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Conserved domains on  [gi|1889623460|ref|WP_182717850|]
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MULTISPECIES: ATP-binding protein [unclassified Pseudoalteromonas]

Protein Classification

sensor histidine kinase family protein( domain architecture ID 1001650)

sensor histidine kinase family protein, part of a two-component regulatory system, functions as a protein kinase that phosphorylates a target protein in response to various signals; may be a hybrid sensor histidine kinase/response regulator

CATH:  3.30.565.10
EC:  2.7.13.3
PubMed:  10637609|10339418
SCOP:  4001957

Graphical summary

 Zoom to residue level

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List of domain hits

Name Accession Description Interval E-value
PRK11107 super family cl35992
hybrid sensory histidine kinase BarA; Provisional
483-1014 2.29e-101

hybrid sensory histidine kinase BarA; Provisional


The actual alignment was detected with superfamily member PRK11107:

Pssm-ID: 236848 [Multi-domain]  Cd Length: 919  Bit Score: 339.52  E-value: 2.29e-101
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  483 LNSTLEQKVRQrTTELESAIEQALAASKSKSDFIANISHEIRTPMNGVLGML-EMLKEDtLTQQQQQYLELANSSANSLM 561
Cdd:PRK11107   265 LRETLEQMEIQ-NVELDLAKKRAQEAARIKSEFLANMSHELRTPLNGVIGFTrQTLKTP-LTPTQRDYLQTIERSANNLL 342
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  562 TLINDILDFSKIEAGKLDIDNHSFDVITVCSDMITSMALQAQRKGLEVFLHTDKVIDRMLVGDSHRLKQILINLLNNAFK 641
Cdd:PRK11107   343 AIINDILDFSKLEAGKLVLENIPFSLRETLDEVVTLLAHSAHEKGLELTLNIDPDVPDNVIGDPLRLQQIITNLVGNAIK 422
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  642 FTHQGEVSLTLGCQYLTEEKLLMSFVIEDSGIGIAEKNIDKLFEAFTQEDTSTTRHFGGTGLGLSICRKLAQLMGGDISV 721
Cdd:PRK11107   423 FTESGNIDILVELRALSNTKVQLEVQIRDTGIGISERQQSQLFQAFRQADASISRRHGGTGLGLVITQKLVNEMGGDISF 502
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  722 TSEKGQGSCFTAQVQLHI---AAEKKLNTAVELAKDIqvgVLIDSDSVYNNVTNLLIKNCQVAANNIQRFdyqAQYQELK 798
Cdd:PRK11107   503 HSQPNRGSTFWFHLPLDLnpnPIIDGLPTDCLAGKRL---LYVEPNSAAAQATLDILSETPLEVTYSPTL---SQLPEAH 576
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  799 VDLLVVDNDHPYLQTLINLCNKQNK-----KYVLIL---RDLLLSKKAKEQVPENChvLNKPLTqdqfSYKLASLFGVNN 870
Cdd:PRK11107   577 YDILLLGLPVTFREPLTMLHERLAKaksmtDFLILAlpcHEQVLAEQLKQDGADAC--LSKPLS----HTRLLPALLEPC 650
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  871 SFLVASQGSEQTEYVEydfsNFKVLLVDDNMINLEVAKAILKNTGVTIVCASDGLDALEiLNTEQTalFDLILMDCQMPN 950
Cdd:PRK11107   651 HHKQPPLLPPTDESRL----PLTVMAVDDNPANLKLIGALLEEQVEHVVLCDSGHQAVE-QAKQRP--FDLILMDIQMPG 723
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1889623460  951 LNGYDTTSAIRSNKAgadYAKVPIIAMTASAMAGDRERCITAGMNDYITKPIKPKVLKDKLAMW 1014
Cdd:PRK11107   724 MDGIRACELIRQLPH---NQNTPIIAVTAHAMAGERERLLSAGMDDYLAKPIDEAMLKQVLLRY 784
RocR super family cl34674
RocR-type transcriptional regulator, contains PAS, AAA-type ATPase, and DNA-binding Fis ...
355-513 2.55e-05

RocR-type transcriptional regulator, contains PAS, AAA-type ATPase, and DNA-binding Fis domains [Transcription, Signal transduction mechanisms];


The actual alignment was detected with superfamily member COG3829:

Pssm-ID: 443041 [Multi-domain]  Cd Length: 448  Bit Score: 47.84  E-value: 2.55e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  355 RKLEFHSLKERNNKIIENSLDAILTVQEDGLISNANKTALQFFDI----IIDHtKFTQLFtlaesDNSCIDETIAQGSkp 430
Cdd:COG3829      2 EELELKELEEELEAILDSLDDGIIVVDADGRITYVNRAAERILGLpreeVIGK-NVTELI-----PNSPLLEVLKTGK-- 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  431 SFEGVYTDPQDQQHFYSITLTSVFDiFTQRHQVAAILRNINSLKQTQVELEKLNstLEQKVRQRTT---------ELESA 501
Cdd:COG3829     74 PVTGVIQKTGGKGKTVIVTAIPIFE-DGEVIGAVETFRDITELKRLERKLREEE--LERGLSAKYTfddiigkspAMKEL 150
                          170
                   ....*....|..
gi 1889623460  502 IEQALAASKSKS 513
Cdd:COG3829    151 LELAKRVAKSDS 162
 
Name Accession Description Interval E-value
PRK11107 PRK11107
hybrid sensory histidine kinase BarA; Provisional
483-1014 2.29e-101

hybrid sensory histidine kinase BarA; Provisional


Pssm-ID: 236848 [Multi-domain]  Cd Length: 919  Bit Score: 339.52  E-value: 2.29e-101
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  483 LNSTLEQKVRQrTTELESAIEQALAASKSKSDFIANISHEIRTPMNGVLGML-EMLKEDtLTQQQQQYLELANSSANSLM 561
Cdd:PRK11107   265 LRETLEQMEIQ-NVELDLAKKRAQEAARIKSEFLANMSHELRTPLNGVIGFTrQTLKTP-LTPTQRDYLQTIERSANNLL 342
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  562 TLINDILDFSKIEAGKLDIDNHSFDVITVCSDMITSMALQAQRKGLEVFLHTDKVIDRMLVGDSHRLKQILINLLNNAFK 641
Cdd:PRK11107   343 AIINDILDFSKLEAGKLVLENIPFSLRETLDEVVTLLAHSAHEKGLELTLNIDPDVPDNVIGDPLRLQQIITNLVGNAIK 422
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  642 FTHQGEVSLTLGCQYLTEEKLLMSFVIEDSGIGIAEKNIDKLFEAFTQEDTSTTRHFGGTGLGLSICRKLAQLMGGDISV 721
Cdd:PRK11107   423 FTESGNIDILVELRALSNTKVQLEVQIRDTGIGISERQQSQLFQAFRQADASISRRHGGTGLGLVITQKLVNEMGGDISF 502
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  722 TSEKGQGSCFTAQVQLHI---AAEKKLNTAVELAKDIqvgVLIDSDSVYNNVTNLLIKNCQVAANNIQRFdyqAQYQELK 798
Cdd:PRK11107   503 HSQPNRGSTFWFHLPLDLnpnPIIDGLPTDCLAGKRL---LYVEPNSAAAQATLDILSETPLEVTYSPTL---SQLPEAH 576
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  799 VDLLVVDNDHPYLQTLINLCNKQNK-----KYVLIL---RDLLLSKKAKEQVPENChvLNKPLTqdqfSYKLASLFGVNN 870
Cdd:PRK11107   577 YDILLLGLPVTFREPLTMLHERLAKaksmtDFLILAlpcHEQVLAEQLKQDGADAC--LSKPLS----HTRLLPALLEPC 650
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  871 SFLVASQGSEQTEYVEydfsNFKVLLVDDNMINLEVAKAILKNTGVTIVCASDGLDALEiLNTEQTalFDLILMDCQMPN 950
Cdd:PRK11107   651 HHKQPPLLPPTDESRL----PLTVMAVDDNPANLKLIGALLEEQVEHVVLCDSGHQAVE-QAKQRP--FDLILMDIQMPG 723
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1889623460  951 LNGYDTTSAIRSNKAgadYAKVPIIAMTASAMAGDRERCITAGMNDYITKPIKPKVLKDKLAMW 1014
Cdd:PRK11107   724 MDGIRACELIRQLPH---NQNTPIIAVTAHAMAGERERLLSAGMDDYLAKPIDEAMLKQVLLRY 784
TMAO_torS TIGR02956
TMAO reductase sytem sensor TorS; This protein, TorS, is part of a regulatory system for the ...
460-1016 2.07e-75

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: 268.18  E-value: 2.07e-75
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  460 RHQVAAILRNINSLKQTQVELEKLNSTLEQKVRQRTTELES--------AIEQALA------ASKSKSDFIANISHEIRT 525
Cdd:TIGR02956  398 RDTAAHNLKLQADERQVAQELQEHKESLEQLVAQRTQELAEtnerlnaeVKNHAKAraeaeeANRAKSAFLATMSHEIRT 477
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  526 PMNGVLGMLEMLKEDTLTQQQQQYLELANSSANSLMTLINDILDFSKIEAGKLDIDNHSFDVITVCSDMITSMALQAQRK 605
Cdd:TIGR02956  478 PLNGILGTLELLGDTGLTSQQQQYLQVINRSGESLLDILNDILDYSKIEAGHLSISPRPFDLNALLDDVHHLMVSRAQLK 557
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  606 GLEVFLHTDKVIDRMLVGDSHRLKQILINLLNNAFKFTHQGEVSLTLGCQylTEEKLLmsFVIEDSGIGIAEKNIDKLFE 685
Cdd:TIGR02956  558 GIQLRLNIPEQLPNWWQGDGPRIRQVLINLVGNAIKFTDRGSVVLRVSLN--DDSSLL--FEVEDTGCGIAEEEQATLFD 633
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  686 AFTQEDtsTTRHFGGTGLGLSICRKLAQLMGGDISVTSEKGQGSCFTAQVqlhiaaekklntavelakdiqvgvlidsds 765
Cdd:TIGR02956  634 AFTQAD--GRRRSGGTGLGLAISQRLVEAMDGELGVESELGVGSCFWFTL------------------------------ 681
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  766 vynnvtnllikncqvaanniqrfdyqaqyqelkvdllvvdndhpylqtlinlcnkqnkkyvlilrdlllskkakeqvpen 845
Cdd:TIGR02956      --------------------------------------------------------------------------------
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  846 chvlnkPLTQDQfsyklaslfgvnnsflvASQGSEQTEYVeyDFSNFKVLLVDDNMINLEVAKAILKNTGVTIVCASDGL 925
Cdd:TIGR02956  682 ------PLTRGK-----------------PAEDSATLTVI--DLPPQRVLLVEDNEVNQMVAQGFLTRLGHKVTLAESGQ 736
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  926 DALEILNTEQtalFDLILMDCQMPNLNGYDTTSAIRSNKAGADyaKVPIIAMTASAMAGDRERCITAGMNDYITKPIKPK 1005
Cdd:TIGR02956  737 SALECFHQHA---FDLALLDINLPDGDGVTLLQQLRAIYGAKN--EVKFIAFSAHVFNEDVAQYLAAGFDGFLAKPVVEE 811
                          570
                   ....*....|.
gi 1889623460 1006 VLKDKLAMWLK 1016
Cdd:TIGR02956  812 QLTAMIAVILA 822
BaeS COG0642
Signal transduction histidine kinase [Signal transduction mechanisms];
485-732 9.65e-73

Signal transduction histidine kinase [Signal transduction mechanisms];


Pssm-ID: 440407 [Multi-domain]  Cd Length: 328  Bit Score: 244.05  E-value: 9.65e-73
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  485 STLEQKVRQRTTELESAIEQALAASKSKSDFIANISHEIRTPMNGVLGMLEMLkEDTLTQQQQQYLELANSSANSLMTLI 564
Cdd:COG0642     83 LLLLLLLLLLLLLLLALLLLLEEANEAKSRFLANVSHELRTPLTAIRGYLELL-LEELDEEQREYLETILRSADRLLRLI 161
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  565 NDILDFSKIEAGKLDIDNHSFDVITVCSDMITSMALQAQRKGLEVFLHTDKVIdRMLVGDSHRLKQILINLLNNAFKFTH 644
Cdd:COG0642    162 NDLLDLSRLEAGKLELEPEPVDLAELLEEVVELFRPLAEEKGIELELDLPDDL-PTVRGDPDRLRQVLLNLLSNAIKYTP 240
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  645 QG-EVSLTlgcqyLTEEKLLMSFVIEDSGIGIAEKNIDKLFEAFTQEDTSttRHFGGTGLGLSICRKLAQLMGGDISVTS 723
Cdd:COG0642    241 EGgTVTVS-----VRREGDRVRISVEDTGPGIPPEDLERIFEPFFRTDPS--RRGGGTGLGLAIVKRIVELHGGTIEVES 313

                   ....*....
gi 1889623460  724 EKGQGSCFT 732
Cdd:COG0642    314 EPGKGTTFT 322
HATPase_EvgS-ArcB-TorS-like cd16922
Histidine kinase-like ATPase domain of two-component sensor histidine kinases, many are hybrid ...
628-737 4.41e-51

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: 174.99  E-value: 4.41e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  628 LKQILINLLNNAFKFTHQGEVSLTLGCQYLTEEKLLMSFVIEDSGIGIAEKNIDKLFEAFTQEDTSTTRHFGGTGLGLSI 707
Cdd:cd16922      1 LRQILLNLLGNAIKFTEEGEVTLRVSLEEEEEDGVQLRFSVEDTGIGIPEEQQARLFEPFSQADSSTTRKYGGTGLGLAI 80
                           90       100       110
                   ....*....|....*....|....*....|
gi 1889623460  708 CRKLAQLMGGDISVTSEKGQGSCFTAQVQL 737
Cdd:cd16922     81 SKKLVELMGGDISVESEPGQGSTFTFTLPL 110
HATPase_c smart00387
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.
623-732 2.44e-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: 2.44e-34
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460   623 GDSHRLKQILINLLNNAFKFTH-QGEVSLTLgcqylTEEKLLMSFVIEDSGIGIAEKNIDKLFEAFTQEDtSTTRHFGGT 701
Cdd:smart00387    1 GDPDRLRQVLSNLLDNAIKYTPeGGRITVTL-----ERDGDHVEITVEDNGPGIPPEDLEKIFEPFFRTD-KRSRKIGGT 74
                            90       100       110
                    ....*....|....*....|....*....|.
gi 1889623460   702 GLGLSICRKLAQLMGGDISVTSEKGQGSCFT 732
Cdd:smart00387   75 GLGLSIVKKLVELHGGEISVESEPGGGTTFT 105
HATPase_c pfam02518
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the ...
623-739 4.30e-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: 114.77  E-value: 4.30e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  623 GDSHRLKQILINLLNNAFKFT-HQGEVSLTLgcqyltEEKLLMSFVIEDSGIGIAEKNIDKLFEAFTQEDTSTTrhfGGT 701
Cdd:pfam02518    1 GDELRLRQVLSNLLDNALKHAaKAGEITVTL------SEGGELTLTVEDNGIGIPPEDLPRIFEPFSTADKRGG---GGT 71
                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1889623460  702 GLGLSICRKLAQLMGGDISVTSEKGQGSCFTAQVQLHI 739
Cdd:pfam02518   72 GLGLSIVRKLVELLGGTITVESEPGGGTTVTLTLPLAQ 109
BaeS_SmeS NF012163
sensor histidine kinase efflux regulator BaeS;
475-720 3.93e-26

sensor histidine kinase efflux regulator BaeS;


Pssm-ID: 411086 [Multi-domain]  Cd Length: 457  Bit Score: 113.00  E-value: 3.93e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  475 QTQV------ELEKLNSTLEQkvrqrtteLESAIEQAlaaSKSKSDFIANISHEIRTPMNGVLGMLEMLkEDTLTQQQQQ 548
Cdd:NF012163   208 TTRVtptsndELGKLAQDFNQ--------LASTLEKN---EQMRRDFMADISHELRTPLAVLRAELEAI-QDGIRKFTPE 275
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  549 YLELANSSANSLMTLINDILDFSKIEAGKLDIDNHSFDVITVCSDMITSMALQAQRKGLEvfLHTDKVIDRMLVGDSHRL 628
Cdd:NF012163   276 SLDSLQAEVGTLTKLVDDLHDLSMSDEGALAYQKASVDLVPLLEVEGGAFRERFASAGLE--LEVSLPDSSLVFGDRDRL 353
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  629 KQILINLLNNAFKFTHQGevsltlGCQYLTEEKL--LMSFVIEDSGIGIAEKNIDKLFEAFTQEDTSTTRHFGGTGLGLS 706
Cdd:NF012163   354 MQLFNNLLENSLRYTDSG------GSLHISASQRpkEVTLTVADSAPGVSDEQLARLFERFYRVEVSRNRASGGSGLGLA 427
                          250
                   ....*....|....
gi 1889623460  707 ICRKLAQLMGGDIS 720
Cdd:NF012163   428 ISLNIVQAHGGTLH 441
HK_WalK NF033092
cell wall metabolism sensor histidine kinase WalK; This model describes WalK as found in ...
514-732 8.96e-25

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: 110.23  E-value: 8.96e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  514 DFIANISHEIRTPMNGVLGMLEML-----KEDTLtqqQQQYLELANSSANSLMTLINDILDFSKIEAGKLDIDNHSFDVI 588
Cdd:NF033092   374 EFVANVSHELRTPLTTMRSYLEALadgawKDPEL---APRFLGVTQNETERMIRLVNDLLQLSRMDSKDYKLNKEWVNFN 450
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  589 TVCSDMIT--SMALQAQ---------RKGLEVFLHTDKVIdrmlvgdshrlkQILINLLNNAFKFTHQ-GEVSLTLgcqY 656
Cdd:NF033092   451 EFFNYIIDrfEMILKNKnitfkrefpKRDLWVEIDTDKIT------------QVLDNIISNAIKYSPEgGTITFRL---L 515
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1889623460  657 LTEEKLLMSfvIEDSGIGIAEKNIDKLFEAFTQEDTSTTRHFGGTGLGLSICRKLAQLMGGDISVTSEKGQGSCFT 732
Cdd:NF033092   516 ETHNRIIIS--ISDQGLGIPKKDLDKIFDRFYRVDKARSRKMGGTGLGLAIAKEVVEAHGGRIWAESEEGKGTTIY 589
MtrAB_MtrB NF040691
MtrAB system histidine kinase MtrB;
493-731 2.15e-22

MtrAB system histidine kinase MtrB;


Pssm-ID: 468655 [Multi-domain]  Cd Length: 507  Bit Score: 102.03  E-value: 2.15e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  493 QRTTELESAIEQALAASKSKSDFIANISHEIRTPMNGV--LGMLEMLKEDTLTQQQQQYLELANSSANSLMTLINDILDF 570
Cdd:NF040691   252 QMADSLQRQIRQLEELSRLQQRFVSDVSHELRTPLTTIrmAADVIHDSRDDFDPATARSAELLHTELDRFESLLSDLLEI 331
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  571 SKIEAGKLDIDNHSFDVITVCSDMITSMALQAQRKGLEVFLH---TDKVIDrmlvGDSHRLKQILINLLNNAFKFTHQGE 647
Cdd:NF040691   332 SRFDAGAAELDVEPVDLRPLVRRVVDALRQLAERAGVELRVDapgTPVVAE----VDPRRVERVLRNLVVNAIEHGEGKP 407
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  648 VSLTLGCQYLTeekllMSFVIEDSGIGIAEKNIDKLFEAFTQEDTSTTRHFGGTGLGLSICRKLAQLMGGDISVTSEKGQ 727
Cdd:NF040691   408 VVVTVAQDDTA-----VAVTVRDHGVGLKPGEVALVFDRFWRADPARARTTGGTGLGLAIALEDARLHGGWLEAWGRPGQ 482

                   ....
gi 1889623460  728 GSCF 731
Cdd:NF040691   483 GSQF 486
resp_reg_YycF NF040534
response regulator YycF;
893-1001 1.13e-08

response regulator YycF;


Pssm-ID: 439744 [Multi-domain]  Cd Length: 231  Bit Score: 56.65  E-value: 1.13e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  893 KVLLVDDNMINLEVAKAILKNTGVTIVCASDGLDALEILNTEQTalfDLILMDCQMPNLNGYDTTSAIRSNKagadyaKV 972
Cdd:NF040534     2 KILVVDDEKPIADILEFNLKKEGYEVFCAYDGNEALELVEEEVP---DLVLLDIMLPGRDGMEVCREVRKKY------DM 72
                           90       100
                   ....*....|....*....|....*....
gi 1889623460  973 PIIAMTASAMAGDRERCITAGMNDYITKP 1001
Cdd:NF040534    73 PIIMLTAKDSEIDKVLGLELGADDYVTKP 101
RocR COG3829
RocR-type transcriptional regulator, contains PAS, AAA-type ATPase, and DNA-binding Fis ...
355-513 2.55e-05

RocR-type transcriptional regulator, contains PAS, AAA-type ATPase, and DNA-binding Fis domains [Transcription, Signal transduction mechanisms];


Pssm-ID: 443041 [Multi-domain]  Cd Length: 448  Bit Score: 47.84  E-value: 2.55e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  355 RKLEFHSLKERNNKIIENSLDAILTVQEDGLISNANKTALQFFDI----IIDHtKFTQLFtlaesDNSCIDETIAQGSkp 430
Cdd:COG3829      2 EELELKELEEELEAILDSLDDGIIVVDADGRITYVNRAAERILGLpreeVIGK-NVTELI-----PNSPLLEVLKTGK-- 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  431 SFEGVYTDPQDQQHFYSITLTSVFDiFTQRHQVAAILRNINSLKQTQVELEKLNstLEQKVRQRTT---------ELESA 501
Cdd:COG3829     74 PVTGVIQKTGGKGKTVIVTAIPIFE-DGEVIGAVETFRDITELKRLERKLREEE--LERGLSAKYTfddiigkspAMKEL 150
                          170
                   ....*....|..
gi 1889623460  502 IEQALAASKSKS 513
Cdd:COG3829    151 LELAKRVAKSDS 162
 
Name Accession Description Interval E-value
PRK11107 PRK11107
hybrid sensory histidine kinase BarA; Provisional
483-1014 2.29e-101

hybrid sensory histidine kinase BarA; Provisional


Pssm-ID: 236848 [Multi-domain]  Cd Length: 919  Bit Score: 339.52  E-value: 2.29e-101
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  483 LNSTLEQKVRQrTTELESAIEQALAASKSKSDFIANISHEIRTPMNGVLGML-EMLKEDtLTQQQQQYLELANSSANSLM 561
Cdd:PRK11107   265 LRETLEQMEIQ-NVELDLAKKRAQEAARIKSEFLANMSHELRTPLNGVIGFTrQTLKTP-LTPTQRDYLQTIERSANNLL 342
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  562 TLINDILDFSKIEAGKLDIDNHSFDVITVCSDMITSMALQAQRKGLEVFLHTDKVIDRMLVGDSHRLKQILINLLNNAFK 641
Cdd:PRK11107   343 AIINDILDFSKLEAGKLVLENIPFSLRETLDEVVTLLAHSAHEKGLELTLNIDPDVPDNVIGDPLRLQQIITNLVGNAIK 422
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  642 FTHQGEVSLTLGCQYLTEEKLLMSFVIEDSGIGIAEKNIDKLFEAFTQEDTSTTRHFGGTGLGLSICRKLAQLMGGDISV 721
Cdd:PRK11107   423 FTESGNIDILVELRALSNTKVQLEVQIRDTGIGISERQQSQLFQAFRQADASISRRHGGTGLGLVITQKLVNEMGGDISF 502
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  722 TSEKGQGSCFTAQVQLHI---AAEKKLNTAVELAKDIqvgVLIDSDSVYNNVTNLLIKNCQVAANNIQRFdyqAQYQELK 798
Cdd:PRK11107   503 HSQPNRGSTFWFHLPLDLnpnPIIDGLPTDCLAGKRL---LYVEPNSAAAQATLDILSETPLEVTYSPTL---SQLPEAH 576
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  799 VDLLVVDNDHPYLQTLINLCNKQNK-----KYVLIL---RDLLLSKKAKEQVPENChvLNKPLTqdqfSYKLASLFGVNN 870
Cdd:PRK11107   577 YDILLLGLPVTFREPLTMLHERLAKaksmtDFLILAlpcHEQVLAEQLKQDGADAC--LSKPLS----HTRLLPALLEPC 650
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  871 SFLVASQGSEQTEYVEydfsNFKVLLVDDNMINLEVAKAILKNTGVTIVCASDGLDALEiLNTEQTalFDLILMDCQMPN 950
Cdd:PRK11107   651 HHKQPPLLPPTDESRL----PLTVMAVDDNPANLKLIGALLEEQVEHVVLCDSGHQAVE-QAKQRP--FDLILMDIQMPG 723
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1889623460  951 LNGYDTTSAIRSNKAgadYAKVPIIAMTASAMAGDRERCITAGMNDYITKPIKPKVLKDKLAMW 1014
Cdd:PRK11107   724 MDGIRACELIRQLPH---NQNTPIIAVTAHAMAGERERLLSAGMDDYLAKPIDEAMLKQVLLRY 784
PRK15347 PRK15347
two component system sensor kinase;
485-1013 1.28e-83

two component system sensor kinase;


Pssm-ID: 237951 [Multi-domain]  Cd Length: 921  Bit Score: 290.39  E-value: 1.28e-83
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  485 STLEQKVRQRTTELESAIEQALAASKSKSDFIANISHEIRTPMNGVLGMLEMLKEDTLTQQQQQYLELANSSANSLMTLI 564
Cdd:PRK15347   371 DTLENKVAERTQALAEAKQRAEQANKRKSEHLTTISHEIRTPLNGVLGALELLQNTPLTAEQMDLADTARQCTLSLLAII 450
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  565 NDILDFSKIEAGKLDIDNHSFDVITVCSDMITSMALQAQRKG--LEVFLHTDkvIDRMLVGDSHRLKQILINLLNNAFKF 642
Cdd:PRK15347   451 NNLLDFSRIESGQMTLSLEETALLPLLDQAMLTIQGPAQSKSltLRTFVGAH--VPLYLHLDSLRLRQILVNLLGNAVKF 528
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  643 THQGEVSLTLGCQyltEEKLLmsFVIEDSGIGIAEKNIDKLFEAFTQEDTsttrHFGGTGLGLSICRKLAQLMGGDISVT 722
Cdd:PRK15347   529 TETGGIRLRVKRH---EQQLC--FTVEDTGCGIDIQQQQQIFTPFYQADT----HSQGTGLGLTIASSLAKMMGGELTLF 599
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  723 SEKGQGSCFTAQVQLHIAAEKklntavelakdiqvgvlidsdsvynnvtnLLIKNCQVAANNIqrfdyqaqyqelkvdll 802
Cdd:PRK15347   600 STPGVGSCFSLVLPLNEYAPP-----------------------------EPLKGELSAPLAL----------------- 633
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  803 vvdndHPYLQTLINLCNKQNkkyvlilrdlllskkakeqvpENCHVLNKPLtqdqfSYKLASLFgvNNSF-LVASQGSEQ 881
Cdd:PRK15347   634 -----HRQLSAWGITCQPGH---------------------QNPALLDPEL-----AYLPGRLY--DLLQqIIQGAPNEP 680
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  882 TEYVEYDFSNFKVLLVDDNMINLEVAKAILKNTGVTIVCASDGLDALEIlntEQTALFDLILMDCQMPNLNGYDTTSAIR 961
Cdd:PRK15347   681 VINLPLQPWQLQILLVDDVETNRDIIGMMLVELGQQVTTAASGTEALEL---GRQHRFDLVLMDIRMPGLDGLETTQLWR 757
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1889623460  962 SNKAGADyAKVPIIAMTASAMAGDRERCITAGMNDYITKPIKPKVLKDKLAM 1013
Cdd:PRK15347   758 DDPNNLD-PDCMIVALTANAAPEEIHRCKKAGMNHYLTKPVTLAQLARALEL 808
PRK10841 PRK10841
two-component system sensor histidine kinase RcsC;
497-1012 1.70e-75

two-component system sensor histidine kinase RcsC;


