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Conserved domains on  [gi|2651418669|ref|WP_326262544|]
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ATP-binding protein [Bacillus tropicus]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
BaeS COG0642
Signal transduction histidine kinase [Signal transduction mechanisms];
391-731 1.16e-74

Signal transduction histidine kinase [Signal transduction mechanisms];


:

Pssm-ID: 440407 [Multi-domain]  Cd Length: 328  Bit Score: 247.51  E-value: 1.16e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 391 ISDLHQDLIQQTVDNLGLTIHSIMGRMRIQTLLYESQAMTEELQVQSEELQTQAEELQMQAEELRTTNEQLESRTEEAEQ 470
Cdd:COG0642     5 LLLLVLLLLLLLLLLLALLLLLLLLLLLALLLLLALLLLLLLLLLLLLLLALALLALLLLLLLLLLLLLLLLLLLLLLLL 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 471 KTADLQVTKLELEEKASELLRSSKYKSEFLANMSHELRTPLNSILLLSEMLKENHDnhlsDDEIELATVIHSSGKDLLTL 550
Cdd:COG0642    85 LLLLLLLLLLLLLALLLLLEEANEAKSRFLANVSHELRTPLTAIRGYLELLLEELD----EEQREYLETILRSADRLLRL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 551 INDILDLSKVEAGKLDVIFEATNISDMAASMHQNFLHIAAQKNVEFTVEDSDTIPDLfYTDAKRIEQIIKNLLSNAFKFT 630
Cdd:COG0642   161 INDLLDLSRLEAGKLELEPEPVDLAELLEEVVELFRPLAEEKGIELELDLPDDLPTV-RGDPDRLRQVLLNLLSNAIKYT 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 631 EKGS-VSLHFdsietsnlshdmqSISKDWITISVKDTGIGIAKEQHQLIFEAFQQADGAtiRKYGGTGLGLSICKEFARL 709
Cdd:COG0642   240 PEGGtVTVSV-------------RREGDRVRISVEDTGPGIPPEDLERIFEPFFRTDPS--RRGGGTGLGLAIVKRIVEL 304
                         330       340
                  ....*....|....*....|..
gi 2651418669 710 LGGWITLESNVGEGSTFTVYIP 731
Cdd:COG0642   305 HGGTIEVESEPGKGTTFTVTLP 326
CheY COG0784
CheY-like REC (receiver) domain, includes chemotaxis protein CheY and sporulation regulator ...
776-894 4.23e-42

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: 149.62  E-value: 4.23e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 776 KTILIVDDDHRNIFALQNALKKHHANIITAQNGLECLEILKNNTnIDLILMDIMMPNMDGYETMEHIRMNLGLHEIPIIA 855
Cdd:COG0784     6 KRILVVDDNPDNRELLRRLLERLGYEVTTAEDGAEALELLRAGP-PDLILLDINMPGMDGLELLRRIRALPRLPDIPIIA 84
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2651418669 856 LTAKAMPNDKEKCLSAGASDYISKPLNLHQLYSVMSVWL 894
Cdd:COG0784    85 LTAYADEEDRERALEAGADDYLTKPVDPEELLEALRRLL 123
CHASE3 pfam05227
CHASE3 domain; CHASE3 is an extracellular sensory domain, which is present in various classes ...
46-172 1.46e-17

CHASE3 domain; CHASE3 is an extracellular sensory domain, which is present in various classes of transmembrane receptors that are parts of signal transduction pathways in bacteria. Specifically, CHASE3 domains are found in histidine kinases, adenylate cyclases, methyl-accepting chemotaxis proteins and predicted diguanylate cyclases/phosphodiesterases. This domain recognizes pyrene (Matilla et al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).


:

Pssm-ID: 428379  Cd Length: 138  Bit Score: 80.05  E-value: 1.46e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669  46 IDHDFKVLNLTNQVEKELLTIENKAKGFITSNDANYVQSLNAAEKDYEKHYQDLFALLEDNPSQQEKLKQINENITNWIN 125
Cdd:pfam05227   5 VEHTQEVLAALEQLLSALVDAETGQRGYLLTGDESFLEPYEEARAAIPELLARLRALTADNPEQQQRLERLEALIEQKLA 84
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2651418669 126 kEIHPLITNNNSNNVQAI--------DTTQIQSLQSQVTNFRSVEEQLTKKRAAQ 172
Cdd:pfam05227  85 -ELEPTIALRREGGLEAAlalvrsdeGKRLMDAIRALLAEMKAEERRLLEQRTAE 138
CHASE3 COG5278
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
6-509 8.85e-17

Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];


:

Pssm-ID: 444089 [Multi-domain]  Cd Length: 530  Bit Score: 84.57  E-value: 8.85e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669   6 KFSIRYKIMAGYLVIILFLLISFIMLNNQISNLQKSRNfIIDHDFKVLNLTNQVEKELLTIENKAKGFITSNDANYVQSL 85
Cdd:COG5278     3 NLSIRRKLLLGFALALLLLLVLGVLSYLSLNRLREASE-WVEHTYEVLRALEELLSALLDAETGQRGYLLTGDESFLEPY 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669  86 NAAEKDYEKHYQDLFALLEDNPSQQEKLKQINENITNWINkEIHPLITNNNSNNVQ-AIDTTQIQSLQSQVTNFRSVEEQ 164
Cdd:COG5278    82 EEARAEIDELLAELRSLTADNPEQQARLDELEALIDQWLA-ELEQVIALRRAGGLEaALALVRSGEGKALMDEIRARLLL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 165 LTKKRAAQLDTKNNKLEIWLYSLLFLLSCFAIIVSLYISNSITKTIKNVIQAIKSISSKEKITERIHVNSHDEIKDLAHT 244
Cdd:COG5278   161 LALALAALLLAAAALLLLLLALAALLALAELLLLALARALAALLLLLLLEAELAAAAALLAAAAALAALAALELLAALAL 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 245 TNHLLDEISKREWLQTELAELILMYQGVSSIEMLGNKILSGIIQKTQTSCGAFYVREEVEDTVYYVKKASFAEQGADIGK 324
Cdd:COG5278   241 ALALLLAALLLALLAALALAALLAAALLALAALLLALAAAAALAAAAALELAAAEALALAELELELLLAAAAAAAAAAAA 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 325 QSIKMGEGFIGQTALEKKSFILRDIPEEFRYVTTGLLEIRPKNLLVIPVLFEDEVIAVMELVSVTDISDLHQDLIQQTVD 404
Cdd:COG5278   321 AAAALAALLALALATALAAAAAALALLAALLAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVELEVLAIAAAAA 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 405 NLGLTIHSIMGRMRIQTLLYESQAMTEELQVQSEELQTQAEELQMQAEELRTTNEQLESRTEEAEQKTADLQVTKLELEE 484
Cdd:COG5278   401 AAAAEAAAAAAAAAAASAAEALELAEALAEALALAEEEALALAAASSELAEAGAALALAAAEALAEELAAVAALAALAAA 480
                         490       500
                  ....*....|....*....|....*
gi 2651418669 485 KASELLRSSKYKSEFLANMSHELRT 509
Cdd:COG5278   481 AAALAEAEAAAALAAAAALSLALAL 505
 
Name Accession Description Interval E-value
BaeS COG0642
Signal transduction histidine kinase [Signal transduction mechanisms];
391-731 1.16e-74

Signal transduction histidine kinase [Signal transduction mechanisms];


Pssm-ID: 440407 [Multi-domain]  Cd Length: 328  Bit Score: 247.51  E-value: 1.16e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 391 ISDLHQDLIQQTVDNLGLTIHSIMGRMRIQTLLYESQAMTEELQVQSEELQTQAEELQMQAEELRTTNEQLESRTEEAEQ 470
Cdd:COG0642     5 LLLLVLLLLLLLLLLLALLLLLLLLLLLALLLLLALLLLLLLLLLLLLLLALALLALLLLLLLLLLLLLLLLLLLLLLLL 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 471 KTADLQVTKLELEEKASELLRSSKYKSEFLANMSHELRTPLNSILLLSEMLKENHDnhlsDDEIELATVIHSSGKDLLTL 550
Cdd:COG0642    85 LLLLLLLLLLLLLALLLLLEEANEAKSRFLANVSHELRTPLTAIRGYLELLLEELD----EEQREYLETILRSADRLLRL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 551 INDILDLSKVEAGKLDVIFEATNISDMAASMHQNFLHIAAQKNVEFTVEDSDTIPDLfYTDAKRIEQIIKNLLSNAFKFT 630
Cdd:COG0642   161 INDLLDLSRLEAGKLELEPEPVDLAELLEEVVELFRPLAEEKGIELELDLPDDLPTV-RGDPDRLRQVLLNLLSNAIKYT 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 631 EKGS-VSLHFdsietsnlshdmqSISKDWITISVKDTGIGIAKEQHQLIFEAFQQADGAtiRKYGGTGLGLSICKEFARL 709
Cdd:COG0642   240 PEGGtVTVSV-------------RREGDRVRISVEDTGPGIPPEDLERIFEPFFRTDPS--RRGGGTGLGLAIVKRIVEL 304
                         330       340
                  ....*....|....*....|..
gi 2651418669 710 LGGWITLESNVGEGSTFTVYIP 731
Cdd:COG0642   305 HGGTIEVESEPGKGTTFTVTLP 326
PRK11107 PRK11107
hybrid sensory histidine kinase BarA; Provisional
445-896 3.65e-68

hybrid sensory histidine kinase BarA; Provisional


Pssm-ID: 236848 [Multi-domain]  Cd Length: 919  Bit Score: 244.37  E-value: 3.65e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 445 EELQM---QA-EELRTTNEQLEsrteeaeqktadLQVTKLELEEK-ASEllrSSKYKSEFLANMSHELRTPLNSI----- 514
Cdd:PRK11107  252 EEMQQnidQAtSDLRETLEQME------------IQNVELDLAKKrAQE---AARIKSEFLANMSHELRTPLNGVigftr 316
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 515 LLLSEMLKENHDNHLsdDEIELatvihsSGKDLLTLINDILDLSKVEAGKL----------DVIFEATNIsdMAASMHQn 584
Cdd:PRK11107  317 QTLKTPLTPTQRDYL--QTIER------SANNLLAIINDILDFSKLEAGKLvlenipfslrETLDEVVTL--LAHSAHE- 385
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 585 flhiaaqKNVEFTVEDSDTIPDLFYTDAKRIEQIIKNLLSNAFKFTEKGSVSLhfdSIEtsnlshdMQSISKDWITI--S 662
Cdd:PRK11107  386 -------KGLELTLNIDPDVPDNVIGDPLRLQQIITNLVGNAIKFTESGNIDI---LVE-------LRALSNTKVQLevQ 448
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 663 VKDTGIGIAKEQHQLIFEAFQQADGATIRKYGGTGLGLSICKEFARLLGGWITLESNVGEGSTFTVYIP-NL-------- 733
Cdd:PRK11107  449 IRDTGIGISERQQSQLFQAFRQADASISRRHGGTGLGLVITQKLVNEMGGDISFHSQPNRGSTFWFHLPlDLnpnpiidg 528
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 734 ---------------PNGLTNIQVSNLeVAATVDEVI--------------------------PAEVVEETI--VLPETN 770
Cdd:PRK11107  529 lptdclagkrllyvePNSAAAQATLDI-LSETPLEVTysptlsqlpeahydilllglpvtfrePLTMLHERLakAKSMTD 607
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 771 NV-----FQEK--------------------------------------------------TILIVDDDHRN---IFALq 792
Cdd:PRK11107  608 FLilalpCHEQvlaeqlkqdgadaclskplshtrllpallepchhkqppllpptdesrlplTVMAVDDNPANlklIGAL- 686
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 793 naLKKHHANIITAQNGLECLEILKNNTnIDLILMDIMMPNMDGYETMEHIRMNLGLHEIPIIALTAKAMPNDKEKCLSAG 872
Cdd:PRK11107  687 --LEEQVEHVVLCDSGHQAVEQAKQRP-FDLILMDIQMPGMDGIRACELIRQLPHNQNTPIIAVTAHAMAGERERLLSAG 763
                         570       580
                  ....*....|....*....|....
gi 2651418669 873 ASDYISKPLNLHQLYSVMSVWLIK 896
Cdd:PRK11107  764 MDDYLAKPIDEAMLKQVLLRYKPG 787
TMAO_torS TIGR02956
TMAO reductase sytem sensor TorS; This protein, TorS, is part of a regulatory system for the ...
431-894 4.22e-63

TMAO reductase sytem sensor TorS; This protein, TorS, is part of a regulatory system for the torCAD operon that encodes the pterin molybdenum cofactor-containing enzyme trimethylamine-N-oxide (TMAO) reductase (TorA), a cognate chaperone (TorD), and a penta-haem cytochrome (TorC). TorS works together with the inducer-binding protein TorT and the response regulator TorR. TorS contains histidine kinase ATPase (pfam02518), HAMP (pfam00672), phosphoacceptor (pfam00512), and phosphotransfer (pfam01627) domains and a response regulator receiver domain (pfam00072). [Signal transduction, Two-component systems]


Pssm-ID: 274362 [Multi-domain]  Cd Length: 968  Bit Score: 230.44  E-value: 4.22e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 431 EELQVQSEELQTqAEELQMQAEELRttnEQLESRTEEAEQKTADLQVTKLELEEKASELLRSSKYKSEFLANMSHELRTP 510
Cdd:TIGR02956 403 HNLKLQADERQV-AQELQEHKESLE---QLVAQRTQELAETNERLNAEVKNHAKARAEAEEANRAKSAFLATMSHEIRTP 478
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 511 LNSILLLSEMLKenhDNHLSDDEIELATVIHSSGKDLLTLINDILDLSKVEAGKLDVIFEATNISDMAASMHQNFLHIAA 590
Cdd:TIGR02956 479 LNGILGTLELLG---DTGLTSQQQQYLQVINRSGESLLDILNDILDYSKIEAGHLSISPRPFDLNALLDDVHHLMVSRAQ 555
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 591 QKNVEFTVEDSDTIPDLFYTDAKRIEQIIKNLLSNAFKFTEKGSVSLhfdsietsNLSHDMQSIskdwITISVKDTGIGI 670
Cdd:TIGR02956 556 LKGIQLRLNIPEQLPNWWQGDGPRIRQVLINLVGNAIKFTDRGSVVL--------RVSLNDDSS----LLFEVEDTGCGI 623
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 671 AKEQHQLIFEAFQQADGatIRKYGGTGLGLSICKEFARLLGGWITLESNVGEGSTFTVYIPnlpngLTNIQVSNLEVAAT 750
Cdd:TIGR02956 624 AEEEQATLFDAFTQADG--RRRSGGTGLGLAISQRLVEAMDGELGVESELGVGSCFWFTLP-----LTRGKPAEDSATLT 696
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 751 VDEVIPAEVveetivlpetnnvfqektiLIVDDDHRNIFALQNALKKHHANIITAQNGLECLEILKNNTnIDLILMDIMM 830
Cdd:TIGR02956 697 VIDLPPQRV-------------------LLVEDNEVNQMVAQGFLTRLGHKVTLAESGQSALECFHQHA-FDLALLDINL 756
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2651418669 831 PNMDGYETMEHIR-MNLGLHEIPIIALTAKAMPNDKEKCLSAGASDYISKPLNLHQLYSVMSVWL 894
Cdd:TIGR02956 757 PDGDGVTLLQQLRaIYGAKNEVKFIAFSAHVFNEDVAQYLAAGFDGFLAKPVVEEQLTAMIAVIL 821
HATPase_EvgS-ArcB-TorS-like cd16922
Histidine kinase-like ATPase domain of two-component sensor histidine kinases, many are hybrid ...
615-731 3.53e-48

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: 166.13  E-value: 3.53e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 615 IEQIIKNLLSNAFKFTEKGSVSLHFDSIETSNlshdmqsiSKDWITISVKDTGIGIAKEQHQLIFEAFQQADGATIRKYG 694
Cdd:cd16922     1 LRQILLNLLGNAIKFTEEGEVTLRVSLEEEEE--------DGVQLRFSVEDTGIGIPEEQQARLFEPFSQADSSTTRKYG 72
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2651418669 695 GTGLGLSICKEFARLLGGWITLESNVGEGSTFTVYIP 731
Cdd:cd16922    73 GTGLGLAISKKLVELMGGDISVESEPGQGSTFTFTLP 109
CheY COG0784
CheY-like REC (receiver) domain, includes chemotaxis protein CheY and sporulation regulator ...
776-894 4.23e-42

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: 149.62  E-value: 4.23e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 776 KTILIVDDDHRNIFALQNALKKHHANIITAQNGLECLEILKNNTnIDLILMDIMMPNMDGYETMEHIRMNLGLHEIPIIA 855
Cdd:COG0784     6 KRILVVDDNPDNRELLRRLLERLGYEVTTAEDGAEALELLRAGP-PDLILLDINMPGMDGLELLRRIRALPRLPDIPIIA 84
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2651418669 856 LTAKAMPNDKEKCLSAGASDYISKPLNLHQLYSVMSVWL 894
Cdd:COG0784    85 LTAYADEEDRERALEAGADDYLTKPVDPEELLEALRRLL 123
REC_hyHK_CKI1_RcsC-like cd17546
phosphoacceptor receiver (REC) domain of hybrid sensor histidine kinases/response regulators ...
778-890 9.67e-39

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: 139.53  E-value: 9.67e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 778 ILIVDDDHRNIFALQNALKKHHANIITAQNGLECLEILKNNtNIDLILMDIMMPNMDGYETMEHIR-MNLGLHEIPIIAL 856
Cdd:cd17546     1 VLVVDDNPVNRKVLKKLLEKLGYEVDVAENGQEALELLKEE-PFDLVLMDLQMPVMDGLEATRRIReLEGGGRRTPIIAL 79
                          90       100       110
                  ....*....|....*....|....*....|....
gi 2651418669 857 TAKAMPNDKEKCLSAGASDYISKPLNLHQLYSVM 890
Cdd:cd17546    80 TANALEEDREKCLEAGMDDYLSKPVKLDQLKEVL 113
HATPase_c smart00387
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.
610-731 2.42e-34

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


Pssm-ID: 214643 [Multi-domain]  Cd Length: 111  Bit Score: 126.99  E-value: 2.42e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669  610 TDAKRIEQIIKNLLSNAFKFTEKG---SVSLHFDsietsnlshdmqsisKDWITISVKDTGIGIAKEQHQLIFEAFQQAD 686
Cdd:smart00387   1 GDPDRLRQVLSNLLDNAIKYTPEGgriTVTLERD---------------GDHVEITVEDNGPGIPPEDLEKIFEPFFRTD 65
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 2651418669  687 GaTIRKYGGTGLGLSICKEFARLLGGWITLESNVGEGSTFTVYIP 731
Cdd:smart00387  66 K-RSRKIGGTGLGLSIVKKLVELHGGEISVESEPGGGTTFTITLP 109
MtrAB_MtrB NF040691
MtrAB system histidine kinase MtrB;
470-731 2.63e-34

MtrAB system histidine kinase MtrB;


Pssm-ID: 468655 [Multi-domain]  Cd Length: 507  Bit Score: 138.23  E-value: 2.63e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 470 QKTADLQVTKLELEEkasellrSSKYKSEFLANMSHELRTPLNSILLLSEMLkenhdnHLSDDEIELAT-----VIHSSG 544
Cdd:NF040691  252 QMADSLQRQIRQLEE-------LSRLQQRFVSDVSHELRTPLTTIRMAADVI------HDSRDDFDPATarsaeLLHTEL 318
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 545 KDLLTLINDILDLSKVEAG--KLDVifEATNISDMAASMHQNFLHIAAQKNVEFTVEDSDTiPDLFYTDAKRIEQIIKNL 622
Cdd:NF040691  319 DRFESLLSDLLEISRFDAGaaELDV--EPVDLRPLVRRVVDALRQLAERAGVELRVDAPGT-PVVAEVDPRRVERVLRNL 395
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 623 LSNAFKFTEKGSVSLHFDSIETSnlshdmqsiskdwITISVKDTGIGIAKEQHQLIFEAFQQADGATIRKYGGTGLGLSI 702
Cdd:NF040691  396 VVNAIEHGEGKPVVVTVAQDDTA-------------VAVTVRDHGVGLKPGEVALVFDRFWRADPARARTTGGTGLGLAI 462
                         250       260
                  ....*....|....*....|....*....
gi 2651418669 703 CKEFARLLGGWITLESNVGEGSTFTVYIP 731
Cdd:NF040691  463 ALEDARLHGGWLEAWGRPGQGSQFRLTLP 491
HATPase_c pfam02518
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the ...
610-731 1.50e-30

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: 115.93  E-value: 1.50e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 610 TDAKRIEQIIKNLLSNAFKFT---EKGSVSLHFDsietsnlshdmqsiskDWITISVKDTGIGIAKEQHQLIFEAFQQAD 686
Cdd:pfam02518   1 GDELRLRQVLSNLLDNALKHAakaGEITVTLSEG----------------GELTLTVEDNGIGIPPEDLPRIFEPFSTAD 64
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 2651418669 687 gatIRKYGGTGLGLSICKEFARLLGGWITLESNVGEGSTFTVYIP 731
Cdd:pfam02518  65 ---KRGGGGTGLGLSIVRKLVELLGGTITVESEPGGGTTVTLTLP 106
HK_WalK NF033092
cell wall metabolism sensor histidine kinase WalK; This model describes WalK as found in ...
498-731 1.53e-30

cell wall metabolism sensor histidine kinase WalK; This model describes WalK as found in Staphylococcus aureus (sp|Q2G2U4.1|WALK_STAA8). A shorter version, as found in Streptococcus pneumoniae, called WalK(Spn) or VicK, is not included. WalK is part of a two-component system and works with partner protein WalR.


Pssm-ID: 467964 [Multi-domain]  Cd Length: 594  Bit Score: 127.95  E-value: 1.53e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 498 EFLANMSHELRTPLNSILLLSEMLKenhDNHLSDDEI--ELATVIHSSGKDLLTLINDILDLSKVEAGKLDVIFEATNIS 575
Cdd:NF033092  374 EFVANVSHELRTPLTTMRSYLEALA---DGAWKDPELapRFLGVTQNETERMIRLVNDLLQLSRMDSKDYKLNKEWVNFN 450
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 576 DMAASMHQNFLHIAAQKNVEFTVEdsdtIP--DLF-YTDAKRIEQIIKNLLSNAFKFT-EKGSVSLHFdsIETSNLshdm 651
Cdd:NF033092  451 EFFNYIIDRFEMILKNKNITFKRE----FPkrDLWvEIDTDKITQVLDNIISNAIKYSpEGGTITFRL--LETHNR---- 520
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 652 qsiskdwITISVKDTGIGIAKEQHQLIFEAFQQADGATIRKYGGTGLGLSICKEFARLLGGWITLESNVGEGSTFTVYIP 731
Cdd:NF033092  521 -------IIISISDQGLGIPKKDLDKIFDRFYRVDKARSRKMGGTGLGLAIAKEVVEAHGGRIWAESEEGKGTTIYFTLP 593
Response_reg pfam00072
Response regulator receiver domain; This domain receives the signal from the sensor partner in ...
778-886 5.74e-29

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: 111.47  E-value: 5.74e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 778 ILIVDDDHRNIFALQNALKKHHANIITAQNGLECLEILKNNTnIDLILMDIMMPNMDGYETMEHIRmNLGlHEIPIIALT 857
Cdd:pfam00072   1 VLIVDDDPLIRELLRQLLEKEGYVVAEADDGKEALELLKEER-PDLILLDINMPGMDGLELLKRIR-RRD-PTTPVIILT 77
                          90       100
                  ....*....|....*....|....*....
gi 2651418669 858 AKAMPNDKEKCLSAGASDYISKPLNLHQL 886
Cdd:pfam00072  78 AHGDEDDAVEALEAGADDFLSKPFDPDEL 106
pleD PRK09581
response regulator PleD; Reviewed
777-888 1.79e-22

response regulator PleD; Reviewed


Pssm-ID: 236577 [Multi-domain]  Cd Length: 457  Bit Score: 101.52  E-value: 1.79e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 777 TILIVDDDHRNIFALQNALKKHHANIITAQNGLECLEILKNnTNIDLILMDIMMPNMDGYETMEHIRMNLGLHEIPIIAL 856
Cdd:PRK09581    4 RILVVDDIPANVKLLEAKLLAEYYTVLTASSGAEAIAICER-EQPDIILLDVMMPGMDGFEVCRRLKSDPATTHIPVVMV 82
                          90       100       110
                  ....*....|....*....|....*....|..
gi 2651418669 857 TAKAMPNDKEKCLSAGASDYISKPLNLHQLYS 888
Cdd:PRK09581   83 TALDDPEDRVRGLEAGADDFLTKPINDVALFA 114
BaeS_SmeS NF012163
sensor histidine kinase efflux regulator BaeS;
486-731 3.90e-21

sensor histidine kinase efflux regulator BaeS;


Pssm-ID: 411086 [Multi-domain]  Cd Length: 457  Bit Score: 97.59  E-value: 3.90e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 486 ASELLRSSKYKSEFLANMSHELRTPL----NSILLLSEMLKENHDNHLSDDEIELATvihssgkdLLTLINDILDLSKVE 561
Cdd:NF012163  230 ASTLEKNEQMRRDFMADISHELRTPLavlrAELEAIQDGIRKFTPESLDSLQAEVGT--------LTKLVDDLHDLSMSD 301
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 562 AGKLDVIFEATNISDMAASMHQNFLHIAAQKNVEFTVEDSDTIpdLFYTDAKRIEQIIKNLLSNAFKFTEKGSvSLHFDS 641
Cdd:NF012163  302 EGALAYQKASVDLVPLLEVEGGAFRERFASAGLELEVSLPDSS--LVFGDRDRLMQLFNNLLENSLRYTDSGG-SLHISA 378
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 642 IETsnlshdmqsiSKDWiTISVKDTGIGIAKEQHQLIFEAFQQADGATIRKYGGTGLGLSICKEFARLLGGWITLESNVG 721
Cdd:NF012163  379 SQR----------PKEV-TLTVADSAPGVSDEQLARLFERFYRVEVSRNRASGGSGLGLAISLNIVQAHGGTLHAAHSPL 447
                         250
                  ....*....|
gi 2651418669 722 EGSTFTVYIP 731
Cdd:NF012163  448 GGLRIVVTLP 457
CHASE3 pfam05227
CHASE3 domain; CHASE3 is an extracellular sensory domain, which is present in various classes ...
46-172 1.46e-17

CHASE3 domain; CHASE3 is an extracellular sensory domain, which is present in various classes of transmembrane receptors that are parts of signal transduction pathways in bacteria. Specifically, CHASE3 domains are found in histidine kinases, adenylate cyclases, methyl-accepting chemotaxis proteins and predicted diguanylate cyclases/phosphodiesterases. This domain recognizes pyrene (Matilla et al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).


Pssm-ID: 428379  Cd Length: 138  Bit Score: 80.05  E-value: 1.46e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669  46 IDHDFKVLNLTNQVEKELLTIENKAKGFITSNDANYVQSLNAAEKDYEKHYQDLFALLEDNPSQQEKLKQINENITNWIN 125
Cdd:pfam05227   5 VEHTQEVLAALEQLLSALVDAETGQRGYLLTGDESFLEPYEEARAAIPELLARLRALTADNPEQQQRLERLEALIEQKLA 84
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2651418669 126 kEIHPLITNNNSNNVQAI--------DTTQIQSLQSQVTNFRSVEEQLTKKRAAQ 172
Cdd:pfam05227  85 -ELEPTIALRREGGLEAAlalvrsdeGKRLMDAIRALLAEMKAEERRLLEQRTAE 138
CHASE3 COG5278
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
6-509 8.85e-17

Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];


Pssm-ID: 444089 [Multi-domain]  Cd Length: 530  Bit Score: 84.57  E-value: 8.85e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669   6 KFSIRYKIMAGYLVIILFLLISFIMLNNQISNLQKSRNfIIDHDFKVLNLTNQVEKELLTIENKAKGFITSNDANYVQSL 85
Cdd:COG5278     3 NLSIRRKLLLGFALALLLLLVLGVLSYLSLNRLREASE-WVEHTYEVLRALEELLSALLDAETGQRGYLLTGDESFLEPY 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669  86 NAAEKDYEKHYQDLFALLEDNPSQQEKLKQINENITNWINkEIHPLITNNNSNNVQ-AIDTTQIQSLQSQVTNFRSVEEQ 164
Cdd:COG5278    82 EEARAEIDELLAELRSLTADNPEQQARLDELEALIDQWLA-ELEQVIALRRAGGLEaALALVRSGEGKALMDEIRARLLL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 165 LTKKRAAQLDTKNNKLEIWLYSLLFLLSCFAIIVSLYISNSITKTIKNVIQAIKSISSKEKITERIHVNSHDEIKDLAHT 244
Cdd:COG5278   161 LALALAALLLAAAALLLLLLALAALLALAELLLLALARALAALLLLLLLEAELAAAAALLAAAAALAALAALELLAALAL 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 245 TNHLLDEISKREWLQTELAELILMYQGVSSIEMLGNKILSGIIQKTQTSCGAFYVREEVEDTVYYVKKASFAEQGADIGK 324
Cdd:COG5278   241 ALALLLAALLLALLAALALAALLAAALLALAALLLALAAAAALAAAAALELAAAEALALAELELELLLAAAAAAAAAAAA 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 325 QSIKMGEGFIGQTALEKKSFILRDIPEEFRYVTTGLLEIRPKNLLVIPVLFEDEVIAVMELVSVTDISDLHQDLIQQTVD 404
Cdd:COG5278   321 AAAALAALLALALATALAAAAAALALLAALLAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVELEVLAIAAAAA 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 405 NLGLTIHSIMGRMRIQTLLYESQAMTEELQVQSEELQTQAEELQMQAEELRTTNEQLESRTEEAEQKTADLQVTKLELEE 484
Cdd:COG5278   401 AAAAEAAAAAAAAAAASAAEALELAEALAEALALAEEEALALAAASSELAEAGAALALAAAEALAEELAAVAALAALAAA 480
                         490       500
                  ....*....|....*....|....*
gi 2651418669 485 KASELLRSSKYKSEFLANMSHELRT 509
Cdd:COG5278   481 AAALAEAEAAAALAAAAALSLALAL 505
PhoB TIGR02154
phosphate regulon transcriptional regulatory protein PhoB; PhoB is a DNA-binding response ...
776-893 9.74e-15

phosphate regulon transcriptional regulatory protein PhoB; PhoB is a DNA-binding response regulator protein acting with PhoR in a 2-component system responding to phosphate ion. PhoB acts as a positive regulator of gene expression for phosphate-related genes such as phoA, phoS, phoE and ugpAB as well as itself. It is often found proximal to genes for the high-affinity phosphate ABC transporter (pstSCAB; GenProp0190) and presumably regulates these as well. [Regulatory functions, DNA interactions, Signal transduction, Two-component systems]


Pssm-ID: 131209 [Multi-domain]  Cd Length: 226  Bit Score: 74.29  E-value: 9.74e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 776 KTILIVDDDH--RNIFALqnALKKHHANIITAQNGLECLEILKNNTNiDLILMDIMMPNMDGYETMEHIRMNLGLHEIPI 853
Cdd:TIGR02154   3 RRILVVEDEPaiRELIAY--NLEKAGYDVVEAGDGDEALTLINERGP-DLILLDWMLPGTSGIELCRRLRRRPETRAIPI 79
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 2651418669 854 IALTAKAMPNDKEKCLSAGASDYISKPLNLHQLYS-VMSVW 893
Cdd:TIGR02154  80 IMLTARGEEEDRVRGLETGADDYITKPFSPRELLArIKAVL 120
AdeS_HK NF012226
two-component sensor histidine kinase AdeS; Mutations in this component of the two-component ...
486-731 4.11e-13

two-component sensor histidine kinase AdeS; Mutations in this component of the two-component regulatory system for the AdeABC efflux pump can confer adaptive resistance to certain antibiotics, including tigecycline.


Pssm-ID: 411090 [Multi-domain]  Cd Length: 353  Bit Score: 71.56  E-value: 4.11e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 486 ASELLRSSKYKSEFLANMSHELRTPlnsILLLSEMLKENHDNHLSDDEIELatvihssgKDLLT-------LINDILDLS 558
Cdd:NF012226  128 AQKLESSVKNAQVWNAAIAHELRTP---ITILQGRLQGILDGVFEPDPALF--------KSLLNqveglshLVEDLRTLS 196
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 559 KVEAGKLDVIFEATNISDMAASMHQNFLHIAAQKNVEFTVEDSDTipdLFYTDAKRIEQIIKNLLSNAFKFTEKGsvslh 638
Cdd:NF012226  197 LVENQQLRLNYESVDLKDSIEKVLKMFEDRLEQAQLTIVLNLTAT---PVFCDRRRIEQVLIALIDNAIRYANAG----- 268
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 639 fdsietsNLSHDMQSISKDWItISVKDTGIGIAKEQHQLIFEAFQQADGATIRKYGGTGLGLSICKEFARLLGGWITLeS 718
Cdd:NF012226  269 -------KLKISSSVIQDDWI-LQIEDEGPGIAEEYQQDLFNPFFRLEQSRNKEFGGTGLGLAVVHAIVIAHKGSIEY-S 339
                         250
                  ....*....|...
gi 2651418669 719 NVGEGSTFTVYIP 731
Cdd:NF012226  340 NSQGNSVFTIKLP 352
GAF_2 pfam13185
GAF domain; The GAF domain is named after some of the proteins it is found in, including ...
273-411 1.65e-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: 62.48  E-value: 1.65e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 273 SSIEMLGNKILSGIIQKTQTSCGAFYVREEVEDTVyyvkkASFAEQGADIGKQSIKMGEGFIGQTALEKKSFILRDIPEE 352
Cdd:pfam13185   2 ADLEELLDAVLEAAVELGASAVGFILLVDDDGRLA-----AWGGAADELSAALDDPPGEGLVGEALRTGRPVIVNDLAAD 76
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2651418669 353 FRYVTTGLLEIRPKNLLVIPVLFEDEVIAVMELVS--VTDISDLHQDLIQQTVDNLGLTIH 411
Cdd:pfam13185  77 PAKKGLPAGHAGLRSFLSVPLVSGGRVVGVLALGSnrPGAFDEEDLELLELLAEQAAIAIE 137
REC smart00448
cheY-homologous receiver domain; CheY regulates the clockwise rotation of E. coli flagellar ...
776-831 2.04e-11

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


Pssm-ID: 214668 [Multi-domain]  Cd Length: 55  Bit Score: 59.50  E-value: 2.04e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2651418669  776 KTILIVDDDHRNIFALQNALKKHHANIITAQNGLECLEILKNNtNIDLILMDIMMP 831
Cdd:smart00448   1 MRILVVDDDPLLRELLKALLEKEGYEVDEATDGEEALELLKEE-KPDLILLDIMMP 55
HK9-like_sensor cd19410
ligand binding sensor domain of Rhodopseudomonas palustris histidine kinase HK9 and similar ...
47-125 6.82e-08

ligand binding sensor domain of Rhodopseudomonas palustris histidine kinase HK9 and similar proteins; The ligand binding sensor domain of Rhodopseudomonas palustris histidine kinase HK9 and similar proteins forms a homodimer and binds to an as yet uncharacterized ligand, most likely via the dimerization interface, a feature that appears to be conserved in this domain superfamily. This domain is similar to the extracellular sensory domain CHASE3, specifically found in histidine kinases, adenylate cyclases, methyl-accepting chemotaxis proteins and predicted diguanylate cyclases/phosphodiesterases. Environmental factors that are recognized by CHASE3 domains are not known at this time.


