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Conserved domains on  [gi|2129446385|dbj|BDC27239|]
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sensor histidine kinase [Bordetella parapertussis]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PRK13557 super family cl36263
histidine kinase; Provisional
565-985 1.08e-99

histidine kinase; Provisional


The actual alignment was detected with superfamily member PRK13557:

Pssm-ID: 237425 [Multi-domain]  Cd Length: 540  Bit Score: 323.93  E-value: 1.08e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129446385 565 KDGSYHWITWSLS---RAEGN-VYLAGrddtdlkAQAEVLR--QTEDALRQSQKLEAVGRLTGGIAHDFNNMLQGISGAL 638
Cdd:PRK13557  113 KDGSSFWNALFVSpvyNDAGDlVYFFG-------SQLDVSRrrDAEDALRQAQKMEALGQLTGGIAHDFNNLLQVMSGYL 185
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129446385 639 YLIDRKLRRSK--PEEVGKYVRTAQESTDRAARLTQRLLTFSRQQAIDPQVFDPGDILRSMDELFRRYTGEQVRLTLKLP 716
Cdd:PRK13557  186 DVIQAALSHPDadRGRMARSVENIRAAAERAATLTQQLLAFARKQRLEGRVLNLNGLVSGMGELAERTLGDAVTIETDLA 265
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129446385 717 AQSWRVRCDMNQFENAVLNLVINACDAMPAGGDLEIEVAHRELDAAAVQTNPCAEAGEFVEVCVSDMGCGMAPDVLARVF 796
Cdd:PRK13557  266 PDLWNCRIDPTQAEVALLNVLINARDAMPEGGRVTIRTRNVEIEDEDLAMYHGLPPGRYVSIAVTDTGSGMPPEILARVM 345
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129446385 797 EPFFTTKPMGQGTGLGLSMIYGFAQQAGGMVTIASVQAEGTAVRLFLPrhVGEPVALPAPESSEPPAAPAHAAVVALVED 876
Cdd:PRK13557  346 DPFFTTKEEGKGTGLGLSMVYGFAKQSGGAVRIYSEVGEGTTVRLYFP--ASDQAENPEQEPKARAIDRGGTETILIVDD 423
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129446385 877 DEHVRDMVRAALEELNLTVLTAADGDAGHRLLQSDARIDLLLSDVGLPG-MNGHALAQAARALRPALRIILMTGYAD--- 952
Cdd:PRK13557  424 RPDVAELARMILEDFGYRTLVASNGREALEILDSHPEVDLLFTDLIMPGgMNGVMLAREARRRQPKIKVLLTTGYAEasi 503
                         410       420       430
                  ....*....|....*....|....*....|...
gi 2129446385 953 ERENGwARQERDVslIRKPFSPGELTARVCRLL 985
Cdd:PRK13557  504 ERTDA-GGSEFDI--LNKPYRRAELARRVRMVL 533
PAS super family cl21578
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
488-600 2.16e-12

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


The actual alignment was detected with superfamily member TIGR00229:

Pssm-ID: 473914 [Multi-domain]  Cd Length: 124  Bit Score: 65.00  E-value: 2.16e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129446385 488 IWRLSPELLAVADHGGRLVSVNPAVRAILGWSPEQFLAMGLDEGVHPEDLASMQATLEAEPAEGMQPVRHLEsRLLHKDG 567
Cdd:TIGR00229   8 IFESSPDAIIVIDLEGNILYVNPAFEEIFGYSAEELIGRNVLELIPEEDREEVRERIERRLEGEPEPVSEER-RVRRKDG 86
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2129446385 568 SYHWITWSLS--RAEGNV--YLAG-RDDTDLKAQAEVL 600
Cdd:TIGR00229  87 SEIWVEVSVSpiRTNGGElgVVGIvRDITERKEAEEAL 124
GAF COG2203
GAF domain [Signal transduction mechanisms];
16-547 6.83e-12

GAF domain [Signal transduction mechanisms];


:

Pssm-ID: 441805 [Multi-domain]  Cd Length: 712  Bit Score: 69.45  E-value: 6.83e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129446385  16 LARLEDERVMLQRIAAGVPLTDVLLHVMQAVEAQSSVELlTSIAFVDDSGMRLRHVATPSLPAAYVqatdgAAIGPGVAS 95
Cdd:COG2203   189 LERLALLNEISQALRSALDLEELLQRILELAGELLGADR-GAILLVDEDGGELELVAAPGLPEEEL-----GRLPLGEGL 262
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129446385  96 WGAAAFLGTPVYVEDLTVHPNW-PPWREAATQHGLRACWSTPIKAtDGRTLGVFSNYYRQPRLPTREDIEAIALVTRTAA 174
Cdd:COG2203   263 AGRALRTGEPVVVNDASTDPRFaPSLRELLLALGIRSLLCVPLLV-DGRLIGVLALYSKEPRAFTEEDLELLEALADQAA 341
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129446385 175 LAIERHLTEQALRnssVRWRGMFERMQEGFFLAEAQRDSTGSVDDFTLLEINPAFETQSGLAVGQTLGPMLRVMSPAAAD 254
Cdd:COG2203   342 IAIERARLYEALE---AALAALLQELALLRLLLDLELTLLRLRQLLLELLLALLLLLSLLGAELLLLLLDAADLSGLLAL 418
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129446385 255 SIMRIFVGVIESGEPAQFEVEAPGPPQACYECRAGKEGHDRVAALFLNVTARKLAESELWERQYRKNFLLTLGDRMREIH 334
Cdd:COG2203   419 EGLLLLDLLLLLLLLRRILLLRVLRRLLLGDEEGLVLLLALAELELLEILELLVLLAVILLALALLAALLLLLLLLLALL 498
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129446385 335 QQDQIEQMVCEELGRHLELGAVAVMESVPQRGDRIAASWGPRPPYDGRSMLESAPLTPDYYEAVRKGRTAYLSPYLAGPA 414
Cdd:COG2203   499 ALSALAVLASLLLALLLLLLLLLLLLLLGLLAALAADLLLLAAALLEDLLILLLVLLLERELLTLVGVLLLLGLSVLLIE 578
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129446385 415 GNQQPSAIVVPLRRWGRADGTLLVRPDPTHPLKGTDIAFIEEAAERMCEAIERSQYARVLEQRVEHAIAERDRIWRLSPE 494
Cdd:COG2203   579 LALALILALALLELLLVAVGDLLLLERDLLLLLVLLVRLLLELLVVTLELTVLVVLAAVEDSALLLRLALALASLVLLRA 658
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2129446385 495 LLAVADHGGRLVSVNPAVRAILGWSPEQFLAMGLDEGVHPEDLASMQATLEAE 547
Cdd:COG2203   659 LLATELDLILDSSLLLGLLLLGALLLLGGGLALLLSIGLGLGVARLLQLSVLE 711
 
Name Accession Description Interval E-value
PRK13557 PRK13557
histidine kinase; Provisional
565-985 1.08e-99

histidine kinase; Provisional


Pssm-ID: 237425 [Multi-domain]  Cd Length: 540  Bit Score: 323.93  E-value: 1.08e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129446385 565 KDGSYHWITWSLS---RAEGN-VYLAGrddtdlkAQAEVLR--QTEDALRQSQKLEAVGRLTGGIAHDFNNMLQGISGAL 638
Cdd:PRK13557  113 KDGSSFWNALFVSpvyNDAGDlVYFFG-------SQLDVSRrrDAEDALRQAQKMEALGQLTGGIAHDFNNLLQVMSGYL 185
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129446385 639 YLIDRKLRRSK--PEEVGKYVRTAQESTDRAARLTQRLLTFSRQQAIDPQVFDPGDILRSMDELFRRYTGEQVRLTLKLP 716
Cdd:PRK13557  186 DVIQAALSHPDadRGRMARSVENIRAAAERAATLTQQLLAFARKQRLEGRVLNLNGLVSGMGELAERTLGDAVTIETDLA 265
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129446385 717 AQSWRVRCDMNQFENAVLNLVINACDAMPAGGDLEIEVAHRELDAAAVQTNPCAEAGEFVEVCVSDMGCGMAPDVLARVF 796
Cdd:PRK13557  266 PDLWNCRIDPTQAEVALLNVLINARDAMPEGGRVTIRTRNVEIEDEDLAMYHGLPPGRYVSIAVTDTGSGMPPEILARVM 345
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129446385 797 EPFFTTKPMGQGTGLGLSMIYGFAQQAGGMVTIASVQAEGTAVRLFLPrhVGEPVALPAPESSEPPAAPAHAAVVALVED 876
Cdd:PRK13557  346 DPFFTTKEEGKGTGLGLSMVYGFAKQSGGAVRIYSEVGEGTTVRLYFP--ASDQAENPEQEPKARAIDRGGTETILIVDD 423
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129446385 877 DEHVRDMVRAALEELNLTVLTAADGDAGHRLLQSDARIDLLLSDVGLPG-MNGHALAQAARALRPALRIILMTGYAD--- 952
Cdd:PRK13557  424 RPDVAELARMILEDFGYRTLVASNGREALEILDSHPEVDLLFTDLIMPGgMNGVMLAREARRRQPKIKVLLTTGYAEasi 503
                         410       420       430
                  ....*....|....*....|....*....|...
gi 2129446385 953 ERENGwARQERDVslIRKPFSPGELTARVCRLL 985
Cdd:PRK13557  504 ERTDA-GGSEFDI--LNKPYRRAELARRVRMVL 533
NtrB COG3852
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms];
486-850 2.01e-82

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


Pssm-ID: 443061 [Multi-domain]  Cd Length: 361  Bit Score: 271.33  E-value: 2.01e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129446385 486 DRIWRLSPELLAVADHGGRLVSVNPAVRAILGWSPEQFLAMGLDEgVHPEDlASMQATLEAEPAEGmQPVRHLESRLLHK 565
Cdd:COG3852    10 RAILDSLPDAVIVLDADGRITYVNPAAERLLGLSAEELLGRPLAE-LFPED-SPLRELLERALAEG-QPVTEREVTLRRK 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129446385 566 DGSYHWITWSLSR---AEGNVYLAG--RDDTDLKaqaevlrQTEDALRQSQKLEAVGRLTGGIAHDFNNMLQGISGALYL 640
Cdd:COG3852    87 DGEERPVDVSVSPlrdAEGEGGVLLvlRDITERK-------RLERELRRAEKLAAVGELAAGLAHEIRNPLTGIRGAAQL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129446385 641 IDRKLrrsKPEEVGKYVRTAQESTDRAARLTQRLLTFSRQQAIDPQVFDPGDILRSMDELFRRYTGEQVRLTLKLPAQSW 720
Cdd:COG3852   160 LEREL---PDDELREYTQLIIEEADRLNNLVDRLLSFSRPRPPEREPVNLHEVLERVLELLRAEAPKNIRIVRDYDPSLP 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129446385 721 RVRCDMNQFENAVLNLVINACDAMPAGGDLEIEVAHRELDaaavqTNPCAEAGEFVEVCVSDMGCGMAPDVLARVFEPFF 800
Cdd:COG3852   237 EVLGDPDQLIQVLLNLVRNAAEAMPEGGTITIRTRVERQV-----TLGGLRPRLYVRIEVIDNGPGIPEEILDRIFEPFF 311
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|
gi 2129446385 801 TTKPmgQGTGLGLSMIYGFAQQAGGMVTIASVQAEGTAVRLFLPRHVGEP 850
Cdd:COG3852   312 TTKE--KGTGLGLAIVQKIVEQHGGTIEVESEPGKGTTFRIYLPLEQAEE 359
HATPase_CckA-like cd16919
Histidine kinase-like ATPase domain of two-component sensor hybrid histidine kinases, similar ...
729-844 2.33e-44

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: 156.00  E-value: 2.33e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129446385 729 FENAVLNLVINACDAMPAGGDLEIEVAHRELDAAAVQTNPCAEAGEFVEVCVSDMGCGMAPDVLARVFEPFFTTKPMGQG 808
Cdd:cd16919     1 LELAILNLAVNARDAMPEGGRLTIETSNQRVDADYALNYRDLIPGNYVCLEVSDTGSGMPAEVLRRAFEPFFTTKEVGKG 80
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2129446385 809 TGLGLSMIYGFAQQAGGMVTIASVQAEGTAVRLFLP 844
Cdd:cd16919    81 TGLGLSMVYGFVKQSGGHLRIYSEPGVGTTVRIYLP 116
HATPase_c smart00387
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.
725-844 1.69e-23

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


Pssm-ID: 214643 [Multi-domain]  Cd Length: 111  Bit Score: 96.18  E-value: 1.69e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129446385  725 DMNQFENAVLNLVINACDAMPAGGDLEIEVAHReldaaavqtnpcaeaGEFVEVCVSDMGCGMAPDVLARVFEPFFTTKP 804
Cdd:smart00387   2 DPDRLRQVLSNLLDNAIKYTPEGGRITVTLERD---------------GDHVEITVEDNGPGIPPEDLEKIFEPFFRTDK 66
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 2129446385  805 ---MGQGTGLGLSMIYGFAQQAGGMVTIASVQAEGTAVRLFLP 844
Cdd:smart00387  67 rsrKIGGTGLGLSIVKKLVELHGGEISVESEPGGGTTFTITLP 109
HATPase_c pfam02518
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the ...
732-844 4.07e-21

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


Pssm-ID: 460579 [Multi-domain]  Cd Length: 109  Bit Score: 89.35  E-value: 4.07e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129446385 732 AVLNLVINACDAMPAGGDLEIEVahreldaaavqtnpcaEAGEFVEVCVSDMGCGMAPDVLARVFEPFFTT-KPMGQGTG 810
Cdd:pfam02518   9 VLSNLLDNALKHAAKAGEITVTL----------------SEGGELTLTVEDNGIGIPPEDLPRIFEPFSTAdKRGGGGTG 72
                          90       100       110
                  ....*....|....*....|....*....|....
gi 2129446385 811 LGLSMIYGFAQQAGGMVTIASVQAEGTAVRLFLP 844
Cdd:pfam02518  73 LGLSIVRKLVELLGGTITVESEPGGGTTVTLTLP 106
sensory_box TIGR00229
PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain ...
488-600 2.16e-12

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


Pssm-ID: 272971 [Multi-domain]  Cd Length: 124  Bit Score: 65.00  E-value: 2.16e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129446385 488 IWRLSPELLAVADHGGRLVSVNPAVRAILGWSPEQFLAMGLDEGVHPEDLASMQATLEAEPAEGMQPVRHLEsRLLHKDG 567
Cdd:TIGR00229   8 IFESSPDAIIVIDLEGNILYVNPAFEEIFGYSAEELIGRNVLELIPEEDREEVRERIERRLEGEPEPVSEER-RVRRKDG 86
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2129446385 568 SYHWITWSLS--RAEGNV--YLAG-RDDTDLKAQAEVL 600
Cdd:TIGR00229  87 SEIWVEVSVSpiRTNGGElgVVGIvRDITERKEAEEAL 124
PAS cd00130
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
492-578 6.72e-12

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


Pssm-ID: 238075 [Multi-domain]  Cd Length: 103  Bit Score: 63.04  E-value: 6.72e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129446385 492 SPELLAVADHGGRLVSVNPAVRAILGWSPEQFLAMGLDEGVHPEDLASMQATLEAEPAEGmqPVRHLESRLLHKDGSYHW 571
Cdd:cd00130     1 LPDGVIVLDLDGRILYANPAAEQLLGYSPEELIGKSLLDLIHPEDREELRERLENLLSGG--EPVTLEVRLRRKDGSVIW 78

                  ....*..
gi 2129446385 572 ITWSLSR 578
Cdd:cd00130    79 VLVSLTP 85
GAF COG2203
GAF domain [Signal transduction mechanisms];
16-547 6.83e-12

GAF domain [Signal transduction mechanisms];


Pssm-ID: 441805 [Multi-domain]  Cd Length: 712  Bit Score: 69.45  E-value: 6.83e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129446385  16 LARLEDERVMLQRIAAGVPLTDVLLHVMQAVEAQSSVELlTSIAFVDDSGMRLRHVATPSLPAAYVqatdgAAIGPGVAS 95
Cdd:COG2203   189 LERLALLNEISQALRSALDLEELLQRILELAGELLGADR-GAILLVDEDGGELELVAAPGLPEEEL-----GRLPLGEGL 262
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129446385  96 WGAAAFLGTPVYVEDLTVHPNW-PPWREAATQHGLRACWSTPIKAtDGRTLGVFSNYYRQPRLPTREDIEAIALVTRTAA 174
Cdd:COG2203   263 AGRALRTGEPVVVNDASTDPRFaPSLRELLLALGIRSLLCVPLLV-DGRLIGVLALYSKEPRAFTEEDLELLEALADQAA 341
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129446385 175 LAIERHLTEQALRnssVRWRGMFERMQEGFFLAEAQRDSTGSVDDFTLLEINPAFETQSGLAVGQTLGPMLRVMSPAAAD 254
Cdd:COG2203   342 IAIERARLYEALE---AALAALLQELALLRLLLDLELTLLRLRQLLLELLLALLLLLSLLGAELLLLLLDAADLSGLLAL 418
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129446385 255 SIMRIFVGVIESGEPAQFEVEAPGPPQACYECRAGKEGHDRVAALFLNVTARKLAESELWERQYRKNFLLTLGDRMREIH 334
Cdd:COG2203   419 EGLLLLDLLLLLLLLRRILLLRVLRRLLLGDEEGLVLLLALAELELLEILELLVLLAVILLALALLAALLLLLLLLLALL 498
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129446385 335 QQDQIEQMVCEELGRHLELGAVAVMESVPQRGDRIAASWGPRPPYDGRSMLESAPLTPDYYEAVRKGRTAYLSPYLAGPA 414
Cdd:COG2203   499 ALSALAVLASLLLALLLLLLLLLLLLLLGLLAALAADLLLLAAALLEDLLILLLVLLLERELLTLVGVLLLLGLSVLLIE 578
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129446385 415 GNQQPSAIVVPLRRWGRADGTLLVRPDPTHPLKGTDIAFIEEAAERMCEAIERSQYARVLEQRVEHAIAERDRIWRLSPE 494
Cdd:COG2203   579 LALALILALALLELLLVAVGDLLLLERDLLLLLVLLVRLLLELLVVTLELTVLVVLAAVEDSALLLRLALALASLVLLRA 658
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2129446385 495 LLAVADHGGRLVSVNPAVRAILGWSPEQFLAMGLDEGVHPEDLASMQATLEAE 547
Cdd:COG2203   659 LLATELDLILDSSLLLGLLLLGALLLLGGGLALLLSIGLGLGVARLLQLSVLE 711
GAF_2 pfam13185
GAF domain; The GAF domain is named after some of the proteins it is found in, including ...
35-178 1.20e-11

GAF domain; The GAF domain is named after some of the proteins it is found in, including cGMP-specific phosphodiesterases, adenylyl cyclases and FhlA. It is also found in guanylyl cyclases and phytochromes. The structure of a GAF domain shows that the domain shares a similar fold with the PAS domain. This domain can bind O2, CO and NO (Matilla et.al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).


Pssm-ID: 433019 [Multi-domain]  Cd Length: 137  Bit Score: 63.25  E-value: 1.20e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129446385  35 LTDVLLHVMQAVEAQSSVELlTSIAFVDDSGmrlrHVATPSLPAAYVQATDGAAIGPGVasWGAAAFLGTPVYVEDLTVH 114
Cdd:pfam13185   4 LEELLDAVLEAAVELGASAV-GFILLVDDDG----RLAAWGGAADELSAALDDPPGEGL--VGEALRTGRPVIVNDLAAD 76
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2129446385 115 PNWPPWReaATQHGLRACWSTPIKAtDGRTLGVFSNYYRQPRLPTREDIEAIALVTRTAALAIE 178
Cdd:pfam13185  77 PAKKGLP--AGHAGLRSFLSVPLVS-GGRVVGVLALGSNRPGAFDEEDLELLELLAEQAAIAIE 137
PAS COG2202
PAS domain [Signal transduction mechanisms];
477-600 5.94e-11

PAS domain [Signal transduction mechanisms];


Pssm-ID: 441804 [Multi-domain]  Cd Length: 258  Bit Score: 63.89  E-value: 5.94e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129446385 477 RVEHAIAERDRIWRL----SPELLAVADHGGRLVSVNPAVRAILGWSPEQFLAMGLDEGVHPEDLASMQATLEaEPAEGM 552
Cdd:COG2202   127 RAEEALRESEERLRLlvenAPDGIFVLDLDGRILYVNPAAEELLGYSPEELLGKSLLDLLHPEDRERLLELLR-RLLEGG 205
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2129446385 553 QPVRHLESRLLHKDGSYHWITWSLSRAEGNVYLAG-----RDDTDLKAQAEVL 600
Cdd:COG2202   206 RESYELELRLKDGDGRWVWVEASAVPLRDGGEVIGvlgivRDITERKRAEEAL 258
PAS_3 pfam08447
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
506-572 8.73e-10

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


Pssm-ID: 430001 [Multi-domain]  Cd Length: 89  Bit Score: 56.19  E-value: 8.73e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2129446385 506 VSVNPAVRAILGWSPEQFLAMGLD--EGVHPEDLASMQATLEAEPAEGmQPVRHlESRLLHKDGSYHWI 572
Cdd:pfam08447   2 IYWSPRFEEILGYTPEELLGKGESwlDLVHPDDRERVREALWEALKGG-EPYSG-EYRIRRKDGEYRWV 68
nifL_nitrog TIGR02938
nitrogen fixation negative regulator NifL; NifL is a modulator of the nitrogen fixation ...
474-844 2.16e-09

nitrogen fixation negative regulator NifL; NifL is a modulator of the nitrogen fixation positive regulator protein NifA, and is therefore a negative regulator. It binds NifA. NifA and NifL are encoded by adjacent genes. [Central intermediary metabolism, Nitrogen fixation, Regulatory functions, Protein interactions]


Pssm-ID: 131984 [Multi-domain]  Cd Length: 494  Bit Score: 61.07  E-value: 2.16e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129446385 474 LEQRVEHAIAERDRIWRLSPELLAVADHGGRLVSVNPAVRAI-----LGWSPEQFLAMGLDEGVHP-EDLASMQATLEAE 547
Cdd:TIGR02938 121 LEQVVANQKLLIESVVDAAPVAFVLLDPTGRVILDNQEYKKLatdlrVKEPAHTVLDLLREAWREAlAENWPQQLAFSNR 200
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129446385 548 PAE----GMQPVRHLE---SRLLHKDGSYHwiTWSLSRAEGNVYLAGRDDTDLKAQAE--VLRQTEDALRQSQKLEAVGR 618
Cdd:TIGR02938 201 EARfdrgGGRPARWLSctgSVIGMESDCAD--SFFCAAEQPYLLLTIADISNLREEQEraRLSALQALMAEEERLEAIRE 278
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129446385 619 LTGGIAHDFNNMLQGISGALYLIDRKLRRSKPEEVGKYVRTAQESTDRAARLTQRLLTFSRQQAIDPqvFDPGDILR--- 695
Cdd:TIGR02938 279 TLSAAIHRLQGPMNLISAAISVLQRRGDDAGNPASAAMLQQALSAGREHMEALRQVIPQSPQEIVVP--VNLNQILRdvi 356
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129446385 696 --SMDELFRRYTGEQVRLTLKLPAqswrVRCDMNQFENAVLNLVINACDAMPAGGdleieVAHRELDAAAVQTNPCaeag 773
Cdd:TIGR02938 357 tlSTPRLLAAGIVVDWQPAATLPA----ILGRELQLRSLFKALVDNAIEAMNIKG-----WKRRELSITTALNGDL---- 423
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2129446385 774 efVEVCVSDMGCGMAPDVLARVFEPFFTTK-PMGQGTGLGLSMIYGFAQQAGGMVTIASVQAEGTAVRLFLP 844
Cdd:TIGR02938 424 --IVVSILDSGPGIPQDLRYKVFEPFFTTKgGSRKHIGMGLSVAQEIVADHGGIIDLDDDYSEGCRIIVEFR 493
PAS smart00091
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
483-545 3.60e-08