Pssm-ID: 182772 [Multi-domain]  Cd Length: 924  Bit Score: 267.61  E-value: 1.70e-75
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  497 ELESAIEQAlaaSKSKSDFIANISHEIRTPMNGVLGMLEMLKEDTLTQQQQQYLELANSSANSLMTLINDILDFSKIEAG 576
Cdd:PRK10841   435 EMAQAAEQA---SQSKSMFLATVSHELRTPLYGIIGNLDLLQTKELPKGVDRLVTAMNNSSSLLLKIISDILDFSKIESE 511
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  577 KLDIDNHSFDVITVCSDMITSMALQAQRKGLEVFLHTDKVIDRMLVGDSHRLKQILINLLNNAFKFTHQGEVSLTLGCQ- 655
Cdd:PRK10841   512 QLKIEPREFSPREVINHITANYLPLVVKKRLGLYCFIEPDVPVALNGDPMRLQQVISNLLSNAIKFTDTGCIVLHVRVDg 591
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  656 -YLteekllmSFVIEDSGIGIAEKNIDKLFEAFTQEDTSTTRHFGGTGLGLSICRKLAQLMGGDISVTSEKGQGSCFTAQ 734
Cdd:PRK10841   592 dYL-------SFRVRDTGVGIPAKEVVRLFDPFFQVGTGVQRNFQGTGLGLAICEKLINMMDGDISVDSEPGMGSQFTIR 664
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  735 VQLHiAAEKKLNTAVELAKDIQVGVLIDSDSVYNNVTNLLikncqvAANNIQRFDYQAQyQELKVDLLVVDND---HPYL 811
Cdd:PRK10841   665 IPLY-GAQYPQKKGVEGLQGKRCWLAVRNASLEQFLETLL------QRSGIQVQRYEGQ-EPTPEDVLITDDPvqkKWQG 736
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  812 QTLINLCNKQNkkyvlilrdlllsKKAKEQVPEN-CHVLNKPLTQDQFsykLASLFGVNNSFLVASQGSEQTEYVEYDFS 890
Cdd:PRK10841   737 RAVITFCRRHI-------------GIPLEIAPGEwVHSTATPHELPAL---LARIYRIELESDDSANALPSTDKAVSDND 800
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  891 NFKVLLVDDNMINLEVAKAILKNTGVTIVCASDGLDALEILNTEQTalfDLILMDCQMPNLNGYDTTSAIRSnkagaDYA 970
Cdd:PRK10841   801 DMMILVVDDHPINRRLLADQLGSLGYQCKTANDGVDALNVLSKNHI---DIVLTDVNMPNMDGYRLTQRLRQ-----LGL 872
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|..
gi 1889623460  971 KVPIIAMTASAMAGDRERCITAGMNDYITKPIKPKVLKDKLA 1012
Cdd:PRK10841   873 TLPVIGVTANALAEEKQRCLEAGMDSCLSKPVTLDVLKQTLT 914
TMAO_torS TIGR02956
TMAO reductase sytem sensor TorS; This protein, TorS, is part of a regulatory system for the ...
460-1016 2.07e-75

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: 268.18  E-value: 2.07e-75
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  460 RHQVAAILRNINSLKQTQVELEKLNSTLEQKVRQRTTELES--------AIEQALA------ASKSKSDFIANISHEIRT 525
Cdd:TIGR02956  398 RDTAAHNLKLQADERQVAQELQEHKESLEQLVAQRTQELAEtnerlnaeVKNHAKAraeaeeANRAKSAFLATMSHEIRT 477
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  526 PMNGVLGMLEMLKEDTLTQQQQQYLELANSSANSLMTLINDILDFSKIEAGKLDIDNHSFDVITVCSDMITSMALQAQRK 605
Cdd:TIGR02956  478 PLNGILGTLELLGDTGLTSQQQQYLQVINRSGESLLDILNDILDYSKIEAGHLSISPRPFDLNALLDDVHHLMVSRAQLK 557
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  606 GLEVFLHTDKVIDRMLVGDSHRLKQILINLLNNAFKFTHQGEVSLTLGCQylTEEKLLmsFVIEDSGIGIAEKNIDKLFE 685
Cdd:TIGR02956  558 GIQLRLNIPEQLPNWWQGDGPRIRQVLINLVGNAIKFTDRGSVVLRVSLN--DDSSLL--FEVEDTGCGIAEEEQATLFD 633
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  686 AFTQEDtsTTRHFGGTGLGLSICRKLAQLMGGDISVTSEKGQGSCFTAQVqlhiaaekklntavelakdiqvgvlidsds 765
Cdd:TIGR02956  634 AFTQAD--GRRRSGGTGLGLAISQRLVEAMDGELGVESELGVGSCFWFTL------------------------------ 681
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  766 vynnvtnllikncqvaanniqrfdyqaqyqelkvdllvvdndhpylqtlinlcnkqnkkyvlilrdlllskkakeqvpen 845
Cdd:TIGR02956      --------------------------------------------------------------------------------
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  846 chvlnkPLTQDQfsyklaslfgvnnsflvASQGSEQTEYVeyDFSNFKVLLVDDNMINLEVAKAILKNTGVTIVCASDGL 925
Cdd:TIGR02956  682 ------PLTRGK-----------------PAEDSATLTVI--DLPPQRVLLVEDNEVNQMVAQGFLTRLGHKVTLAESGQ 736
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  926 DALEILNTEQtalFDLILMDCQMPNLNGYDTTSAIRSNKAGADyaKVPIIAMTASAMAGDRERCITAGMNDYITKPIKPK 1005
Cdd:TIGR02956  737 SALECFHQHA---FDLALLDINLPDGDGVTLLQQLRAIYGAKN--EVKFIAFSAHVFNEDVAQYLAAGFDGFLAKPVVEE 811
                          570
                   ....*....|.
gi 1889623460 1006 VLKDKLAMWLK 1016
Cdd:TIGR02956  812 QLTAMIAVILA 822
BaeS COG0642
Signal transduction histidine kinase [Signal transduction mechanisms];
485-732 9.65e-73

Signal transduction histidine kinase [Signal transduction mechanisms];


Pssm-ID: 440407 [Multi-domain]  Cd Length: 328  Bit Score: 244.05  E-value: 9.65e-73
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  485 STLEQKVRQRTTELESAIEQALAASKSKSDFIANISHEIRTPMNGVLGMLEMLkEDTLTQQQQQYLELANSSANSLMTLI 564
Cdd:COG0642     83 LLLLLLLLLLLLLLLALLLLLEEANEAKSRFLANVSHELRTPLTAIRGYLELL-LEELDEEQREYLETILRSADRLLRLI 161
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  565 NDILDFSKIEAGKLDIDNHSFDVITVCSDMITSMALQAQRKGLEVFLHTDKVIdRMLVGDSHRLKQILINLLNNAFKFTH 644
Cdd:COG0642    162 NDLLDLSRLEAGKLELEPEPVDLAELLEEVVELFRPLAEEKGIELELDLPDDL-PTVRGDPDRLRQVLLNLLSNAIKYTP 240
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  645 QG-EVSLTlgcqyLTEEKLLMSFVIEDSGIGIAEKNIDKLFEAFTQEDTSttRHFGGTGLGLSICRKLAQLMGGDISVTS 723
Cdd:COG0642    241 EGgTVTVS-----VRREGDRVRISVEDTGPGIPPEDLERIFEPFFRTDPS--RRGGGTGLGLAIVKRIVELHGGTIEVES 313

                   ....*....
gi 1889623460  724 EKGQGSCFT 732
Cdd:COG0642    314 EPGKGTTFT 322
PRK11091 PRK11091
aerobic respiration control sensor protein ArcB; Provisional
454-1007 1.22e-67

aerobic respiration control sensor protein ArcB; Provisional


Pssm-ID: 236842 [Multi-domain]  Cd Length: 779  Bit Score: 242.54  E-value: 1.22e-67
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  454 FDIFTQRHQVAAILRNINSLKQTQVELEKlnstleqkvrqrttelesaieqalaASKSKSDFIANISHEIRTPMNGVLGM 533
Cdd:PRK11091   250 YDRVGKRHGLMGFGRDITERKRYQDALEK-------------------------ASRDKTTFISTISHELRTPLNGIVGL 304
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  534 LEMLKEDTLTQQQQQYLELANSSANSLMTLINDILDFSKIEAGKLDIDNHSFDVITVCSDMITSMALQAQRKGLEVFLHT 613
Cdd:PRK11091   305 SRILLDTELTAEQRKYLKTIHVSAITLGNIFNDIIDMDKMERRKLQLDNQPIDFTDFLADLENLSGLQAEQKGLRFDLEP 384
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  614 DKVIDRMLVGDSHRLKQILINLLNNAFKFTHQGEVSLTlgCQYLTEEKLLmsFVIEDSGIGIAEKNIDKLFEAFTQ-EDT 692
Cdd:PRK11091   385 LLPLPHKVITDGTRLRQILWNLISNAVKFTQQGGVTVR--VRYEEGDMLT--FEVEDSGIGIPEDELDKIFAMYYQvKDS 460
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  693 STTRHFGGTGLGLSICRKLAQLMGGDISVTSEKGQGSCFTAQVqlhiaaekklntavelakdiqvgvlidsdsvynnvtn 772
Cdd:PRK11091   461 HGGKPATGTGIGLAVSKRLAQAMGGDITVTSEEGKGSCFTLTI------------------------------------- 503
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  773 llikncqvaanniqrfdyqaqyqelkvdllvvdndhpylqtlinlcnkqnkkyvlilrdlllskkakeQVPENCHVLNKP 852
Cdd:PRK11091   504 --------------------------------------------------------------------HAPAVAEEVEDA 515
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  853 LTQDQfsYKLASLfgvnnsflvasqgseqteyveydfsnfKVLLVDDNMINLEVAKAILKNTGVTIVCASDGLDALEILN 932
Cdd:PRK11091   516 FDEDD--MPLPAL---------------------------NILLVEDIELNVIVARSVLEKLGNSVDVAMTGKEALEMFD 566
                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1889623460  933 TEQtalFDLILMDCQMPNLNGYDTTSAIRSNKAGADYAkvPIIAMTASAMAgDRERCITAGMNDYITKPIKPKVL 1007
Cdd:PRK11091   567 PDE---YDLVLLDIQLPDMTGLDIARELRERYPREDLP--PLVALTANVLK-DKKEYLDAGMDDVLSKPLSVPAL 635
KdpD COG2205
K+-sensing histidine kinase KdpD [Signal transduction mechanisms];
497-732 2.07e-66

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


Pssm-ID: 441807 [Multi-domain]  Cd Length: 239  Bit Score: 223.25  E-value: 2.07e-66
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  497 ELESAIEQALAASKSKSDFIANISHEIRTPMNGVLGMLEMLKEDT--LTQQQQQYLELANSSANSLMTLINDILDFSKIE 574
Cdd:COG2205      1 ELEEALEELEELERLKSEFLANVSHELRTPLTSILGAAELLLDEEdlSPEERRELLEIIRESAERLLRLIEDLLDLSRLE 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  575 AGKLDIDNHSFDVITVCSDMITSMALQAQRKGLEVFLHTDKViDRMLVGDSHRLKQILINLLNNAFKFTHQG-EVSLTLG 653
Cdd:COG2205     81 SGKLSLELEPVDLAELLEEAVEELRPLAEEKGIRLELDLPPE-LPLVYADPELLEQVLANLLDNAIKYSPPGgTITISAR 159
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1889623460  654 CQyltEEKLLmsFVIEDSGIGIAEKNIDKLFEAFTQEDTstTRHFGGTGLGLSICRKLAQLMGGDISVTSEKGQGSCFT 732
Cdd:COG2205    160 RE---GDGVR--ISVSDNGPGIPEEELERIFERFYRGDN--SRGEGGTGLGLAIVKRIVEAHGGTIWVESEPGGGTTFT 231
WalK COG5002
Sensor histidine kinase WalK [Signal transduction mechanisms];
369-732 9.07e-64

Sensor histidine kinase WalK [Signal transduction mechanisms];


Pssm-ID: 444026 [Multi-domain]  Cd Length: 390  Bit Score: 221.35  E-value: 9.07e-64
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  369 IIENSLDAILTVQEDGLISNANKTALQFFDIIIDHTKFTQLFTLAESDNSCIDETIAQGSKPSFEGVYTDPQDQQHFYSI 448
Cdd:COG5002     22 LLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLALLLLLLLLLLLLLALLLLLLLLLLLLALALLLLALLLLLLLLLLLLAL 101
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  449 TLTSVFDIFTQRHQVAAILRNINSLKQTQVELEKLNSTLEQKVRQRTTELESAIEQALAASKSKSDFIANISHEIRTPMN 528
Cdd:COG5002    102 LILLLLLALLILLAALLLLLSELLLLLLLLGRLSLRLSALLLGLLLLAAVERDITELERLEQMRREFVANVSHELRTPLT 181
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  529 GVLGMLEMLKEDTLTQ--QQQQYLELANSSANSLMTLINDILDFSKIEAGKLDIDNHSFDVITVCSDMITSMALQAQRKG 606
Cdd:COG5002    182 SIRGYLELLLDGAADDpeERREYLEIILEEAERLSRLVNDLLDLSRLESGELKLEKEPVDLAELLEEVVEELRPLAEEKG 261
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  607 LEVFLHTDKViDRMLVGDSHRLKQILINLLNNAFKFTHQG-EVSLTLgcqylTEEKLLMSFVIEDSGIGIAEKNIDKLFE 685
Cdd:COG5002    262 IELELDLPED-PLLVLGDPDRLEQVLTNLLDNAIKYTPEGgTITVSL-----REEDDQVRISVRDTGIGIPEEDLPRIFE 335
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*..
gi 1889623460  686 AFTQEDTSTTRHFGGTGLGLSICRKLAQLMGGDISVTSEKGQGSCFT 732
Cdd:COG5002    336 RFYRVDKSRSRETGGTGLGLAIVKHIVEAHGGRIWVESEPGKGTTFT 382
HATPase_EvgS-ArcB-TorS-like cd16922
Histidine kinase-like ATPase domain of two-component sensor histidine kinases, many are hybrid ...
628-737 4.41e-51

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: 174.99  E-value: 4.41e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  628 LKQILINLLNNAFKFTHQGEVSLTLGCQYLTEEKLLMSFVIEDSGIGIAEKNIDKLFEAFTQEDTSTTRHFGGTGLGLSI 707
Cdd:cd16922      1 LRQILLNLLGNAIKFTEEGEVTLRVSLEEEEEDGVQLRFSVEDTGIGIPEEQQARLFEPFSQADSSTTRKYGGTGLGLAI 80
                           90       100       110
                   ....*....|....*....|....*....|
gi 1889623460  708 CRKLAQLMGGDISVTSEKGQGSCFTAQVQL 737
Cdd:cd16922     81 SKKLVELMGGDISVESEPGQGSTFTFTLPL 110
KinE COG5809
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome ...
349-732 4.44e-51

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: 187.87  E-value: 4.44e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  349 YQRYINRKLefHSLKERNNKIIENSLDAILTVQEDGLISNANKTALQFFDIIID---HTKFTQLFTLAESDNSC--IDET 423
Cdd:COG5809    128 ERKRMEEAL--RESEEKFRLIFNHSPDGIIVTDLDGRIIYANPAACKLLGISIEeliGKSILELIHSDDQENVAafISQL 205
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  424 IAQGSKPSFEGVYTDPQDQQHFYSITLTSVFDiFTQRHQVAAILRNINSLKQTQVELEKLNSTleqkvrqrtteleSAIE 503
Cdd:COG5809    206 LKDGGIAQGEVRFWTKDGRWRLLEASGAPIKK-NGEVDGIVIIFRDITERKKLEELLRKSEKL-------------SVVG 271
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  504 QaLAASksksdfianISHEIRTPMNGVLGMLEMLKeDTLTQQQQQYLELANSSANSLMTLINDILDFSKIEAGKLdidnH 583
Cdd:COG5809    272 E-LAAG---------IAHEIRNPLTSLKGFIQLLK-DTIDEEQKTYLDIMLSELDRIESIISEFLVLAKPQAIKY----E 336
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  584 SFDVITVCSDMITSMALQAQRKGLEVFLHTDKVIDrMLVGDSHRLKQILINLLNNAFKFT-HQGEVSLTLGCQYltEEKL 662
Cdd:COG5809    337 PKDLNTLIEEVIPLLQPQALLKNVQIELELEDDIP-DILGDENQLKQVFINLLKNAIEAMpEGGNITIETKAED--DDKV 413
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  663 LMSfvIEDSGIGIAEKNIDKLFEAFtqedtSTTRHfGGTGLGLSICRKLAQLMGGDISVTSEKGQGSCFT 732
Cdd:COG5809    414 VIS--VTDEGCGIPEERLKKLGEPF-----YTTKE-KGTGLGLMVSYKIIEEHGGKITVESEVGKGTTFS 475
COG4251 COG4251
Bacteriophytochrome (light-regulated signal transduction histidine kinase) [Signal ...
286-732 5.27e-47

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


Pssm-ID: 443393 [Multi-domain]  Cd Length: 503  Bit Score: 176.51  E-value: 5.27e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  286 HDLPSHYYLKQRISLENNISMLPLELAVSINTDILAKDVAKRRDHFVLVIISLFTALWLLVWLYQRYINRKLEFHSLKER 365
Cdd:COG4251     63 LLLLLLLLLLLVLAALALLLLLLLLELALVLLALLLVLLLLLALLLLLALLLLLELLLLLLALLLLLLLLALLLLEELAL 142
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  366 NNKIIENSLDAILTVQEDGLISNANKTALQFFDIIIDHTKFTQLFTLAESDNSCIDETIAQGSKPSFEGVYTDPQDQQHF 445
Cdd:COG4251    143 LRLALALLLLLLLLLLLLLLLLALILALLLAALAELELLLLLLLVLLLLLLLLLLLLLLLLRLLLELLLLLEAELLLSLG 222
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  446 YSITLTSVFDIFTQRHQVAAILRNINSLKQTQVELEKLNSTLEQKVRQRTTELEsaieqalAASKSKSDFIANISHEIRT 525
Cdd:COG4251    223 GGLGLLLLLLLLLVLLLLLILLLLLLILVLELLELRLELEELEEELEERTAELE-------RSNEELEQFAYVASHDLRE 295
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  526 PMNGVLGMLEMLKED---TLTQQQQQYLELANSSANSLMTLINDILDFSKIeaGKLDIDNHSFDVITVCSDMITSMALQA 602
Cdd:COG4251    296 PLRKISGFSQLLEEDygdKLDEEGREYLERIRDAAERMQALIDDLLAYSRV--GRQELEFEPVDLNELLEEVLEDLEPRI 373
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  603 QRKGLEVflhtdkVIDRMLV--GDSHRLKQILINLLNNAFKFTHQGEV-SLTLGCQyltEEKLLMSFVIEDSGIGIAEKN 679
Cdd:COG4251    374 EERGAEI------EVGPLPTvrGDPTLLRQVFQNLISNAIKYSRPGEPpRIEIGAE---REGGEWVFSVRDNGIGIDPEY 444
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1889623460  680 IDKLFEAFTQedTSTTRHFGGTGLGLSICRKLAQLMGGDISVTSEKGQGSCFT 732
Cdd:COG4251    445 AEKIFEIFQR--LHSRDEYEGTGIGLAIVKKIVERHGGRIWVESEPGEGATFY 495
REC_hyHK_CKI1_RcsC-like cd17546
phosphoacceptor receiver (REC) domain of hybrid sensor histidine kinases/response regulators ...
894-1011 1.64e-46

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: 161.87  E-value: 1.64e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  894 VLLVDDNMINLEVAKAILKNTGVTIVCASDGLDALEILNTEQtalFDLILMDCQMPNLNGYDTTSAIRsnKAGADYAKVP 973
Cdd:cd17546      1 VLVVDDNPVNRKVLKKLLEKLGYEVDVAENGQEALELLKEEP---FDLVLMDLQMPVMDGLEATRRIR--ELEGGGRRTP 75
                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1889623460  974 IIAMTASAMAGDRERCITAGMNDYITKPIKPKVLKDKL 1011
Cdd:cd17546     76 IIALTANALEEDREKCLEAGMDDYLSKPVKLDQLKEVL 113
PRK11466 PRK11466
hybrid sensory histidine kinase TorS; Provisional
487-741 3.90e-45

hybrid sensory histidine kinase TorS; Provisional


Pssm-ID: 236914 [Multi-domain]  Cd Length: 914  Bit Score: 176.63  E-value: 3.90e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  487 LEQKVRQRTTELESAI---EQALA----ASKSKSDFIANISHEIRTPMNGVLGMLEMLKEDTLTQQQQQYLELANSSANS 559
Cdd:PRK11466   412 LAAQVKARTAELQELViehRQARAeaekASQAKSAFLAAMSHEIRTPLYGILGTAQLLADNPALNAQRDDLRAITDSGES 491
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  560 LMTLINDILDFSKIEAG--KLDIDNHSFDVITVCSDMITSMALQAQRKGLEVFLHTDKVIDRMLVGDSHRLKQILINLLN 637
Cdd:PRK11466   492 LLTILNDILDYSAIEAGgkNVSVSDEPFEPRPLLESTLQLMSGRVKGRPIRLATDIADDLPTALMGDPRRIRQVITNLLS 571
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  638 NAFKFTHQGEVSLTLGCQyltEEKLLMSfvIEDSGIGIAEKNIDKLFEAFTQedTSTTRhfGGTGLGLSICRKLAQLMGG 717
Cdd:PRK11466   572 NALRFTDEGSIVLRSRTD---GEQWLVE--VEDSGCGIDPAKLAEIFQPFVQ--VSGKR--GGTGLGLTISSRLAQAMGG 642
                          250       260
                   ....*....|....*....|....
gi 1889623460  718 DISVTSEKGQGSCFTAQVQLHIAA 741
Cdd:PRK11466   643 ELSATSTPEVGSCFCLRLPLRVAT 666
NtrB COG3852
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms];
362-732 4.78e-45

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


Pssm-ID: 443061 [Multi-domain]  Cd Length: 361  Bit Score: 166.56  E-value: 4.78e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  362 LKERNNKIIENSLDAILTVQEDGLISNANKTALQFFDI----IIDHTkFTQLFTLAESDNSCIDETIAQGSKPS-FEGVY 436
Cdd:COG3852      5 SEELLRAILDSLPDAVIVLDADGRITYVNPAAERLLGLsaeeLLGRP-LAELFPEDSPLRELLERALAEGQPVTeREVTL 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  437 TDPQDQQHFYSITLTSVFDIFTQRHqVAAILRNINSLKQtqveleklnstLEQKVRQRttelesaiEQALAASKsksdFI 516
Cdd:COG3852     84 RRKDGEERPVDVSVSPLRDAEGEGG-VLLVLRDITERKR-----------LERELRRA--------EKLAAVGE----LA 139
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  517 ANISHEIRTPMNGVLGMLEMLKEDTLTQQQQQYLELANSSANSLMTLINDILDFSKIEAGKLdidnHSFDVITVCSDMIT 596
Cdd:COG3852    140 AGLAHEIRNPLTGIRGAAQLLERELPDDELREYTQLIIEEADRLNNLVDRLLSFSRPRPPER----EPVNLHEVLERVLE 215
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  597 SMALQAqRKGLEVFLHTDKVIDRMLvGDSHRLKQILINLLNNAFK-FTHQGEVSLTLGCQYLTEE-----KLLMSFVIED 670
Cdd:COG3852    216 LLRAEA-PKNIRIVRDYDPSLPEVL-GDPDQLIQVLLNLVRNAAEaMPEGGTITIRTRVERQVTLgglrpRLYVRIEVID 293
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1889623460  671 SGIGIAEKNIDKLFEAFTqedtsTTRhFGGTGLGLSICRKLAQLMGGDISVTSEKGQGSCFT 732
Cdd:COG3852    294 NGPGIPEEILDRIFEPFF-----TTK-EKGTGLGLAIVQKIVEQHGGTIEVESEPGKGTTFR 349
CheY COG0784
CheY-like REC (receiver) domain, includes chemotaxis protein CheY and sporulation regulator ...
888-1016 1.54e-44

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: 156.93  E-value: 1.54e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  888 DFSNFKVLLVDDNMINLEVAKAILKNTGVTIVCASDGLDALEILNTEQtalFDLILMDCQMPNLNGYDTTSAIRSNKAGA 967
Cdd:COG0784      2 PLGGKRILVVDDNPDNRELLRRLLERLGYEVTTAEDGAEALELLRAGP---PDLILLDINMPGMDGLELLRRIRALPRLP 78
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 1889623460  968 DyakVPIIAMTASAMAGDRERCITAGMNDYITKPIKPKVLKDKLAMWLK 1016
Cdd:COG0784     79 D---IPIIALTAYADEEDRERALEAGADDYLTKPVDPEELLEALRRLLA 124
PleD COG3706
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate ...
893-1011 1.19e-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: 139.27  E-value: 1.19e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  893 KVLLVDDNMINLEVAKAILKNTGVTIVCASDGLDALEILNTEQtalFDLILMDCQMPNLNGYDTTSAIRSNKAGADyakV 972
Cdd:COG3706      3 RILVVDDDPTNRKLLRRLLEAAGYEVVEAADGEEALELLQEHR---PDLILLDLEMPDMDGLELCRRLRADPRTAD---I 76
                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1889623460  973 PIIAMTASAMAGDRERCITAGMNDYITKPIKPKVLKDKL 1011
Cdd:COG3706     77 PIIFLTALDDEEDRARALEAGADDYLTKPFDPEELLARV 115
NtrY COG5000
Signal transduction histidine kinase NtrY involved in nitrogen fixation and metabolism ...
330-744 2.01e-37

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: 146.26  E-value: 2.01e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  330 HFVLVIISLFTALWLLVWLYqRYINRKL-------------------------EFHSL---------------------K 363
Cdd:COG5000     11 LLLIALLLLLLALWLALLLA-RRLTRPLrrlaeatravaagdlsvrlpvtgddEIGELarafnrmtdqlkeqreeleerR 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  364 ERNNKIIENSLDAILTVQEDGLISNANKTALQFFDIIIDHTKFTQLFTLAEsdNSCIDETIAQGSKPSFEGVYTDPQDQQ 443
Cdd:COG5000     90 RYLETILENLPAGVIVLDADGRITLANPAAERLLGIPLEELIGKPLEELLP--ELDLAELLREALERGWQEEIELTRDGR 167
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  444 HFYSITLTSvfdiFTQRHQVAaILRNInslkqtqveleklnstleqkvrqrtTELESAieQALAAsksKSDFIANISHEI 523
Cdd:COG5000    168 RTLLVRASP----LRDDGYVI-VFDDI-------------------------TELLRA--ERLAA---WGELARRIAHEI 212
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  524 RTPMNGVLGMLEMLKEDTLTQQQQQ------YLELANSSANSLMTLINDILDFSKIEAGKLDIdnhsFDVITVCSDMITS 597
Cdd:COG5000    213 KNPLTPIQLSAERLRRKLADKLEEDredlerALDTIIRQVDRLKRIVDEFLDFARLPEPQLEP----VDLNELLREVLAL 288
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  598 MALQAQRKGLEVFLHTDKViDRMLVGDSHRLKQILINLLNNAFKFT-HQGEVSLTLgcqYLTEEKLlmSFVIEDSGIGIA 676
Cdd:COG5000    289 YEPALKEKDIRLELDLDPD-LPEVLADRDQLEQVLINLLKNAIEAIeEGGEIEVST---RREDGRV--RIEVSDNGPGIP 362
                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1889623460  677 EKNIDKLFEAFTqedtsTTRHfGGTGLGLSICRKLAQLMGGDISVTSEKGQGSCFTaqVQLHIAAEKK 744
Cdd:COG5000    363 EEVLERIFEPFF-----TTKP-KGTGLGLAIVKKIVEEHGGTIELESRPGGGTTFT--IRLPLAEEAE 422
COG4191 COG4191
Signal transduction histidine kinase regulating C4-dicarboxylate transport system [Signal ...
475-732 1.45e-36

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


Pssm-ID: 443345 [Multi-domain]  Cd Length: 361  Bit Score: 141.86  E-value: 1.45e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  475 QTQVELEKLNSTLEQkVRQRTTELESAIEQALAASKSKS--DFIANISHEIRTPMNGVLGMLEMLKEDTLTQQQ----QQ 548
Cdd:COG4191    104 EENAELEELERDITE-LERAEEELRELQEQLVQSEKLAAlgELAAGIAHEINNPLAAILGNAELLRRRLEDEPDpeelRE 182
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  549 YLELANSSANSLMTLINDILDFSKIEAGKLdidnHSFDVITVCSDMITSMALQAQRKGLEVFLHTDKVIDRMLvGDSHRL 628
Cdd:COG4191    183 ALERILEGAERAAEIVRSLRAFSRRDEEER----EPVDLNELIDEALELLRPRLKARGIEVELDLPPDLPPVL-GDPGQL 257
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  629 KQILINLLNN---AFKFTHQGEVSLTLGCQyltEEKLLMSfvIEDSGIGIAEKNIDKLFEAFTqedtsTTRHFG-GTGLG 704
Cdd:COG4191    258 EQVLLNLLINaidAMEEGEGGRITISTRRE---GDYVVIS--VRDNGPGIPPEVLERIFEPFF-----TTKPVGkGTGLG 327
                          250       260
                   ....*....|....*....|....*...
gi 1889623460  705 LSICRKLAQLMGGDISVTSEKGQGSCFT 732
Cdd:COG4191    328 LSISYGIVEKHGGRIEVESEPGGGTTFT 355
PRK09959 PRK09959
acid-sensing system histidine kinase EvgS;
490-1012 1.58e-35

acid-sensing system histidine kinase EvgS;