Pssm-ID: 438628  Cd Length: 125  Bit Score: 51.83  E-value: 6.82e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2651418669  47 DHDFKVLNLTNQVEKELLTIENKAKGFITSNDANYVQSLNAAEKDYEKHYQDLFALLEDNPSQQEKLKQINENITNWIN 125
Cdd:cd19410     1 EHTYEVLSELERLLSLLKDAETGQRGYLLTGDESYLEPYNAARARLPALLAELRELTADNPAQQARLDELEPLIDEKLA 79
HAMP cd06225
Histidine kinase, Adenylyl cyclase, Methyl-accepting protein, and Phosphatase (HAMP) domain; ...
207-252 4.03e-04

Histidine kinase, Adenylyl cyclase, Methyl-accepting protein, and Phosphatase (HAMP) domain; HAMP is a signaling domain which occurs in a wide variety of signaling proteins, many of which are bacterial. The HAMP domain consists of two alpha helices connected by an extended linker. The structure of the Af1503 HAMP dimer from Archaeoglobus fulgidus has been solved using nuclear magnetic resonance, revealing a parallel four-helix bundle; this structure has been confirmed by cross-linking analysis of HAMP domains from the Escherichia coli aerotaxis receptor Aer. It has been suggested that the four-helix arrangement can rotate between the unusually packed conformation observed in the NMR structure and a canonical coiled-coil arrangement. Such rotation may coincide with signal transduction, but a common mechanism by which HAMP domains relay a variety of input signals has yet to be established.


Pssm-ID: 381743 [Multi-domain]  Cd Length: 45  Bit Score: 38.58  E-value: 4.03e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 2651418669 207 TKTIKNVIQAIKSISSKEkITERIHVNSHDEIKDLAHTTNHLLDEI 252
Cdd:cd06225     1 TRPLRRLTEAARRIAEGD-LDVRVPVRSKDEIGELARAFNQMAERL 45
GAF smart00065
Domain present in phytochromes and cGMP-specific phosphodiesterases; Mutations within these ...
280-426 3.59e-03

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: 38.90  E-value: 3.59e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669  280 NKILSGIIQKTQTSCGAFYVREEvEDTVYYVKKASFAEQGADIGkQSIKMGEGFIGQTALEKKSFILRDIPEEFRY-VTT 358
Cdd:smart00065   7 QTILEELRQLLGADRVLIYLVDE-NDRGELVLVAADGLTLPTLG-IRFPLDEGLAGRVAETGRPLNIPDVEADPLFaEDL 84
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2651418669  359 GLLEIRPKNLLVIPVLFEDEVIAVMELVSVTDISDLHQD---LIQQTVDNLGLTIHsimgrmriQTLLYES 426
Cdd:smart00065  85 LGRYQGVRSFLAVPLVADGELVGVLALHNKKSPRPFTEEdeeLLQALANQLAIALA--------NAQLYEE 147
 
Name Accession Description Interval E-value
BaeS COG0642
Signal transduction histidine kinase [Signal transduction mechanisms];
391-731 1.16e-74

Signal transduction histidine kinase [Signal transduction mechanisms];


Pssm-ID: 440407 [Multi-domain]  Cd Length: 328  Bit Score: 247.51  E-value: 1.16e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 391 ISDLHQDLIQQTVDNLGLTIHSIMGRMRIQTLLYESQAMTEELQVQSEELQTQAEELQMQAEELRTTNEQLESRTEEAEQ 470
Cdd:COG0642     5 LLLLVLLLLLLLLLLLALLLLLLLLLLLALLLLLALLLLLLLLLLLLLLLALALLALLLLLLLLLLLLLLLLLLLLLLLL 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 471 KTADLQVTKLELEEKASELLRSSKYKSEFLANMSHELRTPLNSILLLSEMLKENHDnhlsDDEIELATVIHSSGKDLLTL 550
Cdd:COG0642    85 LLLLLLLLLLLLLALLLLLEEANEAKSRFLANVSHELRTPLTAIRGYLELLLEELD----EEQREYLETILRSADRLLRL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 551 INDILDLSKVEAGKLDVIFEATNISDMAASMHQNFLHIAAQKNVEFTVEDSDTIPDLfYTDAKRIEQIIKNLLSNAFKFT 630
Cdd:COG0642   161 INDLLDLSRLEAGKLELEPEPVDLAELLEEVVELFRPLAEEKGIELELDLPDDLPTV-RGDPDRLRQVLLNLLSNAIKYT 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 631 EKGS-VSLHFdsietsnlshdmqSISKDWITISVKDTGIGIAKEQHQLIFEAFQQADGAtiRKYGGTGLGLSICKEFARL 709
Cdd:COG0642   240 PEGGtVTVSV-------------RREGDRVRISVEDTGPGIPPEDLERIFEPFFRTDPS--RRGGGTGLGLAIVKRIVEL 304
                         330       340
                  ....*....|....*....|..
gi 2651418669 710 LGGWITLESNVGEGSTFTVYIP 731
Cdd:COG0642   305 HGGTIEVESEPGKGTTFTVTLP 326
KdpD COG2205
K+-sensing histidine kinase KdpD [Signal transduction mechanisms];
481-731 4.27e-70

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


Pssm-ID: 441807 [Multi-domain]  Cd Length: 239  Bit Score: 231.72  E-value: 4.27e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 481 ELEEKASELLRSSKYKSEFLANMSHELRTPLNSILLLSEMLKENHDNhLSDDEIELATVIHSSGKDLLTLINDILDLSKV 560
Cdd:COG2205     1 ELEEALEELEELERLKSEFLANVSHELRTPLTSILGAAELLLDEEDL-SPEERRELLEIIRESAERLLRLIEDLLDLSRL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 561 EAGKLDVIFEATNISDMAASMHQNFLHIAAQKNVEFTVEDSDTIPdLFYTDAKRIEQIIKNLLSNAFKFTEKGS-VSLHF 639
Cdd:COG2205    80 ESGKLSLELEPVDLAELLEEAVEELRPLAEEKGIRLELDLPPELP-LVYADPELLEQVLANLLDNAIKYSPPGGtITISA 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 640 dsietsnlshdmqSISKDWITISVKDTGIGIAKEQHQLIFEAFQQADGAtiRKYGGTGLGLSICKEFARLLGGWITLESN 719
Cdd:COG2205   159 -------------RREGDGVRISVSDNGPGIPEEELERIFERFYRGDNS--RGEGGTGLGLAIVKRIVEAHGGTIWVESE 223
                         250
                  ....*....|..
gi 2651418669 720 VGEGSTFTVYIP 731
Cdd:COG2205   224 PGGGTTFTVTLP 235
PRK11107 PRK11107
hybrid sensory histidine kinase BarA; Provisional
445-896 3.65e-68

hybrid sensory histidine kinase BarA; Provisional


Pssm-ID: 236848 [Multi-domain]  Cd Length: 919  Bit Score: 244.37  E-value: 3.65e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 445 EELQM---QA-EELRTTNEQLEsrteeaeqktadLQVTKLELEEK-ASEllrSSKYKSEFLANMSHELRTPLNSI----- 514
Cdd:PRK11107  252 EEMQQnidQAtSDLRETLEQME------------IQNVELDLAKKrAQE---AARIKSEFLANMSHELRTPLNGVigftr 316
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 515 LLLSEMLKENHDNHLsdDEIELatvihsSGKDLLTLINDILDLSKVEAGKL----------DVIFEATNIsdMAASMHQn 584
Cdd:PRK11107  317 QTLKTPLTPTQRDYL--QTIER------SANNLLAIINDILDFSKLEAGKLvlenipfslrETLDEVVTL--LAHSAHE- 385
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 585 flhiaaqKNVEFTVEDSDTIPDLFYTDAKRIEQIIKNLLSNAFKFTEKGSVSLhfdSIEtsnlshdMQSISKDWITI--S 662
Cdd:PRK11107  386 -------KGLELTLNIDPDVPDNVIGDPLRLQQIITNLVGNAIKFTESGNIDI---LVE-------LRALSNTKVQLevQ 448
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 663 VKDTGIGIAKEQHQLIFEAFQQADGATIRKYGGTGLGLSICKEFARLLGGWITLESNVGEGSTFTVYIP-NL-------- 733
Cdd:PRK11107  449 IRDTGIGISERQQSQLFQAFRQADASISRRHGGTGLGLVITQKLVNEMGGDISFHSQPNRGSTFWFHLPlDLnpnpiidg 528
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 734 ---------------PNGLTNIQVSNLeVAATVDEVI--------------------------PAEVVEETI--VLPETN 770
Cdd:PRK11107  529 lptdclagkrllyvePNSAAAQATLDI-LSETPLEVTysptlsqlpeahydilllglpvtfrePLTMLHERLakAKSMTD 607
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 771 NV-----FQEK--------------------------------------------------TILIVDDDHRN---IFALq 792
Cdd:PRK11107  608 FLilalpCHEQvlaeqlkqdgadaclskplshtrllpallepchhkqppllpptdesrlplTVMAVDDNPANlklIGAL- 686
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 793 naLKKHHANIITAQNGLECLEILKNNTnIDLILMDIMMPNMDGYETMEHIRMNLGLHEIPIIALTAKAMPNDKEKCLSAG 872
Cdd:PRK11107  687 --LEEQVEHVVLCDSGHQAVEQAKQRP-FDLILMDIQMPGMDGIRACELIRQLPHNQNTPIIAVTAHAMAGERERLLSAG 763
                         570       580
                  ....*....|....*....|....
gi 2651418669 873 ASDYISKPLNLHQLYSVMSVWLIK 896
Cdd:PRK11107  764 MDDYLAKPIDEAMLKQVLLRYKPG 787
WalK COG5002
Sensor histidine kinase WalK [Signal transduction mechanisms];
368-731 2.67e-67

Sensor histidine kinase WalK [Signal transduction mechanisms];


Pssm-ID: 444026 [Multi-domain]  Cd Length: 390  Bit Score: 229.82  E-value: 2.67e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 368 LLVIPVLFEDEVIAVMELVSVTDISDLHQDLIQQTVDNLGLTIHSIMGRMRIQTLLYESQAMTEELQVQSEELQTQAEEL 447
Cdd:COG5002    39 LLLLLLLLLLLLLLALLLLLLLLLLLLLALLLLLLLLLLLLALALLLLALLLLLLLLLLLLALLILLLLLALLILLAALL 118
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 448 QMQAEELRTTNEQLESRTEEAEQKTADLQVTKLEleEKASELLRSSKYKSEFLANMSHELRTPLNSILLLSEMLKENhDN 527
Cdd:COG5002   119 LLLSELLLLLLLLGRLSLRLSALLLGLLLLAAVE--RDITELERLEQMRREFVANVSHELRTPLTSIRGYLELLLDG-AA 195
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 528 HLSDDEIELATVIHSSGKDLLTLINDILDLSKVEAGKLDVIFEATNISDMAASMHQNFLHIAAQKNVEFTVEDSDTIPDL 607
Cdd:COG5002   196 DDPEERREYLEIILEEAERLSRLVNDLLDLSRLESGELKLEKEPVDLAELLEEVVEELRPLAEEKGIELELDLPEDPLLV 275
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 608 fYTDAKRIEQIIKNLLSNAFKFTEKGS---VSLhfdsietsnlshdmqSISKDWITISVKDTGIGIAKEQHQLIFEAFQQ 684
Cdd:COG5002   276 -LGDPDRLEQVLTNLLDNAIKYTPEGGtitVSL---------------REEDDQVRISVRDTGIGIPEEDLPRIFERFYR 339
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*..
gi 2651418669 685 ADGATIRKYGGTGLGLSICKEFARLLGGWITLESNVGEGSTFTVYIP 731
Cdd:COG5002   340 VDKSRSRETGGTGLGLAIVKHIVEAHGGRIWVESEPGKGTTFTITLP 386
TMAO_torS TIGR02956
TMAO reductase sytem sensor TorS; This protein, TorS, is part of a regulatory system for the ...
431-894 4.22e-63

TMAO reductase sytem sensor TorS; This protein, TorS, is part of a regulatory system for the torCAD operon that encodes the pterin molybdenum cofactor-containing enzyme trimethylamine-N-oxide (TMAO) reductase (TorA), a cognate chaperone (TorD), and a penta-haem cytochrome (TorC). TorS works together with the inducer-binding protein TorT and the response regulator TorR. TorS contains histidine kinase ATPase (pfam02518), HAMP (pfam00672), phosphoacceptor (pfam00512), and phosphotransfer (pfam01627) domains and a response regulator receiver domain (pfam00072). [Signal transduction, Two-component systems]


Pssm-ID: 274362 [Multi-domain]  Cd Length: 968  Bit Score: 230.44  E-value: 4.22e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 431 EELQVQSEELQTqAEELQMQAEELRttnEQLESRTEEAEQKTADLQVTKLELEEKASELLRSSKYKSEFLANMSHELRTP 510
Cdd:TIGR02956 403 HNLKLQADERQV-AQELQEHKESLE---QLVAQRTQELAETNERLNAEVKNHAKARAEAEEANRAKSAFLATMSHEIRTP 478
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 511 LNSILLLSEMLKenhDNHLSDDEIELATVIHSSGKDLLTLINDILDLSKVEAGKLDVIFEATNISDMAASMHQNFLHIAA 590
Cdd:TIGR02956 479 LNGILGTLELLG---DTGLTSQQQQYLQVINRSGESLLDILNDILDYSKIEAGHLSISPRPFDLNALLDDVHHLMVSRAQ 555
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 591 QKNVEFTVEDSDTIPDLFYTDAKRIEQIIKNLLSNAFKFTEKGSVSLhfdsietsNLSHDMQSIskdwITISVKDTGIGI 670
Cdd:TIGR02956 556 LKGIQLRLNIPEQLPNWWQGDGPRIRQVLINLVGNAIKFTDRGSVVL--------RVSLNDDSS----LLFEVEDTGCGI 623
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 671 AKEQHQLIFEAFQQADGatIRKYGGTGLGLSICKEFARLLGGWITLESNVGEGSTFTVYIPnlpngLTNIQVSNLEVAAT 750
Cdd:TIGR02956 624 AEEEQATLFDAFTQADG--RRRSGGTGLGLAISQRLVEAMDGELGVESELGVGSCFWFTLP-----LTRGKPAEDSATLT 696
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 751 VDEVIPAEVveetivlpetnnvfqektiLIVDDDHRNIFALQNALKKHHANIITAQNGLECLEILKNNTnIDLILMDIMM 830
Cdd:TIGR02956 697 VIDLPPQRV-------------------LLVEDNEVNQMVAQGFLTRLGHKVTLAESGQSALECFHQHA-FDLALLDINL 756
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2651418669 831 PNMDGYETMEHIR-MNLGLHEIPIIALTAKAMPNDKEKCLSAGASDYISKPLNLHQLYSVMSVWL 894
Cdd:TIGR02956 757 PDGDGVTLLQQLRaIYGAKNEVKFIAFSAHVFNEDVAQYLAAGFDGFLAKPVVEEQLTAMIAVIL 821
PRK15347 PRK15347
two component system sensor kinase;
454-886 8.60e-60

two component system sensor kinase;


Pssm-ID: 237951 [Multi-domain]  Cd Length: 921  Bit Score: 220.28  E-value: 8.60e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 454 LRTTNEQ---LESRTEEaeqKTadlqvtkLELEEKASELLRSSKYKSEFLANMSHELRTPLNSILLLSEMLKenhDNHLS 530
Cdd:PRK15347  363 LDTLNEQydtLENKVAE---RT-------QALAEAKQRAEQANKRKSEHLTTISHEIRTPLNGVLGALELLQ---NTPLT 429
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 531 DDEIELATVIHSSGKDLLTLINDILDLSKVEAGKLDVIFEATNISDMA-ASMHQnfLHIAAQ-KNVEFTVEDSDTIPDLF 608
Cdd:PRK15347  430 AEQMDLADTARQCTLSLLAIINNLLDFSRIESGQMTLSLEETALLPLLdQAMLT--IQGPAQsKSLTLRTFVGAHVPLYL 507
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 609 YTDAKRIEQIIKNLLSNAFKFTEKGSVSLHFDSietsnlshdmqsiSKDWITISVKDTGIGIAKEQHQLIFEAFQQADGA 688
Cdd:PRK15347  508 HLDSLRLRQILVNLLGNAVKFTETGGIRLRVKR-------------HEQQLCFTVEDTGCGIDIQQQQQIFTPFYQADTH 574
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 689 TirkyGGTGLGLSICKEFARLLGGWITLESNVGEGSTF------TVYIPNLP-----------------------NGLTN 739
Cdd:PRK15347  575 S----QGTGLGLTIASSLAKMMGGELTLFSTPGVGSCFslvlplNEYAPPEPlkgelsaplalhrqlsawgitcqPGHQN 650
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 740 IQVSNLEVA-------ATVDEVI---PAEVVEETIVLPetnnvFQEKtILIVDD--DHRNIFALQNALKKHHanIITAQN 807
Cdd:PRK15347  651 PALLDPELAylpgrlyDLLQQIIqgaPNEPVINLPLQP-----WQLQ-ILLVDDveTNRDIIGMMLVELGQQ--VTTAAS 722
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 808 GLECLEILKNNTnIDLILMDIMMPNMDGYETMEHIRMNL-GLH-EIPIIALTAKAMPNDKEKCLSAGASDYISKPLNLHQ 885
Cdd:PRK15347  723 GTEALELGRQHR-FDLVLMDIRMPGLDGLETTQLWRDDPnNLDpDCMIVALTANAAPEEIHRCKKAGMNHYLTKPVTLAQ 801

                  .
gi 2651418669 886 L 886
Cdd:PRK15347  802 L 802
PRK11091 PRK11091
aerobic respiration control sensor protein ArcB; Provisional
489-890 3.78e-58

aerobic respiration control sensor protein ArcB; Provisional


Pssm-ID: 236842 [Multi-domain]  Cd Length: 779  Bit Score: 213.65  E-value: 3.78e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 489 LLRSSKYKSEFLANMSHELRTPLNSILLLSEMLKenhDNHLSDDEIELATVIHSSGKDLLTLINDILDLSKVEAGKLDVI 568
Cdd:PRK11091  276 LEKASRDKTTFISTISHELRTPLNGIVGLSRILL---DTELTAEQRKYLKTIHVSAITLGNIFNDIIDMDKMERRKLQLD 352
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 569 FEATNISDMAASMhQNFLHI-AAQKNVEFTVEDSDTIPDLFYTDAKRIEQIIKNLLSNAFKFTEKGSVSLhfdSIETSNl 647
Cdd:PRK11091  353 NQPIDFTDFLADL-ENLSGLqAEQKGLRFDLEPLLPLPHKVITDGTRLRQILWNLISNAVKFTQQGGVTV---RVRYEE- 427
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 648 shdmqsisKDWITISVKDTGIGIAKEQHQLIFEAFQQA-DGATIRKYGGTGLGLSICKEFARLLGGWITLESNVGEGSTF 726
Cdd:PRK11091  428 --------GDMLTFEVEDSGIGIPEDELDKIFAMYYQVkDSHGGKPATGTGIGLAVSKRLAQAMGGDITVTSEEGKGSCF 499
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 727 TVYIPnlpngltniqvsnlevAATVDEVIPAEVVEETIVLPETNnvfqektILIVDDDHRNIFALQNALKKHHANIITAQ 806
Cdd:PRK11091  500 TLTIH----------------APAVAEEVEDAFDEDDMPLPALN-------ILLVEDIELNVIVARSVLEKLGNSVDVAM 556
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 807 NGLECLEILKNNtNIDLILMDIMMPNMDGYETMEHIRMNLGLHEI-PIIALTAKAMpNDKEKCLSAGASDYISKPLNLHQ 885
Cdd:PRK11091  557 TGKEALEMFDPD-EYDLVLLDIQLPDMTGLDIARELRERYPREDLpPLVALTANVL-KDKKEYLDAGMDDVLSKPLSVPA 634

                  ....*
gi 2651418669 886 LYSVM 890
Cdd:PRK11091  635 LTAMI 639
COG4251 COG4251
Bacteriophytochrome (light-regulated signal transduction histidine kinase) [Signal ...
248-731 4.84e-57

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


Pssm-ID: 443393 [Multi-domain]  Cd Length: 503  Bit Score: 204.63  E-value: 4.84e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 248 LLDEISKREWLQTELAELILMYQGVSSIEMLGNKILSGIIQKTQTSCGAFYVREEVEDTVYYVKKASFAEQGADIGKQSI 327
Cdd:COG4251    35 LLLLALLVLLLLLIRLLLLLLLSLLALLLLLLLLLLLLLVLAALALLLLLLLLELALVLLALLLVLLLLLALLLLLALLL 114
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 328 KMGEGFIGQTALEKKSFILRDIPEEFRYVTTGLLEIRPKNLLVIPVLFEDEVIAVMELVSVTDIsDLHQDLIQQTVDNLG 407
Cdd:COG4251   115 LLELLLLLLALLLLLLLLALLLLEELALLRLALALLLLLLLLLLLLLLLLALILALLLAALAEL-ELLLLLLLVLLLLLL 193
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 408 LTIHSIMGRMRIQTLLYESQAMTEELQVQSEELQTQAEELQMQAEELRTTNEQLESRTEEAEQKTADLQVTKLELEEKAS 487
Cdd:COG4251   194 LLLLLLLLLLRLLLELLLLLEAELLLSLGGGLGLLLLLLLLLVLLLLLILLLLLLILVLELLELRLELEELEEELEERTA 273
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 488 ELLRSSKYKSEFLANMSHELRTPLNSILLLSEMLKENHDNHLSDDEIELATVIHSSGKDLLTLINDILDLSKVEAGKLDv 567
Cdd:COG4251   274 ELERSNEELEQFAYVASHDLREPLRKISGFSQLLEEDYGDKLDEEGREYLERIRDAAERMQALIDDLLAYSRVGRQELE- 352
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 568 iFEATNISDMAASMHQNFLHIAAQKNVEFTVEDSDTIpdlfYTDAKRIEQIIKNLLSNAFKFTEKGSV-SLHFDSIETsn 646
Cdd:COG4251   353 -FEPVDLNELLEEVLEDLEPRIEERGAEIEVGPLPTV----RGDPTLLRQVFQNLISNAIKYSRPGEPpRIEIGAERE-- 425
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 647 lshdmqsisKDWITISVKDTGIGIAKEQHQLIFEAFQQADGAtiRKYGGTGLGLSICKEFARLLGGWITLESNVGEGSTF 726
Cdd:COG4251   426 ---------GGEWVFSVRDNGIGIDPEYAEKIFEIFQRLHSR--DEYEGTGIGLAIVKKIVERHGGRIWVESEPGEGATF 494

                  ....*
gi 2651418669 727 TVYIP 731
Cdd:COG4251   495 YFTLP 499
PRK10841 PRK10841
two-component system sensor histidine kinase RcsC;
479-893 4.15e-53

two-component system sensor histidine kinase RcsC;


Pssm-ID: 182772 [Multi-domain]  Cd Length: 924  Bit Score: 200.20  E-value: 4.15e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 479 KLE--LEEKASELLRSSKYKSEFLANMSHELRTPLNSILLLSEMLKENHdnhLSDDEIELATVIHSSGKDLLTLINDILD 556
Cdd:PRK10841  428 KMEesLQEMAQAAEQASQSKSMFLATVSHELRTPLYGIIGNLDLLQTKE---LPKGVDRLVTAMNNSSSLLLKIISDILD 504
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 557 LSKVEAGKLDVifEATNISDMAASMH--QNFLHIAAQKNVE-FTVEDSDtIPDLFYTDAKRIEQIIKNLLSNAFKFTEKG 633
Cdd:PRK10841  505 FSKIESEQLKI--EPREFSPREVINHitANYLPLVVKKRLGlYCFIEPD-VPVALNGDPMRLQQVISNLLSNAIKFTDTG 581
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 634 SVSLHFdsietsnlshdmqSISKDWITISVKDTGIGI-AKEQHQLiFEAFQQADGATIRKYGGTGLGLSICKEFARLLGG 712
Cdd:PRK10841  582 CIVLHV-------------RVDGDYLSFRVRDTGVGIpAKEVVRL-FDPFFQVGTGVQRNFQGTGLGLAICEKLINMMDG 647
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 713 WITLESNVGEGSTFTVYIP----------NLPN-----------------------GLTNIQVSNLEVAATV-DEVI--- 755
Cdd:PRK10841  648 DISVDSEPGMGSQFTIRIPlygaqypqkkGVEGlqgkrcwlavrnasleqfletllQRSGIQVQRYEGQEPTpEDVLitd 727
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 756 ----------------------PAEVVE-----------------------------ETIVLPETNNVFQEK---TILIV 781
Cdd:PRK10841  728 dpvqkkwqgravitfcrrhigiPLEIAPgewvhstatphelpallariyrielesddSANALPSTDKAVSDNddmMILVV 807
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 782 DDDHRNIFALQNALKKHHANIITAQNGLECLEILKNNTnIDLILMDIMMPNMDGYETMEHIRmNLGlHEIPIIALTAKAM 861
Cdd:PRK10841  808 DDHPINRRLLADQLGSLGYQCKTANDGVDALNVLSKNH-IDIVLTDVNMPNMDGYRLTQRLR-QLG-LTLPVIGVTANAL 884
                         490       500       510
                  ....*....|....*....|....*....|..
gi 2651418669 862 PNDKEKCLSAGASDYISKPLNLHQLYSVMSVW 893
Cdd:PRK10841  885 AEEKQRCLEAGMDSCLSKPVTLDVLKQTLTVY 916
HATPase_EvgS-ArcB-TorS-like cd16922
Histidine kinase-like ATPase domain of two-component sensor histidine kinases, many are hybrid ...
615-731 3.53e-48

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: 166.13  E-value: 3.53e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 615 IEQIIKNLLSNAFKFTEKGSVSLHFDSIETSNlshdmqsiSKDWITISVKDTGIGIAKEQHQLIFEAFQQADGATIRKYG 694
Cdd:cd16922     1 LRQILLNLLGNAIKFTEEGEVTLRVSLEEEEE--------DGVQLRFSVEDTGIGIPEEQQARLFEPFSQADSSTTRKYG 72
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2651418669 695 GTGLGLSICKEFARLLGGWITLESNVGEGSTFTVYIP 731
Cdd:cd16922    73 GTGLGLAISKKLVELMGGDISVESEPGQGSTFTFTLP 109
PRK09959 PRK09959
acid-sensing system histidine kinase EvgS;
482-891 5.45e-47

acid-sensing system histidine kinase EvgS;


Pssm-ID: 182169 [Multi-domain]  Cd Length: 1197  Bit Score: 182.63  E-value: 5.45e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669  482 LEEKASELLRSSKYKSEFLANMSHELRTPLNSILLLSEMLKenhDNHLSDDE-IELATVIHSSGKDLLTLINDILDLSKV 560
Cdd:PRK09959   698 LEVERNKAINATVAKSQFLATMSHEIRTPISSIMGFLELLS---GSGLSKEQrVEAISLAYATGQSLLGLIGEILDVDKI 774
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669  561 EAGKLDVIFEATNISDMAASMHQNFLHIAAQKNVEFTVedSDTIPD--LFYTDAKRIEQIIKNLLSNAFKFTEKGSVSLh 638
Cdd:PRK09959   775 ESGNYQLQPQWVDIPTLVQNTCHSFGAIAASKSIALSC--SSTFPDhyLVKIDPQAFKQVLSNLLSNALKFTTEGAVKI- 851
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669  639 fdsieTSNLSH--DMQSIskdwITISVKDTGIGIAKEQHQLIFEAFQQADGAtiRKYGGTGLGLSICKEFARLLGGWITL 716
Cdd:PRK09959   852 -----TTSLGHidDNHAV----IKMTIMDSGSGLSQEEQQQLFKRYSQTSAG--RQQTGSGLGLMICKELIKNMQGDLSL 920
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669  717 ESNVGEGSTFTVYIPnlpngltniqVSNLEVAATVDevipaEVVEETIVLPEtnnvfqEKTILIVDDDHRNIFALQNALK 796
Cdd:PRK09959   921 ESHPGIGTTFTITIP----------VEISQQVATVE-----AKAEQPITLPE------KLSILIADDHPTNRLLLKRQLN 979
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669  797 KHHANIITAQNGLECLEILkNNTNIDLILMDIMMPNMDGYETMEHIRMNLGlhEIPIIALTAKAMPNDKEKCLSAGASDY 876
Cdd:PRK09959   980 LLGYDVDEATDGVQALHKV-SMQHYDLLITDVNMPNMDGFELTRKLREQNS--SLPIWGLTANAQANEREKGLSCGMNLC 1056
                          410
                   ....*....|....*
gi 2651418669  877 ISKPLNLHQLYSVMS 891
Cdd:PRK09959  1057 LFKPLTLDVLKTHLS 1071
PRK11466 PRK11466
hybrid sensory histidine kinase TorS; Provisional
439-835 2.78e-43

hybrid sensory histidine kinase TorS; Provisional


Pssm-ID: 236914 [Multi-domain]  Cd Length: 914  Bit Score: 170.09  E-value: 2.78e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 439 ELQTQAEELQMQAEELRTTNEQLESRTEEAEQKTADLQVTKLELEEKASELLRSSKYKSEFLANMSHELRTPLNSILLLS 518
Cdd:PRK11466  387 ELDTIGRLMDAFRSNVHALNRHREQLAAQVKARTAELQELVIEHRQARAEAEKASQAKSAFLAAMSHEIRTPLYGILGTA 466
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 519 EMLKENHDNHLSDDEIElatVIHSSGKDLLTLINDILDLSKVEAGKLDVI-----FEATNISDMAASMHQNFLHiaaQKN 593
Cdd:PRK11466  467 QLLADNPALNAQRDDLR---AITDSGESLLTILNDILDYSAIEAGGKNVSvsdepFEPRPLLESTLQLMSGRVK---GRP 540
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 594 VEFTVEDSDTIPDLFYTDAKRIEQIIKNLLSNAFKFTEKGSVSLHFDSIETSnlshdmqsiskdWItISVKDTGIGIAKE 673
Cdd:PRK11466  541 IRLATDIADDLPTALMGDPRRIRQVITNLLSNALRFTDEGSIVLRSRTDGEQ------------WL-VEVEDSGCGIDPA 607
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 674 QHQLIFEAFQQADGatirKYGGTGLGLSICKEFARLLGGWITLESNVGEGSTFTVYIPnlpngltnIQVSNLEVAATVDE 753
Cdd:PRK11466  608 KLAEIFQPFVQVSG----KRGGTGLGLTISSRLAQAMGGELSATSTPEVGSCFCLRLP--------LRVATAPVPKTVNQ 675
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 754 viPAEVVEETIVLPETNNVFQEKTILIvdddhrnifaLQNALKKHHAniitAQNGLECLEILKNNTNIDLILMDIMMPNM 833
Cdd:PRK11466  676 --AVRLDGLRLLLIEDNPLTQRITAEM----------LNTSGAQVVA----VGNAAQALETLQNSEPFAAALVDFDLPDY 739

                  ..
gi 2651418669 834 DG 835
Cdd:PRK11466  740 DG 741
CheY COG0784
CheY-like REC (receiver) domain, includes chemotaxis protein CheY and sporulation regulator ...
776-894 4.23e-42

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: 149.62  E-value: 4.23e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 776 KTILIVDDDHRNIFALQNALKKHHANIITAQNGLECLEILKNNTnIDLILMDIMMPNMDGYETMEHIRMNLGLHEIPIIA 855
Cdd:COG0784     6 KRILVVDDNPDNRELLRRLLERLGYEVTTAEDGAEALELLRAGP-PDLILLDINMPGMDGLELLRRIRALPRLPDIPIIA 84
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2651418669 856 LTAKAMPNDKEKCLSAGASDYISKPLNLHQLYSVMSVWL 894
Cdd:COG0784    85 LTAYADEEDRERALEAGADDYLTKPVDPEELLEALRRLL 123
REC_hyHK_CKI1_RcsC-like cd17546
phosphoacceptor receiver (REC) domain of hybrid sensor histidine kinases/response regulators ...
778-890 9.67e-39

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: 139.53  E-value: 9.67e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 778 ILIVDDDHRNIFALQNALKKHHANIITAQNGLECLEILKNNtNIDLILMDIMMPNMDGYETMEHIR-MNLGLHEIPIIAL 856
Cdd:cd17546     1 VLVVDDNPVNRKVLKKLLEKLGYEVDVAENGQEALELLKEE-PFDLVLMDLQMPVMDGLEATRRIReLEGGGRRTPIIAL 79
                          90       100       110
                  ....*....|....*....|....*....|....
gi 2651418669 857 TAKAMPNDKEKCLSAGASDYISKPLNLHQLYSVM 890
Cdd:cd17546    80 TANALEEDREKCLEAGMDDYLSKPVKLDQLKEVL 113
COG4191 COG4191
Signal transduction histidine kinase regulating C4-dicarboxylate transport system [Signal ...
360-731 1.22e-38

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


Pssm-ID: 443345 [Multi-domain]  Cd Length: 361  Bit Score: 147.64  E-value: 1.22e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 360 LLEIRPKNLLVIPVLFEDEVIAVMELVSVTDISDLHQDLIQQTVDNLGLTIHSIMGRMRIQTLLYESQAMTEELQVQSEE 439
Cdd:COG4191    11 LLALLRALALALALLLLLLLLLLALLLLLLALLLALLALLLLLLLLLLLLLLELLLLLLALLGGLLRLLLLLGLLLLLLL 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 440 LQTQAEELQMQAEELRTTNEQLESRTEEAEQKTAdlqvtklELEEKASELLRSSKYKS--EFLANMSHELRTPLNSILLL 517
Cdd:COG4191    91 EALLLLLLAALDAEENAELEELERDITELERAEE-------ELRELQEQLVQSEKLAAlgELAAGIAHEINNPLAAILGN 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 518 SEMLKENHDNHLSDDEI-ELATVIHSSGKDLLTLINDILDLSKVEAGKLdvifEATNISDMAASMHQNFLHIAAQKNVEF 596
Cdd:COG4191   164 AELLRRRLEDEPDPEELrEALERILEGAERAAEIVRSLRAFSRRDEEER----EPVDLNELIDEALELLRPRLKARGIEV 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 597 TVEDSDTIPdLFYTDAKRIEQIIKNLLSN---AFKFTEKGSVSlhfdsIETSnlshdmqsISKDWITISVKDTGIGIAKE 673
Cdd:COG4191   240 ELDLPPDLP-PVLGDPGQLEQVLLNLLINaidAMEEGEGGRIT-----ISTR--------REGDYVVISVRDNGPGIPPE 305
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2651418669 674 QHQLIFEAFqqadgATIRKYG-GTGLGLSICKEFARLLGGWITLESNVGEGSTFTVYIP 731
Cdd:COG4191   306 VLERIFEPF-----FTTKPVGkGTGLGLSISYGIVEKHGGRIEVESEPGGGTTFTITLP 359
PleD COG3706
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate ...
777-886 3.66e-37

