGFEVAIRVRKFHS 706
Cdd:cd17581     1 VLAVDDSLVDRKVIERLLRISSCRVTAVDSGKRALEFLGledeedssnFNEPKVNMIITDYCMPGMTGYDLLKKVKESSA 80

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1027852989 707 -HGWPLIIALSATSEELVwDRCLQVGINGLIRKPV 740
Cdd:cd17581    81 lKEIPVVIMSSENIPTRI-SRCLEEGAEDFLLKPV 114
REC_OmpR_KdpE-like cd17620
phosphoacceptor receiver (REC) domain of KdpE-like OmpR family response regulators; KdpE is a ...
 636-721 5.39e-09

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: 54.09  E-value: 5.39e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027852989 636 VLLADDDDVNRMVTKKLLEKLGCQVIAVSTGFQCLSAMGHSKTSiqVVILDLHMPEMDGFEVAIRVRkfhshGW---PlI 712
Cdd:cd17620     1 ILVIEDEPQIRRFLRTALEAHGYRVFEAETGQEGLLEAATRKPD--LIILDLGLPDMDGLEVIRRLR-----EWsavP-V 72


                  ....*....
gi 1027852989 713 IALSATSEE 721
Cdd:cd17620    73 IVLSARDEE 81
REC_OmpR_BsPhoP-like cd19937
phosphoacceptor receiver (REC) domain of BsPhoP-like OmpR family response regulators; Bacillus ...
 640-739 1.43e-08

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: 53.43  E-value: 1.43e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027852989 640 DDDDVNRMVtKKLLEKLGCQVIAVSTGFQCLSAMghSKTSIQVVILDLHMPEMDGFEVAIRVRKFHSHGWPLIIALSATS 719
Cdd:cd19937     5 DEEDIVELL-KYNLEKEGYEVVTAYDGEEALKRA--KDEKPDLIILDLMLPGIDGLEVCRILRSDPKTSSIPIIMLTAKG 81

                          90       100
                  ....*....|....*....|..
gi 1027852989 720 EELvwDRC--LQVGINGLIRKP 739
Cdd:cd19937    82 EEF--DKVlgLELGADDYITKP 101
REC_CheY_CheY3 cd19923
phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY3 and similar CheY ...
 634-753 1.59e-08

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: 53.50  E-value: 1.59e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027852989 634 LQVLLADDDDVNRMVTKKLLEKLGCQVIAVST-GFQCLSAMghSKTSIQVVILDLHMPEMDGFEV--AIRVRKFHSHGWP 710
Cdd:cd19923     1 MKVLVVDDFSTMRRIIKNLLKELGFNNVEEAEdGVDALEKL--KAGGFDFVITDWNMPNMDGLELlkTIRADGALSHLPV 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1027852989 711 LIIALSATSEELVwdRCLQVGINGLIRKPVLLQGMAEELQRVL 753
Cdd:cd19923    79 LMVTAEAKKENVI--AAAQAGVNNYIVKPFTAATLKEKLEKIF 119
REC_CheY cd17542
phosphoacceptor receiver (REC) domain of chemotaxis protein CheY; The chemotaxis response ...
 635-753 1.64e-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: 53.05  E-value: 1.64e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027852989 635 QVLLADDDDVNRMVTKKLLEKLGCQVIA-VSTGFQCLSAMGHSKtsIQVVILDLHMPEMDGFEVAIRVRKFHSHGwpLII 713
Cdd:cd17542     2 KVLIVDDAAFMRMMLKDILTKAGYEVVGeAANGEEAVEKYKELK--PDLVTMDITMPEMDGIEALKEIKKIDPNA--KVI 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1027852989 714 ALSATSEELVWDRCLQVGINGLIRKPVLLQGMAEELQRVL 753
Cdd:cd17542    78 MCSAMGQEEMVKEAIKAGAKDFIVKPFQPERVLEAVEKVL 117
REC_hyHK cd17598
phosphoacceptor receiver (REC) domain of uncharacterized hybrid sensor histidine kinase ...
 636-753 2.29e-08

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: 52.71  E-value: 2.29e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027852989 636 VLLADDDDVNRMVTKKLLEKLGCQVIAVSTGFQCLSAMGHSKTSIqvVILDLHMPEMDGFEVAIRVRKFHSHGWPLIIAL 715
Cdd:cd17598     1 ILIVEDSPTQAEQLKHILEEQGYKVQVARNGREALAMLAEHRPTL--VISDIVMPEMDGYELCRKIKSDPDLKDIPVILL 78

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1027852989 716 SATSEELVWDRCLQVGINGLIRKPVLLQGMAEELQRVL 753
Cdd:cd17598    79 TTLSDPRDVIRGLECGADNFITKPYDEKYLLSRIKYIL 116
REC_PA4781-like cd19920
phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase PA4781 and similar ...
 636-740 3.43e-08

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: 51.74  E-value: 3.43e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027852989 636 VLLADDDDVNRMVTKKLLEKLGCQVIAVSTGFQCLSAMGHSKtsIQVVILDLHMPEMDGFEVAIRVRK-FHSHGWPLII- 713
Cdd:cd19920     1 ILIVDDVPDNLRLLSELLRAAGYRVLVATDGQQALQRAQAEP--PDLILLDVMMPGMDGFEVCRRLKAdPATRHIPVIFl 78

                          90       100
                  ....*....|....*....|....*...
gi 1027852989 714 -ALSATSEELvwdRCLQVGINGLIRKPV 740
Cdd:cd19920    79 tALTDTEDKV---KGFELGAVDYITKPF 103
REC_NtrC cd19919
phosphoacceptor receiver (REC) domain of DNA-binding transcriptional regulator NtrC; ...
 635-713 5.69e-08

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: 51.50  E-value: 5.69e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1027852989 635 QVLLADDDDVNRMVTKKLLEKLGCQVIAVSTGFQCLSAMGHSKTsiQVVILDLHMPEMDGFEVAIRVRKFHSHgWPLII 713
Cdd:cd19919     2 TVWIVDDDSSIRWVLERALAGAGLTVTSFENAQEALAALASSQP--DVLISDIRMPGMDGLALLAQIKQRHPD-LPVII 77
REC smart00448
cheY-homologous receiver domain; CheY regulates the clockwise rotation of E. coli flagellar ...
 636-690 8.96e-08

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


Pssm-ID: 214668 [Multi-domain]  Cd Length: 55  Bit Score: 49.10  E-value: 8.96e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1027852989  636 VLLADDDDVNRMVTKKLLEKLGCQVIAVSTGFQCLSAMghSKTSIQVVILDLHMP 690
Cdd:smart00448   3 ILVVDDDPLLRELLKALLEKEGYEVDEATDGEEALELL--KEEKPDLILLDIMMP 55
REC_RssB-like cd17555
phosphoacceptor receiver (REC) domain of Pseudomonas aeruginosa RssB and similar domains; ...
 636-703 9.08e-08

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: 51.05  E-value: 9.08e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1027852989 636 VLLADDDDVNRMVTKKLLEKLGCQVIAVSTGFQCLSAMGHSKtsIQVVILDLHMPEMDGFEVAIRVRK 703
Cdd:cd17555     3 ILVIDDDEVVRESIAAYLEDSGFQVLQAADGRQGLELFRSEQ--PDLVLCDLRMPEMDGLEVLKQITK 68
REC_CheV-like cd19924
phosphoacceptor receiver (REC) domain of chemotaxis protein CheV and similar proteins; This ...
 636-739 1.17e-07