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


Pssm-ID: 214512  Cd Length: 67  Bit Score: 50.86  E-value: 3.60e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2129446385  483 AERDRIWRLSPELLAVADHGGRLVSVNPAVRAILGWSPEQFLAMGLDEGVHPEDLASMQATLE 545
Cdd:smart00091   1 ERLRAILESLPDGIFVLDLDGRILYANPAAEELLGYSPEELIGKSLLELIHPEDRERVQEALQ 63
PRK09776 PRK09776
putative diguanylate cyclase; Provisional
471-602 1.74e-04

putative diguanylate cyclase; Provisional


Pssm-ID: 182070 [Multi-domain]  Cd Length: 1092  Bit Score: 45.82  E-value: 1.74e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129446385  471 ARVLEQ-RVE-HAIAERDRIWRLSPEL----LAVADHGGRLVSVNPAVRAILGWSPEQFLAMGLDEGVHPEDLASMQATL 544
Cdd:PRK09776   265 TMVMYAfRAErKHISESETRFRNAMEYsaigMALVGTEGQWLQVNKALCQFLGYSQEELRGLTFQQLTWPEDLNKDLQQV 344
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2129446385  545 EaEPAEGMQPVRHLESRLLHKDGSYHW--ITWSLSRAEGNV---YLAGRDD-TDLKAQAEVLRQ 602
Cdd:PRK09776   345 E-KLLSGEINSYSMEKRYYRRDGEVVWalLAVSLVRDTDGTplyFIAQIEDiNELKRTEQVNER 407
PRK11359 PRK11359
cyclic-di-GMP phosphodiesterase; Provisional
106-184 4.53e-04

cyclic-di-GMP phosphodiesterase; Provisional


Pssm-ID: 183097 [Multi-domain]  Cd Length: 799  Bit Score: 44.38  E-value: 4.53e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129446385 106 VYVEDLTVHPNWP-PWreAATQH----GLRACWSTPIKATDGRTLGVFSNYYRQPRLPTREdIEAIA-LVTRTAALAIER 179
Cdd:PRK11359  289 SHVSLFALRNGMPiHW--ASSSHgaeyQNAQSWSATIRQRDGAPAGTLQIKTSSGAETSAF-IERVAdISQHLAALALEQ 365

                  ....*
gi 2129446385 180 HLTEQ 184
Cdd:PRK11359  366 EKSRQ 370
GAF smart00065
Domain present in phytochromes and cGMP-specific phosphodiesterases; Mutations within these ...
52-187 9.64e-04

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


Pssm-ID: 214500 [Multi-domain]  Cd Length: 149  Bit Score: 40.83  E-value: 9.64e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129446385   52 VELLTSIAFVDDSGMRLRHVATPSLPAAYVQATD-----GAAIGPGVASWGAAAFLGTPVYVEDLTVHPNWppWREAATQ 126
Cdd:smart00065  10 LEELRQLLGADRVLIYLVDENDRGELVLVAADGLtlptlGIRFPLDEGLAGRVAETGRPLNIPDVEADPLF--AEDLLGR 87
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2129446385  127 H-GLRACWSTPIKAtDGRTLGVFSNYYR-QPRLPTREDIEAIALVTRTAALAIERHLTEQALR 187
Cdd:smart00065  88 YqGVRSFLAVPLVA-DGELVGVLALHNKkSPRPFTEEDEELLQALANQLAIALANAQLYEELR 149
 
Name Accession Description Interval E-value
PRK13557 PRK13557
histidine kinase; Provisional
565-985 1.08e-99

histidine kinase; Provisional


Pssm-ID: 237425 [Multi-domain]  Cd Length: 540  Bit Score: 323.93  E-value: 1.08e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129446385 565 KDGSYHWITWSLS---RAEGN-VYLAGrddtdlkAQAEVLR--QTEDALRQSQKLEAVGRLTGGIAHDFNNMLQGISGAL 638
Cdd:PRK13557  113 KDGSSFWNALFVSpvyNDAGDlVYFFG-------SQLDVSRrrDAEDALRQAQKMEALGQLTGGIAHDFNNLLQVMSGYL 185
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129446385 639 YLIDRKLRRSK--PEEVGKYVRTAQESTDRAARLTQRLLTFSRQQAIDPQVFDPGDILRSMDELFRRYTGEQVRLTLKLP 716
Cdd:PRK13557  186 DVIQAALSHPDadRGRMARSVENIRAAAERAATLTQQLLAFARKQRLEGRVLNLNGLVSGMGELAERTLGDAVTIETDLA 265
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129446385 717 AQSWRVRCDMNQFENAVLNLVINACDAMPAGGDLEIEVAHRELDAAAVQTNPCAEAGEFVEVCVSDMGCGMAPDVLARVF 796
Cdd:PRK13557  266 PDLWNCRIDPTQAEVALLNVLINARDAMPEGGRVTIRTRNVEIEDEDLAMYHGLPPGRYVSIAVTDTGSGMPPEILARVM 345
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129446385 797 EPFFTTKPMGQGTGLGLSMIYGFAQQAGGMVTIASVQAEGTAVRLFLPrhVGEPVALPAPESSEPPAAPAHAAVVALVED 876
Cdd:PRK13557  346 DPFFTTKEEGKGTGLGLSMVYGFAKQSGGAVRIYSEVGEGTTVRLYFP--ASDQAENPEQEPKARAIDRGGTETILIVDD 423
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129446385 877 DEHVRDMVRAALEELNLTVLTAADGDAGHRLLQSDARIDLLLSDVGLPG-MNGHALAQAARALRPALRIILMTGYAD--- 952
Cdd:PRK13557  424 RPDVAELARMILEDFGYRTLVASNGREALEILDSHPEVDLLFTDLIMPGgMNGVMLAREARRRQPKIKVLLTTGYAEasi 503
                         410       420       430
                  ....*....|....*....|....*....|...
gi 2129446385 953 ERENGwARQERDVslIRKPFSPGELTARVCRLL 985
Cdd:PRK13557  504 ERTDA-GGSEFDI--LNKPYRRAELARRVRMVL 533
NtrB COG3852
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms];
486-850 2.01e-82

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


Pssm-ID: 443061 [Multi-domain]  Cd Length: 361  Bit Score: 271.33  E-value: 2.01e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129446385 486 DRIWRLSPELLAVADHGGRLVSVNPAVRAILGWSPEQFLAMGLDEgVHPEDlASMQATLEAEPAEGmQPVRHLESRLLHK 565
Cdd:COG3852    10 RAILDSLPDAVIVLDADGRITYVNPAAERLLGLSAEELLGRPLAE-LFPED-SPLRELLERALAEG-QPVTEREVTLRRK 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129446385 566 DGSYHWITWSLSR---AEGNVYLAG--RDDTDLKaqaevlrQTEDALRQSQKLEAVGRLTGGIAHDFNNMLQGISGALYL 640
Cdd:COG3852    87 DGEERPVDVSVSPlrdAEGEGGVLLvlRDITERK-------RLERELRRAEKLAAVGELAAGLAHEIRNPLTGIRGAAQL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129446385 641 IDRKLrrsKPEEVGKYVRTAQESTDRAARLTQRLLTFSRQQAIDPQVFDPGDILRSMDELFRRYTGEQVRLTLKLPAQSW 720
Cdd:COG3852   160 LEREL---PDDELREYTQLIIEEADRLNNLVDRLLSFSRPRPPEREPVNLHEVLERVLELLRAEAPKNIRIVRDYDPSLP 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129446385 721 RVRCDMNQFENAVLNLVINACDAMPAGGDLEIEVAHRELDaaavqTNPCAEAGEFVEVCVSDMGCGMAPDVLARVFEPFF 800
Cdd:COG3852   237 EVLGDPDQLIQVLLNLVRNAAEAMPEGGTITIRTRVERQV-----TLGGLRPRLYVRIEVIDNGPGIPEEILDRIFEPFF 311
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|
gi 2129446385 801 TTKPmgQGTGLGLSMIYGFAQQAGGMVTIASVQAEGTAVRLFLPRHVGEP 850
Cdd:COG3852   312 TTKE--KGTGLGLAIVQKIVEQHGGTIEVESEPGKGTTFRIYLPLEQAEE 359
COG4191 COG4191
Signal transduction histidine kinase regulating C4-dicarboxylate transport system [Signal ...
471-846 2.80e-81

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


Pssm-ID: 443345 [Multi-domain]  Cd Length: 361  Bit Score: 268.20  E-value: 2.80e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129446385 471 ARVLEQRVEHAIAERDRIWRLSPELLAVADHGGRLVSVNPAVRAILGWSPEQFLAMGLDEGVHPEDLASMQATLEAEPAE 550
Cdd:COG4191     1 ALRLLLLLLLLLALLRALALALALLLLLLLLLLALLLLLLALLLALLALLLLLLLLLLLLLLELLLLLLALLGGLLRLLL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129446385 551 GMQPVRHLESRLLHKDGSYHWITWSLSRAEGnvylAGRDDTDLKAQAEVLRQTEDALRQSQKLEAVGRLTGGIAHDFNNM 630
Cdd:COG4191    81 LLGLLLLLLLEALLLLLLAALDAEENAELEE----LERDITELERAEEELRELQEQLVQSEKLAALGELAAGIAHEINNP 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129446385 631 LQGISGALYLIDRKLRRS-KPEEVGKYVRTAQESTDRAARLTQRLLTFSRQQAIDPQVFDPGDILRSMDELFRRYTGEQ- 708
Cdd:COG4191   157 LAAILGNAELLRRRLEDEpDPEELREALERILEGAERAAEIVRSLRAFSRRDEEEREPVDLNELIDEALELLRPRLKARg 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129446385 709 VRLTLKLPAQSWRVRCDMNQFENAVLNLVINACDAMPAGGDLEIEVAhreldaaavqtnpCAEAGEFVEVCVSDMGCGMA 788
Cdd:COG4191   237 IEVELDLPPDLPPVLGDPGQLEQVLLNLLINAIDAMEEGEGGRITIS-------------TRREGDYVVISVRDNGPGIP 303
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2129446385 789 PDVLARVFEPFFTTKPMGQGTGLGLSMIYGFAQQAGGMVTIASVQAEGTAVRLFLPRH 846
Cdd:COG4191   304 PEVLERIFEPFFTTKPVGKGTGLGLSISYGIVEKHGGRIEVESEPGGGTTFTITLPLA 361
NtrY COG5000
Signal transduction histidine kinase NtrY involved in nitrogen fixation and metabolism ...
422-850 2.48e-65

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: 226.38  E-value: 2.48e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129446385 422 IVVPLRRwgRADGTLLVRP---DPTHPLKGTD-IAFIEEAAERMCEAIERSQyaRVLEQRVEHAiaerDRIWRLSPELLA 497
Cdd:COG5000    33 LTRPLRR--LAEATRAVAAgdlSVRLPVTGDDeIGELARAFNRMTDQLKEQR--EELEERRRYL----ETILENLPAGVI 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129446385 498 VADHGGRLVSVNPAVRAILGWSPEQFLAMGLDEGVHPEDLASMQATLEAEPAEGMQPVRHLESRLLHkdgsyhwITWSLS 577
Cdd:COG5000   105 VLDADGRITLANPAAERLLGIPLEELIGKPLEELLPELDLAELLREALERGWQEEIELTRDGRRTLL-------VRASPL 177
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129446385 578 RAEGNVYLAgRDDTDLkaqaevlrqtedalRQSQKLEAVGRLTGGIAHDFNNMLQGISGALYLIDRKLRRSKP---EEVG 654
Cdd:COG5000   178 RDDGYVIVF-DDITEL--------------LRAERLAAWGELARRIAHEIKNPLTPIQLSAERLRRKLADKLEedrEDLE 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129446385 655 KYVRTAQESTDRAARLTQRLLTFSRQQAIDPQVFDPGDILRSMDELFR-RYTGEQVRLTLKLPAQSWRVRCDMNQFENAV 733
Cdd:COG5000   243 RALDTIIRQVDRLKRIVDEFLDFARLPEPQLEPVDLNELLREVLALYEpALKEKDIRLELDLDPDLPEVLADRDQLEQVL 322
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129446385 734 LNLVINACDAMPAGGDLEIEVAHReldaaavqtnpcaeaGEFVEVCVSDMGCGMAPDVLARVFEPFFTTKPmgQGTGLGL 813
Cdd:COG5000   323 INLLKNAIEAIEEGGEIEVSTRRE---------------DGRVRIEVSDNGPGIPEEVLERIFEPFFTTKP--KGTGLGL 385
                         410       420       430
                  ....*....|....*....|....*....|....*..
gi 2129446385 814 SMIYGFAQQAGGMVTIASVQAEGTAVRLFLPRHVGEP 850
Cdd:COG5000   386 AIVKKIVEEHGGTIELESRPGGGTTFTIRLPLAEEAE 422
BaeS COG0642
Signal transduction histidine kinase [Signal transduction mechanisms];
505-846 2.07e-49

Signal transduction histidine kinase [Signal transduction mechanisms];


Pssm-ID: 440407 [Multi-domain]  Cd Length: 328  Bit Score: 178.18  E-value: 2.07e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129446385 505 LVSVNPAVRAILGWSPEQFLAMGLDEGVHPEDLASMQATLEAEPAEGMQPVRHLESRLLHKDGSYHWITWSLSRAEGNVY 584
Cdd:COG0642     8 LVLLLLLLLLLLLALLLLLLLLLLLALLLLLALLLLLLLLLLLLLLLALALLALLLLLLLLLLLLLLLLLLLLLLLLLLL 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129446385 585 LAGRDDTDLKAQAEVLRQTEDALRqsqkleavgRLTGGIAHDFNNMLQGISGALYLidrkLRRSKPEEVGKYVRTAQEST 664
Cdd:COG0642    88 LLLLLLLLLLALLLLLEEANEAKS---------RFLANVSHELRTPLTAIRGYLEL----LLEELDEEQREYLETILRSA 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129446385 665 DRAARLTQRLLTFSRQQA----IDPQVFDPGDILRSMDELFR-RYTGEQVRLTLKLPAQSWRVRCDMNQFENAVLNLVIN 739
Cdd:COG0642   155 DRLLRLINDLLDLSRLEAgkleLEPEPVDLAELLEEVVELFRpLAEEKGIELELDLPDDLPTVRGDPDRLRQVLLNLLSN 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129446385 740 ACDAMPAGGDLEIEVAhreldaaavqtnpcaEAGEFVEVCVSDMGCGMAPDVLARVFEPFFTTKP--MGQGTGLGLSMIY 817
Cdd:COG0642   235 AIKYTPEGGTVTVSVR---------------REGDRVRISVEDTGPGIPPEDLERIFEPFFRTDPsrRGGGTGLGLAIVK 299
                         330       340
                  ....*....|....*....|....*....
gi 2129446385 818 GFAQQAGGMVTIASVQAEGTAVRLFLPRH 846
Cdd:COG0642   300 RIVELHGGTIEVESEPGKGTTFTVTLPLA 328
KinE COG5809
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome ...
492-851 1.23e-48

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


Pssm-ID: 444511 [Multi-domain]  Cd Length: 489  Bit Score: 180.56  E-value: 1.23e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129446385 492 SPELLAVADHGGRLVSVNPAVRAILGWSPEQFLAMGLDEGVHPEDLASMQATLeAEPAEGmQPVRHLESRLLHKDGSYHW 571
Cdd:COG5809   150 SPDGIIVTDLDGRIIYANPAACKLLGISIEELIGKSILELIHSDDQENVAAFI-SQLLKD-GGIAQGEVRFWTKDGRWRL 227
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129446385 572 ITWSLSRAEGNVYLAG-----RDDTDLKaqaevlrQTEDALRQSQKLEAVGRLTGGIAHDFNNMLQGISGALYLidrkLR 646
Cdd:COG5809   228 LEASGAPIKKNGEVDGiviifRDITERK-------KLEELLRKSEKLSVVGELAAGIAHEIRNPLTSLKGFIQL----LK 296
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129446385 647 RSKPEEVGKYVRTAQESTDRAARLTQRLLTFSRQQAIDPQVFDPGDILRSMDELFRR---YTGEQVRLTL--KLPAqswr 721
Cdd:COG5809   297 DTIDEEQKTYLDIMLSELDRIESIISEFLVLAKPQAIKYEPKDLNTLIEEVIPLLQPqalLKNVQIELELedDIPD---- 372
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129446385 722 VRCDMNQFENAVLNLVINACDAMPAGGDLEIEVAhreldaaavqtnpcAEAGEFVEVCVSDMGCGMAPDVLARVFEPFFT 801
Cdd:COG5809   373 ILGDENQLKQVFINLLKNAIEAMPEGGNITIETK--------------AEDDDKVVISVTDEGCGIPEERLKKLGEPFYT 438
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|
gi 2129446385 802 TKPmgQGTGLGLSMIYGFAQQAGGMVTIASVQAEGTAVRLFLPRHVGEPV 851
Cdd:COG5809   439 TKE--KGTGLGLMVSYKIIEEHGGKITVESEVGKGTTFSITLPIKLSEQV 486
HATPase_CckA-like cd16919
Histidine kinase-like ATPase domain of two-component sensor hybrid histidine kinases, similar ...
729-844 2.33e-44

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: 156.00  E-value: 2.33e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129446385 729 FENAVLNLVINACDAMPAGGDLEIEVAHRELDAAAVQTNPCAEAGEFVEVCVSDMGCGMAPDVLARVFEPFFTTKPMGQG 808
Cdd:cd16919     1 LELAILNLAVNARDAMPEGGRLTIETSNQRVDADYALNYRDLIPGNYVCLEVSDTGSGMPAEVLRRAFEPFFTTKEVGKG 80
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2129446385 809 TGLGLSMIYGFAQQAGGMVTIASVQAEGTAVRLFLP 844
Cdd:cd16919    81 TGLGLSMVYGFVKQSGGHLRIYSEPGVGTTVRIYLP 116
KdpD COG2205
K+-sensing histidine kinase KdpD [Signal transduction mechanisms];
600-846 2.65e-43

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


Pssm-ID: 441807 [Multi-domain]  Cd Length: 239  Bit Score: 157.38  E-value: 2.65e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129446385 600 LRQTEDALRQSQKLEAvgRLTGGIAHDFNNMLQGISGALYLIDRKLRRSkPEEVGKYVRTAQESTDRAARLTQRLLTFSR 679
Cdd:COG2205     2 LEEALEELEELERLKS--EFLANVSHELRTPLTSILGAAELLLDEEDLS-PEERRELLEIIRESAERLLRLIEDLLDLSR 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129446385 680 QQA----IDPQVFDPGDILRSMDELFR-RYTGEQVRLTLKLPAQSWRVRCDMNQFENAVLNLVINACDAMPAGGDLEIEV 754
Cdd:COG2205    79 LESgklsLELEPVDLAELLEEAVEELRpLAEEKGIRLELDLPPELPLVYADPELLEQVLANLLDNAIKYSPPGGTITISA 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129446385 755 AhreldaaavqtnpcaEAGEFVEVCVSDMGCGMAPDVLARVFEPFFTTKPMG--QGTGLGLSMIYGFAQQAGGMVTIASV 832
Cdd:COG2205   159 R---------------REGDGVRISVSDNGPGIPEEELERIFERFYRGDNSRgeGGTGLGLAIVKRIVEAHGGTIWVESE 223
                         250
                  ....*....|....
gi 2129446385 833 QAEGTAVRLFLPRH 846
Cdd:COG2205   224 PGGGTTFTVTLPLA 237
KinA COG5805
Sporulation sensor histidine kinase A (Stage II sporulation protein SpoIIF/SpoIIJ) [Cell cycle ...
492-844 5.37e-43

Sporulation sensor histidine kinase A (Stage II sporulation protein SpoIIF/SpoIIJ) [Cell cycle control, cell division, chromosome partitioning, Signal transduction mechanisms];


Pssm-ID: 444507 [Multi-domain]  Cd Length: 496  Bit Score: 164.13  E-value: 5.37e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129446385 492 SPELLAVADHGGRLVSVNPAVRAILGWSPEQFLAMGLDEGVHPEDLASMQATLEaEPAEGMQPvRHLESRLLHKDGSYHW 571
Cdd:COG5805   166 SPDLICVIDTDGRILFINESIERLFGAPREELIGKNLLELLHPCDKEEFKERIE-SITEVWQE-FIIEREIITKDGRIRY 243
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129446385 572 ITWS----LSRAEGNVYL--AGRDDTDLKaqaevlrQTEDALRQSQKLEAVGRLTGGIAHDFNNMLQGISGALYLIdrkl 645
Cdd:COG5805   244 FEAVivplIDTDGSVKGIlvILRDITEKK-------EAEELMARSEKLSIAGQLAAGIAHEIRNPLTSIKGFLQLL---- 312
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129446385 646 rRSKPEEVGKYVRTAQESTDRAARLTQRLLTFSRQQAIDPQVFDPGDILRSMDELFR---RYTGEQVRLTLKLPAQSwrV 722
Cdd:COG5805   313 -QPGIEDKEEYFDIMLSELDRIESIISEFLALAKPQAVNKEKENINELIQDVVTLLEteaILHNIQIRLELLDEDPF--I 389
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129446385 723 RCDMNQFENAVLNLVINACDAMPAGGDLEIEVAhreldaaavqtnpcaEAGEFVEVCVSDMGCGMAPDVLARVFEPFFTT 802
Cdd:COG5805   390 YCDENQIKQVFINLIKNAIEAMPNGGTITIHTE---------------EEDNSVIIRVIDEGIGIPEERLKKLGEPFFTT 454
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|..
gi 2129446385 803 KPmgQGTGLGLSMIYGFAQQAGGMVTIASVQAEGTAVRLFLP 844
Cdd:COG5805   455 KE--KGTGLGLMVSYKIIENHNGTIDIDSKVGKGTTFTITLP 494
PRK13837 PRK13837
two-component system VirA-like sensor kinase;
593-990 1.09e-42

two-component system VirA-like sensor kinase;