Pssm-ID: 182169 [Multi-domain]  Cd Length: 1197  Bit Score: 146.80  E-value: 1.58e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  490 KVRQRTTELESAIEQALAASKSKSDFIANISHEIRTPMNGVLGMLEMLKEDTLTQQQ-QQYLELANSSANSLMTLINDIL 568
Cdd:PRK09959   690 ETRDLIHALEVERNKAINATVAKSQFLATMSHEIRTPISSIMGFLELLSGSGLSKEQrVEAISLAYATGQSLLGLIGEIL 769
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  569 DFSKIEAGKLDIDNHSFDVITVCSDMITSMALQAQRKGLEVFLhTDKVIDRMLVG-DSHRLKQILINLLNNAFKFTHQGE 647
Cdd:PRK09959   770 DVDKIESGNYQLQPQWVDIPTLVQNTCHSFGAIAASKSIALSC-SSTFPDHYLVKiDPQAFKQVLSNLLSNALKFTTEGA 848
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  648 VSLTLGCQYLTEEKLLMSFVIEDSGIGIAEKNIDKLFEAFTQedTSTTRHFGGTGLGLSICRKLAQLMGGDISVTSEKGQ 727
Cdd:PRK09959   849 VKITTSLGHIDDNHAVIKMTIMDSGSGLSQEEQQQLFKRYSQ--TSAGRQQTGSGLGLMICKELIKNMQGDLSLESHPGI 926
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  728 GSCFTAQVQLHIaaekklntavelakdIQvgvlidsdsvynnvtnllikncQVAAnniqrfdyqaqyqelkvdllvvdnd 807
Cdd:PRK09959   927 GTTFTITIPVEI---------------SQ----------------------QVAT------------------------- 944
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  808 hpylqtlinlcnkqnkkyvlilrdllLSKKAKEqvpenchvlnkPLTQDQfsyklaslfgvnnsflvasqgseqteyvey 887
Cdd:PRK09959   945 --------------------------VEAKAEQ-----------PITLPE------------------------------ 957
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  888 dfsNFKVLLVDDNMINLEVAKAILKNTGVTIVCASDGLDALEILNTEQtalFDLILMDCQMPNLNGYDTTSAIRSNKaga 967
Cdd:PRK09959   958 ---KLSILIADDHPTNRLLLKRQLNLLGYDVDEATDGVQALHKVSMQH---YDLLITDVNMPNMDGFELTRKLREQN--- 1028
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....*
gi 1889623460  968 dyAKVPIIAMTASAMAGDRERCITAGMNDYITKPIKPKVLKDKLA 1012
Cdd:PRK09959  1029 --SSLPIWGLTANAQANEREKGLSCGMNLCLFKPLTLDVLKTHLS 1071
phoR_proteo TIGR02966
phosphate regulon sensor kinase PhoR; Members of this protein family are the regulatory ...
362-733 3.22e-35

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: 137.34  E-value: 3.22e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  362 LKERNNKIIENSLDAILTVQEDGLISNANKTALQFFDI------------IIDHTKFTQLFTLAESDNSCIDETiaqgsk 429
Cdd:TIGR02966    4 LLSRFRAAAQALPDAVVVLDEEGQIEWCNPAAERLLGLrwpddlgqritnLIRHPEFVEYLAAGRFSEPLELPS------ 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  430 psfegvytdPQDQQHFYSITLTSVFDiftqrHQVAAILRNINSLKQtqveleklnstLEQkVRQrttelesaieqalaas 509
Cdd:TIGR02966   78 ---------PINSERVLEIRIAPYGE-----EQKLLVARDVTRLRR-----------LEQ-MRR---------------- 115
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  510 ksksDFIANISHEIRTPMNGVLGMLEMLKEDTLTQQQQQ--YLELANSSANSLMTLINDILDFSKIEAGKLDIDNHSFDV 587
Cdd:TIGR02966  116 ----DFVANVSHELRTPLTVLRGYLETLADGPDEDPEEWnrALEIMLEQSQRMQSLVEDLLTLSRLESAASPLEDEPVDM 191
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  588 ITVCSDMITSMALQAQRKGLEVFLHTDKVIDrmLVGDSHRLKQILINLLNNAFKFT-HQGEVSLTLgcqYLTEEKLLmsF 666
Cdd:TIGR02966  192 PALLDHLRDEAEALSQGKNHQITFEIDGGVD--VLGDEDELRSAFSNLVSNAIKYTpEGGTITVRW---RRDGGGAE--F 264
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1889623460  667 VIEDSGIGIAEKNIDKLFEAFTQEDTSTTRHFGGTGLGLSICRKLAQLMGGDISVTSEKGQGSCFTA 733
Cdd:TIGR02966  265 SVTDTGIGIAPEHLPRLTERFYRVDKSRSRDTGGTGLGLAIVKHVLSRHHARLEIESELGKGSTFSF 331
HATPase_c smart00387
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.
623-732 2.44e-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: 2.44e-34
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460   623 GDSHRLKQILINLLNNAFKFTH-QGEVSLTLgcqylTEEKLLMSFVIEDSGIGIAEKNIDKLFEAFTQEDtSTTRHFGGT 701
Cdd:smart00387    1 GDPDRLRQVLSNLLDNAIKYTPeGGRITVTL-----ERDGDHVEITVEDNGPGIPPEDLEKIFEPFFRTD-KRSRKIGGT 74
                            90       100       110
                    ....*....|....*....|....*....|.
gi 1889623460   702 GLGLSICRKLAQLMGGDISVTSEKGQGSCFT 732
Cdd:smart00387   75 GLGLSIVKKLVELHGGEISVESEPGGGTTFT 105
RpfG COG3437
Response regulator c-di-GMP phosphodiesterase, RpfG family, contains REC and HD-GYP domains ...
890-1012 5.72e-32

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: 124.51  E-value: 5.72e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  890 SNFKVLLVDDNMINLEVAKAILKNTGVTIVCASDGLDALEILnteQTALFDLILMDCQMPNLNGYDTTSAIRSNKAGADy 969
Cdd:COG3437      5 QAPTVLIVDDDPENLELLRQLLRTLGYDVVTAESGEEALELL---LEAPPDLILLDVRMPGMDGFELLRLLRADPSTRD- 80
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 1889623460  970 akVPIIAMTASAMAGDRERCITAGMNDYITKPIKPKVLKDKLA 1012
Cdd:COG3437     81 --IPVIFLTALADPEDRERALEAGADDYLTKPFDPEELLARVR 121
REC_DivK-like cd17548
phosphoacceptor receiver (REC) domain of DivK and similar proteins; Caulobacter crescentus ...
893-1012 6.35e-31

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: 117.64  E-value: 6.35e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  893 KVLLVDDNMINLEVAKAILKNTGVTIVCASDGLDALEILNTEQtalFDLILMDCQMPNLNGYDTTSAIRSNKAGADyakV 972
Cdd:cd17548      1 KILIVEDNPLNMKLARDLLESAGYEVLEAADGEEALEIARKEK---PDLILMDIQLPGMDGLEATRLLKEDPATRD---I 74
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1889623460  973 PIIAMTASAMAGDRERCITAGMNDYITKPIKPKVLKDKLA 1012
Cdd:cd17548     75 PVIALTAYAMKGDREKILEAGCDGYISKPIDTREFLETVA 114
HATPase_c pfam02518
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the ...
623-739 4.30e-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: 114.77  E-value: 4.30e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  623 GDSHRLKQILINLLNNAFKFT-HQGEVSLTLgcqyltEEKLLMSFVIEDSGIGIAEKNIDKLFEAFTQEDTSTTrhfGGT 701
Cdd:pfam02518    1 GDELRLRQVLSNLLDNALKHAaKAGEITVTL------SEGGELTLTVEDNGIGIPPEDLPRIFEPFSTADKRGG---GGT 71
                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1889623460  702 GLGLSICRKLAQLMGGDISVTSEKGQGSCFTAQVQLHI 739
Cdd:pfam02518   72 GLGLSIVRKLVELLGGTITVESEPGGGTTVTLTLPLAQ 109
OmpR COG0745
DNA-binding response regulator, OmpR family, contains REC and winged-helix (wHTH) domain ...
893-1011 5.90e-29

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: 115.05  E-value: 5.90e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  893 KVLLVDDNMINLEVAKAILKNTGVTIVCASDGLDALEILNTEQtalFDLILMDCQMPNLNGYDTTSAIRsnkagADYAKV 972
Cdd:COG0745      3 RILVVEDDPDIRELLADALEREGYEVDTAADGEEALELLEEER---PDLILLDLMLPGMDGLEVCRRLR-----ARPSDI 74
                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1889623460  973 PIIAMTASAMAGDRERCITAGMNDYITKPIKPKVLKDKL 1011
Cdd:COG0745     75 PIIMLTARDDEEDRVRGLEAGADDYLTKPFDPEELLARI 113
Response_reg pfam00072
Response regulator receiver domain; This domain receives the signal from the sensor partner in ...
894-1012 7.01e-28

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: 108.78  E-value: 7.01e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  894 VLLVDDNMINLEVAKAILKNTGVTIVCASDGLDALEILNTEQtalFDLILMDCQMPNLNGYDTTSAIRsnkagADYAKVP 973
Cdd:pfam00072    1 VLIVDDDPLIRELLRQLLEKEGYVVAEADDGKEALELLKEER---PDLILLDINMPGMDGLELLKRIR-----RRDPTTP 72
                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1889623460  974 IIAMTASAMAGDRERCITAGMNDYITKPIKPKVLKDKLA 1012
Cdd:pfam00072   73 VIILTAHGDEDDAVEALEAGADDFLSKPFDPDELLAAIR 111
BaeS_SmeS NF012163
sensor histidine kinase efflux regulator BaeS;
475-720 3.93e-26

sensor histidine kinase efflux regulator BaeS;


Pssm-ID: 411086 [Multi-domain]  Cd Length: 457  Bit Score: 113.00  E-value: 3.93e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  475 QTQV------ELEKLNSTLEQkvrqrtteLESAIEQAlaaSKSKSDFIANISHEIRTPMNGVLGMLEMLkEDTLTQQQQQ 548
Cdd:NF012163   208 TTRVtptsndELGKLAQDFNQ--------LASTLEKN---EQMRRDFMADISHELRTPLAVLRAELEAI-QDGIRKFTPE 275
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  549 YLELANSSANSLMTLINDILDFSKIEAGKLDIDNHSFDVITVCSDMITSMALQAQRKGLEvfLHTDKVIDRMLVGDSHRL 628
Cdd:NF012163   276 SLDSLQAEVGTLTKLVDDLHDLSMSDEGALAYQKASVDLVPLLEVEGGAFRERFASAGLE--LEVSLPDSSLVFGDRDRL 353
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  629 KQILINLLNNAFKFTHQGevsltlGCQYLTEEKL--LMSFVIEDSGIGIAEKNIDKLFEAFTQEDTSTTRHFGGTGLGLS 706
Cdd:NF012163   354 MQLFNNLLENSLRYTDSG------GSLHISASQRpkEVTLTVADSAPGVSDEQLARLFERFYRVEVSRNRASGGSGLGLA 427
                          250
                   ....*....|....
gi 1889623460  707 ICRKLAQLMGGDIS 720
Cdd:NF012163   428 ISLNIVQAHGGTLH 441
REC cd00156
phosphoacceptor receiver (REC) domain of response regulators (RRs) and pseudo response ...
895-1001 7.12e-25

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: 99.61  E-value: 7.12e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  895 LLVDDNMINLEVAKAILKNTGVTIVCASDGLDALEILNTEQtalFDLILMDCQMPNLNGYDTTSAIRSNkagadYAKVPI 974
Cdd:cd00156      1 LIVDDDPAIRELLKSLLEREGYEVDTAADGEEALELLREER---PDLVLLDLMMPGMDGLELLRKLREL-----PPDIPV 72
                           90       100
                   ....*....|....*....|....*..
gi 1889623460  975 IAMTASAMAGDRERCITAGMNDYITKP 1001
Cdd:cd00156     73 IVLTAKADEEDAVRALELGADDYLVKP 99
REC_2_DhkD-like cd17580
second phosphoacceptor receiver (REC) domain of Dictyostelium discoideum hybrid signal ...
894-1007 8.62e-25

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: 99.84  E-value: 8.62e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  894 VLLVDDNMINLEVAKAILKNTGVTIVCASDGLDALEILnteQTALFDLILMDCQMPNLNGYDTTSAIRSNKAGADyakVP 973
Cdd:cd17580      1 ILVVDDNEDAAEMLALLLELEGAEVTTAHSGEEALEAA---QRFRPDVILSDIGMPGMDGYELARRLRELPWLAN---TP 74
                           90       100       110
                   ....*....|....*....|....*....|....
gi 1889623460  974 IIAMTASAMAGDRERCITAGMNDYITKPIKPKVL 1007
Cdd:cd17580     75 AIALTGYGQPEDRERALEAGFDAHLVKPVDPDEL 108
HK_WalK NF033092
cell wall metabolism sensor histidine kinase WalK; This model describes WalK as found in ...
514-732 8.96e-25

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: 110.23  E-value: 8.96e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  514 DFIANISHEIRTPMNGVLGMLEML-----KEDTLtqqQQQYLELANSSANSLMTLINDILDFSKIEAGKLDIDNHSFDVI 588
Cdd:NF033092   374 EFVANVSHELRTPLTTMRSYLEALadgawKDPEL---APRFLGVTQNETERMIRLVNDLLQLSRMDSKDYKLNKEWVNFN 450
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  589 TVCSDMIT--SMALQAQ---------RKGLEVFLHTDKVIdrmlvgdshrlkQILINLLNNAFKFTHQ-GEVSLTLgcqY 656
Cdd:NF033092   451 EFFNYIIDrfEMILKNKnitfkrefpKRDLWVEIDTDKIT------------QVLDNIISNAIKYSPEgGTITFRL---L 515
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1889623460  657 LTEEKLLMSfvIEDSGIGIAEKNIDKLFEAFTQEDTSTTRHFGGTGLGLSICRKLAQLMGGDISVTSEKGQGSCFT 732
Cdd:NF033092   516 ETHNRIIIS--ISDQGLGIPKKDLDKIFDRFYRVDKARSRKMGGTGLGLAIAKEVVEAHGGRIWAESEEGKGTTIY 589
REC_D1_PleD-like cd17538
first (D1) phosphoacceptor receiver (REC) domain of response regulator PleD and similar ...
893-1002 1.65e-24

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: 98.72  E-value: 1.65e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  893 KVLLVDDNMINLEVAKAILKNTGVTIVCASDGLDALEILNTEQtalFDLILMDCQMPNLNGYDTTSAIRSNKAGADyakV 972
Cdd:cd17538      1 KILVVDDEPANRELLEALLSAEGYEVLTADSGQEALALAEEEL---PDLILLDVMMPGMDGFEVCRRLKEDPETRH---I 74
                           90       100       110
                   ....*....|....*....|....*....|
gi 1889623460  973 PIIAMTASAMAGDRERCITAGMNDYITKPI 1002
Cdd:cd17538     75 PVIMITALDDREDRIRGLEAGADDFLSKPI 104
REC_PA4781-like cd19920
phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase PA4781 and similar ...
894-1002 2.02e-24

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: 98.35  E-value: 2.02e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  894 VLLVDDNMINLEVAKAILKNTGVTIVCASDGLDALEILnteQTALFDLILMDCQMPNLNGYDTTSAIRSNKAGADyakVP 973
Cdd:cd19920      1 ILIVDDVPDNLRLLSELLRAAGYRVLVATDGQQALQRA---QAEPPDLILLDVMMPGMDGFEVCRRLKADPATRH---IP 74
                           90       100
                   ....*....|....*....|....*....
gi 1889623460  974 IIAMTASAMAGDRERCITAGMNDYITKPI 1002
Cdd:cd19920     75 VIFLTALTDTEDKVKGFELGAVDYITKPF 103
KinA COG5805
Sporulation sensor histidine kinase A (Stage II sporulation protein SpoIIF/SpoIIJ) [Cell cycle ...
363-732 5.07e-24

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: 107.12  E-value: 5.07e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  363 KERNNKIIENSLDAILTVQEDGLISNANKTALQFFDI----IIDhTKFTQLFTLA--ESDNSCIDETIAQGSKPSFEGVY 436
Cdd:COG5805    156 EERLQTLIENSPDLICVIDTDGRILFINESIERLFGApreeLIG-KNLLELLHPCdkEEFKERIESITEVWQEFIIEREI 234
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  437 TDPQDQQHFYSITLTSVFDIFTQRHQVAAILRNINSLKQTQVEL---EKLNstleqkvrqrttelesaIEQALAASksks 513
Cdd:COG5805    235 ITKDGRIRYFEAVIVPLIDTDGSVKGILVILRDITEKKEAEELMarsEKLS-----------------IAGQLAAG---- 293
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  514 dfianISHEIRTPMNGVLGMLEML---KEDTltqqqQQYLELANSSANSLMTLINDILDFSKIEAgkldIDNHSFDVITV 590
Cdd:COG5805    294 -----IAHEIRNPLTSIKGFLQLLqpgIEDK-----EEYFDIMLSELDRIESIISEFLALAKPQA----VNKEKENINEL 359
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  591 CSDMITSMALQAQRKGLEV-FLHTDKVIDrmLVGDSHRLKQILINLLNNAFKFTHQ-GEVSLTlgcQYLTEEKLLMSfvI 668
Cdd:COG5805    360 IQDVVTLLETEAILHNIQIrLELLDEDPF--IYCDENQIKQVFINLIKNAIEAMPNgGTITIH---TEEEDNSVIIR--V 432
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1889623460  669 EDSGIGIAEKNIDKLFEAF--TQEDtsttrhfgGTGLGLSICRKLAQLMGGDISVTSEKGQGSCFT 732
Cdd:COG5805    433 IDEGIGIPEERLKKLGEPFftTKEK--------GTGLGLMVSYKIIENHNGTIDIDSKVGKGTTFT 490
REC_RpfG-like cd17551
phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase response regulator ...
893-1004 6.13e-23

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: 94.82  E-value: 6.13e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  893 KVLLVDDNMINLEVAKAILKNTG-VTIVCASDGLDALEILNTEQtalFDLILMDCQMPNLNGYDTTSAIRSNKAGADyak 971
Cdd:cd17551      2 RILIVDDNPTNLLLLEALLRSAGyLEVVSFTDPREALAWCRENP---PDLILLDYMMPGMDGLEFIRRLRALPGLED--- 75
                           90       100       110
                   ....*....|....*....|....*....|...
gi 1889623460  972 VPIIAMTASAMAGDRERCITAGMNDYITKPIKP 1004
Cdd:cd17551     76 VPIVMITADTDREVRLRALEAGATDFLTKPFDP 108
REC_OmpR cd17574
phosphoacceptor receiver (REC) domain of OmpR family response regulators; OmpR-like proteins ...
895-1001 1.67e-22

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: 92.86  E-value: 1.67e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  895 LLVDDNMINLEVAKAILKNTGVTIVCASDGLDALEILNTEQtalFDLILMDCQMPNLNGYDTTSAIRSNKagadyAKVPI 974
Cdd:cd17574      1 LVVEDDEEIAELLSDYLEKEGYEVDTAADGEEALELAREEQ---PDLIILDVMLPGMDGFEVCRRLREKG-----SDIPI 72
                           90       100
                   ....*....|....*....|....*..
gi 1889623460  975 IAMTASAMAGDRERCITAGMNDYITKP 1001
Cdd:cd17574     73 IMLTAKDEEEDKVLGLELGADDYITKP 99
MtrAB_MtrB NF040691
MtrAB system histidine kinase MtrB;
493-731 2.15e-22

MtrAB system histidine kinase MtrB;


Pssm-ID: 468655 [Multi-domain]  Cd Length: 507  Bit Score: 102.03  E-value: 2.15e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  493 QRTTELESAIEQALAASKSKSDFIANISHEIRTPMNGV--LGMLEMLKEDTLTQQQQQYLELANSSANSLMTLINDILDF 570
Cdd:NF040691   252 QMADSLQRQIRQLEELSRLQQRFVSDVSHELRTPLTTIrmAADVIHDSRDDFDPATARSAELLHTELDRFESLLSDLLEI 331
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  571 SKIEAGKLDIDNHSFDVITVCSDMITSMALQAQRKGLEVFLH---TDKVIDrmlvGDSHRLKQILINLLNNAFKFTHQGE 647
Cdd:NF040691   332 SRFDAGAAELDVEPVDLRPLVRRVVDALRQLAERAGVELRVDapgTPVVAE----VDPRRVERVLRNLVVNAIEHGEGKP 407
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  648 VSLTLGCQYLTeekllMSFVIEDSGIGIAEKNIDKLFEAFTQEDTSTTRHFGGTGLGLSICRKLAQLMGGDISVTSEKGQ 727
Cdd:NF040691   408 VVVTVAQDDTA-----VAVTVRDHGVGLKPGEVALVFDRFWRADPARARTTGGTGLGLAIALEDARLHGGWLEAWGRPGQ 482

                   ....
gi 1889623460  728 GSCF 731
Cdd:NF040691   483 GSQF 486
PRK09303 PRK09303
histidine kinase;
455-732 6.11e-22

histidine kinase;


Pssm-ID: 236462 [Multi-domain]  Cd Length: 380  Bit Score: 99.26  E-value: 6.11e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  455 DIFTQ------RHQVAAILRNINSLKQTQVELEKLNST-----LEQKVRQRTTELESAIEQAlaasKSKSDFIANISHEI 523
Cdd:PRK09303    87 NIFQQlknwwpRWQQEGATYSGLGENLQPSEIDSGRYSqellqLSDELFVLRQENETLLEQL----KFKDRVLAMLAHDL 162
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  524 RTPMNGV---LGMLEMLKEDTLTQQQQQYLE-LANSSANSLMT---LINDILDFSKIEAGKLDIDNHSFDVITVCSDMIT 596
Cdd:PRK09303   163 RTPLTAAslaLETLELGQIDEDTELKPALIEqLQDQARRQLEEierLITDLLEVGRTRWEALRFNPQKLDLGSLCQEVIL 242
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  597 SMALQAQRKGLEvfLHTDKVIDRMLV-GDSHRLKQILINLLNNAFKFT-HQGEVSLTLgcQYLTEEKLLMSfvIEDSGIG 674
Cdd:PRK09303   243 ELEKRWLAKSLE--IQTDIPSDLPSVyADQERIRQVLLNLLDNAIKYTpEGGTITLSM--LHRTTQKVQVS--ICDTGPG 316
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  675 IAEKNIDKLFE-AFT-QEDTSTTrhfgGTGLGLSICRKLAQLMGGDISVTSEKGQGSCFT 732
Cdd:PRK09303   317 IPEEEQERIFEdRVRlPRDEGTE----GYGIGLSVCRRIVRVHYGQIWVDSEPGQGSCFH 372
KinB COG5806
Sporulation sensor histidine kinase B [Cell cycle control, cell division, chromosome ...
481-732 1.03e-21

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


Pssm-ID: 444508 [Multi-domain]  Cd Length: 412  Bit Score: 98.79  E-value: 1.03e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  481 EKLNSTLEQKVR-QRTTELESAIEqaLAASksksdfianISHEIRTPMNGVLGMLEMLKEDTLTQQ-QQQYLELANSSAN 558
Cdd:COG5806    180 ENLIENILLRKElQRAEKLEVVSE--LAAS---------IAHEVRNPLTVVRGFIQLLQEPELSDEkRKQYIRIALEELD 248
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  559 SLMTLINDILDFSKIEAGKLDIDNHSFDVITVcSDMITSMALqaqRKGLEVflHTDKVIDRMLVGDSHRLKQILINLLNN 638
Cdd:COG5806    249 RAEAIITDYLTFAKPQPEKLEKIDVSEELEHV-IDVLSPYAN---MNNVEI--QTELEPGLYIEGDRQKLQQCLINIIKN 322
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  639 AFKFTHQ-GEVSLTLgcqYLTEEKLLMSfvIEDSGIGIAEKNIDKLFEAF--TQEDtsttrhfgGTGLGLSICRKLAQLM 715
Cdd:COG5806    323 GIEAMPNgGTLTIDV---SIDKNKVIIS--IKDTGVGMTKEQLERLGEPYfsTKEK--------GTGLGTMVSYRIIEAM 389
                          250
                   ....*....|....*..
gi 1889623460  716 GGDISVTSEKGQGSCFT 732
Cdd:COG5806    390 NGTIRVESEVGKGTTFT 406
AtoC COG2204
DNA-binding transcriptional response regulator, NtrC family, contains REC, AAA-type ATPase, ...
893-1012 1.08e-20

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: 95.80  E-value: 1.08e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  893 KVLLVDDNMINLEVAKAILKNTGVTIVCASDGLDALEILNTEQtalFDLILMDCQMPNLNGYDTTSAIRsnkagADYAKV 972
Cdd:COG2204      4 RILVVDDDPDIRRLLKELLERAGYEVETAASGEEALALLREEP---PDLVLLDLRMPGMDGLELLRELR-----ALDPDL 75
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1889623460  973 PIIAMTASAMAGDRERCITAGMNDYITKPIKPKVLKDKLA 1012
Cdd:COG2204     76 PVILLTGYGDVETAVEAIKAGAFDYLTKPFDLEELLAAVE 115
YesN COG4753
Two-component response regulator, YesN/AraC family, consists of REC and AraC-type DNA-binding ...
893-1001 4.13e-20

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: 86.37  E-value: 4.13e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  893 KVLLVDDNMINLEVAKAIL-KNTGVTIVC-ASDGLDALEILNTEQtalFDLILMDCQMPNLNGYDTTSAIRsnkagADYA 970
Cdd:COG4753      1 KVLIVDDEPLIREGLKRILeWEAGFEVVGeAENGEEALELLEEHK---PDLVITDINMPGMDGLELLEAIR-----ELDP 72
                           90       100       110
                   ....*....|....*....|....*....|.
gi 1889623460  971 KVPIIAMTASAMAGDRERCITAGMNDYITKP 1001
Cdd:COG4753     73 DTKIIILSGYSDFEYAQEAIKLGADDYLLKP 103
CitB COG4565
DNA-binding response regulator DpiB of citrate/malate metabolism [Transcription, Signal ...
890-1016 7.01e-20

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


Pssm-ID: 443622 [Multi-domain]  Cd Length: 138  Bit Score: 86.95  E-value: 7.01e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  890 SNFKVLLVDDNMINLEVAKAILKNTG--VTIVCASDGLDALEILNTEQtalFDLILMDCQMPNLNGYDTTSAIRsnkagA 967
Cdd:COG4565      2 KMIRVLIVEDDPMVAELLRRYLERLPgfEVVGVASSGEEALALLAEHR---PDLILLDIYLPDGDGLELLRELR-----A 73
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 1889623460  968 DYAKVPIIAMTASAMAGDRERCITAGMNDYITKPIKPKVLKDKLAMWLK 1016
Cdd:COG4565     74 RGPDVDVIVITAARDPETVREALRAGVVDYLIKPFTFERLREALERYLE 122
HisKA pfam00512
His Kinase A (phospho-acceptor) domain; dimerization and phospho-acceptor domain of histidine ...
511-576 7.87e-20

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


Pssm-ID: 459839 [Multi-domain]  Cd Length: 66  Bit Score: 84.19  E-value: 7.87e-20
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1889623460  511 SKSDFIANISHEIRTPMNGVLGMLEMLKEDTLTQQQQQYLELANSSANSLMTLINDILDFSKIEAG 576
Cdd:pfam00512    1 AKSEFLANLSHELRTPLTAIRGYLELLRDEKLDEEQREYLETILRSAERLLRLINDLLDLSRIEAG 66
PRK11360 PRK11360
two-component system sensor histidine kinase AtoS;
363-745 9.27e-20

two-component system sensor histidine kinase AtoS;


