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Conserved domains on  [gi|1823315871|gb|QIP30589|]
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response regulator [Deinococcus radiodurans]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
CheA COG0643
Chemotaxis protein histidine kinase CheA [Signal transduction mechanisms];
187-801 2.28e-128

Chemotaxis protein histidine kinase CheA [Signal transduction mechanisms];


:

Pssm-ID: 440408 [Multi-domain]  Cd Length: 563  Bit Score: 399.17  E-value: 2.28e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823315871 187 DNAEVWEYFAPEVHEHLASLREQL----GRGEDAD-LQVMFRAAHTIKGSAYMVGLPPLGDFAHGMEDLLGAAREGAVSL 261
Cdd:COG0643     2 DMDELLEIFLEEARELLEQLEEGLlaleQDPDDPElLNAIFRAAHTLKGSAGMLGLDALAELAHALEDLLDALRNGELAL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823315871 262 SSDVRGLLAEATDTIGDLLTVAAG-----ADGAALPAQLTAVTARLRSAHSGEQTPVPPM----------SAAAPVVAPV 326
Cdd:COG0643    82 TPELIDLLLEALDALRALLDALEAggeppADISALLARLDASEEAIEEVVADEVEISPPApaalepapaaAPPAEAAAAA 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823315871 327 PAPAPAAATSIRVPAARLEGLMDQLGELVTARARMTQLLSRLDElqgsmtasqerfqrtvrdfeerylnpdmvreegaap 406
Cdd:COG0643   162 AEAAAAASETVRVDVERLDRLMNLVGELVITRARLEQLAEELED------------------------------------ 205
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823315871 407 ttrmggldlsqqfaelefdtyndlnilsrsitelsadfaevrrrlsDTAAELSEENEQLGKLVRRLRLDVNQTSRVAFSQ 486
Cdd:COG0643   206 ----------------------------------------------ESLRELEEALEQLSRLTRELQDGVMRLRMVPIST 239
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823315871 487 TTARLRRW----AREQQADLTLQVEGEDVLIESGILQRISDPLLHLLTNAAYHGLasESAESRRAAGKNPQGTVWIRAAE 562
Cdd:COG0643   240 VFNRFPRMvrdlARELGKEVELVIEGEETELDRTVLERLGDPLVHLVRNAVDHGI--ETPEERLAAGKPETGTITLSAYH 317
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823315871 563 QGNFLEVTVADDGQGLDYARIRERALERGLRSAQELEQLSSDELGRLILLPGFSTAREVGNVAGRGVGLDVVATAVRQLG 642
Cdd:COG0643   318 EGGRVVIEVSDDGRGLDLEKIRAKAIEKGLITAEEAAALSDEELLELIFAPGFSTAEEVTDLSGRGVGMDVVKTNIEALG 397
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823315871 643 GELLISSERGVGTAFTLRVPTTQRIMDVLHLDLGaGHHAALPVGSVRSLRDVPLGDLRRDDGQLWLDFGGQPVPVVDARP 722
Cdd:COG0643   398 GTIEIESEPGKGTTFTLRLPLTLAIIDGLLVRVG-GETYAIPLSSVEEVLRLDPDDIETVEGREVIRLRGELLPLVRLGE 476
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823315871 723 IWGHAPQDTDTE-AHLAVVSSISGLLALRVHDFGDIEEVAVTAPSGLLAPLDYLAGMAVSGTGQVLAILDPAGVLRLSRR 801
Cdd:COG0643   477 LLGLPGAEPEGErGPVVVVRSGGRRVALVVDELLGQQEVVIKPLGPLLRRVPGISGATILGDGRVALILDVAALVRSARA 556
CheY COG0784
CheY-like REC (receiver) domain, includes chemotaxis protein CheY and sporulation regulator ...
817-942 3.85e-35

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: 129.97  E-value: 3.85e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823315871 817 GNQRLLLVDDSLSVRRLVGRMLERGGYQVVTASDGQEALDLLQQDaDFGAVVTDLEMPRVNGYELLSAVRARPATAGLPM 896
Cdd:COG0784     4 GGKRILVVDDNPDNRELLRRLLERLGYEVTTAEDGAEALELLRAG-PPDLILLDINMPGMDGLELLRRIRALPRLPDIPI 82
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1823315871 897 LVMTTRAGEKHQRLAFQLGADDYFTKPVNEALLLRRLGTLQQAQQA 942
Cdd:COG0784    83 IALTAYADEEDRERALEAGADDYLTKPVDPEELLEALRRLLARASA 128
HPT cd00088
Histidine Phosphotransfer domain, involved in signalling through a two part component systems ...
6-109 9.57e-05

Histidine Phosphotransfer domain, involved in signalling through a two part component systems in which an autophosphorylating histidine protein kinase serves as a phosphoryl donor to a response regulator protein; the response regulator protein is modulated by phosphorylation and dephosphorylation of a conserved aspartic acid residue; two-component proteins are abundant in most eubacteria; In E. coli there are 62 two-component proteins involved in a variety of processes such as chemotaxis, osmoregulation, metabolism and transport 1; also present in both Gram positive and Gram negative pathogenic bacteria where they regulate basic housekeeping functions and control expression of toxins and other proteins important for pathogenesis; in archaea and eukaryotes, two-component pathways constitute a very small number of all signaling systems; in fungi they mediate environmental stress responses and, in pathogenic yeast, hyphal development. In Dictyostelium and in plants, they are involved in important processes such as osmoregulation, cell growth, and differentiation; to date two-component proteins have not been identified in animals; in most prokaryotic systems, the output response is effected directly by the RR, which functions as a transcription factor while in eukaryotic systems, two-component proteins are found at the beginning of signaling pathways where they interface with more conventional eukaryotic signaling strategies such as MAP kinase and cyclic nucleotide cascades


:

Pssm-ID: 238041 [Multi-domain]  Cd Length: 94  Bit Score: 41.98  E-value: 9.57e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823315871   6 SELLESFREEAAEVLSGLEEGVTGLRTlsgaaghahdtpelAAHLGDLSVLAHRLRGSAALYGYAQLSTLASLQERLLDA 85
Cdd:cd00088     2 EELLELFLEEAEELLEELERALLELED--------------AEDLNEIFRAAHTLKGSAASLGLQRLAQLAHQLEDLLDA 67
                          90       100
                  ....*....|....*....|....*..
gi 1823315871  86 ---RPQLDREQHQEFLTLLEQVNAALR 109
Cdd:cd00088    68 lrdGLEVTPELIDLLLDALDALKAELE 94
 
Name Accession Description Interval E-value
CheA COG0643
Chemotaxis protein histidine kinase CheA [Signal transduction mechanisms];
187-801 2.28e-128

Chemotaxis protein histidine kinase CheA [Signal transduction mechanisms];


Pssm-ID: 440408 [Multi-domain]  Cd Length: 563  Bit Score: 399.17  E-value: 2.28e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823315871 187 DNAEVWEYFAPEVHEHLASLREQL----GRGEDAD-LQVMFRAAHTIKGSAYMVGLPPLGDFAHGMEDLLGAAREGAVSL 261
Cdd:COG0643     2 DMDELLEIFLEEARELLEQLEEGLlaleQDPDDPElLNAIFRAAHTLKGSAGMLGLDALAELAHALEDLLDALRNGELAL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823315871 262 SSDVRGLLAEATDTIGDLLTVAAG-----ADGAALPAQLTAVTARLRSAHSGEQTPVPPM----------SAAAPVVAPV 326
Cdd:COG0643    82 TPELIDLLLEALDALRALLDALEAggeppADISALLARLDASEEAIEEVVADEVEISPPApaalepapaaAPPAEAAAAA 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823315871 327 PAPAPAAATSIRVPAARLEGLMDQLGELVTARARMTQLLSRLDElqgsmtasqerfqrtvrdfeerylnpdmvreegaap 406
Cdd:COG0643   162 AEAAAAASETVRVDVERLDRLMNLVGELVITRARLEQLAEELED------------------------------------ 205
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823315871 407 ttrmggldlsqqfaelefdtyndlnilsrsitelsadfaevrrrlsDTAAELSEENEQLGKLVRRLRLDVNQTSRVAFSQ 486
Cdd:COG0643   206 ----------------------------------------------ESLRELEEALEQLSRLTRELQDGVMRLRMVPIST 239
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823315871 487 TTARLRRW----AREQQADLTLQVEGEDVLIESGILQRISDPLLHLLTNAAYHGLasESAESRRAAGKNPQGTVWIRAAE 562
Cdd:COG0643   240 VFNRFPRMvrdlARELGKEVELVIEGEETELDRTVLERLGDPLVHLVRNAVDHGI--ETPEERLAAGKPETGTITLSAYH 317
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823315871 563 QGNFLEVTVADDGQGLDYARIRERALERGLRSAQELEQLSSDELGRLILLPGFSTAREVGNVAGRGVGLDVVATAVRQLG 642
Cdd:COG0643   318 EGGRVVIEVSDDGRGLDLEKIRAKAIEKGLITAEEAAALSDEELLELIFAPGFSTAEEVTDLSGRGVGMDVVKTNIEALG 397
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823315871 643 GELLISSERGVGTAFTLRVPTTQRIMDVLHLDLGaGHHAALPVGSVRSLRDVPLGDLRRDDGQLWLDFGGQPVPVVDARP 722
Cdd:COG0643   398 GTIEIESEPGKGTTFTLRLPLTLAIIDGLLVRVG-GETYAIPLSSVEEVLRLDPDDIETVEGREVIRLRGELLPLVRLGE 476
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823315871 723 IWGHAPQDTDTE-AHLAVVSSISGLLALRVHDFGDIEEVAVTAPSGLLAPLDYLAGMAVSGTGQVLAILDPAGVLRLSRR 801
Cdd:COG0643   477 LLGLPGAEPEGErGPVVVVRSGGRRVALVVDELLGQQEVVIKPLGPLLRRVPGISGATILGDGRVALILDVAALVRSARA 556
HATPase_CheA-like cd16916
Histidine kinase-like ATPase domain of the chemotaxis protein histidine kinase CheA, and some ...
483-662 1.84e-77

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


Pssm-ID: 340393 [Multi-domain]  Cd Length: 178  Bit Score: 250.19  E-value: 1.84e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823315871 483 AFSQTTARLRRWAREQQADLTLQVEGEDVLIESGILQRISDPLLHLLTNAAYHGLasESAESRRAAGKNPQGTVWIRAAE 562
Cdd:cd16916     1 VFSRFPRLVRDLARELGKQVELVVEGEDTELDKSVLEKLADPLTHLLRNAVDHGI--EAPEERLAAGKPPEGTITLRAEH 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823315871 563 QGNFLEVTVADDGQGLDYARIRERALERGLRSAQELEQLSSDELGRLILLPGFSTAREVGNVAGRGVGLDVVATAVRQLG 642
Cdd:cd16916    79 QGNQVVIEVSDDGRGIDREKIREKAIERGLITADEAATLSDDEVLNLIFAPGFSTAEQVTDVSGRGVGMDVVKRSIESLG 158
                         170       180
                  ....*....|....*....|
gi 1823315871 643 GELLISSERGVGTAFTLRVP 662
Cdd:cd16916   159 GTIEVESEPGQGTTFTIRLP 178
CheY COG0784
CheY-like REC (receiver) domain, includes chemotaxis protein CheY and sporulation regulator ...
817-942 3.85e-35

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: 129.97  E-value: 3.85e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823315871 817 GNQRLLLVDDSLSVRRLVGRMLERGGYQVVTASDGQEALDLLQQDaDFGAVVTDLEMPRVNGYELLSAVRARPATAGLPM 896
Cdd:COG0784     4 GGKRILVVDDNPDNRELLRRLLERLGYEVTTAEDGAEALELLRAG-PPDLILLDINMPGMDGLELLRRIRALPRLPDIPI 82
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1823315871 897 LVMTTRAGEKHQRLAFQLGADDYFTKPVNEALLLRRLGTLQQAQQA 942
Cdd:COG0784    83 IALTAYADEEDRERALEAGADDYLTKPVDPEELLEALRRLLARASA 128
PRK10547 PRK10547
chemotaxis protein CheA; Provisional
218-669 5.43e-33

chemotaxis protein CheA; Provisional


Pssm-ID: 236712 [Multi-domain]  Cd Length: 670  Bit Score: 136.40  E-value: 5.43e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823315871 218 LQVMFRAAHTIKGSAYMVGLPPLGDFAHGMEDLLGAAREGAVSLSSDVRGLLAEATDTIGDLLTV---AAGADGAALP-- 292
Cdd:PRK10547   38 LNAIFRAAHSIKGGAGTFGFTVLQETTHLMENLLDEARRGEMQLNTDIINLFLETKDIMQEQLDAyktSQEPDAASFEyi 117
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823315871 293 ----AQLTavtarLRSAHSGEQTPVPPMSAAAPVVAPVPAPAPAAATSIRVPAARLEG-----LMDQLGELVTararMTQ 363
Cdd:PRK10547  118 cqalRQLA-----LEAKGETPSAVTRLSVVAIQEKSEPQDESPRSQSGLRIILSRLKAgevdlLEEELGNLGT----LTD 188
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823315871 364 LLSRLDELQGSM--TASQERFQrTVRDFeerYLNPDMVR-EEGAAPTTRMGGLDLSQQFAELEFDTYNDLNILSRSITEL 440
Cdd:PRK10547  189 VVKGADSLEATLpgSVAEDDIT-AVLCF---VIEADQITfETAVAAPQEKAEETTEVVEVSPKISVPPVLKLAAEQAPAG 264
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823315871 441 SADFAEVRRRLSDTAAELS-EENEQL----GKLV--------RRLRLD----------VNQTSRVA-------------- 483
Cdd:PRK10547  265 RVEREKTARSSESTSIRVAvEKVDQLinlvGELVitqsmlaqRSSELDpvnhgdlitsMGQLQRNArdlqesvmsirmmp 344
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823315871 484 ----FSqttaRLRRWAREQQADLTLQVE----GEDVLIESGILQRISDPLLHLLTNAAYHGLasESAESRRAAGKNPQGT 555
Cdd:PRK10547  345 meyvFS----RFPRLVRDLAGKLGKQVEltlvGSSTELDKSLIERIIDPLTHLVRNSLDHGI--ELPEKRLAAGKNSVGN 418
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823315871 556 VWIRAAEQGNFLEVTVADDGQGLDYARIRERALERGLRSAqelEQLSSDELGRLILLPGFSTAREVGNVAGRGVGLDVVA 635
Cdd:PRK10547  419 LILSAEHQGGNICIEVTDDGAGLNRERILAKAASQGLAVS---ENMSDEEVGMLIFAPGFSTAEQVTDVSGRGVGMDVVK 495
                         490       500       510
                  ....*....|....*....|....*....|....
gi 1823315871 636 TAVRQLGGELLISSERGVGTAFTLRVPTTQRIMD 669
Cdd:PRK10547  496 RNIQEMGGHVEIQSKQGKGTTIRILLPLTLAILD 529
REC cd00156
phosphoacceptor receiver (REC) domain of response regulators (RRs) and pseudo response ...
822-923 1.18e-28

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: 110.39  E-value: 1.18e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823315871 822 LLVDDSLSVRRLVGRMLERGGYQVVTASDGQEALDLLQQDaDFGAVVTDLEMPRVNGYELLSAVRARPatAGLPMLVMTT 901
Cdd:cd00156     1 LIVDDDPAIRELLKSLLEREGYEVDTAADGEEALELLREE-RPDLVLLDLMMPGMDGLELLRKLRELP--PDIPVIVLTA 77
                          90       100
                  ....*....|....*....|..
gi 1823315871 902 RAGEKHQRLAFQLGADDYFTKP 923
Cdd:cd00156    78 KADEEDAVRALELGADDYLVKP 99
Response_reg pfam00072
Response regulator receiver domain; This domain receives the signal from the sensor partner in ...
822-933 4.06e-24

Response regulator receiver domain; This domain receives the signal from the sensor partner in bacterial two-component systems. It is usually found N-terminal to a DNA binding effector domain.


Pssm-ID: 395025 [Multi-domain]  Cd Length: 111  Bit Score: 97.99  E-value: 4.06e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823315871 822 LLVDDSLSVRRLVGRMLERGGYQVVTASDGQEALDLLQQDaDFGAVVTDLEMPRVNGYELLSAVRARPATagLPMLVMTT 901
Cdd:pfam00072   2 LIVDDDPLIRELLRQLLEKEGYVVAEADDGKEALELLKEE-RPDLILLDINMPGMDGLELLKRIRRRDPT--TPVIILTA 78
                          90       100       110
                  ....*....|....*....|....*....|..
gi 1823315871 902 RAGEKHQRLAFQLGADDYFTKPVNEALLLRRL 933
Cdd:pfam00072  79 HGDEDDAVEALEAGADDFLSKPFDPDELLAAI 110
PRK10610 PRK10610
chemotaxis protein CheY;
815-936 8.13e-18

chemotaxis protein CheY;


Pssm-ID: 170568 [Multi-domain]  Cd Length: 129  Bit Score: 80.40  E-value: 8.13e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823315871 815 ATGNQRLLLVDDSLSVRRLVGRMLERGGYQ-VVTASDGQEALDLLQQdADFGAVVTDLEMPRVNGYELLSAVRARPATAG 893
Cdd:PRK10610    2 ADKELKFLVVDDFSTMRRIVRNLLKELGFNnVEEAEDGVDALNKLQA-GGFGFVISDWNMPNMDGLELLKTIRADGAMSA 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1823315871 894 LPMLVMTTRAGEKHQRLAFQLGADDYFTKPVNEALLLRRLGTL 936
Cdd:PRK10610   81 LPVLMVTAEAKKENIIAAAQAGASGYVVKPFTAATLEEKLNKI 123
HATPase_c smart00387
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.
523-662 1.69e-16

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


Pssm-ID: 214643 [Multi-domain]  Cd Length: 111  Bit Score: 76.15  E-value: 1.69e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823315871  523 DPLLHLLTNAAYHGLasesaesrRAAGknPQGTVWIRAAEQGNFLEVTVADDGQGLDyarireralerglrsaqeleqls 602
Cdd:smart00387   4 DRLRQVLSNLLDNAI--------KYTP--EGGRITVTLERDGDHVEITVEDNGPGIP----------------------- 50
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823315871  603 sDELGRLILLPGFSTAREVGNVAGRGVGLDVVATAVRQLGGELLISSERGVGTAFTLRVP 662
Cdd:smart00387  51 -PEDLEKIFEPFFRTDKRSRKIGGTGLGLSIVKKLVELHGGEISVESEPGGGTTFTITLP 109
REC smart00448
cheY-homologous receiver domain; CheY regulates the clockwise rotation of E. coli flagellar ...
820-874 5.37e-13

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: 64.13  E-value: 5.37e-13
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1823315871  820 RLLLVDDSLSVRRLVGRMLERGGYQVVTASDGQEALDLLQQDaDFGAVVTDLEMP 874
Cdd:smart00448   2 RILVVDDDPLLRELLKALLEKEGYEVDEATDGEEALELLKEE-KPDLILLDIMMP 55
resp_reg_YycF NF040534
response regulator YycF;
819-944 4.35e-11

response regulator YycF;


Pssm-ID: 439744 [Multi-domain]  Cd Length: 231  Bit Score: 63.97  E-value: 4.35e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823315871 819 QRLLLVDDSLSVRRLVGRMLERGGYQVVTASDGQEALDL-LQQDADFgaVVTDLEMPRVNGYELLSAVRArpaTAGLPML 897
Cdd:NF040534    1 KKILVVDDEKPIADILEFNLKKEGYEVFCAYDGNEALELvEEEVPDL--VLLDIMLPGRDGMEVCREVRK---KYDMPII 75
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1823315871 898 VMTTRAGEKHQRLAFQLGADDYFTKPV-NEALLLRRLGTLQQAQQAGV 944
Cdd:NF040534   76 MLTAKDSEIDKVLGLELGADDYVTKPFsTRELIARVKANLRRHQQQNT 123
HATPase_c pfam02518
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the ...
518-665 9.58e-11

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


Pssm-ID: 460579 [Multi-domain]  Cd Length: 109  Bit Score: 59.69  E-value: 9.58e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823315871 518 LQRIsdpLLHLLTNAAyhglasesaesrRAAGKNPQGTVWIraaEQGNFLEVTVADDGQGLDYARIREralerglrsaqe 597
Cdd:pfam02518   6 LRQV---LSNLLDNAL------------KHAAKAGEITVTL---SEGGELTLTVEDNGIGIPPEDLPR------------ 55
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1823315871 598 leqlssdelgrliLLPGFSTAREVGnVAGRGVGLDVVATAVRQLGGELLISSERGVGTAFTLRVPTTQ 665
Cdd:pfam02518  56 -------------IFEPFSTADKRG-GGGTGLGLSIVRKLVELLGGTITVESEPGGGTTVTLTLPLAQ 109
HPT cd00088
Histidine Phosphotransfer domain, involved in signalling through a two part component systems ...
6-109 9.57e-05

Histidine Phosphotransfer domain, involved in signalling through a two part component systems in which an autophosphorylating histidine protein kinase serves as a phosphoryl donor to a response regulator protein; the response regulator protein is modulated by phosphorylation and dephosphorylation of a conserved aspartic acid residue; two-component proteins are abundant in most eubacteria; In E. coli there are 62 two-component proteins involved in a variety of processes such as chemotaxis, osmoregulation, metabolism and transport 1; also present in both Gram positive and Gram negative pathogenic bacteria where they regulate basic housekeeping functions and control expression of toxins and other proteins important for pathogenesis; in archaea and eukaryotes, two-component pathways constitute a very small number of all signaling systems; in fungi they mediate environmental stress responses and, in pathogenic yeast, hyphal development. In Dictyostelium and in plants, they are involved in important processes such as osmoregulation, cell growth, and differentiation; to date two-component proteins have not been identified in animals; in most prokaryotic systems, the output response is effected directly by the RR, which functions as a transcription factor while in eukaryotic systems, two-component proteins are found at the beginning of signaling pathways where they interface with more conventional eukaryotic signaling strategies such as MAP kinase and cyclic nucleotide cascades


Pssm-ID: 238041 [Multi-domain]  Cd Length: 94  Bit Score: 41.98  E-value: 9.57e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823315871   6 SELLESFREEAAEVLSGLEEGVTGLRTlsgaaghahdtpelAAHLGDLSVLAHRLRGSAALYGYAQLSTLASLQERLLDA 85
Cdd:cd00088     2 EELLELFLEEAEELLEELERALLELED--------------AEDLNEIFRAAHTLKGSAASLGLQRLAQLAHQLEDLLDA 67
                          90       100
                  ....*....|....*....|....*..
gi 1823315871  86 ---RPQLDREQHQEFLTLLEQVNAALR 109
Cdd:cd00088    68 lrdGLEVTPELIDLLLDALDALKAELE 94
HPT smart00073
Histidine Phosphotransfer domain; Contains an active histidine residue that mediates ...
7-109 9.46e-04

Histidine Phosphotransfer domain; Contains an active histidine residue that mediates phosphotransfer reactions. Domain detected only in eubacteria. This alignment is an extension to that shown in the Cell structure paper.


Pssm-ID: 197502 [Multi-domain]  Cd Length: 92  Bit Score: 39.15  E-value: 9.46e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823315871    7 ELLESFREEAAEVLSGLEEGVtglrtlsGAAGHAHDtpelAAHLGDLSVLAHRLRGSAALYGYAQLSTLASLQERLLDAR 86
Cdd:smart00073   1 GGLELFREELAEFLQSLEEGL-------LELEKALD----AQDVNEIFRAAHTLKGSAGSLGLQQLAQLCHQLENLLDAL 69
                           90       100
                   ....*....|....*....|...
gi 1823315871   87 PQLDREQHQEFLTLLEQVNAALR 109
Cdd:smart00073  70 RSGEVELTPDLLDLLLELVDVLK 92
Hpt pfam01627
Hpt domain; The histidine-containing phosphotransfer (HPt) domain is a novel protein module ...
7-107 1.07e-03

Hpt domain; The histidine-containing phosphotransfer (HPt) domain is a novel protein module with an active histidine residue that mediates phosphotransfer reactions in the two-component signaling systems. A multistep phosphorelay involving the HPt domain has been suggested for these signaling pathways. The crystal structure of the HPt domain of the anaerobic sensor kinase ArcB has been determined. The domain consists of six alpha helices containing a four-helix bundle-folding. The pattern of sequence similarity of the HPt domains of ArcB and components in other signaling systems can be interpreted in light of the three-dimensional structure and supports the conclusion that the HPt domains have a common structural motif both in prokaryotes and eukaryotes. In S. cerevisiae ypd1p this domain has been shown to contain a binding surface for Ssk1p (response regulator receiver domain containing protein pfam00072).