Pssm-ID: 237526 [Multi-domain]  Cd Length: 828  Bit Score: 168.32  E-value: 1.09e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129446385 593 LKAQAEVLrqtEDALRQSQKLEAVGRLTGGIAHDFNNMLQGISGALYLIDRKLRRSKPeeVGKYVRTAQESTDRAARLTQ 672
Cdd:PRK13837  430 LETERDAL---ERRLEHARRLEAVGTLASGIAHNFNNILGAILGYAEMALNKLARHSR--AARYIDEIISAGARARLIID 504
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129446385 673 RLLTFSRQQAIDPQVFDPGDILRSMDELFRRYTGEQVRLTLKLPAQSWRVRCDMNQFENAVLNLVINACDAMPAGGDLEI 752
Cdd:PRK13837  505 QILAFGRKGERNTKPFDLSELVTEIAPLLRVSLPPGVELDFDQDQEPAVVEGNPAELQQVLMNLCSNAAQAMDGAGRVDI 584
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129446385 753 EVAHRELDAAAVQTNPCAEAGEFVEVCVSDMGCGMAPDVLARVFEPFFTTKPmgQGTGLGLSMIYGFAQQAGGMVTIASV 832
Cdd:PRK13837  585 SLSRAKLRAPKVLSHGVLPPGRYVLLRVSDTGAGIDEAVLPHIFEPFFTTRA--GGTGLGLATVHGIVSAHAGYIDVQST 662
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129446385 833 QAEGTAVRLFLPRHVGEPVAlPAPESSEPPAAPAHAAVVALVEDDEHVRDMVR---AAL--EELNLTVLTAADGdaghRL 907
Cdd:PRK13837  663 VGRGTRFDVYLPPSSKVPVA-PQAFFGPGPLPRGRGETVLLVEPDDATLERYEeklAALgyEPVGFSTLAAAIA----WI 737
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129446385 908 LQSDARIDLLLsdVGLPGMNGHALAQAARALRPALRIILMTGYADERENGwARQERDVSLIRKPFSPGELTARVCRLLAA 987
Cdd:PRK13837  738 SKGPERFDLVL--VDDRLLDEEQAAAALHAAAPTLPIILGGNSKTMALSP-DLLASVAEILAKPISSRTLAYALRTALAT 814

                  ...
gi 2129446385 988 SQD 990
Cdd:PRK13837  815 ARA 817
KinC COG5807
Sporulation sensor histidine kinase C [Cell cycle control, cell division, chromosome ...
493-845 4.19e-42

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


Pssm-ID: 444509 [Multi-domain]  Cd Length: 358  Bit Score: 158.03  E-value: 4.19e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129446385 493 PELLAVADHGGRLVSVNPAVRAILGWSPEQFLAMGLDEGVHpedlasmqaTLEAEPAEGMQPVRHLESRLLHKDGSYHWI 572
Cdd:COG5807    37 LEFVFFIDSKGEILECNDFAEDLYGLSQNEYIGKTFVEEKC---------ILKDEQLYNKEAFDRIEISYLTKNGEFDEI 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129446385 573 TWSLSRAEGNVYLAGRDDTDLKAQAEvlrqTEDALRQSQKLEAVGRLTGGIAHDFNNMLQGISGALYLIDRKLRRSKPEE 652
Cdd:COG5807   108 IYPIYYKDGVILGLITVYRDITKRKE----AEDKLLRSEKLSVAGELAAGIAHEIRNPLTSIKGFLQLLQESREDSEREE 183
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129446385 653 vgkYVRTAQESTDRAARLTQRLLTFSRQQAIDPQVFDPGDILRSMDELFRrYTGEQ--VRLTLKLPAQSWRVRCDMNQFE 730
Cdd:COG5807   184 ---YFNIIISEIDRINTIITELLVLSKPKKFNFKKLNLNDVLEDVIALLS-TEAILknISIKYDLADDEPVINGDKNQLK 259
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129446385 731 NAVLNLVINACDAMPAGGDLEIEVAhREldaaavqtnpcaeaGEFVEVCVSDMGCGMAPDVLARVFEPFFTTKpmGQGTG 810
Cdd:COG5807   260 QVFINLIKNAIEAMETGGNITIKTY-VE--------------GDFVVISVKDEGIGIPEEVLEKIGEPFFTTK--EEGTG 322
                         330       340       350
                  ....*....|....*....|....*....|....*
gi 2129446385 811 LGLSMIYGFAQQAGGMVTIASVQAEGTAVRLFLPR 845
Cdd:COG5807   323 LGLSICKKIIEEHNGTIEVESKPGKGTTFTIYLPL 357
PRK11360 PRK11360
two-component system sensor histidine kinase AtoS;
495-849 1.00e-37

two-component system sensor histidine kinase AtoS;


Pssm-ID: 236901 [Multi-domain]  Cd Length: 607  Bit Score: 150.50  E-value: 1.00e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129446385 495 LLAVaDHGGRLVSVNPAVRAILGWSPEQFLAMGLDEgVHPED--LAS-MQATLEaepaEGMQpVRHLESRLLHKDGSYHw 571
Cdd:PRK11360  275 VIAI-DRQGKITTMNPAAEVITGLQRHELVGKPYSE-LFPPNtpFASpLLDTLE----HGTE-HVDLEISFPGRDRTIE- 346
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129446385 572 ITWSLSR---AEGNV---YLAGRDDTDLKAQAEVLRQTEdalrqsqKLEAVGRLTGGIAHDFNNMLQGISGALYLIDRKL 645
Cdd:PRK11360  347 LSVSTSLlhnTHGEMigaLVIFSDLTERKRLQRRVARQE-------RLAALGELVAGVAHEIRNPLTAIRGYVQIWRQQT 419
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129446385 646 RRSKPEevgKYVRTAQESTDRAARLTQRLLTFSRQQAIDPQVFDPGDILRSMDELFRRYTG-EQVRLTLKLPAQSWRVRC 724
Cdd:PRK11360  420 SDPPSQ---EYLSVVLREVDRLNKVIDQLLEFSRPRESQWQPVSLNALVEEVLQLFQTAGVqARVDFETELDNELPPIWA 496
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129446385 725 DMNQFENAVLNLVINACDAMPAGGDLEIEVaHRELDAAavqtnpcaeagefVEVCVSDMGCGMAPDVLARVFEPFFTTKP 804
Cdd:PRK11360  497 DPELLKQVLLNILINAVQAISARGKIRIRT-WQYSDGQ-------------VAVSIEDNGCGIDPELLKKIFDPFFTTKA 562
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*
gi 2129446385 805 mgQGTGLGLSMIYGFAQQAGGMVTIASVQAEGTAVRLFLPRHVGE 849
Cdd:PRK11360  563 --KGTGLGLALSQRIINAHGGDIEVESEPGVGTTFTLYLPINPQG 605
WalK COG5002
Sensor histidine kinase WalK [Signal transduction mechanisms];
464-845 1.31e-35

Sensor histidine kinase WalK [Signal transduction mechanisms];


Pssm-ID: 444026 [Multi-domain]  Cd Length: 390  Bit Score: 140.07  E-value: 1.31e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129446385 464 AIERSQYARVLEQRVEHAIAERDRIWRLSPELLAVADHGGRLVSVNPAVRAILGWSPEQFLAMGLDEGVHPEDLASMQAT 543
Cdd:COG5002    29 LLLLLLLLLLLLLLLLLLLLLLLLALLLLLLLLLLLLLALLLLLLLLLLLLALALLLLALLLLLLLLLLLLALLILLLLL 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129446385 544 LEAEPAEGMQPVRHLESRLLHKDGSYHWITWSLSRAEGNVYLAGRDDTDLKaQAEVLRQtedalrqsqkleavgRLTGGI 623
Cdd:COG5002   109 ALLILLAALLLLLSELLLLLLLLGRLSLRLSALLLGLLLLAAVERDITELE-RLEQMRR---------------EFVANV 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129446385 624 AHDFNNMLQGISGALYLIDRKLRRSkPEEVGKYVRTAQESTDRAARLTQRLLTFSRQQA----IDPQVFDPGDILRSMDE 699
Cdd:COG5002   173 SHELRTPLTSIRGYLELLLDGAADD-PEERREYLEIILEEAERLSRLVNDLLDLSRLESgelkLEKEPVDLAELLEEVVE 251
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129446385 700 LFR-RYTGEQVRLTLKLPAQSWRVRCDMNQFENAVLNLVINACDAMPAGGDLEIEVahreldaaavqtnpcAEAGEFVEV 778
Cdd:COG5002   252 ELRpLAEEKGIELELDLPEDPLLVLGDPDRLEQVLTNLLDNAIKYTPEGGTITVSL---------------REEDDQVRI 316
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2129446385 779 CVSDMGCGMAPDVLARVFEPFFTTKP----MGQGTGLGLSMIYGFAQQAGGMVTIASVQAEGTAVRLFLPR 845
Cdd:COG5002   317 SVRDTGIGIPEEDLPRIFERFYRVDKsrsrETGGTGLGLAIVKHIVEAHGGRIWVESEPGKGTTFTITLPL 387
HATPase_AtoS-like cd16943
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
728-845 2.35e-27

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: 107.12  E-value: 2.35e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129446385 728 QFENAVLNLVINACDAMPAGGDLEIEVAHREldaaavqtnpcaeagEFVEVCVSDMGCGMAPDVLARVFEPFFTTKPMGQ 807
Cdd:cd16943     3 QLNQVLLNLLVNAAQAMEGRGRITIRTWAHV---------------DQVLIEVEDTGSGIDPEILGRIFDPFFTTKPVGE 67
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2129446385 808 GTGLGLSMIYGFAQQAGGMVTIASVQAEGTAVRLFLPR 845
Cdd:cd16943    68 GTGLGLSLSYRIIQKHGGTIRVASVPGGGTRFTIILPI 105
PRK10364 PRK10364
two-component system sensor histidine kinase ZraS;
601-844 2.52e-27

two-component system sensor histidine kinase ZraS;


Pssm-ID: 236674 [Multi-domain]  Cd Length: 457  Bit Score: 116.81  E-value: 2.52e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129446385 601 RQTEDALRQSQKLEAVGRLTGGIAHDFNNMLQGISG-ALYLIDRKLRRSKPEEVGKYVrtAQEStDRAARLTQRLLTFSR 679
Cdd:PRK10364  222 QLLQDEMKRKEKLVALGHLAAGVAHEIRNPLSSIKGlAKYFAERAPAGGEAHQLAQVM--AKEA-DRLNRVVSELLELVK 298
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129446385 680 QQAIDPQVFDPGDILRSMDELFR---RYTGEQVRLTLK--LPAqswrVRCDMNQFENAVLNLVINACDAMPAGGDLEIEV 754
Cdd:PRK10364  299 PTHLALQAVDLNDLINHSLQLVSqdaNSREIQLRFTANdtLPE----IQADPDRLTQVLLNLYLNAIQAIGQHGVISVTA 374
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129446385 755 AhreldaaavqtnpcaEAGEFVEVCVSDMGCGMAPDVLARVFEPFFTTKpmGQGTGLGLSMIYGFAQQAGGMVTIASVQA 834
Cdd:PRK10364  375 S---------------ESGAGVKISVTDSGKGIAADQLEAIFTPYFTTK--AEGTGLGLAVVHNIVEQHGGTIQVASQEG 437
                         250
                  ....*....|
gi 2129446385 835 EGTAVRLFLP 844
Cdd:PRK10364  438 KGATFTLWLP 447
COG4251 COG4251
Bacteriophytochrome (light-regulated signal transduction histidine kinase) [Signal ...
421-846 1.37e-24

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


Pssm-ID: 443393 [Multi-domain]  Cd Length: 503  Bit Score: 109.10  E-value: 1.37e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129446385 421 AIVVPLRRWGRADGTLLVRPDPTHPLKGTDIAFIEEAAERMCEAIERSQYARVLEQRVEHAIAERDRIWRLSPELLAVAD 500
Cdd:COG4251    83 LLLLLELALVLLALLLVLLLLLALLLLLALLLLLELLLLLLALLLLLLLLALLLLEELALLRLALALLLLLLLLLLLLLL 162
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129446385 501 HGGRLVSVNPAVRAILGWSPEQFLAMGLDEGVHPEDLASMQATLEAEPAEGMQPVRHLESRLLHKDGSYHWITWSLSRAE 580
Cdd:COG4251   163 LLALILALLLAALAELELLLLLLLVLLLLLLLLLLLLLLLLRLLLELLLLLEAELLLSLGGGLGLLLLLLLLLVLLLLLI 242
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129446385 581 GNVYLAGRDDTDLKAQAEVLRQTEDALRQSQKLEAV----GRLTGGIAHDFNNMLQGISGALYLIDRKLRRSKPEEVGKY 656
Cdd:COG4251   243 LLLLLLILVLELLELRLELEELEEELEERTAELERSneelEQFAYVASHDLREPLRKISGFSQLLEEDYGDKLDEEGREY 322
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129446385 657 VRTAQESTDRAARLTQRLLTFSR--QQAIDPQVFDPGDILRS-MDELFRRYTGEQVRLTL-KLPaqswRVRCDMNQFENA 732
Cdd:COG4251   323 LERIRDAAERMQALIDDLLAYSRvgRQELEFEPVDLNELLEEvLEDLEPRIEERGAEIEVgPLP----TVRGDPTLLRQV 398
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129446385 733 VLNLVINACDAMPAGGDLEIEVAhreldaaavqtnpCAEAGEFVEVCVSDMGCGMAPDVLARVFEPFFTTKPMGQ--GTG 810
Cdd:COG4251   399 FQNLISNAIKYSRPGEPPRIEIG-------------AEREGGEWVFSVRDNGIGIDPEYAEKIFEIFQRLHSRDEyeGTG 465
                         410       420       430
                  ....*....|....*....|....*....|....*.
gi 2129446385 811 LGLSMIYGFAQQAGGMVTIASVQAEGTAVRLFLPRH 846
Cdd:COG4251   466 IGLAIVKKIVERHGGRIWVESEPGEGATFYFTLPKA 501
HATPase_c smart00387
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.
725-844 1.69e-23

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


Pssm-ID: 214643 [Multi-domain]  Cd Length: 111  Bit Score: 96.18  E-value: 1.69e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129446385  725 DMNQFENAVLNLVINACDAMPAGGDLEIEVAHReldaaavqtnpcaeaGEFVEVCVSDMGCGMAPDVLARVFEPFFTTKP 804
Cdd:smart00387   2 DPDRLRQVLSNLLDNAIKYTPEGGRITVTLERD---------------GDHVEITVEDNGPGIPPEDLEKIFEPFFRTDK 66
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 2129446385  805 ---MGQGTGLGLSMIYGFAQQAGGMVTIASVQAEGTAVRLFLP 844
Cdd:smart00387  67 rsrKIGGTGLGLSIVKKLVELHGGEISVESEPGGGTTFTITLP 109
HATPase_c pfam02518
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the ...
732-844 4.07e-21

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


Pssm-ID: 460579 [Multi-domain]  Cd Length: 109  Bit Score: 89.35  E-value: 4.07e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129446385 732 AVLNLVINACDAMPAGGDLEIEVahreldaaavqtnpcaEAGEFVEVCVSDMGCGMAPDVLARVFEPFFTT-KPMGQGTG 810
Cdd:pfam02518   9 VLSNLLDNALKHAAKAGEITVTL----------------SEGGELTLTVEDNGIGIPPEDLPRIFEPFSTAdKRGGGGTG 72
                          90       100       110
                  ....*....|....*....|....*....|....
gi 2129446385 811 LGLSMIYGFAQQAGGMVTIASVQAEGTAVRLFLP 844
Cdd:pfam02518  73 LGLSIVRKLVELLGGTITVESEPGGGTTVTLTLP 106
HATPase_HupT_MifS-like cd16976
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
730-843 2.43e-20

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: 86.74  E-value: 2.43e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129446385 730 ENAVLNLVINACDAMPAGGDLEIEVAHRELDAAAVqtnpcaeagefveVCVSDMGCGMAPDVLARVFEPFFTTKPMGQGT 809
Cdd:cd16976     2 QQVLMNLLQNALDAMGKVENPRIRIAARRLGGRLV-------------LVVRDNGPGIAEEHLSRVFDPFFTTKPVGKGT 68
                          90       100       110
                  ....*....|....*....|....*....|....
gi 2129446385 810 GLGLSMIYGFAQQAGGMVTIASVQAEGTAVRLFL 843
Cdd:cd16976    69 GLGLSISYGIVEEHGGRLSVANEEGAGARFTFDL 102
CitA COG3290
Sensor histidine kinase DipB regulating citrate/malate metabolism [Signal transduction ...
451-845 8.36e-20

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


Pssm-ID: 442519 [Multi-domain]  Cd Length: 389  Bit Score: 92.60  E-value: 8.36e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129446385 451 IAFIEEAAERMCEAIERSQYARVLEQRVEHAIA----ERDRIWRLSPELLAVADHGGRLVSVNPAVRAILGWSPeqfLAM 526
Cdd:COG3290    48 ILLLLLLILLLILLLLLLLLLAALLLKLLEEIArlveEREAVLESIREGVIAVDRDGRITLINDAARRLLGLDA---IGR 124
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129446385 527 GLDEgVHPEDLASMQATLEAEPAEGMQPVRhleSRLLHKDGsyhwitwslsRAEGNVYLAgRDDTDLKAQAEVLRQTE-- 604
Cdd:COG3290   125 PIDE-VLAEVLETGERDEEILLNGRVLVVN---RVPIRDDG----------RVVGAVATF-RDRTELERLEEELEGVKel 189
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129446385 605 -DALRqSQKleavgrltggiaHDFNNMLQGISGALYLIdrklrrsKPEEVGKYVrtaQESTDRAARLTQRLLTFSRQQAI 683
Cdd:COG3290   190 aEALR-AQR------------HDFRNHLHTISGLLQLG-------EYDEALEYI---DEISEELQELIDSLLSRIGNPVL 246
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129446385 684 DPqvfdpgdILRSMDELFRRytgEQVRLTLKLPAQSWRVRCDMNQFENAVLNLVINACDAMPAGGDLEIEVahrELDAAa 763
Cdd:COG3290   247 AA-------LLLGKAARARE---RGIDLTIDIDSDLPDLPLSDTDLVTILGNLLDNAIEAVEKLPEEERRV---ELSIR- 312
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129446385 764 vqtnpcaEAGEFVEVCVSDMGCGMAPDVLARVFEPFFTTKPmGQGTGLGLSMIYGFAQQAGGMVTIASVQAEGTAVRLFL 843
Cdd:COG3290   313 -------DDGDELVIEVEDSGPGIPEELLEKIFERGFSTKL-GEGRGLGLALVKQIVEKYGGTIEVESEEGEGTVFTVRL 384

                  ..
gi 2129446385 844 PR 845
Cdd:COG3290   385 PK 386
COG4192 COG4192
Signal transduction histidine kinase regulating phosphoglycerate transport system [Signal ...
600-831 9.69e-20

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


Pssm-ID: 443346 [Multi-domain]  Cd Length: 640  Bit Score: 94.75  E-value: 9.69e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129446385 600 LRQTEDALRQSQKLEAVGRLTGGIAHDFNNMLQGISGALYLIDRKLRRSKPEEVGKYVRTAQESTDRAARLTQRLLTFSR 679
Cdd:COG4192   417 LRQTQDELIQAAKMAVVGQTMTSLAHELNQPLNAMSMYLFSAKKALEQENYAQLPTSLDKIEGLIERMDKIIKSLRQFSR 496
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129446385 680 QQAIDPQVFDPGD-ILRSMDELFRRYTGEQVRLTLKLPAQswrVRCDMNQFENAVLNLVINACDAMPaggdleievAHRE 758
Cdd:COG4192   497 KSDTPLQPVDLRQvIEQAWELVESRAKPQQITLHIPDDLM---VQGDQVLLEQVLVNLLVNALDAVA---------TQPQ 564
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2129446385 759 LDAAAVQTNpcaeagEFVEVCVSDMGCGMApdVLARVFEPFFTTKPMgqGTGLGLSMIYGFAQQAGGMVTIAS 831
Cdd:COG4192   565 ISVDLLSNA------ENLRVAISDNGNGWP--LVDKLFTPFTTTKEV--GLGLGLSICRSIMQQFGGDLYLAS 627
CheY COG0784
CheY-like REC (receiver) domain, includes chemotaxis protein CheY and sporulation regulator ...
875-989 1.14e-19

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: 85.67  E-value: 1.14e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129446385 875 EDDEHVRDMVRAALEELNLTVLTAADGDAGHRLLQSDaRIDLLLSDVGLPGMNGHALAQA--ARALRPALRIILMTGYAD 952
Cdd:COG0784    12 DDNPDNRELLRRLLERLGYEVTTAEDGAEALELLRAG-PPDLILLDINMPGMDGLELLRRirALPRLPDIPIIALTAYAD 90
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2129446385 953 ERENGWARQERDVSLIRKPFSPGELTARVCRLLAASQ 989
Cdd:COG0784    91 EEDRERALEAGADDYLTKPVDPEELLEALRRLLARAS 127
REC_hyHK_blue-like cd18161
phosphoacceptor receiver (REC) domain of hybrid sensor histidine kinase/response regulators ...
875-972 5.21e-17

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: 77.39  E-value: 5.21e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129446385 875 EDDEHVRDMVRAALEELNLTVLTAADGDAGHRLLQSDARIDLLLSDVGLPG-MNGHALAQAARALRPALRIILMTGYAdE 953
Cdd:cd18161     5 EDDPDVRRLTAEVLEDLGYTVLEAASGDEALDLLESGPDIDLLVTDVIMPGgMNGSQLAEEARRRRPDLKVLLTSGYA-E 83
                          90
                  ....*....|....*....
gi 2129446385 954 RENGWARQERDVSLIRKPF 972
Cdd:cd18161    84 NAIEGGDLAPGVDVLSKPF 102
AtoC COG2204
DNA-binding transcriptional response regulator, NtrC family, contains REC, AAA-type ATPase, ...
875-989 6.08e-17

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: 84.24  E-value: 6.08e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129446385 875 EDDEHVRDMVRAALEELNLTVLTAADGDAGHRLLQSDaRIDLLLSDVGLPGMNGHALAQAARALRPALRIILMTGYADER 954
Cdd:COG2204     9 DDDPDIRRLLKELLERAGYEVETAASGEEALALLREE-PPDLVLLDLRMPGMDGLELLRELRALDPDLPVILLTGYGDVE 87
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2129446385 955 ENGWARQERDVSLIRKPFSPGELTARVCRLLAASQ 989
Cdd:COG2204    88 TAVEAIKAGAFDYLTKPFDLEELLAAVERALERRR 122
OmpR COG0745
DNA-binding response regulator, OmpR family, contains REC and winged-helix (wHTH) domain ...
875-989 1.73e-16

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: 79.23  E-value: 1.73e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129446385 875 EDDEHVRDMVRAALEELNLTVLTAADGDAGHRLLQSDaRIDLLLSDVGLPGMNGHALAQAARALRPALRIILMTGYADEr 954
Cdd:COG0745     8 EDDPDIRELLADALEREGYEVDTAADGEEALELLEEE-RPDLILLDLMLPGMDGLEVCRRLRARPSDIPIIMLTARDDE- 85
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 2129446385 955 engwarQERDVSL-------IRKPFSPGELTARVCRLLAASQ 989
Cdd:COG0745    86 ------EDRVRGLeagaddyLTKPFDPEELLARIRALLRRRA 121
HATPase_TmoS-FixL-DctS-like cd16920
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
730-844 3.45e-16

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Rhizobium meliloti FixL, and Rhodobacter capsulatus DctS; includes hybrid sensor histidine kinase similar to Pseudomonas mendocina TmoS; This family includes the histidine kinase-like ATPase (HATPase) domains of various histidine kinases (HKs) of two-component signal transduction systems (TCSs), such as Pseudomonas mendocina TmoS HK of the TmoS-TmoT TCS, which controls the expression of the toluene-4-monooxygenase pathway, Rhizobium meliloti FixL HK of the FixL-FixJ TCS, which regulates the expression of the genes related to nitrogen fixation in the root nodule in response to O(2) levels, and Rhodobacter capsulatus DctS of the DctS-DctR TCS, which controls synthesis of the high-affinity C4-dicarboxylate transport system. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA) and PAS sensor domain(s); many are hybrid sensor histidine kinases as they also contain a REC signal receiver domain.