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: 137.73  E-value: 3.66e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 777 TILIVDDDHRNIFALQNALKKHHANIITAQNGLECLEILKNNtNIDLILMDIMMPNMDGYETMEHIRMNLGLHEIPIIAL 856
Cdd:COG3706     3 RILVVDDDPTNRKLLRRLLEAAGYEVVEAADGEEALELLQEH-RPDLILLDLEMPDMDGLELCRRLRADPRTADIPIIFL 81
                          90       100       110
                  ....*....|....*....|....*....|
gi 2651418669 857 TAKAMPNDKEKCLSAGASDYISKPLNLHQL 886
Cdd:COG3706    82 TALDDEEDRARALEAGADDYLTKPFDPEEL 111
NtrB COG3852
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms];
406-731 3.27e-36

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


Pssm-ID: 443061 [Multi-domain]  Cd Length: 361  Bit Score: 140.75  E-value: 3.27e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 406 LGLTIHSIMGRmRIQTLLYESQAMTEELQvqseelqtqaeelQMQAEELRTTNEQLESRTEEAEQKTADLQVTKLELEEK 485
Cdd:COG3852    40 LGLSAEELLGR-PLAELFPEDSPLRELLE-------------RALAEGQPVTEREVTLRRKDGEERPVDVSVSPLRDAEG 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 486 AS-----------------ELLRSSKYKS--EFLANMSHELRTPLNSILLLSEMLKENhdnhLSDDEI-ELATVIHSSGK 545
Cdd:COG3852   106 EGgvllvlrditerkrlerELRRAEKLAAvgELAAGLAHEIRNPLTGIRGAAQLLERE----LPDDELrEYTQLIIEEAD 181
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 546 DLLTLINDILDLSKVEAGKldviFEATNISDMAASMHQnFLHIAAQKNVEFTVEDSDTIPDLfYTDAKRIEQIIKNLLSN 625
Cdd:COG3852   182 RLNNLVDRLLSFSRPRPPE----REPVNLHEVLERVLE-LLRAEAPKNIRIVRDYDPSLPEV-LGDPDQLIQVLLNLVRN 255
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 626 AFK-FTEKGSVSLhfdSIETSNLSHDMQSISKDWITISVKDTGIGIAKEQHQLIFEAFQqadgATirKYGGTGLGLSICK 704
Cdd:COG3852   256 AAEaMPEGGTITI---RTRVERQVTLGGLRPRLYVRIEVIDNGPGIPEEILDRIFEPFF----TT--KEKGTGLGLAIVQ 326
                         330       340
                  ....*....|....*....|....*..
gi 2651418669 705 EFARLLGGWITLESNVGEGSTFTVYIP 731
Cdd:COG3852   327 KIVEQHGGTIEVESEPGKGTTFRIYLP 353
HATPase_c smart00387
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.
610-731 2.42e-34

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


Pssm-ID: 214643 [Multi-domain]  Cd Length: 111  Bit Score: 126.99  E-value: 2.42e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669  610 TDAKRIEQIIKNLLSNAFKFTEKG---SVSLHFDsietsnlshdmqsisKDWITISVKDTGIGIAKEQHQLIFEAFQQAD 686
Cdd:smart00387   1 GDPDRLRQVLSNLLDNAIKYTPEGgriTVTLERD---------------GDHVEITVEDNGPGIPPEDLEKIFEPFFRTD 65
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 2651418669  687 GaTIRKYGGTGLGLSICKEFARLLGGWITLESNVGEGSTFTVYIP 731
Cdd:smart00387  66 K-RSRKIGGTGLGLSIVKKLVELHGGEISVESEPGGGTTFTITLP 109
MtrAB_MtrB NF040691
MtrAB system histidine kinase MtrB;
470-731 2.63e-34

MtrAB system histidine kinase MtrB;


Pssm-ID: 468655 [Multi-domain]  Cd Length: 507  Bit Score: 138.23  E-value: 2.63e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 470 QKTADLQVTKLELEEkasellrSSKYKSEFLANMSHELRTPLNSILLLSEMLkenhdnHLSDDEIELAT-----VIHSSG 544
Cdd:NF040691  252 QMADSLQRQIRQLEE-------LSRLQQRFVSDVSHELRTPLTTIRMAADVI------HDSRDDFDPATarsaeLLHTEL 318
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 545 KDLLTLINDILDLSKVEAG--KLDVifEATNISDMAASMHQNFLHIAAQKNVEFTVEDSDTiPDLFYTDAKRIEQIIKNL 622
Cdd:NF040691  319 DRFESLLSDLLEISRFDAGaaELDV--EPVDLRPLVRRVVDALRQLAERAGVELRVDAPGT-PVVAEVDPRRVERVLRNL 395
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 623 LSNAFKFTEKGSVSLHFDSIETSnlshdmqsiskdwITISVKDTGIGIAKEQHQLIFEAFQQADGATIRKYGGTGLGLSI 702
Cdd:NF040691  396 VVNAIEHGEGKPVVVTVAQDDTA-------------VAVTVRDHGVGLKPGEVALVFDRFWRADPARARTTGGTGLGLAI 462
                         250       260
                  ....*....|....*....|....*....
gi 2651418669 703 CKEFARLLGGWITLESNVGEGSTFTVYIP 731
Cdd:NF040691  463 ALEDARLHGGWLEAWGRPGQGSQFRLTLP 491
RpfG COG3437
Response regulator c-di-GMP phosphodiesterase, RpfG family, contains REC and HD-GYP domains ...
771-894 3.96e-34

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: 130.67  E-value: 3.96e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 771 NVFQEKTILIVDDDHRNIFALQNALKKHHANIITAQNGLECLEILKNNTnIDLILMDIMMPNMDGYETMEHIRMNLGLHE 850
Cdd:COG3437     2 RTGQAPTVLIVDDDPENLELLRQLLRTLGYDVVTAESGEEALELLLEAP-PDLILLDVRMPGMDGFELLRLLRADPSTRD 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 2651418669 851 IPIIALTAKAMPNDKEKCLSAGASDYISKPLNLHQLYSVMSVWL 894
Cdd:COG3437    81 IPVIFLTALADPEDRERALEAGADDYLTKPFDPEELLARVRNAL 124
phoR_proteo TIGR02966
phosphate regulon sensor kinase PhoR; Members of this protein family are the regulatory ...
487-730 6.13e-34

phosphate regulon sensor kinase PhoR; Members of this protein family are the regulatory histidine kinase PhoR associated with the phosphate ABC transporter in most Proteobacteria. Related proteins from Gram-positive organisms are not included in this model. The phoR gene usually is adjacent to the response regulator phoB gene (TIGR02154). [Signal transduction, Two-component systems]


Pssm-ID: 274368 [Multi-domain]  Cd Length: 333  Bit Score: 133.49  E-value: 6.13e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 487 SELLRSSKYKSEFLANMSHELRTPLNSILLLSEMLKENHDNHLSDDEIELATvIHSSGKDLLTLINDILDLSKVEAGKLD 566
Cdd:TIGR02966 105 TRLRRLEQMRRDFVANVSHELRTPLTVLRGYLETLADGPDEDPEEWNRALEI-MLEQSQRMQSLVEDLLTLSRLESAASP 183
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 567 VIFEATNISDMAASMHQNFLHIAAQKNVEFTVEDsDTIPDLFyTDAKRIEQIIKNLLSNAFKFT-EKGSVSLHFDSIEts 645
Cdd:TIGR02966 184 LEDEPVDMPALLDHLRDEAEALSQGKNHQITFEI-DGGVDVL-GDEDELRSAFSNLVSNAIKYTpEGGTITVRWRRDG-- 259
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 646 nlshdmqsiskDWITISVKDTGIGIAKEQHQLIFEAFQQADGATIRKYGGTGLGLSICKEFARLLGGWITLESNVGEGST 725
Cdd:TIGR02966 260 -----------GGAEFSVTDTGIGIAPEHLPRLTERFYRVDKSRSRDTGGTGLGLAIVKHVLSRHHARLEIESELGKGST 328

                  ....*
gi 2651418669 726 FTVYI 730
Cdd:TIGR02966 329 FSFIF 333
NtrY COG5000
Signal transduction histidine kinase NtrY involved in nitrogen fixation and metabolism ...
452-731 2.87e-33

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: 133.55  E-value: 2.87e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 452 EELRTTNEQLESRTEEAEQKTADLQVTKLELEEK------ASELLRSSKYKS--EFLANMSHELRTPLNSILLLSEMLKE 523
Cdd:COG5000   149 REALERGWQEEIELTRDGRRTLLVRASPLRDDGYvivfddITELLRAERLAAwgELARRIAHEIKNPLTPIQLSAERLRR 228
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 524 NHDNHLSDDE---IELATVIHSSGKDLLTLINDILDLSKVEAGKLdvifEATNISDMAASMHQNFLHIAAQKNVEFTVED 600
Cdd:COG5000   229 KLADKLEEDRedlERALDTIIRQVDRLKRIVDEFLDFARLPEPQL----EPVDLNELLREVLALYEPALKEKDIRLELDL 304
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 601 SDTIPDLfYTDAKRIEQIIKNLLSNAFKFTEKG---SVSLHFDSietsnlshdmqsiskDWITISVKDTGIGIAKEQHQL 677
Cdd:COG5000   305 DPDLPEV-LADRDQLEQVLINLLKNAIEAIEEGgeiEVSTRRED---------------GRVRIEVSDNGPGIPEEVLER 368
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2651418669 678 IFEAFqqadgATIRKyGGTGLGLSICKEFARLLGGWITLESNVGEGSTFTVYIP 731
Cdd:COG5000   369 IFEPF-----FTTKP-KGTGLGLAIVKKIVEEHGGTIELESRPGGGTTFTIRLP 416
OmpR COG0745
DNA-binding response regulator, OmpR family, contains REC and winged-helix (wHTH) domain ...
776-886 3.43e-32

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: 124.30  E-value: 3.43e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 776 KTILIVDDDHRNIFALQNALKKHHANIITAQNGLECLEILKNNTnIDLILMDIMMPNMDGYETMEHIRMNLglHEIPIIA 855
Cdd:COG0745     2 PRILVVEDDPDIRELLADALEREGYEVDTAADGEEALELLEEER-PDLILLDLMLPGMDGLEVCRRLRARP--SDIPIIM 78
                          90       100       110
                  ....*....|....*....|....*....|.
gi 2651418669 856 LTAKAMPNDKEKCLSAGASDYISKPLNLHQL 886
Cdd:COG0745    79 LTARDDEEDRVRGLEAGADDYLTKPFDPEEL 109
KinE COG5809
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome ...
481-731 1.37e-30

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: 126.63  E-value: 1.37e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 481 ELEEKASELLRSSKYK--SEFLANMSHELRTPLNSIL----LLSEMLKENHDNHLSddeielatVIHSSGKDLLTLINDI 554
Cdd:COG5809   253 ERKKLEELLRKSEKLSvvGELAAGIAHEIRNPLTSLKgfiqLLKDTIDEEQKTYLD--------IMLSELDRIESIISEF 324
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 555 LDLSKVEAGKldviFEATNISDMaasMHQNFLHIAAQ---KNVEFTVEDSDTIPDLfYTDAKRIEQIIKNLLSNAFKFTE 631
Cdd:COG5809   325 LVLAKPQAIK----YEPKDLNTL---IEEVIPLLQPQallKNVQIELELEDDIPDI-LGDENQLKQVFINLLKNAIEAMP 396
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 632 KGSvslhfdsietsNLSHDMQSISKDWITISVKDTGIGIAKEQHQLIFEAFqqadgATiRKYGGTGLGLSICKEFARLLG 711
Cdd:COG5809   397 EGG-----------NITIETKAEDDDKVVISVTDEGCGIPEERLKKLGEPF-----YT-TKEKGTGLGLMVSYKIIEEHG 459
                         250       260
                  ....*....|....*....|
gi 2651418669 712 GWITLESNVGEGSTFTVYIP 731
Cdd:COG5809   460 GKITVESEVGKGTTFSITLP 479
HATPase_c pfam02518
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the ...
610-731 1.50e-30

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: 115.93  E-value: 1.50e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 610 TDAKRIEQIIKNLLSNAFKFT---EKGSVSLHFDsietsnlshdmqsiskDWITISVKDTGIGIAKEQHQLIFEAFQQAD 686
Cdd:pfam02518   1 GDELRLRQVLSNLLDNALKHAakaGEITVTLSEG----------------GELTLTVEDNGIGIPPEDLPRIFEPFSTAD 64
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 2651418669 687 gatIRKYGGTGLGLSICKEFARLLGGWITLESNVGEGSTFTVYIP 731
Cdd:pfam02518  65 ---KRGGGGTGLGLSIVRKLVELLGGTITVESEPGGGTTVTLTLP 106
HK_WalK NF033092
cell wall metabolism sensor histidine kinase WalK; This model describes WalK as found in ...
498-731 1.53e-30

cell wall metabolism sensor histidine kinase WalK; This model describes WalK as found in Staphylococcus aureus (sp|Q2G2U4.1|WALK_STAA8). A shorter version, as found in Streptococcus pneumoniae, called WalK(Spn) or VicK, is not included. WalK is part of a two-component system and works with partner protein WalR.


Pssm-ID: 467964 [Multi-domain]  Cd Length: 594  Bit Score: 127.95  E-value: 1.53e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 498 EFLANMSHELRTPLNSILLLSEMLKenhDNHLSDDEI--ELATVIHSSGKDLLTLINDILDLSKVEAGKLDVIFEATNIS 575
Cdd:NF033092  374 EFVANVSHELRTPLTTMRSYLEALA---DGAWKDPELapRFLGVTQNETERMIRLVNDLLQLSRMDSKDYKLNKEWVNFN 450
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 576 DMAASMHQNFLHIAAQKNVEFTVEdsdtIP--DLF-YTDAKRIEQIIKNLLSNAFKFT-EKGSVSLHFdsIETSNLshdm 651
Cdd:NF033092  451 EFFNYIIDRFEMILKNKNITFKRE----FPkrDLWvEIDTDKITQVLDNIISNAIKYSpEGGTITFRL--LETHNR---- 520
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 652 qsiskdwITISVKDTGIGIAKEQHQLIFEAFQQADGATIRKYGGTGLGLSICKEFARLLGGWITLESNVGEGSTFTVYIP 731
Cdd:NF033092  521 -------IIISISDQGLGIPKKDLDKIFDRFYRVDKARSRKMGGTGLGLAIAKEVVEAHGGRIWAESEEGKGTTIYFTLP 593
REC_OmpR cd17574
phosphoacceptor receiver (REC) domain of OmpR family response regulators; OmpR-like proteins ...
779-880 1.94e-30

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: 115.20  E-value: 1.94e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 779 LIVDDDHRNIFALQNALKKHHANIITAQNGLECLEILKNNtNIDLILMDIMMPNMDGYETMEHIRMNLglHEIPIIALTA 858
Cdd:cd17574     1 LVVEDDEEIAELLSDYLEKEGYEVDTAADGEEALELAREE-QPDLIILDVMLPGMDGFEVCRRLREKG--SDIPIIMLTA 77
                          90       100
                  ....*....|....*....|..
gi 2651418669 859 KAMPNDKEKCLSAGASDYISKP 880
Cdd:cd17574    78 KDEEEDKVLGLELGADDYITKP 99
REC_PA4781-like cd19920
phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase PA4781 and similar ...
778-880 1.19e-29

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: 113.37  E-value: 1.19e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 778 ILIVDDDHRNIFALQNALKKHHANIITAQNGLECLEILKNNtNIDLILMDIMMPNMDGYETMEHIRMNLGLHEIPIIALT 857
Cdd:cd19920     1 ILIVDDVPDNLRLLSELLRAAGYRVLVATDGQQALQRAQAE-PPDLILLDVMMPGMDGFEVCRRLKADPATRHIPVIFLT 79
                          90       100
                  ....*....|....*....|...
gi 2651418669 858 AKAMPNDKEKCLSAGASDYISKP 880
Cdd:cd19920    80 ALTDTEDKVKGFELGAVDYITKP 102
REC cd00156
phosphoacceptor receiver (REC) domain of response regulators (RRs) and pseudo response ...
779-880 2.12e-29

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: 112.32  E-value: 2.12e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 779 LIVDDDHRNIFALQNALKKHHANIITAQNGLECLEILKNNtNIDLILMDIMMPNMDGYETMEHIRMNlgLHEIPIIALTA 858
Cdd:cd00156     1 LIVDDDPAIRELLKSLLEREGYEVDTAADGEEALELLREE-RPDLVLLDLMMPGMDGLELLRKLREL--PPDIPVIVLTA 77
                          90       100
                  ....*....|....*....|..
gi 2651418669 859 KAMPNDKEKCLSAGASDYISKP 880
Cdd:cd00156    78 KADEEDAVRALELGADDYLVKP 99
Response_reg pfam00072
Response regulator receiver domain; This domain receives the signal from the sensor partner in ...
778-886 5.74e-29

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: 111.47  E-value: 5.74e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 778 ILIVDDDHRNIFALQNALKKHHANIITAQNGLECLEILKNNTnIDLILMDIMMPNMDGYETMEHIRmNLGlHEIPIIALT 857
Cdd:pfam00072   1 VLIVDDDPLIRELLRQLLEKEGYVVAEADDGKEALELLKEER-PDLILLDINMPGMDGLELLKRIR-RRD-PTTPVIILT 77
                          90       100
                  ....*....|....*....|....*....
gi 2651418669 858 AKAMPNDKEKCLSAGASDYISKPLNLHQL 886
Cdd:pfam00072  78 AHGDEDDAVEALEAGADDFLSKPFDPDEL 106
REC_DivK-like cd17548
phosphoacceptor receiver (REC) domain of DivK and similar proteins; Caulobacter crescentus ...
777-889 2.88e-28

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: 109.94  E-value: 2.88e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 777 TILIVDDDHRNIFALQNALKKHHANIITAQNGLECLEILKNNTnIDLILMDIMMPNMDGYETMEHIRMNLGLHEIPIIAL 856
Cdd:cd17548     1 KILIVEDNPLNMKLARDLLESAGYEVLEAADGEEALEIARKEK-PDLILMDIQLPGMDGLEATRLLKEDPATRDIPVIAL 79
                          90       100       110
                  ....*....|....*....|....*....|...
gi 2651418669 857 TAKAMPNDKEKCLSAGASDYISKPLNLHQLYSV 889
Cdd:cd17548    80 TAYAMKGDREKILEAGCDGYISKPIDTREFLET 112
KinD COG5808
Sporulation sensor histidine kinase D [Cell cycle control, cell division, chromosome ...
461-731 1.23e-27

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


Pssm-ID: 444510 [Multi-domain]  Cd Length: 454  Bit Score: 117.16  E-value: 1.23e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 461 LESRTEEAEQKTADLQVTKLELeekasellrsskyKSEFLANMSHELRTPLNSILLLSEMLKENHDNHLSDDEIElatVI 540
Cdd:COG5808   219 LLKRKTLLERVIQEINTQKLEL-------------IGTFAASTAHEIRNPLTSIKGFIQLLQEKYPELEDQKYFD---II 282
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 541 HSSGKDLLTLINDILDLSKVEAGKLdvifEATNISDMAASMHQNFLHIAAQKNVEFTVEDSDTiPDLFYTDAKRIEQIIK 620
Cdd:COG5808   283 QEEIQRINQIVSEFLVLGKPTAKKL----ELDDLNELIEEILSIIDSEANLKNIRVEKQSLDE-PLHIKCDKDRIKQVLL 357
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 621 NLLSNAFKFTEKGSVSLhfdsIETSNLshdmqsisKDWITISVKDTGIGIAKEQHQLIFEAFqqadgaTIRKYGGTGLGL 700
Cdd:COG5808   358 NLIKNAIEAMKEGGKLT----ISIEND--------DEKAVIEVIDNGEGIPEDIIDEIFEPF------VTTKEGGTGLGL 419
                         250       260       270
                  ....*....|....*....|....*....|.
gi 2651418669 701 SICKEFARLLGGWITLESNVGEGSTFTVYIP 731
Cdd:COG5808   420 SVCKRIVEMHGGEIDIESEEGKGTTFTIRLP 450
REC_2_DhkD-like cd17580
second phosphoacceptor receiver (REC) domain of Dictyostelium discoideum hybrid signal ...
778-886 1.44e-27

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: 107.54  E-value: 1.44e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 778 ILIVDD--DHRNIFALqnALKKHHANIITAQNGLECLEILKNNTnIDLILMDIMMPNMDGYETMEHIRMNLGLHEIPIIA 855
Cdd:cd17580     1 ILVVDDneDAAEMLAL--LLELEGAEVTTAHSGEEALEAAQRFR-PDVILSDIGMPGMDGYELARRLRELPWLANTPAIA 77
                          90       100       110
                  ....*....|....*....|....*....|.
gi 2651418669 856 LTAKAMPNDKEKCLSAGASDYISKPLNLHQL 886
Cdd:cd17580    78 LTGYGQPEDRERALEAGFDAHLVKPVDPDEL 108
REC_D1_PleD-like cd17538
first (D1) phosphoacceptor receiver (REC) domain of response regulator PleD and similar ...
777-880 4.46e-27

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: 106.04  E-value: 4.46e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 777 TILIVDDDHRNIFALQNALKKHHANIITAQNGLECLEILKNNTnIDLILMDIMMPNMDGYETMEHIRMNLGLHEIPIIAL 856
Cdd:cd17538     1 KILVVDDEPANRELLEALLSAEGYEVLTADSGQEALALAEEEL-PDLILLDVMMPGMDGFEVCRRLKEDPETRHIPVIMI 79
                          90       100
                  ....*....|....*....|....
gi 2651418669 857 TAKAMPNDKEKCLSAGASDYISKP 880
Cdd:cd17538    80 TALDDREDRIRGLEAGADDFLSKP 103
HATPase_TutC-TodS-like cd16925
Histidine kinase-like ATPase domain of hybrid sensor histidine kinases similar to Pseudomonas ...
611-731 1.76e-26

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: 104.50  E-value: 1.76e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 611 DAKRIEQIIKNLLSNAFKFT-EKGSVSLhfdSIETSNLSHdmqsiskdwITISVKDTGIGIAKEQHQLIFEAFQQADGAT 689
Cdd:cd16925     1 DAEKYERVVLNLLSNAFKFTpDGGRIRC---ILEKFRLNR---------FLLTVSDSGPGIPPNLREEIFERFRQGDGSS 68
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 2651418669 690 IRKYGGTGLGLSICKEFARLLGGWITLESNVGEGSTFTVYIP 731
Cdd:cd16925    69 TRAHGGTGLGLSIVKEFVELHGGTVTVSDAPGGGALFQVELP 110
REC_RpfG-like cd17551
phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase response regulator ...
777-882 1.78e-24

phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase response regulator RpfG and similar proteins; Cyclic di-GMP phosphodiesterase response regulator RpfG, together with sensory/regulatory protein RpfC, constitute a two-component system implicated in sensing and responding to the diffusible signal factor (DSF) that is essential for cell-cell signaling. RpfC is a hybrid sensor/histidine kinase that phosphorylates and activates RpfG, which degrades cyclic di-GMP to GMP, leading to the activation of Clp, a global transcriptional regulator that regulates a large set of genes in the DSF pathway. RpfG contains a CheY-like receiver domain attached to a histidine-aspartic acid-glycine-tyrosine-proline (HD-GYP) cyclic di-GMP phosphodiesterase domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381103 [Multi-domain]  Cd Length: 118  Bit Score: 99.05  E-value: 1.78e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 777 TILIVDDDHRNIFALQNALKKH-HANIITAQNGLECLEILKNNTnIDLILMDIMMPNMDGYETMEHIRMNLGLHEIPIIA 855
Cdd:cd17551     2 RILIVDDNPTNLLLLEALLRSAgYLEVVSFTDPREALAWCRENP-PDLILLDYMMPGMDGLEFIRRLRALPGLEDVPIVM 80
                          90       100
                  ....*....|....*....|....*..
gi 2651418669 856 LTAKAMPNDKEKCLSAGASDYISKPLN 882
Cdd:cd17551    81 ITADTDREVRLRALEAGATDFLTKPFD 107
AtoC COG2204
DNA-binding transcriptional response regulator, NtrC family, contains REC, AAA-type ATPase, ...
774-886 8.26e-24

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


Pssm-ID: 441806 [Multi-domain]  Cd Length: 418  Bit Score: 105.05  E-value: 8.26e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 774 QEKTILIVDDDHRNIFALQNALKKHHANIITAQNGLECLEILKNNtNIDLILMDIMMPNMDGYETMEHIRMNLglHEIPI 853
Cdd:COG2204     1 SMARILVVDDDPDIRRLLKELLERAGYEVETAASGEEALALLREE-PPDLVLLDLRMPGMDGLELLRELRALD--PDLPV 77
                          90       100       110
                  ....*....|....*....|....*....|...
gi 2651418669 854 IALTAKAMPNDKEKCLSAGASDYISKPLNLHQL 886
Cdd:COG2204    78 ILLTGYGDVETAVEAIKAGAFDYLTKPFDLEEL 110
PRK09303 PRK09303
histidine kinase;
420-731 3.01e-23

histidine kinase;


Pssm-ID: 236462 [Multi-domain]  Cd Length: 380  Bit Score: 102.72  E-value: 3.01e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 420 QTLLYESQAMTEELQVQSEELQTQAEELQMQAE--ELRTTNEQLESRTeeaeqktadlqvtkleleekasellrssKYKS 497
Cdd:PRK09303  101 QEGATYSGLGENLQPSEIDSGRYSQELLQLSDElfVLRQENETLLEQL----------------------------KFKD 152
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 498 EFLANMSHELRTPLNSILLLSEMLKENHDNHLSDDEIELAT----VIHSSGKDLLTLINDILDLSKVEAGKLDVIFEATN 573
Cdd:PRK09303  153 RVLAMLAHDLRTPLTAASLALETLELGQIDEDTELKPALIEqlqdQARRQLEEIERLITDLLEVGRTRWEALRFNPQKLD 232
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 574 ISDMAASMHQNFLHIAAQKNVEFTvedSDTIPDL--FYTDAKRIEQIIKNLLSNAFKFTEKGsvslhfDSIETSNLSHDM 651
Cdd:PRK09303  233 LGSLCQEVILELEKRWLAKSLEIQ---TDIPSDLpsVYADQERIRQVLLNLLDNAIKYTPEG------GTITLSMLHRTT 303
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 652 QsiskdWITISVKDTGIGIAKEQHQLIFEA---FQQADGATirkygGTGLGLSICKEFARLLGGWITLESNVGEGSTFTV 728
Cdd:PRK09303  304 Q-----KVQVSICDTGPGIPEEEQERIFEDrvrLPRDEGTE-----GYGIGLSVCRRIVRVHYGQIWVDSEPGQGSCFHF 373

                  ...
gi 2651418669 729 YIP 731
Cdd:PRK09303  374 TLP 376
YesN COG4753
Two-component response regulator, YesN/AraC family, consists of REC and AraC-type DNA-binding ...
777-880 3.68e-23

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


Pssm-ID: 443786 [Multi-domain]  Cd Length: 103  Bit Score: 94.84  E-value: 3.68e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 777 TILIVDDDHRNIFALQNALKKH--HANIITAQNGLECLEILKNNtNIDLILMDIMMPNMDGYETMEHIRMNlgLHEIPII 854
Cdd:COG4753     1 KVLIVDDEPLIREGLKRILEWEagFEVVGEAENGEEALELLEEH-KPDLVITDINMPGMDGLELLEAIREL--DPDTKII 77
                          90       100
                  ....*....|....*....|....*.
gi 2651418669 855 ALTAKAMPNDKEKCLSAGASDYISKP 880
Cdd:COG4753    78 ILSGYSDFEYAQEAIKLGADDYLLKP 103
REC_Rcp-like cd17557
phosphoacceptor receiver (REC) domain of cyanobacterial phytochrome response regulator Rcp and ...
777-886 4.19e-23

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


Pssm-ID: 381108 [Multi-domain]  Cd Length: 129  Bit Score: 95.56  E-value: 4.19e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 777 TILIVDDDHRNIFALQNALKKHH--ANIITAQNGLECLEIL------KNNTNIDLILMDIMMPNMDGYETMEHIRMNLGL 848
Cdd:cd17557     1 TILLVEDNPGDAELIQEAFKEAGvpNELHVVRDGEEALDFLrgegeyADAPRPDLILLDLNMPRMDGFEVLREIKADPDL 80
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2651418669 849 HEIPIIALTAKAMPNDKEKCLSAGASDYISKPLNLHQL 886
Cdd:cd17557    81 RRIPVVVLTTSDAEEDIERAYELGANSYIVKPVDFEEF 118
pleD PRK09581
response regulator PleD; Reviewed
777-888 1.79e-22

response regulator PleD; Reviewed


Pssm-ID: 236577 [Multi-domain]  Cd Length: 457  Bit Score: 101.52  E-value: 1.79e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 777 TILIVDDDHRNIFALQNALKKHHANIITAQNGLECLEILKNnTNIDLILMDIMMPNMDGYETMEHIRMNLGLHEIPIIAL 856
Cdd:PRK09581    4 RILVVDDIPANVKLLEAKLLAEYYTVLTASSGAEAIAICER-EQPDIILLDVMMPGMDGFEVCRRLKSDPATTHIPVVMV 82
                          90       100       110
                  ....*....|....*....|....*....|..
gi 2651418669 857 TAKAMPNDKEKCLSAGASDYISKPLNLHQLYS 888
Cdd:PRK09581   83 TALDDPEDRVRGLEAGADDFLTKPINDVALFA 114
REC_Ycf29 cd19927
phosphoacceptor receiver (REC) domain of probable transcriptional regulator Ycf29; Ycf29 is a ...
778-880 3.00e-22

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: 92.06  E-value: 3.00e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 778 ILIVDDDHRNIFALQNALKKHHANIITAQNGLECLEILkNNTNIDLILMDIMMPNMDGYETMEHIRMNLGLHEIPIIALT 857
Cdd:cd19927     1 ILLVDDDPGIRLAVKDYLEDQGFTVIAASNGLEALDLL-NQYIPDLIISDIIMPGVDGYSLLGKLRKNADFDTIPVIFLT 79
                          90       100
                  ....*....|....*....|...
gi 2651418669 858 AKAMPNDKEKCLSAGASDYISKP 880
Cdd:cd19927    80 AKGMTSDRIKGYNAGCDGYLSKP 102
CitB COG4565
DNA-binding response regulator DpiB of citrate/malate metabolism [Transcription, Signal ...
777-886 5.73e-22

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


Pssm-ID: 443622 [Multi-domain]  Cd Length: 138  Bit Score: 92.73  E-value: 5.73e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 777 TILIVDDDHRNIFALQNALKKH--HANIITAQNGLECLEILKNNtNIDLILMDIMMPNMDGYETMEHIRMNLglHEIPII 854
Cdd:COG4565     5 RVLIVEDDPMVAELLRRYLERLpgFEVVGVASSGEEALALLAEH-RPDLILLDIYLPDGDGLELLRELRARG--PDVDVI 81
                          90       100       110
                  ....*....|....*....|....*....|..
gi 2651418669 855 ALTAKAMPNDKEKCLSAGASDYISKPLNLHQL 886
Cdd:COG4565    82 VITAARDPETVREALRAGVVDYLIKPFTFERL 113
cztS_silS_copS TIGR01386
heavy metal sensor kinase; Members of this family contain a sensor histidine kinase domain ...
497-731 7.03e-22

heavy metal sensor kinase; Members of this family contain a sensor histidine kinase domain (pfam00512) and a domain found in bacterial signal proteins (pfam00672). This group is separated phylogenetically from related proteins with similar architecture and contains a number of proteins associated with heavy metal resistance efflux systems for copper, silver, cadmium, and/or zinc.