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: 50.45  E-value: 1.17e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027852989 636 VLLADDDDVNRMVTKKLLEKLGCQVIAVSTGFQCLSAMGHSKTS-------IQVVILDLHMPEMDGFEVAIRVR---KFH 705
Cdd:cd19924     1 ILVVDDSPTARKQLRDLLKNLGFEIAEAVDGEEALNKLENLAKEgndlskeLDLIITDIEMPKMDGYELTFELRddpRLA 80

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1027852989 706 ShgWPLIIALSATSEELVwDRCLQVGINGLIRKP 739
Cdd:cd19924    81 N--IPVILNSSLSGEFSR-ARGKKVGADAYLAKF 111
PRK09958 PRK09958
acid-sensing system DNA-binding response regulator EvgA;
637-745 1.41e-07

acid-sensing system DNA-binding response regulator EvgA;


Pssm-ID: 182168 [Multi-domain]  Cd Length: 204  Bit Score: 52.59  E-value: 1.41e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027852989 637 LLADDDDVNRMVTKKLLEKLGCQVIA-VSTGFQCLSAMghSKTSIQVVILDLHMPEMDGFEVAIRVRKFHSHGwpLIIAL 715
Cdd:PRK09958    4 IIIDDHPLAIAAIRNLLIKNDIEILAeLTEGGSAVQRV--ETLKPDIVIIDVDIPGVNGIQVLETLRKRQYSG--IIIIV 79

                          90       100       110
                  ....*....|....*....|....*....|
gi 1027852989 716 SATSEELVWDRCLQVGINGLIRKPvllQGM 745
Cdd:PRK09958   80 SAKNDHFYGKHCADAGANGFVSKK---EGM 106
REC_DC-like cd17534
phosphoacceptor receiver (REC) domain of modulated diguanylate cyclase and similar domains; ...
 636-756 2.45e-07

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


Pssm-ID: 381089 [Multi-domain]  Cd Length: 117  Bit Score: 49.71  E-value: 2.45e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027852989 636 VLLADDDDVNRMVTKKLLEKLGCQVIA-VSTGFQCLSAMghSKTSIQVVILDLHMP-EMDGFEVAIRVRKFhsHGWPlII 713
Cdd:cd17534     3 ILIVEDEAIIALDLKEILESLGYEVVGiADSGEEAIELA--EENKPDLILMDINLKgDMDGIEAAREIREK--FDIP-VI 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1027852989 714 ALSATSEELVWDRCLQVGINGLIRKPVllqgMAEELQRVLQRA 756
Cdd:cd17534    78 FLTAYSDEETLERAKETNPYGYLVKPF----NERELKAAIELA 116
REC_HupR-like cd17569
phosphoacceptor receiver (REC) domain of hydrogen uptake protein regulator (HupR) and similar ...
 636-703 3.02e-07

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: 49.71  E-value: 3.02e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1027852989 636 VLLADDDDVNRMVTKKLLEKLGCQVIAVSTGFQCLSAMghSKTSIQVVILDLHMPEMDGFEVAIRVRK 703
Cdd:cd17569     3 ILLVDDEPNILKALKRLLRREGYEVLTATSGEEALEIL--KQEPVDVVISDQRMPGMDGAELLKRVRE 68
REC_DctD-like cd17549
phosphoacceptor receiver (REC) domain of C4-dicarboxylic acid transport protein D (DctD) and ...
 636-703 3.06e-07

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: 49.80  E-value: 3.06e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1027852989 636 VLLADDDDVNRMVTKKLLEKLGCQVIAVSTGFQCLSAMghSKTSIQVVILDLHMPEMDGFEVAIRVRK 703
Cdd:cd17549     1 VLLVDDDADVREALQQTLELAGFRVRAFADAEEALAAL--SPDFPGVVISDIRMPGMDGLELLAQIRE 66
GAF COG2203
GAF domain [Signal transduction mechanisms];
174-398 3.34e-07

GAF domain [Signal transduction mechanisms];


Pssm-ID: 441805 [Multi-domain]  Cd Length: 712  Bit Score: 54.04  E-value: 3.34e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027852989 174 LTREIRKSIDKHNILYTTLVELSKTLNLHNCAVWMPNENRSVMNLTHglSPGSAVEYHRSLPIDDPDVLE-ITKDKGVRI 252
Cdd:COG2203   198 ISQALRSALDLEELLQRILELAGELLGADRGAILLVDEDGGELELVA--APGLPEEELGRLPLGEGLAGRaLRTGEPVVV 275

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027852989 253 --LRQDSVLAAASSGGPGEPCTVAAIRMPLLRAsdfkggtpvlvDTRYAILVLVLPSGDfDWSSNEMEIVEVVADQVAVA 330
Cdd:COG2203   276 ndASTDPRFAPSLRELLLALGIRSLLCVPLLVD-----------GRLIGVLALYSKEPR-AFTEEDLELLEALADQAAIA 343

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1027852989 331 LSHATVLEESQLMREKLEIRNGLLQQAKENAVKATQARNSFQKVMNNGMRQPMHSVLGLLSILQDENF 398
Cdd:COG2203   344 IERARLYEALEAALAALLQELALLRLLLDLELTLLRLRQLLLELLLALLLLLSLLGAELLLLLLDAAD 411
PRK11361 PRK11361
acetoacetate metabolism transcriptional regulator AtoC;
636-756 3.51e-07

acetoacetate metabolism transcriptional regulator AtoC;


Pssm-ID: 183099 [Multi-domain]  Cd Length: 457  Bit Score: 53.31  E-value: 3.51e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027852989 636 VLLADDDD-VNRMVTKkLLEKLGCQVIAVSTGFQCLSAMGHSKTSiqVVILDLHMPEMDGFEVAIRVRKFHShGWPLIIa 714
Cdd:PRK11361    7 ILIVDDEDnVRRMLST-AFALQGFETHCANNGRTALHLFADIHPD--VVLMDIRMPEMDGIKALKEMRSHET-RTPVIL- 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1027852989 715 LSATSEELVWDRCLQVG-------------INGLIRKPVLLQGMAEELqRVLQRA 756
Cdd:PRK11361   82 MTAYAEVETAVEALRCGafdyvikpfdldeLNLIVQRALQLQSMKKEI-RHLHQA 135
REC_OmpR_PmrA-like cd17624
phosphoacceptor receiver (REC) domain of PmrA-like OmpR family response regulators; This ...
 636-755 4.08e-07

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: 49.02  E-value: 4.08e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027852989 636 VLLADDDDVNRMVTKKLLEKLGCQVIAVSTGFQCLSAMGHskTSIQVVILDLHMPEMDGFEVAIRVRKfhsHGWPL-IIA 714
Cdd:cd17624     1 ILLVEDDALLGDGLKTGLRKAGYAVDWVRTGAEAEAALAS--GPYDLVILDLGLPDGDGLDLLRRWRR---QGQSLpVLI 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1027852989 715 LSA--TSEELVwdRCLQVGINGLIRKPVLLqgmaEELQ---RVLQR 755
Cdd:cd17624    76 LTArdGVDDRV--AGLDAGADDYLVKPFAL----EELLarlRALLR 115
REC_OmpR_YycF-like cd17614
phosphoacceptor receiver (REC) domain of YrcF-like OmpR family response regulators; YycF ...
 636-752 6.00e-07