Pssm-ID: 340397 [Multi-domain]  Cd Length: 104  Bit Score: 75.13  E-value: 3.45e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129446385 730 ENAVLNLVINACDAMPAGGDleievAHRELdaaAVQTNPCAEAgeFVEVCVSDMGCGMAPDVLARVFEPFFTTKPmgQGT 809
Cdd:cd16920     2 QQVLINLVRNGIEAMSEGGC-----ERREL---TIRTSPADDR--AVTISVKDTGPGIAEEVAGQLFDPFYTTKS--EGL 69
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2129446385 810 GLGLSMIYGFAQQAGGMVTIASVQAEGTAVRLFLP 844
Cdd:cd16920    70 GMGLSICRSIIEAHGGRLSVESPAGGGATFQFTLP 104
PAS COG2202
PAS domain [Signal transduction mechanisms];
475-681 1.17e-14

PAS domain [Signal transduction mechanisms];


Pssm-ID: 441804 [Multi-domain]  Cd Length: 258  Bit Score: 75.06  E-value: 1.17e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129446385 475 EQRVEHAIAERDRIWRLSPELLAVADHGGRLVSVNPAVRAILGWSPEQFLAMGLDEGVHPEDLASMQATLEAEPAEGmqP 554
Cdd:COG2202     3 EEALEESERRLRALVESSPDAIIITDLDGRILYVNPAFERLTGYSAEELLGKTLRDLLPPEDDDEFLELLRAALAGG--G 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129446385 555 VRHLESRLLHKDGSYHWITWSLS---RAEGNV--YLA-GRDDTDLKaqaevlrQTEDALRQSQKLEAVGRLTGGIAHDFN 628
Cdd:COG2202    81 VWRGELRNRRKDGSLFWVELSISpvrDEDGEItgFVGiARDITERK-------RAEEALRESEERLRLLVENAPDGIFVL 153
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2129446385 629 NMLQGISGALYLIDRKLRRSKPEEVGKYVR--TAQESTDRAARLTQRLLTFSRQQ 681
Cdd:COG2202   154 DLDGRILYVNPAAEELLGYSPEELLGKSLLdlLHPEDRERLLELLRRLLEGGRES 208
RpfG COG3437
Response regulator c-di-GMP phosphodiesterase, RpfG family, contains REC and HD-GYP domains ...
875-986 1.31e-14

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: 74.05  E-value: 1.31e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129446385 875 EDDEHVRDMVRAALEELNLTVLTAADGDAGHRLLQsDARIDLLLSDVGLPGMNGHA--LAQAARALRPALRIILMTGYAD 952
Cdd:COG3437    13 DDDPENLELLRQLLRTLGYDVVTAESGEEALELLL-EAPPDLILLDVRMPGMDGFEllRLLRADPSTRDIPVIFLTALAD 91
                          90       100       110
                  ....*....|....*....|....*....|....
gi 2129446385 953 ERENGWARQERDVSLIRKPFSPGELTARVCRLLA 986
Cdd:COG3437    92 PEDRERALEAGADDYLTKPFDPEELLARVRNALE 125
REC cd00156
phosphoacceptor receiver (REC) domain of response regulators (RRs) and pseudo response ...
875-971 1.32e-14

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: 70.33  E-value: 1.32e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129446385 875 EDDEHVRDMVRAALEELNLTVLTAADGDAGHRLLQSDaRIDLLLSDVGLPGMNGHALAQAARALRPALRIILMTGYADER 954
Cdd:cd00156     4 DDDPAIRELLKSLLEREGYEVDTAADGEEALELLREE-RPDLVLLDLMMPGMDGLELLRKLRELPPDIPVIVLTAKADEE 82
                          90
                  ....*....|....*..
gi 2129446385 955 ENGWARQERDVSLIRKP 971
Cdd:cd00156    83 DAVRALELGADDYLVKP 99
Response_reg pfam00072
Response regulator receiver domain; This domain receives the signal from the sensor partner in ...
875-981 1.92e-14

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: 70.26  E-value: 1.92e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129446385 875 EDDEHVRDMVRAALEELNLTVLTAADGDAGHRLLQSDaRIDLLLSDVGLPGMNGHALAQAARALRPALRIILMTGYADER 954
Cdd:pfam00072   5 DDDPLIRELLRQLLEKEGYVVAEADDGKEALELLKEE-RPDLILLDINMPGMDGLELLKRIRRRDPTTPVIILTAHGDED 83
                          90       100
                  ....*....|....*....|....*..
gi 2129446385 955 ENGWARQERDVSLIRKPFSPGELTARV 981
Cdd:pfam00072  84 DAVEALEAGADDFLSKPFDPDELLAAI 110
PRK11100 PRK11100
sensory histidine kinase CreC; Provisional
631-846 1.57e-13

sensory histidine kinase CreC; Provisional


Pssm-ID: 236846 [Multi-domain]  Cd Length: 475  Bit Score: 74.11  E-value: 1.57e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129446385 631 LQGISGALYLIDRKLrrsKPEEVGKYVRTAQESTDRAARLTQRLLTFSR---QQAID-PQVFDPGDILRS-MDELFRRYT 705
Cdd:PRK11100  271 LAAIRGAAELLQEDP---PPEDRARFTGNILTQSARLQQLIDRLLELARleqRQELEvLEPVALAALLEElVEAREAQAA 347
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129446385 706 GEQVRLTLKLPAQswRVRCDMNQFENAVLNLVINACDAMPAGGDLEIEVAHReldaaavqtnpcaeaGEFVEVCVSDMGC 785
Cdd:PRK11100  348 AKGITLRLRPDDA--RVLGDPFLLRQALGNLLDNAIDFSPEGGTITLSAEVD---------------GEQVALSVEDQGP 410
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2129446385 786 GmAPDV-LARVFEPFFTT-KPMGQ--GTGLGLSMIYGFAQQAGGMVTIASVQAEGTAVRLFLPRH 846
Cdd:PRK11100  411 G-IPDYaLPRIFERFYSLpRPANGrkSTGLGLAFVREVARLHGGEVTLRNRPEGGVLATLTLPRH 474
PleD COG3706
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate ...
875-981 5.77e-13

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: 68.01  E-value: 5.77e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129446385 875 EDDEHVRDMVRAALEELNLTVLTAADGDAGHRLLQSDaRIDLLLSDVGLPGMNGHALAQA--ARALRPALRIILMTGYAD 952
Cdd:COG3706     8 DDDPTNRKLLRRLLEAAGYEVVEAADGEEALELLQEH-RPDLILLDLEMPDMDGLELCRRlrADPRTADIPIIFLTALDD 86
                          90       100
                  ....*....|....*....|....*....
gi 2129446385 953 ERENGWARQERDVSLIRKPFSPGELTARV 981
Cdd:COG3706    87 EEDRARALEAGADDYLTKPFDPEELLARV 115
sensory_box TIGR00229
PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain ...
488-600 2.16e-12

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


Pssm-ID: 272971 [Multi-domain]  Cd Length: 124  Bit Score: 65.00  E-value: 2.16e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129446385 488 IWRLSPELLAVADHGGRLVSVNPAVRAILGWSPEQFLAMGLDEGVHPEDLASMQATLEAEPAEGMQPVRHLEsRLLHKDG 567
Cdd:TIGR00229   8 IFESSPDAIIVIDLEGNILYVNPAFEEIFGYSAEELIGRNVLELIPEEDREEVRERIERRLEGEPEPVSEER-RVRRKDG 86
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2129446385 568 SYHWITWSLS--RAEGNV--YLAG-RDDTDLKAQAEVL 600
Cdd:TIGR00229  87 SEIWVEVSVSpiRTNGGElgVVGIvRDITERKEAEEAL 124
HATPase_NtrY-like cd16944
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
725-844 4.90e-12

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


Pssm-ID: 340420 [Multi-domain]  Cd Length: 108  Bit Score: 63.33  E-value: 4.90e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129446385 725 DMNQFENAVLNLVINACDAMPAGGDLEIEVAHReldaaaVQTNpcaeAGEFVEVCVSDMGCGMAPDVLARVFEPFFTTKP 804
Cdd:cd16944     1 DTTQISQVLTNILKNAAEAIEGRPSDVGEVRIR------VEAD----QDGRIVLIVCDNGKGFPREMRHRATEPYVTTRP 70
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2129446385 805 mgQGTGLGLSMIYGFAQQAGGMVTIASVQAEGTAVRLFLP 844
Cdd:cd16944    71 --KGTGLGLAIVKKIMEEHGGRISLSNREAGGACIRIILP 108
PAS cd00130
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
492-578 6.72e-12

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


Pssm-ID: 238075 [Multi-domain]  Cd Length: 103  Bit Score: 63.04  E-value: 6.72e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129446385 492 SPELLAVADHGGRLVSVNPAVRAILGWSPEQFLAMGLDEGVHPEDLASMQATLEAEPAEGmqPVRHLESRLLHKDGSYHW 571
Cdd:cd00130     1 LPDGVIVLDLDGRILYANPAAEQLLGYSPEELIGKSLLDLIHPEDREELRERLENLLSGG--EPVTLEVRLRRKDGSVIW 78

                  ....*..
gi 2129446385 572 ITWSLSR 578
Cdd:cd00130    79 VLVSLTP 85
GAF COG2203
GAF domain [Signal transduction mechanisms];
16-547 6.83e-12

GAF domain [Signal transduction mechanisms];


Pssm-ID: 441805 [Multi-domain]  Cd Length: 712  Bit Score: 69.45  E-value: 6.83e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129446385  16 LARLEDERVMLQRIAAGVPLTDVLLHVMQAVEAQSSVELlTSIAFVDDSGMRLRHVATPSLPAAYVqatdgAAIGPGVAS 95
Cdd:COG2203   189 LERLALLNEISQALRSALDLEELLQRILELAGELLGADR-GAILLVDEDGGELELVAAPGLPEEEL-----GRLPLGEGL 262
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129446385  96 WGAAAFLGTPVYVEDLTVHPNW-PPWREAATQHGLRACWSTPIKAtDGRTLGVFSNYYRQPRLPTREDIEAIALVTRTAA 174
Cdd:COG2203   263 AGRALRTGEPVVVNDASTDPRFaPSLRELLLALGIRSLLCVPLLV-DGRLIGVLALYSKEPRAFTEEDLELLEALADQAA 341
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129446385 175 LAIERHLTEQALRnssVRWRGMFERMQEGFFLAEAQRDSTGSVDDFTLLEINPAFETQSGLAVGQTLGPMLRVMSPAAAD 254
Cdd:COG2203   342 IAIERARLYEALE---AALAALLQELALLRLLLDLELTLLRLRQLLLELLLALLLLLSLLGAELLLLLLDAADLSGLLAL 418
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129446385 255 SIMRIFVGVIESGEPAQFEVEAPGPPQACYECRAGKEGHDRVAALFLNVTARKLAESELWERQYRKNFLLTLGDRMREIH 334
Cdd:COG2203   419 EGLLLLDLLLLLLLLRRILLLRVLRRLLLGDEEGLVLLLALAELELLEILELLVLLAVILLALALLAALLLLLLLLLALL 498
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129446385 335 QQDQIEQMVCEELGRHLELGAVAVMESVPQRGDRIAASWGPRPPYDGRSMLESAPLTPDYYEAVRKGRTAYLSPYLAGPA 414
Cdd:COG2203   499 ALSALAVLASLLLALLLLLLLLLLLLLLGLLAALAADLLLLAAALLEDLLILLLVLLLERELLTLVGVLLLLGLSVLLIE 578
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129446385 415 GNQQPSAIVVPLRRWGRADGTLLVRPDPTHPLKGTDIAFIEEAAERMCEAIERSQYARVLEQRVEHAIAERDRIWRLSPE 494
Cdd:COG2203   579 LALALILALALLELLLVAVGDLLLLERDLLLLLVLLVRLLLELLVVTLELTVLVVLAAVEDSALLLRLALALASLVLLRA 658
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2129446385 495 LLAVADHGGRLVSVNPAVRAILGWSPEQFLAMGLDEGVHPEDLASMQATLEAE 547
Cdd:COG2203   659 LLATELDLILDSSLLLGLLLLGALLLLGGGLALLLSIGLGLGVARLLQLSVLE 711
GAF_2 pfam13185
GAF domain; The GAF domain is named after some of the proteins it is found in, including ...
35-178 1.20e-11

GAF domain; The GAF domain is named after some of the proteins it is found in, including cGMP-specific phosphodiesterases, adenylyl cyclases and FhlA. It is also found in guanylyl cyclases and phytochromes. The structure of a GAF domain shows that the domain shares a similar fold with the PAS domain. This domain can bind O2, CO and NO (Matilla et.al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).


Pssm-ID: 433019 [Multi-domain]  Cd Length: 137  Bit Score: 63.25  E-value: 1.20e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129446385  35 LTDVLLHVMQAVEAQSSVELlTSIAFVDDSGmrlrHVATPSLPAAYVQATDGAAIGPGVasWGAAAFLGTPVYVEDLTVH 114
Cdd:pfam13185   4 LEELLDAVLEAAVELGASAV-GFILLVDDDG----RLAAWGGAADELSAALDDPPGEGL--VGEALRTGRPVIVNDLAAD 76
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2129446385 115 PNWPPWReaATQHGLRACWSTPIKAtDGRTLGVFSNYYRQPRLPTREDIEAIALVTRTAALAIE 178
Cdd:pfam13185  77 PAKKGLP--AGHAGLRSFLSVPLVS-GGRVVGVLALGSNRPGAFDEEDLELLELLAEQAAIAIE 137
REC_OmpR cd17574
phosphoacceptor receiver (REC) domain of OmpR family response regulators; OmpR-like proteins ...
875-928 2.05e-11

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: 61.27  E-value: 2.05e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2129446385 875 EDDEHVRDMVRAALEELNLTVLTAADGDAGHRLLQSDaRIDLLLSDVGLPGMNG 928
Cdd:cd17574     4 EDDEEIAELLSDYLEKEGYEVDTAADGEEALELAREE-QPDLIILDVMLPGMDG 56
PAS COG2202
PAS domain [Signal transduction mechanisms];
477-600 5.94e-11

PAS domain [Signal transduction mechanisms];


Pssm-ID: 441804 [Multi-domain]  Cd Length: 258  Bit Score: 63.89  E-value: 5.94e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129446385 477 RVEHAIAERDRIWRL----SPELLAVADHGGRLVSVNPAVRAILGWSPEQFLAMGLDEGVHPEDLASMQATLEaEPAEGM 552
Cdd:COG2202   127 RAEEALRESEERLRLlvenAPDGIFVLDLDGRILYVNPAAEELLGYSPEELLGKSLLDLLHPEDRERLLELLR-RLLEGG 205
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2129446385 553 QPVRHLESRLLHKDGSYHWITWSLSRAEGNVYLAG-----RDDTDLKAQAEVL 600
Cdd:COG2202   206 RESYELELRLKDGDGRWVWVEASAVPLRDGGEVIGvlgivRDITERKRAEEAL 258
PRK15347 PRK15347
two component system sensor kinase;
623-844 1.12e-10

two component system sensor kinase;


Pssm-ID: 237951 [Multi-domain]  Cd Length: 921  Bit Score: 65.82  E-value: 1.12e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129446385 623 IAHDFNNMLQGISGALYLidrkLRRSK--PEEVGkYVRTAQESTDRAARLTQRLLTFSRQQAidpqvfdpGDILRSMDEL 700
Cdd:PRK15347  405 ISHEIRTPLNGVLGALEL----LQNTPltAEQMD-LADTARQCTLSLLAIINNLLDFSRIES--------GQMTLSLEET 471
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129446385 701 FRRYTGEQVRLTLKLPAQSWRV--RCDMNQFENAVL------------NLVINACDAMPAGGdLEIEVAHREldaaavqt 766
Cdd:PRK15347  472 ALLPLLDQAMLTIQGPAQSKSLtlRTFVGAHVPLYLhldslrlrqilvNLLGNAVKFTETGG-IRLRVKRHE-------- 542
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2129446385 767 npcaeagEFVEVCVSDMGCGMAPDVLARVFEPFFTTKPMGQGTGLGLSMIYGFAQQAGGMVTIASVQAEGTAVRLFLP 844
Cdd:PRK15347  543 -------QQLCFTVEDTGCGIDIQQQQQIFTPFYQADTHSQGTGLGLTIASSLAKMMGGELTLFSTPGVGSCFSLVLP 613
YesN COG4753
Two-component response regulator, YesN/AraC family, consists of REC and AraC-type DNA-binding ...
875-953 1.31e-10

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: 59.02  E-value: 1.31e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129446385 875 EDDEHVRDMVRAALEELN--LTVLTAADGDAGHRLLQSDaRIDLLLSDVGLPGMNGHALAQAARALRPALRIILMTGYAD 952
Cdd:COG4753     6 DDEPLIREGLKRILEWEAgfEVVGEAENGEEALELLEEH-KPDLVITDINMPGMDGLELLEAIRELDPDTKIIILSGYSD 84

                  .
gi 2129446385 953 E 953
Cdd:COG4753    85 F 85
PtsP COG3605
Signal transduction protein containing GAF and PtsI domains [Signal transduction mechanisms];
23-203 1.45e-10

Signal transduction protein containing GAF and PtsI domains [Signal transduction mechanisms];


Pssm-ID: 442824 [Multi-domain]  Cd Length: 188  Bit Score: 61.45  E-value: 1.45e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129446385  23 RVMLQRIAAGVPLTDVLLHVMQAVEAQSSVELlTSIAFVDDSGMRLRHVATPSLPAAYVQATdGAAIGPGVAswGAAAFL 102
Cdd:COG3605     7 RRISEAVASALDLDEALDRIVRRIAEALGVDV-CSIYLLDPDGGRLELRATEGLNPEAVGKV-RLPLGEGLV--GLVAER 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129446385 103 GTPVYVEDLTVHPNWPpWREAATQHGLRACWSTPIKAtDGRTLGVFSNYYRQPRLPTREDIEAIALVTRTAALAIERHLT 182
Cdd:COG3605    83 GEPLNLADAASHPRFK-YFPETGEEGFRSFLGVPIIR-RGRVLGVLVVQSREPREFTEEEVEFLVTLAAQLAEAIANAEL 160
                         170       180
                  ....*....|....*....|.
gi 2129446385 183 EQALRNSSVRWRGMFERMQEG 203
Cdd:COG3605   161 LGELRAALAELSLAREEEREA 181
PRK11466 PRK11466
hybrid sensory histidine kinase TorS; Provisional
769-986 1.67e-10

hybrid sensory histidine kinase TorS; Provisional


Pssm-ID: 236914 [Multi-domain]  Cd Length: 914  Bit Score: 65.31  E-value: 1.67e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129446385 769 CAEAGEFVEVcvSDMGCGMAPDVLARVFEPFFTTKPMGQGTGLGLSMIYGFAQQAGGMVTIASVQAEGTAVRLFLP-RHv 847
Cdd:PRK11466  588 TDGEQWLVEV--EDSGCGIDPAKLAEIFQPFVQVSGKRGGTGLGLTISSRLAQAMGGELSATSTPEVGSCFCLRLPlRV- 664
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129446385 848 gepvALPAPESSEPPAAPAHAAVVALVEDDEHVRDMVRAALEELNLTVLTAADGDAGHRLLQSDARIDLLLSDVGLPGMN 927
Cdd:PRK11466  665 ----ATAPVPKTVNQAVRLDGLRLLLIEDNPLTQRITAEMLNTSGAQVVAVGNAAQALETLQNSEPFAAALVDFDLPDYD 740
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2129446385 928 GHALAQAARALRPALRIILMTGYA-DErengwARQERDVSL----IRKPFSPGELtarvCRLLA 986
Cdd:PRK11466  741 GITLARQLAQQYPSLVLIGFSAHViDE-----TLRQRTSSLfrgiIPKPVPREVL----GQLLA 795
REC_OmpR_PhoB cd17618
phosphoacceptor receiver (REC) domain of PhoB response regulator from the OmpR family; The ...
875-985 1.89e-10

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


Pssm-ID: 381133 [Multi-domain]  Cd Length: 118  Bit Score: 59.19  E-value: 1.89e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129446385 875 EDDEHVRDMVRAALEELNLTVLTAADGDAGHRLLQsDARIDLLLSDVGLPGMNG-----HALAQAARALRPalrIILMTG 949
Cdd:cd17618     7 EDEPAIREMIAFNLERAGFDVVEAEDAESAVNLIV-EPRPDLILLDWMLPGGSGiqfirRLKRDEMTRDIP---IIMLTA 82
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2129446385 950 YADERE--NGWARQERDvsLIRKPFSPGELTARVCRLL 985
Cdd:cd17618    83 RGEEEDkvRGLEAGADD--YITKPFSPRELVARIKAVL 118
HATPase_BasS-like cd16940
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
732-843 3.45e-10

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Escherichia coli BasS; This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component sensor histidine kinase (HKs) similar to Escherichia coli BasS HK of the BasS-BasR two-component regulatory system (TCS). Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA); some contain a HAMP sensory domain, while some an N-terminal two-component sensor kinase domain.