Pssm-ID: 273593 [Multi-domain]  Cd Length: 457  Bit Score: 99.77  E-value: 7.03e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 497 SEFLANMSHELRTPLNSILLLSEMLkenhdnhLSDDEI--ELATVIHSSGKDL--LT-LINDILDLSKVEAGKLDVIFEA 571
Cdd:TIGR01386 242 SQFSADLAHELRTPLTNLLGQTQVA-------LSQPRTgeEYREVLESNLEELerLSrMVSDMLFLARADNGQLALERVR 314
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 572 TNISDMAASMHQNFLHIAAQKNVEFTVEDSDTIPdlfyTDAKRIEQIIKNLLSNAFKFTEKGS---VSLHFDSIETsnls 648
Cdd:TIGR01386 315 LDLAAELAKVAEYFEPLAEERGVRIRVEGEGLVR----GDPQMFRRAISNLLSNALRHTPDGGtitVRIERRSDEV---- 386
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 649 hdmqsiskdwiTISVKDTGIGIAKEQHQLIFEAFQQADGATIRKYGGTGLGLSICKEFARLLGGWITLESNVGEgSTFTV 728
Cdd:TIGR01386 387 -----------RVSVSNPGPGIPPEHLSRLFDRFYRVDPARSNSGEGTGLGLAIVRSIMEAHGGRASAESPDGK-TRFIL 454

                  ...
gi 2651418669 729 YIP 731
Cdd:TIGR01386 455 RFP 457
BaeS_SmeS NF012163
sensor histidine kinase efflux regulator BaeS;
486-731 3.90e-21

sensor histidine kinase efflux regulator BaeS;


Pssm-ID: 411086 [Multi-domain]  Cd Length: 457  Bit Score: 97.59  E-value: 3.90e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 486 ASELLRSSKYKSEFLANMSHELRTPL----NSILLLSEMLKENHDNHLSDDEIELATvihssgkdLLTLINDILDLSKVE 561
Cdd:NF012163  230 ASTLEKNEQMRRDFMADISHELRTPLavlrAELEAIQDGIRKFTPESLDSLQAEVGT--------LTKLVDDLHDLSMSD 301
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 562 AGKLDVIFEATNISDMAASMHQNFLHIAAQKNVEFTVEDSDTIpdLFYTDAKRIEQIIKNLLSNAFKFTEKGSvSLHFDS 641
Cdd:NF012163  302 EGALAYQKASVDLVPLLEVEGGAFRERFASAGLELEVSLPDSS--LVFGDRDRLMQLFNNLLENSLRYTDSGG-SLHISA 378
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 642 IETsnlshdmqsiSKDWiTISVKDTGIGIAKEQHQLIFEAFQQADGATIRKYGGTGLGLSICKEFARLLGGWITLESNVG 721
Cdd:NF012163  379 SQR----------PKEV-TLTVADSAPGVSDEQLARLFERFYRVEVSRNRASGGSGLGLAISLNIVQAHGGTLHAAHSPL 447
                         250
                  ....*....|
gi 2651418669 722 EGSTFTVYIP 731
Cdd:NF012163  448 GGLRIVVTLP 457
REC_RR468-like cd17552
phosphoacceptor receiver (REC) domain of Thermotoga maritima response regulator RR468 and ...
776-882 4.36e-21

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: 89.53  E-value: 4.36e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 776 KTILIVDDDHRNIFALQNALKKHHA-NIITAQNGLECLEILKNNTnIDLILMDIMMPNMDGYETMEHIRMNLGLHEIPII 854
Cdd:cd17552     2 KRILVIDDEEDIREVVQACLEKLAGwEVLTASSGQEGLEKAATEQ-PDAILLDVMMPDMDGLATLKKLQANPETQSIPVI 80
                          90       100
                  ....*....|....*....|....*...
gi 2651418669 855 ALTAKAMPNDKEKCLSAGASDYISKPLN 882
Cdd:cd17552    81 LLTAKAQPSDRQRFASLGVAGVIAKPFD 108
HATPase_FilI-like cd16921
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
615-731 6.44e-21

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: 88.54  E-value: 6.44e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 615 IEQIIKNLLSNAFKFTEKGSVS-LHFDSIETSNlshdmqsiskDWiTISVKDTGIGIAKEQHQLIFEAFQQADGATirKY 693
Cdd:cd16921     1 LGQVLTNLLGNAIKFRRPRRPPrIEVGAEDVGE----------EW-TFYVRDNGIGIDPEYAEKVFGIFQRLHSRE--EY 67
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2651418669 694 GGTGLGLSICKEFARLLGGWITLESNVGEGSTFTVYIP 731
Cdd:cd16921    68 EGTGVGLAIVRKIIERHGGRIWLESEPGEGTTFYFTLP 105
REC_OmpR_PrrA-like cd17627
phosphoacceptor receiver (REC) domain of PrrA-like OmpR family response regulators; The ...
778-886 1.67e-19

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: 84.74  E-value: 1.67e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 778 ILIVDDDHRNIFALQNALKKHHANIITAQNGLECLEILKNNtNIDLILMDIMMPNMDGYETMEHIRMnlGLHEIPIIALT 857
Cdd:cd17627     1 ILVVDDDRAVRESLRRSLRFEGYEVETAVDGAEALRVISGN-RPDAVVLDVMMPRLDGLEVCRRLRA--AGNDLPILVLT 77
                          90       100
                  ....*....|....*....|....*....
gi 2651418669 858 AKAMPNDKEKCLSAGASDYISKPLNLHQL 886
Cdd:cd17627    78 ARDSVSDRVAGLDAGADDYLVKPFALEEL 106
REC_OmpR_BsPhoP-like cd19937
phosphoacceptor receiver (REC) domain of BsPhoP-like OmpR family response regulators; Bacillus ...
779-886 2.17e-19

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: 84.63  E-value: 2.17e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 779 LIVDDDHRNIFALQNALKKHHANIITAQNGLECLEILKNNtNIDLILMDIMMPNMDGYETMEHIRMNLGLHEIPIIALTA 858
Cdd:cd19937     1 LVVDDEEDIVELLKYNLEKEGYEVVTAYDGEEALKRAKDE-KPDLIILDLMLPGIDGLEVCRILRSDPKTSSIPIIMLTA 79
                          90       100
                  ....*....|....*....|....*...
gi 2651418669 859 KAMPNDKEKCLSAGASDYISKPLNLHQL 886
Cdd:cd19937    80 KGEEFDKVLGLELGADDYITKPFSPREL 107
PRK11360 PRK11360
two-component system sensor histidine kinase AtoS;
498-731 2.77e-19

two-component system sensor histidine kinase AtoS;


Pssm-ID: 236901 [Multi-domain]  Cd Length: 607  Bit Score: 92.72  E-value: 2.77e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 498 EFLANMSHELRTPLNSILLLSEMLKENHDNHLSddEIELATVIHSSGKdLLTLINDILDLSKVEAGKldviFEATNISDM 577
Cdd:PRK11360  392 ELVAGVAHEIRNPLTAIRGYVQIWRQQTSDPPS--QEYLSVVLREVDR-LNKVIDQLLEFSRPRESQ----WQPVSLNAL 464
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 578 AASMHQNFLHIAAQKNVEFTVEDSDTIPdLFYTDAKRIEQIIKNLLSNAFK-FTEKGSVSlhfdsIETsnlshdmQSISK 656
Cdd:PRK11360  465 VEEVLQLFQTAGVQARVDFETELDNELP-PIWADPELLKQVLLNILINAVQaISARGKIR-----IRT-------WQYSD 531
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2651418669 657 DWITISVKDTGIGIAKEQHQLIFEAFQQAdgatirKYGGTGLGLSICKEFARLLGGWITLESNVGEGSTFTVYIP 731
Cdd:PRK11360  532 GQVAVSIEDNGCGIDPELLKKIFDPFFTT------KAKGTGLGLALSQRIINAHGGDIEVESEPGVGTTFTLYLP 600
PRK10549 PRK10549
two-component system sensor histidine kinase BaeS;
486-731 7.33e-19

two-component system sensor histidine kinase BaeS;


Pssm-ID: 182539 [Multi-domain]  Cd Length: 466  Bit Score: 90.46  E-value: 7.33e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 486 ASELLRSSKYKSEFLANMSHELRTPLnSIL-----LLSEMLKENHDNHLSDDEIELATvihssgkdLLTLINDILDLSKV 560
Cdd:PRK10549  230 ASTLEKNEQMRRDFMADISHELRTPL-AVLrgeleAIQDGVRKFTPESVASLQAEVGT--------LTKLVDDLHQLSLS 300
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 561 EAGKLDVIFEATNISDMAASMHQNFLHIAAQKNVEFTVEDSDTIPdlFYTDAKRIEQIIKNLLSNAFKFTEKGSvSLHFd 640
Cdd:PRK10549  301 DEGALAYRKTPVDLVPLLEVAGGAFRERFASRGLTLQLSLPDSAT--VFGDPDRLMQLFNNLLENSLRYTDSGG-SLHI- 376
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 641 sieTSNLSHDMQSIskDWitisvKDTGIGIAKEQHQLIFEAFQQADGATIRKYGGTGLGLSICKEFARLLGGWITLESNV 720
Cdd:PRK10549  377 ---SAEQRDKTLRL--TF-----ADSAPGVSDEQLQKLFERFYRTEGSRNRASGGSGLGLAICLNIVEAHNGRIIAAHSP 446
                         250
                  ....*....|.
gi 2651418669 721 GEGSTFTVYIP 731
Cdd:PRK10549  447 FGGVSITVELP 457
REC_OmpR_CusR-like cd19935
phosphoacceptor receiver (REC) domain of CusR-like OmpR family response regulators; ...
778-880 9.78e-19

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: 82.10  E-value: 9.78e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 778 ILIVDDDHRNIFALQNALKKHHANIITAQNGLECLEILKNNtNIDLILMDIMMPNMDGYETMEHIRMNLglHEIPIIALT 857
Cdd:cd19935     1 ILVVEDEKKLAEYLKKGLTEEGYAVDVAYDGEDGLHLALTN-EYDLIILDVMLPGLDGLEVLRRLRAAG--KQTPVLMLT 77
                          90       100
                  ....*....|....*....|...
gi 2651418669 858 AKAMPNDKEKCLSAGASDYISKP 880
Cdd:cd19935    78 ARDSVEDRVKGLDLGADDYLVKP 100
PRK10955 PRK10955
envelope stress response regulator transcription factor CpxR;
778-886 3.82e-18

envelope stress response regulator transcription factor CpxR;


Pssm-ID: 182864 [Multi-domain]  Cd Length: 232  Bit Score: 84.47  E-value: 3.82e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 778 ILIVDDDHRNIFALQNALKKHHANIITAQNGLECLEILknNTNIDLILMDIMMPNMDGYETMEHIRMNlglHEIPIIALT 857
Cdd:PRK10955    4 ILLVDDDRELTSLLKELLEMEGFNVIVAHDGEQALDLL--DDSIDLLLLDVMMPKKNGIDTLKELRQT---HQTPVIMLT 78
                          90       100
                  ....*....|....*....|....*....
gi 2651418669 858 AKAMPNDKEKCLSAGASDYISKPLNLHQL 886
Cdd:PRK10955   79 ARGSELDRVLGLELGADDYLPKPFNDREL 107
REC_CheY4-like cd17562
phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY4 and similar CheY ...
776-889 1.17e-17

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: 79.65  E-value: 1.17e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 776 KTILIVDDDHRNIFALQNALKKHHANIITAQNGLECLEILKNnTNIDLILMDIMMPNMDGYETMEHIRMNLGLHEIPIIA 855
Cdd:cd17562     1 KKILAVDDSASIRQMVSFTLRGAGYEVVEAADGRDALSKAQS-KKFDLIITDQNMPNMDGIELIKELRKLPAYKFTPILM 79
                          90       100       110
                  ....*....|....*....|....*....|....
gi 2651418669 856 LTAKAMPNDKEKCLSAGASDYISKPLNLHQLYSV 889
Cdd:cd17562    80 LTTESSDEKKQEGKAAGATGWLVKPFDPEQLLEV 113
REC_CheC-like cd17593
phosphoacceptor receiver (REC) domain of uncharacterized response regulators containing a CheC ...
776-889 1.24e-17

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


Pssm-ID: 381124 [Multi-domain]  Cd Length: 117  Bit Score: 79.50  E-value: 1.24e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 776 KTILIVDDD---HRnifALQNALKKH-HANIITAQNGLECLEILKNNtNIDLILMDIMMPNMDGYETMEHIRMNlgLHEI 851
Cdd:cd17593     1 MKVLICDDSsmaRK---QLARALPADwDVEITFAENGEEALEILREG-RIDVLFLDLTMPVMDGYEVLEALPVE--QLET 74
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2651418669 852 PIIALTAKAMPNDKEKCLSAGASDYISKPLNLHQLYSV 889
Cdd:cd17593    75 KVIVVSGDVQPEAKERVLELGALAFLKKPFDPEKLAQL 112
CHASE3 pfam05227
CHASE3 domain; CHASE3 is an extracellular sensory domain, which is present in various classes ...
46-172 1.46e-17

CHASE3 domain; CHASE3 is an extracellular sensory domain, which is present in various classes of transmembrane receptors that are parts of signal transduction pathways in bacteria. Specifically, CHASE3 domains are found in histidine kinases, adenylate cyclases, methyl-accepting chemotaxis proteins and predicted diguanylate cyclases/phosphodiesterases. This domain recognizes pyrene (Matilla et al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).


Pssm-ID: 428379  Cd Length: 138  Bit Score: 80.05  E-value: 1.46e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669  46 IDHDFKVLNLTNQVEKELLTIENKAKGFITSNDANYVQSLNAAEKDYEKHYQDLFALLEDNPSQQEKLKQINENITNWIN 125
Cdd:pfam05227   5 VEHTQEVLAALEQLLSALVDAETGQRGYLLTGDESFLEPYEEARAAIPELLARLRALTADNPEQQQRLERLEALIEQKLA 84
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2651418669 126 kEIHPLITNNNSNNVQAI--------DTTQIQSLQSQVTNFRSVEEQLTKKRAAQ 172
Cdd:pfam05227  85 -ELEPTIALRREGGLEAAlalvrsdeGKRLMDAIRALLAEMKAEERRLLEQRTAE 138
REC_ETR-like cd19933
phosphoacceptor receiver (REC) domain of plant ethylene receptors ETR1, ETR2, and EIN4, and ...
778-890 1.78e-17

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


Pssm-ID: 381160 [Multi-domain]  Cd Length: 117  Bit Score: 78.98  E-value: 1.78e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 778 ILIVDDDHRNIFALQNALKKHHANIITAQNGLECLEILKN-NTNIDLILMDIMMPNMDGYETMEHIRMNLGLHEIP-IIA 855
Cdd:cd19933     3 VLLVDDNAVNRMVTKGLLEKLGCEVTTVSSGEECLNLLASaEHSFQLVLLDLCMPEMDGFEVALRIRKLFGRRERPlIVA 82
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2651418669 856 LTAKAMPNDKEKCLSAGASDYISKPLNLHQLYSVM 890
Cdd:cd19933    83 LTANTDDSTREKCLSLGMNGVITKPVSLHALGDEL 117
REC_OmpR_PhoB cd17618
phosphoacceptor receiver (REC) domain of PhoB response regulator from the OmpR family; The ...
776-886 1.90e-17

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: 78.83  E-value: 1.90e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 776 KTILIVDDDH--RNIFALqnALKKHHANIITAQNGLECLEILKNnTNIDLILMDIMMPNMDGYETMEHIRMNLGLHEIPI 853
Cdd:cd17618     1 RTILIVEDEPaiREMIAF--NLERAGFDVVEAEDAESAVNLIVE-PRPDLILLDWMLPGGSGIQFIRRLKRDEMTRDIPI 77
                          90       100       110
                  ....*....|....*....|....*....|...
gi 2651418669 854 IALTAKAMPNDKEKCLSAGASDYISKPLNLHQL 886
Cdd:cd17618    78 IMLTARGEEEDKVRGLEAGADDYITKPFSPREL 110
CitA COG3290
Sensor histidine kinase DipB regulating citrate/malate metabolism [Signal transduction ...
589-731 3.81e-17

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


Pssm-ID: 442519 [Multi-domain]  Cd Length: 389  Bit Score: 84.51  E-value: 3.81e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 589 AAQKNVEFTVEDSDTIPDLFYTDAKrIEQIIKNLLSNAFKFTEKGSVSLHFDSIETSnlshdmqsISKDWITISVKDTGI 668
Cdd:COG3290   257 ARERGIDLTIDIDSDLPDLPLSDTD-LVTILGNLLDNAIEAVEKLPEEERRVELSIR--------DDGDELVIEVEDSGP 327
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2651418669 669 GIAKEQHQLIFEafqqaDGATIRKYGGTGLGLSICKEFARLLGGWITLESNVGEGSTFTVYIP 731
Cdd:COG3290   328 GIPEELLEKIFE-----RGFSTKLGEGRGLGLALVKQIVEKYGGTIEVESEEGEGTVFTVRLP 385
REC_OmpR_DrrD-like cd17625
phosphoacceptor receiver (REC) domain of DrrD-like OmpR family response regulators; DrrD is a ...
779-886 4.57e-17

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: 77.65  E-value: 4.57e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 779 LIVDDDHRNIFALQNALKKHHANIITAQNGLECLEILKNNtNIDLILMDIMMPNMDGYETMEHIRMNlgLHEIPIIALTA 858
Cdd:cd17625     1 LVVEDEKDLSEAITKHLKKEGYTVDVCFDGEEGLEYALSG-IYDLIILDIMLPGMDGLEVLKSLREE--GIETPVLLLTA 77
                          90       100
                  ....*....|....*....|....*...
gi 2651418669 859 KAMPNDKEKCLSAGASDYISKPLNLHQL 886
Cdd:cd17625    78 LDAVEDRVKGLDLGADDYLPKPFSLAEL 105
REC_OmpR_MtPhoP-like cd17615
phosphoacceptor receiver (REC) domain of MtPhoP-like OmpR family response regulators; ...
777-886 6.01e-17

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


Pssm-ID: 381131 [Multi-domain]  Cd Length: 118  Bit Score: 77.39  E-value: 6.01e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 777 TILIVDDDHRNIFALQNALKKHHANIITAQNGLECLEILKNnTNIDLILMDIMMPNMDGYETMEHIRMNLglHEIPIIAL 856
Cdd:cd17615     1 RVLVVDDEPNITELLSMALRYEGWDVETAADGAEALAAARE-FRPDAVVLDIMLPDMDGLEVLRRLRADG--PDVPVLFL 77
                          90       100       110
                  ....*....|....*....|....*....|
gi 2651418669 857 TAKAMPNDKEKCLSAGASDYISKPLNLHQL 886
Cdd:cd17615    78 TAKDSVEDRIAGLTAGGDDYVTKPFSLEEV 107
PRK10490 PRK10490
sensor protein KdpD; Provisional
479-731 8.59e-17

sensor protein KdpD; Provisional


Pssm-ID: 236701 [Multi-domain]  Cd Length: 895  Bit Score: 85.47  E-value: 8.59e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 479 KLELEEkasELLRSSkykseFLANMSHELRTPLNSILLLSEML-------KENHDNHLSddeiELATVIHSSGKdlltLI 551
Cdd:PRK10490  655 RLASER---EQLRNA-----LLAALSHDLRTPLTVLFGQAEILtldlaseGSPHARQAS----EIRQQVLNTTR----LV 718
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 552 NDILDLSKVEAGKLDVIFEATNISDMAASMHQNFLHIAAQKNVEFTVEDSDTipdLFYTDAKRIEQIIKNLLSNAFKFT- 630
Cdd:PRK10490  719 NNLLDMARIQSGGFNLRKEWLTLEEVVGSALQMLEPGLSGHPINLSLPEPLT---LIHVDGPLFERVLINLLENAVKYAg 795
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 631 EKGSVSLHfdsietsnlshdmQSISKDWITISVKDTGIGIAKEQHQLIFEAFQQADG-ATIRkygGTGLGLSICKEFARL 709
Cdd:PRK10490  796 AQAEIGID-------------AHVEGERLQLDVWDNGPGIPPGQEQLIFDKFARGNKeSAIP---GVGLGLAICRAIVEV 859
                         250       260
                  ....*....|....*....|..
gi 2651418669 710 LGGWITLESNVGEGSTFTVYIP 731
Cdd:PRK10490  860 HGGTIWAENRPEGGACFRVTLP 881
CHASE3 COG5278
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
6-509 8.85e-17

Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];


Pssm-ID: 444089 [Multi-domain]  Cd Length: 530  Bit Score: 84.57  E-value: 8.85e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669   6 KFSIRYKIMAGYLVIILFLLISFIMLNNQISNLQKSRNfIIDHDFKVLNLTNQVEKELLTIENKAKGFITSNDANYVQSL 85
Cdd:COG5278     3 NLSIRRKLLLGFALALLLLLVLGVLSYLSLNRLREASE-WVEHTYEVLRALEELLSALLDAETGQRGYLLTGDESFLEPY 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669  86 NAAEKDYEKHYQDLFALLEDNPSQQEKLKQINENITNWINkEIHPLITNNNSNNVQ-AIDTTQIQSLQSQVTNFRSVEEQ 164
Cdd:COG5278    82 EEARAEIDELLAELRSLTADNPEQQARLDELEALIDQWLA-ELEQVIALRRAGGLEaALALVRSGEGKALMDEIRARLLL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 165 LTKKRAAQLDTKNNKLEIWLYSLLFLLSCFAIIVSLYISNSITKTIKNVIQAIKSISSKEKITERIHVNSHDEIKDLAHT 244
Cdd:COG5278   161 LALALAALLLAAAALLLLLLALAALLALAELLLLALARALAALLLLLLLEAELAAAAALLAAAAALAALAALELLAALAL 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 245 TNHLLDEISKREWLQTELAELILMYQGVSSIEMLGNKILSGIIQKTQTSCGAFYVREEVEDTVYYVKKASFAEQGADIGK 324
Cdd:COG5278   241 ALALLLAALLLALLAALALAALLAAALLALAALLLALAAAAALAAAAALELAAAEALALAELELELLLAAAAAAAAAAAA 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 325 QSIKMGEGFIGQTALEKKSFILRDIPEEFRYVTTGLLEIRPKNLLVIPVLFEDEVIAVMELVSVTDISDLHQDLIQQTVD 404
Cdd:COG5278   321 AAAALAALLALALATALAAAAAALALLAALLAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVELEVLAIAAAAA 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 405 NLGLTIHSIMGRMRIQTLLYESQAMTEELQVQSEELQTQAEELQMQAEELRTTNEQLESRTEEAEQKTADLQVTKLELEE 484
Cdd:COG5278   401 AAAAEAAAAAAAAAAASAAEALELAEALAEALALAEEEALALAAASSELAEAGAALALAAAEALAEELAAVAALAALAAA 480
                         490       500
                  ....*....|....*....|....*
gi 2651418669 485 KASELLRSSKYKSEFLANMSHELRT 509
Cdd:COG5278   481 AAALAEAEAAAALAAAAALSLALAL 505
REC_2_GGDEF cd17544
second phosphoacceptor receiver (REC) domain of uncharacterized GGDEF domain proteins; This ...
778-887 1.03e-16

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


Pssm-ID: 381098 [Multi-domain]  Cd Length: 122  Bit Score: 77.17  E-value: 1.03e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 778 ILIVDDDHRNIFALQNALKKHHANIITAQNGLECLEILKNNTNIDLILMDIMMPNMDGYETMEHIRMNLGLHEIPIIALT 857
Cdd:cd17544     3 VLVVDDSATSRNHLRALLRRHNFQVLEAANGQEALEVLEQHPDIKLVITDYNMPEMDGFELVREIRKKYSRDQLAIIGIS 82
                          90       100       110
                  ....*....|....*....|....*....|
gi 2651418669 858 AKAMPNDKEKCLSAGASDYISKPLNLHQLY 887
Cdd:cd17544    83 ASGDNALSARFIKAGANDFLTKPFLPEEFY 112
REC_CheV-like cd19924
phosphoacceptor receiver (REC) domain of chemotaxis protein CheV and similar proteins; This ...
778-880 1.61e-16

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: 76.26  E-value: 1.61e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 778 ILIVDDDHRNIFALQNALKKHHANIITAQNGLECLEILKN--------NTNIDLILMDIMMPNMDGYETMEHIRMNLGLH 849
Cdd:cd19924     1 ILVVDDSPTARKQLRDLLKNLGFEIAEAVDGEEALNKLENlakegndlSKELDLIITDIEMPKMDGYELTFELRDDPRLA 80
                          90       100       110
                  ....*....|....*....|....*....|.
gi 2651418669 850 EIPIIALTAKAMPNDKEKCLSAGASDYISKP 880
Cdd:cd19924    81 NIPVILNSSLSGEFSRARGKKVGADAYLAKF 111
HisKA smart00388
His Kinase A (phosphoacceptor) domain; Dimerisation and phosphoacceptor domain of histidine ...
496-563 1.77e-16

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


Pssm-ID: 214644 [Multi-domain]  Cd Length: 66  Bit Score: 74.52  E-value: 1.77e-16
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2651418669  496 KSEFLANMSHELRTPLNSILLLSEMLKenhDNHLSDDEIELATVIHSSGKDLLTLINDILDLSKVEAG 563
Cdd:smart00388   2 KREFLANLSHELRTPLTAIRGYLELLL---DTELSEEQREYLETILREAERLLRLINDLLDLSRIEAG 66
PRK13837 PRK13837
two-component system VirA-like sensor kinase;
504-784 1.93e-16

two-component system VirA-like sensor kinase;


Pssm-ID: 237526 [Multi-domain]  Cd Length: 828  Bit Score: 84.34  E-value: 1.93e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 504 SHELRTPLNSILLLSEML--KENHDNHLSDDeieLATVIHSSGKDLLtLINDILDLSKVEAGKLdVIFEATNISDMAASM 581
Cdd:PRK13837  458 AHNFNNILGAILGYAEMAlnKLARHSRAARY---IDEIISAGARARL-IIDQILAFGRKGERNT-KPFDLSELVTEIAPL 532
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 582 hqnfLHIAAQKNVEFTVeDSDTIPDLFYTDAKRIEQIIKNLLSNAFK-FTEKGSVSLHFDSIETSN---LSHDMQSiSKD 657
Cdd:PRK13837  533 ----LRVSLPPGVELDF-DQDQEPAVVEGNPAELQQVLMNLCSNAAQaMDGAGRVDISLSRAKLRApkvLSHGVLP-PGR 606
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 658 WITISVKDTGIGIAKEQHQLIFEAFqqadgATIRKyGGTGLGLSICKEFARLLGGWITLESNVGEGSTFTVYIPNLPngl 737
Cdd:PRK13837  607 YVLLRVSDTGAGIDEAVLPHIFEPF-----FTTRA-GGTGLGLATVHGIVSAHAGYIDVQSTVGRGTRFDVYLPPSS--- 677
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 2651418669 738 tniqvsnlevaatvdeviPAEVVEETIVLPETNNVFQEKTILIVDDD 784
Cdd:PRK13837  678 ------------------KVPVAPQAFFGPGPLPRGRGETVLLVEPD 706
REC_DC-like cd17534
phosphoacceptor receiver (REC) domain of modulated diguanylate cyclase and similar domains; ...
776-890 2.00e-16

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


Pssm-ID: 381089 [Multi-domain]  Cd Length: 117  Bit Score: 75.91  E-value: 2.00e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 776 KTILIVDDDHrnIFA--LQNALKKH-HANIITAQNGLECLEILKNNTnIDLILMDIMMP-NMDGYETMEHIRMNLGlheI 851
Cdd:cd17534     1 KKILIVEDEA--IIAldLKEILESLgYEVVGIADSGEEAIELAEENK-PDLILMDINLKgDMDGIEAAREIREKFD---I 74
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2651418669 852 PIIALTAKAMPNDKEKCLSAGASDYISKPLNLHQLYSVM 890
Cdd:cd17534    75 PVIFLTAYSDEETLERAKETNPYGYLVKPFNERELKAAI 113
REC_OmpR_YycF-like cd17614
phosphoacceptor receiver (REC) domain of YrcF-like OmpR family response regulators; YycF ...
778-886 2.07e-16

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


Pssm-ID: 381130 [Multi-domain]  Cd Length: 115  Bit Score: 75.92  E-value: 2.07e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 778 ILIVDDDHRNIFALQNALKKHHANIITAQNGLECLEILKNnTNIDLILMDIMMPNMDGYETMEHIRMNlglHEIPIIALT 857
Cdd:cd17614     1 ILVVDDEKPISDILKFNLTKEGYEVVTAYDGREALEKVEE-EQPDLILLDLMLPEKDGLEVCREVRKT---SNVPIIMLT 76
                          90       100
                  ....*....|....*....|....*....
gi 2651418669 858 AKAMPNDKEKCLSAGASDYISKPLNLHQL 886
Cdd:cd17614    77 AKDSEVDKVLGLELGADDYVTKPFSNREL 105
REC_YesN-like cd17536
phosphoacceptor receiver (REC) domain of YesN and related helix-turn-helix containing response ...
778-890 2.13e-16

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


Pssm-ID: 381091 [Multi-domain]  Cd Length: 121  Bit Score: 76.22  E-value: 2.13e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 778 ILIVDDDHRNIFALQNAL--KKHHANII-TAQNGLECLEILKNNtNIDLILMDIMMPNMDGYETMEHIRMNlgLHEIPII 854
Cdd:cd17536     1 VLIVDDEPLIREGLKKLIdwEELGFEVVgEAENGEEALELIEEH-KPDIVITDIRMPGMDGLELIEKIREL--YPDIKII 77
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2651418669 855 ALTAKampNDKE---KCLSAGASDYISKPLNLHQLYSVM 890
Cdd:cd17536    78 ILSGY---DDFEyaqKAIRLGVVDYLLKPVDEEELEEAL 113
Spo0F COG5803
Stage 0 sporulation initiation response regulator Spo0F [Cell cycle control, cell division, ...
776-886 2.36e-16

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


Pssm-ID: 444505 [Multi-domain]  Cd Length: 119  Bit Score: 75.99  E-value: 2.36e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 776 KTILIVDDDH--RNIfaLQNALKKHHANIITAQNGLECLEILKNNtNIDLILMDIMMPNMDGYETMEHIRmNLGLhEIPI 853
Cdd:COG5803     3 KKILIVDDQAgiRML--LKEVLKKEGYEVFQAANGKEALEKVKEL-KPDLVLLDMKMPGMDGIEILKEIK-EIDP-DIPV 77
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2651418669 854 IALTA---KAMPNDKEKclsAGASDYISKPLNLHQL 886
Cdd:COG5803    78 IMMTAygeLDMVEEAKE---LGAKGYFTKPFDIDEL 110
HisKA pfam00512
His Kinase A (phospho-acceptor) domain; dimerization and phospho-acceptor domain of histidine ...
496-563 2.58e-16

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


Pssm-ID: 459839 [Multi-domain]  Cd Length: 66  Bit Score: 73.78  E-value: 2.58e-16
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2651418669 496 KSEFLANMSHELRTPLNSILLLSEMLKENHDNHLSDDEIElatVIHSSGKDLLTLINDILDLSKVEAG 563
Cdd:pfam00512   2 KSEFLANLSHELRTPLTAIRGYLELLRDEKLDEEQREYLE---TILRSAERLLRLINDLLDLSRIEAG 66
REC_hyHK cd17598
phosphoacceptor receiver (REC) domain of uncharacterized hybrid sensor histidine kinase ...
778-888 2.65e-16

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


Pssm-ID: 381128 [Multi-domain]  Cd Length: 118  Bit Score: 75.83  E-value: 2.65e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 778 ILIVDDDHRNIFALQNALKKHHANIITAQNGLECLEILKNNTNiDLILMDIMMPNMDGYETMEHIRMNLGLHEIPIIALT 857
Cdd:cd17598     1 ILIVEDSPTQAEQLKHILEEQGYKVQVARNGREALAMLAEHRP-TLVISDIVMPEMDGYELCRKIKSDPDLKDIPVILLT 79
                          90       100       110
                  ....*....|....*....|....*....|.
gi 2651418669 858 AKAMPNDKEKCLSAGASDYISKPLNLHQLYS 888
Cdd:cd17598    80 TLSDPRDVIRGLECGADNFITKPYDEKYLLS 110
REC_CheB-like cd17541
phosphoacceptor receiver (REC) domain of chemotaxis response regulator protein-glutamate ...
778-880 4.16e-16

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


Pssm-ID: 381096 [Multi-domain]  Cd Length: 125  Bit Score: 75.51  E-value: 4.16e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 778 ILIVDDDH--RNIfaLQNALKKH-HANII-TAQNGLECLEILKNnTNIDLILMDIMMPNMDGYETMEHIRmnlGLHEIPI 853
Cdd:cd17541     3 VLIVDDSAvmRKL--LSRILESDpDIEVVgTARDGEEALEKIKE-LKPDVITLDIEMPVMDGLEALRRIM---AERPTPV 76
                          90       100
                  ....*....|....*....|....*....
gi 2651418669 854 IALTAKAMPNDKE--KCLSAGASDYISKP 880
Cdd:cd17541    77 VMVSSLTEEGAEItlEALELGAVDFIAKP 105
REC_OmpR_CpxR cd17623
phosphoacceptor receiver (REC) domain of CpxR-like OmpR family response regulators; CpxR is ...
778-886 4.89e-16

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: 75.03  E-value: 4.89e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 778 ILIVDDDHRNIFALQNALKKHHANIITAQNGLECLEILkNNTNIDLILMDIMMPNMDGYETMEHIRMNlglHEIPIIALT 857
Cdd:cd17623     1 ILLIDDDRELTELLTEYLEMEGFNVRAAHDGEQGLAAL-LEGSPDLVVLDVMLPKMNGLDVLKELRKT---SQVPVLMLT 76
                          90       100
                  ....*....|....*....|....*....
gi 2651418669 858 AKAMPNDKEKCLSAGASDYISKPLNLHQL 886
Cdd:cd17623    77 ARGDDIDRILGLELGADDYLPKPFNPREL 105
phoR PRK11006
phosphate regulon sensor histidine kinase PhoR;
499-732 5.46e-16

phosphate regulon sensor histidine kinase PhoR;


Pssm-ID: 182895 [Multi-domain]  Cd Length: 430  Bit Score: 81.21  E-value: 5.46e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 499 FLANMSHELRTPLNSILLLSEMLKenhdnhlsDDEIELATvihsSGKDLLT----------LINDILDLSKVEAGKLDVI 568
Cdd:PRK11006  207 FFANVSHELRTPLTVLQGYLEMMQ--------DQPLEGAL----REKALHTmreqtqrmegLVKQLLTLSKIEAAPTIDL 274
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 569 FEATNISDM-------AASMHQNflhiaaQKNVEFTVEDSDTIpdlfYTDAKRIEQIIKNLLSNAFKFTEKGSvslhfdS 641
Cdd:PRK11006  275 NEKVDVPMMlrvlereAQTLSQG------KHTITFEVDNSLKV----FGNEDQLRSAISNLVYNAVNHTPEGT------H 338
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 642 IETS--NLSHDMQsiskdwitISVKDTGIGIAKEQHQLIFEAFQQADGATIRKYGGTGLGLSICKEF-----ARLlggwi 714
Cdd:PRK11006  339 ITVRwqRVPQGAE--------FSVEDNGPGIAPEHIPRLTERFYRVDKARSRQTGGSGLGLAIVKHAlshhdSRL----- 405
                         250
                  ....*....|....*...
gi 2651418669 715 TLESNVGEGSTFTVYIPN 732
Cdd:PRK11006  406 EIESEVGKGTRFSFVLPE 423
HATPase_BaeS-like cd16946
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
611-717 7.34e-16

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: 74.04  E-value: 7.34e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 611 DAKRIEQIIKNLLSNAFKFTEKGSvSLHFDSIETSnlshdmqsiskDWITISVKDTGIGIAKEQHQLIFEAFQQADGATI 690
Cdd:cd16946     1 DRDRLQQLFVNLLENSLRYTDTGG-KLRIRAAQTP-----------QEVRLDVEDSAPGVSDDQLARLFERFYRVESSRN 68
                          90       100
                  ....*....|....*....|....*..
gi 2651418669 691 RKYGGTGLGLSICKEFARLLGGWITLE 717
Cdd:cd16946    69 RASGGSGLGLAICHNIALAHGGTISAE 95
AmiR COG3707
Two-component response regulator, AmiR/NasT family, consists of REC and RNA-binding ...
774-892 2.07e-15

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: 75.38  E-value: 2.07e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 774 QEKTILIVDDDHRNIFALQNALKKH-HANIITAQNGLECLEILKNnTNIDLILMDIMMPNMDGYETMEHIRmnlGLHEIP 852
Cdd:COG3707     2 RGLRVLVVDDEPLRRADLREGLREAgYEVVAEAADGEDAVELVRE-LKPDLVIVDIDMPDRDGLEAARQIS---EERPAP 77
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2651418669 853 IIALTAKAMPNDKEKCLSAGASDYISKPLNLHQLYSVMSV 892
Cdd:COG3707    78 VILLTAYSDPELIERALEAGVSAYLVKPLDPEDLLPALEL 117
PRK10364 PRK10364
two-component system sensor histidine kinase ZraS;
501-731 2.31e-15

two-component system sensor histidine kinase ZraS;


Pssm-ID: 236674 [Multi-domain]  Cd Length: 457  Bit Score: 79.45  E-value: 2.31e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 501 ANMSHELRTPLNSILLLS----EMLKENHDNHlsddeiELATVIHSSGKDLLTLINDILDLSKveagKLDVIFEATNISD 576
Cdd:PRK10364  242 AGVAHEIRNPLSSIKGLAkyfaERAPAGGEAH------QLAQVMAKEADRLNRVVSELLELVK----PTHLALQAVDLND 311
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 577 MAASMHQNFLHIAAQKNVEFTVEDSDTIPdLFYTDAKRIEQIIKNLLSNAFKFTEKGSVsLHFDSIEtsnlshdmqsiSK 656
Cdd:PRK10364  312 LINHSLQLVSQDANSREIQLRFTANDTLP-EIQADPDRLTQVLLNLYLNAIQAIGQHGV-ISVTASE-----------SG 378
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2651418669 657 DWITISVKDTGIGIAKEQHQLIFEAFQQAdgatirKYGGTGLGLSICKEFARLLGGWITLESNVGEGSTFTVYIP 731
Cdd:PRK10364  379 AGVKISVTDSGKGIAADQLEAIFTPYFTT------KAEGTGLGLAVVHNIVEQHGGTIQVASQEGKGATFTLWLP 447
REC_OmpR_KdpE-like cd17620
phosphoacceptor receiver (REC) domain of KdpE-like OmpR family response regulators; KdpE is a ...
778-880 2.47e-15