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


Pssm-ID: 381130 [Multi-domain]  Cd Length: 115  Bit Score: 48.57  E-value: 6.00e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027852989 636 VLLADDDDVNRMVTKKLLEKLGCQVIAVSTGFQCLSAMGHSKTSIqvVILDLHMPEMDGFEVAIRVRKfhSHGWPlIIAL 715
Cdd:cd17614     1 ILVVDDEKPISDILKFNLTKEGYEVVTAYDGREALEKVEEEQPDL--ILLDLMLPEKDGLEVCREVRK--TSNVP-IIML 75

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1027852989 716 SATSEELVWDRCLQVGINGLIRKPVllqGMAEELQRV 752
Cdd:cd17614    76 TAKDSEVDKVLGLELGADDYVTKPF---SNRELLARV 109
REC_hyHK_blue-like cd18161
phosphoacceptor receiver (REC) domain of hybrid sensor histidine kinase/response regulators ...
 636-707 6.54e-07

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: 48.11  E-value: 6.54e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1027852989 636 VLLADDDDVNRMVTKKLLEKLGCQVIAVSTGFQCLSAMgHSKTSIQVVILDLHMP-EMDGFEVAIRVRKFHSH 707
Cdd:cd18161     1 VLVVEDDPDVRRLTAEVLEDLGYTVLEAASGDEALDLL-ESGPDIDLLVTDVIMPgGMNGSQLAEEARRRRPD 72
REC_OmpR_CpxR cd17623
phosphoacceptor receiver (REC) domain of CpxR-like OmpR family response regulators; CpxR is ...
 636-755 7.04e-07

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: 48.46  E-value: 7.04e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027852989 636 VLLADDDDVNRMVTKKLLEKLGCQVIAVSTGFQCLSAMGHSktSIQVVILDLHMPEMDGFEVAIRVRKfhSHGWPlIIAL 715
Cdd:cd17623     1 ILLIDDDRELTELLTEYLEMEGFNVRAAHDGEQGLAALLEG--SPDLVVLDVMLPKMNGLDVLKELRK--TSQVP-VLML 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1027852989 716 SATSEELvwDRC--LQVGINGLIRKPVLLQGMAEELQRVLQR 755
Cdd:cd17623    76 TARGDDI--DRIlgLELGADDYLPKPFNPRELVARIRAILRR 115
REC_RR468-like cd17552
phosphoacceptor receiver (REC) domain of Thermotoga maritima response regulator RR468 and ...
 635-754 8.62e-07

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


Pssm-ID: 381104 [Multi-domain]  Cd Length: 121  Bit Score: 48.32  E-value: 8.62e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027852989 635 QVLLADDDDVNRMVTKKLLEKL-GCQVIAVSTGFQCLSAMGHSKtsIQVVILDLHMPEMDGFEVairVRKFHSH----GW 709
Cdd:cd17552     3 RILVIDDEEDIREVVQACLEKLaGWEVLTASSGQEGLEKAATEQ--PDAILLDVMMPDMDGLAT---LKKLQANpetqSI 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1027852989 710 PLIIaLSA---TSEELVWDrclQVGINGLIRKPVLLQGMAEELQRVLQ 754
Cdd:cd17552    78 PVIL-LTAkaqPSDRQRFA---SLGVAGVIAKPFDPLTLAEQIAKLLG 121
REC_Spo0A cd17561
phosphoacceptor receiver (REC) domain of Spo0A; Spo0A is a response regulator of the ...
 634-739 8.80e-07

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


Pssm-ID: 381109 [Multi-domain]  Cd Length: 108  Bit Score: 47.99  E-value: 8.80e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027852989 634 LQVLLADDD-DVNRMVTKKLLEKLGCQVIAVS-TGFQCLSAMGHSKTSiqVVILDLHMPEMDGFEVAIRVRKFHSHGWPL 711
Cdd:cd17561     2 IKVLIADDNrEFVQLLEEYLNSQPDMEVVGVAhNGQEALELIEEKEPD--VLLLDIIMPHLDGIGVLEKLRRMRLEKRPK 79

                          90       100
                  ....*....|....*....|....*...
gi 1027852989 712 IIALSATSEELVWDRCLQVGINGLIRKP 739
Cdd:cd17561    80 IIMLTAFGQEDITQRAVELGASYYILKP 107
REC_OmpR_MtPhoP-like cd17615
phosphoacceptor receiver (REC) domain of MtPhoP-like OmpR family response regulators; ...
 636-756 1.38e-06

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: 47.73  E-value: 1.38e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027852989 636 VLLADDDDVNRMVTKKLLEKLGCQVIAVSTGFQCLSAMghSKTSIQVVILDLHMPEMDGFEVAIRVRKfHSHGWPliiAL 715
Cdd:cd17615     2 VLVVDDEPNITELLSMALRYEGWDVETAADGAEALAAA--REFRPDAVVLDIMLPDMDGLEVLRRLRA-DGPDVP---VL 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1027852989 716 SATSEELVWDRC--LQVGINGLIRKPVLLQGMAEELQRVLQRA 756
Cdd:cd17615    76 FLTAKDSVEDRIagLTAGGDDYVTKPFSLEEVVARLRALLRRS 118
REC_RocR cd17530
phosphoacceptor receiver (REC) domain of response regulator RocR; The response regulator RocR ...
 634-717 1.57e-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: 47.82  E-value: 1.57e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027852989 634 LQVLLADDDDVNRMVTKKLLEKLGC-QVIAVSTGFQCLSAMGHSKTSIqvVILDLHMPEMDGFEVairVRKFHSHGWPLI 712
Cdd:cd17530     1 LRVLVLDDDPFQCMMAATILEDLGPgNVDEADDGREALVILLCNAPDI--IICDLKMPDMDGIEF---LRHLAESHSNAA 75


                  ....*
gi 1027852989 713 IALSA 717
Cdd:cd17530    76 VILMS 80
REC_citrate_TCS cd19925
phosphoacceptor receiver (REC) domain of citrate family two-component system response ...
 634-751 1.71e-06

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: 47.62  E-value: 1.71e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027852989 634 LQVLLADDDDVNRMVTKKLLEKL-GCQVIA-VSTGFQCLSAMGHskTSIQVVILDLHMPEMDGFEVAIRVRKFHSHGwpL 711
Cdd:cd19925     1 INVLIVEDDPMVAEIHRAYVEQVpGFTVIGtAGTGEEALKLLKE--RQPDLILLDIYLPDGNGLDLLRELRAAGHDV--D 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1027852989 712 IIALSATSEELVWDRCLQVGINGLIRKPVLLQGMAEELQR 751
Cdd:cd19925    77 VIVVTAANDVETVREALRLGVVDYLIKPFTFERLRQRLER 116
Spo0F COG5803
Stage 0 sporulation initiation response regulator Spo0F [Cell cycle control, cell division, ...
 635-753 2.04e-06