Pssm-ID: 340417 [Multi-domain]  Cd Length: 113  Bit Score: 58.19  E-value: 3.45e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129446385 732 AVLNLVINACDAMPAGGDLEIEVahrELDAAAVqtnpcaeagefveVCVSDMGCGMAPDVLARVFEPFFTTKPM-GQGTG 810
Cdd:cd16940    17 LLRNLVDNAVRYSPQGSRVEIKL---SADDGAV-------------IRVEDNGPGIDEEELEALFERFYRSDGQnYGGSG 80
                          90       100       110
                  ....*....|....*....|....*....|...
gi 2129446385 811 LGLSMIYGFAQQAGGMVTIASVQAEGTAVRLFL 843
Cdd:cd16940    81 LGLSIVKRIVELHGGQIFLGNAQGGGLEAWVRL 113
COG3920 COG3920
Two-component sensor histidine kinase, HisKA and HATPase domains [Signal transduction ...
323-844 3.96e-10

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


Pssm-ID: 443125 [Multi-domain]  Cd Length: 495  Bit Score: 63.39  E-value: 3.96e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129446385 323 LLTLGDRMREIHQQDQIEQMVCEELGRHLELGAVAVMESVPQRGDRIAASWGPRPPYDGRSMLESAPLTPDYYEAVRKGR 402
Cdd:COG3920     1 LLLALLLLLLLALAALLLLAALLLLAAALLLALLALLLLALLLLALLLASALLALLALSAAALAAALAVALAAAVGAAAA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129446385 403 TAYLSPYLAGPAGNQQPSAIVVPLRRWGRADGTLLVRPDPTHPLKGTDIAFIEEAAERMCEAIERSQYARVLEQRVEHAI 482
Cdd:COG3920    81 LLALLVLLLLLLLAAAALALALLLAALAGLLLLAALLLLRLVALLAALALLALLLLLLLLLAILALAELAVALAELAAAL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129446385 483 AERDRIWRLSPELLAVADHGGRLVSVNPAVRAILGWSPEQFLAMGLDEGVHPEDLASMQATLEAEPAEGMQPVRHLE--- 559
Cdd:COG3920   161 LLLAEELAALRLAAAALLLLLAALLDLGLALAALAAAALLALLLALELLLALLLLLLLLLALLLVLLAALLRLRAAVlee 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129446385 560 SRLLHKDGSYHWITWSLSRAEGNVYLAGRDDTDLKAQAEVLRQTEDALRQSQKLEAVgrLTGGIAHDFNNMLQGISGaly 639
Cdd:COG3920   241 LERRRRARGLGRLLLLLLLLLLLLRALLLLAAGIRLVITERKRAEEELEASLEEKEL--LLRELHHRVKNNLQVVSS--- 315
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129446385 640 LIDRKLRRSKPEEVGKYVRTAQestDR--AARLTQRLLTfsrqQAIDPQVFDPGDILRS-MDELFRRYTGEQVRLTLKLP 716
Cdd:COG3920   316 LLRLQARRADDPEAREALEESQ---NRiqALALVHELLY----QSEDWEGVDLRDYLRElLEPLRDSYGGRGIRIELDGP 388
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129446385 717 AqswrVRCDMNQfenAV-----LN-LVINACD-AMPAGGDLEIEVAhreldaaavqtnpCAEAGEFVEVCVSDMGCGMAP 789
Cdd:COG3920   389 D----VELPADA---AVplgliLNeLVTNALKhAFLSGEGGRIRVS-------------WRREDGRLRLTVSDNGVGLPE 448
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2129446385 790 DVlarvfepffttkPMGQGTGLGLSMIYGFAQQAGGMVTIASvqAEGTAVRLFLP 844
Cdd:COG3920   449 DV------------DPPARKGLGLRLIRALVRQLGGTLELDR--PEGTRVRITFP 489
HATPase_DpiB-CitA-like cd16915
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
735-844 4.34e-10

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: 57.68  E-value: 4.34e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129446385 735 NLVINACDAMPAGGDL--EIEVAHRELdaaavqtnpcaeaGEFVEVCVSDMGCGMAPDVLARVFEPFFTTKPMGqGTGLG 812
Cdd:cd16915     7 NLIDNALDALAATGAPnkQVEVFLRDE-------------GDDLVIEVRDTGPGIAPELRDKVFERGVSTKGQG-ERGIG 72
                          90       100       110
                  ....*....|....*....|....*....|..
gi 2129446385 813 LSMIYGFAQQAGGMVTIASVQAEGTAVRLFLP 844
Cdd:cd16915    73 LALVRQSVERLGGSITVESEPGGGTTFSIRIP 104
HATPase_EvgS-ArcB-TorS-like cd16922
Histidine kinase-like ATPase domain of two-component sensor histidine kinases, many are hybrid ...
733-844 6.26e-10

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: 57.50  E-value: 6.26e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129446385 733 VLNLVINACDAMPAGG-DLEIEVAHRELDAAAVqtnpcaeagefvEVCVSDMGCGMAPDVLARVFEPFF-----TTKPMG 806
Cdd:cd16922     5 LLNLLGNAIKFTEEGEvTLRVSLEEEEEDGVQL------------RFSVEDTGIGIPEEQQARLFEPFSqadssTTRKYG 72
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2129446385 807 qGTGLGLSMIYGFAQQAGGMVTIASVQAEGTAVRLFLP 844
Cdd:cd16922    73 -GTGLGLAISKKLVELMGGDISVESEPGQGSTFTFTLP 109
PAS_3 pfam08447
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
506-572 8.73e-10

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


Pssm-ID: 430001 [Multi-domain]  Cd Length: 89  Bit Score: 56.19  E-value: 8.73e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2129446385 506 VSVNPAVRAILGWSPEQFLAMGLD--EGVHPEDLASMQATLEAEPAEGmQPVRHlESRLLHKDGSYHWI 572
Cdd:pfam08447   2 IYWSPRFEEILGYTPEELLGKGESwlDLVHPDDRERVREALWEALKGG-EPYSG-EYRIRRKDGEYRWV 68
CitB COG4565
DNA-binding response regulator DpiB of citrate/malate metabolism [Transcription, Signal ...
875-990 9.45e-10

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


Pssm-ID: 443622 [Multi-domain]  Cd Length: 138  Bit Score: 57.67  E-value: 9.45e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129446385 875 EDDEHVRDMVRAALEELNL--TVLTAADGDAGHRLLQSDaRIDLLLSDVGLPGMNGHALAQAARALRPALRIILMTGYAD 952
Cdd:COG4565    10 EDDPMVAELLRRYLERLPGfeVVGVASSGEEALALLAEH-RPDLILLDIYLPDGDGLELLRELRARGPDVDVIVITAARD 88
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 2129446385 953 ERENGWARQERDVSLIRKPFSPGELTARV------CRLLAASQD 990
Cdd:COG4565    89 PETVREALRAGVVDYLIKPFTFERLREALeryleyRRLLREDQE 132
HATPase_Glnl-NtrB-like cd16918
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
730-844 1.93e-09

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Escherichia coli GlnL (synonyms NtrB and NRII); This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component sensor histidine kinase (HKs), similar to Escherichia coli GlnL/NtrB/NRII HK of the two-component regulatory system (TCS) GlnL/GlnG (NtrB-NtrC, or NRII-NRI), which regulates the transcription of genes encoding metabolic enzymes and permeases in response to carbon and nitrogen status in E. coli and related bacteria. Also included in this family are Rhodobacter capsulatus NtrB, Azospirillum brasilense NtrB, Vibrio alginolyticus NtrB, Rhizobium leguminosarum biovar phaseoli NtrB, and Herbaspirillum seropedicae NtrB. Escherichia coli GlnL/NtrB/NRII is both a kinase and a phosphatase, catalyzing the phosphorylation and dephosphorylation of GlnG/NtrC/NRI. The kinase and phosphatase activities of GlnL/NtrB/NRII are regulated by the PII signal transduction protein, which on binding to GlnL/NtrB/NRII, inhibits the kinase activity of GlnL/NtrB/NRII and activates the GlnL/NtrB/NRII phosphatase activity. Proteins having this HATPase domain also have a histidine kinase dimerization and phosphoacceptor domain (HisKA); some also contain PAS sensor domain(s).


Pssm-ID: 340395 [Multi-domain]  Cd Length: 109  Bit Score: 55.87  E-value: 1.93e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129446385 730 ENAVLNLVINACDAMPaGGDLEIEVAHRELDAAAV----QTNPCaeagefvEVCVSDMGCGMAPDVLARVFEPFFTTKPm 805
Cdd:cd16918     2 IQVFLNLVRNAAQALA-GSGGEIILRTRTQRQVTLghprHRLAL-------RVSVIDNGPGIPPDLQDTIFYPMVSGRE- 72
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2129446385 806 gQGTGLGLSMIYGFAQQAGGMVTIASvQAEGTAVRLFLP 844
Cdd:cd16918    73 -NGTGLGLAIAQNIVSQHGGVIECDS-QPGHTVFSVSLP 109
nifL_nitrog TIGR02938
nitrogen fixation negative regulator NifL; NifL is a modulator of the nitrogen fixation ...
474-844 2.16e-09

nitrogen fixation negative regulator NifL; NifL is a modulator of the nitrogen fixation positive regulator protein NifA, and is therefore a negative regulator. It binds NifA. NifA and NifL are encoded by adjacent genes. [Central intermediary metabolism, Nitrogen fixation, Regulatory functions, Protein interactions]


Pssm-ID: 131984 [Multi-domain]  Cd Length: 494  Bit Score: 61.07  E-value: 2.16e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129446385 474 LEQRVEHAIAERDRIWRLSPELLAVADHGGRLVSVNPAVRAI-----LGWSPEQFLAMGLDEGVHP-EDLASMQATLEAE 547
Cdd:TIGR02938 121 LEQVVANQKLLIESVVDAAPVAFVLLDPTGRVILDNQEYKKLatdlrVKEPAHTVLDLLREAWREAlAENWPQQLAFSNR 200
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129446385 548 PAE----GMQPVRHLE---SRLLHKDGSYHwiTWSLSRAEGNVYLAGRDDTDLKAQAE--VLRQTEDALRQSQKLEAVGR 618
Cdd:TIGR02938 201 EARfdrgGGRPARWLSctgSVIGMESDCAD--SFFCAAEQPYLLLTIADISNLREEQEraRLSALQALMAEEERLEAIRE 278
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129446385 619 LTGGIAHDFNNMLQGISGALYLIDRKLRRSKPEEVGKYVRTAQESTDRAARLTQRLLTFSRQQAIDPqvFDPGDILR--- 695
Cdd:TIGR02938 279 TLSAAIHRLQGPMNLISAAISVLQRRGDDAGNPASAAMLQQALSAGREHMEALRQVIPQSPQEIVVP--VNLNQILRdvi 356
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129446385 696 --SMDELFRRYTGEQVRLTLKLPAqswrVRCDMNQFENAVLNLVINACDAMPAGGdleieVAHRELDAAAVQTNPCaeag 773
Cdd:TIGR02938 357 tlSTPRLLAAGIVVDWQPAATLPA----ILGRELQLRSLFKALVDNAIEAMNIKG-----WKRRELSITTALNGDL---- 423
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2129446385 774 efVEVCVSDMGCGMAPDVLARVFEPFFTTK-PMGQGTGLGLSMIYGFAQQAGGMVTIASVQAEGTAVRLFLP 844
Cdd:TIGR02938 424 --IVVSILDSGPGIPQDLRYKVFEPFFTTKgGSRKHIGMGLSVAQEIVADHGGIIDLDDDYSEGCRIIVEFR 493
REC_CpdR_CckA-like cd18160
phosphoacceptor receiver (REC) domain of Brucella abortus CpdR and CckA, and similar domains; ...
875-972 4.58e-09

phosphoacceptor receiver (REC) domain of Brucella abortus CpdR and CckA, and similar domains; Two-component systems (TCSs), consisting of a sensor and a response regulator, are used by bacteria to adapt to changing environments. Processes regulated by TCSs in bacteria include sporulation, pathogenicity, virulence, chemotaxis and membrane transport. Response regulators share the common phosphoacceptor REC domain and differ output domains such as DNA, RNA, ligand, and protein-binding, or enzymatic domain. CpdR is a stand-alone REC protein. CckA is a sensor histidine kinase containing N-terminal PAS domains and a C-terminal REC domain. CpdR and CckA are components of a regulatory phosphorelay system (composed of CckA, ChpT, CtrA and CpdR) that controls Brucella abortus cell growth, division, and intracellular survival inside mammalian host cells. CckA autophosphorylates in the presence of ATP and transfers a phosphoryl group to the conserved aspartic acid residue on its C-terminal REC domain, which is relayed to the ChpT phosphotransferase. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381144 [Multi-domain]  Cd Length: 103  Bit Score: 54.82  E-value: 4.58e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129446385 875 EDDEHVRDMVRAALEELNLTVLTAADGDAGHRLLQSDARIDLLLSDVGLPGMNGHALAQAARALRPALRIILMTGYAder 954
Cdd:cd18160     6 DDEPSVRKFIVTTLKKAGYAVTEAESGAEALEKLQQGKDIDIVVTDIVMPEMDGIELAREARKIDPDVKILFISGGA--- 82
                          90       100
                  ....*....|....*....|.
gi 2129446385 955 ENGWARQ---ERDVSLIRKPF 972
Cdd:cd18160    83 AAAPELLsdaVGDNATLKKPF 103
REC_CheY4-like cd17562
phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY4 and similar CheY ...
875-985 5.72e-09

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: 55.00  E-value: 5.72e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129446385 875 EDDEHVRDMVRAALEELNLTVLTAADGDAGHRLLQSDaRIDLLLSDVGLPGMNGhALAQAARALRPALR----IILMTGY 950
Cdd:cd17562     7 DDSASIRQMVSFTLRGAGYEVVEAADGRDALSKAQSK-KFDLIITDQNMPNMDG-IELIKELRKLPAYKftpiLMLTTES 84
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 2129446385 951 ADEREN--------GWarqerdvslIRKPFSPGELTARVCRLL 985
Cdd:cd17562    85 SDEKKQegkaagatGW---------LVKPFDPEQLLEVVKKVL 118
REC_2_DhkD-like cd17580
second phosphoacceptor receiver (REC) domain of Dictyostelium discoideum hybrid signal ...
875-979 1.07e-08

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: 54.00  E-value: 1.07e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129446385 875 EDDEHVRDMVRAALEELNLTVLTAADGDAGHRLLQsDARIDLLLSDVGLPGMNGHALAQAARALRP--ALRIILMTGYAd 952
Cdd:cd17580     5 DDNEDAAEMLALLLELEGAEVTTAHSGEEALEAAQ-RFRPDVILSDIGMPGMDGYELARRLRELPWlaNTPAIALTGYG- 82
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2129446385 953 erengwarQERDVSLIR---------KPFSPGELTA 979
Cdd:cd17580    83 --------QPEDRERALeagfdahlvKPVDPDELIE 110
HATPase_TutC-TodS-like cd16925
Histidine kinase-like ATPase domain of hybrid sensor histidine kinases similar to Pseudomonas ...
725-844 1.17e-08

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


Pssm-ID: 340402 [Multi-domain]  Cd Length: 110  Bit Score: 53.65  E-value: 1.17e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129446385 725 DMNQFENAVLNLVINACDAMPAGGDLEIEVAhreldaaAVQTNPCaeagefvEVCVSDMGCGMAPDVLARVFEPFFTTKP 804
Cdd:cd16925     1 DAEKYERVVLNLLSNAFKFTPDGGRIRCILE-------KFRLNRF-------LLTVSDSGPGIPPNLREEIFERFRQGDG 66
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 2129446385 805 MGQ----GTGLGLSMIYGFAQQAGGMVTIASVQAEGTAVRLFLP 844
Cdd:cd16925    67 SSTrahgGTGLGLSIVKEFVELHGGTVTVSDAPGGGALFQVELP 110
REC_TrrA-like cd17554
phosphoacceptor receiver (REC) domain of Thermotoga maritima response regulator TrrA and ...
875-959 1.84e-08

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: 53.38  E-value: 1.84e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129446385 875 EDDEHVRDMVRAALEELNLTVLTAADGDAGHRLLQSDaRIDLLLSDVGLPGMNGHALAQAARALRPALRIILMTGYADER 954
Cdd:cd17554     7 DDEENIRELYKEELEDEGYEVVTAGNGEEALEKLESE-DPDLVILDIKMPGMDGLETLRKIREKKPDLPVIICTAYSEYK 85

                  ....*..
gi 2129446385 955 EN--GWA 959
Cdd:cd17554    86 SDfsSWA 92
PAS smart00091
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
483-545 3.60e-08

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


Pssm-ID: 214512  Cd Length: 67  Bit Score: 50.86  E-value: 3.60e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2129446385  483 AERDRIWRLSPELLAVADHGGRLVSVNPAVRAILGWSPEQFLAMGLDEGVHPEDLASMQATLE 545
Cdd:smart00091   1 ERLRAILESLPDGIFVLDLDGRILYANPAAEELLGYSPEELIGKSLLELIHPEDRERVQEALQ 63
HATPase_BceS-YxdK-YvcQ-like cd16948
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
736-844 5.36e-08

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Bacillus subtilis BceS, YxdK, and Bacillus thuringiensis YvcQ; This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component sensor histidine kinase (HKs) such as Bacillus subtilis BceS and Bacillus thuringiensis YvcQ, the HKs of the two-component regulatory system (TCSs) BceS-BceR and YvcQ-YvcP, repsectively, which are both involved in regulating bacitracin resistance. It also includes the HATPase domain of YxdK, the HK of YxdK-YxdJ TCS involved in sensing antimicrobial compounds.


Pssm-ID: 340424 [Multi-domain]  Cd Length: 109  Bit Score: 51.90  E-value: 5.36e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129446385 736 LVINACDAMPAGGDLEIEVAHREldaaavqtnpcaeagEFVEVCVSDMGCGMAPDVLARVFEPFFTTK---PMGQGTGLG 812
Cdd:cd16948    13 IVSNALKYSKQGGKIEIYSETNE---------------QGVVLSIKDFGIGIPEEDLPRVFDKGFTGEngrNFQESTGMG 77
                          90       100       110
                  ....*....|....*....|....*....|..
gi 2129446385 813 LSMIYGFAQQAGGMVTIASVQAEGTAVRLFLP 844
Cdd:cd16948    78 LYLVKKLCDKLGHKIDVESEVGEGTTFTITFP 109
PRK11361 PRK11361
acetoacetate metabolism transcriptional regulator AtoC;
875-985 5.82e-08

acetoacetate metabolism transcriptional regulator AtoC;


Pssm-ID: 183099 [Multi-domain]  Cd Length: 457  Bit Score: 56.40  E-value: 5.82e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129446385 875 EDDEHVRDMVRAALEELNLTVLTAADGDAGHRLLqSDARIDLLLSDVGLPGMNGHALAQAARALRPALRIILMTGYADER 954
Cdd:PRK11361   11 DDEDNVRRMLSTAFALQGFETHCANNGRTALHLF-ADIHPDVVLMDIRMPEMDGIKALKEMRSHETRTPVILMTAYAEVE 89
                          90       100       110
                  ....*....|....*....|....*....|.
gi 2129446385 955 ENGWARQERDVSLIRKPFSPGELTARVCRLL 985
Cdd:PRK11361   90 TAVEALRCGAFDYVIKPFDLDELNLIVQRAL 120
COG4567 COG4567
DNA-binding response regulator, ActR/RegA family, consists of REC and Fis-type HTH domains ...
875-952 5.89e-08

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


Pssm-ID: 443624 [Multi-domain]  Cd Length: 177  Bit Score: 53.38  E-value: 5.89e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2129446385 875 EDDEHVRDMVRAALEELNLTVLTAADGDAGHRLLQsDARIDLLLSDVGLPGMNGHALAQAARALRPALRIILMTGYAD 952
Cdd:COG4567    11 DDDEAFARVLARALERRGFEVTTAASVEEALALLE-QAPPDYAVLDLRLGDGSGLDLIEALRERDPDARIVVLTGYAS 87
REC smart00448
cheY-homologous receiver domain; CheY regulates the clockwise rotation of E. coli flagellar ...
875-924 1.08e-07

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


Pssm-ID: 214668 [Multi-domain]  Cd Length: 55  Bit Score: 49.10  E-value: 1.08e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 2129446385  875 EDDEHVRDMVRAALEELNLTVLTAADGDAGHRLLQSDaRIDLLLSDVGLP 924
Cdd:smart00448   7 DDDPLLRELLKALLEKEGYEVDEATDGEEALELLKEE-KPDLILLDIMMP 55
HATPase_CreC-like cd16945
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
730-838 2.30e-07

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Escherichia coli CreC; This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component sensor histidine kinase (HKs) such as Escherichia coli CreC of the CreC-CreB two-component regulatory system (TCS) involved in catabolic regulation. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA), and accessory sensory domain(s) such as HAMP, CACHE or PAS.


Pssm-ID: 340421 [Multi-domain]  Cd Length: 106  Bit Score: 50.15  E-value: 2.30e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129446385 730 ENAVLNLVINACDAMPAGGDLEIEVahrELDaaavqtnpcaeaGEFVEVCVSDMGCGMAPDVLARVFEPFFT-TKPMGQ- 807
Cdd:cd16945     6 RQAINNLLDNAIDFSPEGGLIALQL---EAD------------TEGIELLVFDEGSGIPDYALNRVFERFYSlPRPHSGq 70
                          90       100       110
                  ....*....|....*....|....*....|..
gi 2129446385 808 -GTGLGLSMIYGFAQQAGGMVTIASVQAEGTA 838
Cdd:cd16945    71 kSTGLGLAFVQEVAQLHGGRITLRNRPDGVLA 102
REC_HupR-like cd17569
phosphoacceptor receiver (REC) domain of hydrogen uptake protein regulator (HupR) and similar ...
876-952 2.54e-07

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


Pssm-ID: 381113 [Multi-domain]  Cd Length: 118  Bit Score: 50.09  E-value: 2.54e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2129446385 876 DDEHVRDMVRAALEELNLTVLTAADGDAGHRLLQSDaRIDLLLSDVGLPGMNGHALAQAARALRP-ALRIILmTGYAD 952
Cdd:cd17569     8 DEPNILKALKRLLRREGYEVLTATSGEEALEILKQE-PVDVVISDQRMPGMDGAELLKRVRERYPdTVRILL-TGYAD 83
PRK10337 PRK10337
sensor protein QseC; Provisional
665-841 2.61e-07

sensor protein QseC; Provisional


Pssm-ID: 182388 [Multi-domain]  Cd Length: 449  Bit Score: 54.27  E-value: 2.61e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129446385 665 DRAARLTQRLLTFSRQQAID-PQVFDP---GDILRS--MDELfrrYTGEQVRLTLKLPAQSWRVrCDMNQ---FENAVLN 735
Cdd:PRK10337  284 DRATRLVDQLLTLSRLDSLDnLQDVAEiplEDLLQSavMDIY---HTAQQAGIDVRLTLNAHPV-IRTGQpllLSLLVRN 359
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129446385 736 LVINACDAMPAGGDLEIEVAHRELDaaavqtnpcaeagefvevcVSDMGCGMAPDVLARVFEPFFttKPMGQ---GTGLG 812
Cdd:PRK10337  360 LLDNAIRYSPQGSVVDVTLNARNFT-------------------VRDNGPGVTPEALARIGERFY--RPPGQeatGSGLG 418
                         170       180
                  ....*....|....*....|....*....
gi 2129446385 813 LSMIYGFAQQAGGMVTIASVQAEGTAVRL 841
Cdd:PRK10337  419 LSIVRRIAKLHGMNVSFGNAPEGGFEAKV 447
REC_RR468-like cd17552
phosphoacceptor receiver (REC) domain of Thermotoga maritima response regulator RR468 and ...
875-985 2.66e-07

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


Pssm-ID: 381104 [Multi-domain]  Cd Length: 121  Bit Score: 50.24  E-value: 2.66e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129446385 875 EDDEHVRDMVRAALEEL-NLTVLTAADGDAGHRLLQSDaRIDLLLSDVGLPGMNGhALAQAARALRPALR---IILMTGY 950
Cdd:cd17552     8 DDEEDIREVVQACLEKLaGWEVLTASSGQEGLEKAATE-QPDAILLDVMMPDMDG-LATLKKLQANPETQsipVILLTAK 85
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2129446385 951 ADEREngwarQERDVSL-----IRKPFSPGELTARVCRLL 985
Cdd:cd17552    86 AQPSD-----RQRFASLgvagvIAKPFDPLTLAEQIAKLL 120
HisKA pfam00512
His Kinase A (phospho-acceptor) domain; dimerization and phospho-acceptor domain of histidine ...
615-682 2.75e-07