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: 72.20  E-value: 2.47e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 778 ILIVDDDH--RNifALQNALKKHHANIITAQNGLECLEILKNNtNIDLILMDIMMPNMDGYETMEHIRmnlGLHEIPIIA 855
Cdd:cd17620     1 ILVIEDEPqiRR--FLRTALEAHGYRVFEAETGQEGLLEAATR-KPDLIILDLGLPDMDGLEVIRRLR---EWSAVPVIV 74
                          90       100
                  ....*....|....*....|....*
gi 2651418669 856 LTAKAMPNDKEKCLSAGASDYISKP 880
Cdd:cd17620    75 LSARDEESDKIAALDAGADDYLTKP 99
orf27 CHL00148
Ycf27; Reviewed
769-880 3.11e-15

Ycf27; Reviewed


Pssm-ID: 214376 [Multi-domain]  Cd Length: 240  Bit Score: 76.29  E-value: 3.11e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 769 TNNVFQEKtILIVDDDH--RNIfaLQNALKKHHANIITAQNGLECLEILKNNtNIDLILMDIMMPNMDGYETMEHIRMNl 846
Cdd:CHL00148    1 TMENSKEK-ILVVDDEAyiRKI--LETRLSIIGYEVITASDGEEALKLFRKE-QPDLVILDVMMPKLDGYGVCQEIRKE- 75
                          90       100       110
                  ....*....|....*....|....*....|....
gi 2651418669 847 glHEIPIIALTAKAMPNDKEKCLSAGASDYISKP 880
Cdd:CHL00148   76 --SDVPIIMLTALGDVSDRITGLELGADDYVVKP 107
HATPase_TmoS-FixL-DctS-like cd16920
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
615-731 4.54e-15

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


Pssm-ID: 340397 [Multi-domain]  Cd Length: 104  Bit Score: 71.66  E-value: 4.54e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 615 IEQIIKNLLSNAFKFTEKGSVslhfdsiETSNLSHDMQSISKDWITISVKDTGIGIAKEQHQLIFEAFqqadgaTIRKYG 694
Cdd:cd16920     1 IQQVLINLVRNGIEAMSEGGC-------ERRELTIRTSPADDRAVTISVKDTGPGIAEEVAGQLFDPF------YTTKSE 67
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2651418669 695 GTGLGLSICKEFARLLGGWITLESNVGEGSTFTVYIP 731
Cdd:cd16920    68 GLGMGLSICRSIIEAHGGRLSVESPAGGGATFQFTLP 104
HATPase_DpiB-CitA-like cd16915
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
618-731 4.71e-15

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: 71.55  E-value: 4.71e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 618 IIKNLLSNAFKFT-------EKGSVSLHFDSietsnlshdmqsiskDWITISVKDTGIGIAKEQHQLIFEAfqqadGATI 690
Cdd:cd16915     4 IVGNLIDNALDALaatgapnKQVEVFLRDEG---------------DDLVIEVRDTGPGIAPELRDKVFER-----GVST 63
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 2651418669 691 RKYGGTGLGLSICKEFARLLGGWITLESNVGEGSTFTVYIP 731
Cdd:cd16915    64 KGQGERGIGLALVRQSVERLGGSITVESEPGGGTTFSIRIP 104
REC_CheY_CheY3 cd19923
phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY3 and similar CheY ...
778-886 4.97e-15

phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY3 and similar CheY family proteins; CheY family chemotaxis response regulators (RRs) comprise about 17% of bacterial RRs and almost half of all RRs in archaea. This subfamily contains Vibrio cholerae CheY3, Escherichia coli CheY, and similar CheY family RRs. CheY proteins control bacterial motility and participate in signaling phosphorelays and in protein-protein interactions. CheY RRs contain only the REC domain with no output/effector domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381150 [Multi-domain]  Cd Length: 119  Bit Score: 71.99  E-value: 4.97e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 778 ILIVDDDH--RNIfaLQNALKK-HHANIITAQNGLECLEILKNNtNIDLILMDIMMPNMDGYETMEHIRMNLGLHEIPII 854
Cdd:cd19923     3 VLVVDDFStmRRI--IKNLLKElGFNNVEEAEDGVDALEKLKAG-GFDFVITDWNMPNMDGLELLKTIRADGALSHLPVL 79
                          90       100       110
                  ....*....|....*....|....*....|..
gi 2651418669 855 ALTAKAMPNDKEKCLSAGASDYISKPLNLHQL 886
Cdd:cd19923    80 MVTAEAKKENVIAAAQAGVNNYIVKPFTAATL 111
REC_typeA_ARR cd17581
phosphoacceptor receiver (REC) domain of type A Arabidopsis response regulators (ARRs) and ...
778-883 5.34e-15

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


Pssm-ID: 381119 [Multi-domain]  Cd Length: 122  Bit Score: 72.01  E-value: 5.34e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 778 ILIVDDDHRNIFALQNALKKHHANIITAQNGLECLEIL----------KNNTNIDLILMDIMMPNMDGYETMEHIRMNLG 847
Cdd:cd17581     1 VLAVDDSLVDRKVIERLLRISSCRVTAVDSGKRALEFLgledeedssnFNEPKVNMIITDYCMPGMTGYDLLKKVKESSA 80
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2651418669 848 LHEIPIIALTAKAMPNDKEKCLSAGASDYISKPLNL 883
Cdd:cd17581    81 LKEIPVVIMSSENIPTRISRCLEEGAEDFLLKPVKL 116
HATPase_CpxA-like cd16949
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
615-731 6.97e-15

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: 71.20  E-value: 6.97e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 615 IEQIIKNLLSNAFKFTeKGSVSLHFdsietsnlshdmqSISKDWITISVKDTGIGIAKEQHQLIFEAFQQADGATIRKYG 694
Cdd:cd16949     1 LARALENVLRNALRYS-PSKILLDI-------------SQDGDQWTITITDDGPGVPEDQLEQIFLPFYRVDSARDRESG 66
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2651418669 695 GTGLGLSICKEFARLLGGWITLESNVGEGSTFTVYIP 731
Cdd:cd16949    67 GTGLGLAIAERAIEQHGGKIKASNRKPGGLRVRIWLP 103
PRK13557 PRK13557
histidine kinase; Provisional
600-837 8.70e-15

histidine kinase; Provisional


Pssm-ID: 237425 [Multi-domain]  Cd Length: 540  Bit Score: 78.17  E-value: 8.70e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 600 DSDTIPDLFYT--DAKRIEQIIKNLLSNAFK-FTEKGSVSlhfdsIETSNLSHDMQSI-------SKDWITISVKDTGIG 669
Cdd:PRK13557  261 ETDLAPDLWNCriDPTQAEVALLNVLINARDaMPEGGRVT-----IRTRNVEIEDEDLamyhglpPGRYVSIAVTDTGSG 335
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 670 IAKEQHQLIFEAFqqadgATIRKYG-GTGLGLSICKEFARLLGGWITLESNVGEGSTFTVYIPnlpngltniqvsnleva 748
Cdd:PRK13557  336 MPPEILARVMDPF-----FTTKEEGkGTGLGLSMVYGFAKQSGGAVRIYSEVGEGTTVRLYFP----------------- 393
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 749 aTVDEVIPAEVVEETIVLPETNNvfqeKTILIVDDDHRNIFALQNALKKHHANIITAQNGLECLEILKNNTNIDLILMDI 828
Cdd:PRK13557  394 -ASDQAENPEQEPKARAIDRGGT----ETILIVDDRPDVAELARMILEDFGYRTLVASNGREALEILDSHPEVDLLFTDL 468
                         250
                  ....*....|
gi 2651418669 829 MMP-NMDGYE 837
Cdd:PRK13557  469 IMPgGMNGVM 478
PhoB TIGR02154
phosphate regulon transcriptional regulatory protein PhoB; PhoB is a DNA-binding response ...
776-893 9.74e-15

phosphate regulon transcriptional regulatory protein PhoB; PhoB is a DNA-binding response regulator protein acting with PhoR in a 2-component system responding to phosphate ion. PhoB acts as a positive regulator of gene expression for phosphate-related genes such as phoA, phoS, phoE and ugpAB as well as itself. It is often found proximal to genes for the high-affinity phosphate ABC transporter (pstSCAB; GenProp0190) and presumably regulates these as well. [Regulatory functions, DNA interactions, Signal transduction, Two-component systems]


Pssm-ID: 131209 [Multi-domain]  Cd Length: 226  Bit Score: 74.29  E-value: 9.74e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 776 KTILIVDDDH--RNIFALqnALKKHHANIITAQNGLECLEILKNNTNiDLILMDIMMPNMDGYETMEHIRMNLGLHEIPI 853
Cdd:TIGR02154   3 RRILVVEDEPaiRELIAY--NLEKAGYDVVEAGDGDEALTLINERGP-DLILLDWMLPGTSGIELCRRLRRRPETRAIPI 79
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 2651418669 854 IALTAKAMPNDKEKCLSAGASDYISKPLNLHQLYS-VMSVW 893
Cdd:TIGR02154  80 IMLTARGEEEDRVRGLETGADDYITKPFSPRELLArIKAVL 120
HisKA cd00082
Histidine Kinase A (dimerization/phosphoacceptor) domain; Histidine Kinase A dimers are formed ...
496-559 1.23e-14

Histidine Kinase A (dimerization/phosphoacceptor) domain; Histidine Kinase A dimers are formed through parallel association of 2 domains creating 4-helix bundles; usually these domains contain a conserved His residue and are activated via trans-autophosphorylation by the catalytic domain of the histidine kinase. They subsequently transfer the phosphoryl group to the Asp acceptor residue of a response regulator protein. Two-component signalling systems, consisting of a histidine protein kinase that senses a signal input and a response regulator that mediates the output, are ancient and evolutionarily conserved signaling mechanisms in prokaryotes and eukaryotes.


Pssm-ID: 119399 [Multi-domain]  Cd Length: 65  Bit Score: 69.16  E-value: 1.23e-14
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2651418669 496 KSEFLANMSHELRTPLNSILLLSEMLKENhdNHLSDDEIELATVIHSSGKDLLTLINDILDLSK 559
Cdd:cd00082     4 KGEFLANVSHELRTPLTAIRGALELLEEE--LLDDEEQREYLERIREEAERLLRLINDLLDLSR 65
PRK11100 PRK11100
sensory histidine kinase CreC; Provisional
502-723 1.73e-14

sensory histidine kinase CreC; Provisional


Pssm-ID: 236846 [Multi-domain]  Cd Length: 475  Bit Score: 76.81  E-value: 1.73e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 502 NMSHELRTPLNSILLLSEMLKENHDnhlSDDEIELATVIHSSGKDLLTLINDILDLSKVEAGK-LDVIfEATNISDMAAS 580
Cdd:PRK11100  262 TLTHELKSPLAAIRGAAELLQEDPP---PEDRARFTGNILTQSARLQQLIDRLLELARLEQRQeLEVL-EPVALAALLEE 337
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 581 MHQNFLHIAAQKNVEFTVEDSDT-IP-DLFYtdakrIEQIIKNLLSNAFKFT-EKGSVSLhfdSIETSNlshdmqsiskD 657
Cdd:PRK11100  338 LVEAREAQAAAKGITLRLRPDDArVLgDPFL-----LRQALGNLLDNAIDFSpEGGTITL---SAEVDG----------E 399
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2651418669 658 WITISVKDTGIGI---AKEQhqlIFEAF---QQADGAtiRKygGTGLGLSICKEFARLLGGWITLEsNVGEG 723
Cdd:PRK11100  400 QVALSVEDQGPGIpdyALPR---IFERFyslPRPANG--RK--STGLGLAFVREVARLHGGEVTLR-NRPEG 463
REC_typeB_ARR-like cd17584
phosphoacceptor receiver (REC) domain of type B Arabidopsis response regulators (ARRs) and ...
778-886 3.56e-14

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: 69.58  E-value: 3.56e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 778 ILIVDDDHRNIFALQNALKKHHANIITAQNGLECLEILKNNTN-IDLILMDIMMPNMDGYETMEHIRMNLglhEIPIIAL 856
Cdd:cd17584     1 VLVVDDDPTCLAILKRMLLRCGYQVTTCTDAEEALSMLRENKDeFDLVITDVHMPDMDGFEFLELIRLEM---DLPVIMM 77
                          90       100       110
                  ....*....|....*....|....*....|
gi 2651418669 857 TAKAMPNDKEKCLSAGASDYISKPLNLHQL 886
Cdd:cd17584    78 SADGSTSTVMKGLAHGACDYLLKPVSIEDL 107
REC_HupR-like cd17569
phosphoacceptor receiver (REC) domain of hydrogen uptake protein regulator (HupR) and similar ...
776-843 5.32e-14

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: 68.97  E-value: 5.32e-14
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2651418669 776 KTILIVDDDHRNIFALQNALKKHHANIITAQNGLECLEILKNNtNIDLILMDIMMPNMDGYETMEHIR 843
Cdd:cd17569     1 PTILLVDDEPNILKALKRLLRREGYEVLTATSGEEALEILKQE-PVDVVISDQRMPGMDGAELLKRVR 67
REC_NarL-like cd17535
phosphoacceptor receiver (REC) domain of NarL (Nitrate/Nitrite response regulator L) family ...
778-886 1.09e-13

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


Pssm-ID: 381090 [Multi-domain]  Cd Length: 117  Bit Score: 68.31  E-value: 1.09e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 778 ILIVDDDHrnIF--ALQNALKKHH--ANIITAQNGLECLEILKNNTnIDLILMDIMMPNMDGYETMEHIRmnLGLHEIPI 853
Cdd:cd17535     1 VLIVDDHP--LVreGLRRLLESEPdiEVVGEAADGEEALALLRELR-PDVVLMDLSMPGMDGIEALRRLR--RRYPDLKV 75
                          90       100       110
                  ....*....|....*....|....*....|...
gi 2651418669 854 IALTAKAMPNDKEKCLSAGASDYISKPLNLHQL 886
Cdd:cd17535    76 IVLTAHDDPEYVLRALKAGAAGYLLKDSSPEEL 108
REC_RssB-like cd17555
phosphoacceptor receiver (REC) domain of Pseudomonas aeruginosa RssB and similar domains; ...
776-881 1.16e-13

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


Pssm-ID: 381107 [Multi-domain]  Cd Length: 116  Bit Score: 68.00  E-value: 1.16e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 776 KTILIVDDDH--RNIFALQnaLKKHHANIITAQNGLECLEILKNNTnIDLILMDIMMPNMDGYETMEHIRmnlGLH-EIP 852
Cdd:cd17555     1 ATILVIDDDEvvRESIAAY--LEDSGFQVLQAADGRQGLELFRSEQ-PDLVLCDLRMPEMDGLEVLKQIT---KESpDTP 74
                          90       100
                  ....*....|....*....|....*....
gi 2651418669 853 IIALTAKAMPNDKEKCLSAGASDYISKPL 881
Cdd:cd17555    75 VIVVSGAGVMSDAVEALRLGAWDYLTKPI 103
HATPase_BasS-like cd16940
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
617-723 1.16e-13

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: 68.20  E-value: 1.16e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 617 QIIKNLLSNAFKFTEKGSVSlhfdSIETSNLSHDMqsiskdwitISVKDTGIGIAKEQHQLIFEAFQQADGatiRKYGGT 696
Cdd:cd16940    16 LLLRNLVDNAVRYSPQGSRV----EIKLSADDGAV---------IRVEDNGPGIDEEELEALFERFYRSDG---QNYGGS 79
                          90       100
                  ....*....|....*....|....*..
gi 2651418669 697 GLGLSICKEFARLLGGWITLESNVGEG 723
Cdd:cd16940    80 GLGLSIVKRIVELHGGQIFLGNAQGGG 106
HATPase_CckA-like cd16919
Histidine kinase-like ATPase domain of two-component sensor hybrid histidine kinases, similar ...
616-731 1.21e-13

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: 68.18  E-value: 1.21e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 616 EQIIKNLLSNAFKFTEKGSvSLHFD-SIETSNLSHDMQS---ISKDWITISVKDTGIGIAKEQHQLIFEAFqqadgATIR 691
Cdd:cd16919     2 ELAILNLAVNARDAMPEGG-RLTIEtSNQRVDADYALNYrdlIPGNYVCLEVSDTGSGMPAEVLRRAFEPF-----FTTK 75
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 2651418669 692 KYG-GTGLGLSICKEFARLLGGWITLESNVGEGSTFTVYIP 731
Cdd:cd16919    76 EVGkGTGLGLSMVYGFVKQSGGHLRIYSEPGVGTTVRIYLP 116
REC_OmpR_PmrA-like cd17624
phosphoacceptor receiver (REC) domain of PmrA-like OmpR family response regulators; This ...
778-886 1.39e-13

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


Pssm-ID: 381139 [Multi-domain]  Cd Length: 115  Bit Score: 67.90  E-value: 1.39e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 778 ILIVDDDHRNIFALQNALKKHHANIITAQNGLECLEILKNnTNIDLILMDIMMPNMDGYETMEHIRMNlGLhEIPIIALT 857
Cdd:cd17624     1 ILLVEDDALLGDGLKTGLRKAGYAVDWVRTGAEAEAALAS-GPYDLVILDLGLPDGDGLDLLRRWRRQ-GQ-SLPVLILT 77
                          90       100
                  ....*....|....*....|....*....
gi 2651418669 858 AKAMPNDKEKCLSAGASDYISKPLNLHQL 886
Cdd:cd17624    78 ARDGVDDRVAGLDAGADDYLVKPFALEEL 106
PRK10604 PRK10604
sensor protein RstB; Provisional
488-731 2.44e-13

sensor protein RstB; Provisional


Pssm-ID: 236724 [Multi-domain]  Cd Length: 433  Bit Score: 73.10  E-value: 2.44e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 488 ELLRSSKyksEFLANMSHELRTPLNSILLLSEMLkenhDNhLSDDEIElatVIHSSGKDLLTLINDILDLSKVEAGKLDV 567
Cdd:PRK10604  207 ALIASKK---QLIDGIAHELRTPLVRLRYRLEMS----DN-LSAAESQ---ALNRDIGQLEALIEELLTYARLDRPQNEL 275
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 568 IFEATNISDMAASMHQNFLHIAAQKNVEFtveDSDTIPDLFYTDAKRIEQIIKNLLSNAFKFTEkGSVSLHfdsietsnL 647
Cdd:PRK10604  276 HLSEPDLPAWLSTHLADIQAVTPEKTVRL---DTPHQGDYGALDMRLMERVLDNLLNNALRYAH-SRVRVS--------L 343
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 648 SHDmqsisKDWITISVKDTGIGIAKEQHQLIFEAFQQADGATIRKYGGTGLGLSICKEFARLLGGWITLESNVGEGSTFT 727
Cdd:PRK10604  344 LLD-----GNQACLIVEDDGPGIPPEERERVFEPFVRLDPSRDRATGGCGLGLAIVHSIALAMGGSVNCDESELGGARFS 418

                  ....
gi 2651418669 728 VYIP 731
Cdd:PRK10604  419 FSWP 422
KinA COG5805
Sporulation sensor histidine kinase A (Stage II sporulation protein SpoIIF/SpoIIJ) [Cell cycle ...
485-731 2.55e-13

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: 73.23  E-value: 2.55e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 485 KASELLRSSKYKS---EFLANMSHELRTPLNSI-----LLLSEMLKENHDNHLSDDEIELATVIhssgkdlltlINDILD 556
Cdd:COG5805   273 EAEELMARSEKLSiagQLAAGIAHEIRNPLTSIkgflqLLQPGIEDKEEYFDIMLSELDRIESI----------ISEFLA 342
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 557 LSKVEAgkldVIFEATNISDMAASMHQNFLHIAAQKNVEFTVEDSDTIPDLfYTDAKRIEQIIKNLLSNAFKFTEK-GSV 635
Cdd:COG5805   343 LAKPQA----VNKEKENINELIQDVVTLLETEAILHNIQIRLELLDEDPFI-YCDENQIKQVFINLIKNAIEAMPNgGTI 417
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 636 SLHfdsIETSNlshdmqsiskDWITISVKDTGIGIAKEQHQLIFEAFQQAdgatirKYGGTGLGLSICKEFARLLGGWIT 715
Cdd:COG5805   418 TIH---TEEED----------NSVIIRVIDEGIGIPEERLKKLGEPFFTT------KEKGTGLGLMVSYKIIENHNGTID 478
                         250
                  ....*....|....*.
gi 2651418669 716 LESNVGEGSTFTVYIP 731
Cdd:COG5805   479 IDSKVGKGTTFTITLP 494
AdeS_HK NF012226
two-component sensor histidine kinase AdeS; Mutations in this component of the two-component ...
486-731 4.11e-13

two-component sensor histidine kinase AdeS; Mutations in this component of the two-component regulatory system for the AdeABC efflux pump can confer adaptive resistance to certain antibiotics, including tigecycline.


Pssm-ID: 411090 [Multi-domain]  Cd Length: 353  Bit Score: 71.56  E-value: 4.11e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 486 ASELLRSSKYKSEFLANMSHELRTPlnsILLLSEMLKENHDNHLSDDEIELatvihssgKDLLT-------LINDILDLS 558
Cdd:NF012226  128 AQKLESSVKNAQVWNAAIAHELRTP---ITILQGRLQGILDGVFEPDPALF--------KSLLNqveglshLVEDLRTLS 196
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 559 KVEAGKLDVIFEATNISDMAASMHQNFLHIAAQKNVEFTVEDSDTipdLFYTDAKRIEQIIKNLLSNAFKFTEKGsvslh 638
Cdd:NF012226  197 LVENQQLRLNYESVDLKDSIEKVLKMFEDRLEQAQLTIVLNLTAT---PVFCDRRRIEQVLIALIDNAIRYANAG----- 268
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 639 fdsietsNLSHDMQSISKDWItISVKDTGIGIAKEQHQLIFEAFQQADGATIRKYGGTGLGLSICKEFARLLGGWITLeS 718
Cdd:NF012226  269 -------KLKISSSVIQDDWI-LQIEDEGPGIAEEYQQDLFNPFFRLEQSRNKEFGGTGLGLAVVHAIVIAHKGSIEY-S 339
                         250
                  ....*....|...
gi 2651418669 719 NVGEGSTFTVYIP 731
Cdd:NF012226  340 NSQGNSVFTIKLP 352
REC_OmpR_ChvI-like cd19936
phosphoacceptor receiver (REC) domain of ChvI-like OmpR family response regulators; ...
778-880 5.87e-13

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


Pssm-ID: 381163 [Multi-domain]  Cd Length: 99  Bit Score: 65.54  E-value: 5.87e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 778 ILIVDDDhRNIF-ALQNALKKHHANIITAQNGLECLEILkNNTNIDLILMDIMMPNMDGYETMEHIRMNlglHEIPIIAL 856
Cdd:cd19936     1 IALVDDD-RNILtSVSMALEAEGFSVETYTDGASALDGL-NARPPDLAILDIKMPRMDGMELLQRLRQK---STLPVIFL 75
                          90       100
                  ....*....|....*....|....
gi 2651418669 857 TAKAMPNDKEKCLSAGASDYISKP 880
Cdd:cd19936    76 TSKDDEIDEVFGLRMGADDYITKP 99
REC_TrrA-like cd17554
phosphoacceptor receiver (REC) domain of Thermotoga maritima response regulator TrrA and ...
776-886 6.70e-13

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: 65.71  E-value: 6.70e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 776 KTILIVDDDhRNIFAL-QNALKKHHANIITAQNGLECLEILKNNtNIDLILMDIMMPNMDGYETMEHIRmnlGLH-EIPI 853
Cdd:cd17554     1 KKILVVDDE-ENIRELyKEELEDEGYEVVTAGNGEEALEKLESE-DPDLVILDIKMPGMDGLETLRKIR---EKKpDLPV 75
                          90       100       110
                  ....*....|....*....|....*....|...
gi 2651418669 854 IALTakAMPNDKEKCLSAGASDYISKPLNLHQL 886
Cdd:cd17554    76 IICT--AYSEYKSDFSSWAADAYVVKSSDLTEL 106
HATPase_EcPhoR-like cd16952
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
619-731 1.42e-12

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


Pssm-ID: 340428 [Multi-domain]  Cd Length: 108  Bit Score: 64.92  E-value: 1.42e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 619 IKNLLSNAFKFT-EKGSVSLHFDSIETSnlshdmqsiskdwITISVKDTGIGIAKEQHQLIFEAFQQADGATIRKYGGTG 697
Cdd:cd16952     5 FSNLVSNAVKYTpPSDTITVRWSQEESG-------------ARLSVEDTGPGIPPEHIPRLTERFYRVDIERCRNTGGTG 71
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2651418669 698 LGLSICKEF-----ARLLggwitLESNVGEGSTFTVYIP 731
Cdd:cd16952    72 LGLAIVKHVmsrhdARLL-----IASELGKGSRFTCLFP 105
REC_OmpR_MtrA-like cd17626
phosphoacceptor receiver (REC) domain of MtrA-like OmpR family response regulators; MtrA is ...
778-886 1.70e-12

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: 64.80  E-value: 1.70e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 778 ILIVDDDHRNIFALQNALKKHHANIITAQNGLECLEILKNnTNIDLILMDIMMPNMDGYETMEHIRMNLGlheIPIIALT 857
Cdd:cd17626     3 ILVVDDDAALAEMIGIVLRGEGFDPAFCGDGTQALAAFRE-VRPDLVLLDLMLPGIDGIEVCRQIRAESG---VPIVMLT 78
                          90       100
                  ....*....|....*....|....*....
gi 2651418669 858 AKAMPNDKEKCLSAGASDYISKPLNLHQL 886
Cdd:cd17626    79 AKSDTVDVVLGLESGADDYVAKPFKPKEL 107
ompR PRK09468
osmolarity response regulator; Provisional
778-886 1.75e-12

osmolarity response regulator; Provisional


Pssm-ID: 181883 [Multi-domain]  Cd Length: 239  Bit Score: 68.08  E-value: 1.75e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 778 ILIVDDDHRNIFALQNALKKHHANIITAQNGlECLEILKNNTNIDLILMDIMMPNMDGYETMEHIRMNLglHEIPIIALT 857
Cdd:PRK09468    8 ILVVDDDMRLRALLERYLTEQGFQVRSAANA-EQMDRLLTRESFHLMVLDLMLPGEDGLSICRRLRSQN--NPTPIIMLT 84
                          90       100
                  ....*....|....*....|....*....
gi 2651418669 858 AKAMPNDKEKCLSAGASDYISKPLNLHQL 886
Cdd:PRK09468   85 AKGEEVDRIVGLEIGADDYLPKPFNPREL 113
cpxA PRK09470
envelope stress sensor histidine kinase CpxA;
444-714 2.14e-12

envelope stress sensor histidine kinase CpxA;


Pssm-ID: 236532 [Multi-domain]  Cd Length: 461  Bit Score: 70.35  E-value: 2.14e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 444 AEELQMQAEELRT----TNEQLESRTEEAEQKTADLQVTKLELEEKASellrsskYKSEFLANMSHELRTPLNSILLLSE 519
Cdd:PRK09470  194 ARKLKNAADEVAQgnlrQHPELETGPQEFRQAGASFNQMVTALERMMT-------SQQRLLSDISHELRTPLTRLQLATA 266
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 520 MLKENHDnhlsdDEIELaTVIHSSGKDLLTLINDILDLSKVEAgKLDVIFEATNISDMAASMHQNFLHIAAQKNVEFTVE 599
Cdd:PRK09470  267 LLRRRQG-----ESKEL-ERIETEAQRLDSMINDLLVLSRNQQ-KNHLERETFKANSLWSEVLEDAKFEAEQMGKSLTVS 339
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 600 dsdTIPDLF--YTDAKRIEQIIKNLLSNAFKFTeKGSVSLHFdsietsnlshdmqSISKDWITISVKDTGIGIAKEQHQL 677
Cdd:PRK09470  340 ---APPGPWpiNGNPNALASALENIVRNALRYS-HTKIEVAF-------------SVDKDGLTITVDDDGPGVPEEEREQ 402
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 2651418669 678 IFEAFQQADGATIRKYGGTGLGLSICKEFARLLGGWI 714
Cdd:PRK09470  403 IFRPFYRVDEARDRESGGTGLGLAIVENAIQQHRGWV 439
PRK11361 PRK11361
acetoacetate metabolism transcriptional regulator AtoC;
777-886 3.54e-12

acetoacetate metabolism transcriptional regulator AtoC;


Pssm-ID: 183099 [Multi-domain]  Cd Length: 457  Bit Score: 69.49  E-value: 3.54e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 777 TILIVDDDHRNIFALQNALKKHHANIITAQNGLECLEILKNnTNIDLILMDIMMPNMDGYETMEHIR-MNLGlheIPIIA 855
Cdd:PRK11361    6 RILIVDDEDNVRRMLSTAFALQGFETHCANNGRTALHLFAD-IHPDVVLMDIRMPEMDGIKALKEMRsHETR---TPVIL 81
                          90       100       110
                  ....*....|....*....|....*....|.
gi 2651418669 856 LTAKAMPNDKEKCLSAGASDYISKPLNLHQL 886
Cdd:PRK11361   82 MTAYAEVETAVEALRCGAFDYVIKPFDLDEL 112
REC_PatA-like cd17602
phosphoacceptor receiver (REC) domain of PatA and similar domains; Nostoc sp. (or Anabaena sp.) ...
778-880 4.79e-12

phosphoacceptor receiver (REC) domain of PatA and similar domains; Nostoc sp. (or Anabaena sp.) PatA is necessary for proper patterning of heterocysts along filaments. PatA contains phosphoacceptor REC domain at its C-terminus and an N-terminal PATAN (PatA N-terminus) domain, which was proposed in a bioinformatics study to mediate protein-protein interactions. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays. Some members of this group may have an inactive REC domain, lacking canonical metal-binding and active site residues.


Pssm-ID: 381129 [Multi-domain]  Cd Length: 102  Bit Score: 63.16  E-value: 4.79e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 778 ILIVDDDHRNIFALQNALKKHHANIITAQNGLECLEILKNnTNIDLILMDIMMPNMDGYETMEHIRMNLGLHEIPIIALT 857
Cdd:cd17602     1 VACVDDRPSIQKMIEYFLEKQGFRVVVIDDPLRALTTLLN-SKPDLILIDIDMPDLDGYELCSLLRKSSALKDTPIIMLT 79
                          90       100
                  ....*....|....*....|...
gi 2651418669 858 AKAMPNDKEKCLSAGASDYISKP 880
Cdd:cd17602    80 GKDGLVDRIRAKMAGASGYLTKP 102
LytT COG3279
DNA-binding response regulator, LytR/AlgR family [Transcription, Signal transduction ...
777-890 5.75e-12

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


Pssm-ID: 442510 [Multi-domain]  Cd Length: 235  Bit Score: 66.38  E-value: 5.75e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 777 TILIVDDDHRNIFALQNALKKH-HANII-TAQNGLECLEILKNNtNIDLILMDIMMPNMDGYETMEHIRMNlgLHEIPII 854
Cdd:COG3279     3 KILIVDDEPLARERLERLLEKYpDLEVVgEASNGEEALELLEEH-KPDLVFLDIQMPGLDGFELARQLREL--DPPPPII 79
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2651418669 855 ALTAkampnDKEKCLSA---GASDYISKPLNLHQLYSVM 890
Cdd:COG3279    80 FTTA-----YDEYALEAfevNAVDYLLKPIDEERLAKAL 113
REC_NtrC cd19919
phosphoacceptor receiver (REC) domain of DNA-binding transcriptional regulator NtrC; ...
776-885 6.28e-12

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: 63.06  E-value: 6.28e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 776 KTILIVDDDHRNIFALQNALKKHHANIITAQNGLECLEILKNNTNiDLILMDIMMPNMDGYETMEHIRMNLGlhEIPIIA 855
Cdd:cd19919     1 KTVWIVDDDSSIRWVLERALAGAGLTVTSFENAQEALAALASSQP-DVLISDIRMPGMDGLALLAQIKQRHP--DLPVII 77
                          90       100       110
                  ....*....|....*....|....*....|...
gi 2651418669 856 LTAKAmpnDKEKCLSA---GASDYISKPLNLHQ 885
Cdd:cd19919    78 MTAHS---DLDSAVSAyqgGAFEYLPKPFDIDE 107
HATPase_BceS-YxdK-YvcQ-like cd16948
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
610-731 6.35e-12

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: 63.07  E-value: 6.35e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 610 TDAKRIEQIIKNLLSNAFKFTEKGSvSLHFDSIETsnlshdmqsisKDWITISVKDTGIGIAKEQHQLIFEAFqqADGAT 689
Cdd:cd16948     1 TDAKWLSFIIGQIVSNALKYSKQGG-KIEIYSETN-----------EQGVVLSIKDFGIGIPEEDLPRVFDKG--FTGEN 66
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 2651418669 690 IRKYG-GTGLGLSICKEFARLLGGWITLESNVGEGSTFTVYIP 731
Cdd:cd16948    67 GRNFQeSTGMGLYLVKKLCDKLGHKIDVESEVGEGTTFTITFP 109
HATPase_AtoS-like cd16943
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
615-731 9.88e-12

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: 62.44  E-value: 9.88e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 615 IEQIIKNLLSNAFK-FTEKGSVSlhfdsIETSnLSHDMQsiskdwiTISVKDTGIGIAKEQHQLIFEAFqqadgATIRKY 693
Cdd:cd16943     4 LNQVLLNLLVNAAQaMEGRGRIT-----IRTW-AHVDQV-------LIEVEDTGSGIDPEILGRIFDPF-----FTTKPV 65
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2651418669 694 G-GTGLGLSICKEFARLLGGWITLESNVGEGSTFTVYIP 731
Cdd:cd16943    66 GeGTGLGLSLSYRIIQKHGGTIRVASVPGGGTRFTIILP 104
REC_OmpR_RegX3-like cd17621
phosphoacceptor receiver (REC) domain of RegX3-like OmpR family response regulators; RegX3 is ...
778-880 1.38e-11

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


Pssm-ID: 381136 [Multi-domain]  Cd Length: 99  Bit Score: 61.83  E-value: 1.38e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 778 ILIVDDDHRNIFALQNALKKHHANIITAQNGLECLEILKNNtNIDLILMDIMMPNMDGYETMEHIRmnlGLHEIPIIALT 857
Cdd:cd17621     1 VLVVEDEESFSDPLAYLLRKEGFEVTVATDGPAALAEFDRA-GADIVLLDLMLPGLSGTEVCRQLR---ARSNVPVIMVT 76
                          90       100
                  ....*....|....*....|...
gi 2651418669 858 AKAMPNDKEKCLSAGASDYISKP 880
Cdd:cd17621    77 AKDSEIDKVVGLELGADDYVTKP 99
PRK10365 PRK10365
sigma-54-dependent response regulator transcription factor ZraR;
778-886 1.40e-11

sigma-54-dependent response regulator transcription factor ZraR;