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


Pssm-ID: 444505 [Multi-domain]  Cd Length: 119  Bit Score: 47.10  E-value: 2.04e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027852989 635 QVLLADDDDVNRMVTKKLLEKLGCQVIAVSTGFQCLSAMGHSKtsIQVVILDLHMPEMDGFEVAIRVRKFHSHgwPLIIA 714
Cdd:COG5803     4 KILIVDDQAGIRMLLKEVLKKEGYEVFQAANGKEALEKVKELK--PDLVLLDMKMPGMDGIEILKEIKEIDPD--IPVIM 79

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1027852989 715 LSATSEELVWDRCLQVGINGLIRKPVLLQGMAEELQRVL 753
Cdd:COG5803    80 MTAYGELDMVEEAKELGAKGYFTKPFDIDELREAVNKLL 118
REC_DivK-like cd17548
phosphoacceptor receiver (REC) domain of DivK and similar proteins; Caulobacter crescentus ...
 636-740 2.58e-06

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: 46.76  E-value: 2.58e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027852989 636 VLLADDDDVNRMVTKKLLEKLGCQVIAVSTGFQCLSAMGHSKTSIqvVILDLHMPEMDGFEVAIRVRKF-HSHGWPlIIA 714
Cdd:cd17548     2 ILIVEDNPLNMKLARDLLESAGYEVLEAADGEEALEIARKEKPDL--ILMDIQLPGMDGLEATRLLKEDpATRDIP-VIA 78

                          90       100       110
                  ....*....|....*....|....*....|
gi 1027852989 715 LSATS----EElvwdRCLQVGINGLIRKPV 740
Cdd:cd17548    79 LTAYAmkgdRE----KILEAGCDGYISKPI 104
CitB COG2197
DNA-binding response regulator, NarL/FixJ family, contains REC and HTH domains [Signal ...
 636-701 3.21e-06

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


Pssm-ID: 441799 [Multi-domain]  Cd Length: 131  Bit Score: 47.19  E-value: 3.21e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1027852989 636 VLLADDDDVNRMVTKKLLEKL-GCQVIA-VSTGFQCLSAMGHskTSIQVVILDLHMPEMDGFEVAIRV 701
Cdd:COG2197     4 VLIVDDHPLVREGLRALLEAEpDIEVVGeAADGEEALELLEE--LRPDVVLLDIRMPGMDGLEALRRL 69
orf27 CHL00148
Ycf27; Reviewed
 635-756 4.08e-06

Ycf27; Reviewed


Pssm-ID: 214376 [Multi-domain]  Cd Length: 240  Bit Score: 48.94  E-value: 4.08e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027852989 635 QVLLADDDDVNRMVTKKLLEKLGCQVIAVSTGFQCLSAMghSKTSIQVVILDLHMPEMDGFEVAIRVRKfhSHGWPlIIA 714
Cdd:CHL00148    8 KILVVDDEAYIRKILETRLSIIGYEVITASDGEEALKLF--RKEQPDLVILDVMMPKLDGYGVCQEIRK--ESDVP-IIM 82

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1027852989 715 LSATSEelVWDRC--LQVGINGLIRKPVLLQGMAEELQRVLQRA 756
Cdd:CHL00148   83 LTALGD--VSDRItgLELGADDYVVKPFSPKELEARIRSVLRRT 124
REC_LytTR_AlgR-like cd17532
phosphoacceptor receiver (REC) domain of LytTR/AlgR family response regulators similar to AlgR; ...
 636-755 4.14e-06

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: 46.38  E-value: 4.14e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027852989 636 VLLADDDDVNRMVTKKLLEKLG-CQVIA-VSTGFQCLSAMGHSKtsIQVVILDLHMPEMDGFEVAIRVRKFHSHgwPLII 713
Cdd:cd17532     1 ALIVDDEPLAREELRYLLEEHPdIEIVGeAENGEEALEAIEELK--PDVVFLDIQMPGLDGLELAKKLSKLAKP--PLIV 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1027852989 714 ALSATSEELVwdRCLQVGINGLIRKPVLLQGMAEELQRVLQR 755
Cdd:cd17532    77 FVTAYDEYAV--EAFELNAVDYLLKPFSEERLAEALAKLRKR 116
GAF smart00065
Domain present in phytochromes and cGMP-specific phosphodiesterases; Mutations within these ...
 185-341 4.47e-06

Domain present in phytochromes and cGMP-specific phosphodiesterases; Mutations within these domains in PDE6B result in autosomal recessive inheritance of retinitis pigmentosa.


Pssm-ID: 214500 [Multi-domain]  Cd Length: 149  Bit Score: 46.99  E-value: 4.47e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027852989  185 HNILYTTLVELSKTLNLHNCAVWMPNENRS---VMNLTHGLSPGSaveYHRSLPIDDPDVLEITKDKGVRILR--QDSVL 259
Cdd:smart00065   3 EELLQTILEELRQLLGADRVLIYLVDENDRgelVLVAADGLTLPT---LGIRFPLDEGLAGRVAETGRPLNIPdvEADPL 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027852989  260 AAASSGGPgEPCTVAAIRMPLLRasdfkGGTPVlvdtryAILVLVLPSGDFDWSSNEMEIVEVVADQVAVALSHATVLEE 339
Cdd:smart00065  80 FAEDLLGR-YQGVRSFLAVPLVA-----DGELV------GVLALHNKKSPRPFTEEDEELLQALANQLAIALANAQLYEE 147


                   ..
gi 1027852989  340 SQ 341
Cdd:smart00065 148 LR 149
REC_CheY4-like cd17562
phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY4 and similar CheY ...
 636-753 5.40e-06

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: 46.14  E-value: 5.40e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027852989 636 VLLADDDDVNRMVTKKLLEKLGCQVIAVSTGFQCLSAMghSKTSIQVVILDLHMPEMDGFEVAIRVRKFHSHGWPLIIAL 715
Cdd:cd17562     3 ILAVDDSASIRQMVSFTLRGAGYEVVEAADGRDALSKA--QSKKFDLIITDQNMPNMDGIELIKELRKLPAYKFTPILML 80

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1027852989 716 SATSEELVWDRCLQVGINGLIRKPVLLQGMAEELQRVL 753
Cdd:cd17562    81 TTESSDEKKQEGKAAGATGWLVKPFDPEQLLEVVKKVL 118
PRK10955 PRK10955
envelope stress response regulator transcription factor CpxR;
635-756 6.06e-06

envelope stress response regulator transcription factor CpxR;


Pssm-ID: 182864 [Multi-domain]  Cd Length: 232  Bit Score: 48.26  E-value: 6.06e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027852989 635 QVLLADDDDVNRMVTKKLLEKLGCQVIAVSTGFQCLSAMghsKTSIQVVILDLHMPEMDGFEVAIRVRKFHSHgwPlIIA 714
Cdd:PRK10955    3 KILLVDDDRELTSLLKELLEMEGFNVIVAHDGEQALDLL---DDSIDLLLLDVMMPKKNGIDTLKELRQTHQT--P-VIM 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1027852989 715 LSATSEELvwDRC--LQVGINGLIRKPVLLQGMAEELQRVLQRA 756
Cdd:PRK10955   77 LTARGSEL--DRVlgLELGADDYLPKPFNDRELVARIRAILRRS 118
COG4567 COG4567
DNA-binding response regulator, ActR/RegA family, consists of REC and Fis-type HTH domains ...
 636-705 8.18e-06