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


Pssm-ID: 459839 [Multi-domain]  Cd Length: 66  Bit Score: 48.36  E-value: 2.75e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2129446385 615 AVGRLTGGIAHDFNNMLQGISGALYLIdrkLRRSKPEEVGKYVRTAQESTDRAARLTQRLLTFSRQQA 682
Cdd:pfam00512   1 AKSEFLANLSHELRTPLTAIRGYLELL---RDEKLDEEQREYLETILRSAERLLRLINDLLDLSRIEA 65
GAF pfam01590
GAF domain; This domain is present in cGMP-specific phosphodiesterases, adenylyl and guanylyl ...
97-177 2.83e-07

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


Pssm-ID: 460259 [Multi-domain]  Cd Length: 133  Bit Score: 50.56  E-value: 2.83e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129446385  97 GAAAFLGTPVYVEDLTVHPNWPPWREAATQHGLRACWSTPIKAtDGRTLGVFSNYYRQPRLpTREDIEAIALVTRTAALA 176
Cdd:pfam01590  55 VTVLRTGRPLVVPDAAGDPRFLDPLLLLRNFGIRSLLAVPIID-DGELLGVLVLHHPRPPF-TEEELELLEVLADQVAIA 132

                  .
gi 2129446385 177 I 177
Cdd:pfam01590 133 L 133
REC_YesN-like cd17536
phosphoacceptor receiver (REC) domain of YesN and related helix-turn-helix containing response ...
875-952 3.93e-07

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: 49.64  E-value: 3.93e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129446385 875 EDDEHVRDMVRAAL--EELNLT-VLTAADGDAGHRLLQSDaRIDLLLSDVGLPGMNGHALAQAARALRPALRIILMTGYA 951
Cdd:cd17536     5 DDEPLIREGLKKLIdwEELGFEvVGEAENGEEALELIEEH-KPDIVITDIRMPGMDGLELIEKIRELYPDIKIIILSGYD 83

                  .
gi 2129446385 952 D 952
Cdd:cd17536    84 D 84
REC_OmpR_BsPhoP-like cd19937
phosphoacceptor receiver (REC) domain of BsPhoP-like OmpR family response regulators; Bacillus ...
875-985 3.93e-07

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: 49.58  E-value: 3.93e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129446385 875 EDDEHVRDMVRAALEELNLTVLTAADGDAGHRLLQSDaRIDLLLSDVGLPGMNG-----HALAQAARALRPalrIILMTG 949
Cdd:cd19937     4 DDEEDIVELLKYNLEKEGYEVVTAYDGEEALKRAKDE-KPDLIILDLMLPGIDGlevcrILRSDPKTSSIP---IIMLTA 79
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 2129446385 950 YADErengwarQERDVSL-------IRKPFSPGELTARVCRLL 985
Cdd:cd19937    80 KGEE-------FDKVLGLelgaddyITKPFSPRELLARVKAVL 115
PRK10604 PRK10604
sensor protein RstB; Provisional
670-855 7.37e-07

sensor protein RstB; Provisional


Pssm-ID: 236724 [Multi-domain]  Cd Length: 433  Bit Score: 52.68  E-value: 7.37e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129446385 670 LTQRLLTFSR----QQAIDPQVFDPGDILRSMDELFRRYTGEqVRLTLKLPAQSWRVRCDMNQFENAVLNLVINACDAmp 745
Cdd:PRK10604  258 LIEELLTYARldrpQNELHLSEPDLPAWLSTHLADIQAVTPE-KTVRLDTPHQGDYGALDMRLMERVLDNLLNNALRY-- 334
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129446385 746 AGGDLEIEVAHReldaaavqtnpcaeaGEFVEVCVSDMGCGMAPDVLARVFEPFFTTKPMGQ----GTGLGLSMIYGFAQ 821
Cdd:PRK10604  335 AHSRVRVSLLLD---------------GNQACLIVEDDGPGIPPEERERVFEPFVRLDPSRDratgGCGLGLAIVHSIAL 399
                         170       180       190
                  ....*....|....*....|....*....|....
gi 2129446385 822 QAGGMVTIASVQAEGTAVRLFLPRHVGEPVALPA 855
Cdd:PRK10604  400 AMGGSVNCDESELGGARFSFSWPVWHNLPQFTSA 433
REC_DctD-like cd17549
phosphoacceptor receiver (REC) domain of C4-dicarboxylic acid transport protein D (DctD) and ...
875-987 8.42e-07

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


Pssm-ID: 381101 [Multi-domain]  Cd Length: 130  Bit Score: 49.03  E-value: 8.42e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129446385 875 EDDEHVRDMVRAALEELNLTVLTAADGDAGHRLLQSDaRIDLLLSDVGLPGMNGHALAQAARALRPALRIILMTGYAder 954
Cdd:cd17549     5 DDDADVREALQQTLELAGFRVRAFADAEEALAALSPD-FPGVVISDIRMPGMDGLELLAQIRELDPDLPVILITGHG--- 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 2129446385 955 engwarqerDVSL------------IRKPFSPGELTARVCRLLAA 987
Cdd:cd17549    81 ---------DVPMaveamragaydfLEKPFDPERLLDVVRRALEK 116
REC_NarL-like cd17535
phosphoacceptor receiver (REC) domain of NarL (Nitrate/Nitrite response regulator L) family ...
875-986 2.68e-06

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: 47.12  E-value: 2.68e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129446385 875 EDDEHVRDMVRAALE-ELNLTVL-TAADGDAGHRLLQsDARIDLLLSDVGLPGMNGHALAQAARALRPALRIILMTGYAD 952
Cdd:cd17535     5 DDHPLVREGLRRLLEsEPDIEVVgEAADGEEALALLR-ELRPDVVLMDLSMPGMDGIEALRRLRRRYPDLKVIVLTAHDD 83
                          90       100       110
                  ....*....|....*....|....*....|....
gi 2129446385 953 ERENGWARQERDVSLIRKPFSPGELTARVCRLLA 986
Cdd:cd17535    84 PEYVLRALKAGAAGYLLKDSSPEELIEAIRAVAA 117
PAS pfam00989
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
483-581 2.91e-06

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


Pssm-ID: 395786 [Multi-domain]  Cd Length: 113  Bit Score: 47.03  E-value: 2.91e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129446385 483 AERDRIWRLSPELLAVADHGGRLVSVNPAVRAILGWSPEQFLAMGLDEGVHPEDLASMQATLEaEPAEGMQPVRHLESRL 562
Cdd:pfam00989   1 EDLRAILESLPDGIFVVDEDGRILYVNAAAEELLGLSREEVIGKSLLDLIPEEDDAEVAELLR-QALLQGEESRGFEVSF 79
                          90       100
                  ....*....|....*....|.
gi 2129446385 563 LHKDGSYHWI--TWSLSRAEG 581
Cdd:pfam00989  80 RVPDGRPRHVevRASPVRDAG 100
phoR PRK11006
phosphate regulon sensor histidine kinase PhoR;
654-816 3.46e-06

phosphate regulon sensor histidine kinase PhoR;


Pssm-ID: 182895 [Multi-domain]  Cd Length: 430  Bit Score: 50.78  E-value: 3.46e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129446385 654 GKYVRTAQESTDRAARLTQRLLTFSRQQA---ID-PQVFDPGDILRSMDELFRRYTGEQVRLTLKLPAQsWRVRCDMNQF 729
Cdd:PRK11006  240 EKALHTMREQTQRMEGLVKQLLTLSKIEAaptIDlNEKVDVPMMLRVLEREAQTLSQGKHTITFEVDNS-LKVFGNEDQL 318
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129446385 730 ENAVLNLVINACDAMPAGGdlEIEVAHRELDAAAvqtnpcaeagefvEVCVSDMGCGMAPDVLARVFEPFF-----TTKP 804
Cdd:PRK11006  319 RSAISNLVYNAVNHTPEGT--HITVRWQRVPQGA-------------EFSVEDNGPGIAPEHIPRLTERFYrvdkaRSRQ 383
                         170
                  ....*....|..
gi 2129446385 805 MGqGTGLGLSMI 816
Cdd:PRK11006  384 TG-GSGLGLAIV 394
REC_OmpR_DrrD-like cd17625
phosphoacceptor receiver (REC) domain of DrrD-like OmpR family response regulators; DrrD is a ...
875-985 3.50e-06

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: 46.83  E-value: 3.50e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129446385 875 EDDEHVRDMVRAALEELNLTVLTAADGDAGhrLLQSDARI-DLLLSDVGLPGMNGHALAQAARALRPALRIILMT--GYA 951
Cdd:cd17625     4 EDEKDLSEAITKHLKKEGYTVDVCFDGEEG--LEYALSGIyDLIILDIMLPGMDGLEVLKSLREEGIETPVLLLTalDAV 81
                          90       100       110
                  ....*....|....*....|....*....|....
gi 2129446385 952 DERENGWARQERDvsLIRKPFSPGELTARVCRLL 985
Cdd:cd17625    82 EDRVKGLDLGADD--YLPKPFSLAELLARIRALL 113
HATPase_EnvZ-like cd16950
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
732-844 4.68e-06

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Escherichia coli EnvZ and Pseudomonas aeruginosa BfmS; This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component sensor histidine kinase (HKs) such as Escherichia coli EnvZ of the EnvZ-OmpR two-component regulatory system (TCS), which functions in osmoregulation. It also contains the HATPase domain of Pseudomonas aeruginosa BfmS, the HK of the BfmSR TCS, which functions in the regulation of the rhl quorum-sensing system and bacterial virulence in P. aeruginosa. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA) and a HAMP sensor domain; some also contain a periplasmic domain.


Pssm-ID: 340426 [Multi-domain]  Cd Length: 101  Bit Score: 46.29  E-value: 4.68e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129446385 732 AVLNLVINACDAmpagGDLEIEVAHreldaaavQTNpcaeaGEFVEVCVSDMGCGMAPDVLARVFEPFFTTKPM--GQGT 809
Cdd:cd16950     4 VLSNLVDNALRY----GGGWVEVSS--------DGE-----GNRTRIQVLDNGPGIAPEEVDELFQPFYRGDNArgTSGT 66
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2129446385 810 GLGLSMIYGFAQQAGGMVTIASVQAEGTAVRLFLP 844
Cdd:cd16950    67 GLGLAIVQRISDAHGGSLTLANRAGGGLCARIELP 101
REC_DivK-like cd17548
phosphoacceptor receiver (REC) domain of DivK and similar proteins; Caulobacter crescentus ...
875-928 4.75e-06

phosphoacceptor receiver (REC) domain of DivK and similar proteins; Caulobacter crescentus DivK is an essential response regulator that is involved in the complex phosphorelay pathways controlling both cell division and motility. It localizes cell cycle regulators to specific poles of the cell during division. DivK contains a stand-alone REC domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381100 [Multi-domain]  Cd Length: 115  Bit Score: 46.38  E-value: 4.75e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2129446385 875 EDDEHVRDMVRAALEELNLTVLTAADGDAGHRLLQSdARIDLLLSDVGLPGMNG 928
Cdd:cd17548     6 EDNPLNMKLARDLLESAGYEVLEAADGEEALEIARK-EKPDLILMDIQLPGMDG 58
REC_2_GGDEF cd17544
second phosphoacceptor receiver (REC) domain of uncharacterized GGDEF domain proteins; This ...
875-928 4.88e-06

second phosphoacceptor receiver (REC) domain of uncharacterized GGDEF domain proteins; This family is composed of uncharacterized PleD-like response regulators that contain two N-terminal REC domains and a C-terminal diguanylate cyclase output domain with the characteristic GGDEF motif at the active site. Unlike PleD which contains a REC-like adaptor domain, the second REC domain of these uncharacterized GGDEF domain proteins, described in this model, contains characteristic metal-binding and active site residues. PleD response regulators are global regulators of cell metabolism in some important human pathogens. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381098 [Multi-domain]  Cd Length: 122  Bit Score: 46.74  E-value: 4.88e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2129446385 875 EDDEHVRDMVRAALEELNLTVLTAADGDAGHRLLQSDARIDLLLSDVGLPGMNG 928
Cdd:cd17544     7 DDSATSRNHLRALLRRHNFQVLEAANGQEALEVLEQHPDIKLVITDYNMPEMDG 60
YesM COG2972
Sensor histidine kinase YesM [Signal transduction mechanisms];
661-845 6.23e-06

Sensor histidine kinase YesM [Signal transduction mechanisms];


Pssm-ID: 442211 [Multi-domain]  Cd Length: 445  Bit Score: 50.02  E-value: 6.23e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129446385 661 QESTDRAARLTQRLLTFSRQQAIDPQVFDPgdiLRsmDELF--RRY-TGEQVRLTLKLpaqswRVRCDMnqfENAVLNLV 737
Cdd:COG2972   269 LEDPEEAEEMLEALSKLLRYSLSKGDELVT---LE--EELEliKSYlEIQKLRFGDRL-----EVEIEI---DEELLDLL 335
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129446385 738 I----------NAC----DAMPAGGDLEIEVAHReldaaavqtnpcaeaGEFVEVCVSDMGCGMAPDVLARVFEPfFTTK 803
Cdd:COG2972   336 IpklilqplveNAIehgiEPKEGGGTIRISIRKE---------------GDRLVITVEDNGVGMPEEKLEKLLEE-LSSK 399
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 2129446385 804 PMGQGTGLG-----LSMIYGfaQQAGgmVTIASVQAEGTAVRLFLPR 845
Cdd:COG2972   400 GEGRGIGLRnvrerLKLYYG--EEYG--LEIESEPGEGTTVTIRIPL 442
FixJ COG4566
DNA-binding response regulator, FixJ family, consists of REC and HTH domains [Signal ...
876-990 6.46e-06

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: 47.79  E-value: 6.46e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129446385 876 DDEHVRDMVRAALEELNLTVLTAADGDAghrLLQSD--ARIDLLLSDVGLPGMNGHALAQAARALRPALRIILMTGYADE 953
Cdd:COG4566     7 DDEAVRDSLAFLLESAGLRVETFASAEA---FLAALdpDRPGCLLLDVRMPGMSGLELQEELAARGSPLPVIFLTGHGDV 83
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 2129446385 954 RE------NGwArqerdVSLIRKPFSPGELTARVCRLLAASQD 990
Cdd:COG4566    84 PMavramkAG-A-----VDFLEKPFDDQALLDAVRRALARDRA 120
dpiB PRK15053
sensor histidine kinase DpiB; Provisional
725-845 8.01e-06

sensor histidine kinase DpiB; Provisional


Pssm-ID: 185013 [Multi-domain]  Cd Length: 545  Bit Score: 49.83  E-value: 8.01e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129446385 725 DMNQFENAVLNLVINACDA--MPAGGDLEIEVAhreldaaavqtnpCAEAGEFVEVCVSDMGCGMAPDVLARVFEPFFTT 802
Cdd:PRK15053  429 DSTEFAAIVGNLLDNAFEAslRSDEGNKIVELF-------------LSDEGDDVVIEVADQGCGVPESLRDKIFEQGVST 495
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 2129446385 803 KPMGQGT-GLGLSMIYGFAQQAGGMVTIASVQAEGTAVRLFLPR 845
Cdd:PRK15053  496 RADEPGEhGIGLYLIASYVTRCGGVITLEDNDPCGTLFSIFIPK 539
AmiR COG3707
Two-component response regulator, AmiR/NasT family, consists of REC and RNA-binding ...
875-979 1.23e-05

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: 47.26  E-value: 1.23e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129446385 875 EDDEHVRDMVRAALEELNLTVLTAADGDAGHRLLQSDARIDLLLSDVGLPGMNGHALAQAARALRPAlRIILMTGYADER 954
Cdd:COG3707    10 DDEPLRRADLREGLREAGYEVVAEAADGEDAVELVRELKPDLVIVDIDMPDRDGLEAARQISEERPA-PVILLTAYSDPE 88
                          90       100
                  ....*....|....*....|....*
gi 2129446385 955 ENGWARQERDVSLIRKPFSPGELTA 979
Cdd:COG3707    89 LIERALEAGVSAYLVKPLDPEDLLP 113
GAF COG2203
GAF domain [Signal transduction mechanisms];
153-764 1.24e-05

GAF domain [Signal transduction mechanisms];


Pssm-ID: 441805 [Multi-domain]  Cd Length: 712  Bit Score: 49.42  E-value: 1.24e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129446385 153 RQPRLPTREDIEAIALVTRTAALAIERHLTEQALRNSSVRWRGMFERMQEGFFLAEAQRDSTGSVDDFTLLEINPAFETQ 232
Cdd:COG2203    24 TLLLALLLLALQALERVLETTELALALELLLERLTELRAAARLAAEAAEAALLLILLIDALVLLSLVATAGLVLELADLL 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129446385 233 SGLAVGQTLGPMLRVMSPAAADSIMRIFVGVIESGEPAQFEVEAPGPPQACYECRAGKEGHDRVAALFLNVTARKLAESE 312
Cdd:COG2203   104 LLLRLLALLVLLLVALALAEALAARLLDLLLLGLGGRLRGVVLRGLRSAALLLSRVDTDLVGQLAALAGLILDIARLLTQ 183
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129446385 313 LWERQYRK-NFLLTLGDRMREIHQQDQIEQMVCEELGRHLELGAVAVMESVPQRGD-RIAASWGPRPPYDGRSMLESAPL 390
Cdd:COG2203   184 RARLELERlALLNEISQALRSALDLEELLQRILELAGELLGADRGAILLVDEDGGElELVAAPGLPEEELGRLPLGEGLA 263
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129446385 391 tpdyYEAVRKGRTAYLSPYLAGPAGNQQP----------SAIVVPLRRWGRADGTLLVRPDPTHPLKGTDIAFIEEAAER 460
Cdd:COG2203   264 ----GRALRTGEPVVVNDASTDPRFAPSLrelllalgirSLLCVPLLVDGRLIGVLALYSKEPRAFTEEDLELLEALADQ 339
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129446385 461 MCEAIERSQYARVLEQRVEHAIAERDRIWRLSPELLAVADHGGRLVSVNPAVRAILGWSPEQFLAMGLDEGVHPEDLASM 540
Cdd:COG2203   340 AAIAIERARLYEALEAALAALLQELALLRLLLDLELTLLRLRQLLLELLLALLLLLSLLGAELLLLLLDAADLSGLLALE 419
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129446385 541 QATLEAEPAEGMQPVRHLESRLLHKDGSYHWITWSLSRAEGNVYLAGRDDTDLKAQAEVLRQTEDALRQSQKLEAVGRLT 620
Cdd:COG2203   420 GLLLLDLLLLLLLLRRILLLRVLRRLLLGDEEGLVLLLALAELELLEILELLVLLAVILLALALLAALLLLLLLLLALLA 499
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129446385 621 GGIAHDFNNMLQGISGALYLIDRKLRRSKPEEVGKYVRTAQESTDRAARLTQRLLTFSRQQAIDPQVFDPGDILRSMDEL 700
Cdd:COG2203   500 LSALAVLASLLLALLLLLLLLLLLLLLGLLAALAADLLLLAAALLEDLLILLLVLLLERELLTLVGVLLLLGLSVLLIEL 579
                         570       580       590       600       610       620
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2129446385 701 FRRYTGEQVRLTLKLPAQSWRVRCDMNQFENAVLNLVINACDAMPAGGDLEIEVAHRELDAAAV 764
Cdd:COG2203   580 ALALILALALLELLLVAVGDLLLLERDLLLLLVLLVRLLLELLVVTLELTVLVVLAAVEDSALL 643
REC_OmpR_ArcA_TorR-like cd17619
phosphoacceptor receiver (REC) domain of ArcA- and TorR-like OmpR family response regulators; ...
875-981 1.47e-05

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: 45.07  E-value: 1.47e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129446385 875 EDDEHVRDMVRAALEELNLTVLTAADGDAGHRLLQsDARIDLLLSDVGLPGMNGhALAQAARALRPALRIILMTGYADEr 954
Cdd:cd17619     7 EDEPVTRATLKSYFEQEGYDVSEAGDGEEMRQILA-RQDIDLVLLDINLPGKDG-LSLTRELREQSEVGIILVTGRDDE- 83
                          90       100       110
                  ....*....|....*....|....*....|....
gi 2129446385 955 engwarQERDVSL-------IRKPFSPGELTARV 981
Cdd:cd17619    84 ------VDRIVGLeigaddyVTKPFNPRELLVRA 111
REC_RssB-like cd17555
phosphoacceptor receiver (REC) domain of Pseudomonas aeruginosa RssB and similar domains; ...
875-949 1.48e-05

phosphoacceptor receiver (REC) domain of Pseudomonas aeruginosa RssB and similar domains; Pseudomonas aeruginosa RssB is an orphan atypical response regulator containing a REC domain and a PP2C-type protein phosphatase output domain. Its function is still unknown. Escherichia RssB, which is not included in this subfamily, is a ClpX adaptor protein which alters ClpX specificity by mediating a specific interaction between ClpX and the substrates such as RpoS, an RNA polymerase sigma factor. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381107 [Multi-domain]  Cd Length: 116  Bit Score: 45.27  E-value: 1.48e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2129446385 875 EDDEHVRDMVRAALEELNLTVLTAADGDAGHRLLQSDaRIDLLLSDVGLPGMNGHALAQAARALRPALRIILMTG 949
Cdd:cd17555     7 DDDEVVRESIAAYLEDSGFQVLQAADGRQGLELFRSE-QPDLVLCDLRMPEMDGLEVLKQITKESPDTPVIVVSG 80
PRK11086 PRK11086
sensory histidine kinase DcuS; Provisional
735-844 1.60e-05

sensory histidine kinase DcuS; Provisional


Pssm-ID: 236839 [Multi-domain]  Cd Length: 542  Bit Score: 48.76  E-value: 1.60e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129446385 735 NLVINACDAMPAGGDLEIEVAHRELDaaavqtnpcaeagEFVEVCVSDMGCGMAPDVLARVFEPFFTTKpmGQGTGLGLS 814
Cdd:PRK11086  440 NLIENALEAVGGEEGGEISVSLHYRN-------------GWLHCEVSDDGPGIAPDEIDAIFDKGYSTK--GSNRGVGLY 504
                          90       100       110
                  ....*....|....*....|....*....|
gi 2129446385 815 MIYGFAQQAGGMVTIASVQAEGTAVRLFLP 844
Cdd:PRK11086  505 LVKQSVENLGGSIAVESEPGVGTQFFVQIP 534
PRK09835 PRK09835
Cu(+)/Ag(+) sensor histidine kinase;
707-846 1.61e-05

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


Pssm-ID: 182101 [Multi-domain]  Cd Length: 482  Bit Score: 48.61  E-value: 1.61e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129446385 707 EQVRLTLKLPAQSWRVRCDMNQFENAVLNLVINACDAMPAGgdleievahrelDAAAVQtnpCAEAGEFVEVCVSDMGCG 786
Cdd:PRK09835  354 EERGVELRFVGDPCQVAGDPLMLRRAISNLLSNALRYTPAG------------EAITVR---CQEVDHQVQLVVENPGTP 418
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2129446385 787 MAPDVLARVFEPFFTTKPM----GQGTGLGLSMIYGFAQQAGGMVTIASvQAEGTAVRLFLPRH 846
Cdd:PRK09835  419 IAPEHLPRLFDRFYRVDPSrqrkGEGSGIGLAIVKSIVVAHKGTVAVTS-DARGTRFVISLPRL 481
glnL PRK11073
nitrogen regulation protein NR(II);
601-815 1.62e-05

nitrogen regulation protein NR(II);