Pssm-ID: 182412 [Multi-domain]  Cd Length: 441  Bit Score: 67.75  E-value: 1.40e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 778 ILIVDDDHRNIFALQNALKKHHANIITAQNGLECLEILKNNTnIDLILMDIMMPNMDGYETMEHIR-MNLGlheIPIIAL 856
Cdd:PRK10365    8 ILVVDDDISHCTILQALLRGWGYNVALANSGRQALEQVREQV-FDLVLCDVRMAEMDGIATLKEIKaLNPA---IPVLIM 83
                          90       100       110
                  ....*....|....*....|....*....|
gi 2651418669 857 TAKAMPNDKEKCLSAGASDYISKPLNLHQL 886
Cdd:PRK10365   84 TAYSSVETAVEALKTGALDYLIKPLDFDNL 113
PRK00742 PRK00742
chemotaxis-specific protein-glutamate methyltransferase CheB;
804-880 1.54e-11

chemotaxis-specific protein-glutamate methyltransferase CheB;


Pssm-ID: 234828 [Multi-domain]  Cd Length: 354  Bit Score: 66.71  E-value: 1.54e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 804 TAQNGLECLEILKNnTNIDLILMDIMMPNMDGYETMEHIrmnLGLHEIPII---ALTAKampNDKE--KCLSAGASDYIS 878
Cdd:PRK00742   34 TAPDGLEAREKIKK-LNPDVITLDVEMPVMDGLDALEKI---MRLRPTPVVmvsSLTER---GAEItlRALELGAVDFVT 106

                  ..
gi 2651418669 879 KP 880
Cdd:PRK00742  107 KP 108
GAF_2 pfam13185
GAF domain; The GAF domain is named after some of the proteins it is found in, including ...
273-411 1.65e-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: 62.48  E-value: 1.65e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 273 SSIEMLGNKILSGIIQKTQTSCGAFYVREEVEDTVyyvkkASFAEQGADIGKQSIKMGEGFIGQTALEKKSFILRDIPEE 352
Cdd:pfam13185   2 ADLEELLDAVLEAAVELGASAVGFILLVDDDGRLA-----AWGGAADELSAALDDPPGEGLVGEALRTGRPVIVNDLAAD 76
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2651418669 353 FRYVTTGLLEIRPKNLLVIPVLFEDEVIAVMELVS--VTDISDLHQDLIQQTVDNLGLTIH 411
Cdd:pfam13185  77 PAKKGLPAGHAGLRSFLSVPLVSGGRVVGVLALGSnrPGAFDEEDLELLELLAEQAAIAIE 137
HATPase_RstB-like cd16939
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
615-731 1.91e-11

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


Pssm-ID: 340416 [Multi-domain]  Cd Length: 104  Bit Score: 61.29  E-value: 1.91e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 615 IEQIIKNLLSNAFKFTEKgsvslhfdSIETSNLshdmqsISKDWITISVKDTGIGIAKEQHQLIFEAFQQADGATIRKYG 694
Cdd:cd16939     1 MARALDNLLRNALRYAHR--------TVRIALL------VSGGRLTLIVEDDGPGIPAAARERVFEPFVRLDPSRDRATG 66
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2651418669 695 GTGLGLSICKEFARLLGGWITLESNVGEGSTFTVYIP 731
Cdd:cd16939    67 GFGLGLAIVHRVALWHGGHVECDDSELGGACFRLTWP 103
REC smart00448
cheY-homologous receiver domain; CheY regulates the clockwise rotation of E. coli flagellar ...
776-831 2.04e-11

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


Pssm-ID: 214668 [Multi-domain]  Cd Length: 55  Bit Score: 59.50  E-value: 2.04e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2651418669  776 KTILIVDDDHRNIFALQNALKKHHANIITAQNGLECLEILKNNtNIDLILMDIMMP 831
Cdd:smart00448   1 MRILVVDDDPLLRELLKALLEKEGYEVDEATDGEEALELLKEE-KPDLILLDIMMP 55
REC_CheY cd17542
phosphoacceptor receiver (REC) domain of chemotaxis protein CheY; The chemotaxis response ...
776-881 3.12e-11

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: 61.14  E-value: 3.12e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 776 KTILIVDDDHRNIFALQNALKKHHANII-TAQNGLECLEILKNnTNIDLILMDIMMPNMDGYETMEHIR-MNLGLHEIPI 853
Cdd:cd17542     1 KKVLIVDDAAFMRMMLKDILTKAGYEVVgEAANGEEAVEKYKE-LKPDLVTMDITMPEMDGIEALKEIKkIDPNAKVIMC 79
                          90       100
                  ....*....|....*....|....*...
gi 2651418669 854 IALTAKAMPNDkekCLSAGASDYISKPL 881
Cdd:cd17542    80 SAMGQEEMVKE---AIKAGAKDFIVKPF 104
REC_OmpR_EcPhoP-like cd19934
phosphoacceptor receiver (REC) domain of EcPhoP-like OmpR family response regulators; ...
778-886 3.50e-11

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: 61.14  E-value: 3.50e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 778 ILIVDDDHRNIFALQNALKKHHANIITAQNGLECLeILKNNTNIDLILMDIMMPNMDGYETMEHIRMNlGlHEIPIIALT 857
Cdd:cd19934     1 LLLVEDDALLAAQLKEQLSDAGYVVDVAEDGEEAL-FQGEEEPYDLVVLDLGLPGMDGLSVLRRWRSE-G-RATPVLILT 77
                          90       100
                  ....*....|....*....|....*....
gi 2651418669 858 AKAMPNDKEKCLSAGASDYISKPLNLHQL 886
Cdd:cd19934    78 ARDSWQDKVEGLDAGADDYLTKPFHIEEL 106
psREC_PRR cd17582
pseudo receiver domain of pseudo-response regulators; In Arabidopsis, five pseudo-response ...
778-880 3.53e-11

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


Pssm-ID: 381120 [Multi-domain]  Cd Length: 104  Bit Score: 60.49  E-value: 3.53e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 778 ILIVDDDHRN---IFALqnaLKKHHANIITAQNGLECLEILKN-NTNIDLILMDIMMPNMDGYETMEHIRMNLGLHEIPI 853
Cdd:cd17582     1 VLLVENDDSTrqiVTAL---LRKCSYEVTAASDGLQAWDVLEDeQNEIDLILTEVDLPVSSGFKLLSYIMRHKICKNIPV 77
                          90       100
                  ....*....|....*....|....*..
gi 2651418669 854 IALTAKAMPNDKEKCLSAGASDYISKP 880
Cdd:cd17582    78 IMMSSQDSVGVVFKCLSKGAADYLVKP 104
REC_OmpR_ArcA_TorR-like cd17619
phosphoacceptor receiver (REC) domain of ArcA- and TorR-like OmpR family response regulators; ...
778-886 3.74e-11

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


Pssm-ID: 381134 [Multi-domain]  Cd Length: 113  Bit Score: 60.86  E-value: 3.74e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 778 ILIVDDDHRNIFALQNALKKHHANIITAQNGLECLEILkNNTNIDLILMDIMMPNMDGYETMEHIRMNlglHEIPIIALT 857
Cdd:cd17619     3 ILIVEDEPVTRATLKSYFEQEGYDVSEAGDGEEMRQIL-ARQDIDLVLLDINLPGKDGLSLTRELREQ---SEVGIILVT 78
                          90       100
                  ....*....|....*....|....*....
gi 2651418669 858 AKAMPNDKEKCLSAGASDYISKPLNLHQL 886
Cdd:cd17619    79 GRDDEVDRIVGLEIGADDYVTKPFNPREL 107
HATPase_VanS-like cd16923
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
621-731 6.30e-11

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Enterococcus faecium VanS; This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component sensor histidine kinase (HKs) such as Enterococcus faecium VanS HK of the VanS-VanR two-component regulatory system (TCS) which activates the transcription of vanH, vanA and vanX vancomycin resistance genes. It also contains Ecoli YedV and PcoS, probable members of YedW-YedV TCS and PcoS-PcoR TCS, repectively. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA); most also have a HAMP sensor domain.


Pssm-ID: 340400 [Multi-domain]  Cd Length: 102  Bit Score: 59.71  E-value: 6.30e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 621 NLLSNAFKFTEKGSVsLHFDSIETSnlshdmqsiskDWITISVKDTGIGIAKEQHQLIFEAFQQADGAtiRKYGGTGLGL 700
Cdd:cd16923     7 NLLSNAIKYSPENTR-IYITSFLTD-----------DVVNIMFKNPSSHPLDFKLEKLFERFYRGDNS--RNTEGAGLGL 72
                          90       100       110
                  ....*....|....*....|....*....|.
gi 2651418669 701 SICKEFARLLGGWITLESNvGEGSTFTVYIP 731
Cdd:cd16923    73 SIAKAIIELHGGSASAEYD-DNHDLFKVRLP 102
REC_OmpR_CtrA cd17616
phosphoacceptor receiver (REC) domain of CtrA-like OmpR family response regulators; CtrA is ...
778-886 7.61e-11

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


Pssm-ID: 381132 [Multi-domain]  Cd Length: 114  Bit Score: 60.12  E-value: 7.61e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 778 ILIVDDDHRNIFALQNALKKHHANIITAQNGLECLEILKNnTNIDLILMDIMMPNMDGYETMEHIRmnLGLHEIPIIALT 857
Cdd:cd17616     1 VLLIEDDSATAQSIELMLKSEGFNVYTTDLGEEGLDLGKL-YDYDIILLDLNLPDMSGYEVLRTLR--LAKVKTPILILS 77
                          90       100
                  ....*....|....*....|....*....
gi 2651418669 858 AKAMPNDKEKCLSAGASDYISKPLNLHQL 886
Cdd:cd17616    78 GLADIEDKVKGLGFGADDYMTKPFHKDEL 106
HATPase_YcbM-like cd16947
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
593-728 8.48e-11

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Bacillus subtilis YcbM; This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component sensor histidine kinase (HKs) such as Bacillus subtilis YcbM, a HK of the two-component system YcbM-YcbL. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA).


Pssm-ID: 340423 [Multi-domain]  Cd Length: 125  Bit Score: 60.22  E-value: 8.48e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 593 NVEFTVEDSdtiPDLFYTDAKRIEQIIKNLLSNAFKFTEKG---SVSLHFDSIEtsnlshdmqsiskdwITISVKDTGIG 669
Cdd:cd16947     2 QVEINIPDR---PIYANANTEALQRILKNLISNAIKYGSDGkflGMTLREDEKH---------------VYIDIWDKGKG 63
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2651418669 670 IAKEQHQLIFEAFQQADGATIRKYGGTGLGLSICKEFARLLGGWITLESNVGEGSTFTV 728
Cdd:cd16947    64 ISETEKDHVFERLYTLEDSRNSAKQGNGLGLTITKRLAESMGGSIYVNSKPYEKTVFTV 122
REC_OmpR_kpRstA-like cd17622
phosphoacceptor receiver (REC) domain of kpRstA-like OmpR family response regulators; ...
778-886 8.76e-11

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


Pssm-ID: 381137 [Multi-domain]  Cd Length: 116  Bit Score: 60.08  E-value: 8.76e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 778 ILIVDDDHRNIFALQNALKKHHANIITAQNGLECLEILKNNTNiDLILMDIMMPNMDGYETMEHIRmnlGLHEIPIIALT 857
Cdd:cd17622     3 ILLVEDDPKLARLIADFLESHGFNVVVEHRGDRALEVIAREKP-DAVLLDIMLPGIDGLTLCRDLR---PKYQGPILLLT 78
                          90       100
                  ....*....|....*....|....*....
gi 2651418669 858 AKAMPNDKEKCLSAGASDYISKPLNLHQL 886
Cdd:cd17622    79 ALDSDIDHILGLELGADDYVVKPVEPAVL 107
REC_PdtaR-like cd19932
phosphoacceptor receiver (REC) domain of PdtaR and similar proteins; This subfamily includes ...
776-892 9.72e-11

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


Pssm-ID: 381159 [Multi-domain]  Cd Length: 118  Bit Score: 59.73  E-value: 9.72e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 776 KTILIVDDDHRNIFALQNALKKHHANII-TAQNGLECLEILKNNtNIDLILMDIMMPNMDGYETMEHIRmnlGLHEIPII 854
Cdd:cd19932     1 VRVLIAEDEALIRMDLREMLEEAGYEVVgEASDGEEAVELAKKH-KPDLVIMDVKMPRLDGIEAAKIIT---SENIAPIV 76
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2651418669 855 ALTAKAMPNDKEKCLSAGASDYISKPLNLHQLYSVMSV 892
Cdd:cd19932    77 LLTAYSQQDLVERAKEAGAMAYLVKPFSESDLIPAIEM 114
HATPase_EnvZ-like cd16950
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
615-731 1.00e-10

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: 59.38  E-value: 1.00e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 615 IEQIIKNLLSNAFKFTeKGSVSLHFDsietsnlshdmqsISKDWITISVKDTGIGIAKEQHQLIFEAFQQADGAtiRKYG 694
Cdd:cd16950     1 LKRVLSNLVDNALRYG-GGWVEVSSD-------------GEGNRTRIQVLDNGPGIAPEEVDELFQPFYRGDNA--RGTS 64
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2651418669 695 GTGLGLSICKEFARLLGGWITLESNVGEGSTFTVYIP 731
Cdd:cd16950    65 GTGLGLAIVQRISDAHGGSLTLANRAGGGLCARIELP 101
PRK09835 PRK09835
Cu(+)/Ag(+) sensor histidine kinase;
496-733 1.13e-10

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


Pssm-ID: 182101 [Multi-domain]  Cd Length: 482  Bit Score: 64.79  E-value: 1.13e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 496 KSEFLANMSHELRTPLNSILLLSEMLkenhdnhLSDD--EIELATVIHSSGKD---LLTLINDILDLSKVEAGKLDVIFE 570
Cdd:PRK09835  262 QSNFSADIAHEIRTPITNLITQTEIA-------LSQSrsQKELEDVLYSNLEEltrMAKMVSDMLFLAQADNNQLIPEKK 334
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 571 ATNISDMAASMHQNFLHIAAQKNVEFTVEDSdtiPDLFYTDAKRIEQIIKNLLSNAFKFTEKG-SVSLHFdsietsnlsh 649
Cdd:PRK09835  335 MLDLADEVGKVFDFFEAWAEERGVELRFVGD---PCQVAGDPLMLRRAISNLLSNALRYTPAGeAITVRC---------- 401
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 650 dmqSISKDWITISVKDTGIGIAKEQHQLIFEAFQQADGATIRKYGGTGLGLSICKEFARLLGGWITLESNVgEGSTFTVY 729
Cdd:PRK09835  402 ---QEVDHQVQLVVENPGTPIAPEHLPRLFDRFYRVDPSRQRKGEGSGIGLAIVKSIVVAHKGTVAVTSDA-RGTRFVIS 477

                  ....
gi 2651418669 730 IPNL 733
Cdd:PRK09835  478 LPRL 481
REC_DctD-like cd17549
phosphoacceptor receiver (REC) domain of C4-dicarboxylic acid transport protein D (DctD) and ...
778-882 1.22e-10

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


Pssm-ID: 381101 [Multi-domain]  Cd Length: 130  Bit Score: 59.81  E-value: 1.22e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 778 ILIVDDDHRNIFALQNALKKHHANIITAQNGLECLEILKNNTNiDLILMDIMMPNMDGYETMEHIR-MNlglHEIPIIAL 856
Cdd:cd17549     1 VLLVDDDADVREALQQTLELAGFRVRAFADAEEALAALSPDFP-GVVISDIRMPGMDGLELLAQIReLD---PDLPVILI 76
                          90       100       110
                  ....*....|....*....|....*....|....
gi 2651418669 857 TA--------KAMpndkekclSAGASDYISKPLN 882
Cdd:cd17549    77 TGhgdvpmavEAM--------RAGAYDFLEKPFD 102
REC_Spo0A cd17561
phosphoacceptor receiver (REC) domain of Spo0A; Spo0A is a response regulator of the ...
778-880 1.25e-10

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


Pssm-ID: 381109 [Multi-domain]  Cd Length: 108  Bit Score: 59.16  E-value: 1.25e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 778 ILIVDDDHRNIFALQNALKKHHANII--TAQNGLECLEILKNnTNIDLILMDIMMPNMDGYETMEHIRMNLGLHEIPIIA 855
Cdd:cd17561     4 VLIADDNREFVQLLEEYLNSQPDMEVvgVAHNGQEALELIEE-KEPDVLLLDIIMPHLDGIGVLEKLRRMRLEKRPKIIM 82
                          90       100
                  ....*....|....*....|....*
gi 2651418669 856 LTAKAMPNDKEKCLSAGASDYISKP 880
Cdd:cd17561    83 LTAFGQEDITQRAVELGASYYILKP 107
envZ PRK09467
osmolarity sensor protein; Provisional
500-704 1.82e-10

osmolarity sensor protein; Provisional


Pssm-ID: 236531 [Multi-domain]  Cd Length: 435  Bit Score: 64.16  E-value: 1.82e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 500 LANMSHELRTPLNSILLLSEMLKENhDNHLSDdeielatvihssgkdllTLINDILDLSKVEAGKLDVI-------FEAT 572
Cdd:PRK09467  233 MAGVSHDLRTPLTRIRLATEMMSEE-DGYLAE-----------------SINKDIEECNAIIEQFIDYLrtgqempMEMA 294
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 573 NISDMAASMhqnflhIAAQKNVEFTVE-DSDTIPDLFYTDAKRIEQIIKNLLSNAFKFTeKG--SVSLHFDsietsnlsh 649
Cdd:PRK09467  295 DLNALLGEV------IAAESGYEREIEtALQPGPIEVPMNPIAIKRALANLVVNAARYG-NGwiKVSSGTE--------- 358
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2651418669 650 dmqsisKDWITISVKDTGIGIAKEQHQLIFEAFQQADGAtiRKYGGTGLGLSICK 704
Cdd:PRK09467  359 ------GKRAWFQVEDDGPGIPPEQLKHLFQPFTRGDSA--RGSSGTGLGLAIVK 405
PRK10610 PRK10610
chemotaxis protein CheY;
779-881 2.07e-10

chemotaxis protein CheY;


Pssm-ID: 170568 [Multi-domain]  Cd Length: 129  Bit Score: 59.22  E-value: 2.07e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 779 LIVDDDHRNIFALQNALKK-HHANIITAQNGLECLEILKNNtNIDLILMDIMMPNMDGYETMEHIRMNLGLHEIPIIALT 857
Cdd:PRK10610    9 LVVDDFSTMRRIVRNLLKElGFNNVEEAEDGVDALNKLQAG-GFGFVISDWNMPNMDGLELLKTIRADGAMSALPVLMVT 87
                          90       100
                  ....*....|....*....|....
gi 2651418669 858 AKAMPNDKEKCLSAGASDYISKPL 881
Cdd:PRK10610   88 AEAKKENIIAAAQAGASGYVVKPF 111
REC_OmpR_BaeR-like cd19938
phosphoacceptor receiver (REC) domain of BaeR-like OmpR family response regulators; BaeR is ...
777-880 2.26e-10

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: 58.54  E-value: 2.26e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 777 TILIVDDDHRNIFALQNALKKHHANIITAQNGLECLEILKNNTNiDLILMDIMMPNMDGYETMEHIRmnlGLHEIPIIAL 856
Cdd:cd19938     1 RILIVEDEPKLAQLLIDYLRAAGYAPTLLAHGDQVLPYVRHTPP-DLILLDLMLPGTDGLTLCREIR---RFSDVPIIMV 76
                          90       100
                  ....*....|....*....|....
gi 2651418669 857 TAKAMPNDKEKCLSAGASDYISKP 880
Cdd:cd19938    77 TARVEEIDRLLGLELGADDYICKP 100
PRK11517 PRK11517
DNA-binding response regulator HprR;
778-886 2.60e-10

DNA-binding response regulator HprR;


Pssm-ID: 183172 [Multi-domain]  Cd Length: 223  Bit Score: 61.45  E-value: 2.60e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 778 ILIVDDDHRNIFALQNALKKHHANIITAQNGLECLEiLKNNTNIDLILMDIMMPNMDGYETMEHIRMnlgLHEIPIIALT 857
Cdd:PRK11517    3 ILLIEDNQRTQEWVTQGLSEAGYVIDAVSDGRDGLY-LALKDDYALIILDIMLPGMDGWQILQTLRT---AKQTPVICLT 78
                          90       100
                  ....*....|....*....|....*....
gi 2651418669 858 AKAMPNDKEKCLSAGASDYISKPLNLHQL 886
Cdd:PRK11517   79 ARDSVDDRVRGLDSGANDYLVKPFSFSEL 107
REC_OmpR_NsrR-like cd18159
phosphoacceptor receiver (REC) domain of Streptococcus agalactiae NsrR-like OmpR family ...
778-880 2.70e-10

phosphoacceptor receiver (REC) domain of Streptococcus agalactiae NsrR-like OmpR family response regulators; Streptococcus agalactiae NsrR is a lantibiotic resistance-associated response regulator and is part of the nisin resistance operon. It is a member of the NsrRK two-component system (TCS) that is involved in the regulation of lantibiotic resistance genes such as a membrane-associated lipoprotein of LanI, and the nsr gene cluster which encodes for the resistance protein NSR and the ABC transporter NsrFP, both conferring resistance against nisin. This subfamily also includes Staphylococcus epidermidis GraR, part of the GraR/GraS TCS involved in resistance against cationic antimicrobial peptides, and Bacillus subtilis BceR, part of the BceS/BceR TCS involved in the regulation of bacitracin resistance. Members of this subfamily belong to the OmpR family of DNA-binding response regulators, which contain N-terminal receiver (REC) and C-terminal DNA-binding winged helix-turn-helix effector domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381143 [Multi-domain]  Cd Length: 113  Bit Score: 58.45  E-value: 2.70e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 778 ILIVDDDHRNIFALQNALKKHHANIITAQNGLECLEILKNnTNIDLILMDIMMPNMDGYETMEHIRMNLglhEIPIIALT 857
Cdd:cd18159     1 ILIVEDDETIASLLKKHLEKWGYEVVLIEDFEDVLEEFLQ-FKPDLVLLDINLPYFDGFYWCREIRQIS---NVPIIFIS 76
                          90       100
                  ....*....|....*....|...
gi 2651418669 858 AKAMPNDKEKCLSAGASDYISKP 880
Cdd:cd18159    77 SRDDNMDQVMAINMGGDDYITKP 99
REC_NtrX-like cd17550
phosphoacceptor receiver (REC) domain of nitrogen assimilation regulatory protein NtrX and ...
778-886 8.21e-10

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: 57.12  E-value: 8.21e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 778 ILIVDDDhRNIFA-LQNALKKHHANIITAQNGLECLEILKNNTnIDLILMDIMMPNMDGYETMEHIRMNlgLHEIPIIAL 856
Cdd:cd17550     1 ILIVDDE-EDIREsLSGILEDEGYEVDTAADGEEALKLIKERR-PDLVLLDIWLPDMDGLELLKEIKEK--YPDLPVIMI 76
                          90       100       110
                  ....*....|....*....|....*....|
gi 2651418669 857 TAKAMPNDKEKCLSAGASDYISKPLNLHQL 886
Cdd:cd17550    77 SGHGTIETAVKATKLGAYDFIEKPLSLDRL 106
PRK10755 PRK10755
two-component system sensor histidine kinase PmrB;
499-717 1.04e-09

two-component system sensor histidine kinase PmrB;


Pssm-ID: 236751 [Multi-domain]  Cd Length: 356  Bit Score: 61.14  E-value: 1.04e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 499 FLANMSHELRTPLNSILLLSEMLKENHdnhlsddEIELATVIhsSGKDLLTL-INDILDLSKVEAGkldviFEATN---- 573
Cdd:PRK10755  140 FTADVAHELRTPLAGIRLHLELLEKQH-------HIDVAPLI--ARLDQMMHtVEQLLQLARAGQS-----FSSGHyqtv 205
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 574 --ISDMAASMHQNFLHIAAQKNVEFTVEDSDTIPDLfYTDAKRIEQIIKNLLSNAFKFTEKGSvslhfdSIETSnLSHDM 651
Cdd:PRK10755  206 klLEDVILPSQDELSEMLEQRQQTLLLPESAADITV-QGDATLLRLLLRNLVENAHRYSPEGS------TITIK-LSQED 277
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2651418669 652 QSISkdwitISVKDTGIGIAKEQHQLIFEAFQQADgatiRKYGGTGLGLSICKEFARLLGGWITLE 717
Cdd:PRK10755  278 GGAV-----LAVEDEGPGIDESKCGELSKAFVRMD----SRYGGIGLGLSIVSRITQLHHGQFFLQ 334
PRK12555 PRK12555
chemotaxis-specific protein-glutamate methyltransferase CheB;
778-880 1.11e-09

chemotaxis-specific protein-glutamate methyltransferase CheB;


Pssm-ID: 237135 [Multi-domain]  Cd Length: 337  Bit Score: 61.05  E-value: 1.11e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 778 ILIVDDDHRNIFALQNALKKH--HANIITAQNGLECLEILKNNTNiDLILMDIMMPNMDGYETMEHIrmnLGLHEIPIIA 855
Cdd:PRK12555    3 IGIVNDSPLAVEALRRALARDpdHEVVWVATDGAQAVERCAAQPP-DVILMDLEMPRMDGVEATRRI---MAERPCPILI 78
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2651418669 856 LTA----------KAMpndkekclSAGASDYISKP 880
Cdd:PRK12555   79 VTSlternasrvfEAM--------GAGALDAVDTP 105
REC_CpdR_CckA-like cd18160
phosphoacceptor receiver (REC) domain of Brucella abortus CpdR and CckA, and similar domains; ...
777-880 1.84e-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: 55.59  E-value: 1.84e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 777 TILIVDDDHRNIFALQNALKKHHANIITAQNGLECLEILKNNTNIDLILMDIMMPNMDGYETMEHIRMnlgLH-EIPIIA 855
Cdd:cd18160     1 TILLADDEPSVRKFIVTTLKKAGYAVTEAESGAEALEKLQQGKDIDIVVTDIVMPEMDGIELAREARK---IDpDVKILF 77
                          90       100
                  ....*....|....*....|....*..
gi 2651418669 856 LT--AKAMPNDKEKclSAGASDYISKP 880
Cdd:cd18160    78 ISggAAAAPELLSD--AVGDNATLKKP 102
PRK10710 PRK10710
DNA-binding transcriptional regulator BaeR; Provisional
766-880 3.34e-09

DNA-binding transcriptional regulator BaeR; Provisional


Pssm-ID: 182665 [Multi-domain]  Cd Length: 240  Bit Score: 58.16  E-value: 3.34e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 766 LPETNNvfqEKTILIVDDDHR----NIFALQNA-LKKHHANiitaqNGLECLEILKNnTNIDLILMDIMMPNMDGYETME 840
Cdd:PRK10710    4 LPIDEN---TPRILIVEDEPKlgqlLIDYLQAAsYATTLLS-----HGDEVLPYVRQ-TPPDLILLDLMLPGTDGLTLCR 74
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2651418669 841 HIRmnlGLHEIPIIALTAKAMPNDKEKCLSAGASDYISKP 880
Cdd:PRK10710   75 EIR---RFSDIPIVMVTAKIEEIDRLLGLEIGADDYICKP 111
REC_OmpR_BfmR-like cd19939
phosphoacceptor receiver (REC) domain of BfmR-like OmpR family response regulators; ...
778-880 3.45e-09

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


Pssm-ID: 381166 [Multi-domain]  Cd Length: 116  Bit Score: 55.46  E-value: 3.45e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 778 ILIVDDDHRNIFALQNALKKHHANIITAQNGLECLEILKNnTNIDLILMDIMMPNMDGYETMEHIRMNlglHEIPIIALT 857
Cdd:cd19939     2 ILIVEDELELARLTRDYLIKAGLEVSVFTDGQRAVRRIID-EQPSLVVLDIMLPGMDGLTVCREVREH---SHVPILMLT 77
                          90       100
                  ....*....|....*....|...
gi 2651418669 858 AKAMPNDKEKCLSAGASDYISKP 880
Cdd:cd19939    78 ARTEEMDRVLGLEMGADDYLCKP 100
PRK11086 PRK11086
sensory histidine kinase DcuS; Provisional
589-731 3.86e-09

sensory histidine kinase DcuS; Provisional


Pssm-ID: 236839 [Multi-domain]  Cd Length: 542  Bit Score: 60.31  E-value: 3.86e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 589 AAQKNVEFTVEDSDTIPDLFytDAKRIEQ---IIKNLLSNAF---KFTEKG--SVSLHFdsietsnlshdmqsiSKDWIT 660
Cdd:PRK11086  407 ARELGITLIISEDSQLPDSG--DEDQVHElitILGNLIENALeavGGEEGGeiSVSLHY---------------RNGWLH 469
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2651418669 661 ISVKDTGIGIAKEQHQLIFEAFQQADGAtirkygGTGLGLSICKEFARLLGGWITLESNVGEGSTFTVYIP 731
Cdd:PRK11086  470 CEVSDDGPGIAPDEIDAIFDKGYSTKGS------NRGVGLYLVKQSVENLGGSIAVESEPGVGTQFFVQIP 534
REC_citrate_TCS cd19925
phosphoacceptor receiver (REC) domain of citrate family two-component system response ...
777-880 5.00e-09

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


Pssm-ID: 381152 [Multi-domain]  Cd Length: 118  Bit Score: 54.94  E-value: 5.00e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 777 TILIVDDDHRNIFALQNALKKH---HAnIITAQNGLECLEILKNnTNIDLILMDIMMPNMDGYETMEHIRMNlgLHEIPI 853
Cdd:cd19925     2 NVLIVEDDPMVAEIHRAYVEQVpgfTV-IGTAGTGEEALKLLKE-RQPDLILLDIYLPDGNGLDLLRELRAA--GHDVDV 77
                          90       100       110
                  ....*....|....*....|....*....|
gi 2651418669 854 IALTAKampNDKE---KCLSAGASDYISKP 880
Cdd:cd19925    78 IVVTAA---NDVEtvrEALRLGVVDYLIKP 104
HATPase_ETR2_ERS2-EIN4-like cd16938
Histidine kinase-like ATPase domain of Arabidopsis thaliana ETR2, ERS2, and EIN4, and related ...
604-730 5.97e-09

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


Pssm-ID: 340415 [Multi-domain]  Cd Length: 133  Bit Score: 55.16  E-value: 5.97e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 604 IPDLFYTDAKRIEQIIKNLLSNAFKFTEKG-----SVSLHFDSIETSNLSHDM--QSISKDWITISVKdtgIGIAKEQHQ 676
Cdd:cd16938     1 LPDVVVGDERRVFQVLLHMLGNLLKMRNGGgnitfRVFLEGGSEDRSDRDWGPwrPSMSDESVEIRFE---VEINDSGSP 77
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2651418669 677 LIFEAFQQAdgATIRKYG----GTGLGLSICKEFARLLGGWITLESNVGEGSTFTVYI 730
Cdd:cd16938    78 SIESASMRN--SLNRRYNlselGEHLSFSICKQLVQLMGGNIWIVPGSGLGTTMSLLL 133
REC_NtrC1-like cd17572
phosphoacceptor receiver (REC) domain of nitrogen regulatory protein C 1 (NtrC1) from Aquifex ...
778-886 6.06e-09

phosphoacceptor receiver (REC) domain of nitrogen regulatory protein C 1 (NtrC1) from Aquifex aeolicus and similar NtrC family response regulators; NtrC family proteins are transcriptional regulators that have REC, AAA+ ATPase/sigma-54 interaction, and DNA-binding output domains. This subfamily of NtrC proteins include Aquifex aeolicus NtrC1 and Vibrio quorum-sensing signal integrator LuxO. The N-terminal REC domain of NtrC proteins regulate the activity of the protein and its phosphorylation controls the AAA+ domain oligomerization, while the central AAA+ domain participates in nucleotide binding, hydrolysis, oligomerization, and sigma54 interaction. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381114 [Multi-domain]  Cd Length: 121  Bit Score: 54.90  E-value: 6.06e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 778 ILIVDDDHRNIFALQNALKKHHANIITAQNGLECLEILKNNTnIDLILMDIMMPNMDGYETMEHIRMNLGlhEIPIIALT 857
Cdd:cd17572     1 VLLVEDSPSLAALYQEYLSDEGYKVTHVETGKEALAFLSDQP-PDVVLLDLKLPDMSGMEILKWIQERSL--PTSVIVIT 77
                          90       100
                  ....*....|....*....|....*....
gi 2651418669 858 AKAMPNDKEKCLSAGASDYISKPLNLHQL 886
Cdd:cd17572    78 AHGSVDIAVEAMRLGAYDFLEKPFDADRL 106
PRK10529 PRK10529
DNA-binding transcriptional activator KdpE; Provisional
777-894 6.33e-09

DNA-binding transcriptional activator KdpE; Provisional


Pssm-ID: 182522 [Multi-domain]  Cd Length: 225  Bit Score: 57.12  E-value: 6.33e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 777 TILIVDDDHRNIFALQNALKKHHANII---TAQNGLecleILKNNTNIDLILMDIMMPNMDGYETMEHIRMnlgLHEIPI 853
Cdd:PRK10529    3 NVLIVEDEQAIRRFLRTALEGDGMRVFeaeTLQRGL----LEAATRKPDLIILDLGLPDGDGIEFIRDLRQ---WSAIPV 75
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 2651418669 854 IALTAKAMPNDKEKCLSAGASDYISKPLNLHQLYSVMSVWL 894
Cdd:PRK10529   76 IVLSARSEESDKIAALDAGADDYLSKPFGIGELQARLRVAL 116
PRK10161 PRK10161
phosphate response regulator transcription factor PhoB;
776-886 6.48e-09

phosphate response regulator transcription factor PhoB;


Pssm-ID: 182277 [Multi-domain]  Cd Length: 229  Bit Score: 57.42  E-value: 6.48e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 776 KTILIVDDDhrnifalqnALKKHHANIITAQNGLECLEILKNNTNI--------DLILMDIMMPNMDGYETMEHIRMNLG 847
Cdd:PRK10161    3 RRILVVEDE---------APIREMVCFVLEQNGFQPVEAEDYDSAVnqlnepwpDLILLDWMLPGGSGIQFIKHLKRESM 73
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2651418669 848 LHEIPIIALTAKAMPNDKEKCLSAGASDYISKPLNLHQL 886
Cdd:PRK10161   74 TRDIPVVMLTARGEEEDRVRGLETGADDYITKPFSPKEL 112
PRK10693 PRK10693
two-component system response regulator RssB;
805-881 2.34e-08

two-component system response regulator RssB;