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: 46.83  E-value: 8.18e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027852989 636 VLLADDDDVNRMVTKKLLEKLGCQVIAVSTGFQCLSAMghSKTSIQVVILDLHMPEMDGFEVAIRVRKFH 705
Cdd:COG4567     7 LLLVDDDEAFARVLARALERRGFEVTTAASVEEALALL--EQAPPDYAVLDLRLGDGSGLDLIEALRERD 74
PLN03029 PLN03029
type-a response regulator protein; Provisional
 634-742 8.74e-06

type-a response regulator protein; Provisional


Pssm-ID: 215544 [Multi-domain]  Cd Length: 222  Bit Score: 47.72  E-value: 8.74e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027852989 634 LQVLLADDDDVNRMVTKKLLEKLGCQVIAVSTGFQCLSAMG------------------HSKTSIQVVILDLHMPEMDGF 695
Cdd:PLN03029    9 FHVLAVDDSLIDRKLIEKLLKTSSYQVTTVDSGSKALKFLGlheddrsnpdtpsvspnsHQEVEVNLIITDYCMPGMTGY 88

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1027852989 696 EVAIRVRKFHS-HGWPLIIALSATSEELVwDRCLQVGINGLIRKPVLL 742
Cdd:PLN03029   89 DLLKKIKESSSlRNIPVVIMSSENVPSRI-TRCLEEGAEEFFLKPVQL 135
REC_TrrA-like cd17554
phosphoacceptor receiver (REC) domain of Thermotoga maritima response regulator TrrA and ...
 636-720 8.88e-06

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


Pssm-ID: 381106 [Multi-domain]  Cd Length: 113  Bit Score: 45.29  E-value: 8.88e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027852989 636 VLLADDDDVNRMVTKKLLEKLGCQVIAVSTGFQCLSAMGHSKtsIQVVILDLHMPEMDGFEVAIRVRKFHShGWPLIIaL 715
Cdd:cd17554     3 ILVVDDEENIRELYKEELEDEGYEVVTAGNGEEALEKLESED--PDLVILDIKMPGMDGLETLRKIREKKP-DLPVII-C 78


                  ....*
gi 1027852989 716 SATSE 720
Cdd:cd17554    79 TAYSE 83
REC_Ycf29 cd19927
phosphoacceptor receiver (REC) domain of probable transcriptional regulator Ycf29; Ycf29 is a ...
 636-739 1.07e-05

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: 44.68  E-value: 1.07e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027852989 636 VLLADDDDVNRMVTKKLLEKLGCQVIAVSTGFQCLSAMghSKTSIQVVILDLHMPEMDGFEVAIRVRKFHSHGWPLIIAL 715
Cdd:cd19927     1 ILLVDDDPGIRLAVKDYLEDQGFTVIAASNGLEALDLL--NQYIPDLIISDIIMPGVDGYSLLGKLRKNADFDTIPVIFL 78

                          90       100
                  ....*....|....*....|....*.
gi 1027852989 716 saTSEELVWDRCL--QVGINGLIRKP 739
Cdd:cd19927    79 --TAKGMTSDRIKgyNAGCDGYLSKP 102
REC_CheB-like cd17541
phosphoacceptor receiver (REC) domain of chemotaxis response regulator protein-glutamate ...
 636-721 1.39e-05

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: 45.08  E-value: 1.39e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027852989 636 VLLADDDDVNRMVTKKLLEKLGC-QVIAV-STGFQCLSAMghSKTSIQVVILDLHMPEMDGFEVairVRKFHSHGWPLII 713
Cdd:cd17541     3 VLIVDDSAVMRKLLSRILESDPDiEVVGTaRDGEEALEKI--KELKPDVITLDIEMPVMDGLEA---LRRIMAERPTPVV 77


                  ....*...
gi 1027852989 714 ALSATSEE 721
Cdd:cd17541    78 MVSSLTEE 85
REC_OmpR_PrrA-like cd17627
phosphoacceptor receiver (REC) domain of PrrA-like OmpR family response regulators; The ...
 636-755 1.67e-05

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: 44.68  E-value: 1.67e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027852989 636 VLLADDDDVNRMVTKKLLEKLGCQVIAVSTGFQCLSAMghSKTSIQVVILDLHMPEMDGFEVAIRVRKFHSHgWPlIIAL 715
Cdd:cd17627     1 ILVVDDDRAVRESLRRSLRFEGYEVETAVDGAEALRVI--SGNRPDAVVLDVMMPRLDGLEVCRRLRAAGND-LP-ILVL 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1027852989 716 SATSEelVWDRC--LQVGINGLIRKPVLLQGMAEELQRVLQR 755
Cdd:cd17627    77 TARDS--VSDRVagLDAGADDYLVKPFALEELLARVRALLRR 116
psREC_PRR cd17582
pseudo receiver domain of pseudo-response regulators; In Arabidopsis, five pseudo-response ...
 636-695 1.81e-05

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


Pssm-ID: 381120 [Multi-domain]  Cd Length: 104  Bit Score: 44.31  E-value: 1.81e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027852989 636 VLLADDDDVNRMVTKKLLEKLGCQVIAVSTGFQCLSAMGHSKTSIQVVILDLHMPEMDGF 695
Cdd:cd17582     1 VLLVENDDSTRQIVTALLRKCSYEVTAASDGLQAWDVLEDEQNEIDLILTEVDLPVSSGF 60
PRK15369 PRK15369
two component system response regulator;
677-738 2.24e-05

two component system response regulator;


Pssm-ID: 185267 [Multi-domain]  Cd Length: 211  Bit Score: 46.23  E-value: 2.24e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1027852989 677 KTSIQVVILDLHMPEMDGFEVAIRVRKfhshGWP--LIIALSATSEELVWDRCLQVGINGLIRK 738
Cdd:PRK15369   47 QLEPDIVILDLGLPGMNGLDVIPQLHQ----RWPamNILVLTARQEEHMASRTLAAGALGYVLK 106
PRK10610 PRK10610
chemotaxis protein CheY;
632-757 4.01e-05

chemotaxis protein CheY;


Pssm-ID: 170568 [Multi-domain]  Cd Length: 129  Bit Score: 43.81  E-value: 4.01e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027852989 632 KGLQVLLADDDDVNRMVTKKLLEKLGCQ-VIAVSTGFQCLSAMGHSktSIQVVILDLHMPEMDGFEVAIRVRKFHSHG-W 709
Cdd:PRK10610    4 KELKFLVVDDFSTMRRIVRNLLKELGFNnVEEAEDGVDALNKLQAG--GFGFVISDWNMPNMDGLELLKTIRADGAMSaL 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1027852989 710 P-LIIALSATSEELVwdRCLQVGINGLIRKPVLLQGMAEELQRVLQRAG 757
Cdd:PRK10610   82 PvLMVTAEAKKENII--AAAQAGASGYVVKPFTAATLEEKLNKIFEKLG 128
FixJ COG4566
DNA-binding response regulator, FixJ family, consists of REC and HTH domains [Signal ...
 636-713 4.69e-05