Pssm-ID: 236901 [Multi-domain]  Cd Length: 607  Bit Score: 94.65  E-value: 9.27e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  363 KERNNKIIENSLDAILTVQEDGLISNANKTALQFFDIIIDH---TKFTQLFTLAESDNSCIDETIAQGSK-----PSFEG 434
Cdd:PRK11360   261 RSLNELILESIADGVIAIDRQGKITTMNPAAEVITGLQRHElvgKPYSELFPPNTPFASPLLDTLEHGTEhvdleISFPG 340
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  435 vytdpQDQQHFYSITLTSVFDifTQRHQVAAIL--RNINSLKQTQVELeklnstleqkvrQRTTELESAIEqalaasksk 512
Cdd:PRK11360   341 -----RDRTIELSVSTSLLHN--THGEMIGALVifSDLTERKRLQRRV------------ARQERLAALGE--------- 392
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  513 sdFIANISHEIRTPMNGVLGMLEMLKEDTLTQQQQQYLELANSSANSLMTLINDILDFSKIEAGKLDidnhSFDVITVCS 592
Cdd:PRK11360   393 --LVAGVAHEIRNPLTAIRGYVQIWRQQTSDPPSQEYLSVVLREVDRLNKVIDQLLEFSRPRESQWQ----PVSLNALVE 466
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  593 DMITSMALQAQRKGLEVFLHTDKVIDRMLVgDSHRLKQILINLLNNAFKfTHQGEVSLTLGCQYLTEEKLLMSfvIEDSG 672
Cdd:PRK11360   467 EVLQLFQTAGVQARVDFETELDNELPPIWA-DPELLKQVLLNILINAVQ-AISARGKIRIRTWQYSDGQVAVS--IEDNG 542
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1889623460  673 IGIAEKNIDKLFEAFTqedtsTTRHfGGTGLGLSICRKLAQLMGGDISVTSEKGQGSCFTaqVQLHIAAEKKL 745
Cdd:PRK11360   543 CGIDPELLKKIFDPFF-----TTKA-KGTGLGLALSQRIINAHGGDIEVESEPGVGTTFT--LYLPINPQGNQ 607
REC_CheY_CheY3 cd19923
phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY3 and similar CheY ...
893-1011 9.52e-20

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: 85.85  E-value: 9.52e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  893 KVLLVDDNMINLEVAKAILKNTGVT-IVCASDGLDALEILnteQTALFDLILMDCQMPNLNGYDTTSAIRSNkagADYAK 971
Cdd:cd19923      2 KVLVVDDFSTMRRIIKNLLKELGFNnVEEAEDGVDALEKL---KAGGFDFVITDWNMPNMDGLELLKTIRAD---GALSH 75
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 1889623460  972 VPIIAMTASAmagDRERCIT---AGMNDYITKPIKPKVLKDKL 1011
Cdd:cd19923     76 LPVLMVTAEA---KKENVIAaaqAGVNNYIVKPFTAATLKEKL 115
cztS_silS_copS TIGR01386
heavy metal sensor kinase; Members of this family contain a sensor histidine kinase domain ...
513-726 1.23e-19

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: 93.22  E-value: 1.23e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  513 SDFIANISHEIRTPMNGVLGMLEML--KEDTLtqqqQQYLELANSSA---NSLMTLINDILDFSKIEAGKLDIDNHSFDv 587
Cdd:TIGR01386  242 SQFSADLAHELRTPLTNLLGQTQVAlsQPRTG----EEYREVLESNLeelERLSRMVSDMLFLARADNGQLALERVRLD- 316
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  588 itvcsdmitsmaLQAQ-RKGLEVFL----HTDKVIDR----MLVGDSHRLKQILINLLNNAFKFTHQGEvSLTLGCQYLT 658
Cdd:TIGR01386  317 ------------LAAElAKVAEYFEplaeERGVRIRVegegLVRGDPQMFRRAISNLLSNALRHTPDGG-TITVRIERRS 383
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1889623460  659 EEKLLMsfvIEDSGIGIAEKNIDKLFEAFTQEDTSTTRHFGGTGLGLSICRKLAQLMGGDISVTSEKG 726
Cdd:TIGR01386  384 DEVRVS---VSNPGPGIPPEHLSRLFDRFYRVDPARSNSGEGTGLGLAIVRSIMEAHGGRASAESPDG 448
phoR PRK11006
phosphate regulon sensor histidine kinase PhoR;
514-744 2.59e-19

phosphate regulon sensor histidine kinase PhoR;


Pssm-ID: 182895 [Multi-domain]  Cd Length: 430  Bit Score: 92.00  E-value: 2.59e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  514 DFIANISHEIRTPMNGVLGMLEMLKEDTLTQQqqqylelANSSANSLMT--------LINDILDFSKIEAG-KLDIDnhs 584
Cdd:PRK11006   206 NFFANVSHELRTPLTVLQGYLEMMQDQPLEGA-------LREKALHTMReqtqrmegLVKQLLTLSKIEAApTIDLN--- 275
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  585 fDVITVcSDMITSMALQAQrkGLEVFLHTDKV-IDRML--VGDSHRLKQILINLLNNAFKFTHQG---EVsltlgCQYLT 658
Cdd:PRK11006   276 -EKVDV-PMMLRVLEREAQ--TLSQGKHTITFeVDNSLkvFGNEDQLRSAISNLVYNAVNHTPEGthiTV-----RWQRV 346
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  659 EEKllMSFVIEDSGIGIAEKNIDKLFEAFTQEDTSTTRHFGGTGLGLSICRKLAQLMGGDISVTSEKGQGSCFTAQVQLH 738
Cdd:PRK11006   347 PQG--AEFSVEDNGPGIAPEHIPRLTERFYRVDKARSRQTGGSGLGLAIVKHALSHHDSRLEIESEVGKGTRFSFVLPER 424

                   ....*.
gi 1889623460  739 IAAEKK 744
Cdd:PRK11006   425 LIAKNS 430
REC_ETR-like cd19933
phosphoacceptor receiver (REC) domain of plant ethylene receptors ETR1, ETR2, and EIN4, and ...
893-1011 4.04e-19

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: 83.99  E-value: 4.04e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  893 KVLLVDDNMINLEVAKAILKNTGVTIVCASDGLDALEILNTEQTAlFDLILMDCQMPNLNGYDTTSAIRsnKAGADYAKV 972
Cdd:cd19933      2 KVLLVDDNAVNRMVTKGLLEKLGCEVTTVSSGEECLNLLASAEHS-FQLVLLDLCMPEMDGFEVALRIR--KLFGRRERP 78
                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1889623460  973 PIIAMTASAMAGDRERCITAGMNDYITKPIKPKVLKDKL 1011
Cdd:cd19933     79 LIVALTANTDDSTREKCLSLGMNGVITKPVSLHALGDEL 117
HisKA smart00388
His Kinase A (phosphoacceptor) domain; Dimerisation and phosphoacceptor domain of histidine ...
511-576 4.33e-19

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


Pssm-ID: 214644 [Multi-domain]  Cd Length: 66  Bit Score: 81.84  E-value: 4.33e-19
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1889623460   511 SKSDFIANISHEIRTPMNGVLGMLEMLKEDTLTQQQQQYLELANSSANSLMTLINDILDFSKIEAG 576
Cdd:smart00388    1 AKREFLANLSHELRTPLTAIRGYLELLLDTELSEEQREYLETILREAERLLRLINDLLDLSRIEAG 66
PRK10604 PRK10604
sensor protein RstB; Provisional
504-732 6.35e-19

sensor protein RstB; Provisional


Pssm-ID: 236724 [Multi-domain]  Cd Length: 433  Bit Score: 90.82  E-value: 6.35e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  504 QALAASKSKsdFIANISHEIRTPMNGVLGMLEMLkeDTLTQQQQQYLelaNSSANSLMTLINDILDFSKIEAGKLDIDNH 583
Cdd:PRK10604   206 NALIASKKQ--LIDGIAHELRTPLVRLRYRLEMS--DNLSAAESQAL---NRDIGQLEALIEELLTYARLDRPQNELHLS 278
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  584 SFDVITVCSDMITSMALQAQRKGLEV-FLHTDKVIdrmlVGDSHRLKQILINLLNNAFKFTHQG-EVSLTL-GCQYLTEe 660
Cdd:PRK10604   279 EPDLPAWLSTHLADIQAVTPEKTVRLdTPHQGDYG----ALDMRLMERVLDNLLNNALRYAHSRvRVSLLLdGNQACLI- 353
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1889623460  661 kllmsfvIEDSGIGIAEKNIDKLFEAFTQEDTSTTRHFGGTGLGLSICRKLAQLMGGDISVTSEKGQGSCFT 732
Cdd:PRK10604   354 -------VEDDGPGIPPEERERVFEPFVRLDPSRDRATGGCGLGLAIVHSIALAMGGSVNCDESELGGARFS 418
HATPase_FilI-like cd16921
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
628-732 2.82e-18

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


Pssm-ID: 340398 [Multi-domain]  Cd Length: 105  Bit Score: 81.22  E-value: 2.82e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  628 LKQILINLLNNAFKFTHQGEVS-LTLGCQYLTEEKLlmsFVIEDSGIGIAEKNIDKLFEAFTQEDTSTtrHFGGTGLGLS 706
Cdd:cd16921      1 LGQVLTNLLGNAIKFRRPRRPPrIEVGAEDVGEEWT---FYVRDNGIGIDPEYAEKVFGIFQRLHSRE--EYEGTGVGLA 75
                           90       100
                   ....*....|....*....|....*.
gi 1889623460  707 ICRKLAQLMGGDISVTSEKGQGSCFT 732
Cdd:cd16921     76 IVRKIIERHGGRIWLESEPGEGTTFY 101
CitA COG3290
Sensor histidine kinase DipB regulating citrate/malate metabolism [Signal transduction ...
331-735 4.36e-18

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


Pssm-ID: 442519 [Multi-domain]  Cd Length: 389  Bit Score: 87.60  E-value: 4.36e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  331 FVLVIISLFTALWLLVWLYQRYINRKLEFHSLKERNNKIIENSLDAILTVQEDGLISNANKTALQFFDIIIDHTKFTQLF 410
Cdd:COG3290     51 LLLLILLLILLLLLLLLLAALLLKLLEEIARLVEEREAVLESIREGVIAVDRDGRITLINDAARRLLGLDAIGRPIDEVL 130
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  411 TLAESDnscidetiaqgskpsfeGVYTDPQDQQHFYSITLTSVFDIFTQRHQVAAILRNINSLKQTQVELEKLNSTLEqk 490
Cdd:COG3290    131 AEVLET-----------------GERDEEILLNGRVLVVNRVPIRDDGRVVGAVATFRDRTELERLEEELEGVKELAE-- 191
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  491 vrqrttelesaieqALAAsksksdfianISHEIRTPMNGVLGMLEMLKEDTLtqqqqqyLELANSSANSLMTLINDILDF 570
Cdd:COG3290    192 --------------ALRA----------QRHDFRNHLHTISGLLQLGEYDEA-------LEYIDEISEELQELIDSLLSR 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  571 skieagkldIDNHSFDVItvcsdmITSMALQAQRKGLEVFLHTDKVIDRMLVGDSHrLKQILINLLNNAF-----KFTHQ 645
Cdd:COG3290    241 ---------IGNPVLAAL------LLGKAARARERGIDLTIDIDSDLPDLPLSDTD-LVTILGNLLDNAIeavekLPEEE 304
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  646 GEVSLTLGCqylTEEKLLmsFVIEDSGIGIAEKNIDKLFEaftqeDTSTTRHFGGTGLGLSICRKLAQLMGGDISVTSEK 725
Cdd:COG3290    305 RRVELSIRD---DGDELV--IEVEDSGPGIPEELLEKIFE-----RGFSTKLGEGRGLGLALVKQIVEKYGGTIEVESEE 374
                          410
                   ....*....|
gi 1889623460  726 GQGSCFTAQV 735
Cdd:COG3290    375 GEGTVFTVRL 384
PRK11100 PRK11100
sensory histidine kinase CreC; Provisional
521-741 4.64e-18

sensory histidine kinase CreC; Provisional


Pssm-ID: 236846 [Multi-domain]  Cd Length: 475  Bit Score: 88.36  E-value: 4.64e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  521 HEIRTPMNGVLGMLEMLKEDTLTQQQQQYLELANSSANSLMTLINDILDFSKIEAGKLDIDNHSFDVITVCSDMITSMAL 600
Cdd:PRK11100   265 HELKSPLAAIRGAAELLQEDPPPEDRARFTGNILTQSARLQQLIDRLLELARLEQRQELEVLEPVALAALLEELVEAREA 344
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  601 QAQRKGLEVFLHTDkviDRMLVGDSHRLKQILINLLNNAFKFTHQG-EVSLTLGcqyLTEEKLLmsFVIEDSGIGIAEKN 679
Cdd:PRK11100   345 QAAAKGITLRLRPD---DARVLGDPFLLRQALGNLLDNAIDFSPEGgTITLSAE---VDGEQVA--LSVEDQGPGIPDYA 416
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1889623460  680 IDKLFEAFTqedtSTTRHFGG---TGLGLSICRKLAQLMGGDISVTSEKGQGSCftAQVQLHIAA 741
Cdd:PRK11100   417 LPRIFERFY----SLPRPANGrksTGLGLAFVREVARLHGGEVTLRNRPEGGVL--ATLTLPRHF 475
HATPase_BaeS-like cd16946
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
624-720 4.67e-18

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: 80.58  E-value: 4.67e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  624 DSHRLKQILINLLNNAFKFTHQGEvSLTLGCQYLTEEkllMSFVIEDSGIGIAEKNIDKLFEAFTQEDTSTTRHFGGTGL 703
Cdd:cd16946      1 DRDRLQQLFVNLLENSLRYTDTGG-KLRIRAAQTPQE---VRLDVEDSAPGVSDDQLARLFERFYRVESSRNRASGGSGL 76
                           90
                   ....*....|....*..
gi 1889623460  704 GLSICRKLAQLMGGDIS 720
Cdd:cd16946     77 GLAICHNIALAHGGTIS 93
PRK13837 PRK13837
two-component system VirA-like sensor kinase;
489-731 5.26e-18

two-component system VirA-like sensor kinase;


Pssm-ID: 237526 [Multi-domain]  Cd Length: 828  Bit Score: 89.35  E-value: 5.26e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  489 QKVRQRTTELESAIEQA--LAASKSksdFIANISHEIRTPMNGVLGMLEM----LKEDTLTQQqqqYLELANSSANSLMT 562
Cdd:PRK13837   428 RRLETERDALERRLEHArrLEAVGT---LASGIAHNFNNILGAILGYAEMalnkLARHSRAAR---YIDEIISAGARARL 501
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  563 LINDILDFSKieagKLDIDNHSFDVITVCSDMITSMALQAQRkGLEVFLHTDKviDRMLV-GDSHRLKQILINLLNNAFK 641
Cdd:PRK13837   502 IIDQILAFGR----KGERNTKPFDLSELVTEIAPLLRVSLPP-GVELDFDQDQ--EPAVVeGNPAELQQVLMNLCSNAAQ 574
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  642 -FTHQGEVSLTLGCQYLTEEKLLMSFVI----------EDSGIGIAEKNIDKLFEAFTqedtsTTRHfGGTGLGLSICRK 710
Cdd:PRK13837   575 aMDGAGRVDISLSRAKLRAPKVLSHGVLppgryvllrvSDTGAGIDEAVLPHIFEPFF-----TTRA-GGTGLGLATVHG 648
                          250       260
                   ....*....|....*....|.
gi 1889623460  711 LAQLMGGDISVTSEKGQGSCF 731
Cdd:PRK13837   649 IVSAHAGYIDVQSTVGRGTRF 669
HATPase_RstB-like cd16939
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
628-732 1.87e-17

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: 78.63  E-value: 1.87e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  628 LKQILINLLNNAFKFTH-QGEVSLTLGCQYLTeekllmsFVIEDSGIGIAEKNIDKLFEAFTQEDTSTTRHFGGTGLGLS 706
Cdd:cd16939      1 MARALDNLLRNALRYAHrTVRIALLVSGGRLT-------LIVEDDGPGIPAAARERVFEPFVRLDPSRDRATGGFGLGLA 73
                           90       100
                   ....*....|....*....|....*..
gi 1889623460  707 ICRKLAQLMGGDISVT-SEKGqGSCFT 732
Cdd:cd16939     74 IVHRVALWHGGHVECDdSELG-GACFR 99
REC_Ycf29 cd19927
phosphoacceptor receiver (REC) domain of probable transcriptional regulator Ycf29; Ycf29 is a ...
894-1001 2.73e-17

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: 78.19  E-value: 2.73e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  894 VLLVDDNMINLEVAKAILKNTGVTIVCASDGLDALEILNTEqtaLFDLILMDCQMPNLNGYDTTSAIRSNkagADYAKVP 973
Cdd:cd19927      1 ILLVDDDPGIRLAVKDYLEDQGFTVIAASNGLEALDLLNQY---IPDLIISDIIMPGVDGYSLLGKLRKN---ADFDTIP 74
                           90       100
                   ....*....|....*....|....*...
gi 1889623460  974 IIAMTASAMAGDRERCITAGMNDYITKP 1001
Cdd:cd19927     75 VIFLTAKGMTSDRIKGYNAGCDGYLSKP 102
HATPase_TutC-TodS-like cd16925
Histidine kinase-like ATPase domain of hybrid sensor histidine kinases similar to Pseudomonas ...
624-735 2.79e-17

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: 78.30  E-value: 2.79e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  624 DSHRLKQILINLLNNAFKFTHQG-------EVSLTLGCQylteekllmsFVIEDSGIGIAEKNIDKLFEAFTQEDTSTTR 696
Cdd:cd16925      1 DAEKYERVVLNLLSNAFKFTPDGgrircilEKFRLNRFL----------LTVSDSGPGIPPNLREEIFERFRQGDGSSTR 70
                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1889623460  697 HFGGTGLGLSICRKLAQLMGGDISVTSEKGQGSCFTAQV 735
Cdd:cd16925     71 AHGGTGLGLSIVKEFVELHGGTVTVSDAPGGGALFQVEL 109
PRK10549 PRK10549
two-component system sensor histidine kinase BaeS;
511-720 4.98e-17

two-component system sensor histidine kinase BaeS;


Pssm-ID: 182539 [Multi-domain]  Cd Length: 466  Bit Score: 85.07  E-value: 4.98e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  511 SKSDFIANISHEIRTPMNGVLGMLEMLKEDT--LTQQQQQYL--ELANssansLMTLINDILDFSKIEAGKLDIDNHSFD 586
Cdd:PRK10549   239 MRRDFMADISHELRTPLAVLRGELEAIQDGVrkFTPESVASLqaEVGT-----LTKLVDDLHQLSLSDEGALAYRKTPVD 313
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  587 VITVCSDMITSMALQAQRKGLEvfLHTDKVIDRMLVGDSHRLKQILINLLNNAFKFTH-QGEVSLTLGcqyLTEEKLLMS 665
Cdd:PRK10549   314 LVPLLEVAGGAFRERFASRGLT--LQLSLPDSATVFGDPDRLMQLFNNLLENSLRYTDsGGSLHISAE---QRDKTLRLT 388
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1889623460  666 FviEDSGIGIAEKNIDKLFEAFTQEDTSTTRHFGGTGLGLSICRKLAQLMGGDIS 720
Cdd:PRK10549   389 F--ADSAPGVSDEQLQKLFERFYRTEGSRNRASGGSGLGLAICLNIVEAHNGRII 441
PRK10618 PRK10618
phosphotransfer intermediate protein in two-component regulatory system with RcsBC; Provisional
473-774 6.00e-17

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


Pssm-ID: 236726 [Multi-domain]  Cd Length: 894  Bit Score: 86.14  E-value: 6.00e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  473 LKQTQVELEKlnstlEQKVRQRttelesaieqalaasksksdFIANISHEIRTPMNGVLGMLEMLKEDTLTQQQQQYLEL 552
Cdd:PRK10618   436 LQQAQREYEK-----NQQARKA--------------------FLQNIGDELKQPLQSLAQLAAQLRQTSDEEQQQPELDQ 490
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  553 ANSSANSLMTLINDILDFSKIEAGKLDIDNHSFDVITVCSDMITSMALQAQRKGLEVFLHTDKVIDRMLVGDSHRLKQIL 632
Cdd:PRK10618   491 LAEQSDVLVRLVDNIQLLNMLETQDWKPEQELFSLQDLIDEVLPEVLPAIKRKGLQLLIHNHLKAEQLRIGDRDALRKIL 570
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  633 INLLNNAFKFTHQGEVSLTlgCQYLTEEKLLMSFVIEDSGIGIAEKNIDKL---FEAFTQEDtsttRHFGGTGLGLSICR 709
Cdd:PRK10618   571 LLLLNYAITTTAYGKITLE--VDQDESSPDRLTIRILDTGAGVSIKELDNLhfpFLNQTQGD----RYGKASGLTFFLCN 644
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1889623460  710 KLAQLMGGDISVTSEKGQGSCFTaqVQLHIAAEKKLNTAVE--LAKDIQVGVLIDSDSVYNNVTNLL 774
Cdd:PRK10618   645 QLCRKLGGHLTIKSREGLGTRYS--IHLKMLAADPEVEEEEekLLDGVTVLLDITSEEVRKIVTRQL 709
HATPase_BasS-like cd16940
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
623-737 4.23e-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 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: 75.13  E-value: 4.23e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  623 GDSHRLKQILINLLNNAFKFTHQG-EVSLTLgcqyltEEKLLMSFVIEDSGIGIAEKNIDKLFEAFTQEDTsttRHFGGT 701
Cdd:cd16940      9 GDALLLFLLLRNLVDNAVRYSPQGsRVEIKL------SADDGAVIRVEDNGPGIDEEELEALFERFYRSDG---QNYGGS 79
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1889623460  702 GLGLSICRKLAQLMGGdiSVTSEKGQGSCFTAQVQL 737
Cdd:cd16940     80 GLGLSIVKRIVELHGG--QIFLGNAQGGGLEAWVRL 113
REC_CheY4-like cd17562
phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY4 and similar CheY ...
893-1007 6.40e-16

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: 74.64  E-value: 6.40e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  893 KVLLVDDNMINLEVAKAILKNTGVTIVCASDGLDALEILNTEQtalFDLILMDCQMPNLNGYDTTSAIRSNKAgadYAKV 972
Cdd:cd17562      2 KILAVDDSASIRQMVSFTLRGAGYEVVEAADGRDALSKAQSKK---FDLIITDQNMPNMDGIELIKELRKLPA---YKFT 75
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1889623460  973 PIIAMTASAMAGDRERCITAGMNDYITKPIKPKVL 1007
Cdd:cd17562     76 PILMLTTESSDEKKQEGKAAGATGWLVKPFDPEQL 110
REC_Rcp-like cd17557
phosphoacceptor receiver (REC) domain of cyanobacterial phytochrome response regulator Rcp and ...
893-1002 7.55e-16

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: 74.76  E-value: 7.55e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  893 KVLLVDDNMINLEVAKAILKNTGVT--IVCASDGLDALEILNTE----QTALFDLILMDCQMPNLNGYDTTSAIRSNkag 966
Cdd:cd17557      1 TILLVEDNPGDAELIQEAFKEAGVPneLHVVRDGEEALDFLRGEgeyaDAPRPDLILLDLNMPRMDGFEVLREIKAD--- 77
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1889623460  967 ADYAKVPIIAMTASAMAGDRERCITAGMNDYITKPI 1002
Cdd:cd17557     78 PDLRRIPVVVLTTSDAEEDIERAYELGANSYIVKPV 113
REC_OmpR_PhoB cd17618
phosphoacceptor receiver (REC) domain of PhoB response regulator from the OmpR family; The ...
893-1007 1.56e-15

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


Pssm-ID: 381133 [Multi-domain]  Cd Length: 118  Bit Score: 73.82  E-value: 1.56e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  893 KVLLVDDNMINLEVAKAILKNTGVTIVCASDGLDALEILnteQTALFDLILMDCQMPNLNGYDTTSAIRSNKAGADyakV 972
Cdd:cd17618      2 TILIVEDEPAIREMIAFNLERAGFDVVEAEDAESAVNLI---VEPRPDLILLDWMLPGGSGIQFIRRLKRDEMTRD---I 75
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1889623460  973 PIIAMTASAMAGDRERCITAGMNDYITKPIKPKVL 1007
Cdd:cd17618     76 PIIMLTARGEEEDKVRGLEAGADDYITKPFSPREL 110
HATPase_TmoS-FixL-DctS-like cd16920
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
628-732 2.25e-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: 72.81  E-value: 2.25e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  628 LKQILINLLNNAFKFTHQGEVS---LTLgcQYLTEEKLLMSFVIEDSGIGIAEKNIDKLFEAFTqedtsTTRHfGGTGLG 704
Cdd:cd16920      1 IQQVLINLVRNGIEAMSEGGCErreLTI--RTSPADDRAVTISVKDTGPGIAEEVAGQLFDPFY-----TTKS-EGLGMG 72
                           90       100
                   ....*....|....*....|....*...
gi 1889623460  705 LSICRKLAQLMGGDISVTSEKGQGSCFT 732
Cdd:cd16920     73 LSICRSIIEAHGGRLSVESPAGGGATFQ 100
REC_OmpR_BsPhoP-like cd19937
phosphoacceptor receiver (REC) domain of BsPhoP-like OmpR family response regulators; Bacillus ...
895-1007 2.40e-15

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: 73.08  E-value: 2.40e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  895 LLVDDNMINLEVAKAILKNTGVTIVCASDGLDALEILNTEQtalFDLILMDCQMPNLNGYDTTSAIRSNKagaDYAKVPI 974
Cdd:cd19937      1 LVVDDEEDIVELLKYNLEKEGYEVVTAYDGEEALKRAKDEK---PDLIILDLMLPGIDGLEVCRILRSDP---KTSSIPI 74
                           90       100       110
                   ....*....|....*....|....*....|...
gi 1889623460  975 IAMTASAMAGDRERCITAGMNDYITKPIKPKVL 1007
Cdd:cd19937     75 IMLTAKGEEFDKVLGLELGADDYITKPFSPREL 107
REC_CheV-like cd19924
phosphoacceptor receiver (REC) domain of chemotaxis protein CheV and similar proteins; This ...
894-1001 2.46e-15

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: 72.80  E-value: 2.46e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  894 VLLVDDNMINLEVAKAILKNTGVTIVCASDGLDALEILN------TEQTALFDLILMDCQMPNLNGYDTTSAIRSNKAga 967
Cdd:cd19924      1 ILVVDDSPTARKQLRDLLKNLGFEIAEAVDGEEALNKLEnlakegNDLSKELDLIITDIEMPKMDGYELTFELRDDPR-- 78
                           90       100       110
                   ....*....|....*....|....*....|....
gi 1889623460  968 dYAKVPIIAMTASAMAGDRERCITAGMNDYITKP 1001
Cdd:cd19924     79 -LANIPVILNSSLSGEFSRARGKKVGADAYLAKF 111
REC_typeB_ARR-like cd17584
phosphoacceptor receiver (REC) domain of type B Arabidopsis response regulators (ARRs) and ...
894-1014 2.58e-15

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: 73.05  E-value: 2.58e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  894 VLLVDDNMINLEVAKAILKNTGVTIVCASDGLDALEILNtEQTALFDLILMDCQMPNLNGYDTTSAIRSNKagadyaKVP 973
Cdd:cd17584      1 VLVVDDDPTCLAILKRMLLRCGYQVTTCTDAEEALSMLR-ENKDEFDLVITDVHMPDMDGFEFLELIRLEM------DLP 73
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 1889623460  974 IIAMTASAMAGDRERCITAGMNDYITKPIKPKVLKDklaMW 1014
Cdd:cd17584     74 VIMMSADGSTSTVMKGLAHGACDYLLKPVSIEDLKN---IW 111
HisKA cd00082
Histidine Kinase A (dimerization/phosphoacceptor) domain; Histidine Kinase A dimers are formed ...
509-572 3.50e-15

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: 70.70  E-value: 3.50e-15
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1889623460  509 SKSKSDFIANISHEIRTPMNGVLGMLEMLKEDTL-TQQQQQYLELANSSANSLMTLINDILDFSK 572
Cdd:cd00082      1 LQAKGEFLANVSHELRTPLTAIRGALELLEEELLdDEEQREYLERIREEAERLLRLINDLLDLSR 65
PRK10364 PRK10364
two-component system sensor histidine kinase ZraS;
489-744 3.76e-15

two-component system sensor histidine kinase ZraS;