Pssm-ID: 426352 [Multi-domain]  Cd Length: 84  Bit Score: 38.87  E-value: 1.07e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823315871   7 ELLESFREEAAEVLSGLEEgvtglrtlsgaAGHAHDTPELAAHlgdlsvlAHRLRGSAALYGYAQLSTLA-SLQERLLDA 85
Cdd:pfam01627   1 ELLELFLEEAPELLEQLEQ-----------ALDAEDLEALFRA-------AHTLKGSAGSLGLPALAELAhELEDLLREG 62
                          90       100
                  ....*....|....*....|..
gi 1823315871  86 RPQLDREQHQEFLTLLEQVNAA 107
Cdd:pfam01627  63 ELPLDPELLEALRDLLEALRAA 84
PEP_resp_reg TIGR02915
PEP-CTERM-box response regulator transcription factor; Members of this protein family share ...
821-929 5.41e-03

PEP-CTERM-box response regulator transcription factor; Members of this protein family share full-length homology with (but do not include) the acetoacetate metabolism regulatory protein AtoC (see SP|Q06065). These proteins have a Fis family DNA binding sequence (pfam02954), a response regulator receiver domain (pfam00072), and sigma-54 interaction domain (pfam00158). [Regulatory functions, DNA interactions]


Pssm-ID: 274348 [Multi-domain]  Cd Length: 445  Bit Score: 40.50  E-value: 5.41e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823315871 821 LLLVDDSLSVRRLVGRMLErgGYQVVTASDGQEALDLLQQDADfgAVVT-DLEMP-----RVNGYELLSAV-RARPATAg 893
Cdd:TIGR02915   1 LLIVEDDLGLQKQLKWSFA--DYELAVAADRESAIALVRRHEP--AVVTlDLGLPpdadgASEGLAALQQIlAIAPDTK- 75
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1823315871 894 lpMLVMTTRAGEKHQRLAFQLGADDYFTKPVNEALL 929
Cdd:TIGR02915  76 --VIVITGNDDRENAVKAIGLGAYDFYQKPIDPDVL 109
 
Name Accession Description Interval E-value
CheA COG0643
Chemotaxis protein histidine kinase CheA [Signal transduction mechanisms];
187-801 2.28e-128

Chemotaxis protein histidine kinase CheA [Signal transduction mechanisms];


Pssm-ID: 440408 [Multi-domain]  Cd Length: 563  Bit Score: 399.17  E-value: 2.28e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823315871 187 DNAEVWEYFAPEVHEHLASLREQL----GRGEDAD-LQVMFRAAHTIKGSAYMVGLPPLGDFAHGMEDLLGAAREGAVSL 261
Cdd:COG0643     2 DMDELLEIFLEEARELLEQLEEGLlaleQDPDDPElLNAIFRAAHTLKGSAGMLGLDALAELAHALEDLLDALRNGELAL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823315871 262 SSDVRGLLAEATDTIGDLLTVAAG-----ADGAALPAQLTAVTARLRSAHSGEQTPVPPM----------SAAAPVVAPV 326
Cdd:COG0643    82 TPELIDLLLEALDALRALLDALEAggeppADISALLARLDASEEAIEEVVADEVEISPPApaalepapaaAPPAEAAAAA 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823315871 327 PAPAPAAATSIRVPAARLEGLMDQLGELVTARARMTQLLSRLDElqgsmtasqerfqrtvrdfeerylnpdmvreegaap 406
Cdd:COG0643   162 AEAAAAASETVRVDVERLDRLMNLVGELVITRARLEQLAEELED------------------------------------ 205
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823315871 407 ttrmggldlsqqfaelefdtyndlnilsrsitelsadfaevrrrlsDTAAELSEENEQLGKLVRRLRLDVNQTSRVAFSQ 486
Cdd:COG0643   206 ----------------------------------------------ESLRELEEALEQLSRLTRELQDGVMRLRMVPIST 239
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823315871 487 TTARLRRW----AREQQADLTLQVEGEDVLIESGILQRISDPLLHLLTNAAYHGLasESAESRRAAGKNPQGTVWIRAAE 562
Cdd:COG0643   240 VFNRFPRMvrdlARELGKEVELVIEGEETELDRTVLERLGDPLVHLVRNAVDHGI--ETPEERLAAGKPETGTITLSAYH 317
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823315871 563 QGNFLEVTVADDGQGLDYARIRERALERGLRSAQELEQLSSDELGRLILLPGFSTAREVGNVAGRGVGLDVVATAVRQLG 642
Cdd:COG0643   318 EGGRVVIEVSDDGRGLDLEKIRAKAIEKGLITAEEAAALSDEELLELIFAPGFSTAEEVTDLSGRGVGMDVVKTNIEALG 397
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823315871 643 GELLISSERGVGTAFTLRVPTTQRIMDVLHLDLGaGHHAALPVGSVRSLRDVPLGDLRRDDGQLWLDFGGQPVPVVDARP 722
Cdd:COG0643   398 GTIEIESEPGKGTTFTLRLPLTLAIIDGLLVRVG-GETYAIPLSSVEEVLRLDPDDIETVEGREVIRLRGELLPLVRLGE 476
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823315871 723 IWGHAPQDTDTE-AHLAVVSSISGLLALRVHDFGDIEEVAVTAPSGLLAPLDYLAGMAVSGTGQVLAILDPAGVLRLSRR 801
Cdd:COG0643   477 LLGLPGAEPEGErGPVVVVRSGGRRVALVVDELLGQQEVVIKPLGPLLRRVPGISGATILGDGRVALILDVAALVRSARA 556
HATPase_CheA-like cd16916
Histidine kinase-like ATPase domain of the chemotaxis protein histidine kinase CheA, and some ...
483-662 1.84e-77

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


Pssm-ID: 340393 [Multi-domain]  Cd Length: 178  Bit Score: 250.19  E-value: 1.84e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823315871 483 AFSQTTARLRRWAREQQADLTLQVEGEDVLIESGILQRISDPLLHLLTNAAYHGLasESAESRRAAGKNPQGTVWIRAAE 562
Cdd:cd16916     1 VFSRFPRLVRDLARELGKQVELVVEGEDTELDKSVLEKLADPLTHLLRNAVDHGI--EAPEERLAAGKPPEGTITLRAEH 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823315871 563 QGNFLEVTVADDGQGLDYARIRERALERGLRSAQELEQLSSDELGRLILLPGFSTAREVGNVAGRGVGLDVVATAVRQLG 642
Cdd:cd16916    79 QGNQVVIEVSDDGRGIDREKIREKAIERGLITADEAATLSDDEVLNLIFAPGFSTAEQVTDVSGRGVGMDVVKRSIESLG 158
                         170       180
                  ....*....|....*....|
gi 1823315871 643 GELLISSERGVGTAFTLRVP 662
Cdd:cd16916   159 GTIEVESEPGQGTTFTIRLP 178
CheY COG0784
CheY-like REC (receiver) domain, includes chemotaxis protein CheY and sporulation regulator ...
817-942 3.85e-35

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: 129.97  E-value: 3.85e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823315871 817 GNQRLLLVDDSLSVRRLVGRMLERGGYQVVTASDGQEALDLLQQDaDFGAVVTDLEMPRVNGYELLSAVRARPATAGLPM 896
Cdd:COG0784     4 GGKRILVVDDNPDNRELLRRLLERLGYEVTTAEDGAEALELLRAG-PPDLILLDINMPGMDGLELLRRIRALPRLPDIPI 82
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1823315871 897 LVMTTRAGEKHQRLAFQLGADDYFTKPVNEALLLRRLGTLQQAQQA 942
Cdd:COG0784    83 IALTAYADEEDRERALEAGADDYLTKPVDPEELLEALRRLLARASA 128
PleD COG3706
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate ...
820-936 5.64e-35

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: 131.57  E-value: 5.64e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823315871 820 RLLLVDDSLSVRRLVGRMLERGGYQVVTASDGQEALDLLQQDaDFGAVVTDLEMPRVNGYELLSAVRARPATAGLPMLVM 899
Cdd:COG3706     3 RILVVDDDPTNRKLLRRLLEAAGYEVVEAADGEEALELLQEH-RPDLILLDLEMPDMDGLELCRRLRADPRTADIPIIFL 81
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1823315871 900 TTRAGEKHQRLAFQLGADDYFTKPVNEALLLRRLGTL 936
Cdd:COG3706    82 TALDDEEDRARALEAGADDYLTKPFDPEELLARVDLV 118
PRK10547 PRK10547
chemotaxis protein CheA; Provisional
218-669 5.43e-33

chemotaxis protein CheA; Provisional


Pssm-ID: 236712 [Multi-domain]  Cd Length: 670  Bit Score: 136.40  E-value: 5.43e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823315871 218 LQVMFRAAHTIKGSAYMVGLPPLGDFAHGMEDLLGAAREGAVSLSSDVRGLLAEATDTIGDLLTV---AAGADGAALP-- 292
Cdd:PRK10547   38 LNAIFRAAHSIKGGAGTFGFTVLQETTHLMENLLDEARRGEMQLNTDIINLFLETKDIMQEQLDAyktSQEPDAASFEyi 117
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823315871 293 ----AQLTavtarLRSAHSGEQTPVPPMSAAAPVVAPVPAPAPAAATSIRVPAARLEG-----LMDQLGELVTararMTQ 363
Cdd:PRK10547  118 cqalRQLA-----LEAKGETPSAVTRLSVVAIQEKSEPQDESPRSQSGLRIILSRLKAgevdlLEEELGNLGT----LTD 188
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823315871 364 LLSRLDELQGSM--TASQERFQrTVRDFeerYLNPDMVR-EEGAAPTTRMGGLDLSQQFAELEFDTYNDLNILSRSITEL 440
Cdd:PRK10547  189 VVKGADSLEATLpgSVAEDDIT-AVLCF---VIEADQITfETAVAAPQEKAEETTEVVEVSPKISVPPVLKLAAEQAPAG 264
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823315871 441 SADFAEVRRRLSDTAAELS-EENEQL----GKLV--------RRLRLD----------VNQTSRVA-------------- 483
Cdd:PRK10547  265 RVEREKTARSSESTSIRVAvEKVDQLinlvGELVitqsmlaqRSSELDpvnhgdlitsMGQLQRNArdlqesvmsirmmp 344
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823315871 484 ----FSqttaRLRRWAREQQADLTLQVE----GEDVLIESGILQRISDPLLHLLTNAAYHGLasESAESRRAAGKNPQGT 555
Cdd:PRK10547  345 meyvFS----RFPRLVRDLAGKLGKQVEltlvGSSTELDKSLIERIIDPLTHLVRNSLDHGI--ELPEKRLAAGKNSVGN 418
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823315871 556 VWIRAAEQGNFLEVTVADDGQGLDYARIRERALERGLRSAqelEQLSSDELGRLILLPGFSTAREVGNVAGRGVGLDVVA 635
Cdd:PRK10547  419 LILSAEHQGGNICIEVTDDGAGLNRERILAKAASQGLAVS---ENMSDEEVGMLIFAPGFSTAEQVTDVSGRGVGMDVVK 495
                         490       500       510
                  ....*....|....*....|....*....|....
gi 1823315871 636 TAVRQLGGELLISSERGVGTAFTLRVPTTQRIMD 669
Cdd:PRK10547  496 RNIQEMGGHVEIQSKQGKGTTIRILLPLTLAILD 529
OmpR COG0745
DNA-binding response regulator, OmpR family, contains REC and winged-helix (wHTH) domain ...
820-936 7.11e-31

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: 120.45  E-value: 7.11e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823315871 820 RLLLVDDSLSVRRLVGRMLERGGYQVVTASDGQEALDLLQQDaDFGAVVTDLEMPRVNGYELLSAVRARPATagLPMLVM 899
Cdd:COG0745     3 RILVVEDDPDIRELLADALEREGYEVDTAADGEEALELLEEE-RPDLILLDLMLPGMDGLEVCRRLRARPSD--IPIIML 79
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1823315871 900 TTRAGEKHQRLAFQLGADDYFTKPVNEALLLRRLGTL 936
Cdd:COG0745    80 TARDDEEDRVRGLEAGADDYLTKPFDPEELLARIRAL 116
RpfG COG3437
Response regulator c-di-GMP phosphodiesterase, RpfG family, contains REC and HD-GYP domains ...
818-942 6.76e-29

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: 115.65  E-value: 6.76e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823315871 818 NQRLLLVDDSLSVRRLVGRMLERGGYQVVTASDGQEALDLLQQdADFGAVVTDLEMPRVNGYELLSAVRARPATAGLPML 897
Cdd:COG3437     6 APTVLIVDDDPENLELLRQLLRTLGYDVVTAESGEEALELLLE-APPDLILLDVRMPGMDGFELLRLLRADPSTRDIPVI 84
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1823315871 898 VMTTRAGEKHQRLAFQLGADDYFTKPVNEALLLRRLGTLQQAQQA 942
Cdd:COG3437    85 FLTALADPEDRERALEAGADDYLTKPFDPEELLARVRNALELRRL 129
REC cd00156
phosphoacceptor receiver (REC) domain of response regulators (RRs) and pseudo response ...
822-923 1.18e-28

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: 110.39  E-value: 1.18e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823315871 822 LLVDDSLSVRRLVGRMLERGGYQVVTASDGQEALDLLQQDaDFGAVVTDLEMPRVNGYELLSAVRARPatAGLPMLVMTT 901
Cdd:cd00156     1 LIVDDDPAIRELLKSLLEREGYEVDTAADGEEALELLREE-RPDLVLLDLMMPGMDGLELLRKLRELP--PDIPVIVLTA 77
                          90       100
                  ....*....|....*....|..
gi 1823315871 902 RAGEKHQRLAFQLGADDYFTKP 923
Cdd:cd00156    78 KADEEDAVRALELGADDYLVKP 99
REC_hyHK_CKI1_RcsC-like cd17546
phosphoacceptor receiver (REC) domain of hybrid sensor histidine kinases/response regulators ...
821-933 3.28e-26

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: 103.70  E-value: 3.28e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823315871 821 LLLVDDSLSVRRLVGRMLERGGYQVVTASDGQEALDLLQQDaDFGAVVTDLEMPRVNGYELLSAVRARPATAG-LPMLVM 899
Cdd:cd17546     1 VLVVDDNPVNRKVLKKLLEKLGYEVDVAENGQEALELLKEE-PFDLVLMDLQMPVMDGLEATRRIRELEGGGRrTPIIAL 79
                          90       100       110
                  ....*....|....*....|....*....|....
gi 1823315871 900 TTRAGEKHQRLAFQLGADDYFTKPVNEALLLRRL 933
Cdd:cd17546    80 TANALEEDREKCLEAGMDDYLSKPVKLDQLKEVL 113
AtoC COG2204
DNA-binding transcriptional response regulator, NtrC family, contains REC, AAA-type ATPase, ...
820-942 4.13e-25

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: 109.28  E-value: 4.13e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823315871 820 RLLLVDDSLSVRRLVGRMLERGGYQVVTASDGQEALDLLQQDaDFGAVVTDLEMPRVNGYELLSAVRARPATagLPMLVM 899
Cdd:COG2204     4 RILVVDDDPDIRRLLKELLERAGYEVETAASGEEALALLREE-PPDLVLLDLRMPGMDGLELLRELRALDPD--LPVILL 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1823315871 900 TTRAGEKHQRLAFQLGADDYFTKPVNEALLLRRLGTLQQAQQA 942
Cdd:COG2204    81 TGYGDVETAVEAIKAGAFDYLTKPFDLEELLAAVERALERRRL 123
REC_Rcp-like cd17557
phosphoacceptor receiver (REC) domain of cyanobacterial phytochrome response regulator Rcp and ...
820-937 6.29e-25

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: 100.95  E-value: 6.29e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823315871 820 RLLLVDDSLSVRRLVGRMLERGG--YQVVTASDGQEALDLLQQDADFGA------VVTDLEMPRVNGYELLSAVRARPAT 891
Cdd:cd17557     1 TILLVEDNPGDAELIQEAFKEAGvpNELHVVRDGEEALDFLRGEGEYADaprpdlILLDLNMPRMDGFEVLREIKADPDL 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1823315871 892 AGLPMLVMTTRAGEKHQRLAFQLGADDYFTKPVNEALLLRRLGTLQ 937
Cdd:cd17557    81 RRIPVVVLTTSDAEEDIERAYELGANSYIVKPVDFEEFVEAIRSLG 126
REC_CheY4-like cd17562
phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY4 and similar CheY ...
820-930 6.77e-25

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: 100.45  E-value: 6.77e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823315871 820 RLLLVDDSLSVRRLVGRMLERGGYQVVTASDGQEALDLLQQDAdFGAVVTDLEMPRVNGYELLSAVRARPATAGLPMLVM 899
Cdd:cd17562     2 KILAVDDSASIRQMVSFTLRGAGYEVVEAADGRDALSKAQSKK-FDLIITDQNMPNMDGIELIKELRKLPAYKFTPILML 80
                          90       100       110
                  ....*....|....*....|....*....|.
gi 1823315871 900 TTRAGEKHQRLAFQLGADDYFTKPVNEALLL 930
Cdd:cd17562    81 TTESSDEKKQEGKAAGATGWLVKPFDPEQLL 111
REC_OmpR cd17574
phosphoacceptor receiver (REC) domain of OmpR family response regulators; OmpR-like proteins ...
822-923 8.90e-25

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: 99.40  E-value: 8.90e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823315871 822 LLVDDSLSVRRLVGRMLERGGYQVVTASDGQEALDLLQQDaDFGAVVTDLEMPRVNGYELLSAVRARPATagLPMLVMTT 901
Cdd:cd17574     1 LVVEDDEEIAELLSDYLEKEGYEVDTAADGEEALELAREE-QPDLIILDVMLPGMDGFEVCRRLREKGSD--IPIIMLTA 77
                          90       100
                  ....*....|....*....|..
gi 1823315871 902 RAGEKHQRLAFQLGADDYFTKP 923
Cdd:cd17574    78 KDEEEDKVLGLELGADDYITKP 99
REC_CheV-like cd19924
phosphoacceptor receiver (REC) domain of chemotaxis protein CheV and similar proteins; This ...
821-923 2.03e-24

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: 98.60  E-value: 2.03e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823315871 821 LLLVDDSLSVRRLVGRMLERGGYQVVTASDGQEALDLLQQDADFGA--------VVTDLEMPRVNGYELLSAVRARPATA 892
Cdd:cd19924     1 ILVVDDSPTARKQLRDLLKNLGFEIAEAVDGEEALNKLENLAKEGNdlskeldlIITDIEMPKMDGYELTFELRDDPRLA 80
                          90       100       110
                  ....*....|....*....|....*....|.
gi 1823315871 893 GLPMLVMTTRAGEKHQRLAFQLGADDYFTKP 923
Cdd:cd19924    81 NIPVILNSSLSGEFSRARGKKVGADAYLAKF 111
Response_reg pfam00072
Response regulator receiver domain; This domain receives the signal from the sensor partner in ...
822-933 4.06e-24

Response regulator receiver domain; This domain receives the signal from the sensor partner in bacterial two-component systems. It is usually found N-terminal to a DNA binding effector domain.


Pssm-ID: 395025 [Multi-domain]  Cd Length: 111  Bit Score: 97.99  E-value: 4.06e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823315871 822 LLVDDSLSVRRLVGRMLERGGYQVVTASDGQEALDLLQQDaDFGAVVTDLEMPRVNGYELLSAVRARPATagLPMLVMTT 901
Cdd:pfam00072   2 LIVDDDPLIRELLRQLLEKEGYVVAEADDGKEALELLKEE-RPDLILLDINMPGMDGLELLKRIRRRDPT--TPVIILTA 78
                          90       100       110
                  ....*....|....*....|....*....|..
gi 1823315871 902 RAGEKHQRLAFQLGADDYFTKPVNEALLLRRL 933
Cdd:pfam00072  79 HGDEDDAVEALEAGADDFLSKPFDPDELLAAI 110
YesN COG4753
Two-component response regulator, YesN/AraC family, consists of REC and AraC-type DNA-binding ...
820-923 5.53e-23

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: 94.46  E-value: 5.53e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823315871 820 RLLLVDDSLSVRRLVGRMLER-GGYQVV-TASDGQEALDLLQQDaDFGAVVTDLEMPRVNGYELLSAVRARPATAglPML 897
Cdd:COG4753     1 KVLIVDDEPLIREGLKRILEWeAGFEVVgEAENGEEALELLEEH-KPDLVITDINMPGMDGLELLEAIRELDPDT--KII 77
                          90       100
                  ....*....|....*....|....*.
gi 1823315871 898 VMTTRAGEKHQRLAFQLGADDYFTKP 923
Cdd:COG4753    78 ILSGYSDFEYAQEAIKLGADDYLLKP 103
REC_CheY_CheY3 cd19923
phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY3 and similar CheY ...
820-933 2.28e-22

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: 93.17  E-value: 2.28e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823315871 820 RLLLVDDSLSVRRLVGRMLERGGYQVVT-ASDGQEALDLLQQdADFGAVVTDLEMPRVNGYELLSAVRARPATAGLPMLV 898
Cdd:cd19923     2 KVLVVDDFSTMRRIIKNLLKELGFNNVEeAEDGVDALEKLKA-GGFDFVITDWNMPNMDGLELLKTIRADGALSHLPVLM 80
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1823315871 899 MTTRAGEKHQRLAFQLGADDYFTKPVNEALLLRRL 933
Cdd:cd19923    81 VTAEAKKENVIAAAQAGVNNYIVKPFTAATLKEKL 115
REC_RpfG-like cd17551
phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase response regulator ...
820-931 5.95e-22

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: 91.73  E-value: 5.95e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823315871 820 RLLLVDDSLSVRRLVGRMLERGGY-QVVTASDGQEALDLLQQDaDFGAVVTDLEMPRVNGYELLSAVRARPATAGLPMLV 898
Cdd:cd17551     2 RILIVDDNPTNLLLLEALLRSAGYlEVVSFTDPREALAWCREN-PPDLILLDYMMPGMDGLEFIRRLRALPGLEDVPIVM 80
                          90       100       110
                  ....*....|....*....|....*....|....
gi 1823315871 899 MTTRAGEKHQRLAFQLGADDYFTKPVNEA-LLLR 931
Cdd:cd17551    81 ITADTDREVRLRALEAGATDFLTKPFDPVeLLAR 114
REC_2_GGDEF cd17544
second phosphoacceptor receiver (REC) domain of uncharacterized GGDEF domain proteins; This ...
822-923 1.81e-21

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: 90.66  E-value: 1.81e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823315871 822 LLVDDSLSVRRLVGRMLERGGYQVVTASDGQEALDLLQQDADFGAVVTDLEMPRVNGYELLSAVRARPATAGLPML---- 897
Cdd:cd17544     4 LVVDDSATSRNHLRALLRRHNFQVLEAANGQEALEVLEQHPDIKLVITDYNMPEMDGFELVREIRKKYSRDQLAIIgisa 83
                          90       100       110
                  ....*....|....*....|....*....|.
gi 1823315871 898 ----VMTTRagekhqrlaF-QLGADDYFTKP 923
Cdd:cd17544    84 sgdnALSAR---------FiKAGANDFLTKP 105
REC_OmpR_BsPhoP-like cd19937
phosphoacceptor receiver (REC) domain of BsPhoP-like OmpR family response regulators; Bacillus ...
822-932 2.59e-21

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: 90.03  E-value: 2.59e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823315871 822 LLVDDSLSVRRLVGRMLERGGYQVVTASDGQEALDLLQQDaDFGAVVTDLEMPRVNGYELLSAVRARPATAGLPMLVMTT 901
Cdd:cd19937     1 LVVDDEEDIVELLKYNLEKEGYEVVTAYDGEEALKRAKDE-KPDLIILDLMLPGIDGLEVCRILRSDPKTSSIPIIMLTA 79
                          90       100       110
                  ....*....|....*....|....*....|.
gi 1823315871 902 RAGEKHQRLAFQLGADDYFTKPVNEALLLRR 932
Cdd:cd19937    80 KGEEFDKVLGLELGADDYITKPFSPRELLAR 110
REC_2_DhkD-like cd17580
second phosphoacceptor receiver (REC) domain of Dictyostelium discoideum hybrid signal ...
822-931 2.95e-20

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: 86.74  E-value: 2.95e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823315871 822 LLVDDSLSVRRLVGRMLERGGYQVVTASDGQEALDLLQQDAdFGAVVTDLEMPRVNGYELLSAVRARPATAGLPMLVMTT 901
Cdd:cd17580     2 LVVDDNEDAAEMLALLLELEGAEVTTAHSGEEALEAAQRFR-PDVILSDIGMPGMDGYELARRLRELPWLANTPAIALTG 80
                          90       100       110
                  ....*....|....*....|....*....|
gi 1823315871 902 RAGEKHQRLAFQLGADDYFTKPVNEALLLR 931
Cdd:cd17580    81 YGQPEDRERALEAGFDAHLVKPVDPDELIE 110
REC_PA4781-like cd19920
phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase PA4781 and similar ...
821-924 1.11e-19