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


Pssm-ID: 443623 [Multi-domain]  Cd Length: 196  Bit Score: 45.09  E-value: 4.69e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1027852989 636 VLLADDDDVNRMVTKKLLEKLGCQVIAVSTGFQCLSAMGHSKTSiqVVILDLHMPEMDGFEVAIRVRKFHSHgWPLII 713
Cdd:COG4566     2 VYIVDDDEAVRDSLAFLLESAGLRVETFASAEAFLAALDPDRPG--CLLLDVRMPGMSGLELQEELAARGSP-LPVIF 76
REC_NtrC1-like cd17572
phosphoacceptor receiver (REC) domain of nitrogen regulatory protein C 1 (NtrC1) from Aquifex ...
 636-703 5.62e-05

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: 43.34  E-value: 5.62e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1027852989 636 VLLADDDDVNRMVTKKLLEKLGCQVIAVSTGFQCLSAMGHSKTsiQVVILDLHMPEMDGFEVAIRVRK 703
Cdd:cd17572     1 VLLVEDSPSLAALYQEYLSDEGYKVTHVETGKEALAFLSDQPP--DVVLLDLKLPDMSGMEILKWIQE 66
REC_OmpR_VirG cd17594
phosphoacceptor receiver (REC) domain of VirG-like OmpR family response regulators; VirG is ...
 636-752 5.94e-05

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: 42.82  E-value: 5.94e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027852989 636 VLLADDDDVNRMVTKKLLEKLGCQVIAVSTGFQCLSAMGHSktSIQVVILDLHMPEMDGFEVAIRVRKfhSHGWPLIIAL 715
Cdd:cd17594     2 VLVVDDDAAMRHLLILYLRERGFDVTAAADGAEEARLMLHR--RVDLVLLDLRLGQESGLDLLRTIRA--RSDVPIIIIS 77

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1027852989 716 SATSEELVWDRCLQVGINGLIRKPVllqGMAEELQRV 752
Cdd:cd17594    78 GDRRDEIDRVVGLELGADDYLAKPF---GLRELLARV 111
REC_OmpR_BfmR-like cd19939
phosphoacceptor receiver (REC) domain of BfmR-like OmpR family response regulators; ...
 636-755 6.47e-05

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


Pssm-ID: 381166 [Multi-domain]  Cd Length: 116  Bit Score: 42.75  E-value: 6.47e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027852989 636 VLLADDDDVNRMVTKKLLEKLGCQVIAVSTGFQCLSAMghSKTSIQVVILDLHMPEMDGFEVAIRVRKFHSHGwplIIAL 715
Cdd:cd19939     2 ILIVEDELELARLTRDYLIKAGLEVSVFTDGQRAVRRI--IDEQPSLVVLDIMLPGMDGLTVCREVREHSHVP---ILML 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1027852989 716 SATSEELvwDRCL--QVGINGLIRKPVLLQGMAEELQRVLQR 755
Cdd:cd19939    77 TARTEEM--DRVLglEMGADDYLCKPFSPRELLARVRALLRR 116
HisKA pfam00512
His Kinase A (phospho-acceptor) domain; dimerization and phospho-acceptor domain of histidine ...
 367-433 1.04e-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: 41.04  E-value: 1.04e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1027852989 367 ARNSFQKVMNNGMRQPMHSVLGLLSILQDENfTSSNQRIIIDTMMRTSTVLSTLTNDAMDISEKDEG 433
Cdd:pfam00512   1 AKSEFLANLSHELRTPLTAIRGYLELLRDEK-LDEEQREYLETILRSAERLLRLINDLLDLSRIEAG 66
REC_PatA-like cd17602
phosphoacceptor receiver (REC) domain of PatA and similar domains; Nostoc sp. (or Anabaena sp.) ...
 640-739 1.50e-04

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: 41.59  E-value: 1.50e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027852989 640 DDDDVNRMVTKKLLEKLGCQVIAVSTGFQCLSAMGHSKTsiQVVILDLHMPEMDGFEVAIRVRKfHSH--GWPLIIalsA 717
Cdd:cd17602     5 DDRPSIQKMIEYFLEKQGFRVVVIDDPLRALTTLLNSKP--DLILIDIDMPDLDGYELCSLLRK-SSAlkDTPIIM---L 78

                          90       100
                  ....*....|....*....|....
gi 1027852989 718 TSEELVWDRCLQ--VGINGLIRKP 739
Cdd:cd17602    79 TGKDGLVDRIRAkmAGASGYLTKP 102
REC_OmpR_PhoB cd17618
phosphoacceptor receiver (REC) domain of PhoB response regulator from the OmpR family; The ...
 635-739 1.76e-04

phosphoacceptor receiver (REC) domain of PhoB response regulator from the OmpR family; The transcription factor PhoB is a component of the PhoR/PhoB two-component system, a key regulatory protein network that facilitates response to inorganic phosphate (Pi) starvation conditions by turning on the phosphate (pho) regulon whose products are involved in phosphorus uptake and metabolism. PhoB is a member of the OmpR family of DNA-binding response regulators that contains REC and winged helix-turn-helix (wHTH) DNA-binding output effector domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381133 [Multi-domain]  Cd Length: 118  Bit Score: 41.85  E-value: 1.76e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027852989 635 QVLLADDDDVNRMVTKKLLEKLGCQVIAVSTGFQCLSAMGHSKTSIqvVILDLHMPEMDGFEVAIRVRKFHSHGWPLIIA 714
Cdd:cd17618     2 TILIVEDEPAIREMIAFNLERAGFDVVEAEDAESAVNLIVEPRPDL--ILLDWMLPGGSGIQFIRRLKRDEMTRDIPIIM 79

                          90       100
                  ....*....|....*....|....*
gi 1027852989 715 LSATSEELVWDRCLQVGINGLIRKP 739
Cdd:cd17618    80 LTARGEEEDKVRGLEAGADDYITKP 104
REC_OmpR_NsrR-like cd18159
phosphoacceptor receiver (REC) domain of Streptococcus agalactiae NsrR-like OmpR family ...
 636-753 1.81e-04

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: 41.50  E-value: 1.81e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027852989 636 VLLADDDDVNRMVTKKLLEKLGCQVIAVSTGFQCLSAMGHSKTSiqVVILDLHMPEMDGFEVAIRVRKfHSHGwPlIIAL 715
Cdd:cd18159     1 ILIVEDDETIASLLKKHLEKWGYEVVLIEDFEDVLEEFLQFKPD--LVLLDINLPYFDGFYWCREIRQ-ISNV-P-IIFI 75

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1027852989 716 SATSEELVWDRCLQVGINGLIRKPVLLQGMAEELQRVL 753
Cdd:cd18159    76 SSRDDNMDQVMAINMGGDDYITKPFDLDVLLAKIKAIL 113
REC_RegA-like cd17563
phosphoacceptor receiver (REC) domain of photosynthetic apparatus regulatory protein RegA; ...
 636-697 3.16e-04

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


Pssm-ID: 381111 [Multi-domain]  Cd Length: 112  Bit Score: 40.89  E-value: 3.16e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1027852989 636 VLLADDDDVNRMVTKKLLEKLGCQVIAVSTGFQCLSAmgHSKTSIQVVILDLHMPEMDGFEV 697
Cdd:cd17563     3 LLLVDDDEVFAERLARALERRGFEVETAHSVEEALAL--AREEKPDYAVLDLRLGGDSGLDL 62
REC_OmpR_ChvI-like cd19936
phosphoacceptor receiver (REC) domain of ChvI-like OmpR family response regulators; ...
 636-739 3.78e-04