Pssm-ID: 236674 [Multi-domain]  Cd Length: 457  Bit Score: 79.06  E-value: 3.76e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  489 QKVRQRTTELESAI--EQALAASkskSDFIANISHEIRTPMNGVLGMLEMLKEDTLTQQQQQylELAN---SSANSLMTL 563
Cdd:PRK10364   215 RRYLRSRQLLQDEMkrKEKLVAL---GHLAAGVAHEIRNPLSSIKGLAKYFAERAPAGGEAH--QLAQvmaKEADRLNRV 289
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  564 INDILDFSK-----IEAGKL-DIDNHSFDVITvcSDmitsmalqAQRKGLEVFLHTDKVIDRMLVgDSHRLKQILINLLN 637
Cdd:PRK10364   290 VSELLELVKpthlaLQAVDLnDLINHSLQLVS--QD--------ANSREIQLRFTANDTLPEIQA-DPDRLTQVLLNLYL 358
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  638 NAFK-FTHQGEVSLTLgcqylTEEKLLMSFVIEDSGIGIAEKNIDKLFEAFTqedtsTTRHfGGTGLGLSICRKLAQLMG 716
Cdd:PRK10364   359 NAIQaIGQHGVISVTA-----SESGAGVKISVTDSGKGIAADQLEAIFTPYF-----TTKA-EGTGLGLAVVHNIVEQHG 427
                          250       260
                   ....*....|....*....|....*...
gi 1889623460  717 GDISVTSEKGQGSCFTaqVQLHIAAEKK 744
Cdd:PRK10364   428 GTIQVASQEGKGATFT--LWLPVNITRR 453
orf27 CHL00148
Ycf27; Reviewed
890-1016 4.63e-15

Ycf27; Reviewed


Pssm-ID: 214376 [Multi-domain]  Cd Length: 240  Bit Score: 75.91  E-value: 4.63e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  890 SNFKVLLVDDNMINLEVAKAILKNTGVTIVCASDGLDALEILNTEQTalfDLILMDCQMPNLNGYDTTSAIRSNkagady 969
Cdd:CHL00148     5 SKEKILVVDDEAYIRKILETRLSIIGYEVITASDGEEALKLFRKEQP---DLVILDVMMPKLDGYGVCQEIRKE------ 75
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 1889623460  970 AKVPIIAMTASAMAGDRERCITAGMNDYITKPIKPKVLKDKLAMWLK 1016
Cdd:CHL00148    76 SDVPIIMLTALGDVSDRITGLELGADDYVVKPFSPKELEARIRSVLR 122
REC_NarL-like cd17535
phosphoacceptor receiver (REC) domain of NarL (Nitrate/Nitrite response regulator L) family ...
894-1009 5.83e-15

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: 72.16  E-value: 5.83e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  894 VLLVDDNMINLEVAKAIL-KNTGVTIVC-ASDGLDALEILNTEQtalFDLILMDCQMPNLNGYDTTSAIRSnkagaDYAK 971
Cdd:cd17535      1 VLIVDDHPLVREGLRRLLeSEPDIEVVGeAADGEEALALLRELR---PDVVLMDLSMPGMDGIEALRRLRR-----RYPD 72
                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1889623460  972 VPIIAMTASAMAGDRERCITAGMNDYITKPIKPKVLKD 1009
Cdd:cd17535     73 LKVIVLTAHDDPEYVLRALKAGAAGYLLKDSSPEELIE 110
HATPase_AtoS-like cd16943
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
628-732 6.55e-15

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: 71.68  E-value: 6.55e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  628 LKQILINLLNNAFK-FTHQGEVSLTlgcQYLTEEKLLMSfvIEDSGIGIAEKNIDKLFEAFTqedtsTTRHFG-GTGLGL 705
Cdd:cd16943      4 LNQVLLNLLVNAAQaMEGRGRITIR---TWAHVDQVLIE--VEDTGSGIDPEILGRIFDPFF-----TTKPVGeGTGLGL 73
                           90       100
                   ....*....|....*....|....*..
gi 1889623460  706 SICRKLAQLMGGDISVTSEKGQGSCFT 732
Cdd:cd16943     74 SLSYRIIQKHGGTIRVASVPGGGTRFT 100
HATPase_YcbM-like cd16947
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
623-732 1.12e-14

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: 71.39  E-value: 1.12e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  623 GDSHRLKQILINLLNNAFKFTHQGEVsltLGcQYLTEEKLLMSFVIEDSGIGIAEKNIDKLFE-AFTQEDtSTTRHFGGT 701
Cdd:cd16947     16 ANTEALQRILKNLISNAIKYGSDGKF---LG-MTLREDEKHVYIDIWDKGKGISETEKDHVFErLYTLED-SRNSAKQGN 90
                           90       100       110
                   ....*....|....*....|....*....|.
gi 1889623460  702 GLGLSICRKLAQLMGGDISVTSEKGQGSCFT 732
Cdd:cd16947     91 GLGLTITKRLAESMGGSIYVNSKPYEKTVFT 121
HATPase_PhoQ-like cd16954
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
603-731 1.26e-14

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: 71.51  E-value: 1.26e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  603 QRKGLEVFLHTDKVIdrMLVGDSHRLKQILINLLNNAFKFTHqGEVSLTLgcqYLTEEKLLMsfVIEDSGIGIAEKNIDK 682
Cdd:cd16954     15 QRKGVSISLDISPEL--RFPGERNDLMELLGNLLDNACKWCL-EFVEVTA---RQTDGGLHL--IVDDDGPGVPESQRSK 86
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 1889623460  683 LFEAFTQEDTSTTrhfgGTGLGLSICRKLAQLMGGDISVTSEKGQGSCF 731
Cdd:cd16954     87 IFQRGQRLDEQRP----GQGLGLAIAKEIVEQYGGELSLSDSPLGGARF 131
AmiR COG3707
Two-component response regulator, AmiR/NasT family, consists of REC and RNA-binding ...
893-1013 2.12e-14

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: 72.68  E-value: 2.12e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  893 KVLLVDDNMINLEVAKAILKNTGVTIV-CASDGLDALEILNTEQtalFDLILMDCQMPNLNGYDTTSAIRSNKAgadyak 971
Cdd:COG3707      5 RVLVVDDEPLRRADLREGLREAGYEVVaEAADGEDAVELVRELK---PDLVIVDIDMPDRDGLEAARQISEERP------ 75
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1889623460  972 VPIIAMTASAMAGDRERCITAGMNDYITKPIKPKVLKDKLAM 1013
Cdd:COG3707     76 APVILLTAYSDPELIERALEAGVSAYLVKPLDPEDLLPALEL 117
PhoB TIGR02154
phosphate regulon transcriptional regulatory protein PhoB; PhoB is a DNA-binding response ...
893-1007 3.80e-14

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: 72.75  E-value: 3.80e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  893 KVLLVDDNMINLEVAKAILKNTGVTIVCASDGLDALEILNTEqtaLFDLILMDCQMPNLNGYDTtsaIRSNKAGADYAKV 972
Cdd:TIGR02154    4 RILVVEDEPAIRELIAYNLEKAGYDVVEAGDGDEALTLINER---GPDLILLDWMLPGTSGIEL---CRRLRRRPETRAI 77
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1889623460  973 PIIAMTASAMAGDRERCITAGMNDYITKPIKPKVL 1007
Cdd:TIGR02154   78 PIIMLTARGEEEDRVRGLETGADDYITKPFSPREL 112
REC_OmpR_PrrA-like cd17627
phosphoacceptor receiver (REC) domain of PrrA-like OmpR family response regulators; The ...
894-1001 6.67e-14

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


Pssm-ID: 381142 [Multi-domain]  Cd Length: 116  Bit Score: 68.95  E-value: 6.67e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  894 VLLVDDNMINLEVAKAILKNTGVTIVCASDGLDALEILNTEQTalfDLILMDCQMPNLNGYDTTSAIRsnKAGADyakVP 973
Cdd:cd17627      1 ILVVDDDRAVRESLRRSLRFEGYEVETAVDGAEALRVISGNRP---DAVVLDVMMPRLDGLEVCRRLR--AAGND---LP 72
                           90       100
                   ....*....|....*....|....*...
gi 1889623460  974 IIAMTASAMAGDRERCITAGMNDYITKP 1001
Cdd:cd17627     73 ILVLTARDSVSDRVAGLDAGADDYLVKP 100
HATPase_HupT_MifS-like cd16976
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
628-732 2.03e-13

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: 67.10  E-value: 2.03e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  628 LKQILINLLNNAFKFTHQGEV-SLTLGCQYLTEEKLLmsfVIEDSGIGIAEKNIDKLFEAFTqedtsTTRHFG-GTGLGL 705
Cdd:cd16976      1 IQQVLMNLLQNALDAMGKVENpRIRIAARRLGGRLVL---VVRDNGPGIAEEHLSRVFDPFF-----TTKPVGkGTGLGL 72
                           90       100
                   ....*....|....*....|....*..
gi 1889623460  706 SICRKLAQLMGGDISVTSEKGQGSCFT 732
Cdd:cd16976     73 SISYGIVEEHGGRLSVANEEGAGARFT 99
Spo0F COG5803
Stage 0 sporulation initiation response regulator Spo0F [Cell cycle control, cell division, ...
893-1001 2.41e-13

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: 67.51  E-value: 2.41e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  893 KVLLVDD-----NMINlEVakaiLKNTGVTIVCASDGLDALEILNTEQtalFDLILMDCQMPNLNGYDTTSAIRSnkaga 967
Cdd:COG5803      4 KILIVDDqagirMLLK-EV----LKKEGYEVFQAANGKEALEKVKELK---PDLVLLDMKMPGMDGIEILKEIKE----- 70
                           90       100       110
                   ....*....|....*....|....*....|....
gi 1889623460  968 DYAKVPIIAMTASAMAGDRERCITAGMNDYITKP 1001
Cdd:COG5803     71 IDPDIPVIMMTAYGELDMVEEAKELGAKGYFTKP 104
PRK10490 PRK10490
sensor protein KdpD; Provisional
516-731 3.64e-13

sensor protein KdpD; Provisional


Pssm-ID: 236701 [Multi-domain]  Cd Length: 895  Bit Score: 73.92  E-value: 3.64e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  516 IANISHEIRTPMNGVLGMLEMLKEDtLTQQQQQYLELANSSANSLMT---LINDILDFSKIEAGKLDIDNHSFDVITVCS 592
Cdd:PRK10490   668 LAALSHDLRTPLTVLFGQAEILTLD-LASEGSPHARQASEIRQQVLNttrLVNNLLDMARIQSGGFNLRKEWLTLEEVVG 746
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  593 DMITSMALQAQRKGLEVFLHTDKVidrMLVGDSHRLKQILINLLNNAFKFTHQGevsLTLGCQYLTEEKLLmSFVIEDSG 672
Cdd:PRK10490   747 SALQMLEPGLSGHPINLSLPEPLT---LIHVDGPLFERVLINLLENAVKYAGAQ---AEIGIDAHVEGERL-QLDVWDNG 819
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1889623460  673 IGIAEKNIDKLFEAFTQEDTSTTrhFGGTGLGLSICRKLAQLMGGDISVTSEKGQGSCF 731
Cdd:PRK10490   820 PGIPPGQEQLIFDKFARGNKESA--IPGVGLGLAICRAIVEVHGGTIWAENRPEGGACF 876
REC smart00448
cheY-homologous receiver domain; CheY regulates the clockwise rotation of E. coli flagellar ...
893-949 4.26e-13

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


Pssm-ID: 214668 [Multi-domain]  Cd Length: 55  Bit Score: 64.51  E-value: 4.26e-13
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*..
gi 1889623460   893 KVLLVDDNMINLEVAKAILKNTGVTIVCASDGLDALEILNTEQtalFDLILMDCQMP 949
Cdd:smart00448    2 RILVVDDDPLLRELLKALLEKEGYEVDEATDGEEALELLKEEK---PDLILLDIMMP 55
REC_OmpR_MtrA-like cd17626
phosphoacceptor receiver (REC) domain of MtrA-like OmpR family response regulators; MtrA is ...
893-1007 4.98e-13

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: 66.34  E-value: 4.98e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  893 KVLLVDDNMINLEVAKAILKNTGVTIVCASDGLDALEILNTEQTalfDLILMDCQMPNLNGYDTTSAIRsnkagaDYAKV 972
Cdd:cd17626      2 RILVVDDDAALAEMIGIVLRGEGFDPAFCGDGTQALAAFREVRP---DLVLLDLMLPGIDGIEVCRQIR------AESGV 72
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1889623460  973 PIIAMTASAMAGDRERCITAGMNDYITKPIKPKVL 1007
Cdd:cd17626     73 PIVMLTAKSDTVDVVLGLESGADDYVAKPFKPKEL 107
HATPase_SpaK_NisK-like cd16975
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
624-732 5.68e-13

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: 65.95  E-value: 5.68e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  624 DSHRLKQILINLLNNAFKFT-HQGEVSLTLGCqylteEKLLMSFVIEDSGIGIAEKNIDKLFEAFTQEDTSttRHFGG-T 701
Cdd:cd16975      1 DTLLLSRALINIISNACQYApEGGTVSISIYD-----EEEYLYFEIWDNGHGFSEQDLKKALELFYRDDTS--RRSGGhY 73
                           90       100       110
                   ....*....|....*....|....*....|.
gi 1889623460  702 GLGLSICRKLAQLMGGDISVTSEKGQGSCFT 732
Cdd:cd16975     74 GMGLYIAKNLVEKHGGSLIIENSQKGGAEVT 104
REC_PatA-like cd17602
phosphoacceptor receiver (REC) domain of PatA and similar domains; Nostoc sp. (or Anabaena sp.) ...
894-1001 1.33e-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: 64.70  E-value: 1.33e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  894 VLLVDDNMINLEVAKAILKNTGVTIVCASDGLDALEILNTEQTalfDLILMDCQMPNLNGYDTTSAIRSNKAgadYAKVP 973
Cdd:cd17602      1 VACVDDRPSIQKMIEYFLEKQGFRVVVIDDPLRALTTLLNSKP---DLILIDIDMPDLDGYELCSLLRKSSA---LKDTP 74
                           90       100
                   ....*....|....*....|....*...
gi 1889623460  974 IIAMTASAMAGDRERCITAGMNDYITKP 1001
Cdd:cd17602     75 IIMLTGKDGLVDRIRAKMAGASGYLTKP 102
HATPase_EnvZ-like cd16950
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
628-737 1.42e-12

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


Pssm-ID: 340426 [Multi-domain]  Cd Length: 101  Bit Score: 64.78  E-value: 1.42e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  628 LKQILINLLNNAFKFThQGEVSLTLGcqylTEEKLLmSFVIEDSGIGIAEKNIDKLFEAFTQEDTSttRHFGGTGLGLSI 707
Cdd:cd16950      1 LKRVLSNLVDNALRYG-GGWVEVSSD----GEGNRT-RIQVLDNGPGIAPEEVDELFQPFYRGDNA--RGTSGTGLGLAI 72
                           90       100       110
                   ....*....|....*....|....*....|
gi 1889623460  708 CRKLAQLMGGDISVTSEKGQGSCftAQVQL 737
Cdd:cd16950     73 VQRISDAHGGSLTLANRAGGGLC--ARIEL 100
REC_CheC-like cd17593
phosphoacceptor receiver (REC) domain of uncharacterized response regulators containing a CheC ...
892-1012 1.44e-12

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: 65.25  E-value: 1.44e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  892 FKVLLVDD-NMINLEVAKAILKNTGVTIVCASDGLDALEILNTEQtalFDLILMDCQMPNLNGYDTTSAIRSNKagadyA 970
Cdd:cd17593      1 MKVLICDDsSMARKQLARALPADWDVEITFAENGEEALEILREGR---IDVLFLDLTMPVMDGYEVLEALPVEQ-----L 72
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1889623460  971 KVPIIAMTASAMAGDRERCITAGMNDYITKPIKPKVLKDKLA 1012
Cdd:cd17593     73 ETKVIVVSGDVQPEAKERVLELGALAFLKKPFDPEKLAQLLE 114
REC_OmpR_CusR-like cd19935
phosphoacceptor receiver (REC) domain of CusR-like OmpR family response regulators; ...
894-1001 1.44e-12

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: 64.77  E-value: 1.44e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  894 VLLVDDNMINLEVAKAILKNTGVTIVCASDGLDALEILNTEQtalFDLILMDCQMPNLNGYDTTSAIRSNKAgadyaKVP 973
Cdd:cd19935      1 ILVVEDEKKLAEYLKKGLTEEGYAVDVAYDGEDGLHLALTNE---YDLIILDVMLPGLDGLEVLRRLRAAGK-----QTP 72
                           90       100
                   ....*....|....*....|....*...
gi 1889623460  974 IIAMTASAMAGDRERCITAGMNDYITKP 1001
Cdd:cd19935     73 VLMLTARDSVEDRVKGLDLGADDYLVKP 100
REC_RR468-like cd17552
phosphoacceptor receiver (REC) domain of Thermotoga maritima response regulator RR468 and ...
893-1004 1.69e-12

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: 65.27  E-value: 1.69e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  893 KVLLVDDNMINLEVAKAILKNT-GVTIVCASDGLDALEILNTEQTalfDLILMDCQMPNLNGYDTTSAIRSNKAgadYAK 971
Cdd:cd17552      3 RILVIDDEEDIREVVQACLEKLaGWEVLTASSGQEGLEKAATEQP---DAILLDVMMPDMDGLATLKKLQANPE---TQS 76
                           90       100       110
                   ....*....|....*....|....*....|...
gi 1889623460  972 VPIIAMTASAMAGDRERCITAGMNDYITKPIKP 1004
Cdd:cd17552     77 IPVILLTAKAQPSDRQRFASLGVAGVIAKPFDP 109
REC_CheY cd17542
phosphoacceptor receiver (REC) domain of chemotaxis protein CheY; The chemotaxis response ...
892-1008 1.96e-12

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: 64.99  E-value: 1.96e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  892 FKVLLVDDNMINLEVAKAILKNTGVTIVC-ASDGLDALEILNTEQTalfDLILMDCQMPNLNGYDTTSAIRSNKAGadyA 970
Cdd:cd17542      1 KKVLIVDDAAFMRMMLKDILTKAGYEVVGeAANGEEAVEKYKELKP---DLVTMDITMPEMDGIEALKEIKKIDPN---A 74
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1889623460  971 KVPIIamtaSAMaGDRE---RCITAGMNDYITKPIKP-KVLK 1008
Cdd:cd17542     75 KVIMC----SAM-GQEEmvkEAIKAGAKDFIVKPFQPeRVLE 111
PRK10955 PRK10955
envelope stress response regulator transcription factor CpxR;
893-1007 2.32e-12

envelope stress response regulator transcription factor CpxR;


Pssm-ID: 182864 [Multi-domain]  Cd Length: 232  Bit Score: 67.91  E-value: 2.32e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  893 KVLLVDDNMINLEVAKAILKNTGVTIVCASDGLDALEILNTEqtalFDLILMDCQMPNLNGYDTTSAIRSNKagadyaKV 972
Cdd:PRK10955     3 KILLVDDDRELTSLLKELLEMEGFNVIVAHDGEQALDLLDDS----IDLLLLDVMMPKKNGIDTLKELRQTH------QT 72
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1889623460  973 PIIAMTASAMAGDRERCITAGMNDYITKPIKPKVL 1007
Cdd:PRK10955    73 PVIMLTARGSELDRVLGLELGADDYLPKPFNDREL 107
REC_OmpR_CpxR cd17623
phosphoacceptor receiver (REC) domain of CpxR-like OmpR family response regulators; CpxR is ...
894-1007 2.40e-12

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: 64.63  E-value: 2.40e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  894 VLLVDDNMINLEVAKAILKNTGVTIVCASDGLDALEILNTEQtalFDLILMDCQMPNLNGYDTTSAIRSNkagadyAKVP 973
Cdd:cd17623      1 ILLIDDDRELTELLTEYLEMEGFNVRAAHDGEQGLAALLEGS---PDLVVLDVMLPKMNGLDVLKELRKT------SQVP 71
                           90       100       110
                   ....*....|....*....|....*....|....
gi 1889623460  974 IIAMTASAMAGDRERCITAGMNDYITKPIKPKVL 1007
Cdd:cd17623     72 VLMLTARGDDIDRILGLELGADDYLPKPFNPREL 105
COG4192 COG4192
Signal transduction histidine kinase regulating phosphoglycerate transport system [Signal ...
471-726 4.13e-12

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


Pssm-ID: 443346 [Multi-domain]  Cd Length: 640  Bit Score: 70.10  E-value: 4.13e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  471 NSLKQTQVELEKLNSTLEQKVRQRtteleSAIEQALAASKSK----------SDFIANISHEIRTP---MNGVLGMLEML 537
Cdd:COG4192    387 RLLRVFRDQAIEKTQELETEIEER-----KRIEKNLRQTQDEliqaakmavvGQTMTSLAHELNQPlnaMSMYLFSAKKA 461
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  538 KEDTLTQQQQQYLELANSSANSLMTLINDILDFSKieagKLDIDNHSFDVITVCSDMITSMALQAQRKGLEVFLHTDKVI 617
Cdd:COG4192    462 LEQENYAQLPTSLDKIEGLIERMDKIIKSLRQFSR----KSDTPLQPVDLRQVIEQAWELVESRAKPQQITLHIPDDLMV 537
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  618 drmlVGDSHRLKQILINLLNNAFK-FTHQGEVSLTLgcqYLTEEKLLMSfvIEDSGIGIAEknIDKLFEAFTqedtsTTR 696
Cdd:COG4192    538 ----QGDQVLLEQVLVNLLVNALDaVATQPQISVDL---LSNAENLRVA--ISDNGNGWPL--VDKLFTPFT-----TTK 601
                          250       260       270
                   ....*....|....*....|....*....|..
gi 1889623460  697 HFGgTGLGLSICRKLAQLMGGDISV--TSEKG 726
Cdd:COG4192    602 EVG-LGLGLSICRSIMQQFGGDLYLasTLERG 632
REC_typeA_ARR cd17581
phosphoacceptor receiver (REC) domain of type A Arabidopsis response regulators (ARRs) and ...
894-1005 4.61e-12

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: 63.92  E-value: 4.61e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  894 VLLVDDNMINLEVAKAILKNTGVTIVCASDGLDALEILNTEQTALF--------DLILMDCQMPNLNGYDTTSAIrsnKA 965
Cdd:cd17581      1 VLAVDDSLVDRKVIERLLRISSCRVTAVDSGKRALEFLGLEDEEDSsnfnepkvNMIITDYCMPGMTGYDLLKKV---KE 77
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1889623460  966 GADYAKVPIIAMTASAMAGDRERCITAGMNDYITKPIKPK 1005
Cdd:cd17581     78 SSALKEIPVVIMSSENIPTRISRCLEEGAEDFLLKPVKLA 117
PRK10610 PRK10610
chemotaxis protein CheY;
891-1011 6.40e-12

chemotaxis protein CheY;


Pssm-ID: 170568 [Multi-domain]  Cd Length: 129  Bit Score: 63.84  E-value: 6.40e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  891 NFKVLLVDDNMINLEVAKAILKNTGVTIVC-ASDGLDALeilNTEQTALFDLILMDCQMPNLNGYDTTSAIRSNKAgadY 969
Cdd:PRK10610     5 ELKFLVVDDFSTMRRIVRNLLKELGFNNVEeAEDGVDAL---NKLQAGGFGFVISDWNMPNMDGLELLKTIRADGA---M 78
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1889623460  970 AKVPIIAMTASAMAGDRERCITAGMNDYITKPIKPKVLKDKL 1011
Cdd:PRK10610    79 SALPVLMVTAEAKKENIIAAAQAGASGYVVKPFTAATLEEKL 120
REC_OmpR_YycF-like cd17614
phosphoacceptor receiver (REC) domain of YrcF-like OmpR family response regulators; YycF ...
894-1001 7.22e-12

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: 63.21  E-value: 7.22e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  894 VLLVDDNMINLEVAKAILKNTGVTIVCASDGLDALEILNTEQTalfDLILMDCQMPNLNGYDTTSAIRSNKagadyaKVP 973
Cdd:cd17614      1 ILVVDDEKPISDILKFNLTKEGYEVVTAYDGREALEKVEEEQP---DLILLDLMLPEKDGLEVCREVRKTS------NVP 71
                           90       100
                   ....*....|....*....|....*...
gi 1889623460  974 IIAMTASAMAGDRERCITAGMNDYITKP 1001
Cdd:cd17614     72 IIMLTAKDSEVDKVLGLELGADDYVTKP 99
PRK10755 PRK10755
two-component system sensor histidine kinase PmrB;
454-717 1.07e-11

two-component system sensor histidine kinase PmrB;


Pssm-ID: 236751 [Multi-domain]  Cd Length: 356  Bit Score: 67.69  E-value: 1.07e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  454 FDIFTQRHQVAAILRNINSLkqtqveLEKLNSTLEQKvRQrttelesaieqalaasksksdFIANISHEIRTPMNGVLGM 533
Cdd:PRK10755   107 IAIHSSTLEIEAVTSALNQL------VSRLTSTLDQE-RL---------------------FTADVAHELRTPLAGIRLH 158
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  534 LEMLKEDTLTQQQQQYLELanssaNSLMTLINDILDFSKIE----AG---KLDIDNhsfDVITVCSDMITSMaLQAQRKG 606
Cdd:PRK10755   159 LELLEKQHHIDVAPLIARL-----DQMMHTVEQLLQLARAGqsfsSGhyqTVKLLE---DVILPSQDELSEM-LEQRQQT 229
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  607 LEVFLHTDkviDRMLVGDSHRLKQILINLLNNAFKFTHQG-EVSLTLGCQyltEEKLLMSfvIEDSGIGIAEKNIDKLFE 685
Cdd:PRK10755   230 LLLPESAA---DITVQGDATLLRLLLRNLVENAHRYSPEGsTITIKLSQE---DGGAVLA--VEDEGPGIDESKCGELSK 301
                          250       260       270
                   ....*....|....*....|....*....|..
gi 1889623460  686 AFTQEDTsttrHFGGTGLGLSICRKLAQLMGG 717
Cdd:PRK10755   302 AFVRMDS----RYGGIGLGLSIVSRITQLHHG 329
REC_OmpR_DrrD-like cd17625
phosphoacceptor receiver (REC) domain of DrrD-like OmpR family response regulators; DrrD is a ...
895-1001 1.10e-11

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: 62.62  E-value: 1.10e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  895 LLVDDNMINLEVAKAILKNTGVTIVCASDGLDALEILNTEQtalFDLILMDCQMPNLNGYDTTSAIRSNKAgadyaKVPI 974
Cdd:cd17625      1 LVVEDEKDLSEAITKHLKKEGYTVDVCFDGEEGLEYALSGI---YDLIILDIMLPGMDGLEVLKSLREEGI-----ETPV 72
                           90       100
                   ....*....|....*....|....*..
gi 1889623460  975 IAMTASAMAGDRERCITAGMNDYITKP 1001
Cdd:cd17625     73 LLLTALDAVEDRVKGLDLGADDYLPKP 99
PRK11361 PRK11361
acetoacetate metabolism transcriptional regulator AtoC;
893-1001 1.25e-11

acetoacetate metabolism transcriptional regulator AtoC;


Pssm-ID: 183099 [Multi-domain]  Cd Length: 457  Bit Score: 67.95  E-value: 1.25e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  893 KVLLVDDNMINLEVAKAILKNTGVTIVCASDGLDALEILNTEQTalfDLILMDCQMPNLNGYDTTSAIRSNKAGAdyakv 972
Cdd:PRK11361     6 RILIVDDEDNVRRMLSTAFALQGFETHCANNGRTALHLFADIHP---DVVLMDIRMPEMDGIKALKEMRSHETRT----- 77
                           90       100
                   ....*....|....*....|....*....
gi 1889623460  973 PIIAMTASAMAGDRERCITAGMNDYITKP 1001
Cdd:PRK11361    78 PVILMTAYAEVETAVEALRCGAFDYVIKP 106
psREC_PRR cd17582
pseudo receiver domain of pseudo-response regulators; In Arabidopsis, five pseudo-response ...
894-1001 1.28e-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: 62.03  E-value: 1.28e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  894 VLLVDDNMINLEVAKAILKNTGVTIVCASDGLDALEILNTEQTALfDLILMDCQMPNLNGYDTTSAIRSNKAGADyakVP 973
Cdd:cd17582      1 VLLVENDDSTRQIVTALLRKCSYEVTAASDGLQAWDVLEDEQNEI-DLILTEVDLPVSSGFKLLSYIMRHKICKN---IP 76
                           90       100
                   ....*....|....*....|....*...
gi 1889623460  974 IIAMTASAMAGDRERCITAGMNDYITKP 1001
Cdd:cd17582     77 VIMMSSQDSVGVVFKCLSKGAADYLVKP 104
pleD PRK09581
response regulator PleD; Reviewed
893-1007 1.39e-11

response regulator PleD; Reviewed


Pssm-ID: 236577 [Multi-domain]  Cd Length: 457  Bit Score: 68.00  E-value: 1.39e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  893 KVLLVDDNMINLEVAKAILKNTGVTIVCASDGLDALEILNTEQTalfDLILMDCQMPNLNGYDTTSAIRSNKAgadYAKV 972
Cdd:PRK09581     4 RILVVDDIPANVKLLEAKLLAEYYTVLTASSGAEAIAICEREQP---DIILLDVMMPGMDGFEVCRRLKSDPA---TTHI 77
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1889623460  973 PIIAMTASAMAGDRERCITAGMNDYITKPIKPKVL 1007
Cdd:PRK09581    78 PVVMVTALDDPEDRVRGLEAGADDFLTKPINDVAL 112
HATPase_DpiB-CitA-like cd16915
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
631-735 1.87e-11