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: 84.87  E-value: 1.11e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823315871 821 LLLVDDSLSVRRLVGRMLERGGYQVVTASDGQEALDLLQQdADFGAVVTDLEMPRVNGYELLSAVRARPATAGLPMLVMT 900
Cdd:cd19920     1 ILIVDDVPDNLRLLSELLRAAGYRVLVATDGQQALQRAQA-EPPDLILLDVMMPGMDGFEVCRRLKADPATRHIPVIFLT 79
                          90       100
                  ....*....|....*....|....
gi 1823315871 901 TRAGEKHQRLAFQLGADDYFTKPV 924
Cdd:cd19920    80 ALTDTEDKVKGFELGAVDYITKPF 103
REC_Ycf29 cd19927
phosphoacceptor receiver (REC) domain of probable transcriptional regulator Ycf29; Ycf29 is a ...
821-923 1.23e-19

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: 84.74  E-value: 1.23e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823315871 821 LLLVDDSLSVRRLVGRMLERGGYQVVTASDGQEALDLLQQDAdFGAVVTDLEMPRVNGYELLSAVRARPATAGLPMLVMT 900
Cdd:cd19927     1 ILLVDDDPGIRLAVKDYLEDQGFTVIAASNGLEALDLLNQYI-PDLIISDIIMPGVDGYSLLGKLRKNADFDTIPVIFLT 79
                          90       100
                  ....*....|....*....|...
gi 1823315871 901 TRAGEKHQRLAFQLGADDYFTKP 923
Cdd:cd19927    80 AKGMTSDRIKGYNAGCDGYLSKP 102
REC_CheB-like cd17541
phosphoacceptor receiver (REC) domain of chemotaxis response regulator protein-glutamate ...
820-923 1.29e-18

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: 82.44  E-value: 1.29e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823315871 820 RLLLVDDSLSVRRLVGRMLER-GGYQVV-TASDGQEALDLLQQDA-DfgaVVT-DLEMPRVNGYELLSAVRA-RPatagL 894
Cdd:cd17541     2 RVLIVDDSAVMRKLLSRILESdPDIEVVgTARDGEEALEKIKELKpD---VITlDIEMPVMDGLEALRRIMAeRP----T 74
                          90       100       110
                  ....*....|....*....|....*....|..
gi 1823315871 895 PMLVMTTRAgEKHQRLAFQ---LGADDYFTKP 923
Cdd:cd17541    75 PVVMVSSLT-EEGAEITLEaleLGAVDFIAKP 105
REC_D1_PleD-like cd17538
first (D1) phosphoacceptor receiver (REC) domain of response regulator PleD and similar ...
820-924 2.78e-18

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: 81.00  E-value: 2.78e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823315871 820 RLLLVDDSLSVRRLVGRMLERGGYQVVTASDGQEALDLLQQDA-DFgaVVTDLEMPRVNGYELLSAVRARPATAGLPmLV 898
Cdd:cd17538     1 KILVVDDEPANRELLEALLSAEGYEVLTADSGQEALALAEEELpDL--ILLDVMMPGMDGFEVCRRLKEDPETRHIP-VI 77
                          90       100
                  ....*....|....*....|....*..
gi 1823315871 899 MTTRAGEKHQRL-AFQLGADDYFTKPV 924
Cdd:cd17538    78 MITALDDREDRIrGLEAGADDFLSKPI 104
PRK10610 PRK10610
chemotaxis protein CheY;
815-936 8.13e-18

chemotaxis protein CheY;


Pssm-ID: 170568 [Multi-domain]  Cd Length: 129  Bit Score: 80.40  E-value: 8.13e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823315871 815 ATGNQRLLLVDDSLSVRRLVGRMLERGGYQ-VVTASDGQEALDLLQQdADFGAVVTDLEMPRVNGYELLSAVRARPATAG 893
Cdd:PRK10610    2 ADKELKFLVVDDFSTMRRIVRNLLKELGFNnVEEAEDGVDALNKLQA-GGFGFVISDWNMPNMDGLELLKTIRADGAMSA 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1823315871 894 LPMLVMTTRAGEKHQRLAFQLGADDYFTKPVNEALLLRRLGTL 936
Cdd:PRK10610   81 LPVLMVTAEAKKENIIAAAQAGASGYVVKPFTAATLEEKLNKI 123
REC_typeB_ARR-like cd17584
phosphoacceptor receiver (REC) domain of type B Arabidopsis response regulators (ARRs) and ...
822-926 9.61e-18

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: 79.98  E-value: 9.61e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823315871 822 LLVDDSLSVRRLVGRMLERGGYQVVTASDGQEALDLLQQDAD-FGAVVTDLEMPRVNGYELLSAVRARPataGLPMLVMT 900
Cdd:cd17584     2 LVVDDDPTCLAILKRMLLRCGYQVTTCTDAEEALSMLRENKDeFDLVITDVHMPDMDGFEFLELIRLEM---DLPVIMMS 78
                          90       100
                  ....*....|....*....|....*.
gi 1823315871 901 TRAGEKHQRLAFQLGADDYFTKPVNE 926
Cdd:cd17584    79 ADGSTSTVMKGLAHGACDYLLKPVSI 104
REC_hyHK cd17598
phosphoacceptor receiver (REC) domain of uncharacterized hybrid sensor histidine kinase ...
821-933 2.17e-17

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: 78.91  E-value: 2.17e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823315871 821 LLLVDDSLSVRRLVGRMLERGGYQVVTASDGQEALDLLQQDADfGAVVTDLEMPRVNGYELLSAVRARPATAGLPMLVMT 900
Cdd:cd17598     1 ILIVEDSPTQAEQLKHILEEQGYKVQVARNGREALAMLAEHRP-TLVISDIVMPEMDGYELCRKIKSDPDLKDIPVILLT 79
                          90       100       110
                  ....*....|....*....|....*....|...
gi 1823315871 901 TRAGEKHQRLAFQLGADDYFTKPVNEALLLRRL 933
Cdd:cd17598    80 TLSDPRDVIRGLECGADNFITKPYDEKYLLSRI 112
CitB COG4565
DNA-binding response regulator DpiB of citrate/malate metabolism [Transcription, Signal ...
820-942 2.60e-17

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


Pssm-ID: 443622 [Multi-domain]  Cd Length: 138  Bit Score: 79.24  E-value: 2.60e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823315871 820 RLLLVDDSLSVRRLVGRMLER-GGYQVV-TASDGQEALDLLQQDaDFGAVVTDLEMPRVNGYELLSAVRARpaTAGLPML 897
Cdd:COG4565     5 RVLIVEDDPMVAELLRRYLERlPGFEVVgVASSGEEALALLAEH-RPDLILLDIYLPDGDGLELLRELRAR--GPDVDVI 81
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1823315871 898 VMTTRAGEKHQRLAFQLGADDYFTKPVNEALLLRRLGTLQQAQQA 942
Cdd:COG4565    82 VITAARDPETVREALRAGVVDYLIKPFTFERLREALERYLEYRRL 126
orf27 CHL00148
Ycf27; Reviewed
818-932 1.06e-16

Ycf27; Reviewed


Pssm-ID: 214376 [Multi-domain]  Cd Length: 240  Bit Score: 80.53  E-value: 1.06e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823315871 818 NQRLLLVDDSLSVRRLVGRMLERGGYQVVTASDGQEALDLLQQDADfGAVVTDLEMPRVNGYELLSAVRARpatAGLPML 897
Cdd:CHL00148    6 KEKILVVDDEAYIRKILETRLSIIGYEVITASDGEEALKLFRKEQP-DLVILDVMMPKLDGYGVCQEIRKE---SDVPII 81
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1823315871 898 VMTTRAGEKHQRLAFQLGADDYFTKPVN----EA---LLLRR 932
Cdd:CHL00148   82 MLTALGDVSDRITGLELGADDYVVKPFSpkelEArirSVLRR 123
HATPase_c smart00387
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.
523-662 1.69e-16

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


Pssm-ID: 214643 [Multi-domain]  Cd Length: 111  Bit Score: 76.15  E-value: 1.69e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823315871  523 DPLLHLLTNAAYHGLasesaesrRAAGknPQGTVWIRAAEQGNFLEVTVADDGQGLDyarireralerglrsaqeleqls 602
Cdd:smart00387   4 DRLRQVLSNLLDNAI--------KYTP--EGGRITVTLERDGDHVEITVEDNGPGIP----------------------- 50
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823315871  603 sDELGRLILLPGFSTAREVGNVAGRGVGLDVVATAVRQLGGELLISSERGVGTAFTLRVP 662
Cdd:smart00387  51 -PEDLEKIFEPFFRTDKRSRKIGGTGLGLSIVKKLVELHGGEISVESEPGGGTTFTITLP 109
REC_RR468-like cd17552
phosphoacceptor receiver (REC) domain of Thermotoga maritima response regulator RR468 and ...
818-925 2.16e-16

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: 76.05  E-value: 2.16e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823315871 818 NQRLLLVDDSLSVRRLVGRMLER-GGYQVVTASDGQEALDLLQQDA-DfgAVVTDLEMPRVNGYELLSAVRARPATAGLP 895
Cdd:cd17552     1 SKRILVIDDEEDIREVVQACLEKlAGWEVLTASSGQEGLEKAATEQpD--AILLDVMMPDMDGLATLKKLQANPETQSIP 78
                          90       100       110
                  ....*....|....*....|....*....|
gi 1823315871 896 MLVMTTRAGEKHQRLAFQLGADDYFTKPVN 925
Cdd:cd17552    79 VILLTAKAQPSDRQRFASLGVAGVIAKPFD 108
PRK10955 PRK10955
envelope stress response regulator transcription factor CpxR;
820-946 3.77e-16

envelope stress response regulator transcription factor CpxR;


Pssm-ID: 182864 [Multi-domain]  Cd Length: 232  Bit Score: 78.69  E-value: 3.77e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823315871 820 RLLLVDDSLSVRRLVGRMLERGGYQVVTASDGQEALDLLQQDADFgaVVTDLEMPRVNGYELLSAVRARPATaglPMLVM 899
Cdd:PRK10955    3 KILLVDDDRELTSLLKELLEMEGFNVIVAHDGEQALDLLDDSIDL--LLLDVMMPKKNGIDTLKELRQTHQT---PVIML 77
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1823315871 900 TTRAGEKHQRLAFQLGADDYFTKPVNEALL-------LRRLGTLQQAQQAGVSA 946
Cdd:PRK10955   78 TARGSELDRVLGLELGADDYLPKPFNDRELvariraiLRRSHWSEQQQNNDNGS 131
REC_HupR-like cd17569
phosphoacceptor receiver (REC) domain of hydrogen uptake protein regulator (HupR) and similar ...
820-939 4.31e-16

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: 75.13  E-value: 4.31e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823315871 820 RLLLVDDSLSVRRLVGRMLERGGYQVVTASDGQEALDLLQQDaDFGAVVTDLEMPRVNGYELLSAVRAR-PATAglpMLV 898
Cdd:cd17569     2 TILLVDDEPNILKALKRLLRREGYEVLTATSGEEALEILKQE-PVDVVISDQRMPGMDGAELLKRVRERyPDTV---RIL 77
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1823315871 899 MT--------TRA---GEKHQrlafqlgaddYFTKPVNEALLLRrlgTLQQA 939
Cdd:cd17569    78 LTgyadldaaIEAineGEIYR----------FLTKPWDDEELKE---TIRQA 116
REC_OmpR_PhoB cd17618
phosphoacceptor receiver (REC) domain of PhoB response regulator from the OmpR family; The ...
820-933 5.36e-16

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: 74.98  E-value: 5.36e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823315871 820 RLLLVDDSLSVRRLVGRMLERGGYQVVTASDGQEALDLLQqDADFGAVVTDLEMPRVNGYELLSAVRARPATAGLPMLVM 899
Cdd:cd17618     2 TILIVEDEPAIREMIAFNLERAGFDVVEAEDAESAVNLIV-EPRPDLILLDWMLPGGSGIQFIRRLKRDEMTRDIPIIML 80
                          90       100       110
                  ....*....|....*....|....*....|....
gi 1823315871 900 TTRAGEKHQRLAFQLGADDYFTKPVNEALLLRRL 933
Cdd:cd17618    81 TARGEEEDKVRGLEAGADDYITKPFSPRELVARI 114
REC_TrrA-like cd17554
phosphoacceptor receiver (REC) domain of Thermotoga maritima response regulator TrrA and ...
820-922 5.84e-16

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


Pssm-ID: 381106 [Multi-domain]  Cd Length: 113  Bit Score: 74.56  E-value: 5.84e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823315871 820 RLLLVDDSLSVRRLVGRMLERGGYQVVTASDGQEALDLLQQDaDFGAVVTDLEMPRVNGYELLSAVRARpaTAGLPMLVM 899
Cdd:cd17554     2 KILVVDDEENIRELYKEELEDEGYEVVTAGNGEEALEKLESE-DPDLVILDIKMPGMDGLETLRKIREK--KPDLPVIIC 78
                          90       100
                  ....*....|....*....|....
gi 1823315871 900 TTRAGEKHQrlaFQ-LGADDYFTK 922
Cdd:cd17554    79 TAYSEYKSD---FSsWAADAYVVK 99
HPT smart00073
Histidine Phosphotransfer domain; Contains an active histidine residue that mediates ...
193-276 8.12e-16

Histidine Phosphotransfer domain; Contains an active histidine residue that mediates phosphotransfer reactions. Domain detected only in eubacteria. This alignment is an extension to that shown in the Cell structure paper.


Pssm-ID: 197502 [Multi-domain]  Cd Length: 92  Bit Score: 73.44  E-value: 8.12e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823315871  193 EYFAPEVHEHLASLREQLGRGEDA----DLQVMFRAAHTIKGSAYMVGLPPLGDFAHGMEDLLGAAREGAVSLSSDVRGL 268
Cdd:smart00073   4 ELFREELAEFLQSLEEGLLELEKAldaqDVNEIFRAAHTLKGSAGSLGLQQLAQLCHQLENLLDALRSGEVELTPDLLDL 83

                   ....*...
gi 1823315871  269 LAEATDTI 276
Cdd:smart00073  84 LLELVDVL 91
COG4567 COG4567
DNA-binding response regulator, ActR/RegA family, consists of REC and Fis-type HTH domains ...
816-946 8.85e-16

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: 76.11  E-value: 8.85e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823315871 816 TGNQRLLLVDDSLSVRRLVGRMLERGGYQVVTASDGQEALDLLQQdADFGAVVTDLEMPRVNGYELLSAVRARPATAglP 895
Cdd:COG4567     2 AEDRSLLLVDDDEAFARVLARALERRGFEVTTAASVEEALALLEQ-APPDYAVLDLRLGDGSGLDLIEALRERDPDA--R 78
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823315871 896 MLVMT-----TRAGEkhqrlAFQLGADDYFTKPVN----EALLLRRLGTLQQAQQAGVSA 946
Cdd:COG4567    79 IVVLTgyasiATAVE-----AIKLGADDYLAKPADaddlLAALERAEGDAPAPPENPMSL 133
REC_NtrC cd19919
phosphoacceptor receiver (REC) domain of DNA-binding transcriptional regulator NtrC; ...
819-932 8.86e-16

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: 74.23  E-value: 8.86e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823315871 819 QRLLLVDDSLSVRRLVGRMLERGGYQVVTASDGQEALDLLQQDADfGAVVTDLEMPRVNGYELLSAVRARpaTAGLPMLV 898
Cdd:cd19919     1 KTVWIVDDDSSIRWVLERALAGAGLTVTSFENAQEALAALASSQP-DVLISDIRMPGMDGLALLAQIKQR--HPDLPVII 77
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1823315871 899 MTTragekHQRL-----AFQLGADDYFTKP--VNEAL-LLRR 932
Cdd:cd19919    78 MTA-----HSDLdsavsAYQGGAFEYLPKPfdIDEAVaLVER 114
REC_OmpR_CpxR cd17623
phosphoacceptor receiver (REC) domain of CpxR-like OmpR family response regulators; CpxR is ...
821-933 1.10e-15

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


Pssm-ID: 381138 [Multi-domain]  Cd Length: 115  Bit Score: 73.88  E-value: 1.10e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823315871 821 LLLVDDSLSVRRLVGRMLERGGYQVVTASDGQEALDLLQQDAdFGAVVTDLEMPRVNGYELLSAVRARPAtagLPMLVMT 900
Cdd:cd17623     1 ILLIDDDRELTELLTEYLEMEGFNVRAAHDGEQGLAALLEGS-PDLVVLDVMLPKMNGLDVLKELRKTSQ---VPVLMLT 76
                          90       100       110
                  ....*....|....*....|....*....|...
gi 1823315871 901 TRAGEKHQRLAFQLGADDYFTKPVNEALLLRRL 933
Cdd:cd17623    77 ARGDDIDRILGLELGADDYLPKPFNPRELVARI 109
KdpD COG2205
K+-sensing histidine kinase KdpD [Signal transduction mechanisms];
428-665 3.06e-15

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


Pssm-ID: 441807 [Multi-domain]  Cd Length: 239  Bit Score: 76.10  E-value: 3.06e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823315871 428 NDLNILSRSITELSADFAEVRRRLSDTAAELSEENEQLGKLVRRLrLDVNQTSRVAFS-------------QTTARLRRW 494
Cdd:COG2205    29 TPLTSILGAAELLLDEEDLSPEERRELLEIIRESAERLLRLIEDL-LDLSRLESGKLSlelepvdlaelleEAVEELRPL 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823315871 495 AREQQADLTLQVEGEDVLIE--SGILQRIsdpLLHLLTNAAYHGlasesaesrraagkNPQGTVWIRAAEQGNFLEVTVA 572
Cdd:COG2205   108 AEEKGIRLELDLPPELPLVYadPELLEQV---LANLLDNAIKYS--------------PPGGTITISARREGDGVRISVS 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823315871 573 DDGQGLDyARIRERALERglrsaqeleqlssdelgrlillpgFSTAREVGNVAGRGVGLDVVATAVRQLGGELLISSERG 652
Cdd:COG2205   171 DNGPGIP-EEELERIFER------------------------FYRGDNSRGEGGTGLGLAIVKRIVEAHGGTIWVESEPG 225
                         250
                  ....*....|...
gi 1823315871 653 VGTAFTLRVPTTQ 665
Cdd:COG2205   226 GGTTFTVTLPLAE 238
REC_OmpR_DrrD-like cd17625
phosphoacceptor receiver (REC) domain of DrrD-like OmpR family response regulators; DrrD is a ...
822-936 3.25e-15

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


Pssm-ID: 381140 [Multi-domain]  Cd Length: 115  Bit Score: 72.64  E-value: 3.25e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823315871 822 LLVDDSLSVRRLVGRMLERGGYQVVTASDGQEALDLLQQDAdFGAVVTDLEMPRVNGYELLSAVRA-RPATaglPMLVMT 900
Cdd:cd17625     1 LVVEDEKDLSEAITKHLKKEGYTVDVCFDGEEGLEYALSGI-YDLIILDIMLPGMDGLEVLKSLREeGIET---PVLLLT 76
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1823315871 901 TRAGEKHQRLAFQLGADDYFTKPVNEALLLRRLGTL 936
Cdd:cd17625    77 ALDAVEDRVKGLDLGADDYLPKPFSLAELLARIRAL 112
REC_DctD-like cd17549
phosphoacceptor receiver (REC) domain of C4-dicarboxylic acid transport protein D (DctD) and ...
822-942 5.70e-15

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: 72.52  E-value: 5.70e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823315871 822 LLVDDSLSVRRLVGRMLERGGYQVVTASDGQEALDLLQQDADfGAVVTDLEMPRVNGYELLSAVRARpaTAGLPMLVMT- 900
Cdd:cd17549     2 LLVDDDADVREALQQTLELAGFRVRAFADAEEALAALSPDFP-GVVISDIRMPGMDGLELLAQIREL--DPDLPVILITg 78
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1823315871 901 ----TRAGEkhqrlAFQLGADDYFTKPVNEALLlrrLGTLQQAQQA 942
Cdd:cd17549    79 hgdvPMAVE-----AMRAGAYDFLEKPFDPERL---LDVVRRALEK 116
HPT cd00088
Histidine Phosphotransfer domain, involved in signalling through a two part component systems ...
189-280 7.14e-15

Histidine Phosphotransfer domain, involved in signalling through a two part component systems in which an autophosphorylating histidine protein kinase serves as a phosphoryl donor to a response regulator protein; the response regulator protein is modulated by phosphorylation and dephosphorylation of a conserved aspartic acid residue; two-component proteins are abundant in most eubacteria; In E. coli there are 62 two-component proteins involved in a variety of processes such as chemotaxis, osmoregulation, metabolism and transport 1; also present in both Gram positive and Gram negative pathogenic bacteria where they regulate basic housekeeping functions and control expression of toxins and other proteins important for pathogenesis; in archaea and eukaryotes, two-component pathways constitute a very small number of all signaling systems; in fungi they mediate environmental stress responses and, in pathogenic yeast, hyphal development. In Dictyostelium and in plants, they are involved in important processes such as osmoregulation, cell growth, and differentiation; to date two-component proteins have not been identified in animals; in most prokaryotic systems, the output response is effected directly by the RR, which functions as a transcription factor while in eukaryotic systems, two-component proteins are found at the beginning of signaling pathways where they interface with more conventional eukaryotic signaling strategies such as MAP kinase and cyclic nucleotide cascades


Pssm-ID: 238041 [Multi-domain]  Cd Length: 94  Bit Score: 70.87  E-value: 7.14e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823315871 189 AEVWEYFAPEVHEHLASLREQLGRGEDA-DLQVMFRAAHTIKGSAYMVGLPPLGDFAHGMEDLLGAAREGaVSLSSDVRG 267
Cdd:cd00088     2 EELLELFLEEAEELLEELERALLELEDAeDLNEIFRAAHTLKGSAASLGLQRLAQLAHQLEDLLDALRDG-LEVTPELID 80
                          90
                  ....*....|...
gi 1823315871 268 LLAEATDTIGDLL 280
Cdd:cd00088    81 LLLDALDALKAEL 93
REC_typeA_ARR cd17581
phosphoacceptor receiver (REC) domain of type A Arabidopsis response regulators (ARRs) and ...
822-924 7.65e-15

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: 71.63  E-value: 7.65e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823315871 822 LLVDDSLSVRRLVGRMLERGGYQVVTASDGQEALDLL----------QQDADFGAVVTDLEMPRVNGYELLSAVRARPAT 891
Cdd:cd17581     2 LAVDDSLVDRKVIERLLRISSCRVTAVDSGKRALEFLgledeedssnFNEPKVNMIITDYCMPGMTGYDLLKKVKESSAL 81
                          90       100       110
                  ....*....|....*....|....*....|...
gi 1823315871 892 AGLPMLVMTTRAGEKHQRLAFQLGADDYFTKPV 924
Cdd:cd17581    82 KEIPVVIMSSENIPTRISRCLEEGAEDFLLKPV 114
REC_OmpR_YycF-like cd17614
phosphoacceptor receiver (REC) domain of YrcF-like OmpR family response regulators; YycF ...
821-933 2.35e-14

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: 70.14  E-value: 2.35e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823315871 821 LLLVDDSLSVRRLVGRMLERGGYQVVTASDGQEALDLLQQ-DADFgaVVTDLEMPRVNGYELLSAVRarpATAGLPMLVM 899
Cdd:cd17614     1 ILVVDDEKPISDILKFNLTKEGYEVVTAYDGREALEKVEEeQPDL--ILLDLMLPEKDGLEVCREVR---KTSNVPIIML 75
                          90       100       110
                  ....*....|....*....|....*....|....
gi 1823315871 900 TTRAGEKHQRLAFQLGADDYFTKPVNEALLLRRL 933
Cdd:cd17614    76 TAKDSEVDKVLGLELGADDYVTKPFSNRELLARV 109
FixJ COG4566
DNA-binding response regulator, FixJ family, consists of REC and HTH domains [Signal ...
823-942 2.36e-14