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: 40.12  E-value: 3.78e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027852989 636 VLLADDDDVNRMVTKKLLEKLGCQVIAVSTGFQCLSAMGHSKtsIQVVILDLHMPEMDGFEVAIRVRKFHShgWPlIIAL 715
Cdd:cd19936     1 IALVDDDRNILTSVSMALEAEGFSVETYTDGASALDGLNARP--PDLAILDIKMPRMDGMELLQRLRQKST--LP-VIFL 75

                          90       100
                  ....*....|....*....|....
gi 1027852989 716 SATSEELVWDRCLQVGINGLIRKP 739
Cdd:cd19936    76 TSKDDEIDEVFGLRMGADDYITKP 99
PRK11083 PRK11083
DNA-binding response regulator CreB; Provisional
 653-739 3.93e-04

DNA-binding response regulator CreB; Provisional


Pssm-ID: 236838 [Multi-domain]  Cd Length: 228  Bit Score: 42.64  E-value: 3.93e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027852989 653 LEKLGCQVIAVSTGFQCLSAMGHskTSIQVVILDLHMPEMDGFEVAIRVRKFHSHgWPlIIALSATSEELvwDRC--LQV 730
Cdd:PRK11083   23 LQSEGFTVEWFERGLPALDKLRQ--QPPDLVILDVGLPDISGFELCRQLLAFHPA-LP-VIFLTARSDEV--DRLvgLEI 96


                  ....*....
gi 1027852989 731 GINGLIRKP 739
Cdd:PRK11083   97 GADDYVAKP 105
PRK09935 PRK09935
fimbriae biosynthesis transcriptional regulator FimZ;
632-738 5.39e-04

fimbriae biosynthesis transcriptional regulator FimZ;


Pssm-ID: 182154 [Multi-domain]  Cd Length: 210  Bit Score: 42.17  E-value: 5.39e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027852989 632 KGLQVLLADDDDVNRMVTKKLLEKLGCQVIAVSTGfQCLSAMGHSKT-SIQVVILDLHMPEMDGFEVAIRVRKFHSHgwP 710
Cdd:PRK09935    2 KPASVIIMDTHPIIRMSIEVLLQKNSELQIVLKTD-DYRITIDYLRTrPVDLIIMDIDLPGTDGFTFLKRIKQIQST--V 78

                          90       100
                  ....*....|....*....|....*...
gi 1027852989 711 LIIALSATSEELVWDRCLQVGINGLIRK 738
Cdd:PRK09935   79 KVLFLSSKSECFYAGRAIQAGANGFVSK 106
REC_OmpR_kpRstA-like cd17622
phosphoacceptor receiver (REC) domain of kpRstA-like OmpR family response regulators; ...
 636-740 5.58e-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: 40.44  E-value: 5.58e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027852989 636 VLLADDDDVNRMVtKKLLEKLGCQVIAVSTGFQCLSAMGHSKTsiQVVILDLHMPEMDGFEVAIRVRKFHSHgwPlIIAL 715
Cdd:cd17622     4 LLVEDDPKLARLI-ADFLESHGFNVVVEHRGDRALEVIAREKP--DAVLLDIMLPGIDGLTLCRDLRPKYQG--P-ILLL 77

                          90       100
                  ....*....|....*....|....*
gi 1027852989 716 SATSEELVWDRCLQVGINGLIRKPV 740
Cdd:cd17622    78 TALDSDIDHILGLELGADDYVVKPV 102
REC_OmpR_ArcA_TorR-like cd17619
phosphoacceptor receiver (REC) domain of ArcA- and TorR-like OmpR family response regulators; ...
 636-739 7.83e-04

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: 39.68  E-value: 7.83e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027852989 636 VLLADDDDVNRMVTKKLLEKLGCQVIAVSTGFQCLSAMghSKTSIQVVILDLHMPEMDGFEVAirvRKFHSHGWPLIIAL 715
Cdd:cd17619     3 ILIVEDEPVTRATLKSYFEQEGYDVSEAGDGEEMRQIL--ARQDIDLVLLDINLPGKDGLSLT---RELREQSEVGIILV 77

                          90       100
                  ....*....|....*....|....*.
gi 1027852989 716 SATSEELvwDRC--LQVGINGLIRKP 739
Cdd:cd17619    78 TGRDDEV--DRIvgLEIGADDYVTKP 101
REC_OmpR_DrrD-like cd17625
phosphoacceptor receiver (REC) domain of DrrD-like OmpR family response regulators; DrrD is a ...
 637-703 8.89e-04

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: 39.51  E-value: 8.89e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1027852989 637 LLADDDDVNRMVTKKLLEKLGCQVIAVSTGFQCLSAMGhsKTSIQVVILDLHMPEMDGFEVAIRVRK 703
Cdd:cd17625     1 LVVEDEKDLSEAITKHLKKEGYTVDVCFDGEEGLEYAL--SGIYDLIILDIMLPGMDGLEVLKSLRE 65
PRK15115 PRK15115
response regulator GlrR; Provisional
 632-740 9.48e-04

response regulator GlrR; Provisional


Pssm-ID: 185070 [Multi-domain]  Cd Length: 444  Bit Score: 42.52  E-value: 9.48e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027852989 632 KGLQVLLADDDDVNRMVTKKLLEKLGCQVIAVSTGFQCLSAMGHSKtsIQVVILDLHMPEMDGFEVAIRVRKFHShGWPL 711
Cdd:PRK15115    4 KPAHLLLVDDDPGLLKLLGMRLTSEGYSVVTAESGQEALRVLNREK--VDLVISDLRMDEMDGMQLFAEIQKVQP-GMPV 80

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1027852989 712 II---------ALSATseelvwdrclQVGINGLIRKPV 740
Cdd:PRK15115   81 IIltahgsipdAVAAT----------QQGVFSFLTKPV 108
PRK10693 PRK10693
two-component system response regulator RssB;
664-740 1.40e-03

two-component system response regulator RssB;


Pssm-ID: 182652 [Multi-domain]  Cd Length: 303  Bit Score: 41.51  E-value: 1.40e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1027852989 664 STGFQCLSAMGHSKTSIqvVILDLHMPEMDGFEVairVRKFHSHGWPL-IIALSATSEELVWDRCLQVGINGLIRKPV 740
Cdd:PRK10693    4 ANGVDALELLGGFTPDL--IICDLAMPRMNGIEF---VEHLRNRGDQTpVLVISATENMADIAKALRLGVQDVLLKPV 76
REC_RcNtrC-like cd19928
phosphoacceptor receiver (REC) domain of Rhodobacter capsulatus nitrogen regulatory protein C ...
 636-703 1.41e-03

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: 38.64  E-value: 1.41e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1027852989 636 VLLADDDDVNRMVTKKLLEKLGCQVIAVSTGFQCLSAMGHSKTSIqvVILDLHMPEMDGFEVAIRVRK 703
Cdd:cd19928     1 ILVADDDRAIRTVLTQALGRAGYEVRTTGNAATLWRWVEEGEGDL--VITDVVMPDENGLDLIPRIKK 66
REC_NtrX-like cd17550
phosphoacceptor receiver (REC) domain of nitrogen assimilation regulatory protein NtrX and ...
 636-706 1.80e-03