Pssm-ID: 182652 [Multi-domain]  Cd Length: 303  Bit Score: 56.54  E-value: 2.34e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2651418669 805 AQNGLECLEILKNNTnIDLILMDIMMPNMDGYETMEHIRMNlGLhEIPIIALTAKAMPNDKEKCLSAGASDYISKPL 881
Cdd:PRK10693    3 AANGVDALELLGGFT-PDLIICDLAMPRMNGIEFVEHLRNR-GD-QTPVLVISATENMADIAKALRLGVQDVLLKPV 76
PRK11173 PRK11173
two-component response regulator; Provisional
778-886 2.47e-08

two-component response regulator; Provisional


Pssm-ID: 183013 [Multi-domain]  Cd Length: 237  Bit Score: 55.79  E-value: 2.47e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 778 ILIVDDDHRNIFALQNALKKHHANIITAQNGLECLEILKNNtNIDLILMDIMMPNMDGYETMEHIRMNLglhEIPIIALT 857
Cdd:PRK11173    6 ILIVEDELVTRNTLKSIFEAEGYDVFEATDGAEMHQILSEN-DINLVIMDINLPGKNGLLLARELREQA---NVALMFLT 81
                          90       100
                  ....*....|....*....|....*....
gi 2651418669 858 AKAMPNDKEKCLSAGASDYISKPLNLHQL 886
Cdd:PRK11173   82 GRDNEVDKILGLEIGADDYITKPFNPREL 110
PRK10337 PRK10337
sensor protein QseC; Provisional
499-723 3.55e-08

sensor protein QseC; Provisional


Pssm-ID: 182388 [Multi-domain]  Cd Length: 449  Bit Score: 56.97  E-value: 3.55e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 499 FLANMSHELRTPLNSILLLSEMLKenhdnhLSDDEIEL---ATVIHSSGKDLLT-LINDILDLSKVEAGKLDVIFEATNI 574
Cdd:PRK10337  240 FTSDAAHELRSPLAALKVQTEVAQ------LSDDDPQArkkALLQLHAGIDRATrLVDQLLTLSRLDSLDNLQDVAEIPL 313
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 575 SDMAASMHQNFLHIAAQKNVEFTVEdsdtIPDlfyTDAKRIEQ------IIKNLLSNAFKFTEKGSVslhFDSIETSNls 648
Cdd:PRK10337  314 EDLLQSAVMDIYHTAQQAGIDVRLT----LNA---HPVIRTGQplllslLVRNLLDNAIRYSPQGSV---VDVTLNAR-- 381
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2651418669 649 hdmqsiskdwiTISVKDTGIGIAKEQHQLIFEAFQQADGATIRkygGTGLGLSICKEFARLLGGWITLeSNVGEG 723
Cdd:PRK10337  382 -----------NFTVRDNGPGVTPEALARIGERFYRPPGQEAT---GSGLGLSIVRRIAKLHGMNVSF-GNAPEG 441
HATPase_PhoQ-like cd16954
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
588-730 4.27e-08

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


Pssm-ID: 340430 [Multi-domain]  Cd Length: 135  Bit Score: 52.63  E-value: 4.27e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 588 IAAQKNVEFTVEDSDTIpdLFYTDAKRIEQIIKNLLSNAFKFT-EKGSVSLHFDSietsnlshdmqsiskDWITISVKDT 666
Cdd:cd16954    13 VYQRKGVSISLDISPEL--RFPGERNDLMELLGNLLDNACKWClEFVEVTARQTD---------------GGLHLIVDDD 75
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2651418669 667 GIGIAKEQHQLIFEAFQQADgaTIRKygGTGLGLSICKEFARLLGGWITLESNVGEGSTFTVYI 730
Cdd:cd16954    76 GPGVPESQRSKIFQRGQRLD--EQRP--GQGLGLAIAKEIVEQYGGELSLSDSPLGGARFEVVF 135
PRK15479 PRK15479
transcriptional regulator TctD;
779-886 4.29e-08

transcriptional regulator TctD;


Pssm-ID: 185376 [Multi-domain]  Cd Length: 221  Bit Score: 54.73  E-value: 4.29e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 779 LIVDDDHRNIFA-LQNALKKHHANIITAQNGLECLEILKNNtNIDLILMDIMMPNMDGYETMEHIRMNlGlHEIPIIALT 857
Cdd:PRK15479    3 LLLAEDNRELAHwLEKALVQNGFAVDCVFDGLAADHLLQSE-MYALAVLDINMPGMDGLEVLQRLRKR-G-QTLPVLLLT 79
                          90       100
                  ....*....|....*....|....*....
gi 2651418669 858 AKAMPNDKEKCLSAGASDYISKPLNLHQL 886
Cdd:PRK15479   80 ARSAVADRVKGLNVGADDYLPKPFELEEL 108
PRK10766 PRK10766
two-component system response regulator TorR;
776-886 4.41e-08

two-component system response regulator TorR;


Pssm-ID: 182711 [Multi-domain]  Cd Length: 221  Bit Score: 54.66  E-value: 4.41e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 776 KTILIVDDDHRNIFALQNALKKHHANIITAQNGLECLEILkNNTNIDLILMDIMMPNMDGYETMEHIRMNlglHEIPIIA 855
Cdd:PRK10766    3 YHILVVEDEPVTRARLQGYFEQEGYTVSEAASGAGMREIM-QNQHVDLILLDINLPGEDGLMLTRELRSR---STVGIIL 78
                          90       100       110
                  ....*....|....*....|....*....|.
gi 2651418669 856 LTAKAMPNDKEKCLSAGASDYISKPLNLHQL 886
Cdd:PRK10766   79 VTGRTDSIDRIVGLEMGADDYVTKPLELREL 109
REC_OmpR_VirG cd17594
phosphoacceptor receiver (REC) domain of VirG-like OmpR family response regulators; VirG is ...
777-886 4.48e-08

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: 52.06  E-value: 4.48e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 777 TILIVDDDHRNIFALQNALKKHHANIITAQNGLECLEILKNNTnIDLILMDIMMPNMDGYETMEHIRMNlglHEIPIIAL 856
Cdd:cd17594     1 HVLVVDDDAAMRHLLILYLRERGFDVTAAADGAEEARLMLHRR-VDLVLLDLRLGQESGLDLLRTIRAR---SDVPIIII 76
                          90       100       110
                  ....*....|....*....|....*....|.
gi 2651418669 857 TA-KAMPNDKEKCLSAGASDYISKPLNLHQL 886
Cdd:cd17594    77 SGdRRDEIDRVVGLELGADDYLAKPFGLREL 107
HATPase_HupT_MifS-like cd16976
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
615-728 6.03e-08

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: 51.30  E-value: 6.03e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 615 IEQIIKNLLSNAFKFTEKgsvslhfdsIETSNLSHDMQSISKDWItISVKDTGIGIAKEQHQLIFEAFqqadgATIRKYG 694
Cdd:cd16976     1 IQQVLMNLLQNALDAMGK---------VENPRIRIAARRLGGRLV-LVVRDNGPGIAEEHLSRVFDPF-----FTTKPVG 65
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2651418669 695 -GTGLGLSICKEFARLLGGWITLESNVGEGSTFTV 728
Cdd:cd16976    66 kGTGLGLSISYGIVEEHGGRLSVANEEGAGARFTF 100
HK9-like_sensor cd19410
ligand binding sensor domain of Rhodopseudomonas palustris histidine kinase HK9 and similar ...
47-125 6.82e-08

ligand binding sensor domain of Rhodopseudomonas palustris histidine kinase HK9 and similar proteins; The ligand binding sensor domain of Rhodopseudomonas palustris histidine kinase HK9 and similar proteins forms a homodimer and binds to an as yet uncharacterized ligand, most likely via the dimerization interface, a feature that appears to be conserved in this domain superfamily. This domain is similar to the extracellular sensory domain CHASE3, specifically found in histidine kinases, adenylate cyclases, methyl-accepting chemotaxis proteins and predicted diguanylate cyclases/phosphodiesterases. Environmental factors that are recognized by CHASE3 domains are not known at this time.


Pssm-ID: 438628  Cd Length: 125  Bit Score: 51.83  E-value: 6.82e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2651418669  47 DHDFKVLNLTNQVEKELLTIENKAKGFITSNDANYVQSLNAAEKDYEKHYQDLFALLEDNPSQQEKLKQINENITNWIN 125
Cdd:cd19410     1 EHTYEVLSELERLLSLLKDAETGQRGYLLTGDESYLEPYNAARARLPALLAELRELTADNPAQQARLDELEPLIDEKLA 79
PtsP COG3605
Signal transduction protein containing GAF and PtsI domains [Signal transduction mechanisms];
280-453 7.01e-08

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


Pssm-ID: 442824 [Multi-domain]  Cd Length: 188  Bit Score: 53.36  E-value: 7.01e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 280 NKILSGIIQKTQTSCGAFYVREEVEDTVYYvkkasFAEQG---ADIGKQSIKMGEGFIGQTALEKKSFILRDIPEE--FR 354
Cdd:COG3605    24 DRIVRRIAEALGVDVCSIYLLDPDGGRLEL-----RATEGlnpEAVGKVRLPLGEGLVGLVAERGEPLNLADAASHprFK 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 355 YvTTGLLEIRPKNLLVIPVLFEDEVIAVMELVSVT--DISDLHQDLIQQTVDNLGLTIhsimgrmriqtllyESQAMTEE 432
Cdd:COG3605    99 Y-FPETGEEGFRSFLGVPIIRRGRVLGVLVVQSREprEFTEEEVEFLVTLAAQLAEAI--------------ANAELLGE 163
                         170       180
                  ....*....|....*....|.
gi 2651418669 433 LQVQSEELQTQAEELQMQAEE 453
Cdd:COG3605   164 LRAALAELSLAREEEREAAVE 184
FixJ COG4566
DNA-binding response regulator, FixJ family, consists of REC and HTH domains [Signal ...
777-886 7.27e-08

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: 53.57  E-value: 7.27e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 777 TILIVDDDHRNIFALQNALKKHHANIITAQNGLECLEILKNNTnIDLILMDIMMPNMDGYETMEHIRmNLGLHeIPIIAL 856
Cdd:COG4566     1 TVYIVDDDEAVRDSLAFLLESAGLRVETFASAEAFLAALDPDR-PGCLLLDVRMPGMSGLELQEELA-ARGSP-LPVIFL 77
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2651418669 857 TA--------KAMpndKekclsAGASDYISKPLNLHQL 886
Cdd:COG4566    78 TGhgdvpmavRAM---K-----AGAVDFLEKPFDDQAL 107
HATPase_SpaK_NisK-like cd16975
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
611-730 8.10e-08

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


Pssm-ID: 340434 [Multi-domain]  Cd Length: 107  Bit Score: 51.31  E-value: 8.10e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 611 DAKRIEQIIKNLLSNAFKFT-EKGSVSLHFDSietsnlshdmqsiSKDWITISVKDTGIGIAKEQHQLIFEAFQQADGAT 689
Cdd:cd16975     1 DTLLLSRALINIISNACQYApEGGTVSISIYD-------------EEEYLYFEIWDNGHGFSEQDLKKALELFYRDDTSR 67
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 2651418669 690 iRKYGGTGLGLSICKEFARLLGGWITLESNVGEGSTFTVYI 730
Cdd:cd16975    68 -RSGGHYGMGLYIAKNLVEKHGGSLIIENSQKGGAEVTVKI 107
glnG PRK10923
nitrogen regulation protein NR(I); Provisional
774-883 1.02e-07

nitrogen regulation protein NR(I); Provisional


Pssm-ID: 182842 [Multi-domain]  Cd Length: 469  Bit Score: 55.65  E-value: 1.02e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 774 QEKTILIVDDDHRNIFALQNALKKHHANIITAQNGLECLEILKNNTNiDLILMDIMMPNMDGYETMEHIRMNLGLheIPI 853
Cdd:PRK10923    2 QRGIVWVVDDDSSIRWVLERALAGAGLTCTTFENGNEVLEALASKTP-DVLLSDIRMPGMDGLALLKQIKQRHPM--LPV 78
                          90       100       110
                  ....*....|....*....|....*....|...
gi 2651418669 854 IALTAKAmpnDKEKCLSA---GASDYISKPLNL 883
Cdd:PRK10923   79 IIMTAHS---DLDAAVSAyqqGAFDYLPKPFDI 108
GAF COG2203
GAF domain [Signal transduction mechanisms];
255-491 1.09e-07

GAF domain [Signal transduction mechanisms];


Pssm-ID: 441805 [Multi-domain]  Cd Length: 712  Bit Score: 55.58  E-value: 1.09e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 255 REWLQTELAELILMYQGVSSIEMLGNKILSGIIQKTQTSCGAFYVREEVEDTVYYVKKASFAEQGADigkqSIKMGEGFI 334
Cdd:COG2203   188 ELERLALLNEISQALRSALDLEELLQRILELAGELLGADRGAILLVDEDGGELELVAAPGLPEEELG----RLPLGEGLA 263
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 335 GQTALEKKSFILRDIPEEFRYVTTG---LLEIRPKNLLVIPVLFEDEVIAVMELVSVT--DISDLHQDLIQQTVDNLGLT 409
Cdd:COG2203   264 GRALRTGEPVVVNDASTDPRFAPSLrelLLALGIRSLLCVPLLVDGRLIGVLALYSKEprAFTEEDLELLEALADQAAIA 343
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 410 IHsimgrmriQTLLYESQAMTEELQVQSEELQTQAEELQMQAEELRTTNEQLESRTEEAEQKTADLQVTKLELEEKASEL 489
Cdd:COG2203   344 IE--------RARLYEALEAALAALLQELALLRLLLDLELTLLRLRQLLLELLLALLLLLSLLGAELLLLLLDAADLSGL 415

                  ..
gi 2651418669 490 LR 491
Cdd:COG2203   416 LA 417
HATPase_CreC-like cd16945
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
611-723 1.45e-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: 50.54  E-value: 1.45e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 611 DAKRIEQIIKNLLSNAFKFTEKG---SVSLHFDSietsnlshdmqsiskDWITISVKDTGIGIAKEQHQLIFEAFQQ-AD 686
Cdd:cd16945     1 DPFLLRQAINNLLDNAIDFSPEGgliALQLEADT---------------EGIELLVFDEGSGIPDYALNRVFERFYSlPR 65
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2651418669 687 GATIRKygGTGLGLSICKEFARLLGGWITLEsNVGEG 723
Cdd:cd16945    66 PHSGQK--STGLGLAFVQEVAQLHGGRITLR-NRPDG 99
HATPase_Glnl-NtrB-like cd16918
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
615-731 1.67e-07

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: 50.48  E-value: 1.67e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 615 IEQIIKNLLSNAFKFTEK--GSVSLHFDSIETSNLSHDMQSISkdwITISVKDTGIGIAKEQHQLIFEAFQQAdgatirK 692
Cdd:cd16918     1 LIQVFLNLVRNAAQALAGsgGEIILRTRTQRQVTLGHPRHRLA---LRVSVIDNGPGIPPDLQDTIFYPMVSG------R 71
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2651418669 693 YGGTGLGLSICKEFARLLGGWITLESNVGEgSTFTVYIP 731
Cdd:cd16918    72 ENGTGLGLAIAQNIVSQHGGVIECDSQPGH-TVFSVSLP 109
PLN03029 PLN03029
type-a response regulator protein; Provisional
778-886 2.05e-07

type-a response regulator protein; Provisional


Pssm-ID: 215544 [Multi-domain]  Cd Length: 222  Bit Score: 52.73  E-value: 2.05e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 778 ILIVDDDHRNIFALQNALKKHHANIITAQNGLECLEIL------KNNTN-------------IDLILMDIMMPNMDGYET 838
Cdd:PLN03029   11 VLAVDDSLIDRKLIEKLLKTSSYQVTTVDSGSKALKFLglheddRSNPDtpsvspnshqeveVNLIITDYCMPGMTGYDL 90
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 2651418669 839 MEHIRMNLGLHEIPIIALTAKAMPNDKEKCLSAGASDYISKPLNLHQL 886
Cdd:PLN03029   91 LKKIKESSSLRNIPVVIMSSENVPSRITRCLEEGAEEFFLKPVQLSDL 138
COG4567 COG4567
DNA-binding response regulator, ActR/RegA family, consists of REC and Fis-type HTH domains ...
774-886 3.13e-07

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: 51.46  E-value: 3.13e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 774 QEKTILIVDDDHRNIFALQNALKKHHANIITAQNGLECLEILKNNTnIDLILMDIMMPNMDGYETMEHIRmnlGLH-EIP 852
Cdd:COG4567     3 EDRSLLLVDDDEAFARVLARALERRGFEVTTAASVEEALALLEQAP-PDYAVLDLRLGDGSGLDLIEALR---ERDpDAR 78
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 2651418669 853 IIALTA--------KAMPndkekclsAGASDYISKPLNLHQL 886
Cdd:COG4567    79 IVVLTGyasiatavEAIK--------LGADDYLAKPADADDL 112
PRK09836 PRK09836
DNA-binding transcriptional activator CusR; Provisional
778-886 4.05e-07

DNA-binding transcriptional activator CusR; Provisional


Pssm-ID: 182102 [Multi-domain]  Cd Length: 227  Bit Score: 51.85  E-value: 4.05e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 778 ILIVDDDHRNIFALQNALKKHHANIITAQNGLECLEiLKNNTNIDLILMDIMMPNMDGYETMEHIR-MNLGLheiPIIAL 856
Cdd:PRK09836    3 LLIVEDEKKTGEYLTKGLTEAGFVVDLADNGLNGYH-LAMTGDYDLIILDIMLPDVNGWDIVRMLRsANKGM---PILLL 78
                          90       100       110
                  ....*....|....*....|....*....|
gi 2651418669 857 TAKAMPNDKEKCLSAGASDYISKPLNLHQL 886
Cdd:PRK09836   79 TALGTIEHRVKGLELGADDYLVKPFAFAEL 108
PRK10618 PRK10618
phosphotransfer intermediate protein in two-component regulatory system with RcsBC; Provisional
499-735 4.41e-07

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


Pssm-ID: 236726 [Multi-domain]  Cd Length: 894  Bit Score: 53.78  E-value: 4.41e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 499 FLANMSHELRTPLNSILLLSEMLKenHDNHLSDDEIELATVIHSSgKDLLTLINDILDLSKVEAGKLDVIFEATNISDMA 578
Cdd:PRK10618  453 FLQNIGDELKQPLQSLAQLAAQLR--QTSDEEQQQPELDQLAEQS-DVLVRLVDNIQLLNMLETQDWKPEQELFSLQDLI 529
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 579 ASMHQNFLHIAAQKNVEFTVEDSDTIPDLFYTDAKRIEQIIKNLLSNAFKFTEKGSVSLhfdsietsNLSHDMQSisKDW 658
Cdd:PRK10618  530 DEVLPEVLPAIKRKGLQLLIHNHLKAEQLRIGDRDALRKILLLLLNYAITTTAYGKITL--------EVDQDESS--PDR 599
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2651418669 659 ITISVKDTGIGI-AKEQHQLIFEAFQQADGatiRKYG-GTGLGLSICKEFARLLGGWITLESNVGEGSTFTVYIPNLPN 735
Cdd:PRK10618  600 LTIRILDTGAGVsIKELDNLHFPFLNQTQG---DRYGkASGLTFFLCNQLCRKLGGHLTIKSREGLGTRYSIHLKMLAA 675
REC_WspR-like cd17575
phosphoacceptor receiver (REC) domain of WspR response regulator and similar proteins; The ...
777-879 1.08e-06

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


Pssm-ID: 381117 [Multi-domain]  Cd Length: 128  Bit Score: 48.56  E-value: 1.08e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 777 TILIVDDDHRNIFALQNALKKHhANII--TAQNGLECLEIlKNNTNIDLILMDIMMPNMDGYETMEHIRMNLGLHEIPII 854
Cdd:cd17575     2 MVLLVDDQAIIGEAVRRALADE-EDIDfhYCSDPTEAIEV-ASQIKPTVILQDLVMPGVDGLTLVRFFRANPATRDIPII 79
                          90       100
                  ....*....|....*....|....*
gi 2651418669 855 ALTAKAMPNDKEKCLSAGASDYISK 879
Cdd:cd17575    80 VLSTKEEPEVKSEAFALGANDYLVK 104
CitB COG2197
DNA-binding response regulator, NarL/FixJ family, contains REC and HTH domains [Signal ...
777-842 1.38e-06

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


Pssm-ID: 441799 [Multi-domain]  Cd Length: 131  Bit Score: 48.35  E-value: 1.38e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2651418669 777 TILIVDDDHRNIFALQNALKKHHAN--IITAQNGLECLEILKNnTNIDLILMDIMMPNMDGYETMEHI 842
Cdd:COG2197     3 RVLIVDDHPLVREGLRALLEAEPDIevVGEAADGEEALELLEE-LRPDVVLLDIRMPGMDGLEALRRL 69
PRK10643 PRK10643
two-component system response regulator PmrA;
778-886 2.19e-06

two-component system response regulator PmrA;


Pssm-ID: 182612 [Multi-domain]  Cd Length: 222  Bit Score: 49.65  E-value: 2.19e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 778 ILIVDDDHRNIFALQNALKKHHANIITAQNGLEClEILKNNTNIDLILMDIMMPNMDGYETMEHIRMNLglHEIPIIALT 857
Cdd:PRK10643    3 ILIVEDDTLLLQGLILALQTEGYACDCASTAREA-EALLESGHYSLVVLDLGLPDEDGLHLLRRWRQKK--YTLPVLILT 79
                          90       100
                  ....*....|....*....|....*....
gi 2651418669 858 AKAMPNDKEKCLSAGASDYISKPLNLHQL 886
Cdd:PRK10643   80 ARDTLEDRVAGLDVGADDYLVKPFALEEL 108
REC_RegA-like cd17563
phosphoacceptor receiver (REC) domain of photosynthetic apparatus regulatory protein RegA; ...
776-889 2.90e-06

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: 46.67  E-value: 2.90e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 776 KTILIVDDDhrNIFA--LQNALKKHHANIITAQNGLECLEILKNNTnIDLILMDIMMPNMDGYETMEHIRMNLGlhEIPI 853
Cdd:cd17563     1 KSLLLVDDD--EVFAerLARALERRGFEVETAHSVEEALALAREEK-PDYAVLDLRLGGDSGLDLIPPLRALQP--DARI 75
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 2651418669 854 IALT-----AKAMpndkekclSA---GASDYISKPLNLHQLYSV 889
Cdd:cd17563    76 VVLTgyasiATAV--------EAiklGADDYLAKPADADEILAA 111
REC_PilR cd19926
phosphoacceptor receiver (REC) domain of type 4 fimbriae expression regulatory protein PilR ...
778-880 3.27e-06

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


Pssm-ID: 381153 [Multi-domain]  Cd Length: 100  Bit Score: 46.38  E-value: 3.27e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 778 ILIVDDDHRNIFALQNALKKHHANIITAQNGLECLEILKNNtNIDLILMDIMMPNMDGYETMEHIRMNLGlhEIPIIALT 857
Cdd:cd19926     1 VLVVDDEPDIRELLEITLGRMGLDVRSARNVKEARELLASE-PYDLCLTDMRLPDGSGLELVQHIQQRLP--QTPVAVIT 77
                          90       100
                  ....*....|....*....|...
gi 2651418669 858 AKAMPNDKEKCLSAGASDYISKP 880
Cdd:cd19926    78 AYGSLDTAIEALKAGAFDFLTKP 100
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
433-538 4.10e-06

Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 50.89  E-value: 4.10e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669  433 LQVQSEELQTQAEELQMQAEELRTTNEQLESRTEEAEQKTADLQVTKLELEEKASELLRSS---KYKSEFLANMSHELRT 509
Cdd:pfam15921  588 MQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLELEKVKLVNAGSERLRAVkdiKQERDQLLNEVKTSRN 667
                           90       100
                   ....*....|....*....|....*....
gi 2651418669  510 PLNSILLLSEMLKENHDNhlSDDEIELAT 538
Cdd:pfam15921  668 ELNSLSEDYEVLKRNFRN--KSEEMETTT 694
REC_HP-RR-like cd17573
phosphoacceptor receiver (REC) domain of orphan response regulator HP-RR and similar proteins; ...
778-886 4.13e-06

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


Pssm-ID: 381115 [Multi-domain]  Cd Length: 110  Bit Score: 46.27  E-value: 4.13e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 778 ILIVDDDHRNIFALQNALKKHHANIITAQNgLECLEILKNNTNIDLILMDIMMPNMDGYETMEHIRMNLGlhEIPIIALT 857
Cdd:cd17573     1 ILLIEDDSTLGKEISKGLNEKGYQADVAES-LKDGEYYIDIRNYDLVLVSDKLPDGNGLSIVSRIKEKHP--SIVVIVLS 77
                          90       100
                  ....*....|....*....|....*....
gi 2651418669 858 AKAMPNDKEKCLSAGASDYISKPLNLHQL 886
Cdd:cd17573    78 DNPKTEQEIEAFKEGADDYIAKPFDFKVL 106
REC_Spo0F-like cd17553
phosphoacceptor receiver (REC) domain of Spo0F and similar domains; Spo0F, a stand-alone ...
776-886 4.45e-06

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


Pssm-ID: 381105 [Multi-domain]  Cd Length: 117  Bit Score: 46.39  E-value: 4.45e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 776 KTILIVDDDHRNIFALQNALKKHHANIITAQNGLECLEILKNNTNiDLILMDIMMPNMDGYETMEHirMNLGLHEIPIIA 855
Cdd:cd17553     1 EKILIVDDQYGIRILLNEVFNKEGYQTFQAANGLQALDIVTKERP-DLVLLDMKIPGMDGIEILKR--MKVIDENIRVII 77
                          90       100       110
                  ....*....|....*....|....*....|.
gi 2651418669 856 LTAKAMPNDKEKCLSAGASDYISKPLNLHQL 886
Cdd:cd17553    78 MTAYGELDMIQESKELGALTHFAKPFDIDEI 108
PRK15115 PRK15115
response regulator GlrR; Provisional
778-888 5.91e-06

response regulator GlrR; Provisional


Pssm-ID: 185070 [Multi-domain]  Cd Length: 444  Bit Score: 49.84  E-value: 5.91e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 778 ILIVDDDHRNIFALQNALKKHHANIITAQNGLECLEILkNNTNIDLILMDIMMPNMDGYETMEHI-RMNLGLheiPIIAL 856
Cdd:PRK15115    8 LLLVDDDPGLLKLLGMRLTSEGYSVVTAESGQEALRVL-NREKVDLVISDLRMDEMDGMQLFAEIqKVQPGM---PVIIL 83
                          90       100       110
                  ....*....|....*....|....*....|..
gi 2651418669 857 TAKAMPNDKEKCLSAGASDYISKPLNLHQLYS 888
Cdd:PRK15115   84 TAHGSIPDAVAATQQGVFSFLTKPVDRDALYK 115
HATPase_BvrS-ChvG-like cd16953
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
617-731 9.24e-06

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: 45.26  E-value: 9.24e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 617 QIIKNLLSNAFKFTEKGSVSLHFDSIETSNLshdmqsiskdwITISVKDTGIGIAKEQHQLIFEAF--QQADGATIRKYg 694
Cdd:cd16953     3 QVLRNLIGNAISFSPPDTGRITVSAMPTGKM-----------VTISVEDEGPGIPQEKLESIFDRFytERPANEAFGQH- 70
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 2651418669 695 gTGLGLSICKEFARLLGGWITLES----NVGEGSTFTVYIP 731
Cdd:cd16953    71 -SGLGLSISRQIIEAHGGISVAENhnqpGQVIGARFTVQLP 110
REC_RocR cd17530
phosphoacceptor receiver (REC) domain of response regulator RocR; The response regulator RocR ...
777-842 1.36e-05

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


Pssm-ID: 381086 [Multi-domain]  Cd Length: 123  Bit Score: 45.12  E-value: 1.36e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2651418669 777 TILIVDDDHRNIFALQNALKK-HHANIITAQNGLECLEILKNNtNIDLILMDIMMPNMDGYETMEHI 842
Cdd:cd17530     2 RVLVLDDDPFQCMMAATILEDlGPGNVDEADDGREALVILLCN-APDIIICDLKMPDMDGIEFLRHL 67
marine_sort_HK TIGR03785
proteobacterial dedicated sortase system histidine kinase; This histidine kinase protein is ...
486-731 1.90e-05

proteobacterial dedicated sortase system histidine kinase; This histidine kinase protein is paired with an adjacent response regulator (TIGR03787) gene. It co-occurs with a variant sortase enzyme (TIGR03784), usually in the same gene neighborhood, in proteobacterial species most of which are marine, and with an LPXTG motif-containing sortase target conserved protein (TIGR03788). Sortases and LPXTG proteins are far more common in Gram-positive bacteria, where sortase systems mediate attachment to the cell wall or cross-linking of pilin structures. We give this predicted sensor histidine kinase the gene symbol psdS, for Proteobacterial Dedicated Sortase system Sensor histidine kinase.


Pssm-ID: 163497 [Multi-domain]  Cd Length: 703  Bit Score: 48.59  E-value: 1.90e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 486 ASELLRSSKYkSEFLANMS----HELRTPL---NSILLLSEMLKenhdnhLSDDEIELATVIHSSGKDLLTLINDILDLS 558
Cdd:TIGR03785 472 AQMVARLRQY-THYLENMSsrlsHELRTPVavvRSSLENLELQA------LEQEKQKYLERAREGTERLSMILNNMSEAT 544
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 559 KVEAGKLDVIFEATNISDMAASMHQNFLHIAAQKNVEFTVEDSDTI----PDLfytdakrIEQIIKNLLSNAFKFTEKGS 634
Cdd:TIGR03785 545 RLEQAIQSAEVEDFDLSEVLSGCMQGYQMTYPPQRFELNIPETPLVmrgsPEL-------IAQMLDKLVDNAREFSPEDG 617
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 635 VslhfdsIETSNLSHDMQsiskdwITISVKDTGIGIAKEQHQLIFEAF--QQADGATIRKYggTGLGLSICKEFARLLGG 712
Cdd:TIGR03785 618 L------IEVGLSQNKSH------ALLTVSNEGPPLPEDMGEQLFDSMvsVRDQGAQDQPH--LGLGLYIVRLIADFHQG 683
                         250       260
                  ....*....|....*....|
gi 2651418669 713 WITLESNV-GEGSTFTVYIP 731
Cdd:TIGR03785 684 RIQAENRQqNDGVVFRISLP 703
ComP COG4585
Signal transduction histidine kinase ComP [Signal transduction mechanisms];
511-731 1.92e-05

Signal transduction histidine kinase ComP [Signal transduction mechanisms];


Pssm-ID: 443642 [Multi-domain]  Cd Length: 252  Bit Score: 47.31  E-value: 1.92e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 511 LNSILLLSEMLKENHDNHlSDDEIELATVIHSSGKDLLTLINDIL-DLSKVEAGKLDVifeATNISDMAASMHQnflhiA 589
Cdd:COG4585    69 LSAIKLQLEAARRLLDAD-PEAAREELEEIRELAREALAELRRLVrGLRPPALDDLGL---AAALEELAERLLR-----A 139
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 590 AQKNVEFTVEDSDTIPDLFYTDAkrIEQIIKNLLSNAFKFTEKGSVSLHFdsietsnlshdmqSISKDWITISVKDTGIG 669
Cdd:COG4585   140 AGIRVELDVDGDPDRLPPEVELA--LYRIVQEALTNALKHAGATRVTVTL-------------EVDDGELTLTVRDDGVG 204
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2651418669 670 IAKEQHqlifeafqqadgatirkyGGTGLGLSICKEFARLLGGWITLESNVGEGSTFTVYIP 731
Cdd:COG4585   205 FDPEAA------------------PGGGLGLRGMRERAEALGGTLTIGSAPGGGTRVRATLP 248
REC_GlnL-like cd17565
phosphoacceptor receiver (REC) domain of transcriptional regulatory protein GlnL and similar ...
778-881 2.96e-05

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


Pssm-ID: 381112 [Multi-domain]  Cd Length: 103  Bit Score: 43.80  E-value: 2.96e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 778 ILIVDDDHRNIFALQNALKKHHANII--TAQNGLECLEILKNnTNIDLILMDIMMPNMDGYETMEHIR-MNLGLHEIPII 854
Cdd:cd17565     1 FYIVDDDKNIIKILSDIIEDDDLGEVvgEADNGAQAYDEILF-LQPDIVLIDLLMPGMDGIQLVRKLKdTGSNGKFIMIS 79
                          90       100
                  ....*....|....*....|....*..
gi 2651418669 855 ALTAKAMpndKEKCLSAGASDYISKPL 881
Cdd:cd17565    80 QVSDKEM---IGKAYQAGIEFFINKPI 103
MsrC COG1956
GAF domain-containing protein, putative methionine-R-sulfoxide reductase [Defense mechanisms, ...
297-410 3.16e-05

GAF domain-containing protein, putative methionine-R-sulfoxide reductase [Defense mechanisms, Signal transduction mechanisms];


Pssm-ID: 441559 [Multi-domain]  Cd Length: 156  Bit Score: 44.82  E-value: 3.16e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 297 FYVREEVEDTVyyvkKASFaeQGAdIGKQSIKMGEGFIGQTALEKKSFILRDIPEEFRYVTTGlleIRPKNLLVIPVLFE 376
Cdd:COG1956    49 FYLVDGGGELV----LGPF--QGP-PACTRIPFGKGVCGTAAAEGETQLVPDVHAFPGHIACD---SASRSEIVVPIFKD 118
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2651418669 377 DEVIAVMELVSVT--DISDLHQDLIQQTVDNLGLTI 410
Cdd:COG1956   119 GEVIGVLDIDSPTpgRFDEEDQAGLEALAALLAEAL 154
REC_FixJ cd17537
phosphoacceptor receiver (REC) domain of FixJ family response regulators; FixJ family response ...
777-882 3.45e-05

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


Pssm-ID: 381092 [Multi-domain]  Cd Length: 116  Bit Score: 43.74  E-value: 3.45e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 777 TILIVDDDHRNIFALQNALKKHHANIITAQNGLECLEILKNNTNIDLILmDIMMPNMDGYETMEHIRmNLGLHeIPIIAL 856
Cdd:cd17537     2 TVYVVDDDEAVRDSLAFLLRSVGLAVKTFTSASAFLAAAPPDQPGCLVL-DVRMPGMSGLELQDELL-ARGSN-IPIIFI 78
                          90       100
                  ....*....|....*....|....*....
gi 2651418669 857 TAKA---MpndKEKCLSAGASDYISKPLN 882
Cdd:cd17537    79 TGHGdvpM---AVEAMKAGAVDFLEKPFR 104
PRK13856 PRK13856
two-component response regulator VirG; Provisional
776-894 4.88e-05

two-component response regulator VirG; Provisional


Pssm-ID: 172377 [Multi-domain]  Cd Length: 241  Bit Score: 45.96  E-value: 4.88e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 776 KTILIVDDDHRNIFALQNALKKHHANIITAQNGLECLEILKNNTnIDLILMDIMMPNMDGyetMEHIRMNLGLHEIPIIA 855
Cdd:PRK13856    2 KHVLVIDDDVAMRHLIVEYLTIHAFKVTAVADSQQFNRVLASET-VDVVVVDLNLGREDG---LEIVRSLATKSDVPIII 77
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2651418669 856 LTAKAMPN-DKEKCLSAGASDYISKPLNLHQLYSVMSVWL 894
Cdd:PRK13856   78 ISGDRLEEaDKVVALELGATDFIAKPFGTREFLARIRVAL 117
REC_HupR cd17596
phosphoacceptor receiver (REC) domain of hydrogen uptake protein regulator (HupR); Members of ...
777-886 5.27e-05

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: 43.89  E-value: 5.27e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 777 TILIVDDDHRNIFALQNALKKHHaNIITAQNGLECLEILKNNTnIDLILMDIMMPNMDGYETMEHIRmnlGLHEIPI-IA 855
Cdd:cd17596     2 TILVVDDEVRSLEALRRTLEEDF-DVLTAASAEEALAILEEEW-VQVILCDQRMPGTTGVEFLKEVR---ERWPEVVrII 76
                          90       100       110
                  ....*....|....*....|....*....|..
gi 2651418669 856 LTAKAMPNDKEKCLS-AGASDYISKPLNLHQL 886
Cdd:cd17596    77 ISGYTDSEDIIAGINeAGIYQYLTKPWHPDQL 108
PRK11083 PRK11083
DNA-binding response regulator CreB; Provisional
808-880 6.34e-05