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: 72.44  E-value: 2.36e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823315871 823 LVDDSLSVRRLVGRMLERGGYQVVTASDGQEALDLLQQDAdFGAVVTDLEMPRVNGYELLSAVRARPATagLPMLVMTTR 902
Cdd:COG4566     4 IVDDDEAVRDSLAFLLESAGLRVETFASAEAFLAALDPDR-PGCLLLDVRMPGMSGLELQEELAARGSP--LPVIFLTGH 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1823315871 903 AGEKHQRLAFQLGADDYFTKPVNEALLLRRLGT-LQQAQQA 942
Cdd:COG4566    81 GDVPMAVRAMKAGAVDFLEKPFDDQALLDAVRRaLARDRAR 121
REC_OmpR_kpRstA-like cd17622
phosphoacceptor receiver (REC) domain of kpRstA-like OmpR family response regulators; ...
820-936 5.25e-14

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: 69.33  E-value: 5.25e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823315871 820 RLLLVDDSLSVRRLVGRMLERGGYQVVTASDGQEALDLLQQDADfGAVVTDLEMPRVNGyelLSAVRARPATAGLPMLVM 899
Cdd:cd17622     2 RILLVEDDPKLARLIADFLESHGFNVVVEHRGDRALEVIAREKP-DAVLLDIMLPGIDG---LTLCRDLRPKYQGPILLL 77
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1823315871 900 TTRAGEKHQRLAFQLGADDYFTKPVNEALLLRRLGTL 936
Cdd:cd17622    78 TALDSDIDHILGLELGADDYVVKPVEPAVLLARLRAL 114
REC_OmpR_ChvI-like cd19936
phosphoacceptor receiver (REC) domain of ChvI-like OmpR family response regulators; ...
823-923 6.36e-14

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: 68.24  E-value: 6.36e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823315871 823 LVDDSLSVRRLVGRMLERGGYQVVTASDGQEALD-LLQQDADFgaVVTDLEMPRVNGYELLSAVRARpatAGLPMLVMTT 901
Cdd:cd19936     3 LVDDDRNILTSVSMALEAEGFSVETYTDGASALDgLNARPPDL--AILDIKMPRMDGMELLQRLRQK---STLPVIFLTS 77
                          90       100
                  ....*....|....*....|..
gi 1823315871 902 RAGEKHQRLAFQLGADDYFTKP 923
Cdd:cd19936    78 KDDEIDEVFGLRMGADDYITKP 99
REC_YesN-like cd17536
phosphoacceptor receiver (REC) domain of YesN and related helix-turn-helix containing response ...
821-941 7.69e-14

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: 68.90  E-value: 7.69e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823315871 821 LLLVDDSLSVRRLVGRML--ERGGYQVV-TASDGQEALDLLQQ-DADFgaVVTDLEMPRVNGYELLSAVRAR-PATaglP 895
Cdd:cd17536     1 VLIVDDEPLIREGLKKLIdwEELGFEVVgEAENGEEALELIEEhKPDI--VITDIRMPGMDGLELIEKIRELyPDI---K 75
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1823315871 896 MLVMTtraGekHQ-----RLAFQLGADDYFTKPVNEALLLRrlgTLQQAQQ 941
Cdd:cd17536    76 IIILS---G--YDdfeyaQKAIRLGVVDYLLKPVDEEELEE---ALEKAKE 118
REC_OmpR_PrrA-like cd17627
phosphoacceptor receiver (REC) domain of PrrA-like OmpR family response regulators; The ...
821-936 7.88e-14

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: 68.56  E-value: 7.88e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823315871 821 LLLVDDSLSVRRLVGRMLERGGYQVVTASDGQEALDLLQQDADfGAVVTDLEMPRVNGYELLSAVRArpATAGLPMLVMT 900
Cdd:cd17627     1 ILVVDDDRAVRESLRRSLRFEGYEVETAVDGAEALRVISGNRP-DAVVLDVMMPRLDGLEVCRRLRA--AGNDLPILVLT 77
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1823315871 901 TRAGEKHQRLAFQLGADDYFTKPVNEALLLRRLGTL 936
Cdd:cd17627    78 ARDSVSDRVAGLDAGADDYLVKPFALEELLARVRAL 113
REC_RssB-like cd17555
phosphoacceptor receiver (REC) domain of Pseudomonas aeruginosa RssB and similar domains; ...
820-924 7.88e-14

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: 68.77  E-value: 7.88e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823315871 820 RLLLVDDSLSVRRLVGRMLERGGYQVVTASDGQEALDLLQQDAdFGAVVTDLEMPRVNGYELLSAVRARpaTAGLPMLVM 899
Cdd:cd17555     2 TILVIDDDEVVRESIAAYLEDSGFQVLQAADGRQGLELFRSEQ-PDLVLCDLRMPEMDGLEVLKQITKE--SPDTPVIVV 78
                          90       100
                  ....*....|....*....|....*.
gi 1823315871 900 TTrAGEKHQRL-AFQLGADDYFTKPV 924
Cdd:cd17555    79 SG-AGVMSDAVeALRLGAWDYLTKPI 103
REC_DivK-like cd17548
phosphoacceptor receiver (REC) domain of DivK and similar proteins; Caulobacter crescentus ...
820-925 7.92e-14

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: 68.72  E-value: 7.92e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823315871 820 RLLLVDDSLSVRRLVGRMLERGGYQVVTASDGQEALDLLQQdADFGAVVTDLEMPRVNGYELLSAVRARPATAGLPMLVM 899
Cdd:cd17548     1 KILIVEDNPLNMKLARDLLESAGYEVLEAADGEEALEIARK-EKPDLILMDIQLPGMDGLEATRLLKEDPATRDIPVIAL 79
                          90       100
                  ....*....|....*....|....*.
gi 1823315871 900 TTRAGEKHQRLAFQLGADDYFTKPVN 925
Cdd:cd17548    80 TAYAMKGDREKILEAGCDGYISKPID 105
PRK15479 PRK15479
transcriptional regulator TctD;
820-943 8.10e-14

transcriptional regulator TctD;


Pssm-ID: 185376 [Multi-domain]  Cd Length: 221  Bit Score: 71.68  E-value: 8.10e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823315871 820 RLLLVDDSLSVRRLVGRMLERGGYQVVTASDGQEALDLLQQDaDFGAVVTDLEMPRVNGYELLSAVRARPATagLPMLVM 899
Cdd:PRK15479    2 RLLLAEDNRELAHWLEKALVQNGFAVDCVFDGLAADHLLQSE-MYALAVLDINMPGMDGLEVLQRLRKRGQT--LPVLLL 78
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1823315871 900 TTRAGEKHQRLAFQLGADDYFTKPVN--------EALLLRRLGTLQQAQQAG 943
Cdd:PRK15479   79 TARSAVADRVKGLNVGADDYLPKPFEleeldarlRALLRRSAGQVQEVQQLG 130
REC_OmpR_BfmR-like cd19939
phosphoacceptor receiver (REC) domain of BfmR-like OmpR family response regulators; ...
820-936 1.07e-13

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: 68.17  E-value: 1.07e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823315871 820 RLLLVDDSLSVRRLVGRMLERGGYQVVTASDGQEALD-LLQQDADFgaVVTDLEMPRVNGYELLSAVRARPAtagLPMLV 898
Cdd:cd19939     1 RILIVEDELELARLTRDYLIKAGLEVSVFTDGQRAVRrIIDEQPSL--VVLDIMLPGMDGLTVCREVREHSH---VPILM 75
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1823315871 899 MTTRAGEKHQRLAFQLGADDYFTKPVNEALLLRRLGTL 936
Cdd:cd19939    76 LTARTEEMDRVLGLEMGADDYLCKPFSPRELLARVRAL 113
REC_CheY cd17542
phosphoacceptor receiver (REC) domain of chemotaxis protein CheY; The chemotaxis response ...
820-933 1.28e-13

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


Pssm-ID: 381097 [Multi-domain]  Cd Length: 117  Bit Score: 68.07  E-value: 1.28e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823315871 820 RLLLVDDSLSVRRLVGRMLERGGYQVV-TASDGQEALDLLQQ-DADfgaVVT-DLEMPRVNGYELLSAVRARPATAglpM 896
Cdd:cd17542     2 KVLIVDDAAFMRMMLKDILTKAGYEVVgEAANGEEAVEKYKElKPD---LVTmDITMPEMDGIEALKEIKKIDPNA---K 75
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1823315871 897 LVMTTRAGeKHQRL--AFQLGADDYFTKPVNEALLLRRL 933
Cdd:cd17542    76 VIMCSAMG-QEEMVkeAIKAGAKDFIVKPFQPERVLEAV 113
REC_RegA-like cd17563
phosphoacceptor receiver (REC) domain of photosynthetic apparatus regulatory protein RegA; ...
819-925 1.56e-13

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: 67.85  E-value: 1.56e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823315871 819 QRLLLVDDSLSVRRLVGRMLERGGYQVVTASDGQEALDLLQQDAdFGAVVTDLEMPRVNGYELLSAVRARPATAGLPML- 897
Cdd:cd17563     1 KSLLLVDDDEVFAERLARALERRGFEVETAHSVEEALALAREEK-PDYAVLDLRLGGDSGLDLIPPLRALQPDARIVVLt 79
                          90       100       110
                  ....*....|....*....|....*....|..
gi 1823315871 898 ----VMTTRAgekhqrlAFQLGADDYFTKPVN 925
Cdd:cd17563    80 gyasIATAVE-------AIKLGADDYLAKPAD 104
REC_OmpR_CusR-like cd19935
phosphoacceptor receiver (REC) domain of CusR-like OmpR family response regulators; ...
821-923 2.50e-13

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


Pssm-ID: 381162 [Multi-domain]  Cd Length: 100  Bit Score: 66.69  E-value: 2.50e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823315871 821 LLLVDDSLSVRRLVGRMLERGGYQVVTASDGQEALDLLQQdADFGAVVTDLEMPRVNGYELLSAVRARPATagLPMLVMT 900
Cdd:cd19935     1 ILVVEDEKKLAEYLKKGLTEEGYAVDVAYDGEDGLHLALT-NEYDLIILDVMLPGLDGLEVLRRLRAAGKQ--TPVLMLT 77
                          90       100
                  ....*....|....*....|...
gi 1823315871 901 TRAGEKHQRLAFQLGADDYFTKP 923
Cdd:cd19935    78 ARDSVEDRVKGLDLGADDYLVKP 100
REC_OmpR_CtrA cd17616
phosphoacceptor receiver (REC) domain of CtrA-like OmpR family response regulators; CtrA is ...
821-933 3.00e-13

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


Pssm-ID: 381132 [Multi-domain]  Cd Length: 114  Bit Score: 67.05  E-value: 3.00e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823315871 821 LLLVDDSLSVRRLVGRMLERGGYQVVTASDGQEALDLLQQdADFGAVVTDLEMPRVNGYELLSAVRArpATAGLPMLVMT 900
Cdd:cd17616     1 VLLIEDDSATAQSIELMLKSEGFNVYTTDLGEEGLDLGKL-YDYDIILLDLNLPDMSGYEVLRTLRL--AKVKTPILILS 77
                          90       100       110
                  ....*....|....*....|....*....|...
gi 1823315871 901 TRAGEKHQRLAFQLGADDYFTKPVNEALLLRRL 933
Cdd:cd17616    78 GLADIEDKVKGLGFGADDYMTKPFHKDELVARI 110
BaeS COG0642
Signal transduction histidine kinase [Signal transduction mechanisms];
337-662 3.24e-13

Signal transduction histidine kinase [Signal transduction mechanisms];


Pssm-ID: 440407 [Multi-domain]  Cd Length: 328  Bit Score: 71.86  E-value: 3.24e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823315871 337 IRVPAARLEGLMDQLGELVTARARMTQLLSRLDELQGSMTASQERFQRTVRDFEERYLNPDMVREEGAAPTTRMGGLDLS 416
Cdd:COG0642    10 LLLLLLLLLLLALLLLLLLLLLLALLLLLALLLLLLLLLLLLLLLALALLALLLLLLLLLLLLLLLLLLLLLLLLLLLLL 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823315871 417 QQFAELEFDTYNDLNILSRSITELSADFA-------------------EVRRRLSDTAAELSEENEQLGKLVRRL----R 473
Cdd:COG0642    90 LLLLLLLLALLLLLEEANEAKSRFLANVShelrtpltairgylellleELDEEQREYLETILRSADRLLRLINDLldlsR 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823315871 474 LDVNQTS--RVAFS------QTTARLRRWAREQQADLTLQVEGEDVLIES--GILQRIsdpLLHLLTNAAYHGlasesae 543
Cdd:COG0642   170 LEAGKLElePEPVDlaelleEVVELFRPLAEEKGIELELDLPDDLPTVRGdpDRLRQV---LLNLLSNAIKYT------- 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823315871 544 srraagkNPQGTVWIRAAEQGNFLEVTVADDGQGLDyARIRERALERglrsaqeleqlssdelgrlillpgFSTAREVGN 623
Cdd:COG0642   240 -------PEGGTVTVSVRREGDRVRISVEDTGPGIP-PEDLERIFEP------------------------FFRTDPSRR 287
                         330       340       350
                  ....*....|....*....|....*....|....*....
gi 1823315871 624 VAGRGVGLDVVATAVRQLGGELLISSERGVGTAFTLRVP 662
Cdd:COG0642   288 GGGTGLGLAIVKRIVELHGGTIEVESEPGKGTTFTVTLP 326
LytT COG3279
DNA-binding response regulator, LytR/AlgR family [Transcription, Signal transduction ...
820-942 3.66e-13

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


Pssm-ID: 442510 [Multi-domain]  Cd Length: 235  Bit Score: 69.85  E-value: 3.66e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823315871 820 RLLLVDDSLSVRRLVGRMLER-GGYQVV-TASDGQEALDLLQQDaDFGAVVTDLEMPRVNGYELLSAVRARPATaglPML 897
Cdd:COG3279     3 KILIVDDEPLARERLERLLEKyPDLEVVgEASNGEEALELLEEH-KPDLVFLDIQMPGLDGFELARQLRELDPP---PPI 78
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1823315871 898 VMTTrAGEKHQRLAFQLGADDYFTKPVNEALLLRRLGTLQQAQQA 942
Cdd:COG3279    79 IFTT-AYDEYALEAFEVNAVDYLLKPIDEERLAKALEKAKERLEA 122
REC_OmpR_MtPhoP-like cd17615
phosphoacceptor receiver (REC) domain of MtPhoP-like OmpR family response regulators; ...
820-936 4.01e-13

phosphoacceptor receiver (REC) domain of MtPhoP-like OmpR family response regulators; Mycobacterium tuberculosis PhoP (MtPhoP) is part of the PhoP/PhoR two-component system that is involved in phosphate control by stimulating expression of genes involved in scavenging, transport and mobilization of phosphate, and repressing the utilization of nitrogen sources. Also included in this subfamily is Mycobacterium tuberculosis transcriptional regulatory protein TcrX, part of the two-component regulatory system TcrY/TcrX that may be involved in virulence. Members of this subfamily belong to the OmpR family of DNA-binding response regulators, which are characterized by a REC domain and a winged helix-turn-helix (wHTH) DNA-binding output effector domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381131 [Multi-domain]  Cd Length: 118  Bit Score: 66.61  E-value: 4.01e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823315871 820 RLLLVDDSLSVRRLVGRMLERGGYQVVTASDGQEALDLLQQDADfGAVVTDLEMPRVNGYELLSAVRArpATAGLPMLVM 899
Cdd:cd17615     1 RVLVVDDEPNITELLSMALRYEGWDVETAADGAEALAAAREFRP-DAVVLDIMLPDMDGLEVLRRLRA--DGPDVPVLFL 77
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1823315871 900 TTRAGEKHQRLAFQLGADDYFTKPVNEALLLRRLGTL 936
Cdd:cd17615    78 TAKDSVEDRIAGLTAGGDDYVTKPFSLEEVVARLRAL 114
PRK15347 PRK15347
two component system sensor kinase;
552-940 4.47e-13

two component system sensor kinase;


Pssm-ID: 237951 [Multi-domain]  Cd Length: 921  Bit Score: 73.52  E-value: 4.47e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823315871 552 PQGTVWIRAAEQGNFLEVTVADDGQGLDYARIREralerglrsaqeleqlssdelgrlILLPGFSTArevGNVAGRGVGL 631
Cdd:PRK15347  530 ETGGIRLRVKRHEQQLCFTVEDTGCGIDIQQQQQ------------------------IFTPFYQAD---THSQGTGLGL 582
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823315871 632 DVVATAVRQLGGELLISSERGVGTAFTLRVPTTQrimdvlhldlgagHHAALPV-GSVrslrDVPLGdLRRddgQLWLdf 710
Cdd:PRK15347  583 TIASSLAKMMGGELTLFSTPGVGSCFSLVLPLNE-------------YAPPEPLkGEL----SAPLA-LHR---QLSA-- 639
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823315871 711 ggqpvpvvdarpiWGHAPQDTDTEAHLAvvssisgllalrvhdfgdieevavtAPSgllapLDYLAGmavsgtgqvlail 790
Cdd:PRK15347  640 -------------WGITCQPGHQNPALL-------------------------DPE-----LAYLPG------------- 663
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823315871 791 dpagvlRLSRRpatwlgqAQRQVQATGNQ------------RLLLVDDSLSVRRLVGRMLERGGYQVVTASDGQEALDLL 858
Cdd:PRK15347  664 ------RLYDL-------LQQIIQGAPNEpvinlplqpwqlQILLVDDVETNRDIIGMMLVELGQQVTTAASGTEALELG 730
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823315871 859 QQdADFGAVVTDLEMPRVNGYELLSAVRARPAT--AGLPMLVMTTRAG-EKHQRLAfQLGADDYFTKPVNEALLLRRLGT 935
Cdd:PRK15347  731 RQ-HRFDLVLMDIRMPGLDGLETTQLWRDDPNNldPDCMIVALTANAApEEIHRCK-KAGMNHYLTKPVTLAQLARALEL 808

                  ....*
gi 1823315871 936 LQQAQ 940
Cdd:PRK15347  809 AAEYQ 813
REC_ETR-like cd19933
phosphoacceptor receiver (REC) domain of plant ethylene receptors ETR1, ETR2, and EIN4, and ...
820-924 4.73e-13

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: 66.65  E-value: 4.73e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823315871 820 RLLLVDDSLSVRRLVGRMLERGGYQVVTASDGQEALDLLQQ-DADFGAVVTDLEMPRVNGYELLSAVRARPATAGLPMLV 898
Cdd:cd19933     2 KVLLVDDNAVNRMVTKGLLEKLGCEVTTVSSGEECLNLLASaEHSFQLVLLDLCMPEMDGFEVALRIRKLFGRRERPLIV 81
                          90       100
                  ....*....|....*....|....*..
gi 1823315871 899 MTTRAGEKHQR-LAFQLGADDYFTKPV 924
Cdd:cd19933    82 ALTANTDDSTReKCLSLGMNGVITKPV 108
REC_FixJ cd17537
phosphoacceptor receiver (REC) domain of FixJ family response regulators; FixJ family response ...
823-933 4.86e-13

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


Pssm-ID: 381092 [Multi-domain]  Cd Length: 116  Bit Score: 66.46  E-value: 4.86e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823315871 823 LVDDSLSVRRLVGRMLERGGYQVVTASDGQEALDLLQQDaDFGAVVTDLEMPRVNGYELLSAVRARPATagLPMLVMTTR 902
Cdd:cd17537     5 VVDDDEAVRDSLAFLLRSVGLAVKTFTSASAFLAAAPPD-QPGCLVLDVRMPGMSGLELQDELLARGSN--IPIIFITGH 81
                          90       100       110
                  ....*....|....*....|....*....|.
gi 1823315871 903 AGEKHQRLAFQLGADDYFTKPVNEALLLRRL 933
Cdd:cd17537    82 GDVPMAVEAMKAGAVDFLEKPFRDQVLLDAI 112
REC smart00448
cheY-homologous receiver domain; CheY regulates the clockwise rotation of E. coli flagellar ...
820-874 5.37e-13

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: 64.13  E-value: 5.37e-13
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1823315871  820 RLLLVDDSLSVRRLVGRMLERGGYQVVTASDGQEALDLLQQDaDFGAVVTDLEMP 874
Cdd:smart00448   2 RILVVDDDPLLRELLKALLEKEGYEVDEATDGEEALELLKEE-KPDLILLDIMMP 55
REC_OmpR_PmrA-like cd17624
phosphoacceptor receiver (REC) domain of PmrA-like OmpR family response regulators; This ...
821-923 5.91e-13

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: 65.97  E-value: 5.91e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823315871 821 LLLVDDSLSVRRLVGRMLERGGYQVVTASDGQEALDLLQQdADFGAVVTDLEMPRVNGYELLSAVRARPATagLPMLVMT 900
Cdd:cd17624     1 ILLVEDDALLGDGLKTGLRKAGYAVDWVRTGAEAEAALAS-GPYDLVILDLGLPDGDGLDLLRRWRRQGQS--LPVLILT 77
                          90       100
                  ....*....|....*....|....
gi 1823315871 901 TRAGEkHQRLA-FQLGADDYFTKP 923
Cdd:cd17624    78 ARDGV-DDRVAgLDAGADDYLVKP 100
COG4191 COG4191
Signal transduction histidine kinase regulating C4-dicarboxylate transport system [Signal ...
433-662 7.70e-13

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


Pssm-ID: 443345 [Multi-domain]  Cd Length: 361  Bit Score: 70.98  E-value: 7.70e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823315871 433 LSRSITELSADFAEVRRRLSDTAAELseenEQLGKLVRRLR------------LDVNQtsrvAFSQTTARLRRWAREQQA 500
Cdd:COG4191   166 LLRRRLEDEPDPEELREALERILEGA----ERAAEIVRSLRafsrrdeeerepVDLNE----LIDEALELLRPRLKARGI 237
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823315871 501 DLTLQVEGEDVLIE--SGILQRIsdpLLHLLTNAAYhglasesaesrrAAGKNPQGTVWIRAAEQGNFLEVTVADDGQGL 578
Cdd:COG4191   238 EVELDLPPDLPPVLgdPGQLEQV---LLNLLINAID------------AMEEGEGGRITISTRREGDYVVISVRDNGPGI 302
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823315871 579 DyARIRERALErglrsaqeleqlssdelgrlillPGFSTaREVGNvaGRGVGLDVVATAVRQLGGELLISSERGVGTAFT 658
Cdd:COG4191   303 P-PEVLERIFE-----------------------PFFTT-KPVGK--GTGLGLSISYGIVEKHGGRIEVESEPGGGTTFT 355

                  ....
gi 1823315871 659 LRVP 662
Cdd:COG4191   356 ITLP 359
PRK11361 PRK11361
acetoacetate metabolism transcriptional regulator AtoC;
819-945 1.03e-12

acetoacetate metabolism transcriptional regulator AtoC;


Pssm-ID: 183099 [Multi-domain]  Cd Length: 457  Bit Score: 71.42  E-value: 1.03e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823315871 819 QRLLLVDDSLSVRRLVGRMLERGGYQVVTASDGQEALDLLqQDADFGAVVTDLEMPRVNGYELLSAVRARpaTAGLPMLV 898
Cdd:PRK11361    5 NRILIVDDEDNVRRMLSTAFALQGFETHCANNGRTALHLF-ADIHPDVVLMDIRMPEMDGIKALKEMRSH--ETRTPVIL 81
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1823315871 899 MTTRAGEKHQRLAFQLGADDYFTKPVNEA---LLLRRLGTLQQAQQAGVS 945
Cdd:PRK11361   82 MTAYAEVETAVEALRCGAFDYVIKPFDLDelnLIVQRALQLQSMKKEIRH 131
REC_OmpR_EcPhoP-like cd19934
phosphoacceptor receiver (REC) domain of EcPhoP-like OmpR family response regulators; ...
821-936 1.60e-12

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


Pssm-ID: 381161 [Multi-domain]  Cd Length: 117  Bit Score: 65.00  E-value: 1.60e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823315871 821 LLLVDDSLSVRRLVGRMLERGGYQVVTASDGQEALDLLQQDAdFGAVVTDLEMPRVNGYELLSavRARPATAGLPMLVMT 900
Cdd:cd19934     1 LLLVEDDALLAAQLKEQLSDAGYVVDVAEDGEEALFQGEEEP-YDLVVLDLGLPGMDGLSVLR--RWRSEGRATPVLILT 77
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1823315871 901 TRAGEKHQRLAFQLGADDYFTKPVNEALLLRRLGTL 936
Cdd:cd19934    78 ARDSWQDKVEGLDAGADDYLTKPFHIEELLARLRAL 113
PLN03029 PLN03029
type-a response regulator protein; Provisional
821-931 1.96e-12

type-a response regulator protein; Provisional


Pssm-ID: 215544 [Multi-domain]  Cd Length: 222  Bit Score: 67.75  E-value: 1.96e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823315871 821 LLLVDDSLSVRRLVGRMLERGGYQVVTASDGQEALDLL-------------------QQDADFGAVVTDLEMPRVNGYEL 881
Cdd:PLN03029   11 VLAVDDSLIDRKLIEKLLKTSSYQVTTVDSGSKALKFLglheddrsnpdtpsvspnsHQEVEVNLIITDYCMPGMTGYDL 90
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1823315871 882 LSAVRARPATAGLPMLVMTTRAGEKHQRLAFQLGADDYFTKPVNEALLLR 931
Cdd:PLN03029   91 LKKIKESSSLRNIPVVIMSSENVPSRITRCLEEGAEEFFLKPVQLSDLNR 140
REC_OmpR_NsrR-like cd18159
phosphoacceptor receiver (REC) domain of Streptococcus agalactiae NsrR-like OmpR family ...
821-933 3.16e-12