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: 61.53  E-value: 1.87e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  631 ILINLLNNAFK-FTHQGEVSLTLGCqYLTEEKLLMSFVIEDSGIGIAEKNIDKLFEAftqedTSTTRHFGGTGLGLSICR 709
Cdd:cd16915      4 IVGNLIDNALDaLAATGAPNKQVEV-FLRDEGDDLVIEVRDTGPGIAPELRDKVFER-----GVSTKGQGERGIGLALVR 77
                           90       100
                   ....*....|....*....|....*.
gi 1889623460  710 KLAQLMGGDISVTSEKGQGSCFTAQV 735
Cdd:cd16915     78 QSVERLGGSITVESEPGGGTTFSIRI 103
REC_PdtaR-like cd19932
phosphoacceptor receiver (REC) domain of PdtaR and similar proteins; This subfamily includes ...
893-1007 2.22e-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: 62.05  E-value: 2.22e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  893 KVLLVDDN-MINLEVaKAILKNTGVTIVC-ASDGLDALEILNTEQTalfDLILMDCQMPNLNGYDTTSAIRSNKAGadya 970
Cdd:cd19932      2 RVLIAEDEaLIRMDL-REMLEEAGYEVVGeASDGEEAVELAKKHKP---DLVIMDVKMPRLDGIEAAKIITSENIA---- 73
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1889623460  971 kvPIIAMTASAMAGDRERCITAGMNDYITKPIKPKVL 1007
Cdd:cd19932     74 --PIVLLTAYSQQDLVERAKEAGAMAYLVKPFSESDL 108
cpxA PRK09470
envelope stress sensor histidine kinase CpxA;
497-707 3.75e-11

envelope stress sensor histidine kinase CpxA;


Pssm-ID: 236532 [Multi-domain]  Cd Length: 461  Bit Score: 66.49  E-value: 3.75e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  497 ELESAIEQALAASKS--------------KSDFIANISHEIRTPmngvLGMLEM---LkedtLTQQQQQYLELA--NSSA 557
Cdd:PRK09470   214 ELETGPQEFRQAGASfnqmvtalermmtsQQRLLSDISHELRTP----LTRLQLataL----LRRRQGESKELEriETEA 285
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  558 NSLMTLINDILDFSKIEAgKLDIDNHSFDVITVCSDMITSMALQA-QR-KGLEVFLHTDKvidRMLVGDSHRLKQILINL 635
Cdd:PRK09470   286 QRLDSMINDLLVLSRNQQ-KNHLERETFKANSLWSEVLEDAKFEAeQMgKSLTVSAPPGP---WPINGNPNALASALENI 361
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1889623460  636 LNNAFKFTHQG-EVSLTLGCQYLTeekllmsFVIEDSGIGIAEKNIDKLFEAFTQEDTSTTRHFGGTGLGLSI 707
Cdd:PRK09470   362 VRNALRYSHTKiEVAFSVDKDGLT-------ITVDDDGPGVPEEEREQIFRPFYRVDEARDRESGGTGLGLAI 427
envZ PRK09467
osmolarity sensor protein; Provisional
628-726 4.37e-11

osmolarity sensor protein; Provisional


Pssm-ID: 236531 [Multi-domain]  Cd Length: 435  Bit Score: 66.09  E-value: 4.37e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  628 LKQILINLLNNAFKFTHqGEVSLTLGcqylTEEKLLMsFVIEDSGIGIAEKNIDKLFEAFTQEDTSttRHFGGTGLGLSI 707
Cdd:PRK09467   332 IKRALANLVVNAARYGN-GWIKVSSG----TEGKRAW-FQVEDDGPGIPPEQLKHLFQPFTRGDSA--RGSSGTGLGLAI 403
                           90       100
                   ....*....|....*....|
gi 1889623460  708 CRKLAQLMGGDISVT-SEKG 726
Cdd:PRK09467   404 VKRIVDQHNGKVELGnSEEG 423
REC_RssB-like cd17555
phosphoacceptor receiver (REC) domain of Pseudomonas aeruginosa RssB and similar domains; ...
893-1003 5.06e-11

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: 60.68  E-value: 5.06e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  893 KVLLVDDNMINLEVAKAILKNTGVTIVCASDGLDALEILNTEQtalFDLILMDCQMPNLNGYDTTSAIRsnkagADYAKV 972
Cdd:cd17555      2 TILVIDDDEVVRESIAAYLEDSGFQVLQAADGRQGLELFRSEQ---PDLVLCDLRMPEMDGLEVLKQIT-----KESPDT 73
                           90       100       110
                   ....*....|....*....|....*....|.
gi 1889623460  973 PIIAMTASAMAGDRERCITAGMNDYITKPIK 1003
Cdd:cd17555     74 PVIVVSGAGVMSDAVEALRLGAWDYLTKPIE 104
HATPase_EcPhoR-like cd16952
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
628-732 5.64e-11

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: 60.29  E-value: 5.64e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  628 LKQILINLLNNAFKFTHQGEvslTLGCQYLTEEKLlMSFVIEDSGIGIAEKNIDKLFEAFTQEDTSTTRHFGGTGLGLSI 707
Cdd:cd16952      1 LRSAFSNLVSNAVKYTPPSD---TITVRWSQEESG-ARLSVEDTGPGIPPEHIPRLTERFYRVDIERCRNTGGTGLGLAI 76
                           90       100
                   ....*....|....*....|....*
gi 1889623460  708 CRKLAQLMGGDISVTSEKGQGSCFT 732
Cdd:cd16952     77 VKHVMSRHDARLLIASELGKGSRFT 101
PRK09835 PRK09835
Cu(+)/Ag(+) sensor histidine kinase;
512-724 6.06e-11

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


Pssm-ID: 182101 [Multi-domain]  Cd Length: 482  Bit Score: 65.95  E-value: 6.06e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  512 KSDFIANISHEIRTPMNGVLGMLEMLKEDTLTQQQQQYLELANSSANSLMT-LINDILDFSKIEAGKLDIDNHSFD---- 586
Cdd:PRK09835   262 QSNFSADIAHEIRTPITNLITQTEIALSQSRSQKELEDVLYSNLEELTRMAkMVSDMLFLAQADNNQLIPEKKMLDlade 341
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  587 VITVcSDMITSMALQAQrkgleVFLHTDKviDRMLV-GDSHRLKQILINLLNNAFKFTHQGEvSLTLGCQyltEEKLLMS 665
Cdd:PRK09835   342 VGKV-FDFFEAWAEERG-----VELRFVG--DPCQVaGDPLMLRRAISNLLSNALRYTPAGE-AITVRCQ---EVDHQVQ 409
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1889623460  666 FVIEDSGIGIAEKNIDKLFEAFTQEDTSTTRHFGGTGLGLSICRKLAQLMGGDISVTSE 724
Cdd:PRK09835   410 LVVENPGTPIAPEHLPRLFDRFYRVDPSRQRKGEGSGIGLAIVKSIVVAHKGTVAVTSD 468
REC_OmpR_ArcA_TorR-like cd17619
phosphoacceptor receiver (REC) domain of ArcA- and TorR-like OmpR family response regulators; ...
894-1007 6.76e-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: 60.48  E-value: 6.76e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  894 VLLVDDNMINLEVAKAILKNTGVTIVCASDGLDALEILNTEQTalfDLILMDCQMPNLNGYDTTSAIRSNkagadyAKVP 973
Cdd:cd17619      3 ILIVEDEPVTRATLKSYFEQEGYDVSEAGDGEEMRQILARQDI---DLVLLDINLPGKDGLSLTRELREQ------SEVG 73
                           90       100       110
                   ....*....|....*....|....*....|....
gi 1889623460  974 IIAMTASAMAGDRERCITAGMNDYITKPIKPKVL 1007
Cdd:cd17619     74 IILVTGRDDEVDRIVGLEIGADDYVTKPFNPREL 107
REC_OmpR_BfmR-like cd19939
phosphoacceptor receiver (REC) domain of BfmR-like OmpR family response regulators; ...
893-1007 9.67e-11

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: 60.08  E-value: 9.67e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  893 KVLLVDDNMINLEVAKAILKNTGVTIVCASDGLDALEILNTEQTalfDLILMDCQMPNLNGYDTTSAIRSnkagadYAKV 972
Cdd:cd19939      1 RILIVEDELELARLTRDYLIKAGLEVSVFTDGQRAVRRIIDEQP---SLVVLDIMLPGMDGLTVCREVRE------HSHV 71
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1889623460  973 PIIAMTASAMAGDRERCITAGMNDYITKPIKPKVL 1007
Cdd:cd19939     72 PILMLTARTEEMDRVLGLEMGADDYLCKPFSPREL 106
REC_OmpR_PmrA-like cd17624
phosphoacceptor receiver (REC) domain of PmrA-like OmpR family response regulators; This ...
894-1007 9.85e-11

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


Pssm-ID: 381139 [Multi-domain]  Cd Length: 115  Bit Score: 59.81  E-value: 9.85e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  894 VLLVDDNMINLEVAKAILKNTGVTIVCASDGLDALEILNTEQtalFDLILMDCQMPNLNGYDTTSAIRSNKAgadyaKVP 973
Cdd:cd17624      1 ILLVEDDALLGDGLKTGLRKAGYAVDWVRTGAEAEAALASGP---YDLVILDLGLPDGDGLDLLRRWRRQGQ-----SLP 72
                           90       100       110
                   ....*....|....*....|....*....|....
gi 1889623460  974 IIAMTASAMAGDRERCITAGMNDYITKPIKPKVL 1007
Cdd:cd17624     73 VLILTARDGVDDRVAGLDAGADDYLVKPFALEEL 106
marine_sort_HK TIGR03785
proteobacterial dedicated sortase system histidine kinase; This histidine kinase protein is ...
515-732 1.04e-10

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: 65.92  E-value: 1.04e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  515 FIANISHEIRTPMNGVLGMLEMLKEDTLTQQQQQYLELANSSANSLMTLINDILDFSKIEAGKLDIDNHSFDVITVCSDM 594
Cdd:TIGR03785  488 MSSRLSHELRTPVAVVRSSLENLELQALEQEKQKYLERAREGTERLSMILNNMSEATRLEQAIQSAEVEDFDLSEVLSGC 567
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  595 ITS--MALQAQRKGLEVflhtdKVIDRMLVGDSHRLKQILINLLNNAFKFTHQG---EVSLtlgcqYLTEEKLLMSfvIE 669
Cdd:TIGR03785  568 MQGyqMTYPPQRFELNI-----PETPLVMRGSPELIAQMLDKLVDNAREFSPEDgliEVGL-----SQNKSHALLT--VS 635
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1889623460  670 DSGIGIAEKNIDKLFEAFTQEDTSTTRHFGGTGLGLSICRKLAQLMGGDISV-TSEKGQGSCFT 732
Cdd:TIGR03785  636 NEGPPLPEDMGEQLFDSMVSVRDQGAQDQPHLGLGLYIVRLIADFHQGRIQAeNRQQNDGVVFR 699
REC_2_GGDEF cd17544
second phosphoacceptor receiver (REC) domain of uncharacterized GGDEF domain proteins; This ...
893-1001 1.05e-10

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: 59.84  E-value: 1.05e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  893 KVLLVDDNMINLEVAKAILKNTGVTIVCASDGLDALEILntEQTALFDLILMDCQMPNLNGYDTTSAIRSNkagadYAK- 971
Cdd:cd17544      2 KVLVVDDSATSRNHLRALLRRHNFQVLEAANGQEALEVL--EQHPDIKLVITDYNMPEMDGFELVREIRKK-----YSRd 74
                           90       100       110
                   ....*....|....*....|....*....|.
gi 1889623460  972 -VPIIAMTASAMAGDRERCITAGMNDYITKP 1001
Cdd:cd17544     75 qLAIIGISASGDNALSARFIKAGANDFLTKP 105
HATPase_CpxA-like cd16949
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
628-732 1.24e-10

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: 59.26  E-value: 1.24e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  628 LKQILINLLNNAFKFTHQgEVSLTLGcqyltEEKLLMSFVIEDSGIGIAEKNIDKLFEAFTQEDTSTTRHFGGTGLGLSI 707
Cdd:cd16949      1 LARALENVLRNALRYSPS-KILLDIS-----QDGDQWTITITDDGPGVPEDQLEQIFLPFYRVDSARDRESGGTGLGLAI 74
                           90       100
                   ....*....|....*....|....*
gi 1889623460  708 CRKLAQLMGGDISVTSEKGQGSCFT 732
Cdd:cd16949     75 AERAIEQHGGKIKASNRKPGGLRVR 99
PLN03029 PLN03029
type-a response regulator protein; Provisional
890-1010 1.27e-10

type-a response regulator protein; Provisional


Pssm-ID: 215544 [Multi-domain]  Cd Length: 222  Bit Score: 62.36  E-value: 1.27e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  890 SNFKVLLVDDNMINLEVAKAILKNTGVTIVCASDGLDALEIL-----------------NTEQTALFDLILMDCQMPNLN 952
Cdd:PLN03029     7 SQFHVLAVDDSLIDRKLIEKLLKTSSYQVTTVDSGSKALKFLglheddrsnpdtpsvspNSHQEVEVNLIITDYCMPGMT 86
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1889623460  953 GYDTTSAIrsnKAGADYAKVPIIAMTASAMAGDRERCITAGMNDYITKPI--------KPKVLKDK 1010
Cdd:PLN03029    87 GYDLLKKI---KESSSLRNIPVVIMSSENVPSRITRCLEEGAEEFFLKPVqlsdlnrlKPHMMKTK 149
REC_YesN-like cd17536
phosphoacceptor receiver (REC) domain of YesN and related helix-turn-helix containing response ...
894-1011 1.95e-10

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


Pssm-ID: 381091 [Multi-domain]  Cd Length: 121  Bit Score: 59.27  E-value: 1.95e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  894 VLLVDDNMINLEVAKAIL--KNTGVTIVC-ASDGLDALEILNTEQtalFDLILMDCQMPNLNGYDTTSAIRSNkagadYA 970
Cdd:cd17536      1 VLIVDDEPLIREGLKKLIdwEELGFEVVGeAENGEEALELIEEHK---PDIVITDIRMPGMDGLELIEKIREL-----YP 72
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 1889623460  971 KVPIIAMTASAmagDRE---RCITAGMNDYITKPIKPKVLKDKL 1011
Cdd:cd17536     73 DIKIIILSGYD---DFEyaqKAIRLGVVDYLLKPVDEEELEEAL 113
HATPase_Phy-like cd16932
Histidine kinase-like ATPase domain of plant phytochromes similar to Arabidopsis thaliana ...
623-737 2.47e-10

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


Pssm-ID: 340409 [Multi-domain]  Cd Length: 113  Bit Score: 58.82  E-value: 2.47e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  623 GDSHRLKQILINLLNNAFKFT--HQG--EVSLTLGCQYLTEEKLLMS--FVIEDSGIGIAEKNIDKLFEaftqEDTSTTR 696
Cdd:cd16932      2 GDQIRLQQVLADFLLNAVRFTpsPGGwvEIKVSPTKKQIGDGVHVIHleFRITHPGQGLPEELVQEMFE----ENQWTTQ 77
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 1889623460  697 HfggtGLGLSICRKLAQLMGGDISVTSEKGQgSCFTAQVQL 737
Cdd:cd16932     78 E----GLGLSISRKLVKLMNGDVRYLREAGR-SYFLITLEL 113
PRK11517 PRK11517
DNA-binding response regulator HprR;
893-1001 2.48e-10

DNA-binding response regulator HprR;


Pssm-ID: 183172 [Multi-domain]  Cd Length: 223  Bit Score: 61.45  E-value: 2.48e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  893 KVLLVDDNMINLEVAKAILKNTGVTIVCASDGLDALEILNTEQTALfdlILMDCQMPNLNGYDTTSAIRSNKAgadyakV 972
Cdd:PRK11517     2 KILLIEDNQRTQEWVTQGLSEAGYVIDAVSDGRDGLYLALKDDYAL---IILDIMLPGMDGWQILQTLRTAKQ------T 72
                           90       100
                   ....*....|....*....|....*....
gi 1889623460  973 PIIAMTASAMAGDRERCITAGMNDYITKP 1001
Cdd:PRK11517    73 PVICLTARDSVDDRVRGLDSGANDYLVKP 101
REC_DC-like cd17534
phosphoacceptor receiver (REC) domain of modulated diguanylate cyclase and similar domains; ...
893-1008 2.83e-10

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: 58.57  E-value: 2.83e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  893 KVLLVDDNMINLEVAKAILKNTGVTIV-CASDGLDALEILNTEQTalfDLILMDCQMP-NLNGYDTTSAIRSNKagadya 970
Cdd:cd17534      2 KILIVEDEAIIALDLKEILESLGYEVVgIADSGEEAIELAEENKP---DLILMDINLKgDMDGIEAAREIREKF------ 72
                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1889623460  971 KVPIIAMTASAMAGDRERCITAGMNDYITKPIKPKVLK 1008
Cdd:cd17534     73 DIPVIFLTAYSDEETLERAKETNPYGYLVKPFNERELK 110
REC_OmpR_MtPhoP-like cd17615
phosphoacceptor receiver (REC) domain of MtPhoP-like OmpR family response regulators; ...
893-1001 2.94e-10

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: 58.52  E-value: 2.94e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  893 KVLLVDDNMINLEVAKAILKNTGVTIVCASDGLDALEIlnTEQTALfDLILMDCQMPNLNGYDTTSAIRsnkagADYAKV 972
Cdd:cd17615      1 RVLVVDDEPNITELLSMALRYEGWDVETAADGAEALAA--AREFRP-DAVVLDIMLPDMDGLEVLRRLR-----ADGPDV 72
                           90       100
                   ....*....|....*....|....*....
gi 1889623460  973 PIIAMTASAMAGDRERCITAGMNDYITKP 1001
Cdd:cd17615     73 PVLFLTAKDSVEDRIAGLTAGGDDYVTKP 101
HATPase_BceS-YxdK-YvcQ-like cd16948
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
624-732 3.19e-10

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: 58.07  E-value: 3.19e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  624 DSHRLKQILINLLNNAFKFTHQGEvSLTLGCQYLTEEKLLmsfVIEDSGIGIAEKNIDKLFEA-FTQEdtsTTRHFG-GT 701
Cdd:cd16948      2 DAKWLSFIIGQIVSNALKYSKQGG-KIEIYSETNEQGVVL---SIKDFGIGIPEEDLPRVFDKgFTGE---NGRNFQeST 74
                           90       100       110
                   ....*....|....*....|....*....|.
gi 1889623460  702 GLGLSICRKLAQLMGGDISVTSEKGQGSCFT 732
Cdd:cd16948     75 GMGLYLVKKLCDKLGHKIDVESEVGEGTTFT 105
REC_CheB-like cd17541
phosphoacceptor receiver (REC) domain of chemotaxis response regulator protein-glutamate ...
893-1001 4.12e-10

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: 58.56  E-value: 4.12e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  893 KVLLVDDNMINLEVAKAIL-KNTGVTIV-CASDGLDALEILNTEQtalFDLILMDCQMPNLNGYDTTSAIRSNKagadya 970
Cdd:cd17541      2 RVLIVDDSAVMRKLLSRILeSDPDIEVVgTARDGEEALEKIKELK---PDVITLDIEMPVMDGLEALRRIMAER------ 72
                           90       100       110
                   ....*....|....*....|....*....|...
gi 1889623460  971 KVPIIAMTASAMAGDRE--RCITAGMNDYITKP 1001
Cdd:cd17541     73 PTPVVMVSSLTEEGAEItlEALELGAVDFIAKP 105
PRK10365 PRK10365
sigma-54-dependent response regulator transcription factor ZraR;
891-1011 4.86e-10

sigma-54-dependent response regulator transcription factor ZraR;


Pssm-ID: 182412 [Multi-domain]  Cd Length: 441  Bit Score: 63.13  E-value: 4.86e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  891 NFKVLLVDDNMINLEVAKAILKNTGVTIVCASDGLDALEILnteQTALFDLILMDCQMPNLNGYDTTSAIRS-NKAgady 969
Cdd:PRK10365     5 NIDILVVDDDISHCTILQALLRGWGYNVALANSGRQALEQV---REQVFDLVLCDVRMAEMDGIATLKEIKAlNPA---- 77
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1889623460  970 akVPIIAMTASAMAGDRERCITAGMNDYITKPIKPKVLKDKL 1011
Cdd:PRK10365    78 --IPVLIMTAYSSVETAVEALKTGALDYLIKPLDFDNLQATL 117
REC_TrrA-like cd17554
phosphoacceptor receiver (REC) domain of Thermotoga maritima response regulator TrrA and ...
893-979 5.55e-10

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: 57.62  E-value: 5.55e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  893 KVLLVDDNMINLEVAKAILKNTGVTIVCASDGLDALEILnteQTALFDLILMDCQMPNLNGYDTTSAIRSNKagadyAKV 972
Cdd:cd17554      2 KILVVDDEENIRELYKEELEDEGYEVVTAGNGEEALEKL---ESEDPDLVILDIKMPGMDGLETLRKIREKK-----PDL 73

                   ....*..
gi 1889623460  973 PIIAMTA 979
Cdd:cd17554     74 PVIICTA 80
REC_hyHK cd17598
phosphoacceptor receiver (REC) domain of uncharacterized hybrid sensor histidine kinase ...
894-1007 5.80e-10

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: 57.72  E-value: 5.80e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  894 VLLVDDNMINLEVAKAILKNTGVTIVCASDGLDALEILNTEQTALfdlILMDCQMPNLNGYDTTSAIRSNKagaDYAKVP 973
Cdd:cd17598      1 ILIVEDSPTQAEQLKHILEEQGYKVQVARNGREALAMLAEHRPTL---VISDIVMPEMDGYELCRKIKSDP---DLKDIP 74
                           90       100       110
                   ....*....|....*....|....*....|....
gi 1889623460  974 IIAMTASAMAGDRERCITAGMNDYITKPIKPKVL 1007
Cdd:cd17598     75 VILLTTLSDPRDVIRGLECGADNFITKPYDEKYL 108
LytT COG3279
DNA-binding response regulator, LytR/AlgR family [Transcription, Signal transduction ...
893-1011 7.31e-10

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


Pssm-ID: 442510 [Multi-domain]  Cd Length: 235  Bit Score: 60.22  E-value: 7.31e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  893 KVLLVDDNMINLEVAKAILKNT-GVTIV-CASDGLDALEILNTEQtalFDLILMDCQMPNLNGYDTTSAIRSNKagadyA 970
Cdd:COG3279      3 KILIVDDEPLARERLERLLEKYpDLEVVgEASNGEEALELLEEHK---PDLVFLDIQMPGLDGFELARQLRELD-----P 74
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 1889623460  971 KVPIIAMTAS---AMAGDRERCItagmnDYITKPIKPKVLKDKL 1011
Cdd:COG3279     75 PPPIIFTTAYdeyALEAFEVNAV-----DYLLKPIDEERLAKAL 113
HATPase_CreC-like cd16945
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
628-721 1.03e-09

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: 56.70  E-value: 1.03e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  628 LKQILINLLNNAFKFTHQGEVsLTLGCQYLTEEKLLMsfvIEDSGIGIAEKNIDKLFEAFTqedtSTTRHFGG---TGLG 704
Cdd:cd16945      5 LRQAINNLLDNAIDFSPEGGL-IALQLEADTEGIELL---VFDEGSGIPDYALNRVFERFY----SLPRPHSGqksTGLG 76
                           90
                   ....*....|....*..
gi 1889623460  705 LSICRKLAQLMGGDISV 721
Cdd:cd16945     77 LAFVQEVAQLHGGRITL 93
REC_HupR-like cd17569
phosphoacceptor receiver (REC) domain of hydrogen uptake protein regulator (HupR) and similar ...
892-1011 4.86e-09

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: 55.10  E-value: 4.86e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  892 FKVLLVDDNMINLEVAKAILKNTGVTIVCASDGLDALEILNTEQtalFDLILMDCQMPNLNGYDTTSAIRsnkagADYAK 971
Cdd:cd17569      1 PTILLVDDEPNILKALKRLLRREGYEVLTATSGEEALEILKQEP---VDVVISDQRMPGMDGAELLKRVR-----ERYPD 72
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 1889623460  972 VPIIAMTASAmagDRERCITAgMND-----YITKPIKPKVLKDKL 1011
Cdd:cd17569     73 TVRILLTGYA---DLDAAIEA-INEgeiyrFLTKPWDDEELKETI 113
PRK15479 PRK15479
transcriptional regulator TctD;
893-1001 4.96e-09

transcriptional regulator TctD;


Pssm-ID: 185376 [Multi-domain]  Cd Length: 221  Bit Score: 57.81  E-value: 4.96e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  893 KVLLVDDNMINLEVAKAILKNTGVTIVCASDGLDALEILNTEQTALfdlILMDCQMPNLNGYDTTSAIRsnKAGADyakV 972
Cdd:PRK15479     2 RLLLAEDNRELAHWLEKALVQNGFAVDCVFDGLAADHLLQSEMYAL---AVLDINMPGMDGLEVLQRLR--KRGQT---L 73
                           90       100
                   ....*....|....*....|....*....
gi 1889623460  973 PIIAMTASAMAGDRERCITAGMNDYITKP 1001
Cdd:PRK15479    74 PVLLLTARSAVADRVKGLNVGADDYLPKP 102
REC_OmpR_kpRstA-like cd17622
phosphoacceptor receiver (REC) domain of kpRstA-like OmpR family response regulators; ...
893-1007 1.01e-08

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: 54.31  E-value: 1.01e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  893 KVLLVDDNMINLEVAKAILKNTGVTIVCASDGLDALEILNTEQTalfDLILMDCQMPNLNGYDTTSAIRsnkagaDYAKV 972
Cdd:cd17622      2 RILLVEDDPKLARLIADFLESHGFNVVVEHRGDRALEVIAREKP---DAVLLDIMLPGIDGLTLCRDLR------PKYQG 72
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1889623460  973 PIIAMTASAMAGDRERCITAGMNDYITKPIKPKVL 1007
Cdd:cd17622     73 PILLLTALDSDIDHILGLELGADDYVVKPVEPAVL 107
resp_reg_YycF NF040534
response regulator YycF;
893-1001 1.13e-08

response regulator YycF;


Pssm-ID: 439744 [Multi-domain]  Cd Length: 231  Bit Score: 56.65  E-value: 1.13e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  893 KVLLVDDNMINLEVAKAILKNTGVTIVCASDGLDALEILNTEQTalfDLILMDCQMPNLNGYDTTSAIRSNKagadyaKV 972
Cdd:NF040534     2 KILVVDDEKPIADILEFNLKKEGYEVFCAYDGNEALELVEEEVP---DLVLLDIMLPGRDGMEVCREVRKKY------DM 72
                           90       100
                   ....*....|....*....|....*....
gi 1889623460  973 PIIAMTASAMAGDRERCITAGMNDYITKP 1001
Cdd:NF040534    73 PIIMLTAKDSEIDKVLGLELGADDYVTKP 101
PRK10337 PRK10337
sensor protein QseC; Provisional
602-735 1.44e-08

sensor protein QseC; Provisional


Pssm-ID: 182388 [Multi-domain]  Cd Length: 449  Bit Score: 58.51  E-value: 1.44e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  602 AQRKGLEVFLH--TDKVIDRmlvGDSHRLKQILINLLNNAFKFTHQG-EVSLTLGCQYLTeekllmsfvIEDSGIGIAEK 678
Cdd:PRK10337   328 AQQAGIDVRLTlnAHPVIRT---GQPLLLSLLVRNLLDNAIRYSPQGsVVDVTLNARNFT---------VRDNGPGVTPE 395
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1889623460  679 NIDKLFEAF----TQEDTsttrhfgGTGLGLSICRKLAQLMGGDISVTSEKGQGscFTAQV 735
Cdd:PRK10337   396 ALARIGERFyrppGQEAT-------GSGLGLSIVRRIAKLHGMNVSFGNAPEGG--FEAKV 447
HATPase_BvrS-ChvG-like cd16953
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
628-735 1.82e-08