Pssm-ID: 182947 [Multi-domain]  Cd Length: 348  Bit Score: 48.15  E-value: 1.62e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129446385 601 RQTEDALRQSQKLeAVGRLTGGIAHDFNNMLQGISGALYLIDRKLrrskPE-EVGKYVRTAQESTDRAARLTQRLLtfsr 679
Cdd:PRK11073  116 RLSQEQLQHAQQV-AARDLVRGLAHEIKNPLGGLRGAAQLLSKAL----PDpALTEYTKVIIEQADRLRNLVDRLL---- 186
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129446385 680 qqaiDPQvfDPGdiLRSMDELfrRYTGEQVR--LTLKLPAQSWRVR----------CDMNQFENAVLNLVINACDAM-PA 746
Cdd:PRK11073  187 ----GPQ--RPG--THVTESI--HKVAERVVqlVSLELPDNVRLIRdydpslpelaHDPDQIEQVLLNIVRNALQALgPE 256
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2129446385 747 GGdlEIEVAHRELDAAAVQTNPCAEAGEfVEVCvsDMGCGMAPDVLARVFEPFFTTKPmgQGTGLGLSM 815
Cdd:PRK11073  257 GG--TITLRTRTAFQLTLHGERYRLAAR-IDIE--DNGPGIPPHLQDTLFYPMVSGRE--GGTGLGLSI 318
PRK11173 PRK11173
two-component response regulator; Provisional
876-985 1.71e-05

two-component response regulator; Provisional


Pssm-ID: 183013 [Multi-domain]  Cd Length: 237  Bit Score: 47.32  E-value: 1.71e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129446385 876 DDEHV-RDMVRAALEELNLTVLTAADGDAGHRLLqSDARIDLLLSDVGLPGMNGhalaqaaRALRPALR------IILMT 948
Cdd:PRK11173   10 EDELVtRNTLKSIFEAEGYDVFEATDGAEMHQIL-SENDINLVIMDINLPGKNG-------LLLARELReqanvaLMFLT 81
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2129446385 949 GyadeRENgwarqERDVSL---------IRKPFSPGELTARVCRLL 985
Cdd:PRK11173   82 G----RDN-----EVDKILgleigaddyITKPFNPRELTIRARNLL 118
ompR PRK09468
osmolarity response regulator; Provisional
875-981 1.82e-05

osmolarity response regulator; Provisional


Pssm-ID: 181883 [Multi-domain]  Cd Length: 239  Bit Score: 47.28  E-value: 1.82e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129446385 875 EDDEHVRDMVRAALEELNLTVLTAADGDAGHRLLQSDaRIDLLLSDVGLPGMNGHALAQAARALRPALRIILMTGYADEr 954
Cdd:PRK09468   12 DDDMRLRALLERYLTEQGFQVRSAANAEQMDRLLTRE-SFHLMVLDLMLPGEDGLSICRRLRSQNNPTPIIMLTAKGEE- 89
                          90       100       110
                  ....*....|....*....|....*....|....
gi 2129446385 955 engwarQERDVSL-------IRKPFSPGELTARV 981
Cdd:PRK09468   90 ------VDRIVGLeigaddyLPKPFNPRELLARI 117
glnG PRK10923
nitrogen regulation protein NR(I); Provisional
875-990 2.11e-05

nitrogen regulation protein NR(I); Provisional


Pssm-ID: 182842 [Multi-domain]  Cd Length: 469  Bit Score: 48.33  E-value: 2.11e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129446385 875 EDDEHVRDMVRAALEELNLTVLTAADGDAGHRLLQSDARiDLLLSDVGLPGMNGHALAQAARALRPALRIILMTGYADER 954
Cdd:PRK10923   10 DDDSSIRWVLERALAGAGLTCTTFENGNEVLEALASKTP-DVLLSDIRMPGMDGLALLKQIKQRHPMLPVIIMTAHSDLD 88
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2129446385 955 ENGWARQERDVSLIRKPFSPGELTARVCRLLAASQD 990
Cdd:PRK10923   89 AAVSAYQQGAFDYLPKPFDIDEAVALVERAISHYQE 124
HATPase_FilI-like cd16921
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
734-844 2.41e-05

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


Pssm-ID: 340398 [Multi-domain]  Cd Length: 105  Bit Score: 44.24  E-value: 2.41e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129446385 734 LNLVINACDAMPAGGDLEIEVAHREldaaavqtnpcaEAGEFVeVCVSDMGCGMAPDVLARVFEPF--FTTKPMGQGTGL 811
Cdd:cd16921     6 TNLLGNAIKFRRPRRPPRIEVGAED------------VGEEWT-FYVRDNGIGIDPEYAEKVFGIFqrLHSREEYEGTGV 72
                          90       100       110
                  ....*....|....*....|....*....|...
gi 2129446385 812 GLSMIYGFAQQAGGMVTIASVQAEGTAVRLFLP 844
Cdd:cd16921    73 GLAIVRKIIERHGGRIWLESEPGEGTTFYFTLP 105
REC_NtrC cd19919
phosphoacceptor receiver (REC) domain of DNA-binding transcriptional regulator NtrC; ...
875-952 3.67e-05

phosphoacceptor receiver (REC) domain of DNA-binding transcriptional regulator NtrC; DNA-binding transcriptional regulator NtrC is also called nitrogen regulation protein NR(I) or nitrogen regulator I (NRI). It contains an N-terminal receiver (REC) domain, followed by a sigma-54 interaction domain, and a C-terminal helix-turn-helix DNA-binding domain. It is part of the two-component regulatory system NtrB/NtrC, which controls expression of the nitrogen-regulated (ntr) genes in response to nitrogen limitation. DNA-binding response regulator NtrC is phosphorylated by NtrB; phosphorylation of the N-terminal REC domain activates the central sigma-54 interaction domain and leads to the transcriptional activation from promoters that require sigma(54)-containing RNA polymerase. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381146 [Multi-domain]  Cd Length: 116  Bit Score: 43.80  E-value: 3.67e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2129446385 875 EDDEHVRDMVRAALEELNLTVLTAADGDAGHRLLQSDaRIDLLLSDVGLPGMNGHALAQAARALRPALRIILMTGYAD 952
Cdd:cd19919     7 DDDSSIRWVLERALAGAGLTVTSFENAQEALAALASS-QPDVLISDIRMPGMDGLALLAQIKQRHPDLPVIIMTAHSD 83
PAS_4 pfam08448
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
489-595 3.86e-05

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


Pssm-ID: 312075 [Multi-domain]  Cd Length: 110  Bit Score: 43.94  E-value: 3.86e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129446385 489 WRLSPELLAVADHGGRLVSVNPAVRAILGWSPEQFLAMGLDEgVHPEDLASMQATLEAEPAEGMQPVRHLESRLLhkDGS 568
Cdd:pfam08448   1 LDSLPDALAVLDPDGRVRYANAAAAELFGLPPEELLGKTLAE-LLPPEDAARLERALRRALEGEEPIDFLEELLL--NGE 77
                          90       100       110
                  ....*....|....*....|....*....|...
gi 2129446385 569 YHWITWSLSR---AEGN---VYLAGRDDTDLKA 595
Cdd:pfam08448  78 ERHYELRLTPlrdPDGEvigVLVISRDITERRR 110
envZ PRK09467
osmolarity sensor protein; Provisional
686-844 6.40e-05

osmolarity sensor protein; Provisional


Pssm-ID: 236531 [Multi-domain]  Cd Length: 435  Bit Score: 46.44  E-value: 6.40e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129446385 686 QVFDPGDILRSMDELFRRYTGEQVRLTLKLPAQSWRVRCDMNQFENAVLNLVINAcdAMPAGGDLEIEvAHREldaaavq 765
Cdd:PRK09467  289 MPMEMADLNALLGEVIAAESGYEREIETALQPGPIEVPMNPIAIKRALANLVVNA--ARYGNGWIKVS-SGTE------- 358
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129446385 766 tnpcaeaGEFVEVCVSDMGCGMAPDVLARVFEPFFT--TKPMGQGTGLGLSMIYGFAQQAGGMVTIASVQAEGTAVRLFL 843
Cdd:PRK09467  359 -------GKRAWFQVEDDGPGIPPEQLKHLFQPFTRgdSARGSSGTGLGLAIVKRIVDQHNGKVELGNSEEGGLSARAWL 431

                  .
gi 2129446385 844 P 844
Cdd:PRK09467  432 P 432
PRK09303 PRK09303
histidine kinase;
599-814 7.51e-05

histidine kinase;


Pssm-ID: 236462 [Multi-domain]  Cd Length: 380  Bit Score: 46.10  E-value: 7.51e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129446385 599 VLRQTEDALRQsqKLEAVGRLTGGIAHDFNNMLQGISGALYLID----RKLRRSKPEEVGKYVRTAQESTDRAARLTQRL 674
Cdd:PRK09303  136 VLRQENETLLE--QLKFKDRVLAMLAHDLRTPLTAASLALETLElgqiDEDTELKPALIEQLQDQARRQLEEIERLITDL 213
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129446385 675 LTFSRQQA----IDPQVFDPGDI-LRSMDELFRRYTGEQVRLTLKLPAQSWRVRCDMNQFENAVLNLVINACDAMPAGGD 749
Cdd:PRK09303  214 LEVGRTRWealrFNPQKLDLGSLcQEVILELEKRWLAKSLEIQTDIPSDLPSVYADQERIRQVLLNLLDNAIKYTPEGGT 293
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2129446385 750 LEIEVAHReldaaavqTNpcaeagEFVEVCVSDMGCGMAPDVLARVFEPFFTTKPMGQ--GTGLGLS 814
Cdd:PRK09303  294 ITLSMLHR--------TT------QKVQVSICDTGPGIPEEEQERIFEDRVRLPRDEGteGYGIGLS 346
REC_OmpR_PrrA-like cd17627
phosphoacceptor receiver (REC) domain of PrrA-like OmpR family response regulators; The ...
875-985 7.67e-05

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


Pssm-ID: 381142 [Multi-domain]  Cd Length: 116  Bit Score: 43.14  E-value: 7.67e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129446385 875 EDDEHVRDMVRAALEELNLTVLTAADGDAGHRLLQSDaRIDLLLSDVGLPGMNGHALAQAARALRPALRIILMTGY--AD 952
Cdd:cd17627     5 DDDRAVRESLRRSLRFEGYEVETAVDGAEALRVISGN-RPDAVVLDVMMPRLDGLEVCRRLRAAGNDLPILVLTARdsVS 83
                          90       100       110
                  ....*....|....*....|....*....|...
gi 2129446385 953 ERENGWARQERDvsLIRKPFSPGELTARVCRLL 985
Cdd:cd17627    84 DRVAGLDAGADD--YLVKPFALEELLARVRALL 114
HATPase_RstB-like cd16939
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
730-845 8.14e-05

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Salmonella typhimurium RstB; This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component sensor histidine kinase (HKs) such as Salmonella typhimurium RstB HK of the RstA-RstB two-component regulatory system (TCS), which regulates expression of the constituents participating in pyrimidine metabolism and iron acquisition, and may be required for regulation of Salmonella motility and invasion. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA), and a HAMP sensor domain.


Pssm-ID: 340416 [Multi-domain]  Cd Length: 104  Bit Score: 42.80  E-value: 8.14e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129446385 730 ENAVLNLVINAcdampaggdleIEVAHRELDAAAVQTnpcaeaGEFVEVCVSDMGCGMAPDVLARVFEPFFTTKPMGQ-- 807
Cdd:cd16939     2 ARALDNLLRNA-----------LRYAHRTVRIALLVS------GGRLTLIVEDDGPGIPAAARERVFEPFVRLDPSRDra 64
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2129446385 808 --GTGLGLSMIYGFAQQAGGMVTIASVQAEGTAVRLFLPR 845
Cdd:cd16939    65 tgGFGLGLAIVHRVALWHGGHVECDDSELGGACFRLTWPR 104
REC_hyHK_CKI1_RcsC-like cd17546
phosphoacceptor receiver (REC) domain of hybrid sensor histidine kinases/response regulators ...
875-977 8.75e-05

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: 42.84  E-value: 8.75e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129446385 875 EDDEHVRDMVRAALEELNLTVLTAADGDAGHRLLQSDaRIDLLLSDVGLPGMNGHALAQA---ARALRPALRIILMTGYA 951
Cdd:cd17546     5 DDNPVNRKVLKKLLEKLGYEVDVAENGQEALELLKEE-PFDLVLMDLQMPVMDGLEATRRireLEGGGRRTPIIALTANA 83
                          90       100
                  ....*....|....*....|....*....
gi 2129446385 952 DEREngwARQERDV---SLIRKPFSPGEL 977
Cdd:cd17546    84 LEED---REKCLEAgmdDYLSKPVKLDQL 109
HATPase_SpaK_NisK-like cd16975
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
725-841 9.87e-05

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Bacillus subtilis SpaK and Lactococcus lactis NisK; This family includes histidine kinase-like ATPase (HATPase) domain of two-component sensor histidine kinases similar to Bacillus subtilis SpaK and Lactococcus lactis NisK. SpaK is the histidine kinase (HK) of the SpaK-SpaR two-component regulatory system (TCS), which is involved in the regulation of the biosynthesis of lantibiotic subtilin. NisK is the HK of the NisK-NisR TCS, which is involved in the regulation of the biosynthesis of lantibiotic nisin. SpaK and NisK may function as membrane-associated protein kinases that phosphorylate SpaR and NisR, respectively, in response to environmental signals.


Pssm-ID: 340434 [Multi-domain]  Cd Length: 107  Bit Score: 42.45  E-value: 9.87e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129446385 725 DMNQFENAVLNLVINACDAMPAGGDLEIEVAHREldaaavqtnpcaeagEFVEVCVSDMGCGMAPDVLARVFEPFFTTKP 804
Cdd:cd16975     1 DTLLLSRALINIISNACQYAPEGGTVSISIYDEE---------------EYLYFEIWDNGHGFSEQDLKKALELFYRDDT 65
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2129446385 805 M---GQGTGLGLSMIYGFAQQAGGMVTIASVQAEGTAVRL 841
Cdd:cd16975    66 SrrsGGHYGMGLYIAKNLVEKHGGSLIIENSQKGGAEVTV 105
REC_CheV-like cd19924
phosphoacceptor receiver (REC) domain of chemotaxis protein CheV and similar proteins; This ...
875-929 1.27e-04

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: 42.37  E-value: 1.27e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2129446385 875 EDDEHVRDMVRAALEELNLTVLTAADGDAGHRLLQSDAR--------IDLLLSDVGLPGMNGH 929
Cdd:cd19924     5 DDSPTARKQLRDLLKNLGFEIAEAVDGEEALNKLENLAKegndlskeLDLIITDIEMPKMDGY 67
PRK09959 PRK09959
acid-sensing system histidine kinase EvgS;
472-957 1.67e-04

acid-sensing system histidine kinase EvgS;


Pssm-ID: 182169 [Multi-domain]  Cd Length: 1197  Bit Score: 45.88  E-value: 1.67e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129446385  472 RVLEQRVEHAIAERDRIWRLSPELLAVADHGGRLVSVNPAVRAILGWSPEQFLAMGLDEGVHP-EDLASMQATLEAEPAE 550
Cdd:PRK09959   565 KVIQGDLENQISFRKALSDSLPNPTYVVNWQGNVISHNSAFEHYFTADYYKNAMLPLENSDSPfKDVFSNAHEVTAETKE 644
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129446385  551 GmqpvRHLESRLLHKDGSY------HWITW-SLSRAEGNVYLAGRDDT----DLKAQAEVLRQtedalRQSQKLEAVGRL 619
Cdd:PRK09959   645 N----RTIYTQVFEIDNGIekrcinHWHTLcNLPASDHAVYICGWQDItetrDLIHALEVERN-----KAINATVAKSQF 715
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129446385  620 TGGIAHDFNNMLQGISGALYLIDRK--LRRSKPEEVGKYVRTAQESTDRAARLTQRLLTFSRQQAIDPQVFDPGDILRSM 697
Cdd:PRK09959   716 LATMSHEIRTPISSIMGFLELLSGSglSKEQRVEAISLAYATGQSLLGLIGEILDVDKIESGNYQLQPQWVDIPTLVQNT 795
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129446385  698 DELFRRYTGEQvrlTLKLPAQS-----WRVRCDMNQFENAVLNLVINACDAMPAGG-DLEIEVAHRElDAAAVqtnpcae 771
Cdd:PRK09959   796 CHSFGAIAASK---SIALSCSStfpdhYLVKIDPQAFKQVLSNLLSNALKFTTEGAvKITTSLGHID-DNHAV------- 864
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129446385  772 agefVEVCVSDMGCGMAPDVLARVFEPFFTTKPMGQ--GTGLGLSMIYGFAQQAGGMVTIASVQAEGTAVRLFLPRHVGE 849
Cdd:PRK09959   865 ----IKMTIMDSGSGLSQEEQQQLFKRYSQTSAGRQqtGSGLGLMICKELIKNMQGDLSLESHPGIGTTFTITIPVEISQ 940
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129446385  850 PVAlPAPESSEPPAAPAHAAVVALVEDDEHVRDMVRAALEELNLTVLTAADG-DAGHRLlqSDARIDLLLSDVGLPGMNG 928
Cdd:PRK09959   941 QVA-TVEAKAEQPITLPEKLSILIADDHPTNRLLLKRQLNLLGYDVDEATDGvQALHKV--SMQHYDLLITDVNMPNMDG 1017
                          490       500       510
                   ....*....|....*....|....*....|.
gi 2129446385  929 HALAQAARALRPALRIILMT--GYADERENG 957
Cdd:PRK09959  1018 FELTRKLREQNSSLPIWGLTanAQANEREKG 1048
REC_OmpR_KdpE-like cd17620
phosphoacceptor receiver (REC) domain of KdpE-like OmpR family response regulators; KdpE is a ...
875-929 1.67e-04

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: 41.77  E-value: 1.67e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2129446385 875 EDDEHVRDMVRAALEELNLTVLTAADGDAGHRLLQSDaRIDLLLSDVGLPGMNGH 929
Cdd:cd17620     5 EDEPQIRRFLRTALEAHGYRVFEAETGQEGLLEAATR-KPDLIILDLGLPDMDGL 58
PRK09776 PRK09776
putative diguanylate cyclase; Provisional
471-602 1.74e-04

putative diguanylate cyclase; Provisional


Pssm-ID: 182070 [Multi-domain]  Cd Length: 1092  Bit Score: 45.82  E-value: 1.74e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129446385  471 ARVLEQ-RVE-HAIAERDRIWRLSPEL----LAVADHGGRLVSVNPAVRAILGWSPEQFLAMGLDEGVHPEDLASMQATL 544
Cdd:PRK09776   265 TMVMYAfRAErKHISESETRFRNAMEYsaigMALVGTEGQWLQVNKALCQFLGYSQEELRGLTFQQLTWPEDLNKDLQQV 344
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2129446385  545 EaEPAEGMQPVRHLESRLLHKDGSYHW--ITWSLSRAEGNV---YLAGRDD-TDLKAQAEVLRQ 602
Cdd:PRK09776   345 E-KLLSGEINSYSMEKRYYRRDGEVVWalLAVSLVRDTDGTplyFIAQIEDiNELKRTEQVNER 407
REC_RegA-like cd17563
phosphoacceptor receiver (REC) domain of photosynthetic apparatus regulatory protein RegA; ...
875-951 1.81e-04

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


Pssm-ID: 381111 [Multi-domain]  Cd Length: 112  Bit Score: 42.04  E-value: 1.81e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2129446385 875 EDDEHVRDMVRAALEELNLTVLTAADGDAGHRLLQSDaRIDLLLSDVGLPGMNGHALAQAARALRPALRIILMTGYA 951
Cdd:cd17563     7 DDDEVFAERLARALERRGFEVETAHSVEEALALAREE-KPDYAVLDLRLGGDSGLDLIPPLRALQPDARIVVLTGYA 82
REC_Ycf29 cd19927
phosphoacceptor receiver (REC) domain of probable transcriptional regulator Ycf29; Ycf29 is a ...
875-928 2.01e-04

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: 41.59  E-value: 2.01e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2129446385 875 EDDEHVRDMVRAALEELNLTVLTAADGDAGHRLLqSDARIDLLLSDVGLPGMNG 928
Cdd:cd19927     5 DDDPGIRLAVKDYLEDQGFTVIAASNGLEALDLL-NQYIPDLIISDIIMPGVDG 57
REC_NtrX-like cd17550
phosphoacceptor receiver (REC) domain of nitrogen assimilation regulatory protein NtrX and ...
876-951 3.22e-04

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: 41.33  E-value: 3.22e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2129446385 876 DDEHVRDMVRAALEELNLTVLTAADGDAGHRLLQSDaRIDLLLSDVGLPGMNGHALAQAARALRPALRIILMTGYA 951
Cdd:cd17550     6 DEEDIRESLSGILEDEGYEVDTAADGEEALKLIKER-RPDLVLLDIWLPDMDGLELLKEIKEKYPDLPVIMISGHG 80
REC_HupR cd17596
phosphoacceptor receiver (REC) domain of hydrogen uptake protein regulator (HupR); Members of ...
876-952 3.97e-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: 41.58  E-value: 3.97e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2129446385 876 DDE-HVRDMVRAALEElNLTVLTAADGDAGHRLLQsDARIDLLLSDVGLPGMNGHALAQAARALRPALRIILMTGYAD 952
Cdd:cd17596     7 DDEvRSLEALRRTLEE-DFDVLTAASAEEALAILE-EEWVQVILCDQRMPGTTGVEFLKEVRERWPEVVRIIISGYTD 82
PAS COG2202
PAS domain [Signal transduction mechanisms];
178-313 3.98e-04

PAS domain [Signal transduction mechanisms];


Pssm-ID: 441804 [Multi-domain]  Cd Length: 258  Bit Score: 43.47  E-value: 3.98e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129446385 178 ERHLTEQALRNSSVRWRGMFERMQEGFFLAEAqrdstgsvdDFTLLEINPAFETQSGLAVGQTLG-PMLRVMSPAAADSI 256
Cdd:COG2202   124 ERKRAEEALRESEERLRLLVENAPDGIFVLDL---------DGRILYVNPAAEELLGYSPEELLGkSLLDLLHPEDRERL 194
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2129446385 257 MRIFVGVIEsGEPAQFEVEAPGPPQACYEC--------RAGKEGHDRVAALFLNVTARKLAESEL 313
Cdd:COG2202   195 LELLRRLLE-GGRESYELELRLKDGDGRWVwveasavpLRDGGEVIGVLGIVRDITERKRAEEAL 258
PRK11359 PRK11359
cyclic-di-GMP phosphodiesterase; Provisional
106-184 4.53e-04

cyclic-di-GMP phosphodiesterase; Provisional


Pssm-ID: 183097 [Multi-domain]  Cd Length: 799  Bit Score: 44.38  E-value: 4.53e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129446385 106 VYVEDLTVHPNWP-PWreAATQH----GLRACWSTPIKATDGRTLGVFSNYYRQPRLPTREdIEAIA-LVTRTAALAIER 179
Cdd:PRK11359  289 SHVSLFALRNGMPiHW--ASSSHgaeyQNAQSWSATIRQRDGAPAGTLQIKTSSGAETSAF-IERVAdISQHLAALALEQ 365