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: 63.84  E-value: 3.16e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823315871 821 LLLVDDSLSVRRLVGRMLERGGYQVVTASDGQEALD-LLQQDADFgaVVTDLEMPRVNGYELLSAVRARpatAGLPMLVM 899
Cdd:cd18159     1 ILIVEDDETIASLLKKHLEKWGYEVVLIEDFEDVLEeFLQFKPDL--VLLDINLPYFDGFYWCREIRQI---SNVPIIFI 75
                          90       100       110
                  ....*....|....*....|....*....|....
gi 1823315871 900 TTRAGEKHQRLAFQLGADDYFTKPVNEALLLRRL 933
Cdd:cd18159    76 SSRDDNMDQVMAINMGGDDYITKPFDLDVLLAKI 109
REC_CpdR_CckA-like cd18160
phosphoacceptor receiver (REC) domain of Brucella abortus CpdR and CckA, and similar domains; ...
820-923 3.31e-12

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: 63.68  E-value: 3.31e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823315871 820 RLLLVDDSLSVRRLVGRMLERGGYQVVTASDGQEALDLLQQDADFGAVVTDLEMPRVNGYELlsAVRARPATAGLPMLVM 899
Cdd:cd18160     1 TILLADDEPSVRKFIVTTLKKAGYAVTEAESGAEALEKLQQGKDIDIVVTDIVMPEMDGIEL--AREARKIDPDVKILFI 78
                          90       100
                  ....*....|....*....|....
gi 1823315871 900 TTRAGEKHQRLAFQLGADDYFTKP 923
Cdd:cd18160    79 SGGAAAAPELLSDAVGDNATLKKP 102
pleD PRK09581
response regulator PleD; Reviewed
820-936 5.58e-12

response regulator PleD; Reviewed


Pssm-ID: 236577 [Multi-domain]  Cd Length: 457  Bit Score: 69.16  E-value: 5.58e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823315871 820 RLLLVDDSLSVRRLVGRMLERGGYQVVTASDGQEALDLLQQDA-DFgaVVTDLEMPRVNGYELLSAVRARPATAGLPmLV 898
Cdd:PRK09581    4 RILVVDDIPANVKLLEAKLLAEYYTVLTASSGAEAIAICEREQpDI--ILLDVMMPGMDGFEVCRRLKSDPATTHIP-VV 80
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1823315871 899 MTTRAGEKHQRLA-FQLGADDYFTKPVNEALLLRRLGTL 936
Cdd:PRK09581   81 MVTALDDPEDRVRgLEAGADDFLTKPINDVALFARVKSL 119
REC_NtrX-like cd17550
phosphoacceptor receiver (REC) domain of nitrogen assimilation regulatory protein NtrX and ...
821-939 5.63e-12

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: 63.28  E-value: 5.63e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823315871 821 LLLVDDSLSVRRLVGRMLERGGYQVVTASDGQEALDLLQQDAdFGAVVTDLEMPRVNGYELLSAVRARpaTAGLPMLVMT 900
Cdd:cd17550     1 ILIVDDEEDIRESLSGILEDEGYEVDTAADGEEALKLIKERR-PDLVLLDIWLPDMDGLELLKEIKEK--YPDLPVIMIS 77
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1823315871 901 TRAGEKHQRLAFQLGADDYFTKPVN-EALLLrrlgTLQQA 939
Cdd:cd17550    78 GHGTIETAVKATKLGAYDFIEKPLSlDRLLL----TIERA 113
PRK15115 PRK15115
response regulator GlrR; Provisional
820-943 1.31e-11

response regulator GlrR; Provisional


Pssm-ID: 185070 [Multi-domain]  Cd Length: 444  Bit Score: 67.94  E-value: 1.31e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823315871 820 RLLLVDDSLSVRRLVGRMLERGGYQVVTASDGQEALDLLQQDaDFGAVVTDLEMPRVNGYELLSAVRARpaTAGLPMLVM 899
Cdd:PRK15115    7 HLLLVDDDPGLLKLLGMRLTSEGYSVVTAESGQEALRVLNRE-KVDLVISDLRMDEMDGMQLFAEIQKV--QPGMPVIIL 83
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1823315871 900 TTRAGEKHQRLAFQLGADDYFTKPVNEALLLRRL-GTLQQAQQAG 943
Cdd:PRK15115   84 TAHGSIPDAVAATQQGVFSFLTKPVDRDALYKAIdDALEQSAPAT 128
REC_OmpR_VirG cd17594
phosphoacceptor receiver (REC) domain of VirG-like OmpR family response regulators; VirG is ...
822-933 1.35e-11

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: 62.08  E-value: 1.35e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823315871 822 LLVDDSLSVRRLVGRMLERGGYQVVTASDGQEALDLLQQDAdFGAVVTDLEMPRVNGYELLSAVRARpatAGLPMLVMTT 901
Cdd:cd17594     3 LVVDDDAAMRHLLILYLRERGFDVTAAADGAEEARLMLHRR-VDLVLLDLRLGQESGLDLLRTIRAR---SDVPIIIISG 78
                          90       100       110
                  ....*....|....*....|....*....|...
gi 1823315871 902 RAGEKHQR-LAFQLGADDYFTKPVNEALLLRRL 933
Cdd:cd17594    79 DRRDEIDRvVGLELGADDYLAKPFGLRELLARV 111
ompR PRK09468
osmolarity response regulator; Provisional
818-933 1.44e-11

osmolarity response regulator; Provisional


Pssm-ID: 181883 [Multi-domain]  Cd Length: 239  Bit Score: 65.38  E-value: 1.44e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823315871 818 NQRLLLVDDSLSVRRLVGRMLERGGYQVVTASDGqEALDLLQQDADFGAVVTDLEMPRVNGyelLSAV-RARPATAGLPM 896
Cdd:PRK09468    5 NYKILVVDDDMRLRALLERYLTEQGFQVRSAANA-EQMDRLLTRESFHLMVLDLMLPGEDG---LSICrRLRSQNNPTPI 80
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1823315871 897 LVMTTRAGEKHQRLAFQLGADDYFTKPVNEALLLRRL 933
Cdd:PRK09468   81 IMLTAKGEEVDRIVGLEIGADDYLPKPFNPRELLARI 117
REC_OmpR_ArcA_TorR-like cd17619
phosphoacceptor receiver (REC) domain of ArcA- and TorR-like OmpR family response regulators; ...
820-932 2.51e-11

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


Pssm-ID: 381134 [Multi-domain]  Cd Length: 113  Bit Score: 61.63  E-value: 2.51e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823315871 820 RLLLVDDSLSVRRLVGRMLERGGYQVVTASDGQEALDLLQQdADFGAVVTDLEMPRVNGYELLSAVRARpatAGLPMLVM 899
Cdd:cd17619     2 HILIVEDEPVTRATLKSYFEQEGYDVSEAGDGEEMRQILAR-QDIDLVLLDINLPGKDGLSLTRELREQ---SEVGIILV 77
                          90       100       110
                  ....*....|....*....|....*....|...
gi 1823315871 900 TTRAGEKHQRLAFQLGADDYFTKPVNEALLLRR 932
Cdd:cd17619    78 TGRDDEVDRIVGLEIGADDYVTKPFNPRELLVR 110
CitA COG3290
Sensor histidine kinase DipB regulating citrate/malate metabolism [Signal transduction ...
495-662 3.14e-11

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


Pssm-ID: 442519 [Multi-domain]  Cd Length: 389  Bit Score: 66.41  E-value: 3.14e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823315871 495 AREQQADLTLQVEG--EDVLIESGILQRIsdpLLHLLTNAAYHGLASEsaesrraagkNPQGTVWIRAAEQGNFLEVTVA 572
Cdd:COG3290   257 ARERGIDLTIDIDSdlPDLPLSDTDLVTI---LGNLLDNAIEAVEKLP----------EEERRVELSIRDDGDELVIEVE 323
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823315871 573 DDGQGLDyARIRERALERGlrsaqeleqlssdelgrlillpgFSTAREvgnvAGRGVGLDVVATAVRQLGGELLISSERG 652
Cdd:COG3290   324 DSGPGIP-EELLEKIFERG-----------------------FSTKLG----EGRGLGLALVKQIVEKYGGTIEVESEEG 375
                         170
                  ....*....|
gi 1823315871 653 VGTAFTLRVP 662
Cdd:COG3290   376 EGTVFTVRLP 385
REC_NarL-like cd17535
phosphoacceptor receiver (REC) domain of NarL (Nitrate/Nitrite response regulator L) family ...
822-933 3.15e-11

phosphoacceptor receiver (REC) domain of NarL (Nitrate/Nitrite response regulator L) family response regulators; The NarL family is one of the more abundant families of DNA-binding response regulators (RRs). Members of the NarL family contain a REC domain and a helix-turn-helix (HTH) DNA-binding output domain, with a majority of members containing a LuxR-type HTH domain. They function as transcriptional regulators. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381090 [Multi-domain]  Cd Length: 117  Bit Score: 61.37  E-value: 3.15e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823315871 822 LLVDDSLSVRRLVGRMLER-GGYQVV-TASDGQEALDLLQQdADFGAVVTDLEMPRVNGYELLSAVRARPatAGLPMLVM 899
Cdd:cd17535     2 LIVDDHPLVREGLRRLLESePDIEVVgEAADGEEALALLRE-LRPDVVLMDLSMPGMDGIEALRRLRRRY--PDLKVIVL 78
                          90       100       110
                  ....*....|....*....|....*....|....
gi 1823315871 900 TTRAGEKHQRLAFQLGADDYFTKPVNEALLLRRL 933
Cdd:cd17535    79 TAHDDPEYVLRALKAGAAGYLLKDSSPEELIEAI 112
REC_hyHK_blue-like cd18161
phosphoacceptor receiver (REC) domain of hybrid sensor histidine kinase/response regulators ...
822-924 4.09e-11

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: 60.44  E-value: 4.09e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823315871 822 LLVDDSLSVRRLVGRMLERGGYQVVTASDGQEALDLLQQDADFGAVVTDLEMPR-VNGYELLSAVRA-RPataGLPMLVM 899
Cdd:cd18161     2 LVVEDDPDVRRLTAEVLEDLGYTVLEAASGDEALDLLESGPDIDLLVTDVIMPGgMNGSQLAEEARRrRP---DLKVLLT 78
                          90       100
                  ....*....|....*....|....*..
gi 1823315871 900 T--TRAGEKHQRLAFQLgadDYFTKPV 924
Cdd:cd18161    79 SgyAENAIEGGDLAPGV---DVLSKPF 102
resp_reg_YycF NF040534
response regulator YycF;
819-944 4.35e-11

response regulator YycF;


Pssm-ID: 439744 [Multi-domain]  Cd Length: 231  Bit Score: 63.97  E-value: 4.35e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823315871 819 QRLLLVDDSLSVRRLVGRMLERGGYQVVTASDGQEALDL-LQQDADFgaVVTDLEMPRVNGYELLSAVRArpaTAGLPML 897
Cdd:NF040534    1 KKILVVDDEKPIADILEFNLKKEGYEVFCAYDGNEALELvEEEVPDL--VLLDIMLPGRDGMEVCREVRK---KYDMPII 75
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1823315871 898 VMTTRAGEKHQRLAFQLGADDYFTKPV-NEALLLRRLGTLQQAQQAGV 944
Cdd:NF040534   76 MLTAKDSEIDKVLGLELGADDYVTKPFsTRELIARVKANLRRHQQQNT 123
REC_OmpR_KdpE-like cd17620
phosphoacceptor receiver (REC) domain of KdpE-like OmpR family response regulators; KdpE is a ...
822-923 5.52e-11

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: 59.87  E-value: 5.52e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823315871 822 LLVDDSLSVRRLVGRMLERGGYQVVTASDGQEALDLL-QQDADFgaVVTDLEMPRVNGYELLSAVRarpATAGLPMLVMT 900
Cdd:cd17620     2 LVIEDEPQIRRFLRTALEAHGYRVFEAETGQEGLLEAaTRKPDL--IILDLGLPDMDGLEVIRRLR---EWSAVPVIVLS 76
                          90       100
                  ....*....|....*....|...
gi 1823315871 901 TRAGEKHQRLAFQLGADDYFTKP 923
Cdd:cd17620    77 ARDEESDKIAALDAGADDYLTKP 99
PRK10841 PRK10841
two-component system sensor histidine kinase RcsC;
623-939 5.70e-11

two-component system sensor histidine kinase RcsC;


Pssm-ID: 182772 [Multi-domain]  Cd Length: 924  Bit Score: 66.54  E-value: 5.70e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823315871 623 NVAGRGVGLDVVATAVRQLGGELLISSERGVGTAFTLRVP------TTQRIMDVLH-----LDLgagHHAALPVGSVRSL 691
Cdd:PRK10841  627 NFQGTGLGLAICEKLINMMDGDISVDSEPGMGSQFTIRIPlygaqyPQKKGVEGLQgkrcwLAV---RNASLEQFLETLL 703
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823315871 692 RDVPLGDLRRDDGQLwldfGGQPVPVVDarpiwghapQDTDTEAHLAVVSSISGllalrvHDFGDIEEVA-------VTA 764
Cdd:PRK10841  704 QRSGIQVQRYEGQEP----TPEDVLITD---------DPVQKKWQGRAVITFCR------RHIGIPLEIApgewvhsTAT 764
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823315871 765 PSGLLAPLD--YLAGMAVSGTGQVLaildpagvlrlsrrPATwlgqaQRQVQATGNQRLLLVDDSLSVRRLVGRMLERGG 842
Cdd:PRK10841  765 PHELPALLAriYRIELESDDSANAL--------------PST-----DKAVSDNDDMMILVVDDHPINRRLLADQLGSLG 825
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823315871 843 YQVVTASDGQEALDLLQQDA-DFgaVVTDLEMPRVNGYELLSAVRARPATagLPMLVMTTRA-GEKHQRlAFQLGADDYF 920
Cdd:PRK10841  826 YQCKTANDGVDALNVLSKNHiDI--VLTDVNMPNMDGYRLTQRLRQLGLT--LPVIGVTANAlAEEKQR-CLEAGMDSCL 900
                         330
                  ....*....|....*....
gi 1823315871 921 TKPVNealllrrLGTLQQA 939
Cdd:PRK10841  901 SKPVT-------LDVLKQT 912
HATPase_c pfam02518
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the ...
518-665 9.58e-11

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


Pssm-ID: 460579 [Multi-domain]  Cd Length: 109  Bit Score: 59.69  E-value: 9.58e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823315871 518 LQRIsdpLLHLLTNAAyhglasesaesrRAAGKNPQGTVWIraaEQGNFLEVTVADDGQGLDYARIREralerglrsaqe 597
Cdd:pfam02518   6 LRQV---LSNLLDNAL------------KHAAKAGEITVTL---SEGGELTLTVEDNGIGIPPEDLPR------------ 55
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1823315871 598 leqlssdelgrliLLPGFSTAREVGnVAGRGVGLDVVATAVRQLGGELLISSERGVGTAFTLRVPTTQ 665
Cdd:pfam02518  56 -------------IFEPFSTADKRG-GGGTGLGLSIVRKLVELLGGTITVESEPGGGTTVTLTLPLAQ 109
REC_OmpR_RegX3-like cd17621
phosphoacceptor receiver (REC) domain of RegX3-like OmpR family response regulators; RegX3 is ...
821-923 1.12e-10

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


Pssm-ID: 381136 [Multi-domain]  Cd Length: 99  Bit Score: 59.13  E-value: 1.12e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823315871 821 LLLVDDSLSVRRLVGRMLERGGYQVVTASDGQEALDLLQQD-ADFgaVVTDLEMPRVNGYELLSAVRARpatAGLPMLVM 899
Cdd:cd17621     1 VLVVEDEESFSDPLAYLLRKEGFEVTVATDGPAALAEFDRAgADI--VLLDLMLPGLSGTEVCRQLRAR---SNVPVIMV 75
                          90       100
                  ....*....|....*....|....
gi 1823315871 900 TTRAGEKHQRLAFQLGADDYFTKP 923
Cdd:cd17621    76 TAKDSEIDKVVGLELGADDYVTKP 99
psREC_PRR cd17582
pseudo receiver domain of pseudo-response regulators; In Arabidopsis, five pseudo-response ...
821-923 1.36e-10

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: 58.95  E-value: 1.36e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823315871 821 LLLVDDSLSVRRLVGRMLERGGYQVVTASDGQEALDLLQQDA-DFGAVVTDLEMPRVNGYELLSAVRARPATAGLPMLVM 899
Cdd:cd17582     1 VLLVENDDSTRQIVTALLRKCSYEVTAASDGLQAWDVLEDEQnEIDLILTEVDLPVSSGFKLLSYIMRHKICKNIPVIMM 80
                          90       100
                  ....*....|....*....|....
gi 1823315871 900 TTRAGEKHQRLAFQLGADDYFTKP 923
Cdd:cd17582    81 SSQDSVGVVFKCLSKGAADYLVKP 104
REC_NtrC1-like cd17572
phosphoacceptor receiver (REC) domain of nitrogen regulatory protein C 1 (NtrC1) from Aquifex ...
821-933 1.61e-10

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: 59.52  E-value: 1.61e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823315871 821 LLLVDDSLSVRRLVGRMLERGGYQVVTASDGQEALDLLQQDAdFGAVVTDLEMPRVNGYELLSAVRARPATAglPMLVMT 900
Cdd:cd17572     1 VLLVEDSPSLAALYQEYLSDEGYKVTHVETGKEALAFLSDQP-PDVVLLDLKLPDMSGMEILKWIQERSLPT--SVIVIT 77
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1823315871 901 TRAGEKHQRLAFQLGADDYFTKP---------VNEALLLRRL 933
Cdd:cd17572    78 AHGSVDIAVEAMRLGAYDFLEKPfdadrlrvtVRNALKHRKL 119
PRK09836 PRK09836
DNA-binding transcriptional activator CusR; Provisional
820-936 1.75e-10

DNA-binding transcriptional activator CusR; Provisional


Pssm-ID: 182102 [Multi-domain]  Cd Length: 227  Bit Score: 61.86  E-value: 1.75e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823315871 820 RLLLVDDSLSVRRLVGRMLERGGYQVVTASDGQEALDLlQQDADFGAVVTDLEMPRVNGYELLSAVRArpATAGLPMLVM 899
Cdd:PRK09836    2 KLLIVEDEKKTGEYLTKGLTEAGFVVDLADNGLNGYHL-AMTGDYDLIILDIMLPDVNGWDIVRMLRS--ANKGMPILLL 78
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1823315871 900 TTRAGEKHQRLAFQLGADDYFTKPVNEALLLRRLGTL 936
Cdd:PRK09836   79 TALGTIEHRVKGLELGADDYLVKPFAFAELLARVRTL 115
AmiR COG3707
Two-component response regulator, AmiR/NasT family, consists of REC and RNA-binding ...
820-930 1.91e-10

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


Pssm-ID: 442921 [Multi-domain]  Cd Length: 194  Bit Score: 61.13  E-value: 1.91e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823315871 820 RLLLVDDSLSVRRLVGRMLERGGYQVVT-ASDGQEALDLLQQdADFGAVVTDLEMPRVNGYELLSAVRARPAtagLPMLV 898
Cdd:COG3707     5 RVLVVDDEPLRRADLREGLREAGYEVVAeAADGEDAVELVRE-LKPDLVIVDIDMPDRDGLEAARQISEERP---APVIL 80
                          90       100       110
                  ....*....|....*....|....*....|..
gi 1823315871 899 MTTRAGEKHQRLAFQLGADDYFTKPVNEALLL 930
Cdd:COG3707    81 LTAYSDPELIERALEAGVSAYLVKPLDPEDLL 112
PRK00742 PRK00742
chemotaxis-specific protein-glutamate methyltransferase CheB;
820-923 2.48e-10

chemotaxis-specific protein-glutamate methyltransferase CheB;


Pssm-ID: 234828 [Multi-domain]  Cd Length: 354  Bit Score: 63.25  E-value: 2.48e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823315871 820 RLLLVDDSLSVRRLVGRMLER-GGYQVV-TASDGQEALDLLQQ---DadfgaVVT-DLEMPRVNGyelLSAV----RARP 889
Cdd:PRK00742    5 RVLVVDDSAFMRRLISEILNSdPDIEVVgTAPDGLEAREKIKKlnpD-----VITlDVEMPVMDG---LDALekimRLRP 76
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1823315871 890 atagLPmLVM---TTRAGEKHQRLAFQLGADDYFTKP 923
Cdd:PRK00742   77 ----TP-VVMvssLTERGAEITLRALELGAVDFVTKP 108
REC_PatA-like cd17602
phosphoacceptor receiver (REC) domain of PatA and similar domains; Nostoc sp. (or Anabaena sp.) ...
824-923 2.59e-10

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: 58.15  E-value: 2.59e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823315871 824 VDDSLSVRRLVGRMLERGGYQVVTASDGQEAL-DLLQQDADFgaVVTDLEMPRVNGYELLSAVRARPATAGLPMLVMTTR 902
Cdd:cd17602     4 VDDRPSIQKMIEYFLEKQGFRVVVIDDPLRALtTLLNSKPDL--ILIDIDMPDLDGYELCSLLRKSSALKDTPIIMLTGK 81
                          90       100
                  ....*....|....*....|.
gi 1823315871 903 AGEKHQRLAFQLGADDYFTKP 923
Cdd:cd17602    82 DGLVDRIRAKMAGASGYLTKP 102
PRK11517 PRK11517
DNA-binding response regulator HprR;
820-933 2.94e-10

DNA-binding response regulator HprR;


Pssm-ID: 183172 [Multi-domain]  Cd Length: 223  Bit Score: 61.45  E-value: 2.94e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823315871 820 RLLLVDDSLSVRRLVGRMLERGGYQVVTASDGQEALDLLQQDaDFGAVVTDLEMPRVNGYELLSAVRARPATaglPMLVM 899
Cdd:PRK11517    2 KILLIEDNQRTQEWVTQGLSEAGYVIDAVSDGRDGLYLALKD-DYALIILDIMLPGMDGWQILQTLRTAKQT---PVICL 77
                          90       100       110
                  ....*....|....*....|....*....|....
gi 1823315871 900 TTRAGEKHQRLAFQLGADDYFTKPVNEALLLRRL 933
Cdd:PRK11517   78 TARDSVDDRVRGLDSGANDYLVKPFSFSELLARV 111
PRK13557 PRK13557
histidine kinase; Provisional
782-932 3.35e-10

histidine kinase; Provisional


Pssm-ID: 237425 [Multi-domain]  Cd Length: 540  Bit Score: 63.54  E-value: 3.35e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823315871 782 GTGQVLAILDPAGVLRLSRRPATwlgqAQRQVQATGNQRLLLVDDSLSVRRLVGRMLERGGYQVVTASDGQEALDLLQQD 861
Cdd:PRK13557  383 GEGTTVRLYFPASDQAENPEQEP----KARAIDRGGTETILIVDDRPDVAELARMILEDFGYRTLVASNGREALEILDSH 458
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1823315871 862 ADFGAVVTDLEMP-RVNGYELLSAVRARpaTAGLPMLVMTTRAGEKHQRLAFQLGADDYFTKPVNEALLLRR 932
Cdd:PRK13557  459 PEVDLLFTDLIMPgGMNGVMLAREARRR--QPKIKVLLTTGYAEASIERTDAGGSEFDILNKPYRRAELARR 528
Hpt pfam01627
Hpt domain; The histidine-containing phosphotransfer (HPt) domain is a novel protein module ...
190-276 5.66e-10

Hpt domain; The histidine-containing phosphotransfer (HPt) domain is a novel protein module with an active histidine residue that mediates phosphotransfer reactions in the two-component signaling systems. A multistep phosphorelay involving the HPt domain has been suggested for these signaling pathways. The crystal structure of the HPt domain of the anaerobic sensor kinase ArcB has been determined. The domain consists of six alpha helices containing a four-helix bundle-folding. The pattern of sequence similarity of the HPt domains of ArcB and components in other signaling systems can be interpreted in light of the three-dimensional structure and supports the conclusion that the HPt domains have a common structural motif both in prokaryotes and eukaryotes. In S. cerevisiae ypd1p this domain has been shown to contain a binding surface for Ssk1p (response regulator receiver domain containing protein pfam00072).