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


Pssm-ID: 340429 [Multi-domain]  Cd Length: 110  Bit Score: 53.35  E-value: 1.82e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  628 LKQILINLLNNAFKFT--HQGEVSLTLGcqyltEEKLLMSFVIEDSGIGIAEKNIDKLFEAFTQEDTSTTRHFGGTGLGL 705
Cdd:cd16953      1 LGQVLRNLIGNAISFSppDTGRITVSAM-----PTGKMVTISVEDEGPGIPQEKLESIFDRFYTERPANEAFGQHSGLGL 75
                           90       100       110
                   ....*....|....*....|....*....|....
gi 1889623460  706 SICRKLAQLMGGDISVT--SEKGQ--GSCFTAQV 735
Cdd:cd16953     76 SISRQIIEAHGGISVAEnhNQPGQviGARFTVQL 109
HATPase_Glnl-NtrB-like cd16918
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
628-726 3.01e-08

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: 52.79  E-value: 3.01e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  628 LKQILINLLNNAFKFT--HQGEVSLTLGCQY-----LTEEKLLMSFVIEDSGIGIAEKNIDKLFEAFTqedtsTTRHfGG 700
Cdd:cd16918      1 LIQVFLNLVRNAAQALagSGGEIILRTRTQRqvtlgHPRHRLALRVSVIDNGPGIPPDLQDTIFYPMV-----SGRE-NG 74
                           90       100
                   ....*....|....*....|....*.
gi 1889623460  701 TGLGLSICRKLAQLMGGDISVTSEKG 726
Cdd:cd16918     75 TGLGLAIAQNIVSQHGGVIECDSQPG 100
HATPase_ETR2_ERS2-EIN4-like cd16938
Histidine kinase-like ATPase domain of Arabidopsis thaliana ETR2, ERS2, and EIN4, and related ...
619-732 5.61e-08

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: 52.46  E-value: 5.61e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  619 RMLVGDSHRLKQILINLLNNAFKFTHQG-----EVSLTLGCQYLTEEKLLMS------------FVIEDSGIGiaEKNID 681
Cdd:cd16938      3 DVVVGDERRVFQVLLHMLGNLLKMRNGGgnitfRVFLEGGSEDRSDRDWGPWrpsmsdesveirFEVEINDSG--SPSIE 80
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1889623460  682 KLFEAFTQEDtsttRHFG---GTGLGLSICRKLAQLMGGDISVTSEKGQGSCFT 732
Cdd:cd16938     81 SASMRNSLNR----RYNLselGEHLSFSICKQLVQLMGGNIWIVPGSGLGTTMS 130
HATPase_NtrY-like cd16944
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
624-730 5.70e-08

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: 51.77  E-value: 5.70e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  624 DSHRLKQILINLLNNAFKFTH-----QGEVSLTLGcqylTEEKLLMSFVIEDSGIGIAEKNIDKLFEAFTqedtsTTRHf 698
Cdd:cd16944      1 DTTQISQVLTNILKNAAEAIEgrpsdVGEVRIRVE----ADQDGRIVLIVCDNGKGFPREMRHRATEPYV-----TTRP- 70
                           90       100       110
                   ....*....|....*....|....*....|..
gi 1889623460  699 GGTGLGLSICRKLAQLMGGDISVTSEKGQGSC 730
Cdd:cd16944     71 KGTGLGLAIVKKIMEEHGGRISLSNREAGGAC 102
REC_OmpR_NsrR-like cd18159
phosphoacceptor receiver (REC) domain of Streptococcus agalactiae NsrR-like OmpR family ...
894-1011 7.32e-08

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: 51.51  E-value: 7.32e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  894 VLLV-DDNMINLEVAKAiLKNTGVTIVCASDGLDALEILNTEQTalfDLILMDCQMPNLNGYDTTSAIRSnkagadYAKV 972
Cdd:cd18159      1 ILIVeDDETIASLLKKH-LEKWGYEVVLIEDFEDVLEEFLQFKP---DLVLLDINLPYFDGFYWCREIRQ------ISNV 70
                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1889623460  973 PIIAMTASAMAGDRERCITAGMNDYITKPIKPKVLKDKL 1011
Cdd:cd18159     71 PIIFISSRDDNMDQVMAINMGGDDYITKPFDLDVLLAKI 109
HATPase_VanS-like cd16923
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
628-724 8.28e-08

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: 51.23  E-value: 8.28e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  628 LKQILINLLNNAFKFT-HQGEVSLTLgcqYLTEEKLlmSFVIEDSGIGIAEKNIDKLFEAFTQEDTSttRHFGGTGLGLS 706
Cdd:cd16923      1 LQRVFSNLLSNAIKYSpENTRIYITS---FLTDDVV--NIMFKNPSSHPLDFKLEKLFERFYRGDNS--RNTEGAGLGLS 73
                           90
                   ....*....|....*...
gi 1889623460  707 ICRKLAQLMGGDISVTSE 724
Cdd:cd16923     74 IAKAIIELHGGSASAEYD 91
PRK10161 PRK10161
phosphate response regulator transcription factor PhoB;
893-1007 1.14e-07

phosphate response regulator transcription factor PhoB;


Pssm-ID: 182277 [Multi-domain]  Cd Length: 229  Bit Score: 53.95  E-value: 1.14e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  893 KVLLVDDNMINLEVAKAILKNTGVTIVCASDGLDALEILNTEQTalfDLILMDCQMPNLNGYDTTSAIRSNKAGADyakV 972
Cdd:PRK10161     4 RILVVEDEAPIREMVCFVLEQNGFQPVEAEDYDSAVNQLNEPWP---DLILLDWMLPGGSGIQFIKHLKRESMTRD---I 77
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1889623460  973 PIIAMTASAMAGDRERCITAGMNDYITKPIKPKVL 1007
Cdd:PRK10161    78 PVVMLTARGEEEDRVRGLETGADDYITKPFSPKEL 112
PRK11086 PRK11086
sensory histidine kinase DcuS; Provisional
626-735 1.15e-07

sensory histidine kinase DcuS; Provisional


Pssm-ID: 236839 [Multi-domain]  Cd Length: 542  Bit Score: 55.69  E-value: 1.15e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  626 HRLKQILINLLNNAF---KFTHQGEVSLTLgcQYLTEEkllMSFVIEDSGIGIAEKNIDKLFEaftqEDTSTTrhfG-GT 701
Cdd:PRK11086   432 HELITILGNLIENALeavGGEEGGEISVSL--HYRNGW---LHCEVSDDGPGIAPDEIDAIFD----KGYSTK---GsNR 499
                           90       100       110
                   ....*....|....*....|....*....|....
gi 1889623460  702 GLGLSICRKLAQLMGGDISVTSEKGQGSCFTAQV 735
Cdd:PRK11086   500 GVGLYLVKQSVENLGGSIAVESEPGVGTQFFVQI 533
REC_OmpR_KdpE-like cd17620
phosphoacceptor receiver (REC) domain of KdpE-like OmpR family response regulators; KdpE is a ...
894-1001 1.23e-07

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: 50.63  E-value: 1.23e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  894 VLLVDDNMINLEVAKAILKNTGVTIVCASDGLDALEILNTEQtalFDLILMDCQMPNLNGYDTTSAIRSnkagadYAKVP 973
Cdd:cd17620      1 ILVIEDEPQIRRFLRTALEAHGYRVFEAETGQEGLLEAATRK---PDLIILDLGLPDMDGLEVIRRLRE------WSAVP 71
                           90       100
                   ....*....|....*....|....*...
gi 1889623460  974 IIAMTASAMAGDRERCITAGMNDYITKP 1001
Cdd:cd17620     72 VIVLSARDEESDKIAALDAGADDYLTKP 99
HATPase_CckA-like cd16919
Histidine kinase-like ATPase domain of two-component sensor hybrid histidine kinases, similar ...
665-731 1.61e-07

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: 50.84  E-value: 1.61e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1889623460  665 SFVIEDSGIGIAEKNIDKLFEAFTqedtsTTRHFG-GTGLGLSICRKLAQLMGGDISVTSEKGQGSCF 731
Cdd:cd16919     49 CLEVSDTGSGMPAEVLRRAFEPFF-----TTKEVGkGTGLGLSMVYGFVKQSGGHLRIYSEPGVGTTV 111
REC_OmpR_RegX3-like cd17621
phosphoacceptor receiver (REC) domain of RegX3-like OmpR family response regulators; RegX3 is ...
894-1001 2.22e-07

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: 49.89  E-value: 2.22e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  894 VLLVDDNMINLEVAKAILKNTGVTIVCASDGLDALEILNTEQTalfDLILMDCQMPNLNGYDTTSAIRSNkagadyAKVP 973
Cdd:cd17621      1 VLVVEDEESFSDPLAYLLRKEGFEVTVATDGPAALAEFDRAGA---DIVLLDLMLPGLSGTEVCRQLRAR------SNVP 71
                           90       100
                   ....*....|....*....|....*...
gi 1889623460  974 IIAMTASAMAGDRERCITAGMNDYITKP 1001
Cdd:cd17621     72 VIMVTAKDSEIDKVVGLELGADDYVTKP 99
REC_OmpR_CtrA cd17616
phosphoacceptor receiver (REC) domain of CtrA-like OmpR family response regulators; CtrA is ...
894-1001 2.62e-07

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: 50.10  E-value: 2.62e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  894 VLLVDDNMinlEVAKAI---LKNTGVTIVCASDGLDALEIlntEQTALFDLILMDCQMPNLNGYDTTSAIRSNKagadyA 970
Cdd:cd17616      1 VLLIEDDS---ATAQSIelmLKSEGFNVYTTDLGEEGLDL---GKLYDYDIILLDLNLPDMSGYEVLRTLRLAK-----V 69
                           90       100       110
                   ....*....|....*....|....*....|.
gi 1889623460  971 KVPIIAMTASAMAGDRERCITAGMNDYITKP 1001
Cdd:cd17616     70 KTPILILSGLADIEDKVKGLGFGADDYMTKP 100
REC_OmpR_EcPhoP-like cd19934
phosphoacceptor receiver (REC) domain of EcPhoP-like OmpR family response regulators; ...
894-1007 3.52e-07

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


Pssm-ID: 381161 [Multi-domain]  Cd Length: 117  Bit Score: 49.97  E-value: 3.52e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  894 VLLVDDNMINLEVAKAILKNTGVTIVCASDGLDALEILNTEQtalFDLILMDCQMPNLNGYDTTSAIRSNKAgadyaKVP 973
Cdd:cd19934      1 LLLVEDDALLAAQLKEQLSDAGYVVDVAEDGEEALFQGEEEP---YDLVVLDLGLPGMDGLSVLRRWRSEGR-----ATP 72
                           90       100       110
                   ....*....|....*....|....*....|....
gi 1889623460  974 IIAMTASAMAGDRERCITAGMNDYITKPIKPKVL 1007
Cdd:cd19934     73 VLILTARDSWQDKVEGLDAGADDYLTKPFHIEEL 106
PRK09836 PRK09836
DNA-binding transcriptional activator CusR; Provisional
893-1001 4.01e-07

DNA-binding transcriptional activator CusR; Provisional


Pssm-ID: 182102 [Multi-domain]  Cd Length: 227  Bit Score: 52.23  E-value: 4.01e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  893 KVLLVDDNMINLEVAKAILKNTGVTIVCASDGLDALEIlntEQTALFDLILMDCQMPNLNGYDTTSAIRSNKAGadyakV 972
Cdd:PRK09836     2 KLLIVEDEKKTGEYLTKGLTEAGFVVDLADNGLNGYHL---AMTGDYDLIILDIMLPDVNGWDIVRMLRSANKG-----M 73
                           90       100
                   ....*....|....*....|....*....
gi 1889623460  973 PIIAMTASAMAGDRERCITAGMNDYITKP 1001
Cdd:PRK09836    74 PILLLTALGTIEHRVKGLELGADDYLVKP 102
CitB COG2197
DNA-binding response regulator, NarL/FixJ family, contains REC and HTH domains [Signal ...
893-960 4.06e-07

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


Pssm-ID: 441799 [Multi-domain]  Cd Length: 131  Bit Score: 49.89  E-value: 4.06e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  893 KVLLVDDNMINLEVAKAILKNT-GVTIV-CASDGLDALEILNTEQtalFDLILMDCQMPNLNGYDTTSAI 960
Cdd:COG2197      3 RVLIVDDHPLVREGLRALLEAEpDIEVVgEAADGEEALELLEELR---PDVVLLDIRMPGMDGLEALRRL 69
REC_NarL cd19931
phosphoacceptor receiver (REC) domain of Nitrate/Nitrite response regulator L (NarL); Nitrate ...
894-1011 7.37e-07

phosphoacceptor receiver (REC) domain of Nitrate/Nitrite response regulator L (NarL); Nitrate/nitrite response regulator protein NarL contains an N-terminal REC domain and a C-terminal LuxR family helix-turn-helix (HTH) DNA-binding output domain. Escherichia coli NarL activates the expression of the nitrate reductase (narGHJI) and formate dehydrogenase-N (fdnGHI) operons, and represses the transcription of the fumarate reductase (frdABCD) operon in response to a nitrate/nitrite induction signal. Phosphorylation of the NarL REC domain releases the C-terminal HTH output domain that subsequently binds specific DNA promoter sites to repress or activate gene expression. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381158 [Multi-domain]  Cd Length: 117  Bit Score: 48.88  E-value: 7.37e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  894 VLLVDDN-MINLEVAKAILKNTGVTIVC-ASDGLDALEILNTEQTalfDLILMDCQMPNLNGYDTTSAIRSNKAGADyak 971
Cdd:cd19931      1 VLLIDDHpLLRKGIKQLIELDPDFTVVGeASSGEEGIELAERLDP---DLILLDLNMKGMSGLDTLKALREEGVSAR--- 74
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1889623460  972 vpIIAMTASAMAGDRERCITAGMNDYITKPIKPKVLKDKL 1011
Cdd:cd19931     75 --IVILTVSDAEDDVVTALRAGADGYLLKDMEPEDLLEAL 112
REC_OmpR_BaeR-like cd19938
phosphoacceptor receiver (REC) domain of BaeR-like OmpR family response regulators; BaeR is ...
893-1005 9.19e-07

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: 48.53  E-value: 9.19e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  893 KVLLVDDNMINLEVAKAILKNTGVTIVCASDGLDALEILnteQTALFDLILMDCQMPNLNGYDTTSAIRsnkagaDYAKV 972
Cdd:cd19938      1 RILIVEDEPKLAQLLIDYLRAAGYAPTLLAHGDQVLPYV---RHTPPDLILLDLMLPGTDGLTLCREIR------RFSDV 71
                           90       100       110
                   ....*....|....*....|....*....|...
gi 1889623460  973 PIIAMTASAMAGDRERCITAGMNDYITKPIKPK 1005
Cdd:cd19938     72 PIIMVTARVEEIDRLLGLELGADDYICKPYSPR 104
REC_NtrX-like cd17550
phosphoacceptor receiver (REC) domain of nitrogen assimilation regulatory protein NtrX and ...
894-1003 9.78e-07

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: 48.65  E-value: 9.78e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  894 VLLVDDNMINLEVAKAILKNTGVTIVCASDGLDALEILNTEQtalFDLILMDCQMPNLNGYDTTSAIRsnkagADYAKVP 973
Cdd:cd17550      1 ILIVDDEEDIRESLSGILEDEGYEVDTAADGEEALKLIKERR---PDLVLLDIWLPDMDGLELLKEIK-----EKYPDLP 72
                           90       100       110
                   ....*....|....*....|....*....|...
gi 1889623460  974 IIAMTASamaGDRERCITA---GMNDYITKPIK 1003
Cdd:cd17550     73 VIMISGH---GTIETAVKAtklGAYDFIEKPLS 102
PRK11083 PRK11083
DNA-binding response regulator CreB; Provisional
893-1005 1.19e-06

DNA-binding response regulator CreB; Provisional


Pssm-ID: 236838 [Multi-domain]  Cd Length: 228  Bit Score: 50.73  E-value: 1.19e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  893 KVLLVDDnminlEVAKA-----ILKNTGVTIVCASDGLDALEILnteQTALFDLILMDCQMPNLNGYDTTSAIRSNkaga 967
Cdd:PRK11083     5 TILLVED-----EQAIAdtlvyALQSEGFTVEWFERGLPALDKL---RQQPPDLVILDVGLPDISGFELCRQLLAF---- 72
                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1889623460  968 dYAKVPIIAMTASAMAGDRERCITAGMNDYITKPIKPK 1005
Cdd:PRK11083    73 -HPALPVIFLTARSDEVDRLVGLEIGADDYVAKPFSPR 109
REC_citrate_TCS cd19925
phosphoacceptor receiver (REC) domain of citrate family two-component system response ...
893-1014 1.57e-06

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


Pssm-ID: 381152 [Multi-domain]  Cd Length: 118  Bit Score: 48.01  E-value: 1.57e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  893 KVLLVDDNMINLEVAKAILKNT-GVTIV-CASDGLDALEILNTEQTalfDLILMDCQMPNLNGYDTTSAIRSNKAGADya 970
Cdd:cd19925      2 NVLIVEDDPMVAEIHRAYVEQVpGFTVIgTAGTGEEALKLLKERQP---DLILLDIYLPDGNGLDLLRELRAAGHDVD-- 76
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 1889623460  971 kvpIIAMTASAMAGDRERCITAGMNDYITKPIKPKVLKDKLAMW 1014
Cdd:cd19925     77 ---VIVVTAANDVETVREALRLGVVDYLIKPFTFERLRQRLERY 117
glnL PRK11073
nitrogen regulation protein NR(II);
366-726 1.78e-06

nitrogen regulation protein NR(II);


Pssm-ID: 182947 [Multi-domain]  Cd Length: 348  Bit Score: 51.24  E-value: 1.78e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  366 NNKIIENSLDAILTVQEDGLISNANKTALQFFDII---IDHTKFTQLFTLAESDNSCIDETIAQGSkpSFegvyTDPQ-- 440
Cdd:PRK11073     9 AGQILNSLINSILLLDDDLAIHYANPAAQQLLAQSsrkLFGTPLPELLSYFSLNIELMRESLQAGQ--GF----TDNEvt 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  441 ----DQQHFYSITLTSVFDIFtqrhqvaaILrninslkqtqVELEKLNSTleqkvRQRTTELESAIEQALAaskskSDFI 516
Cdd:PRK11073    83 lvidGRSHILSLTAQRLPEGM--------IL----------LEMAPMDNQ-----RRLSQEQLQHAQQVAA-----RDLV 134
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  517 ANISHEIRTPMNGVLG---MLE-MLKEDTLTQqqqqYLELANSSANSLMTLINDILDFSKieAGKLDIDNHSFDVITVCS 592
Cdd:PRK11073   135 RGLAHEIKNPLGGLRGaaqLLSkALPDPALTE----YTKVIIEQADRLRNLVDRLLGPQR--PGTHVTESIHKVAERVVQ 208
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  593 dmITSMALQAQRK-------GLEVFLHtdkvidrmlvgDSHRLKQILINLLNNAFKFTHQGEVSLTL-----------GC 654
Cdd:PRK11073   209 --LVSLELPDNVRlirdydpSLPELAH-----------DPDQIEQVLLNIVRNALQALGPEGGTITLrtrtafqltlhGE 275
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1889623460  655 QYlteeKLLMSFVIEDSGIGIAEKNIDKLFEAFTqedtstTRHFGGTGLGLSICRKLAQLMGGDISVTSEKG 726
Cdd:PRK11073   276 RY----RLAARIDIEDNGPGIPPHLQDTLFYPMV------SGREGGTGLGLSIARNLIDQHSGKIEFTSWPG 337
ompR PRK09468
osmolarity response regulator; Provisional
891-1007 1.81e-06

osmolarity response regulator; Provisional


Pssm-ID: 181883 [Multi-domain]  Cd Length: 239  Bit Score: 50.36  E-value: 1.81e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  891 NFKVLLVDDNMINLEVAKAILKNTGVTIVCASDGLDALEILNTEqtaLFDLILMDCQMPnlnGYDTTSAIRSNKAGADya 970
Cdd:PRK09468     5 NYKILVVDDDMRLRALLERYLTEQGFQVRSAANAEQMDRLLTRE---SFHLMVLDLMLP---GEDGLSICRRLRSQNN-- 76
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1889623460  971 KVPIIAMTASAMAGDRERCITAGMNDYITKPIKPKVL 1007
Cdd:PRK09468    77 PTPIIMLTAKGEEVDRIVGLEIGADDYLPKPFNPREL 113
REC_OmpR_VirG cd17594
phosphoacceptor receiver (REC) domain of VirG-like OmpR family response regulators; VirG is ...
893-1001 3.36e-06

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: 47.06  E-value: 3.36e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  893 KVLLVDDNMINLEVAKAILKNTGVTIVCASDGLDALEILNTEQTalfDLILMDCQMPNLNGYDTTSAIRSNkagadyAKV 972
Cdd:cd17594      1 HVLVVDDDAAMRHLLILYLRERGFDVTAAADGAEEARLMLHRRV---DLVLLDLRLGQESGLDLLRTIRAR------SDV 71
                           90       100       110
                   ....*....|....*....|....*....|
gi 1889623460  973 PIIAMTASAM-AGDRERCITAGMNDYITKP 1001
Cdd:cd17594     72 PIIIISGDRRdEIDRVVGLELGADDYLAKP 101
REC_PilR cd19926
phosphoacceptor receiver (REC) domain of type 4 fimbriae expression regulatory protein PilR ...
894-1001 4.04e-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: 4.04e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  894 VLLVDDNMINLEVAKAILKNTGVTIVCASDGLDALEILNTEQtalFDLILMDCQMPNLNGYDTTSAIRSNkagadYAKVP 973
Cdd:cd19926      1 VLVVDDEPDIRELLEITLGRMGLDVRSARNVKEARELLASEP---YDLCLTDMRLPDGSGLELVQHIQQR-----LPQTP 72
                           90       100
                   ....*....|....*....|....*...
gi 1889623460  974 IIAMTASAMAGDRERCITAGMNDYITKP 1001
Cdd:cd19926     73 VAVITAYGSLDTAIEALKAGAFDFLTKP 100
PRK10403 PRK10403
nitrate/nitrite response regulator protein NarP;
892-1007 8.13e-06

nitrate/nitrite response regulator protein NarP;


Pssm-ID: 182431 [Multi-domain]  Cd Length: 215  Bit Score: 47.92  E-value: 8.13e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  892 FKVLLVDDNMINLEVAKAILK-NTGVTIVC-ASDGLDALEILNTEQTalfDLILMDCQMPNLNGYDTTSAIRSNKAGADy 969
Cdd:PRK10403     7 FQVLIVDDHPLMRRGVRQLLElDPGFEVVAeAGDGASAIDLANRLDP---DVILLDLNMKGMSGLDTLNALRRDGVTAQ- 82
                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1889623460  970 akvpIIAMTASAMAGDRERCITAGMNDYITKPIKPKVL 1007
Cdd:PRK10403    83 ----IIILTVSDASSDVFALIDAGADGYLLKDSDPEVL 116
REC_OmpR_ChvI-like cd19936
phosphoacceptor receiver (REC) domain of ChvI-like OmpR family response regulators; ...
894-1001 1.01e-05

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


Pssm-ID: 381163 [Multi-domain]  Cd Length: 99  Bit Score: 45.13  E-value: 1.01e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  894 VLLVDDNMINLEVAKAILKNTGVTIVCASDGLDALEILNTEqtaLFDLILMDCQMPNLNGYDTTSAIRSNkagadyAKVP 973
Cdd:cd19936      1 IALVDDDRNILTSVSMALEAEGFSVETYTDGASALDGLNAR---PPDLAILDIKMPRMDGMELLQRLRQK------STLP 71
                           90       100
                   ....*....|....*....|....*...
gi 1889623460  974 IIAMTASAMAGDRERCITAGMNDYITKP 1001
Cdd:cd19936     72 VIFLTSKDDEIDEVFGLRMGADDYITKP 99
PRK15115 PRK15115
response regulator GlrR; Provisional
894-1002 1.49e-05

response regulator GlrR; Provisional


Pssm-ID: 185070 [Multi-domain]  Cd Length: 444  Bit Score: 48.68  E-value: 1.49e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  894 VLLVDDNMINLEVAKAILKNTGVTIVCASDGLDALEILNTEQtalFDLILMDCQMPNLNGYDTTSAIRSNKAGadyakVP 973
Cdd:PRK15115     8 LLLVDDDPGLLKLLGMRLTSEGYSVVTAESGQEALRVLNREK---VDLVISDLRMDEMDGMQLFAEIQKVQPG-----MP 79
                           90       100
                   ....*....|....*....|....*....
gi 1889623460  974 IIAMTASAMAGDRERCITAGMNDYITKPI 1002
Cdd:PRK15115    80 VIILTAHGSIPDAVAATQQGVFSFLTKPV 108
pleD PRK09581
response regulator PleD; Reviewed
877-1004 1.59e-05

response regulator PleD; Reviewed


Pssm-ID: 236577 [Multi-domain]  Cd Length: 457  Bit Score: 48.74  E-value: 1.59e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  877 QGSEQTEYVEyDFSNFKVLLVDDNMINLE-VAKAILKNTGVTIVcaSDGLDALEILNTEQtalFDLILMDCQMPNLNGYD 955
Cdd:PRK09581   142 TALMIMAYAN-KDEDGRILLVDDDVSQAErIANILKEEFRVVVV--SDPSEALFNAAETN---YDLVIVSANFENYDPLR 215
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1889623460  956 TTSAIRSNkagADYAKVPIIAMTAsamAGDRERCITA---GMNDYITKPIKP 1004
Cdd:PRK09581   216 LCSQLRSK---ERTRYVPILLLVD---EDDDPRLVKAlelGVNDYLMRPIDK 261
PRK10651 PRK10651
transcriptional regulator NarL; Provisional
894-1011 1.83e-05

transcriptional regulator NarL; Provisional


Pssm-ID: 182619 [Multi-domain]  Cd Length: 216  Bit Score: 46.95  E-value: 1.83e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  894 VLLVDDN-MINLEVAKAILKNTGVTIVC-ASDGLDALEiLNTEQTAlfDLILMDCQMPNLNGYDTTSAIRSnkAGADYAk 971
Cdd:PRK10651     9 ILLIDDHpMLRTGVKQLISMAPDITVVGeASNGEQGIE-LAESLDP--DLILLDLNMPGMNGLETLDKLRE--KSLSGR- 82
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1889623460  972 vpIIAMTASAMAGDRERCITAGMNDYITKPIKPKVLKDKL 1011
Cdd:PRK10651    83 --IVVFSVSNHEEDVVTALKRGADGYLLKDMEPEDLLKAL 120
PRK10766 PRK10766
two-component system response regulator TorR;
892-1007 2.12e-05

two-component system response regulator TorR;


Pssm-ID: 182711 [Multi-domain]  Cd Length: 221  Bit Score: 46.96  E-value: 2.12e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  892 FKVLLVDDNMINLEVAKAILKNTGVTIVCASDGLDALEILNTEQTalfDLILMDCQMPNLNGYDTTSAIRSNkagadyAK 971
Cdd:PRK10766     3 YHILVVEDEPVTRARLQGYFEQEGYTVSEAASGAGMREIMQNQHV---DLILLDINLPGEDGLMLTRELRSR------ST 73
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1889623460  972 VPIIAMTASAMAGDRERCITAGMNDYITKPIKPKVL 1007
Cdd:PRK10766    74 VGIILVTGRTDSIDRIVGLEMGADDYVTKPLELREL 109
REC_NtrC cd19919
phosphoacceptor receiver (REC) domain of DNA-binding transcriptional regulator NtrC; ...
893-1001 2.13e-05