                  ....*
gi 2129446385 180 HLTEQ 184
Cdd:PRK11359  366 EKSRQ 370
REC_OmpR_BfmR-like cd19939
phosphoacceptor receiver (REC) domain of BfmR-like OmpR family response regulators; ...
875-985 5.61e-04

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: 40.43  E-value: 5.61e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129446385 875 EDDEHVRDMVRAALEELNLTVLTAADGDAGHRLLqSDARIDLLLSDVGLPGMNGhALAQAARALRPALRIILMTGYADER 954
Cdd:cd19939     6 EDELELARLTRDYLIKAGLEVSVFTDGQRAVRRI-IDEQPSLVVLDIMLPGMDG-LTVCREVREHSHVPILMLTARTEEM 83
                          90       100       110
                  ....*....|....*....|....*....|.
gi 2129446385 955 ENGWARQERDVSLIRKPFSPGELTARVCRLL 985
Cdd:cd19939    84 DRVLGLEMGADDYLCKPFSPRELLARVRALL 114
REC_OmpR_BaeR-like cd19938
phosphoacceptor receiver (REC) domain of BaeR-like OmpR family response regulators; BaeR is ...
875-985 5.86e-04

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: 40.44  E-value: 5.86e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129446385 875 EDDEHVRDMVRAALEELNLTVLTAADGDAGHRLLQsDARIDLLLSDVGLPGMNGhALAQAARALRPALRIILMTGYADER 954
Cdd:cd19938     6 EDEPKLAQLLIDYLRAAGYAPTLLAHGDQVLPYVR-HTPPDLILLDLMLPGTDG-LTLCREIRRFSDVPIIMVTARVEEI 83
                          90       100       110
                  ....*....|....*....|....*....|.
gi 2129446385 955 ENGWARQERDVSLIRKPFSPGELTARVCRLL 985
Cdd:cd19938    84 DRLLGLELGADDYICKPYSPREVVARVKAIL 114
REC_OmpR_PmrA-like cd17624
phosphoacceptor receiver (REC) domain of PmrA-like OmpR family response regulators; This ...
875-981 6.27e-04

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: 40.55  E-value: 6.27e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129446385 875 EDDEHVRDMVRAALEELNLTVLTAADGDAGHRLLQSdARIDLLLSDVGLPGMNGHALAQAARALRPALRIILMTgyader 954
Cdd:cd17624     5 EDDALLGDGLKTGLRKAGYAVDWVRTGAEAEAALAS-GPYDLVILDLGLPDGDGLDLLRRWRRQGQSLPVLILT------ 77
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2129446385 955 engwAR---QER--------DVSLIrKPFSPGELTARV 981
Cdd:cd17624    78 ----ARdgvDDRvagldagaDDYLV-KPFALEELLARL 110
PAS_9 pfam13426
PAS domain; This domain is found in many signalling proteins in which it functions as a sensor ...
503-572 6.53e-04

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


Pssm-ID: 463873 [Multi-domain]  Cd Length: 93  Bit Score: 39.75  E-value: 6.53e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2129446385 503 GRLVSVNPAVRAILGWSPEQFLAMGLDEGV-HPEDLASMQATLEAepaegMQPVRHLESRLLHKDGSYHWI 572
Cdd:pfam13426   2 GRIIYVNDAALRLLGYTREELLGKSITDLFaEPEDSERLREALRE-----GKAVREFEVVLYRKDGEPFPV 67
REC_D1_PleD-like cd17538
first (D1) phosphoacceptor receiver (REC) domain of response regulator PleD and similar ...
876-929 7.17e-04

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: 39.79  E-value: 7.17e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2129446385 876 DDEHV-RDMVRAALEELNLTVLTAADGDAGHRLLQSDaRIDLLLSDVGLPGMNGH 929
Cdd:cd17538     6 DDEPAnRELLEALLSAEGYEVLTADSGQEALALAEEE-LPDLILLDVMMPGMDGF 59
HATPase_CpxA-like cd16949
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
773-844 7.73e-04

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Escherichia coli CpxA; This family includes the histidine kinase-like ATPase (HATPase) domains of two-component sensor histidine kinase (HKs) similar to Escherichia coli CpxA, HK of the CpxA-CpxR two-component regulatory system (TCS) which may function in acid stress and in cell wall stability. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA) and a HAMP sensor domain; some also contain a CpxA family periplasmic domain.


Pssm-ID: 340425 [Multi-domain]  Cd Length: 104  Bit Score: 40.00  E-value: 7.73e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2129446385 773 GEFVEVCVSDMGCGMAPDVLARVFEPFFTTKPMGQ----GTGLGLSMIYGFAQQAGGMVTIASVQAEGTAVRLFLP 844
Cdd:cd16949    28 GDQWTITITDDGPGVPEDQLEQIFLPFYRVDSARDresgGTGLGLAIAERAIEQHGGKIKASNRKPGGLRVRIWLP 103
HATPase_BaeS-like cd16946
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
725-844 8.47e-04

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


Pssm-ID: 340422 [Multi-domain]  Cd Length: 109  Bit Score: 39.75  E-value: 8.47e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129446385 725 DMNQFENAVLNLVINACDAMPAGGDLEIEvahreldaaavqtnpCAEAGEFVEVCVSDMGCGMAPDVLARVFEPFF---- 800
Cdd:cd16946     1 DRDRLQQLFVNLLENSLRYTDTGGKLRIR---------------AAQTPQEVRLDVEDSAPGVSDDQLARLFERFYrves 65
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 2129446385 801 -TTKPMGqGTGLGLSMIYGFAQQAGGMVTIASVQAEGTAVRLFLP 844
Cdd:cd16946    66 sRNRASG-GSGLGLAICHNIALAHGGTISAEHSPLGGLRLVLTLP 109
LytT COG3279
DNA-binding response regulator, LytR/AlgR family [Transcription, Signal transduction ...
875-986 9.46e-04

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


Pssm-ID: 442510 [Multi-domain]  Cd Length: 235  Bit Score: 42.11  E-value: 9.46e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129446385 875 EDDEHVRDMVRAALEEL-NLTVL-TAADGDAGHRLLQSDaRIDLLLSDVGLPGMNGHALAQAARALRPALRIILMTGYAD 952
Cdd:COG3279     8 DDEPLARERLERLLEKYpDLEVVgEASNGEEALELLEEH-KPDLVFLDIQMPGLDGFELARQLRELDPPPPIIFTTAYDE 86
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2129446385 953 erengWARQERDVSLIR---KPFSPGELTARVCRLLA 986
Cdd:COG3279    87 -----YALEAFEVNAVDyllKPIDEERLAKALEKAKE 118
REC_OmpR_CpxR cd17623
phosphoacceptor receiver (REC) domain of CpxR-like OmpR family response regulators; CpxR is ...
875-981 9.53e-04

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


Pssm-ID: 381138 [Multi-domain]  Cd Length: 115  Bit Score: 39.98  E-value: 9.53e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129446385 875 EDDEHVRDMVRAALEELNLTVLTAADGDAGHRLLQSDArIDLLLSDVGLPGMNGhALAQAARALRPALRIILMTGYADEr 954
Cdd:cd17623     5 DDDRELTELLTEYLEMEGFNVRAAHDGEQGLAALLEGS-PDLVVLDVMLPKMNG-LDVLKELRKTSQVPVLMLTARGDD- 81
                          90       100       110
                  ....*....|....*....|....*....|....
gi 2129446385 955 engwarQERDVSL-------IRKPFSPGELTARV 981
Cdd:cd17623    82 ------IDRILGLelgaddyLPKPFNPRELVARI 109
CitB COG2197
DNA-binding response regulator, NarL/FixJ family, contains REC and HTH domains [Signal ...
875-928 9.62e-04

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: 40.26  E-value: 9.62e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2129446385 875 EDDEHVRDMVRAALE-ELNLTVL-TAADGDAGHRLLQsDARIDLLLSDVGLPGMNG 928
Cdd:COG2197     8 DDHPLVREGLRALLEaEPDIEVVgEAADGEEALELLE-ELRPDVVLLDIRMPGMDG 62
GAF smart00065
Domain present in phytochromes and cGMP-specific phosphodiesterases; Mutations within these ...
52-187 9.64e-04

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


Pssm-ID: 214500 [Multi-domain]  Cd Length: 149  Bit Score: 40.83  E-value: 9.64e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129446385   52 VELLTSIAFVDDSGMRLRHVATPSLPAAYVQATD-----GAAIGPGVASWGAAAFLGTPVYVEDLTVHPNWppWREAATQ 126
Cdd:smart00065  10 LEELRQLLGADRVLIYLVDENDRGELVLVAADGLtlptlGIRFPLDEGLAGRVAETGRPLNIPDVEADPLF--AEDLLGR 87
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2129446385  127 H-GLRACWSTPIKAtDGRTLGVFSNYYR-QPRLPTREDIEAIALVTRTAALAIERHLTEQALR 187
Cdd:smart00065  88 YqGVRSFLAVPLVA-DGELVGVLALHNKkSPRPFTEEDEELLQALANQLAIALANAQLYEELR 149
REC_OmpR_VirG cd17594
phosphoacceptor receiver (REC) domain of VirG-like OmpR family response regulators; VirG is ...
875-981 1.09e-03

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: 39.74  E-value: 1.09e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129446385 875 EDDEHVRDMVRAALEELNLTVLTAADGDAGHRLLQSDaRIDLLLSDVGLPGMNGhALAQAARALRPALRIILMTGYADER 954
Cdd:cd17594     6 DDDAAMRHLLILYLRERGFDVTAAADGAEEARLMLHR-RVDLVLLDLRLGQESG-LDLLRTIRARSDVPIIIISGDRRDE 83
                          90       100       110
                  ....*....|....*....|....*....|....
gi 2129446385 955 EngwarqERDVSL-------IRKPFSPGELTARV 981
Cdd:cd17594    84 I------DRVVGLelgaddyLAKPFGLRELLARV 111
REC_OmpR_EcPhoP-like cd19934
phosphoacceptor receiver (REC) domain of EcPhoP-like OmpR family response regulators; ...
875-985 2.06e-03

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: 38.80  E-value: 2.06e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129446385 875 EDDEHVRDMVRAALEELNLTVLTAADGDAGHRLLQSDArIDLLLSDVGLPGMNGHALAQAARALRPALRIILMTGyadeR 954
Cdd:cd19934     5 EDDALLAAQLKEQLSDAGYVVDVAEDGEEALFQGEEEP-YDLVVLDLGLPGMDGLSVLRRWRSEGRATPVLILTA----R 79
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2129446385 955 ENgWarQERDVSL-------IRKPFSPGELTARVCRLL 985
Cdd:cd19934    80 DS-W--QDKVEGLdagaddyLTKPFHIEELLARLRALI 114
HATPase_BvrS-ChvG-like cd16953
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
770-828 2.13e-03

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


Pssm-ID: 340429 [Multi-domain]  Cd Length: 110  Bit Score: 38.71  E-value: 2.13e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2129446385 770 AEAGEFVEVCVSDMGCGMAPDVLARVFEPFFTTKP----MGQGTGLGLSMIYGFAQQAGGMVT 828
Cdd:cd16953    28 MPTGKMVTISVEDEGPGIPQEKLESIFDRFYTERPaneaFGQHSGLGLSISRQIIEAHGGISV 90
REC_OmpR_CusR-like cd19935
phosphoacceptor receiver (REC) domain of CusR-like OmpR family response regulators; ...
875-928 2.35e-03

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: 38.19  E-value: 2.35e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2129446385 875 EDDEHVRDMVRAALEELNLTVLTAADGDAGHRLLQSDArIDLLLSDVGLPGMNG 928
Cdd:cd19935     5 EDEKKLAEYLKKGLTEEGYAVDVAYDGEDGLHLALTNE-YDLIILDVMLPGLDG 57
PRK11091 PRK11091
aerobic respiration control sensor protein ArcB; Provisional
770-928 2.43e-03

aerobic respiration control sensor protein ArcB; Provisional


Pssm-ID: 236842 [Multi-domain]  Cd Length: 779  Bit Score: 41.85  E-value: 2.43e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129446385 770 AEAGEFVEVCVSDMGCGMAPDVLARVFEPFFTTK--PMGQ---GTGLGLSMIYGFAQQAGGMVTIASVQAEGTAVRLFLp 844
Cdd:PRK11091  425 YEEGDMLTFEVEDSGIGIPEDELDKIFAMYYQVKdsHGGKpatGTGIGLAVSKRLAQAMGGDITVTSEEGKGSCFTLTI- 503
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129446385 845 rhvgePVALPAPESSEPPAAPAHAAVVAL---VEDDEHVRDMVRAALEELNLTVLTAADGDAGHRLLQSDaRIDLLLSDV 921
Cdd:PRK11091  504 -----HAPAVAEEVEDAFDEDDMPLPALNillVEDIELNVIVARSVLEKLGNSVDVAMTGKEALEMFDPD-EYDLVLLDI 577

                  ....*..
gi 2129446385 922 GLPGMNG 928
Cdd:PRK11091  578 QLPDMTG 584
PRK11083 PRK11083
DNA-binding response regulator CreB; Provisional
908-981 4.11e-03

DNA-binding response regulator CreB; Provisional


Pssm-ID: 236838 [Multi-domain]  Cd Length: 228  Bit Score: 39.95  E-value: 4.11e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129446385 908 LQSDARIDLLLSDVGLPGMNGHALAQAARALRPALRIILMTGYADErengwarQERDVSL-------IRKPFSPGELTAR 980
Cdd:PRK11083   42 KLRQQPPDLVILDVGLPDISGFELCRQLLAFHPALPVIFLTARSDE-------VDRLVGLeigaddyVAKPFSPREVAAR 114

                  .
gi 2129446385 981 V 981
Cdd:PRK11083  115 V 115
REC_CheY cd17542
phosphoacceptor receiver (REC) domain of chemotaxis protein CheY; The chemotaxis response ...
875-985 4.27e-03

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: 38.03  E-value: 4.27e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129446385 875 EDDEHVRDMVRAALEELNLTVL-TAADGDAGHRLLQsDARIDLLLSDVGLPGMNGHALAQAARALRPALRIILMTGYADE 953
Cdd:cd17542     7 DDAAFMRMMLKDILTKAGYEVVgEAANGEEAVEKYK-ELKPDLVTMDITMPEMDGIEALKEIKKIDPNAKVIMCSAMGQE 85
                          90       100       110
                  ....*....|....*....|....*....|..
gi 2129446385 954 RENGWARQERDVSLIRKPFSPGELTARVCRLL 985
Cdd:cd17542    86 EMVKEAIKAGAKDFIVKPFQPERVLEAVEKVL 117
orf27 CHL00148
Ycf27; Reviewed
876-985 4.83e-03

Ycf27; Reviewed


Pssm-ID: 214376 [Multi-domain]  Cd Length: 240  Bit Score: 39.70  E-value: 4.83e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129446385 876 DDE-HVRDMVRAALEELNLTVLTAADGDAGHRLLQSDaRIDLLLSDVGLPGMNGHALAQAaralrpaLR------IILMT 948
Cdd:CHL00148   13 DDEaYIRKILETRLSIIGYEVITASDGEEALKLFRKE-QPDLVILDVMMPKLDGYGVCQE-------IRkesdvpIIMLT 84
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2129446385 949 GYAD--ERENGWARQERDvsLIRKPFSPGELTARVCRLL 985
Cdd:CHL00148   85 ALGDvsDRITGLELGADD--YVVKPFSPKELEARIRSVL 121
HATPase_PDK-like cd16929
Histidine kinase-like ATPase domain of pyruvate dehydrogenase kinase, branched-chain ...
774-844 4.98e-03

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


Pssm-ID: 340406 [Multi-domain]  Cd Length: 169  Bit Score: 38.86  E-value: 4.98e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129446385 774 EFVEVCVSDMGCGMAPDVLARVFEPFFTTK------------------PMGqGTGLGLSMIYGFAQQAGGMVTIASVQAE 835
Cdd:cd16929    82 EDLTIKISDRGGGIPREDLARLFSYMYSTApqpslddfsdlisgtqpsPLA-GFGYGLPMSRLYAEYFGGDLDLQSMEGY 160

                  ....*....
gi 2129446385 836 GTAVRLFLP 844
Cdd:cd16929   161 GTDVYIYLK 169
ComP COG4585
Signal transduction histidine kinase ComP [Signal transduction mechanisms];
625-846 5.05e-03

Signal transduction histidine kinase ComP [Signal transduction mechanisms];


Pssm-ID: 443642 [Multi-domain]  Cd Length: 252  Bit Score: 39.99  E-value: 5.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129446385 625 HDfnNMLQGISGALYLID--RKLRRSKPEEVGKYVRTAQESTDRAARLTQRLLTfsrqqAIDPQVFDPGDILRSMDEL-- 700
Cdd:COG4585    62 HD--GVGQSLSAIKLQLEaaRRLLDADPEAAREELEEIRELAREALAELRRLVR-----GLRPPALDDLGLAAALEELae 134
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129446385 701 -FRRYTGEQVRLTLKLPAQSWRVRCDMNQFEnAVLNLVINAcdampaggdleieVAHRELDAAAVQtnpCAEAGEFVEVC 779
Cdd:COG4585   135 rLLRAAGIRVELDVDGDPDRLPPEVELALYR-IVQEALTNA-------------LKHAGATRVTVT---LEVDDGELTLT 197
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2129446385 780 VSDMGCGMAPDVLArvfepffttkpmgqGTGLGLSMIYGFAQQAGGMVTIASVQAEGTAVRLFLPRH 846
Cdd:COG4585   198 VRDDGVGFDPEAAP--------------GGGLGLRGMRERAEALGGTLTIGSAPGGGTRVRATLPLA 250
PRK10161 PRK10161
phosphate response regulator transcription factor PhoB;
875-981 5.65e-03

phosphate response regulator transcription factor PhoB;


Pssm-ID: 182277 [Multi-domain]  Cd Length: 229  Bit Score: 39.70  E-value: 5.65e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129446385 875 EDDEHVRDMVRAALEELNLTVLTAADGDAGHRLLqSDARIDLLLSDVGLPGMNG-----HALAQAARALRPalrIILMTG 949
Cdd:PRK10161    9 EDEAPIREMVCFVLEQNGFQPVEAEDYDSAVNQL-NEPWPDLILLDWMLPGGSGiqfikHLKRESMTRDIP---VVMLTA 84
                          90       100       110
                  ....*....|....*....|....*....|..
gi 2129446385 950 YADERENGWARQERDVSLIRKPFSPGELTARV 981
Cdd:PRK10161   85 RGEEEDRVRGLETGADDYITKPFSPKELVARI 116
REC_PA4781-like cd19920
phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase PA4781 and similar ...
888-928 5.79e-03

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: 37.49  E-value: 5.79e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 2129446385 888 LEELNLTVLTAADGDAGHRLLQSdARIDLLLSDVGLPGMNG 928
Cdd:cd19920    18 LRAAGYRVLVATDGQQALQRAQA-EPPDLILLDVMMPGMDG 57
REC_OmpR_MtrA-like cd17626
phosphoacceptor receiver (REC) domain of MtrA-like OmpR family response regulators; MtrA is ...
875-981 5.94e-03

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


Pssm-ID: 381141 [Multi-domain]  Cd Length: 115  Bit Score: 37.83  E-value: 5.94e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129446385 875 EDDEHVRDMVRAALEELNLTVLTAADGDAGHRLLQSdARIDLLLSDVGLPGMNGhALAQAARALRPALRIILMTGYADER 954
Cdd:cd17626     7 DDDAALAEMIGIVLRGEGFDPAFCGDGTQALAAFRE-VRPDLVLLDLMLPGIDG-IEVCRQIRAESGVPIVMLTAKSDTV 84
                          90       100
                  ....*....|....*....|....*..
gi 2129446385 955 ENGWARQERDVSLIRKPFSPGELTARV 981
Cdd:cd17626    85 DVVLGLESGADDYVAKPFKPKELVARI 111
REC_typeB_ARR-like cd17584
phosphoacceptor receiver (REC) domain of type B Arabidopsis response regulators (ARRs) and ...
876-979 6.01e-03

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: 37.61  E-value: 6.01e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129446385 876 DDEHVRDMVRAALEELNLTVLTAAD-GDAGHRLLQSDARIDLLLSDVGLPGMNGHaLAQAARALRPALRIILMTgyADER 954
Cdd:cd17584     6 DDPTCLAILKRMLLRCGYQVTTCTDaEEALSMLRENKDEFDLVITDVHMPDMDGF-EFLELIRLEMDLPVIMMS--ADGS 82
                          90       100
                  ....*....|....*....|....*..
gi 2129446385 955 ENGWAR--QERDVSLIRKPFSPGELTA 979
Cdd:cd17584    83 TSTVMKglAHGACDYLLKPVSIEDLKN 109
PRK10955 PRK10955
envelope stress response regulator transcription factor CpxR;
875-988 6.85e-03

envelope stress response regulator transcription factor CpxR;


Pssm-ID: 182864 [Multi-domain]  Cd Length: 232  Bit Score: 39.40  E-value: 6.85e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129446385 875 EDDEHVRDMVRAALEELNLTVLTAADGDAGHRLLqsDARIDLLLSDVGLPGMNGhALAQAARALRPALRIILMTGYADER 954
Cdd:PRK10955    8 DDDRELTSLLKELLEMEGFNVIVAHDGEQALDLL--DDSIDLLLLDVMMPKKNG-IDTLKELRQTHQTPVIMLTARGSEL 84
                          90       100       110
                  ....*....|....*....|....*....|....
gi 2129446385 955 ENGWARQERDVSLIRKPFSPGELTARVCRLLAAS 988
Cdd:PRK10955   85 DRVLGLELGADDYLPKPFNDRELVARIRAILRRS 118
PRK11517 PRK11517
DNA-binding response regulator HprR;
875-981 7.99e-03

DNA-binding response regulator HprR;


Pssm-ID: 183172 [Multi-domain]  Cd Length: 223  Bit Score: 39.11  E-value: 7.99e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129446385 875 EDDEHVRDMVRAALEELNLTVLTAADGDAGHRL-LQSDarIDLLLSDVGLPGMNGHALAQAARALRPALRIILMTGYA-D 952
Cdd:PRK11517    7 EDNQRTQEWVTQGLSEAGYVIDAVSDGRDGLYLaLKDD--YALIILDIMLPGMDGWQILQTLRTAKQTPVICLTARDSvD 84
                          90       100
                  ....*....|....*....|....*....
gi 2129446385 953 ERENGWARQERDvsLIRKPFSPGELTARV 981
Cdd:PRK11517   85 DRVRGLDSGAND--YLVKPFSFSELLARV 111
PRK15369 PRK15369
two component system response regulator;
915-954 8.75e-03

two component system response regulator;


Pssm-ID: 185267 [Multi-domain]  Cd Length: 211  Bit Score: 38.91  E-value: 8.75e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 2129446385 915 DLLLSDVGLPGMNGHALAQAARALRPALRIILMTGYADER 954
Cdd:PRK15369   51 DIVILDLGLPGMNGLDVIPQLHQRWPAMNILVLTARQEEH 90
 
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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