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


Pssm-ID: 381102 [Multi-domain]  Cd Length: 115  Bit Score: 38.63  E-value: 1.80e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1027852989 636 VLLADDDDVNRMVTKKLLEKLGCQVIAVSTGFQCLSAMghSKTSIQVVILDLHMPEMDGFEVAIRVRKFHS 706
Cdd:cd17550     1 ILIVDDEEDIRESLSGILEDEGYEVDTAADGEEALKLI--KERRPDLVLLDIWLPDMDGLELLKEIKEKYP 69
pleD PRK09581
response regulator PleD; Reviewed
 636-702 2.02e-03

response regulator PleD; Reviewed


Pssm-ID: 236577 [Multi-domain]  Cd Length: 457  Bit Score: 41.42  E-value: 2.02e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1027852989 636 VLLADDDDVNRmvtkKLLE-KLGC---QVIAVSTGFQCLSAMghSKTSIQVVILDLHMPEMDGFEVAIRVR 702
Cdd:PRK09581    5 ILVVDDIPANV----KLLEaKLLAeyyTVLTASSGAEAIAIC--EREQPDIILLDVMMPGMDGFEVCRRLK 69
REC_GlnL-like cd17565
phosphoacceptor receiver (REC) domain of transcriptional regulatory protein GlnL and similar ...
 638-740 2.16e-03

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


Pssm-ID: 381112 [Multi-domain]  Cd Length: 103  Bit Score: 38.41  E-value: 2.16e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027852989 638 LADDDDVNRMVTKKLLEK--LGCQVIAVSTGFQclsAMGHSK-TSIQVVILDLHMPEMDGFEVAIRVRKFHSHgwPLIIA 714
Cdd:cd17565     3 IVDDDKNIIKILSDIIEDddLGEVVGEADNGAQ---AYDEILfLQPDIVLIDLLMPGMDGIQLVRKLKDTGSN--GKFIM 77

                          90       100
                  ....*....|....*....|....*.
gi 1027852989 715 LSATSEELVWDRCLQVGINGLIRKPV 740
Cdd:cd17565    78 ISQVSDKEMIGKAYQAGIEFFINKPI 103
REC_DesR-like cd19930
phosphoacceptor receiver (REC) domain of DesR and similar proteins; This group is composed of ...
 636-753 2.64e-03

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


Pssm-ID: 381157 [Multi-domain]  Cd Length: 117  Bit Score: 38.41  E-value: 2.64e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027852989 636 VLLADDDDVNRMVTKKLLE-KLGCQVIA-VSTGFQCLSAMghSKTSIQVVILDLHMPEMDGFEVAIRVRKFHSHGWPLII 713
Cdd:cd19930     1 VLIAEDQEMVRGALAALLElEDDLEVVAqASNGQEALRLV--LKHSPDVAILDIEMPGRTGLEVAAELREELPDTKVLIV 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1027852989 714 ALSATSEELvwDRCLQVGINGLIRKPVLLQGMAEELQRVL 753
Cdd:cd19930    79 TTFGRPGYF--RRALAAGVDGYVLKDRPIEELADAIRTVH 116
REC_OmpR_MtrA-like cd17626
phosphoacceptor receiver (REC) domain of MtrA-like OmpR family response regulators; MtrA is ...
 635-739 3.10e-03

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: 38.22  E-value: 3.10e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027852989 635 QVLLADDDD-VNRMVTKkLLEKLGCQVIAVSTGFQCLSAMGHSKTSIqvVILDLHMPEMDGFEVAIRVRKfhSHGWPlII 713
Cdd:cd17626     2 RILVVDDDAaLAEMIGI-VLRGEGFDPAFCGDGTQALAAFREVRPDL--VLLDLMLPGIDGIEVCRQIRA--ESGVP-IV 75

                          90       100
                  ....*....|....*....|....*.
gi 1027852989 714 ALSATSEELVWDRCLQVGINGLIRKP 739
Cdd:cd17626    76 MLTAKSDTVDVVLGLESGADDYVAKP 101
REC_Spo0F-like cd17553
phosphoacceptor receiver (REC) domain of Spo0F and similar domains; Spo0F, a stand-alone ...
 635-706 3.76e-03

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: 37.92  E-value: 3.76e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1027852989 635 QVLLADDDDVNRMVTKKLLEKLGCQVIAVSTGFQCLSAMghSKTSIQVVILDLHMPEMDGFEVAIRVRKFHS 706
Cdd:cd17553     2 KILIVDDQYGIRILLNEVFNKEGYQTFQAANGLQALDIV--TKERPDLVLLDMKIPGMDGIEILKRMKVIDE 71
PRK10529 PRK10529
DNA-binding transcriptional activator KdpE; Provisional
 636-752 3.95e-03

DNA-binding transcriptional activator KdpE; Provisional


Pssm-ID: 182522 [Multi-domain]  Cd Length: 225  Bit Score: 39.40  E-value: 3.95e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027852989 636 VLLADDDDVNRMVTKKLLEKLGCQVIAVSTGFQCLSAMGHSKTSIqvVILDLHMPEMDGFEVAIRVRKFHShgWPLIIaL 715
Cdd:PRK10529    4 VLIVEDEQAIRRFLRTALEGDGMRVFEAETLQRGLLEAATRKPDL--IILDLGLPDGDGIEFIRDLRQWSA--IPVIV-L 78

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1027852989 716 SATSEELVWDRCLQVGINGLIRKPVllqGMAEELQRV 752
Cdd:PRK10529   79 SARSEESDKIAALDAGADDYLSKPF---GIGELQARL 112
REC_OmpR_BaeR-like cd19938
phosphoacceptor receiver (REC) domain of BaeR-like OmpR family response regulators; BaeR is ...
 635-739 4.77e-03

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


Pssm-ID: 381165 [Multi-domain]  Cd Length: 114  Bit Score: 37.36  E-value: 4.77e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027852989 635 QVLLADDDDVNRMVTKKLLEKLGCQVIAVSTGFQCLSAMGHskTSIQVVILDLHMPEMDGFEVAIRVRKFHShgWPlIIA 714
Cdd:cd19938     1 RILIVEDEPKLAQLLIDYLRAAGYAPTLLAHGDQVLPYVRH--TPPDLILLDLMLPGTDGLTLCREIRRFSD--VP-IIM 75

                          90       100
                  ....*....|....*....|....*..
gi 1027852989 715 LSATSEELvwDRC--LQVGINGLIRKP 739
Cdd:cd19938    76 VTARVEEI--DRLlgLELGADDYICKP 100
ompR PRK09468
osmolarity response regulator; Provisional
 636-739 5.58e-03

osmolarity response regulator; Provisional


Pssm-ID: 181883 [Multi-domain]  Cd Length: 239  Bit Score: 39.19  E-value: 5.58e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027852989 636 VLLADDDDVNRMVTKKLLEKLGCQVIAVSTGFQCLSAMghSKTSIQVVILDLHMPEMDGFEVAIRVRKFHSHgWPlIIAL 715
Cdd:PRK09468    8 ILVVDDDMRLRALLERYLTEQGFQVRSAANAEQMDRLL--TRESFHLMVLDLMLPGEDGLSICRRLRSQNNP-TP-IIML 83

                          90       100
                  ....*....|....*....|....*.
gi 1027852989 716 SATSEELvwDRC--LQVGINGLIRKP 739
Cdd:PRK09468   84 TAKGEEV--DRIvgLEIGADDYLPKP 107
 
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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