Pssm-ID: 426352 [Multi-domain]  Cd Length: 84  Bit Score: 56.59  E-value: 5.66e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823315871 190 EVWEYFAPEVHEHLASLREQLgrgEDADLQVMFRAAHTIKGSAYMVGLPPLGDFAHGMEDLLgaaREGAVSLSSDVRGLL 269
Cdd:pfam01627   1 ELLELFLEEAPELLEQLEQAL---DAEDLEALFRAAHTLKGSAGSLGLPALAELAHELEDLL---REGELPLDPELLEAL 74

                  ....*..
gi 1823315871 270 AEATDTI 276
Cdd:pfam01627  75 RDLLEAL 81
PRK10161 PRK10161
phosphate response regulator transcription factor PhoB;
819-933 6.06e-10

phosphate response regulator transcription factor PhoB;


Pssm-ID: 182277 [Multi-domain]  Cd Length: 229  Bit Score: 60.50  E-value: 6.06e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823315871 819 QRLLLVDDSLSVRRLVGRMLERGGYQVVTASDGQEALDLLQQDADfGAVVTDLEMPRVNGYELLSAVRARPATAGLPMLV 898
Cdd:PRK10161    3 RRILVVEDEAPIREMVCFVLEQNGFQPVEAEDYDSAVNQLNEPWP-DLILLDWMLPGGSGIQFIKHLKRESMTRDIPVVM 81
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1823315871 899 MTTRAGEKHQRLAFQLGADDYFTKPVNEALLLRRL 933
Cdd:PRK10161   82 LTARGEEEDRVRGLETGADDYITKPFSPKELVARI 116
fixJ PRK09390
response regulator FixJ; Provisional
824-946 7.50e-10

response regulator FixJ; Provisional


Pssm-ID: 181815 [Multi-domain]  Cd Length: 202  Bit Score: 59.63  E-value: 7.50e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823315871 824 VDDSLSVRRLVGRMLERGGYQVVTASDGQEALDLLQqDADFGAVVTDLEMPRVNGYELLSAVRARPATagLPMLVMTTRA 903
Cdd:PRK09390    9 VDDDEAMRDSLAFLLDSAGFEVRLFESAQAFLDALP-GLRFGCVVTDVRMPGIDGIELLRRLKARGSP--LPVIVMTGHG 85
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1823315871 904 GEKHQRLAFQLGADDYFTKPVNEALLLRRLGT-LQQAQQAGVSA 946
Cdd:PRK09390   86 DVPLAVEAMKLGAVDFIEKPFEDERLIGAIERaLAQAPEAAKSE 129
PRK11083 PRK11083
DNA-binding response regulator CreB; Provisional
820-923 1.02e-09

DNA-binding response regulator CreB; Provisional


Pssm-ID: 236838 [Multi-domain]  Cd Length: 228  Bit Score: 59.59  E-value: 1.02e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823315871 820 RLLLVDDSLSVRRLVGRMLERGGYQVVTASDGQEALDLLQQDAdFGAVVTDLEMPRVNGYELLSAVRARPATagLPMLVM 899
Cdd:PRK11083    5 TILLVEDEQAIADTLVYALQSEGFTVEWFERGLPALDKLRQQP-PDLVILDVGLPDISGFELCRQLLAFHPA--LPVIFL 81
                          90       100
                  ....*....|....*....|....
gi 1823315871 900 TTRAGEKHQRLAFQLGADDYFTKP 923
Cdd:PRK11083   82 TARSDEVDRLVGLEIGADDYVAKP 105
REC_OmpR_MtrA-like cd17626
phosphoacceptor receiver (REC) domain of MtrA-like OmpR family response regulators; MtrA is ...
819-933 2.03e-09

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


Pssm-ID: 381141 [Multi-domain]  Cd Length: 115  Bit Score: 55.94  E-value: 2.03e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823315871 819 QRLLLVDDSLSVRRLVGRMLERGGYQVVTASDGQEALDLLQQ-DADFgaVVTDLEMPRVNGYELLSAVRarpATAGLPML 897
Cdd:cd17626     1 ARILVVDDDAALAEMIGIVLRGEGFDPAFCGDGTQALAAFREvRPDL--VLLDLMLPGIDGIEVCRQIR---AESGVPIV 75
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1823315871 898 VMTTRAGEKHQRLAFQLGADDYFTKPVNEALLLRRL 933
Cdd:cd17626    76 MLTAKSDTVDVVLGLESGADDYVAKPFKPKELVARI 111
HATPase_CckA-like cd16919
Histidine kinase-like ATPase domain of two-component sensor hybrid histidine kinases, similar ...
498-662 3.27e-09

Histidine kinase-like ATPase domain of two-component sensor hybrid histidine kinases, similar to Brucella abortus 2308 CckA; This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component hybrid sensor histidine kinase (HKs) similar to Brucella abortus 2308 CckA, which is a component of an essential protein phosphorelay that regulates expression of genes required for growth, division, and intracellular survival; phosphoryl transfer initiates from the sensor kinase CckA and proceeds via the ChpT phosphotransferase to two regulatory substrates: the DNA-binding response regulator CtrA and the phospho-receiver protein CpdR. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA), a REC signal receiver domain, and some contain PAS or PAS and GAF sensor domain(s).


Pssm-ID: 340396 [Multi-domain]  Cd Length: 116  Bit Score: 55.46  E-value: 3.27e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823315871 498 QQADLTLQVEGEDVLIESG-ILQRISDPLLHLLTNAAYHGLASesaesrraagknpqgtvwiraaeqGNFLEVTVADDGQ 576
Cdd:cd16919     2 ELAILNLAVNARDAMPEGGrLTIETSNQRVDADYALNYRDLIP------------------------GNYVCLEVSDTGS 57
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823315871 577 GLDyARIRERALErglrsaqeleqlssdelgrlillPGFSTaREVGNvaGRGVGLDVVATAVRQLGGELLISSERGVGTA 656
Cdd:cd16919    58 GMP-AEVLRRAFE-----------------------PFFTT-KEVGK--GTGLGLSMVYGFVKQSGGHLRIYSEPGVGTT 110

                  ....*.
gi 1823315871 657 FTLRVP 662
Cdd:cd16919   111 VRIYLP 116
REC_CheC-like cd17593
phosphoacceptor receiver (REC) domain of uncharacterized response regulators containing a CheC ...
820-934 3.89e-09

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


Pssm-ID: 381124 [Multi-domain]  Cd Length: 117  Bit Score: 55.24  E-value: 3.89e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823315871 820 RLLLVDDSLSVRRLVGRMLERG-GYQVVTASDGQEALDLL-QQDADFgaVVTDLEMPRVNGYELLSAVRARpataGLPML 897
Cdd:cd17593     2 KVLICDDSSMARKQLARALPADwDVEITFAENGEEALEILrEGRIDV--LFLDLTMPVMDGYEVLEALPVE----QLETK 75
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1823315871 898 VMTTRAG---EKHQRlAFQLGADDYFTKPVNEALL---LRRLG 934
Cdd:cd17593    76 VIVVSGDvqpEAKER-VLELGALAFLKKPFDPEKLaqlLEELG 117
REC_WspR-like cd17575
phosphoacceptor receiver (REC) domain of WspR response regulator and similar proteins; The ...
820-922 4.20e-09

phosphoacceptor receiver (REC) domain of WspR response regulator and similar proteins; The GGDEF response regulator WspR is part of the Wsp system that is homologous to chemotaxis systems and also includes the membrane-bound receptor protein WspA. In response to growth on surfaces, WspR is phosphorylated by the Wsp signal transduction complex and is activated, functioning as a diguanylate cyclase (DGC) that catalyzes c-di-GMP synthesis. WspR is a hybrid response regulator-diguanylate cyclase, containing an N-terminal REC domain and a C-terminal GGDEF domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381117 [Multi-domain]  Cd Length: 128  Bit Score: 55.49  E-value: 4.20e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823315871 820 RLLLVDDSLSVRRLVGRML-ERGGYQVVTASDGQEALDLLQQDADfGAVVTDLEMPRVNGYELLSAVRARPATAGLPMLV 898
Cdd:cd17575     2 MVLLVDDQAIIGEAVRRALaDEEDIDFHYCSDPTEAIEVASQIKP-TVILQDLVMPGVDGLTLVRFFRANPATRDIPIIV 80
                          90       100
                  ....*....|....*....|....
gi 1823315871 899 MTTRAGEKHQRLAFQLGADDYFTK 922
Cdd:cd17575    81 LSTKEEPEVKSEAFALGANDYLVK 104
PRK11173 PRK11173
two-component response regulator; Provisional
820-925 5.16e-09

two-component response regulator; Provisional


Pssm-ID: 183013 [Multi-domain]  Cd Length: 237  Bit Score: 57.72  E-value: 5.16e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823315871 820 RLLLVDDSLSVRRLVGRMLERGGYQVVTASDGQEALDLLQqDADFGAVVTDLEMPRVNGYELLSAVRARpatAGLPMLVM 899
Cdd:PRK11173    5 HILIVEDELVTRNTLKSIFEAEGYDVFEATDGAEMHQILS-ENDINLVIMDINLPGKNGLLLARELREQ---ANVALMFL 80
                          90       100
                  ....*....|....*....|....*.
gi 1823315871 900 TTRAGEKHQRLAFQLGADDYFTKPVN 925
Cdd:PRK11173   81 TGRDNEVDKILGLEIGADDYITKPFN 106
NtrY COG5000
Signal transduction histidine kinase NtrY involved in nitrogen fixation and metabolism ...
433-666 5.49e-09

Signal transduction histidine kinase NtrY involved in nitrogen fixation and metabolism regulation [Signal transduction mechanisms];


Pssm-ID: 444024 [Multi-domain]  Cd Length: 422  Bit Score: 59.59  E-value: 5.49e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823315871 433 LSRSITELSADFAEVRRRLSDTaaeLSEENEQLGKLVRRLR------------LDVNQTsrvaFSQTTARLRRWAREQQA 500
Cdd:COG5000   226 LRRKLADKLEEDREDLERALDT---IIRQVDRLKRIVDEFLdfarlpepqlepVDLNEL----LREVLALYEPALKEKDI 298
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823315871 501 DLTLQVEGEDVLIE--SGILQRIsdpLLHLLTNAAyhglasESAESRraagknpqGTVWIRAAEQGNFLEVTVADDGQGL 578
Cdd:COG5000   299 RLELDLDPDLPEVLadRDQLEQV---LINLLKNAI------EAIEEG--------GEIEVSTRREDGRVRIEVSDNGPGI 361
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823315871 579 DyARIRERALErglrsaqeleqlssdelgrlillPGFSTAREvgnvaGRGVGLDVVATAVRQLGGELLISSERGVGTAFT 658
Cdd:COG5000   362 P-EEVLERIFE-----------------------PFFTTKPK-----GTGLGLAIVKKIVEEHGGTIELESRPGGGTTFT 412

                  ....*...
gi 1823315871 659 LRVPTTQR 666
Cdd:COG5000   413 IRLPLAEE 420
REC_OmpR_BaeR-like cd19938
phosphoacceptor receiver (REC) domain of BaeR-like OmpR family response regulators; BaeR is ...
820-923 8.89e-09

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


Pssm-ID: 381165 [Multi-domain]  Cd Length: 114  Bit Score: 54.31  E-value: 8.89e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823315871 820 RLLLVDDSLSVRRLVGRMLERGGYQVVTASDGQEALDLLQQDADfGAVVTDLEMPRVNGYELLSAVRARPAtagLPMLVM 899
Cdd:cd19938     1 RILIVEDEPKLAQLLIDYLRAAGYAPTLLAHGDQVLPYVRHTPP-DLILLDLMLPGTDGLTLCREIRRFSD---VPIIMV 76
                          90       100
                  ....*....|....*....|....
gi 1823315871 900 TTRAGEKHQRLAFQLGADDYFTKP 923
Cdd:cd19938    77 TARVEEIDRLLGLELGADDYICKP 100
REC_PdtaR-like cd19932
phosphoacceptor receiver (REC) domain of PdtaR and similar proteins; This subfamily includes ...
820-930 1.44e-08

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: 53.57  E-value: 1.44e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823315871 820 RLLLVDDSLSVRRLVGRMLERGGYQVV-TASDGQEALDL---LQQDadfgAVVTDLEMPRVNGYELLSAVRARPATaglP 895
Cdd:cd19932     2 RVLIAEDEALIRMDLREMLEEAGYEVVgEASDGEEAVELakkHKPD----LVIMDVKMPRLDGIEAAKIITSENIA---P 74
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1823315871 896 MLVMTTRAGEKHQRLAFQLGADDYFTKPVNEALLL 930
Cdd:cd19932    75 IVLLTAYSQQDLVERAKEAGAMAYLVKPFSESDLI 109
WalK COG5002
Sensor histidine kinase WalK [Signal transduction mechanisms];
442-662 1.45e-08

Sensor histidine kinase WalK [Signal transduction mechanisms];


Pssm-ID: 444026 [Multi-domain]  Cd Length: 390  Bit Score: 58.03  E-value: 1.45e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823315871 442 ADFAEVRRRLSDTAAElseENEQLGKLVRRL----RLDVNQTS--------RVAFSQTTARLRRWAREQQADLTLQVEGE 509
Cdd:COG5002   195 ADDPEERREYLEIILE---EAERLSRLVNDLldlsRLESGELKlekepvdlAELLEEVVEELRPLAEEKGIELELDLPED 271
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823315871 510 DVLIE--SGILQRIsdpLLHLLTNAAYHGlasesaesrraagkNPQGTVWIRAAEQGNFLEVTVADDGQGL---DYARIR 584
Cdd:COG5002   272 PLLVLgdPDRLEQV---LTNLLDNAIKYT--------------PEGGTITVSLREEDDQVRISVRDTGIGIpeeDLPRIF 334
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1823315871 585 ERaLERGlrsaqeleqlssDElgrlillpgfSTAREVGnvaGRGVGLDVVATAVRQLGGELLISSERGVGTAFTLRVP 662
Cdd:COG5002   335 ER-FYRV------------DK----------SRSRETG---GTGLGLAIVKHIVEAHGGRIWVESEPGKGTTFTITLP 386
HATPase_AtoS-like cd16943
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
525-662 2.99e-08

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


Pssm-ID: 340419 [Multi-domain]  Cd Length: 105  Bit Score: 52.42  E-value: 2.99e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823315871 525 LLHLLTNAAyhglaseSAESRRaagknpqGTVWIRAAEQGNFLEVTVADDGQGLDyARIRERalerglrsaqeleqlssd 604
Cdd:cd16943     8 LLNLLVNAA-------QAMEGR-------GRITIRTWAHVDQVLIEVEDTGSGID-PEILGR------------------ 54
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1823315871 605 elgrlILLPgFSTAREVGNvaGRGVGLDVVATAVRQLGGELLISSERGVGTAFTLRVP 662
Cdd:cd16943    55 -----IFDP-FFTTKPVGE--GTGLGLSLSYRIIQKHGGTIRVASVPGGGTRFTIILP 104
glnG PRK10923
nitrogen regulation protein NR(I); Provisional
823-941 3.13e-08

nitrogen regulation protein NR(I); Provisional


Pssm-ID: 182842 [Multi-domain]  Cd Length: 469  Bit Score: 57.19  E-value: 3.13e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823315871 823 LVDDSLSVRRLVGRMLERGGYQVVTASDGQEALDLLQQDADfGAVVTDLEMPRVNGYELLSAVRARPATagLPMLVMTTR 902
Cdd:PRK10923    8 VVDDDSSIRWVLERALAGAGLTCTTFENGNEVLEALASKTP-DVLLSDIRMPGMDGLALLKQIKQRHPM--LPVIIMTAH 84
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1823315871 903 AGEKHQRLAFQLGADDYFTKP--VNEALLL--RRLGTLQQAQQ 941
Cdd:PRK10923   85 SDLDAAVSAYQQGAFDYLPKPfdIDEAVALveRAISHYQEQQQ 127
REC_Spo0F-like cd17553
phosphoacceptor receiver (REC) domain of Spo0F and similar domains; Spo0F, a stand-alone ...
819-923 5.95e-08

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


Pssm-ID: 381105 [Multi-domain]  Cd Length: 117  Bit Score: 51.79  E-value: 5.95e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823315871 819 QRLLLVDDSLSVRRLVGRMLERGGYQVVTASDGQEALDLLQQDADfGAVVTDLEMPRVNGYELLSavRARPATAGLPMLV 898
Cdd:cd17553     1 EKILIVDDQYGIRILLNEVFNKEGYQTFQAANGLQALDIVTKERP-DLVLLDMKIPGMDGIEILK--RMKVIDENIRVII 77
                          90       100
                  ....*....|....*....|....*
gi 1823315871 899 MTTRAGEKHQRLAFQLGADDYFTKP 923
Cdd:cd17553    78 MTAYGELDMIQESKELGALTHFAKP 102
REC_LytTR_AlgR-like cd17532
phosphoacceptor receiver (REC) domain of LytTR/AlgR family response regulators similar to AlgR; ...
822-933 7.10e-08

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


Pssm-ID: 381087 [Multi-domain]  Cd Length: 118  Bit Score: 51.77  E-value: 7.10e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823315871 822 LLVDDSLSVRRLVGRMLER-GGYQVV-TASDGQEALDLLQQDA-DfgAVVTDLEMPRVNGYELLSAVRARPATaglPMLV 898
Cdd:cd17532     2 LIVDDEPLAREELRYLLEEhPDIEIVgEAENGEEALEAIEELKpD--VVFLDIQMPGLDGLELAKKLSKLAKP---PLIV 76
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1823315871 899 MTTrAGEKHQRLAFQLGADDYFTKPVNEALL---LRRL 933
Cdd:cd17532    77 FVT-AYDEYAVEAFELNAVDYLLKPFSEERLaeaLAKL 113
REC_citrate_TCS cd19925
phosphoacceptor receiver (REC) domain of citrate family two-component system response ...
820-933 8.32e-08

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: 51.48  E-value: 8.32e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823315871 820 RLLLVDDSLSVRRLVGRMLER-GGYQVV-TASDGQEALDLLQqDADFGAVVTDLEMPRVNGYELLSAVRARPATAGLpml 897
Cdd:cd19925     2 NVLIVEDDPMVAEIHRAYVEQvPGFTVIgTAGTGEEALKLLK-ERQPDLILLDIYLPDGNGLDLLRELRAAGHDVDV--- 77
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1823315871 898 VMTTRAGE-KHQRLAFQLGADDYFTKPVNEALLLRRL 933
Cdd:cd19925    78 IVVTAANDvETVREALRLGVVDYLIKPFTFERLRQRL 114
PRK10766 PRK10766
two-component system response regulator TorR;
820-946 1.23e-07

two-component system response regulator TorR;


Pssm-ID: 182711 [Multi-domain]  Cd Length: 221  Bit Score: 53.50  E-value: 1.23e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823315871 820 RLLLVDDSLSVR-RLVGrMLERGGYQVVTASDGQEALDLLQ-QDADFgaVVTDLEMPRVNGYELLSAVRARpATAGLpML 897
Cdd:PRK10766    4 HILVVEDEPVTRaRLQG-YFEQEGYTVSEAASGAGMREIMQnQHVDL--ILLDINLPGEDGLMLTRELRSR-STVGI-IL 78
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1823315871 898 VmTTRAGEKHQRLAFQLGADDYFTKPVN--EAL-----LLRRLGTLQQAQQAGVSA 946
Cdd:PRK10766   79 V-TGRTDSIDRIVGLEMGADDYVTKPLElrELLvrvknLLWRISLARQAQPHAQEE 133
REC_Spo0A cd17561
phosphoacceptor receiver (REC) domain of Spo0A; Spo0A is a response regulator of the ...
820-923 1.39e-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: 50.68  E-value: 1.39e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823315871 820 RLLLVDDSlsvRRLVGRMLE----RGGYQVV-TASDGQEALDLL-QQDADFgaVVTDLEMPRVNGYELLSAVRARPATAg 893
Cdd:cd17561     3 KVLIADDN---REFVQLLEEylnsQPDMEVVgVAHNGQEALELIeEKEPDV--LLLDIIMPHLDGIGVLEKLRRMRLEK- 76
                          90       100       110
                  ....*....|....*....|....*....|.
gi 1823315871 894 LPMLVMTTRAG-EKHQRLAFQLGADDYFTKP 923
Cdd:cd17561    77 RPKIIMLTAFGqEDITQRAVELGASYYILKP 107
PRK10816 PRK10816
two-component system response regulator PhoP;
820-938 1.50e-07

two-component system response regulator PhoP;


Pssm-ID: 182755 [Multi-domain]  Cd Length: 223  Bit Score: 53.20  E-value: 1.50e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823315871 820 RLLLVDDSLSVRRLVGRMLERGGYQVVTASDGQEALDLLQQDADFGAVVtDLEMPRVNGYELLSAVRARPATagLPMLVM 899
Cdd:PRK10816    2 RVLVVEDNALLRHHLKVQLQDAGHQVDAAEDAKEADYYLNEHLPDIAIV-DLGLPDEDGLSLIRRWRSNDVS--LPILVL 78
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1823315871 900 TTRAGEKHQRLAFQLGADDYFTKPVN--------EALLLRRLGTLQQ 938
Cdd:PRK10816   79 TARESWQDKVEVLSAGADDYVTKPFHieevmarmQALMRRNSGLASQ 125
PRK11086 PRK11086
sensory histidine kinase DcuS; Provisional
495-662 1.68e-07

sensory histidine kinase DcuS; Provisional


Pssm-ID: 236839 [Multi-domain]  Cd Length: 542  Bit Score: 54.92  E-value: 1.68e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823315871 495 AREQQADLTLQVEGedVLIESGILQRISD---PLLHLLTNAAyhglasesaesrRAAGKNPQGTVWIRAAEQGNFLEVTV 571
Cdd:PRK11086  407 ARELGITLIISEDS--QLPDSGDEDQVHElitILGNLIENAL------------EAVGGEEGGEISVSLHYRNGWLHCEV 472
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823315871 572 ADDGQGLDyarireralerglrsAQELEQlssdelgrlILLPGFSTArevGNvaGRGVGLDVVATAVRQLGGELLISSER 651
Cdd:PRK11086  473 SDDGPGIA---------------PDEIDA---------IFDKGYSTK---GS--NRGVGLYLVKQSVENLGGSIAVESEP 523
                         170
                  ....*....|.
gi 1823315871 652 GVGTAFTLRVP 662
Cdd:PRK11086  524 GVGTQFFVQIP 534
PRK09959 PRK09959
acid-sensing system histidine kinase EvgS;
782-938 1.83e-07

acid-sensing system histidine kinase EvgS;


Pssm-ID: 182169 [Multi-domain]  Cd Length: 1197  Bit Score: 55.51  E-value: 1.83e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823315871  782 GTGQVLAILDPAGVLRlsrRPATWLGQAQRQVQATGNQRLLLVDDSLSVRRLVGRMLERGGYQVVTASDGQEALDLLQQD 861
Cdd:PRK09959   925 GIGTTFTITIPVEISQ---QVATVEAKAEQPITLPEKLSILIADDHPTNRLLLKRQLNLLGYDVDEATDGVQALHKVSMQ 1001
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1823315871  862 aDFGAVVTDLEMPRVNGYELLSAVRARpaTAGLPMLVMTTRAGEKHQRLAFQLGADDYFTKPVNEALLLRRLGTLQQ 938
Cdd:PRK09959  1002 -HYDLLITDVNMPNMDGFELTRKLREQ--NSSLPIWGLTANAQANEREKGLSCGMNLCLFKPLTLDVLKTHLSQLHQ 1075
REC_RcNtrC-like cd19928
phosphoacceptor receiver (REC) domain of Rhodobacter capsulatus nitrogen regulatory protein C ...
821-923 2.34e-07

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: 49.81  E-value: 2.34e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823315871 821 LLLVDDSLSVRRLVGRMLERGGYQVVTASDGQEALDLLQQ-DADFgaVVTDLEMPRVNGYELLSAV-RARPataGLPMLV 898
Cdd:cd19928     1 ILVADDDRAIRTVLTQALGRAGYEVRTTGNAATLWRWVEEgEGDL--VITDVVMPDENGLDLIPRIkKARP---DLPIIV 75
                          90       100
                  ....*....|....*....|....*
gi 1823315871 899 MTTRAGEKHQRLAFQLGADDYFTKP 923
Cdd:cd19928    76 MSAQNTLMTAVKAAERGAFEYLPKP 100
HATPase_DpiB-CitA-like cd16915
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
547-662 2.98e-07

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


Pssm-ID: 340392 [Multi-domain]  Cd Length: 104  Bit Score: 49.59  E-value: 2.98e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823315871 547 AAGKNPQGTVWIRAAEQGNFLEVTVADDGQGLDyARIRERALERGlrsaqeleqlssdelgrlillpgFSTAREvgnvAG 626
Cdd:cd16915    17 AATGAPNKQVEVFLRDEGDDLVIEVRDTGPGIA-PELRDKVFERG-----------------------VSTKGQ----GE 68
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1823315871 627 RGVGLDVVATAVRQLGGELLISSERGVGTAFTLRVP 662
Cdd:cd16915    69 RGIGLALVRQSVERLGGSITVESEPGGGTTFSIRIP 104
PRK10365 PRK10365
sigma-54-dependent response regulator transcription factor ZraR;
817-925 3.47e-07

sigma-54-dependent response regulator transcription factor ZraR;


Pssm-ID: 182412 [Multi-domain]  Cd Length: 441  Bit Score: 53.88  E-value: 3.47e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823315871 817 GNQRLLLVDDSLSVRRLVGRMLERGGYQVVTASDGQEALDLLQQDAdFGAVVTDLEMPRVNGYELLSAVRA-RPAtagLP 895
Cdd:PRK10365    4 DNIDILVVDDDISHCTILQALLRGWGYNVALANSGRQALEQVREQV-FDLVLCDVRMAEMDGIATLKEIKAlNPA---IP 79
                          90       100       110
                  ....*....|....*....|....*....|
gi 1823315871 896 MLVMTTRAGEKHQRLAFQLGADDYFTKPVN 925
Cdd:PRK10365   80 VLIMTAYSSVETAVEALKTGALDYLIKPLD 109
YesM COG2972
Sensor histidine kinase YesM [Signal transduction mechanisms];
501-662 4.42e-07

Sensor histidine kinase YesM [Signal transduction mechanisms];


Pssm-ID: 442211 [Multi-domain]  Cd Length: 445  Bit Score: 53.48  E-value: 4.42e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823315871 501 DLTLQVEGE--DVLIESGILQrisdPLLHlltNAAYHGLASesaesrraagKNPQGTVWIRAAEQGNFLEVTVADDGQGL 578
Cdd:COG2972   322 EVEIEIDEEllDLLIPKLILQ----PLVE---NAIEHGIEP----------KEGGGTIRISIRKEGDRLVITVEDNGVGM 384
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823315871 579 DYARIREralerglrsaqeleqlssdelgrliLLPGFSTAREvgnvaGRGVGLDVVATAVRQLGGE---LLISSERGVGT 655
Cdd:COG2972   385 PEEKLEK-------------------------LLEELSSKGE-----GRGIGLRNVRERLKLYYGEeygLEIESEPGEGT 434

                  ....*..
gi 1823315871 656 AFTLRVP 662
Cdd:COG2972   435 TVTIRIP 441
CheW pfam01584
CheW-like domain; CheW proteins are part of the chemotaxis signaling mechanism in bacteria. ...
677-795 5.47e-07

CheW-like domain; CheW proteins are part of the chemotaxis signaling mechanism in bacteria. CheW interacts with the methyl accepting chemotaxis proteins (MCPs) and relays signals to CheY, which affects flageller rotation. This family includes CheW and other related proteins that are involved in chemotaxis. The CheW-like regulatory domain in CheA binds to CheW, suggesting that these domains can interact with each other.