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


Pssm-ID: 381146 [Multi-domain]  Cd Length: 116  Bit Score: 44.57  E-value: 2.13e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  893 KVLLVDDN-MINLEVAKAiLKNTGVTIVCASDGLDALEILNTEQTalfDLILMDCQMPNLNGYDTTSAIRsnkagADYAK 971
Cdd:cd19919      2 TVWIVDDDsSIRWVLERA-LAGAGLTVTSFENAQEALAALASSQP---DVLISDIRMPGMDGLALLAQIK-----QRHPD 72
                           90       100       110
                   ....*....|....*....|....*....|...
gi 1889623460  972 VPIIAMTASAmagDRERCITA---GMNDYITKP 1001
Cdd:cd19919     73 LPVIIMTAHS---DLDSAVSAyqgGAFEYLPKP 102
REC_WspR-like cd17575
phosphoacceptor receiver (REC) domain of WspR response regulator and similar proteins; The ...
892-1000 2.36e-05

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: 44.71  E-value: 2.36e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  892 FKVLLVDDN-MINLEVAKAILKNTGVTIVCASDGLDALEILN-TEQTalfdLILMDCQMPNLNGYDTTSAIRSNKAGADy 969
Cdd:cd17575      1 IMVLLVDDQaIIGEAVRRALADEEDIDFHYCSDPTEAIEVASqIKPT----VILQDLVMPGVDGLTLVRFFRANPATRD- 75
                           90       100       110
                   ....*....|....*....|....*....|.
gi 1889623460  970 akVPIIAMTASAMAGDRERCITAGMNDYITK 1000
Cdd:cd17575     76 --IPIIVLSTKEEPEVKSEAFALGANDYLVK 104
PRK13557 PRK13557
histidine kinase; Provisional
894-1015 2.53e-05

histidine kinase; Provisional


Pssm-ID: 237425 [Multi-domain]  Cd Length: 540  Bit Score: 48.13  E-value: 2.53e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  894 VLLVDDNMINLEVAKAILKNTGVTIVCASDGLDALEILNTEqtALFDLILMDCQMP-NLNGYDTTSAIRSNkagadYAKV 972
Cdd:PRK13557   418 ILIVDDRPDVAELARMILEDFGYRTLVASNGREALEILDSH--PEVDLLFTDLIMPgGMNGVMLAREARRR-----QPKI 490
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 1889623460  973 PIIAMTASAMAGdRERCITAGMN-DYITKPIKPKVLKDKLAMWL 1015
Cdd:PRK13557   491 KVLLTTGYAEAS-IERTDAGGSEfDILNKPYRRAELARRVRMVL 533
RocR COG3829
RocR-type transcriptional regulator, contains PAS, AAA-type ATPase, and DNA-binding Fis ...
355-513 2.55e-05

RocR-type transcriptional regulator, contains PAS, AAA-type ATPase, and DNA-binding Fis domains [Transcription, Signal transduction mechanisms];


Pssm-ID: 443041 [Multi-domain]  Cd Length: 448  Bit Score: 47.84  E-value: 2.55e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  355 RKLEFHSLKERNNKIIENSLDAILTVQEDGLISNANKTALQFFDI----IIDHtKFTQLFtlaesDNSCIDETIAQGSkp 430
Cdd:COG3829      2 EELELKELEEELEAILDSLDDGIIVVDADGRITYVNRAAERILGLpreeVIGK-NVTELI-----PNSPLLEVLKTGK-- 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  431 SFEGVYTDPQDQQHFYSITLTSVFDiFTQRHQVAAILRNINSLKQTQVELEKLNstLEQKVRQRTT---------ELESA 501
Cdd:COG3829     74 PVTGVIQKTGGKGKTVIVTAIPIFE-DGEVIGAVETFRDITELKRLERKLREEE--LERGLSAKYTfddiigkspAMKEL 150
                          170
                   ....*....|..
gi 1889623460  502 IEQALAASKSKS 513
Cdd:COG3829    151 LELAKRVAKSDS 162
REC_CpdR_CckA-like cd18160
phosphoacceptor receiver (REC) domain of Brucella abortus CpdR and CckA, and similar domains; ...
893-984 5.81e-05

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: 43.26  E-value: 5.81e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  893 KVLLVDDNMINLEVAKAILKNTGVTIVCASDGLDALEILntEQTALFDLILMDCQMPNLNGYDTtsAIRSNKAGADyakV 972
Cdd:cd18160      1 TILLADDEPSVRKFIVTTLKKAGYAVTEAESGAEALEKL--QQGKDIDIVVTDIVMPEMDGIEL--AREARKIDPD---V 73
                           90
                   ....*....|..
gi 1889623460  973 PIIAMTASAMAG 984
Cdd:cd18160     74 KILFISGGAAAA 85
REC_LytTR_AlgR-like cd17532
phosphoacceptor receiver (REC) domain of LytTR/AlgR family response regulators similar to AlgR; ...
894-1012 7.95e-05

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: 42.91  E-value: 7.95e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  894 VLLVDDNMINLEVAKAILKNTG-VTIVC-ASDGLDALEILNTEQTalfDLILMDCQMPNLNGYDTTSAIRSnkagadYAK 971
Cdd:cd17532      1 ALIVDDEPLAREELRYLLEEHPdIEIVGeAENGEEALEAIEELKP---DVVFLDIQMPGLDGLELAKKLSK------LAK 71
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 1889623460  972 VP-IIAMTASamagdRERCITA---GMNDYITKPIKPKVLKDKLA 1012
Cdd:cd17532     72 PPlIVFVTAY-----DEYAVEAfelNAVDYLLKPFSEERLAEALA 111
REC_hyHK_blue-like cd18161
phosphoacceptor receiver (REC) domain of hybrid sensor histidine kinase/response regulators ...
894-1001 1.27e-04

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: 41.95  E-value: 1.27e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  894 VLLVDDNMINLEVAKAILKNTGVTIVCASDGLDALEILntEQTALFDLILMDCQMPN-LNGYDTTSAIRsnkagADYAKV 972
Cdd:cd18161      1 VLVVEDDPDVRRLTAEVLEDLGYTVLEAASGDEALDLL--ESGPDIDLLVTDVIMPGgMNGSQLAEEAR-----RRRPDL 73
                           90       100
                   ....*....|....*....|....*....
gi 1889623460  973 PIIAMTASAMAGDRERCITAGMnDYITKP 1001
Cdd:cd18161     74 KVLLTSGYAENAIEGGDLAPGV-DVLSKP 101
PRK00742 PRK00742
chemotaxis-specific protein-glutamate methyltransferase CheB;
893-1001 1.96e-04

chemotaxis-specific protein-glutamate methyltransferase CheB;


Pssm-ID: 234828 [Multi-domain]  Cd Length: 354  Bit Score: 44.76  E-value: 1.96e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  893 KVLLVDDNMINLEVAKAIL-KNTGVTIVC-ASDGLDALEILNTEQTalfDLILMDCQMPNLNGYDTTSAIRSNKagadya 970
Cdd:PRK00742     5 RVLVVDDSAFMRRLISEILnSDPDIEVVGtAPDGLEAREKIKKLNP---DVITLDVEMPVMDGLDALEKIMRLR------ 75
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1889623460  971 KVPIIaMtASAM--AGDRE--RCITAGMNDYITKP 1001
Cdd:PRK00742    76 PTPVV-M-VSSLteRGAEItlRALELGAVDFVTKP 108
PRK11173 PRK11173
two-component response regulator; Provisional
893-1007 2.10e-04

two-component response regulator; Provisional


Pssm-ID: 183013 [Multi-domain]  Cd Length: 237  Bit Score: 43.85  E-value: 2.10e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  893 KVLLVDDNMINLEVAKAILKNTGVTIVCASDGLDALEILNTEQtalFDLILMDCQMPNLNGYDTTSAIRSNkagadyAKV 972
Cdd:PRK11173     5 HILIVEDELVTRNTLKSIFEAEGYDVFEATDGAEMHQILSEND---INLVIMDINLPGKNGLLLARELREQ------ANV 75
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1889623460  973 PIIAMTASAMAGDRERCITAGMNDYITKPIKPKVL 1007
Cdd:PRK11173    76 ALMFLTGRDNEVDKILGLEIGADDYITKPFNPREL 110
psREC-like_D2_PleD cd17539
REC-like adaptor domain (D2) of response regulator PleD; PleD contains a REC domain (D1) with ...
894-1007 2.10e-04

REC-like adaptor domain (D2) of response regulator PleD; PleD contains a REC domain (D1) with the phosphorylatable aspartate, a pseudo receiver (psREC)-like adaptor domain (D2), and the enzymatic diguanylate cyclase (DGC) domain, also called the GGDEF domain according to a conserved sequence motif, as its output domain. The GGDEF-containing PleD response regulators are global regulators of cell metabolism in some important human pathogens. This model describes the REC-like adaptor domain D2 of PleD, which is an inactive domain.


Pssm-ID: 381094 [Multi-domain]  Cd Length: 124  Bit Score: 41.92  E-value: 2.10e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  894 VLLVDDNMINLEVAKAILKNtGVTIVCASDGLDALEILNTEQtalFDLILMDCQMPNLNGYDTTSAIRSNKAGAdyaKVP 973
Cdd:cd17539      1 VLLVDDRPSSAERIAAMLSS-EHEVVVEADPDEALFRAAEGP---FDLVIVSLALEDFDGLRLCSQLRSLERTR---QLP 73
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1889623460  974 IIAMtasAMAGDRERCITA---GMNDYITKPIKPKVL 1007
Cdd:cd17539     74 ILAV---ADPGDRGRLIRAleiGVNDYLVRPIDPNEL 107
COG4567 COG4567
DNA-binding response regulator, ActR/RegA family, consists of REC and Fis-type HTH domains ...
893-1002 2.73e-04

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: 42.98  E-value: 2.73e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  893 KVLLVDDNMINLEVAKAILKNTGVTIVCASDGLDALEILnteQTALFDLILMDCQMPNLNGYDTTSAIRSNKAGAdyakv 972
Cdd:COG4567      6 SLLLVDDDEAFARVLARALERRGFEVTTAASVEEALALL---EQAPPDYAVLDLRLGDGSGLDLIEALRERDPDA----- 77
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1889623460  973 PIIAMT-----ASAMAGdrercITAGMNDYITKPI 1002
Cdd:COG4567     78 RIVVLTgyasiATAVEA-----IKLGADDYLAKPA 107
glnG PRK10923
nitrogen regulation protein NR(I); Provisional
893-1001 2.88e-04

nitrogen regulation protein NR(I); Provisional


Pssm-ID: 182842 [Multi-domain]  Cd Length: 469  Bit Score: 44.48  E-value: 2.88e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  893 KVLLVDDNMINLEVAKAILKNTGVTIVCASDGLDALEILNTEQTalfDLILMDCQMPNLNGYDTTSAIRSNkagadYAKV 972
Cdd:PRK10923     5 IVWVVDDDSSIRWVLERALAGAGLTCTTFENGNEVLEALASKTP---DVLLSDIRMPGMDGLALLKQIKQR-----HPML 76
                           90       100       110
                   ....*....|....*....|....*....|..
gi 1889623460  973 PIIAMTASAmagDRERCITA---GMNDYITKP 1001
Cdd:PRK10923    77 PVIIMTAHS---DLDAAVSAyqqGAFDYLPKP 105
PRK10693 PRK10693
two-component system response regulator RssB;
920-1003 3.41e-04

two-component system response regulator RssB;


Pssm-ID: 182652 [Multi-domain]  Cd Length: 303  Bit Score: 43.83  E-value: 3.41e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  920 CASDGLDALEILNTEQTalfDLILMDCQMPNLNGYDTTSAIRSnkagaDYAKVPIIAMTASAMAGDRERCITAGMNDYIT 999
Cdd:PRK10693     2 LAANGVDALELLGGFTP---DLIICDLAMPRMNGIEFVEHLRN-----RGDQTPVLVISATENMADIAKALRLGVQDVLL 73

                   ....
gi 1889623460 1000 KPIK 1003
Cdd:PRK10693    74 KPVK 77
PRK10710 PRK10710
DNA-binding transcriptional regulator BaeR; Provisional
940-1005 3.65e-04

DNA-binding transcriptional regulator BaeR; Provisional


Pssm-ID: 182665 [Multi-domain]  Cd Length: 240  Bit Score: 43.14  E-value: 3.65e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1889623460  940 DLILMDCQMPNLNGYDTTSAIRSnkagadYAKVPIIAMTASAMAGDRERCITAGMNDYITKPIKPK 1005
Cdd:PRK10710    56 DLILLDLMLPGTDGLTLCREIRR------FSDIPIVMVTAKIEEIDRLLGLEIGADDYICKPYSPR 115
PRK10815 PRK10815
two-component system sensor histidine kinase PhoQ;
603-723 3.80e-04

two-component system sensor histidine kinase PhoQ;


Pssm-ID: 182754 [Multi-domain]  Cd Length: 485  Bit Score: 44.24  E-value: 3.80e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  603 QRKGLEVFLHTDKVIdrMLVGDSHRLKQILINLLNNAFKFTHQG-EVSLTLGCQYLTeekllmsFVIEDSGIGIAEKNID 681
Cdd:PRK10815   356 QRKGVNITLDISPEI--TFVGEKNDFMEVMGNVLDNACKYCLEFvEISARQTDEHLH-------IVVEDDGPGIPESKRE 426
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1889623460  682 KLFEAFTQEDTSTTrhfgGTGLGLSICRKLAQLMGGDISVTS 723
Cdd:PRK10815   427 LIFDRGQRADTLRP----GQGLGLSVAREITEQYEGKISAGD 464
REC_DesR-like cd19930
phosphoacceptor receiver (REC) domain of DesR and similar proteins; This group is composed of ...
921-1009 4.09e-04

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


Pssm-ID: 381157 [Multi-domain]  Cd Length: 117  Bit Score: 41.10  E-value: 4.09e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  921 ASDGLDALEILNTEQtalFDLILMDCQMPNLNGYDTTSAIRSNKAGadyAKVPIIamTASAMAGDRERCITAGMNDYITK 1000
Cdd:cd19930     30 ASNGQEALRLVLKHS---PDVAILDIEMPGRTGLEVAAELREELPD---TKVLIV--TTFGRPGYFRRALAAGVDGYVLK 101

                   ....*....
gi 1889623460 1001 PIKPKVLKD 1009
Cdd:cd19930    102 DRPIEELAD 110
PAS COG2202
PAS domain [Signal transduction mechanisms];
355-508 4.78e-04

PAS domain [Signal transduction mechanisms];


Pssm-ID: 441804 [Multi-domain]  Cd Length: 258  Bit Score: 43.09  E-value: 4.78e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  355 RKLEFHSLKERNNKIIENSLDAILTVQEDGLISNANKTALQFF-----DIIIDHTKFTQLFTLAESDNSCIDETIAQGSK 429
Cdd:COG2202      2 AEEALEESERRLRALVESSPDAIIITDLDGRILYVNPAFERLTgysaeELLGKTLRDLLPPEDDDEFLELLRAALAGGGV 81
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1889623460  430 PSFEGVYTDPQDQQHFYSITLTSVFDIFTQRHQVAAILRNINSLKQTqveleklnstlEQKVRQRTTELESAIEQALAA 508
Cdd:COG2202     82 WRGELRNRRKDGSLFWVELSISPVRDEDGEITGFVGIARDITERKRA-----------EEALRESEERLRLLVENAPDG 149
YesM COG2972
Sensor histidine kinase YesM [Signal transduction mechanisms];
598-744 4.85e-04

Sensor histidine kinase YesM [Signal transduction mechanisms];


Pssm-ID: 442211 [Multi-domain]  Cd Length: 445  Bit Score: 43.85  E-value: 4.85e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  598 MALQAQR--KGLEVFLHTDKVIDRMLVgdshrLKQILINLLNNAFKF-----THQGEVSLTLgcqYLTEEKLLmsFVIED 670
Cdd:COG2972    310 LEIQKLRfgDRLEVEIEIDEELLDLLI-----PKLILQPLVENAIEHgiepkEGGGTIRISI---RKEGDRLV--ITVED 379
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1889623460  671 SGIGIAEKNIDKLFEAFTQEDtsttrhfGGTGLGLSICRKLAQLMGGD---ISVTSEKGQGscftAQVQLHIAAEKK 744
Cdd:COG2972    380 NGVGMPEEKLEKLLEELSSKG-------EGRGIGLRNVRERLKLYYGEeygLEIESEPGEG----TTVTIRIPLEEE 445
REC_NtrC1-like cd17572
phosphoacceptor receiver (REC) domain of nitrogen regulatory protein C 1 (NtrC1) from Aquifex ...
894-1008 6.55e-04

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: 40.64  E-value: 6.55e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  894 VLLVDDNMINLEVAKAILKNTGVTIVCASDGLDALEILnteQTALFDLILMDCQMPNLNGYDTTSAIRSNKagadyAKVP 973
Cdd:cd17572      1 VLLVEDSPSLAALYQEYLSDEGYKVTHVETGKEALAFL---SDQPPDVVLLDLKLPDMSGMEILKWIQERS-----LPTS 72
                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1889623460  974 IIAMTASA---MAGDRERcitAGMNDYITKPIKPKVLK 1008
Cdd:cd17572     73 VIVITAHGsvdIAVEAMR---LGAYDFLEKPFDADRLR 107
REC_HP-RR-like cd17573
phosphoacceptor receiver (REC) domain of orphan response regulator HP-RR and similar proteins; ...
939-1007 6.86e-04

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: 40.11  E-value: 6.86e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1889623460  939 FDLILMDCQMPNLNGYDTTSAIRSNkagadYAKVPIIAMTASAMAGDRERCITAGMNDYITKPIKPKVL 1007
Cdd:cd17573     43 YDLVLVSDKLPDGNGLSIVSRIKEK-----HPSIVVIVLSDNPKTEQEIEAFKEGADDYIAKPFDFKVL 106
PRK10336 PRK10336
two-component system response regulator QseB;
893-1001 7.27e-04

two-component system response regulator QseB;


Pssm-ID: 182387 [Multi-domain]  Cd Length: 219  Bit Score: 42.19  E-value: 7.27e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  893 KVLLVDDNMINLEVAKAILKNTGVTIVCASDGLDALEILnteQTALFDLILMDCQMPNLNGYDTTSAIRSNKAgadyaKV 972
Cdd:PRK10336     2 RILLIEDDMLIGDGIKTGLSKMGFSVDWFTQGRQGKEAL---YSAPYDAVILDLTLPGMDGRDILREWREKGQ-----RE 73
                           90       100
                   ....*....|....*....|....*....
gi 1889623460  973 PIIAMTASAMAGDRERCITAGMNDYITKP 1001
Cdd:PRK10336    74 PVLILTARDALAERVEGLRLGADDYLCKP 102
PRK12555 PRK12555
chemotaxis-specific protein-glutamate methyltransferase CheB;
893-960 9.99e-04

chemotaxis-specific protein-glutamate methyltransferase CheB;


Pssm-ID: 237135 [Multi-domain]  Cd Length: 337  Bit Score: 42.56  E-value: 9.99e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  893 KVLLVDDNMINLEV-AKAILKNTGVTIV-CASDGLDALEiLNTEQTAlfDLILMDCQMPNLNGYDTTSAI 960
Cdd:PRK12555     2 RIGIVNDSPLAVEAlRRALARDPDHEVVwVATDGAQAVE-RCAAQPP--DVILMDLEMPRMDGVEATRRI 68
REC_HupR cd17596
phosphoacceptor receiver (REC) domain of hydrogen uptake protein regulator (HupR); Members of ...
894-1016 1.34e-03

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


Pssm-ID: 381127 [Multi-domain]  Cd Length: 133  Bit Score: 40.04  E-value: 1.34e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  894 VLLVDDNMINLEVAKAILKnTGVTIVCASDGLDALEILNTEQTalfDLILMDCQMPNLNGYDTTSAIRsnKAGADYAKVP 973
Cdd:cd17596      3 ILVVDDEVRSLEALRRTLE-EDFDVLTAASAEEALAILEEEWV---QVILCDQRMPGTTGVEFLKEVR--ERWPEVVRII 76
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 1889623460  974 IIAMTASA--MAGDRErcitAGMNDYITKPIKPkvlkDKLAMWLK 1016
Cdd:cd17596     77 ISGYTDSEdiIAGINE----AGIYQYLTKPWHP----DQLLLTVR 113
HATPase_PDK-like cd16929
Histidine kinase-like ATPase domain of pyruvate dehydrogenase kinase, branched-chain ...
625-728 1.35e-03

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


Pssm-ID: 340406 [Multi-domain]  Cd Length: 169  Bit Score: 40.79  E-value: 1.35e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  625 SHrLKQILINLLNNAFKFT--HQGEVSLTL-----GCQYLTEEkllMSFVIEDSGIGIAEKNIDKLF------------- 684
Cdd:cd16929     42 SH-LYYILFELLKNAMRATveSHGDDSDDLppikvTVAKGDED---LTIKISDRGGGIPREDLARLFsymystapqpsld 117
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 1889623460  685 -EAFTQEDTSTTrHFGGTGLGLSICRKLAQLMGGDISVTSEKGQG 728
Cdd:cd16929    118 dFSDLISGTQPS-PLAGFGYGLPMSRLYAEYFGGDLDLQSMEGYG 161
PRK10643 PRK10643
two-component system response regulator PmrA;
893-1001 1.35e-03

two-component system response regulator PmrA;


Pssm-ID: 182612 [Multi-domain]  Cd Length: 222  Bit Score: 41.56  E-value: 1.35e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  893 KVLLVDDNMINLEVAKAILKNTGVTIVCASDGLDALEILnteQTALFDLILMDCQMPNLNGYDTTSAIRSNKAGadyakV 972
Cdd:PRK10643     2 KILIVEDDTLLLQGLILALQTEGYACDCASTAREAEALL---ESGHYSLVVLDLGLPDEDGLHLLRRWRQKKYT-----L 73
                           90       100
                   ....*....|....*....|....*....
gi 1889623460  973 PIIAMTASAMAGDRERCITAGMNDYITKP 1001
Cdd:PRK10643    74 PVLILTARDTLEDRVAGLDVGADDYLVKP 102
REC_1_GGDEF cd19921
first phosphoacceptor receiver (REC) domain of uncharacterized GGDEF domain proteins; This ...
893-1000 2.12e-03

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


Pssm-ID: 381148 [Multi-domain]  Cd Length: 115  Bit Score: 39.08  E-value: 2.12e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  893 KVLLVDDN-MINLEVAKAILKNTGVTIVCASDGLDALEILNTEQT---ALFDLILMDCQmpnlNGydttSAIrsnkagaD 968
Cdd:cd19921      1 KVLIVEDSkTFSKVLKHLIAQELGLEVDVAETLAEAKALLEEGDDyfaALVDLNLPDAP----NG----EAV-------D 65
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1889623460  969 YA---KVPIIAMTASAMAGDRERCITAGMNDYITK 1000
Cdd:cd19921     66 LVlekGIPVIVLTGSFDEDKRETLLSKGVVDYVLK 100
REC_TPR cd17589
phosphoacceptor receiver (REC) domain of uncharacterized tetratricopeptide repeat (TPR) ...
894-1011 3.04e-03

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


Pssm-ID: 381123 [Multi-domain]  Cd Length: 115  Bit Score: 38.40  E-value: 3.04e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  894 VLLVDDNMINLEVAKAILKNTGVT-IVCASDGLDALEILNTEQtalFDLILMDCQMPN-LNGYDTTSAIRSNKagadyak 971
Cdd:cd17589      1 FLIVDDQPTFRSMLKSMLRSLGVTrIDTASSGEEALRMCENKT---YDIVLCDYNLGKgKNGQQLLEELRHKK------- 70
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 1889623460  972 vpIIAMTASAM--AGDRERCITAGM-----NDYITKPIKPKVLKDKL 1011
Cdd:cd17589     71 --LISPSTVFImvTGESSRAMVLSAlelepDDYLLKPFTVSELRERL 115
REC_RegA-like cd17563
phosphoacceptor receiver (REC) domain of photosynthetic apparatus regulatory protein RegA; ...
893-1001 3.36e-03

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: 38.19  E-value: 3.36e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  893 KVLLVDDNMINLEVAKAILKNTGVTIVCASDGLDALEILNTEQtalFDLILMDCQMPNLNGYDTTSAIRSNKAGAdyakv 972
Cdd:cd17563      2 SLLLVDDDEVFAERLARALERRGFEVETAHSVEEALALAREEK---PDYAVLDLRLGGDSGLDLIPPLRALQPDA----- 73
                           90       100       110
                   ....*....|....*....|....*....|....
gi 1889623460  973 PIIAMT-----ASAMAGdrercITAGMNDYITKP 1001
Cdd:cd17563     74 RIVVLTgyasiATAVEA-----IKLGADDYLAKP 102
REC_Spo0A cd17561
phosphoacceptor receiver (REC) domain of Spo0A; Spo0A is a response regulator of the ...
893-1001 3.91e-03

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: 37.97  E-value: 3.91e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  893 KVLLVDDN--MINLeVAKAILKNTGVTIV-CASDGLDALEILNTEQTalfDLILMDCQMPNLNGYDTTSAIRSNKagaDY 969
Cdd:cd17561      3 KVLIADDNreFVQL-LEEYLNSQPDMEVVgVAHNGQEALELIEEKEP---DVLLLDIIMPHLDGIGVLEKLRRMR---LE 75
                           90       100       110
                   ....*....|....*....|....*....|..
gi 1889623460  970 AKVPIIAMTASAMAGDRERCITAGMNDYITKP 1001
Cdd:cd17561     76 KRPKIIMLTAFGQEDITQRAVELGASYYILKP 107
PRK10816 PRK10816
two-component system response regulator PhoP;
893-1001 6.01e-03

two-component system response regulator PhoP;


Pssm-ID: 182755 [Multi-domain]  Cd Length: 223  Bit Score: 39.34  E-value: 6.01e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  893 KVLLVDDNMINLEVAKAILKNTGVTIVCASDGLDALEILNtEQTAlfDLILMDCQMPnlnGYDTTSAIRSNKAgaDYAKV 972
Cdd:PRK10816     2 RVLVVEDNALLRHHLKVQLQDAGHQVDAAEDAKEADYYLN-EHLP--DIAIVDLGLP---DEDGLSLIRRWRS--NDVSL 73
                           90       100
                   ....*....|....*....|....*....
gi 1889623460  973 PIIAMTASAMAGDRERCITAGMNDYITKP 1001
Cdd:PRK10816    74 PILVLTARESWQDKVEVLSAGADDYVTKP 102
ComP COG4585
Signal transduction histidine kinase ComP [Signal transduction mechanisms];
635-735 8.13e-03

Signal transduction histidine kinase ComP [Signal transduction mechanisms];


Pssm-ID: 443642 [Multi-domain]  Cd Length: 252  Bit Score: 39.22  E-value: 8.13e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  635 LLNNAFKftHQG--EVSLTLGCqylTEEKLLMSfvIEDSGIGIAEKNIdklfeaftqedtsttrhfGGTGLGLSICRKLA 712
Cdd:COG4585    170 ALTNALK--HAGatRVTVTLEV---DDGELTLT--VRDDGVGFDPEAA------------------PGGGLGLRGMRERA 224
                           90       100
                   ....*....|....*....|...
gi 1889623460  713 QLMGGDISVTSEKGQGSCFTAQV 735
Cdd:COG4585    225 EALGGTLTIGSAPGGGTRVRATL 247
PRK10529 PRK10529
DNA-binding transcriptional activator KdpE; Provisional
940-1001 8.43e-03

DNA-binding transcriptional activator KdpE; Provisional


Pssm-ID: 182522 [Multi-domain]  Cd Length: 225  Bit Score: 39.02  E-value: 8.43e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1889623460  940 DLILMDCQMPNLNGYDTTSAIRSnkagadYAKVPIIAMTASAMAGDRERCITAGMNDYITKP 1001
Cdd:PRK10529    47 DLIILDLGLPDGDGIEFIRDLRQ------WSAIPVIVLSARSEESDKIAALDAGADDYLSKP 102
REC_FixJ cd17537
phosphoacceptor receiver (REC) domain of FixJ family response regulators; FixJ family response ...
894-1011 9.40e-03

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: 37.19  E-value: 9.40e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1889623460  894 VLLVDDNMINLEVAKAILKNTGVTIVCASDGLDALEILNTEQTALfdlILMDCQMPNLNGYDTTSAIRSNKAgadyaKVP 973
Cdd:cd17537      3 VYVVDDDEAVRDSLAFLLRSVGLAVKTFTSASAFLAAAPPDQPGC---LVLDVRMPGMSGLELQDELLARGS-----NIP 74
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 1889623460  974 IIAMTASA---MAgdrERCITAGMNDYITKPIKPKVLKDKL 1011
Cdd:cd17537     75 IIFITGHGdvpMA---VEAMKAGAVDFLEKPFRDQVLLDAI 112
 
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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