DNA-binding response regulator CreB; Provisional


Pssm-ID: 236838 [Multi-domain]  Cd Length: 228  Bit Score: 45.34  E-value: 6.34e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2651418669 808 GLECLEILKNnTNIDLILMDIMMPNMDGYETMEHIRMNLGlhEIPIIALTAKAMPNDKEKCLSAGASDYISKP 880
Cdd:PRK11083   36 GLPALDKLRQ-QPPDLVILDVGLPDISGFELCRQLLAFHP--ALPVIFLTARSDEVDRLVGLEIGADDYVAKP 105
pleD PRK09581
response regulator PleD; Reviewed
771-882 9.09e-05

response regulator PleD; Reviewed


Pssm-ID: 236577 [Multi-domain]  Cd Length: 457  Bit Score: 46.05  E-value: 9.09e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 771 NVFQEKTILIVDDDHRNIFALQNALKKHHANIITAQNGLECLEIlkNNTNIDLILMDIMMPNMDGYETMEHIRMNLGLHE 850
Cdd:PRK09581  151 NKDEDGRILLVDDDVSQAERIANILKEEFRVVVVSDPSEALFNA--AETNYDLVIVSANFENYDPLRLCSQLRSKERTRY 228
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2651418669 851 IPIIALTAkamPNDKEKCLSA---GASDYISKPLN 882
Cdd:PRK09581  229 VPILLLVD---EDDDPRLVKAlelGVNDYLMRPID 260
HAMP COG2770
HAMP domain [Signal transduction mechanisms];
180-579 1.04e-04

HAMP domain [Signal transduction mechanisms];


Pssm-ID: 442051 [Multi-domain]  Cd Length: 631  Bit Score: 45.87  E-value: 1.04e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 180 LEIWLYSLLFLLSCFAIIVSLYISNSITKTIKNVIQAIKSISSKEkITERIHVNSHDEIKDLAHTTNHLLDEISKR---- 255
Cdd:COG2770   210 ALLLLLLLALLALLLALLLALLLARRITRPLRRLAEAARRIAAGD-LDVRIPVSRKDEIGELARAFNRMADSLRESieea 288
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 256 -EWLQTELAELILMYQGVSSIEMLGNKILSGIIQKTQTSCGAFYVREEVEDTVYYVKKASFAEQGADIGKQSIKMGEGFI 334
Cdd:COG2770   289 eEEEELAEAELARLLEALLELLLALLLLLLALLLLAAAALLLELLLLLLLALLLLLLLAADLLLALALAALLLLLALELL 368
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 335 GQTALEKKSFILRDIPEEFRYVTTGLLEIRPKNLLVIPVLFEDEVIAVMELVSVTDISDLHQDLIQQTVDNLGLTIHSIM 414
Cdd:COG2770   369 LEAELLVLLALEALALEAELAAVLALLAALAAALLLLELALEELVLALLALALLALAAAAAAAEAAAAALELAAAAIAAA 448
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 415 GRMRIQTLLYESQAMTEELQVQSEELQTQAEELQMQAEELRTTNEQLESRTEEAEQKTADLQVTKLELEEKASELLRSSK 494
Cdd:COG2770   449 AAAEAEGGLAELEAEELVAAAEALLLLAALLLLAALGALELLLLEEEEEAGAAAEELAEELLLLEGLLLLLLLEAEALEV 528
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 495 YKSEFLANMSHELRTPLNSILLLSEMLKENHDNHLSDDEIELATVIHSSGKDLLTLINDILDLSKVEAGKLDVIFEATNI 574
Cdd:COG2770   529 AEELLELEEAALLLAAAAELAALLALLLALAAVEAAALLLAALLLAAVAALLELAALLLLLLAAAEALAALELELAAAAE 608

                  ....*
gi 2651418669 575 SDMAA 579
Cdd:COG2770   609 AALAE 613
NarQ COG3850
Signal transduction histidine kinase NarQ, nitrate/nitrite-specific [Signal transduction ...
187-484 1.13e-04

Signal transduction histidine kinase NarQ, nitrate/nitrite-specific [Signal transduction mechanisms];


Pssm-ID: 443059 [Multi-domain]  Cd Length: 448  Bit Score: 45.64  E-value: 1.13e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 187 LLFLLSCFAIIVSLYISNSITKTIKNVIQAIKSISSKEkITERIHVNSHDEIKDLAHTTNHLLDEISKREWLQTELAELI 266
Cdd:COG3850   123 RLLLALLLALLLAYLLRRRIVRPLRRLTQAAERIARGD-FDARVPVSGRDELGTLARAFNRMADELQELYAELEEEEELE 201
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 267 LMYQGVSSIEMLGNKILSGIIQKTQTSCGAFYVREEVEDTVYYVKKASFAEQGADIGKqsikmgEGFIGQTALEKKSFIL 346
Cdd:COG3850   202 AELELLALLDELLLLAALLLLLALLLALLLAALLAALLLLLLLQDALAESELLALNIL------AGLLELLLALLLLLLA 275
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 347 RDIPEEFRYVTTGLLEIRPKNLLVIPVLFEDEVIAVMELVSVTDISDLHQDLIQQTVDNLGLTIHSIMGRMRIQTLLYES 426
Cdd:COG3850   276 SALLLLELELLALLLELVELLALAAAEEALLLLVELAALLLLLLLQAIANASLLLIALASVVAALLELASILALQAALEA 355
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2651418669 427 QAMTEELQVQSEELQTQAEELQMQAEELRTTNEQLESRTEEAEQKTADLQVTKLELEE 484
Cdd:COG3850   356 AAAGAALAAAAAAAGLARALAQAGADAAEALGLLAEASEGAAGQGAGLVDVEGGVAGE 413
REC_TrxB cd17595
phosphoacceptor receiver (REC) domain a fused response regulator with a thioredoxin reductase ...
778-841 1.17e-04

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


Pssm-ID: 381126 [Multi-domain]  Cd Length: 135  Bit Score: 42.71  E-value: 1.17e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2651418669 778 ILIVDDDHRNIFALQNALKKHHAN---IITAQNGLECLEILKN----NTNIDLILMDIMMPNMDGYETMEH 841
Cdd:cd17595     3 ILTVDDDPQVLRAVARDLRRQYGKdyrVLRADSGAEALDALKElklrGEAVALFLVDQRMPEMDGVEFLEK 73
PRK10336 PRK10336
two-component system response regulator QseB;
778-883 1.26e-04

two-component system response regulator QseB;


Pssm-ID: 182387 [Multi-domain]  Cd Length: 219  Bit Score: 44.12  E-value: 1.26e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 778 ILIVDDDHRNIFALQNALKKHHANIITAQNGLECLEILKNnTNIDLILMDIMMPNMDGYETMEHIRMNlGLHEiPIIALT 857
Cdd:PRK10336    3 ILLIEDDMLIGDGIKTGLSKMGFSVDWFTQGRQGKEALYS-APYDAVILDLTLPGMDGRDILREWREK-GQRE-PVLILT 79
                          90       100
                  ....*....|....*....|....*.
gi 2651418669 858 AKAMPNDKEKCLSAGASDYISKPLNL 883
Cdd:PRK10336   80 ARDALAERVEGLRLGADDYLCKPFAL 105
REC_LytTR_AlgR-like cd17532
phosphoacceptor receiver (REC) domain of LytTR/AlgR family response regulators similar to AlgR; ...
778-880 1.27e-04

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


Pssm-ID: 381087 [Multi-domain]  Cd Length: 118  Bit Score: 42.52  E-value: 1.27e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 778 ILIVDDDHrniFALQN--ALKKHHANII---TAQNGLECLEILkNNTNIDLILMDIMMPNMDGyetMEHIRMNLGLHEIP 852
Cdd:cd17532     1 ALIVDDEP---LAREElrYLLEEHPDIEivgEAENGEEALEAI-EELKPDVVFLDIQMPGLDG---LELAKKLSKLAKPP 73
                          90       100       110
                  ....*....|....*....|....*....|..
gi 2651418669 853 -IIALTAKampndKEKCLSA---GASDYISKP 880
Cdd:cd17532    74 lIVFVTAY-----DEYAVEAfelNAVDYLLKP 100
PRK10816 PRK10816
two-component system response regulator PhoP;
778-890 1.44e-04

two-component system response regulator PhoP;


Pssm-ID: 182755 [Multi-domain]  Cd Length: 223  Bit Score: 44.34  E-value: 1.44e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 778 ILIVDDdhrnifalqNALKKHHANII---------TAQNGLECLEILKNNTNiDLILMDIMMPNMDGYETMEHIRMNLgl 848
Cdd:PRK10816    3 VLVVED---------NALLRHHLKVQlqdaghqvdAAEDAKEADYYLNEHLP-DIAIVDLGLPDEDGLSLIRRWRSND-- 70
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 2651418669 849 HEIPIIALTAKAMPNDKEKCLSAGASDYISKPLNLHQLYSVM 890
Cdd:PRK10816   71 VSLPILVLTARESWQDKVEVLSAGADDYVTKPFHIEEVMARM 112
HATPase_UhpB-NarQ-NarX-like cd16917
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
617-731 1.58e-04

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


Pssm-ID: 340394 [Multi-domain]  Cd Length: 87  Bit Score: 41.39  E-value: 1.58e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 617 QIIKNLLSNAFKFTEKGSVSLHfdsietsnLSHDmqsisKDWITISVKDTGIGIAKEQHQlifeafqqadgatirkyGGT 696
Cdd:cd16917     3 RIVQEALTNALKHAGASRVRVT--------LSYT-----ADELTLTVVDDGVGFDGPAPP-----------------GGG 52
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2651418669 697 GLGLSICKEFARLLGGWITLESNVGEGSTFTVYIP 731
Cdd:cd16917    53 GFGLLGMRERAELLGGTLTIGSRPGGGTRVTARLP 87
dpiB PRK15053
sensor histidine kinase DpiB; Provisional
611-731 1.65e-04

sensor histidine kinase DpiB; Provisional


Pssm-ID: 185013 [Multi-domain]  Cd Length: 545  Bit Score: 45.21  E-value: 1.65e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 611 DAKRIEQIIKNLLSNAFKFTEKgsvslhfdSIETSNLSHDMQSISKDWITISVKDTGIGIAKEQHQLIFEafqQADGATI 690
Cdd:PRK15053  429 DSTEFAAIVGNLLDNAFEASLR--------SDEGNKIVELFLSDEGDDVVIEVADQGCGVPESLRDKIFE---QGVSTRA 497
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 2651418669 691 RKYGGTGLGLSICKEFARLLGGWITLESNVGEGSTFTVYIP 731
Cdd:PRK15053  498 DEPGEHGIGLYLIASYVTRCGGVITLEDNDPCGTLFSIFIP 538
HATPase_PDK-like cd16929
Histidine kinase-like ATPase domain of pyruvate dehydrogenase kinase, branched-chain ...
615-731 2.38e-04

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: 42.71  E-value: 2.38e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 615 IEQIIKNLLSNAFKFTEK--GSVSLHFDSIETSNLSHDmqsiskDWITISVKDTGIGIAKEQHQLIF-----EAFQQA-- 685
Cdd:cd16929    44 LYYILFELLKNAMRATVEshGDDSDDLPPIKVTVAKGD------EDLTIKISDRGGGIPREDLARLFsymysTAPQPSld 117
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2651418669 686 ------DGATIRKYGGTGLGLSICKEFARLLGGWITLESNVGEGSTFTVYIP 731
Cdd:cd16929   118 dfsdliSGTQPSPLAGFGYGLPMSRLYAEYFGGDLDLQSMEGYGTDVYIYLK 169
HAMP cd06225
Histidine kinase, Adenylyl cyclase, Methyl-accepting protein, and Phosphatase (HAMP) domain; ...
207-252 4.03e-04

Histidine kinase, Adenylyl cyclase, Methyl-accepting protein, and Phosphatase (HAMP) domain; HAMP is a signaling domain which occurs in a wide variety of signaling proteins, many of which are bacterial. The HAMP domain consists of two alpha helices connected by an extended linker. The structure of the Af1503 HAMP dimer from Archaeoglobus fulgidus has been solved using nuclear magnetic resonance, revealing a parallel four-helix bundle; this structure has been confirmed by cross-linking analysis of HAMP domains from the Escherichia coli aerotaxis receptor Aer. It has been suggested that the four-helix arrangement can rotate between the unusually packed conformation observed in the NMR structure and a canonical coiled-coil arrangement. Such rotation may coincide with signal transduction, but a common mechanism by which HAMP domains relay a variety of input signals has yet to be established.


Pssm-ID: 381743 [Multi-domain]  Cd Length: 45  Bit Score: 38.58  E-value: 4.03e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 2651418669 207 TKTIKNVIQAIKSISSKEkITERIHVNSHDEIKDLAHTTNHLLDEI 252
Cdd:cd06225     1 TRPLRRLTEAARRIAEGD-LDVRVPVRSKDEIGELARAFNQMAERL 45
COG4192 COG4192
Signal transduction histidine kinase regulating phosphoglycerate transport system [Signal ...
446-723 4.11e-04

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


Pssm-ID: 443346 [Multi-domain]  Cd Length: 640  Bit Score: 43.91  E-value: 4.11e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 446 ELQMQAEELRTTNEQLESRTEEAEQKTADLQVTKLELEEKASELLRSSKYKS--EFLANMSHELRTPLN--SILLLS--E 519
Cdd:COG4192   381 EIGRIARLLRVFRDQAIEKTQELETEIEERKRIEKNLRQTQDELIQAAKMAVvgQTMTSLAHELNQPLNamSMYLFSakK 460
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 520 MLKENHDNHLSDDEIELATVIHSSGKdlltLINDILDLSKVEAGKL------DVIFEATNISDMAASMHQNFLHIAAQKN 593
Cdd:COG4192   461 ALEQENYAQLPTSLDKIEGLIERMDK----IIKSLRQFSRKSDTPLqpvdlrQVIEQAWELVESRAKPQQITLHIPDDLM 536
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 594 VeftvedsdtipdlfYTDAKRIEQIIKNLLSNAFkftekgsvslhfDSIETSNLSHDMQSISKDWITISVKDTGIGIAKE 673
Cdd:COG4192   537 V--------------QGDQVLLEQVLVNLLVNAL------------DAVATQPQISVDLLSNAENLRVAISDNGNGWPLV 590
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 2651418669 674 QHqlIFEAFqqadgaTIRKYGGTGLGLSICKEFARLLGGWITLESNVGEG 723
Cdd:COG4192   591 DK--LFTPF------TTTKEVGLGLGLSICRSIMQQFGGDLYLASTLERG 632
HATPase_NtrY-like cd16944
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
611-731 4.95e-04

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: 40.60  E-value: 4.95e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 611 DAKRIEQIIKNLLSNAFKFTE-----KGSVSLhfdsietsnlshDMQSISKDWITISVKDTGIGIAKEQHQLIFEAFqqa 685
Cdd:cd16944     1 DTTQISQVLTNILKNAAEAIEgrpsdVGEVRI------------RVEADQDGRIVLIVCDNGKGFPREMRHRATEPY--- 65
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2651418669 686 dgATIRKyGGTGLGLSICKEFARLLGGWITLESNVGEGSTFTVYIP 731
Cdd:cd16944    66 --VTTRP-KGTGLGLAIVKKIMEEHGGRISLSNREAGGACIRIILP 108
PRK10815 PRK10815
two-component system sensor histidine kinase PhoQ;
621-705 6.23e-04

two-component system sensor histidine kinase PhoQ;


Pssm-ID: 182754 [Multi-domain]  Cd Length: 485  Bit Score: 43.47  E-value: 6.23e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 621 NLLSNAFKFTekgsvsLHFdsIETSNLSHDmqsiskDWITISVKDTGIGIAKEQHQLIFEAFQQADgaTIRKygGTGLGL 700
Cdd:PRK10815  385 NVLDNACKYC------LEF--VEISARQTD------EHLHIVVEDDGPGIPESKRELIFDRGQRAD--TLRP--GQGLGL 446

                  ....*
gi 2651418669 701 SICKE 705
Cdd:PRK10815  447 SVARE 451
HATPase_CheA-like cd16916
Histidine kinase-like ATPase domain of the chemotaxis protein histidine kinase CheA, and some ...
659-731 6.48e-04

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


Pssm-ID: 340393 [Multi-domain]  Cd Length: 178  Bit Score: 41.41  E-value: 6.48e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 659 ITISVKDTGIGIAKEQ------------------------HQLIFEA-FQQADgaTIRKYGGTGLGLSICKEFARLLGGW 713
Cdd:cd16916    83 VVIEVSDDGRGIDREKirekaierglitadeaatlsddevLNLIFAPgFSTAE--QVTDVSGRGVGMDVVKRSIESLGGT 160
                          90
                  ....*....|....*...
gi 2651418669 714 ITLESNVGEGSTFTVYIP 731
Cdd:cd16916   161 IEVESEPGQGTTFTIRLP 178
PRK10651 PRK10651
transcriptional regulator NarL; Provisional
777-879 6.55e-04

transcriptional regulator NarL; Provisional


Pssm-ID: 182619 [Multi-domain]  Cd Length: 216  Bit Score: 41.94  E-value: 6.55e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 777 TILIVDDdH---RN----IFALQNALKKhhanIITAQNGLECLEiLKNNTNIDLILMDIMMPNMDGYETMEHIRMNlGLh 849
Cdd:PRK10651    8 TILLIDD-HpmlRTgvkqLISMAPDITV----VGEASNGEQGIE-LAESLDPDLILLDLNMPGMNGLETLDKLREK-SL- 79
                          90       100       110
                  ....*....|....*....|....*....|
gi 2651418669 850 EIPIIALTAKAMPNDKEKCLSAGASDYISK 879
Cdd:PRK10651   80 SGRIVVFSVSNHEEDVVTALKRGADGYLLK 109
HAMP pfam00672
HAMP domain;
202-254 7.15e-04

HAMP domain;


Pssm-ID: 459898 [Multi-domain]  Cd Length: 53  Bit Score: 38.37  E-value: 7.15e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2651418669 202 ISNSITKTIKNVIQAIKSISSKEkITERIHVNSHDEIKDLAHTTNHLLDEISK 254
Cdd:pfam00672   2 LARRILRPLRRLAEAARRIASGD-LDVRLPVSGRDEIGELARAFNQMAERLRE 53
DUF3450 pfam11932
Protein of unknown function (DUF3450); This family of proteins are functionally ...
425-490 8.51e-04

Protein of unknown function (DUF3450); This family of proteins are functionally uncharacterized. This protein is found in bacteria and eukaryotes. Proteins in this family are about 260 amino acids in length.


Pssm-ID: 432198 [Multi-domain]  Cd Length: 238  Bit Score: 41.83  E-value: 8.51e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2651418669 425 ESQAMTEELQVQSEELQTQAEELQMQAEELRTTNEQLESRTEEAEQKTADLQVTKLELEEKASELL 490
Cdd:pfam11932  31 QSQKKIDKWDDEKQELLAEYRALKAELESLEVYNRQLERLVASQEQEIASLERQIEEIERTERELV 96
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
418-537 9.18e-04

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 43.00  E-value: 9.18e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 418 RIQTLLYESQAMTEELQVQSEELQTQAEELQMQAEELRTTNEQLESRTEEAEQKTADLQVTKLELEEKASELLRSSKYKS 497
Cdd:COG1196   317 RLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAA 396
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2651418669 498 EFLANMSHELRTPLNSILLLSEMLKENHDNHLSDDEIELA 537
Cdd:COG1196   397 ELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEE 436
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
423-489 1.11e-03

Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related proteins, ezrin, radixin and moesin. Ezrin was first identified as a constituent of microvilli, radixin as a barbed, end-capping actin-modulating protein from isolated junctional fractions, and moesin as a heparin binding protein. A tumour suppressor molecule responsible for neurofibromatosis type 2 (NF2) is highly similar to ERM proteins and has been designated merlin (moesin-ezrin-radixin-like protein). ERM molecules contain 3 domains, an N-terminal globular domain, an extended alpha-helical domain and a charged C-terminal domain (pfam00769). Ezrin, radixin and merlin also contain a polyproline linker region between the helical and C-terminal domains. The N-terminal domain is highly conserved and is also found in merlin, band 4.1 proteins and members of the band 4.1 superfamily, designated the FERM domain. ERM proteins crosslink actin filaments with plasma membranes. They co-localize with CD44 at actin filament plasma membrane interaction sites, associating with CD44 via their N-terminal domains and with actin filaments via their C-terminal domains. This is the alpha-helical domain, which is involved in intramolecular masking of protein-protein interaction sites, regulating the activity of this proteins.


Pssm-ID: 466641 [Multi-domain]  Cd Length: 120  Bit Score: 39.52  E-value: 1.11e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 423 LYESQAMTEELQVQSEELQTQAEEL---QMQAEELRT-----------TNEQLESRTEEAEQKTADLQVTKLELEEKASE 488
Cdd:pfam20492  29 LEESEETAEELEEERRQAEEEAERLeqkRQEAEEEKErleesaemeaeEKEQLEAELAEAQEEIARLEEEVERKEEEARR 108

                  .
gi 2651418669 489 L 489
Cdd:pfam20492 109 L 109
REC_hyHK_blue-like cd18161
phosphoacceptor receiver (REC) domain of hybrid sensor histidine kinase/response regulators ...
778-843 1.22e-03

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: 39.25  E-value: 1.22e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2651418669 778 ILIVDDDHRNIFALQNALKKHHANIITAQNGLECLEILKNNTNIDLILMDIMMPN-MDGYETMEHIR 843
Cdd:cd18161     1 VLVVEDDPDVRRLTAEVLEDLGYTVLEAASGDEALDLLESGPDIDLLVTDVIMPGgMNGSQLAEEAR 67
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
418-539 1.66e-03

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 42.35  E-value: 1.66e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669  418 RIQTLLYESQAMtEELQVQSEELQTQAEELQMQAEELRTTNEQLESRTEEAEQKTADLQVTKLELEEKASELLRSSKYKS 497
Cdd:TIGR02168  668 TNSSILERRREI-EELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLE 746
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 2651418669  498 EFLANMSHELRTPLNSILLLSEMLKENHDnHLSDDEIELATV 539
Cdd:TIGR02168  747 ERIAQLSKELTELEAEIEELEERLEEAEE-ELAEAEAEIEEL 787
PRK09039 PRK09039
peptidoglycan -binding protein;
396-499 1.84e-03

peptidoglycan -binding protein;


Pssm-ID: 181619 [Multi-domain]  Cd Length: 343  Bit Score: 41.49  E-value: 1.84e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 396 QDLiQQTVDNLGLTIHSIMG-RMRIQTLLYESQAMTEELQVQ--------------SEELQTQAEELQMQAEELRttnEQ 460
Cdd:PRK09039   77 QDL-QDSVANLRASLSAAEAeRSRLQALLAELAGAGAAAEGRagelaqeldsekqvSARALAQVELLNQQIAALR---RQ 152
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 2651418669 461 L----------ESRTEEAEQKTADL-QVTKLELEEKASELlrsSKYKSEF 499
Cdd:PRK09039  153 LaaleaaldasEKRDRESQAKIADLgRRLNVALAQRVQEL---NRYRSEF 199
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
416-484 1.87e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 41.95  E-value: 1.87e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2651418669 416 RMRIQTLLYESQAMTEELQVQSEELQTQAEELQMQAEELRTTNEQLESRTEEAEQKTADLQVTKLELEE 484
Cdd:PRK02224  518 REDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKE 586
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
394-508 1.93e-03

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 41.67  E-value: 1.93e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 394 LHQDLIQQTVDNLGLtIHSIMGRMRIQTLLYESQamTEELQVQSEELQTQAEELQMQAEELRTTNEQLESRTEEAEQKTA 473
Cdd:COG4942   126 LSPEDFLDAVRRLQY-LKYLAPARREQAEELRAD--LAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLA 202
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2651418669 474 DLQVTKLELEEKASELLRSSKYKSEFLANMSHELR 508
Cdd:COG4942   203 RLEKELAELAAELAELQQEAEELEALIARLEAEAA 237
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
416-621 2.80e-03

Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 41.63  E-value: 2.80e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 416 RMRIQTLLYESQAMTEELQVQS-------EELQTQAEELQ-------MQAEELRTTNEQLES--RTEEA--EQKTADLQV 477
Cdd:pfam05483 302 KMSLQRSMSTQKALEEDLQIATkticqltEEKEAQMEELNkakaahsFVVTEFEATTCSLEEllRTEQQrlEKNEDQLKI 381
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 478 TKLELEEKASELLRSSKYKSEFLANMsHELRTPL--NSILLLSEMLKENHDNHLSDDEIELATVIHSSGKDL------LT 549
Cdd:pfam05483 382 ITMELQKKSSELEEMTKFKNNKEVEL-EELKKILaeDEKLLDEKKQFEKIAEELKGKEQELIFLLQAREKEIhdleiqLT 460
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2651418669 550 LINDILDLSKVEAGKLDVIFEATNISDMAASMHQNFLHIaaqKNVEFTVEDSDTIPDLfytdAKRIEQIIKN 621
Cdd:pfam05483 461 AIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLL---ENKELTQEASDMTLEL----KKHQEDIINC 525
COG3920 COG3920
Two-component sensor histidine kinase, HisKA and HATPase domains [Signal transduction ...
622-731 2.81e-03

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


Pssm-ID: 443125 [Multi-domain]  Cd Length: 495  Bit Score: 41.43  E-value: 2.81e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 622 LLSNAFKF----TEKGSVSLHFdsietsnlshdmqSISKDWITISVKDTGIGIAkeqhqlifeafqqadgATIRKYGGTG 697
Cdd:COG3920   407 LVTNALKHaflsGEGGRIRVSW-------------RREDGRLRLTVSDNGVGLP----------------EDVDPPARKG 457
                          90       100       110
                  ....*....|....*....|....*....|....
gi 2651418669 698 LGLSICKEFARLLGGwiTLESNVGEGSTFTVYIP 731
Cdd:COG3920   458 LGLRLIRALVRQLGG--TLELDRPEGTRVRITFP 489
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
399-509 3.34e-03

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 41.08  E-value: 3.34e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 399 IQQTVDNLGLTIHSIMGRMRIQTLlyESQAMTEELQVQSEELQTQAEELQMQAEELRTTNEQLESRTEEAEQKTADLQVT 478
Cdd:COG1196   272 LRLELEELELELEEAQAEEYELLA--ELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEA 349
                          90       100       110
                  ....*....|....*....|....*....|.
gi 2651418669 479 KLELEEKASELLRSSKYKSEFLANMSHELRT 509
Cdd:COG1196   350 EEELEEAEAELAEAEEALLEAEAELAEAEEE 380
GAF smart00065
Domain present in phytochromes and cGMP-specific phosphodiesterases; Mutations within these ...
280-426 3.59e-03

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: 38.90  E-value: 3.59e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669  280 NKILSGIIQKTQTSCGAFYVREEvEDTVYYVKKASFAEQGADIGkQSIKMGEGFIGQTALEKKSFILRDIPEEFRY-VTT 358
Cdd:smart00065   7 QTILEELRQLLGADRVLIYLVDE-NDRGELVLVAADGLTLPTLG-IRFPLDEGLAGRVAETGRPLNIPDVEADPLFaEDL 84
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2651418669  359 GLLEIRPKNLLVIPVLFEDEVIAVMELVSVTDISDLHQD---LIQQTVDNLGLTIHsimgrmriQTLLYES 426
Cdd:smart00065  85 LGRYQGVRSFLAVPLVADGELVGVLALHNKKSPRPFTEEdeeLLQALANQLAIALA--------NAQLYEE 147
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
431-506 3.67e-03

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 41.08  E-value: 3.67e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2651418669 431 EELQVQSEELQTQAEELQMQAEELRTTNEQLESRTEEAEQKTADLQvtkLELEEKASELLRSSKYKSEFLANMSHE 506
Cdd:COG1196   235 RELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELE---LELEEAQAEEYELLAELARLEQDIARL 307
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
427-490 3.69e-03

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 40.58  E-value: 3.69e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2651418669 427 QAMTEELQVQSEELQTQAEELQMQAEELRTTNEQLESRTEEAEQKTADLQVTKLELEEKASELL 490
Cdd:COG3883   132 ADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAE 195
Dynactin pfam12455
Dynein associated protein; This domain family is found in eukaryotes, and is approximately 280 ...
427-556 3.94e-03

Dynein associated protein; This domain family is found in eukaryotes, and is approximately 280 amino acids in length. The family is found in association with pfam01302. There is a single completely conserved residue E that may be functionally important. Dynactin has been associated with Dynein, a kinesin protein which is involved in organelle transport, mitotic spindle assembly and chromosome segregation. Dynactin anchors Dynein to specific subcellular structures.


Pssm-ID: 463591  Cd Length: 287  Bit Score: 40.29  E-value: 3.94e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 427 QAMTEELQVQSEELQTQAEELQMQAEELRTTNEQLESRTEEAEQKTADLQVTKLELEEkASELLrssKYKSEFL--ANMS 504
Cdd:pfam12455   2 QSDLEDLRASQQITESESEDLSSRSRAMMDLNLKLQSSASKAQAKAIDLELRRLEAQQ-ASEHL---EIVQLFLpdSFLR 77
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2651418669 505 HELRTPLNSIL----------LLSEMLKENH---DNHLSDDEIELATVIHSSGKDLLTLINDILD 556
Cdd:pfam12455  78 RGDRDSVLALLlfkrlafkadLLASQIREKFplsESLILKGHVEEQLFFACELLEKLTWLSALCD 142
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
418-498 4.05e-03

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 40.52  E-value: 4.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 418 RIQTLLYESQAMTEELQVQSEELQTQAEELQMQAEELRTTNEQLESRTEEAEQKTADLQVTKLELEEKASELLRSSKYKS 497
Cdd:COG4942   161 ELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAA 240

                  .
gi 2651418669 498 E 498
Cdd:COG4942   241 E 241
PRK15369 PRK15369
two component system response regulator;
778-879 4.36e-03

two component system response regulator;


Pssm-ID: 185267 [Multi-domain]  Cd Length: 211  Bit Score: 39.68  E-value: 4.36e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 778 ILIVDDDHRNIFALQNALKKH-HANII-TAQNGLECLEILKNnTNIDLILMDIMMPNMDGYETMEHIRMNlgLHEIPIIA 855
Cdd:PRK15369    6 ILLVDDHELIINGIKNMLAPYpRYKIVgQVDNGLEVYNACRQ-LEPDIVILDLGLPGMNGLDVIPQLHQR--WPAMNILV 82
                          90       100
                  ....*....|....*....|....
gi 2651418669 856 LTAKAMPNDKEKCLSAGASDYISK 879
Cdd:PRK15369   83 LTARQEEHMASRTLAAGALGYVLK 106
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
418-523 4.52e-03

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 40.81  E-value: 4.52e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669  418 RIQTLLYESQAMTEELQVQSEELQTQAEELQMQAEELRTTNEQLESRTEEAEQKTADLQVTKLELEEKASELLRSSKYKS 497
Cdd:TIGR02168  257 ELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELA 336
                           90       100
                   ....*....|....*....|....*.
gi 2651418669  498 EFLANMSHELRTPLNSILLLSEMLKE 523
Cdd:TIGR02168  337 EELAELEEKLEELKEELESLEAELEE 362
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
418-526 6.30e-03

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 40.43  E-value: 6.30e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669  418 RIQTLLYESQAMTEELQVQSEELQTQAEELQMQAEELRTTNEQLESRTEEAEQKTADLQVTKLELEEKASELLRSSKYKS 497
Cdd:TIGR02168  243 ELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELE 322
                           90       100       110
                   ....*....|....*....|....*....|..
gi 2651418669  498 EFLA---NMSHELRTPLNSILLLSEMLKENHD 526
Cdd:TIGR02168  323 AQLEeleSKLDELAEELAELEEKLEELKEELE 354
HAMP smart00304
HAMP (Histidine kinases, Adenylyl cyclases, Methyl binding proteins, Phosphatases) domain;
204-256 6.46e-03

HAMP (Histidine kinases, Adenylyl cyclases, Methyl binding proteins, Phosphatases) domain;


Pssm-ID: 197640 [Multi-domain]  Cd Length: 53  Bit Score: 35.69  E-value: 6.46e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2651418669  204 NSITKTIKNVIQAIKSISSKEkITERIHVNSHDEIKDLAHTTNHLLDEISKRE 256
Cdd:smart00304   1 RRLLRPLRRLAEAAQRIADGD-LTVRLPVDGRDEIGELARAFNEMADRLEETI 52
REC_RcNtrC-like cd19928
phosphoacceptor receiver (REC) domain of Rhodobacter capsulatus nitrogen regulatory protein C ...
778-880 6.94e-03

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


Pssm-ID: 381155 [Multi-domain]  Cd Length: 100  Bit Score: 37.10  E-value: 6.94e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 778 ILIVDDDHRNIFALQNALKKHHANIITAQNGLECLEILKNNTNiDLILMDIMMPNMDGYETMEHIRMNLGlhEIPIIALT 857
Cdd:cd19928     1 ILVADDDRAIRTVLTQALGRAGYEVRTTGNAATLWRWVEEGEG-DLVITDVVMPDENGLDLIPRIKKARP--DLPIIVMS 77
                          90       100
                  ....*....|....*....|...
gi 2651418669 858 AKAMPNDKEKCLSAGASDYISKP 880
Cdd:cd19928    78 AQNTLMTAVKAAERGAFEYLPKP 100
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
420-489 6.96e-03

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 40.44  E-value: 6.96e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669  420 QTLLYESQAMTEELQVQSEELQTQAEELQMQAEELRTTNEQLESRTEEAEQKTADLQVTKLELEEKASEL 489
Cdd:TIGR02169  708 SQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKL 777
ZapB COG3074
Cell division protein ZapB, interacts with FtsZ [Cell cycle control, cell division, chromosome ...
427-489 7.59e-03

Cell division protein ZapB, interacts with FtsZ [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442308 [Multi-domain]  Cd Length: 79  Bit Score: 36.10  E-value: 7.59e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2651418669 427 QAMTEELQVQSEELQTQAEELQMQAEELRTTNEQLESRTEEAEQKTADLQVTKLELEEKASEL 489
Cdd:COG3074    17 VDTIELLQMEVEELKEKNEELEQENEELQSENEELQSENEQLKTENAEWQERIRSLLGKIDEV 79
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
440-509 9.14e-03

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 39.36  E-value: 9.14e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651418669 440 LQTQAEELQMQAEELRTTNEQLESRTEEAEQKTADLQVTKLELEEKASELLRSSKYKSEFLANMSHELRT 509
Cdd:COG4942   141 LKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAE 210
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
418-489 9.78e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 39.12  E-value: 9.78e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2651418669 418 RIQTLLYESQAMTEELQVQSEELQTQAEELQMQAEELRTTNEQLESRTEEAEQKTADLQVTKLELEEKASEL 489
Cdd:COG4372    39 ELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEA 110
 
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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