Pssm-ID: 460257 [Multi-domain]  Cd Length: 131  Bit Score: 49.51  E-value: 5.47e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823315871 677 AGHHAALPVGSVRSLRDV-PLGDLRRDDGQLW--LDFGGQPVPVVDARPIWGHAPQDTDTEAHLAVVSSISGLLALRVHD 753
Cdd:pfam01584   7 GGETFAIPISKVREILRPpPITPIPGAPGYVLgvINLRGEVLPVIDLRRLLGLPPTEPRERTRVVVVEVGGQVVGLLVDE 86
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1823315871 754 FGDIEEV---AVTAPSGLLAPLDYLAGMAVSGTGQVLAILDPAGV 795
Cdd:pfam01584  87 VIGVLEIvikQIEPPLGLGRVAGYISGATILGDGRVVLILDVEAL 131
CitB COG2197
DNA-binding response regulator, NarL/FixJ family, contains REC and HTH domains [Signal ...
820-885 5.69e-07

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: 49.51  E-value: 5.69e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1823315871 820 RLLLVDDSLSVRRLVGRMLER-GGYQVV-TASDGQEALDLLQQdADFGAVVTDLEMPRVNGYELLSAV 885
Cdd:COG2197     3 RVLIVDDHPLVREGLRALLEAePDIEVVgEAADGEEALELLEE-LRPDVVLLDIRMPGMDGLEALRRL 69
REC_PilR cd19926
phosphoacceptor receiver (REC) domain of type 4 fimbriae expression regulatory protein PilR ...
822-923 8.44e-07

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


Pssm-ID: 381153 [Multi-domain]  Cd Length: 100  Bit Score: 48.30  E-value: 8.44e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823315871 822 LLVDDSLSVRRLVGRMLERGGYQVVTASDGQEALDLLQQDAdFGAVVTDLEMPRVNGYELLSAVRARpaTAGLPMLVMTT 901
Cdd:cd19926     2 LVVDDEPDIRELLEITLGRMGLDVRSARNVKEARELLASEP-YDLCLTDMRLPDGSGLELVQHIQQR--LPQTPVAVITA 78
                          90       100
                  ....*....|....*....|..
gi 1823315871 902 RAGEKHQRLAFQLGADDYFTKP 923
Cdd:cd19926    79 YGSLDTAIEALKAGAFDFLTKP 100
REC_1_GGDEF cd19921
first phosphoacceptor receiver (REC) domain of uncharacterized GGDEF domain proteins; This ...
820-922 1.43e-06

first 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 contains characteristic metal-binding and active site residues. PleD response regulators are global regulators of cell metabolism in some important human pathogens. This model describes the first REC domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381148 [Multi-domain]  Cd Length: 115  Bit Score: 47.94  E-value: 1.43e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823315871 820 RLLLVDDSLSVRRLVGRML-ERGGYQVVTASDGQEALDLLQQDADFGAVVTDLEMPRV-NGyELLSAVRARpataGLPML 897
Cdd:cd19921     1 KVLIVEDSKTFSKVLKHLIaQELGLEVDVAETLAEAKALLEEGDDYFAALVDLNLPDApNG-EAVDLVLEK----GIPVI 75
                          90       100
                  ....*....|....*....|....*
gi 1823315871 898 VMTTRAGEKHQRLAFQLGADDYFTK 922
Cdd:cd19921    76 VLTGSFDEDKRETLLSKGVVDYVLK 100
REC_TPR cd17589
phosphoacceptor receiver (REC) domain of uncharacterized tetratricopeptide repeat (TPR) ...
822-933 1.50e-06

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


Pssm-ID: 381123 [Multi-domain]  Cd Length: 115  Bit Score: 48.03  E-value: 1.50e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823315871 822 LLVDDSLSVRRLVGRMLERGGY-QVVTASDGQEALDLLQQDaDFGAVVTDLEM-PRVNGYELLSAVRAR---PATAGLpm 896
Cdd:cd17589     2 LIVDDQPTFRSMLKSMLRSLGVtRIDTASSGEEALRMCENK-TYDIVLCDYNLgKGKNGQQLLEELRHKkliSPSTVF-- 78
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1823315871 897 lVMTTraGEKHQRL---AFQLGADDYFTKPVNEALLLRRL 933
Cdd:cd17589    79 -IMVT--GESSRAMvlsALELEPDDYLLKPFTVSELRERL 115
CheA_reg cd00731
CheA regulatory domain; CheA is a histidine protein kinase present in bacteria and archea. ...
667-794 1.84e-06

CheA regulatory domain; CheA is a histidine protein kinase present in bacteria and archea. Activated by the chemotaxis receptor a histidine phosphoryl group from CheA is passed directly to an aspartate in the response regulator CheY. This signalling mechanism is modulated by the methyl accepting chemotaxis proteins (MCPs). MCPs form a highly interconnected, tightly packed array within the membrane that is organized, at least in part, through interactions with CheW and CheA. The CheA regulatory domain belongs to the family of CheW_like proteins and has been proposed to mediate interaction with the kinase regulator CheW.


Pssm-ID: 238373 [Multi-domain]  Cd Length: 132  Bit Score: 47.94  E-value: 1.84e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823315871 667 IMDVLHLDLGaGHHAALPVGSVRSLRDVPLGDLRRDDG-QLWLDFGGQPVPVVDARPIWGHAPQDTD-TEAHLAVVSSIS 744
Cdd:cd00731     3 IIKGLLVRVG-DETYAIPLSAVVETVRIKPKDIKRVDGgKEVINVRGELLPLVRLGELFNVRGENEEpDEGVVVVVRTGG 81
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1823315871 745 GLLALRVHDFGDIEEVAVTAPSGLLAPLDYLAGMAVSGTGQVLAILDPAG 794
Cdd:cd00731    82 RKAALVVDQIIGQEEVVIKPLGGFLSNIPGISGATILGDGRVALILDVPA 131
psREC-like_D2_PleD cd17539
REC-like adaptor domain (D2) of response regulator PleD; PleD contains a REC domain (D1) with ...
822-935 2.94e-06

REC-like adaptor domain (D2) of response regulator PleD; PleD contains a REC domain (D1) with the phosphorylatable aspartate, a pseudo receiver (psREC)-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 the REC-like adaptor domain D2 of PleD, which is an inactive domain.


Pssm-ID: 381094 [Multi-domain]  Cd Length: 124  Bit Score: 47.31  E-value: 2.94e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823315871 822 LLVDDSLSVRRLVGRMLeRGGYQVVTASDGQEALdLLQQDADFGAVVTDLEMPRVNGYELLSAVRARPATAGLPMLVMTT 901
Cdd:cd17539     2 LLVDDRPSSAERIAAML-SSEHEVVVEADPDEAL-FRAAEGPFDLVIVSLALEDFDGLRLCSQLRSLERTRQLPILAVAD 79
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1823315871 902 rAGEKhQRL--AFQLGADDYFTKPVNEALLLRRLGT 935
Cdd:cd17539    80 -PGDR-GRLirALEIGVNDYLVRPIDPNELLARVRT 113
PRK11107 PRK11107
hybrid sensory histidine kinase BarA; Provisional
628-929 3.23e-06

hybrid sensory histidine kinase BarA; Provisional


Pssm-ID: 236848 [Multi-domain]  Cd Length: 919  Bit Score: 51.00  E-value: 3.23e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823315871 628 GVGLDVVATA--VRQLGGELLISSERGVGTAF--TLRVPTTQR-IMDVLHLDLGAGHHAALpvgsvrslrdvplgdlrrd 702
Cdd:PRK11107  481 GTGLGLVITQklVNEMGGDISFHSQPNRGSTFwfHLPLDLNPNpIIDGLPTDCLAGKRLLY------------------- 541
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823315871 703 dgqlwldfggqpvpvVDARPIWGHAPQD-----------TDTEAHLAVVSSISGLLALRVHDFGDIEEVAVTapsglLAP 771
Cdd:PRK11107  542 ---------------VEPNSAAAQATLDilsetplevtySPTLSQLPEAHYDILLLGLPVTFREPLTMLHER-----LAK 601
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823315871 772 LDYLAG---MAVSGTGQVLA-----------ILDPAGVLRLSR-----RPATWLGQAQRQVQATGNQRLLLVDDSLSVRR 832
Cdd:PRK11107  602 AKSMTDfliLALPCHEQVLAeqlkqdgadacLSKPLSHTRLLPallepCHHKQPPLLPPTDESRLPLTVMAVDDNPANLK 681
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823315871 833 LVGRMLERGGYQVVTASDGQEALDLLQQDAdFGAVVTDLEMPRVNGYELLSAVRARPATAGLPMLVMT--TRAGEKHQRL 910
Cdd:PRK11107  682 LIGALLEEQVEHVVLCDSGHQAVEQAKQRP-FDLILMDIQMPGMDGIRACELIRQLPHNQNTPIIAVTahAMAGERERLL 760
                         330
                  ....*....|....*....
gi 1823315871 911 afQLGADDYFTKPVNEALL 929
Cdd:PRK11107  761 --SAGMDDYLAKPIDEAML 777
H-kinase_dim pfam02895
Signal transducing histidine kinase, homodimeric domain; This helical bundle domain is the ...
336-394 3.97e-06

Signal transducing histidine kinase, homodimeric domain; This helical bundle domain is the homodimer interface of the signal transducing histidine kinase family.


Pssm-ID: 427045 [Multi-domain]  Cd Length: 66  Bit Score: 45.31  E-value: 3.97e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1823315871 336 SIRVPAARLEGLMDQLGELVTARARMTQLLSRLDELQGS-----MTASQERFQRTVRDFEERYL 394
Cdd:pfam02895   1 TIRVDVEKLDRLMNLVGELVIARNRLVQLLERLEEYGGDtlleeLKEALQQLDRLTRELQEAVM 64
PksD COG3321
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ...
5-656 4.24e-06

Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442550 [Multi-domain]  Cd Length: 1386  Bit Score: 51.03  E-value: 4.24e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823315871    5 HSELLESFREEAAEVLSGLEEGVTGLRTLSGAAGHAHDTPELAAHLgdlsvLAHRLR-------GSAALY--GYAQL--- 72
Cdd:COG3321    723 HSPLMEPALEEFRAALAGVTPRAPRIPLISNVTGTWLTGEALDADY-----WVRHLRqpvrfadAVEALLadGVRVFlev 797
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823315871   73 ---STLASLQERLLDARPQ------LDREQHQEfltlleqvnAALRQGLSRLQAGGDDHDLGLLFARSGGATT------L 137
Cdd:COG3321    798 gpgPVLTGLVRQCLAAAGDavvlpsLRRGEDEL---------AQLLTALAQLWVAGVPVDWSALYPGRGRRRVplptypF 868
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823315871  138 QRLLQQRPDAFQIRASRLHHAPPSDTPSETAEDAPAPLTVAQEVQAFVRDNAEVWEYFAPEVHEHLASLREQLGRGEDAD 217
Cdd:COG3321    869 QREDAAAALLAAALAAALAAAAALGALLLAALAAALAAALLALAAAAAAALALAAAALAALLALVALAAAAAALLALAAA 948
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823315871  218 lQVMFRAAHTIKGSAYMVGLPPLGDFAHGMEDLLGAAREGAVSLSSDVRGLLAEATDTIGDLLTVAAGADGAALPAQLTA 297
Cdd:COG3321    949 -AAAAAAALAAAEAGALLLLAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAALALLAAAALLLAAAAAAAALLALAAL 1027
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823315871  298 VTARLRSAHSGEQTPVPPMSAAAPVVAPVPAPAPAAATSIRVPAARLEGLMDQLGELVTARARMTQLLSRLDELQGSMTA 377
Cdd:COG3321   1028 LAAAAAALAAAAAAAAAAAALAALAAAAAAAAALALALAALLLLAALAELALAAAALALAAALAAAALALALAALAAALL 1107
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823315871  378 SQERFQRTVRDFEERYLNPDMVREEGAAPTTRMGGLDLSQQFAELEFDTYNDLNILSRSITELSADFAEVRRRLSDTAAE 457
Cdd:COG3321   1108 LLALLAALALAAAAAALLALAALLAAAAAAAALAAAAAAAAALALAAAAAALAAALAAALLAAAALLLALALALAAALAA 1187
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823315871  458 LSEENEQLGKLVRRLRLDVNQTSRVAFSQTTARLRRWAREQQADLTLQVEGEDVLIESGILQRISDPLLHLLTNAAYHGL 537
Cdd:COG3321   1188 ALAGLAALLLAALLAALLAALLALALAALAAAAAALLAAAAAAAALALLALAAAAAAVAALAAAAAALLAALAALALLAA 1267
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823315871  538 ASESAESRRAAGKNPQGTVWIRAAEQGNFLEVTVADDGQGLDYARIRERALERGLRSAQELEQLSSDELGRLILLPGFST 617
Cdd:COG3321   1268 AAGLAALAAAAAAAAAALALAAAAAAAAAALAALLAAAAAAAAAAAAAAAAAALAAALLAAALAALAAAVAAALALAAAA 1347
                          650       660       670
                   ....*....|....*....|....*....|....*....
gi 1823315871  618 AREVGNVAGRGVGLDVVATAVRQLGGELLISSERGVGTA 656
Cdd:COG3321   1348 AAAAAAAAAAAAAAALAAAAGAAAAAAALALAALAAAVA 1386
REC_HP-RR-like cd17573
phosphoacceptor receiver (REC) domain of orphan response regulator HP-RR and similar proteins; ...
821-933 5.12e-06

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


Pssm-ID: 381115 [Multi-domain]  Cd Length: 110  Bit Score: 46.27  E-value: 5.12e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823315871 821 LLLVDDSLSVRRLVGRMLERGGYQV-VTAS--DGQEALDLLQQDAdfgaVVTDLEMPRVNGYELLSAVRARpaTAGLPML 897
Cdd:cd17573     1 ILLIEDDSTLGKEISKGLNEKGYQAdVAESlkDGEYYIDIRNYDL----VLVSDKLPDGNGLSIVSRIKEK--HPSIVVI 74
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1823315871 898 VMTTRAGEKHQRLAFQLGADDYFTKPVNEALLLRRL 933
Cdd:cd17573    75 VLSDNPKTEQEIEAFKEGADDYIAKPFDFKVLVARI 110
PRK10529 PRK10529
DNA-binding transcriptional activator KdpE; Provisional
818-933 6.14e-06

DNA-binding transcriptional activator KdpE; Provisional


Pssm-ID: 182522 [Multi-domain]  Cd Length: 225  Bit Score: 48.26  E-value: 6.14e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823315871 818 NQRLLLVDDSLSVRRLVGRMLERGGYQVVTASDGQEAL-DLLQQDADFgaVVTDLEMPRVNGYELLSAVRARPAtagLPM 896
Cdd:PRK10529    1 MTNVLIVEDEQAIRRFLRTALEGDGMRVFEAETLQRGLlEAATRKPDL--IILDLGLPDGDGIEFIRDLRQWSA---IPV 75
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1823315871 897 LVMTTRAGEKHQRLAFQLGADDYFTKPVNEALLLRRL 933
Cdd:PRK10529   76 IVLSARSEESDKIAALDAGADDYLSKPFGIGELQARL 112
ComP COG4585
Signal transduction histidine kinase ComP [Signal transduction mechanisms];
440-666 1.00e-05

Signal transduction histidine kinase ComP [Signal transduction mechanisms];


Pssm-ID: 443642 [Multi-domain]  Cd Length: 252  Bit Score: 48.08  E-value: 1.00e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823315871 440 LSADFAEVRRRLSDTAAELSEENEQLGKLVRRLRLDVNQTSRVAfSQTTARLRRWAREQQADLTLQVEGEDVLIESGI-- 517
Cdd:COG4585    83 LDADPEAAREELEEIRELAREALAELRRLVRGLRPPALDDLGLA-AALEELAERLLRAAGIRVELDVDGDPDRLPPEVel 161
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823315871 518 -LQRIsdpLLHLLTNAAYHGLASEsaesrraagknpqgtVWIRAAEQGNFLEVTVADDGQGLDyarireralerglrsaq 596
Cdd:COG4585   162 aLYRI---VQEALTNALKHAGATR---------------VTVTLEVDDGELTLTVRDDGVGFD----------------- 206
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823315871 597 eleqlssdelgrlillpgfstareVGNVAGRGVGLDVVATAVRQLGGELLISSERGVGTAFTLRVPTTQR 666
Cdd:COG4585   207 ------------------------PEAAPGGGLGLRGMRERAEALGGTLTIGSAPGGGTRVRATLPLAAA 252
pleD PRK09581
response regulator PleD; Reviewed
818-935 1.40e-05

response regulator PleD; Reviewed


Pssm-ID: 236577 [Multi-domain]  Cd Length: 457  Bit Score: 48.74  E-value: 1.40e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823315871 818 NQRLLLVD-DSLSVRRLVGRMLERggYQVVTASDGQEALDLlQQDADFGAVVTDLEMPRVNGYELLSAVRARPATAGLPM 896
Cdd:PRK09581  155 DGRILLVDdDVSQAERIANILKEE--FRVVVVSDPSEALFN-AAETNYDLVIVSANFENYDPLRLCSQLRSKERTRYVPI 231
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1823315871 897 LVMTtRAGEKHQRL-AFQLGADDYFTKPVNEALLLRRLGT 935
Cdd:PRK09581  232 LLLV-DEDDDPRLVkALELGVNDYLMRPIDKNELLARVRT 270
PRK11466 PRK11466
hybrid sensory histidine kinase TorS; Provisional
796-881 1.58e-05

hybrid sensory histidine kinase TorS; Provisional


Pssm-ID: 236914 [Multi-domain]  Cd Length: 914  Bit Score: 48.75  E-value: 1.58e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823315871 796 LRLS-RRPATWLGQAQRQVQATGNQRLLLVDDSLSVRRLVGRMLERGGYQVVTASDGQEALDLLQQDADFGAVVTDLEMP 874
Cdd:PRK11466  658 LRLPlRVATAPVPKTVNQAVRLDGLRLLLIEDNPLTQRITAEMLNTSGAQVVAVGNAAQALETLQNSEPFAAALVDFDLP 737

                  ....*..
gi 1823315871 875 RVNGYEL 881
Cdd:PRK11466  738 DYDGITL 744
PRK10336 PRK10336
two-component system response regulator QseB;
820-923 2.08e-05

two-component system response regulator QseB;


Pssm-ID: 182387 [Multi-domain]  Cd Length: 219  Bit Score: 46.81  E-value: 2.08e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823315871 820 RLLLVDDSLSVRRLVGRMLERGGYQVVTASDGQEALDLLQQdADFGAVVTDLEMPRVNGYELLSAVRARPATAglPMLVM 899
Cdd:PRK10336    2 RILLIEDDMLIGDGIKTGLSKMGFSVDWFTQGRQGKEALYS-APYDAVILDLTLPGMDGRDILREWREKGQRE--PVLIL 78
                          90       100
                  ....*....|....*....|....
gi 1823315871 900 TTRAGEKHQRLAFQLGADDYFTKP 923
Cdd:PRK10336   79 TARDALAERVEGLRLGADDYLCKP 102
PRK11091 PRK11091
aerobic respiration control sensor protein ArcB; Provisional
820-925 2.59e-05

aerobic respiration control sensor protein ArcB; Provisional


Pssm-ID: 236842 [Multi-domain]  Cd Length: 779  Bit Score: 48.01  E-value: 2.59e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823315871 820 RLLLVDD-SLSVrrLVGR-MLERGGYQVVTASDGQEALDLLQQDaDFGAVVTDLEMPRVNGYELLSAVRARPATAGLPML 897
Cdd:PRK11091  527 NILLVEDiELNV--IVARsVLEKLGNSVDVAMTGKEALEMFDPD-EYDLVLLDIQLPDMTGLDIARELRERYPREDLPPL 603
                          90       100
                  ....*....|....*....|....*...
gi 1823315871 898 VMTTRAGEKHQRLAFQLGADDYFTKPVN 925
Cdd:PRK11091  604 VALTANVLKDKKEYLDAGMDDVLSKPLS 631
REC_TrxB cd17595
phosphoacceptor receiver (REC) domain a fused response regulator with a thioredoxin reductase ...
821-887 2.78e-05

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


Pssm-ID: 381126 [Multi-domain]  Cd Length: 135  Bit Score: 44.63  E-value: 2.78e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1823315871 821 LLLVDDSLSVRRLVGRMLER---GGYQVVTASDGQEALDLLQQDADFGAVV----TDLEMPRVNGYELLSAVRA 887
Cdd:cd17595     3 ILTVDDDPQVLRAVARDLRRqygKDYRVLRADSGAEALDALKELKLRGEAValflVDQRMPEMDGVEFLEKAME 76
HATPase_EL346-LOV-HK-like cd16951
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
501-610 3.17e-05

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Erythrobacter litoralis blue light-activated histidine kinase 2; This domain family includes the histidine kinase-like ATPase (HATPase) domain of blue light-activated histidine kinase 2 of Erythrobacter litoralis (EL346). Signaling commonly occurs within HK dimers, however EL346 functions as a monomer. Also included in this family are the HATPase domains of ethanolamine utilization sensory transduction histidine kinase (EutW), whereby regulation of ethanolamine, a carbon and nitrogen source for gut bacteria, results in autophosphorylation and subsequent phosphoryl transfer to a response regulator (EutV) containing an RNA-binding domain. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA); some have an accessory PAS sensor domain, while some have an N-terminal histidine kinase domain.


Pssm-ID: 340427 [Multi-domain]  Cd Length: 131  Bit Score: 44.33  E-value: 3.17e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823315871 501 DLTLQVEGEDVLIESGILQRISDPLLHLLTNAAYHGLasesaeSRRAagknpQGTVWIRAAEQGNFLEVTVADDGQGLDy 580
Cdd:cd16951    20 DIRINITGDTGPVSSEVATAIGLVVNELLQNALKHAF------SDRE-----GGTITIRSVVDGDYLRITVIDDGVGLP- 87
                          90       100       110
                  ....*....|....*....|....*....|
gi 1823315871 581 arIRERALERGLRSAQELEQLSSDELGRLI 610
Cdd:cd16951    88 --QDEDWPNKGSLGLQIVRSLVEGELKAFL 115
HATPase_HupT_MifS-like cd16976
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
547-659 4.47e-05

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


Pssm-ID: 340435 [Multi-domain]  Cd Length: 102  Bit Score: 43.21  E-value: 4.47e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823315871 547 AAGKNPQGTVWIRAAEQGNFLEVTVADDGQGldyarIRERALERglrsaqeleqlssdelgrlILLPGFSTaREVGNvaG 626
Cdd:cd16976    15 AMGKVENPRIRIAARRLGGRLVLVVRDNGPG-----IAEEHLSR-------------------VFDPFFTT-KPVGK--G 67
                          90       100       110
                  ....*....|....*....|....*....|...
gi 1823315871 627 RGVGLDVVATAVRQLGGELLISSERGVGTAFTL 659
Cdd:cd16976    68 TGLGLSISYGIVEEHGGRLSVANEEGAGARFTF 100
PRK10643 PRK10643
two-component system response regulator PmrA;
820-936 5.49e-05

two-component system response regulator PmrA;


Pssm-ID: 182612 [Multi-domain]  Cd Length: 222  Bit Score: 45.41  E-value: 5.49e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823315871 820 RLLLVDDSLSVRRLVGRMLERGGYQVVTASDGQEALDLLQQdADFGAVVTDLEMPRVNGYELLSavRARPATAGLPMLVM 899
Cdd:PRK10643    2 KILIVEDDTLLLQGLILALQTEGYACDCASTAREAEALLES-GHYSLVVLDLGLPDEDGLHLLR--RWRQKKYTLPVLIL 78
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1823315871 900 TTRAGEKHQRLAFQLGADDYFTKPVNEALLLRRLGTL 936
Cdd:PRK10643   79 TARDTLEDRVAGLDVGADDYLVKPFALEELHARIRAL 115
HPT cd00088
Histidine Phosphotransfer domain, involved in signalling through a two part component systems ...
6-109 9.57e-05

Histidine Phosphotransfer domain, involved in signalling through a two part component systems in which an autophosphorylating histidine protein kinase serves as a phosphoryl donor to a response regulator protein; the response regulator protein is modulated by phosphorylation and dephosphorylation of a conserved aspartic acid residue; two-component proteins are abundant in most eubacteria; In E. coli there are 62 two-component proteins involved in a variety of processes such as chemotaxis, osmoregulation, metabolism and transport 1; also present in both Gram positive and Gram negative pathogenic bacteria where they regulate basic housekeeping functions and control expression of toxins and other proteins important for pathogenesis; in archaea and eukaryotes, two-component pathways constitute a very small number of all signaling systems; in fungi they mediate environmental stress responses and, in pathogenic yeast, hyphal development. In Dictyostelium and in plants, they are involved in important processes such as osmoregulation, cell growth, and differentiation; to date two-component proteins have not been identified in animals; in most prokaryotic systems, the output response is effected directly by the RR, which functions as a transcription factor while in eukaryotic systems, two-component proteins are found at the beginning of signaling pathways where they interface with more conventional eukaryotic signaling strategies such as MAP kinase and cyclic nucleotide cascades


Pssm-ID: 238041 [Multi-domain]  Cd Length: 94  Bit Score: 41.98  E-value: 9.57e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823315871   6 SELLESFREEAAEVLSGLEEGVTGLRTlsgaaghahdtpelAAHLGDLSVLAHRLRGSAALYGYAQLSTLASLQERLLDA 85
Cdd:cd00088     2 EELLELFLEEAEELLEELERALLELED--------------AEDLNEIFRAAHTLKGSAASLGLQRLAQLAHQLEDLLDA 67
                          90       100
                  ....*....|....*....|....*..
gi 1823315871  86 ---RPQLDREQHQEFLTLLEQVNAALR 109
Cdd:cd00088    68 lrdGLEVTPELIDLLLDALDALKAELE 94
PRK13856 PRK13856
two-component response regulator VirG; Provisional
819-933 1.22e-04

two-component response regulator VirG; Provisional


Pssm-ID: 172377 [Multi-domain]  Cd Length: 241  Bit Score: 44.80  E-value: 1.22e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823315871 819 QRLLLVDDSLSVRRLVGRMLERGGYQVVTASDGQEALDLLQQDAdFGAVVTDLEMPRVNGYELlsaVRARPATAGLPMLV 898
Cdd:PRK13856    2 KHVLVIDDDVAMRHLIVEYLTIHAFKVTAVADSQQFNRVLASET-VDVVVVDLNLGREDGLEI---VRSLATKSDVPIII 77
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1823315871 899 MT-TRAGEKHQRLAFQLGADDYFTKPVNEALLLRRL 933
Cdd:PRK13856   78 ISgDRLEEADKVVALELGATDFIAKPFGTREFLARI 113
PRK10710 PRK10710
DNA-binding transcriptional regulator BaeR; Provisional
814-923 1.45e-04

DNA-binding transcriptional regulator BaeR; Provisional


Pssm-ID: 182665 [Multi-domain]  Cd Length: 240  Bit Score: 44.29  E-value: 1.45e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823315871 814 QATGNQRLLLVDDSLSVRRLVGRMLERGGYQVVTASDGQEALDLLQQDADfGAVVTDLEMPRVNGYELLSAVRArpaTAG 893
Cdd:PRK10710    6 IDENTPRILIVEDEPKLGQLLIDYLQAASYATTLLSHGDEVLPYVRQTPP-DLILLDLMLPGTDGLTLCREIRR---FSD 81
                          90       100       110
                  ....*....|....*....|....*....|
gi 1823315871 894 LPMLVMTTRAGEKHQRLAFQLGADDYFTKP 923
Cdd:PRK10710   82 IPIVMVTAKIEEIDRLLGLEIGADDYICKP 111
REC_DesR-like cd19930
phosphoacceptor receiver (REC) domain of DesR and similar proteins; This group is composed of ...
821-922 1.73e-04

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: 41.87  E-value: 1.73e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823315871 821 LLLVDDSLSVRRLVGRMLER-GGYQVVT-ASDGQEALDLLQQDAdFGAVVTDLEMPRVNGYELLSAVRAR-PATAglpML 897
Cdd:cd19930     1 VLIAEDQEMVRGALAALLELeDDLEVVAqASNGQEALRLVLKHS-PDVAILDIEMPGRTGLEVAAELREElPDTK---VL 76
                          90       100
                  ....*....|....*....|....*
gi 1823315871 898 VMTTRAGEKHQRLAFQLGADDYFTK 922
Cdd:cd19930    77 IVTTFGRPGYFRRALAAGVDGYVLK 101
PRK12555 PRK12555
chemotaxis-specific protein-glutamate methyltransferase CheB;
820-924 1.82e-04

chemotaxis-specific protein-glutamate methyltransferase CheB;


Pssm-ID: 237135 [Multi-domain]  Cd Length: 337  Bit Score: 44.87  E-value: 1.82e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823315871 820 RLLLVDDSLSVRRLVGRMLE-RGGYQVV-TASDGQEALDLLQQDA-DFgaVVTDLEMPRVNGYELLSAV-RARPatagLP 895
Cdd:PRK12555    2 RIGIVNDSPLAVEALRRALArDPDHEVVwVATDGAQAVERCAAQPpDV--ILMDLEMPRMDGVEATRRImAERP----CP 75
                          90       100       110
                  ....*....|....*....|....*....|.
gi 1823315871 896 MLVMTTRAGEKHQRL--AFQLGADDYFTKPV 924
Cdd:PRK12555   76 ILIVTSLTERNASRVfeAMGAGALDAVDTPT 106
HATPase_EvgS-ArcB-TorS-like cd16922
Histidine kinase-like ATPase domain of two-component sensor histidine kinases, many are hybrid ...
552-662 1.99e-04

Histidine kinase-like ATPase domain of two-component sensor histidine kinases, many are hybrid sensor histidine kinases, similar to Escherichia coli EvgS, ArcB, TorS, BarA, RcsC; This family contains the histidine kinase-like ATPase (HATPase) domains of various two-component hybrid sensor histidine kinases (HKs), including the following Escherichia coli HKs: EvgS, a HK of the EvgS-EvgA two-component system (TCS) that confers acid resistance; ArcB, a HK of the ArcB-ArcA TCS that modulates the expression of numerous genes in response to respiratory growth conditions; TorS, a HK of the TorS-TorR TCS which is involved in the anaerobic utilization of trimethylamine-N-oxide; BarA, a HK of the BarA-UvrY TCS involved in the regulation of carbon metabolism; and RcsC, a HK of the RcsB-RcsC TCS which regulates the expression of the capsule operon and of the cell division gene ftsZ. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA), with most having accessory sensor domain(s) such as GAF, PAS and CHASE; many are hybrid sensor histidine kinases as they also contain a REC signal receiver domain.


Pssm-ID: 340399 [Multi-domain]  Cd Length: 110  Bit Score: 41.71  E-value: 1.99e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823315871 552 PQGTVWIRAA-----EQGNFLEVTVADDGQGLdyarireralerglrSAQELEQLssdelgrlillpgF--------STA 618
Cdd:cd16922    17 EEGEVTLRVSleeeeEDGVQLRFSVEDTGIGI---------------PEEQQARL-------------FepfsqadsSTT 68
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1823315871 619 REVGnvaGRGVGLDVVATAVRQLGGELLISSERGVGTAFTLRVP 662
Cdd:cd16922    69 RKYG---GTGLGLAISKKLVELMGGDISVESEPGQGSTFTFTLP 109
PRK10693 PRK10693
two-component system response regulator RssB;
848-924 2.45e-04

two-component system response regulator RssB;


Pssm-ID: 182652 [Multi-domain]  Cd Length: 303  Bit Score: 44.21  E-value: 2.45e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823315871 848 ASDGQEALDLL-QQDADFgaVVTDLEMPRVNGYELLSAVRARPATagLPMLVMTtrAGEKHQRLA--FQLGADDYFTKPV 924
Cdd:PRK10693    3 AANGVDALELLgGFTPDL--IICDLAMPRMNGIEFVEHLRNRGDQ--TPVLVIS--ATENMADIAkaLRLGVQDVLLKPV 76
PRK10364 PRK10364
two-component system sensor histidine kinase ZraS;
553-662 2.81e-04

two-component system sensor histidine kinase ZraS;


Pssm-ID: 236674 [Multi-domain]  Cd Length: 457  Bit Score: 44.39  E-value: 2.81e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823315871 553 QGTVWIRAAEQGNFLEVTVADDGQGLdyarireralerglrSAQELEQlssdelgrlILLPGFSTAREvgnvaGRGVGLD 632
Cdd:PRK10364  367 HGVISVTASESGAGVKISVTDSGKGI---------------AADQLEA---------IFTPYFTTKAE-----GTGLGLA 417
                          90       100       110
                  ....*....|....*....|....*....|
gi 1823315871 633 VVATAVRQLGGELLISSERGVGTAFTLRVP 662
Cdd:PRK10364  418 VVHNIVEQHGGTIQVASQEGKGATFTLWLP 447
REC_HupR cd17596
phosphoacceptor receiver (REC) domain of hydrogen uptake protein regulator (HupR); Members of ...
819-888 4.71e-04

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


Pssm-ID: 381127 [Multi-domain]  Cd Length: 133  Bit Score: 41.20  E-value: 4.71e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823315871 819 QRLLLVDDSLSVRRLVGRMLERGgYQVVTASDGQEALDLLQqDADFGAVVTDLEMPRVNGYELLSAVRAR 888
Cdd:cd17596     1 PTILVVDDEVRSLEALRRTLEED-FDVLTAASAEEALAILE-EEWVQVILCDQRMPGTTGVEFLKEVRER 68
PRK11100 PRK11100
sensory histidine kinase CreC; Provisional
445-663 5.69e-04

sensory histidine kinase CreC; Provisional


Pssm-ID: 236846 [Multi-domain]  Cd Length: 475  Bit Score: 43.68  E-value: 5.69e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823315871 445 AEVRRRLSDTaaeLSEENEQLGKLVRRL--------RLDVNQTSRVAFSQTTARL--RRWAREQQADLTLQVEGED--VL 512
Cdd:PRK11100  287 PEDRARFTGN---ILTQSARLQQLIDRLlelarleqRQELEVLEPVALAALLEELveAREAQAAAKGITLRLRPDDarVL 363
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823315871 513 IESGILQRisdPLLHLLTNAAYHglasesaesrraagKNPQGTVWIRAAEQGNFLEVTVADDGQGL-DYAriRERALERg 591
Cdd:PRK11100  364 GDPFLLRQ---ALGNLLDNAIDF--------------SPEGGTITLSAEVDGEQVALSVEDQGPGIpDYA--LPRIFER- 423
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1823315871 592 lrsaqeleqlssdelgrlillpGFSTAREVGNVAGRGVGLDVVATAVRQLGGELLISSERGVGTAFTLRVPT 663
Cdd:PRK11100  424 ----------------------FYSLPRPANGRKSTGLGLAFVREVARLHGGEVTLRNRPEGGVLATLTLPR 473
NtrB COG3852
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms];
556-666 6.46e-04

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


Pssm-ID: 443061 [Multi-domain]  Cd Length: 361  Bit Score: 42.91  E-value: 6.46e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823315871 556 VWIRAAEQGNFLEVTVADDGQGLDyARIRERalerglrsaqeleqlssdelgrlILLPGFSTaREvgnvAGRGVGLDVVA 635
Cdd:COG3852   276 VTLGGLRPRLYVRIEVIDNGPGIP-EEILDR-----------------------IFEPFFTT-KE----KGTGLGLAIVQ 326
                          90       100       110
                  ....*....|....*....|....*....|.
gi 1823315871 636 TAVRQLGGELLISSERGVGTAFTLRVPTTQR 666
Cdd:COG3852   327 KIVEQHGGTIEVESEPGKGTTFRIYLPLEQA 357
HPT smart00073
Histidine Phosphotransfer domain; Contains an active histidine residue that mediates ...
7-109 9.46e-04

Histidine Phosphotransfer domain; Contains an active histidine residue that mediates phosphotransfer reactions. Domain detected only in eubacteria. This alignment is an extension to that shown in the Cell structure paper.


Pssm-ID: 197502 [Multi-domain]  Cd Length: 92  Bit Score: 39.15  E-value: 9.46e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823315871    7 ELLESFREEAAEVLSGLEEGVtglrtlsGAAGHAHDtpelAAHLGDLSVLAHRLRGSAALYGYAQLSTLASLQERLLDAR 86
Cdd:smart00073   1 GGLELFREELAEFLQSLEEGL-------LELEKALD----AQDVNEIFRAAHTLKGSAGSLGLQQLAQLCHQLENLLDAL 69
                           90       100
                   ....*....|....*....|...
gi 1823315871   87 PQLDREQHQEFLTLLEQVNAALR 109
Cdd:smart00073  70 RSGEVELTPDLLDLLLELVDVLK 92
Hpt pfam01627
Hpt domain; The histidine-containing phosphotransfer (HPt) domain is a novel protein module ...
7-107 1.07e-03

Hpt domain; The histidine-containing phosphotransfer (HPt) domain is a novel protein module with an active histidine residue that mediates phosphotransfer reactions in the two-component signaling systems. A multistep phosphorelay involving the HPt domain has been suggested for these signaling pathways. The crystal structure of the HPt domain of the anaerobic sensor kinase ArcB has been determined. The domain consists of six alpha helices containing a four-helix bundle-folding. The pattern of sequence similarity of the HPt domains of ArcB and components in other signaling systems can be interpreted in light of the three-dimensional structure and supports the conclusion that the HPt domains have a common structural motif both in prokaryotes and eukaryotes. In S. cerevisiae ypd1p this domain has been shown to contain a binding surface for Ssk1p (response regulator receiver domain containing protein pfam00072).


Pssm-ID: 426352 [Multi-domain]  Cd Length: 84  Bit Score: 38.87  E-value: 1.07e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823315871   7 ELLESFREEAAEVLSGLEEgvtglrtlsgaAGHAHDTPELAAHlgdlsvlAHRLRGSAALYGYAQLSTLA-SLQERLLDA 85
Cdd:pfam01627   1 ELLELFLEEAPELLEQLEQ-----------ALDAEDLEALFRA-------AHTLKGSAGSLGLPALAELAhELEDLLREG 62
                          90       100
                  ....*....|....*....|..
gi 1823315871  86 RPQLDREQHQEFLTLLEQVNAA 107
Cdd:pfam01627  63 ELPLDPELLEALRDLLEALRAA 84
PRK10701 PRK10701
DNA-binding transcriptional regulator RstA; Provisional
818-942 1.30e-03

DNA-binding transcriptional regulator RstA; Provisional


Pssm-ID: 236738 [Multi-domain]  Cd Length: 240  Bit Score: 41.55  E-value: 1.30e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823315871 818 NQRLLLVDDSLSVRRLVGRMLERGGYQVVTASDGQEALD-LLQQDADFgaVVTDLEMPRVNGYELLSAVRARPATaglPM 896
Cdd:PRK10701    1 MNKIVFVEDDAEVGSLIAAYLAKHDIDVTVEPRGDRAEAtILREQPDL--VLLDIMLPGKDGMTICRDLRPKWQG---PI 75
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1823315871 897 LVMTTRAGEKHQRLAFQLGADDYFTKPVNEALLLRRLGT-LQQAQQA 942
Cdd:PRK10701   76 VLLTSLDSDMNHILALEMGACDYILKTTPPAVLLARLRLhLRQNEQA 122
REC_DC-like cd17534
phosphoacceptor receiver (REC) domain of modulated diguanylate cyclase and similar domains; ...
820-860 1.57e-03

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: 39.31  E-value: 1.57e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1823315871 820 RLLLVDDSLSVRRLVGRMLERGGYQVV-TASDGQEALDLLQQ 860
Cdd:cd17534     2 KILIVEDEAIIALDLKEILESLGYEVVgIADSGEEAIELAEE 43
COG3920 COG3920
Two-component sensor histidine kinase, HisKA and HATPase domains [Signal transduction ...
500-666 3.02e-03

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


Pssm-ID: 443125 [Multi-domain]  Cd Length: 495  Bit Score: 41.04  E-value: 3.02e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823315871 500 ADLTLQVEGEDVLIESGILQRISdPLLH-LLTNAAYHGLASesaesrraagkNPQGTVWIRAAEQGNFLEVTVADDGQGL 578
Cdd:COG3920   379 RGIRIELDGPDVELPADAAVPLG-LILNeLVTNALKHAFLS-----------GEGGRIRVSWRREDGRLRLTVSDNGVGL 446
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823315871 579 DyarireralerglrsaqeleqlssdelgrlillPGFSTARevgnvaGRGVGLDVVATAVRQLGGELLISSERgvGTAFT 658
Cdd:COG3920   447 P---------------------------------EDVDPPA------RKGLGLRLIRALVRQLGGTLELDRPE--GTRVR 485

                  ....*...
gi 1823315871 659 LRVPTTQR 666
Cdd:COG3920   486 ITFPLAEL 493
CheW COG0835
Chemotaxis signal transduction protein CheW [Signal transduction mechanisms];
712-800 3.73e-03

Chemotaxis signal transduction protein CheW [Signal transduction mechanisms];


Pssm-ID: 440597  Cd Length: 151  Bit Score: 39.09  E-value: 3.73e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823315871 712 GQPVPVVDARPIWGHAPQDTDTEAHLAVVSSISGLLALRVHDFGDIEEV---AVTAPSGLLAPL--DYLAGMAVSGtGQV 786
Cdd:COG0835    54 GRVVPVIDLRALLGLPPTEDTERTRIIVLEVGGRVVGLLVDSVSGVVRIdpdDIEPPPELLSGGlaPFITGVAKLD-DRL 132
                          90
                  ....*....|....
gi 1823315871 787 LAILDPAGVLRLSR 800
Cdd:COG0835   133 ILLLDLEKLLAEEE 146
PEP_resp_reg TIGR02915
PEP-CTERM-box response regulator transcription factor; Members of this protein family share ...
821-929 5.41e-03

PEP-CTERM-box response regulator transcription factor; Members of this protein family share full-length homology with (but do not include) the acetoacetate metabolism regulatory protein AtoC (see SP|Q06065). These proteins have a Fis family DNA binding sequence (pfam02954), a response regulator receiver domain (pfam00072), and sigma-54 interaction domain (pfam00158). [Regulatory functions, DNA interactions]


Pssm-ID: 274348 [Multi-domain]  Cd Length: 445  Bit Score: 40.50  E-value: 5.41e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823315871 821 LLLVDDSLSVRRLVGRMLErgGYQVVTASDGQEALDLLQQDADfgAVVT-DLEMP-----RVNGYELLSAV-RARPATAg 893
Cdd:TIGR02915   1 LLIVEDDLGLQKQLKWSFA--DYELAVAADRESAIALVRRHEP--AVVTlDLGLPpdadgASEGLAALQQIlAIAPDTK- 75
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1823315871 894 lpMLVMTTRAGEKHQRLAFQLGADDYFTKPVNEALL 929
Cdd:TIGR02915  76 --VIVITGNDDRENAVKAIGLGAYDFYQKPIDPDVL 109
PksD COG3321
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ...
599-946 7.25e-03

Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442550 [Multi-domain]  Cd Length: 1386  Bit Score: 40.24  E-value: 7.25e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823315871  599 EQLSSDELGRLILLPGFSTAREVGNVAGRGVGLDVVATAVRQLGGELLISSERGVGTAFTLRVPTTQRimdvLHLDLGAG 678
Cdd:COG3321    850 SALYPGRGRRRVPLPTYPFQREDAAAALLAAALAAALAAAAALGALLLAALAAALAAALLALAAAAAA----ALALAAAA 925
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823315871  679 HHAALPVGSVRSLRDVPLGDLRRDDGQLWLDFGGQPVPVVDARPIWGHAPQDTDTEAHLAVVSSISGLLALRVHDFGDIE 758
Cdd:COG3321    926 LAALLALVALAAAAAALLALAAAAAAAAAALAAAEAGALLLLAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAALALL 1005
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823315871  759 EVAVTAPSGLLAPLDYLAGMAVSGTGQVLAILDPAGVLRLSRRPATWLGQAQRQVQATGNQRLLLVDDSLSVRRLVGRML 838
Cdd:COG3321   1006 AAAALLLAAAAAAAALLALAALLAAAAAALAAAAAAAAAAAALAALAAAAAAAAALALALAALLLLAALAELALAAAALA 1085
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823315871  839 ERGGYQVVTASDGQEALDLLQQDADFGAVVTDLEMPRVNGYELLSAVRARPATAGLPMLVMTTRAGEKHQRLAFQLGADD 918
Cdd:COG3321   1086 LAAALAAAALALALAALAAALLLLALLAALALAAAAAALLALAALLAAAAAAAALAAAAAAAAALALAAAAAALAAALAA 1165
                          330       340
                   ....*....|....*....|....*...
gi 1823315871  919 YFTKPVNEALLLRRLGTLQQAQQAGVSA 946
Cdd:COG3321   1166 ALLAAAALLLALALALAAALAAALAGLA 1193
RsbW COG2172
Anti-sigma regulatory factor (Ser/Thr protein kinase) [Signal transduction mechanisms];
489-607 7.78e-03

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


Pssm-ID: 441775 [Multi-domain]  Cd Length: 127  Bit Score: 37.59  E-value: 7.78e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823315871 489 ARLRRWAREQQADLTLQVEGEDVLIEsgilqrisdpllhLLTNAAYHGlasesaesrraAGKNPQGTVWIRAAEQGNFLE 568
Cdd:COG2172    16 RAVRALLRELGLDEDDADDLVLAVSE-------------AVTNAVRHA-----------YGGDPDGPVEVELELDPDGLE 71
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1823315871 569 VTVADDGQGLDYARIRERALE-----RGLRSAQELeqlsSDELG 607
Cdd:COG2172    72 IEVRDEGPGFDPEDLPDPYSTlaeggRGLFLIRRL----MDEVE 111
 
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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