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Conserved domains on  [gi|504416374|ref|WP_014603476|]
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MULTISPECIES: chemotaxis protein CheA [Pseudomonas]

Protein Classification

chemotaxis protein CheA( domain architecture ID 11428864)

chemotaxis protein CheA is a sensor histitine protein kinase that transmits sensory signals from chemoreceptors to the flagellar motors

CATH:  3.30.565.10|3.30.565.10
EC:  2.7.13.3
Gene Ontology:  GO:0005524|GO:0007165|GO:0000155|GO:0006935
PubMed:  31374212|10339418|10637609
SCOP:  4001957|4001957

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CheA COG0643
Chemotaxis protein histidine kinase CheA [Signal transduction mechanisms];
4-639 0e+00

Chemotaxis protein histidine kinase CheA [Signal transduction mechanisms];


:

Pssm-ID: 440408 [Multi-domain]  Cd Length: 563  Bit Score: 712.34  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504416374   4 DMSQFLQVFFEETEEHLATLELLLIGLDLDRPDSETLHGIFRAAHSIKGSSGMFGFDDITAVTHELETLLDRIRCGQMGL 83
Cdd:COG0643    2 DMDELLEIFLEEARELLEQLEEGLLALEQDPDDPELLNAIFRAAHTLKGSAGMLGLDALAELAHALEDLLDALRNGELAL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504416374  84 RPDMISSFLEARDVLQRLLDAHRSGRPDPgvpllETVERLRGWLRAPEQEAAEEGFGLFDDAPTSPARETAdddafgffd 163
Cdd:COG0643   82 TPELIDLLLEALDALRALLDALEAGGEPP-----ADISALLARLDASEEAIEEVVADEVEISPPAPAALEP--------- 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504416374 164 egpgaperaaapeafglfdeapgapaaseafglfddAPGSPPTEERAfglfdgapgspaapsapaqavaapargAVAPVR 243
Cdd:COG0643  148 ------------------------------------APAAAPPAEAA---------------------------AAAAEA 164

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504416374 244 GDGESGSIRVSVEKIDSLINLVGELVITQAMLGQLGEQLDPSHHERLQHALAQLEHNTRDLQESVMSIRMLPINFIFSRF 323
Cdd:COG0643  165 AAAASETVRVDVERLDRLMNLVGELVITRARLEQLAEELEDESLRELEEALEQLSRLTRELQDGVMRLRMVPISTVFNRF 244

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504416374 324 PRLVRDTATRLGKQVELHLHGEHTELDKSVIEKLSDPLTHIVRNSIDHGIETPAERLAAGKPASGTVKLAASHQGGSVVV 403
Cdd:COG0643  245 PRMVRDLARELGKEVELVIEGEETELDRTVLERLGDPLVHLVRNAVDHGIETPEERLAAGKPETGTITLSAYHEGGRVVI 324

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504416374 404 EVSDDGRGLSRPRILAKARERNLPVHDG---MSDAEVWQLVFMPGFSTAETVTELSGRGVGMDVVKRNIGAMGGRIDIDS 480
Cdd:COG0643  325 EVSDDGRGLDLEKIRAKAIEKGLITAEEaaaLSDEELLELIFAPGFSTAEEVTDLSGRGVGMDVVKTNIEALGGTIEIES 404

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504416374 481 APGMGTRIGIRLPLTLAILDGLIVAVEAVNYVIPLTYIVESLQARSDDVRGLGGEDnaMIRVRGEYLPLFSLHELLRIGG 560
Cdd:COG0643  405 EPGKGTTFTLRLPLTLAIIDGLLVRVGGETYAIPLSSVEEVLRLDPDDIETVEGRE--VIRLRGELLPLVRLGELLGLPG 482

                        570       580       590       600       610       620       630
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 504416374 561 EAPAPEQGIVVILESEGRSFALQVDELVGQQQVVIKSLEQNFRRVEGIAGATIMGDGSVALILDVDALPRLAAREDTAD 639
Cdd:COG0643  483 AEPEGERGPVVVVRSGGRRVALVVDELLGQQEVVIKPLGPLLRRVPGISGATILGDGRVALILDVAALVRSARARARAA 561
 
Name Accession Description Interval E-value
CheA COG0643
Chemotaxis protein histidine kinase CheA [Signal transduction mechanisms];
4-639 0e+00

Chemotaxis protein histidine kinase CheA [Signal transduction mechanisms];


Pssm-ID: 440408 [Multi-domain]  Cd Length: 563  Bit Score: 712.34  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504416374   4 DMSQFLQVFFEETEEHLATLELLLIGLDLDRPDSETLHGIFRAAHSIKGSSGMFGFDDITAVTHELETLLDRIRCGQMGL 83
Cdd:COG0643    2 DMDELLEIFLEEARELLEQLEEGLLALEQDPDDPELLNAIFRAAHTLKGSAGMLGLDALAELAHALEDLLDALRNGELAL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504416374  84 RPDMISSFLEARDVLQRLLDAHRSGRPDPgvpllETVERLRGWLRAPEQEAAEEGFGLFDDAPTSPARETAdddafgffd 163
Cdd:COG0643   82 TPELIDLLLEALDALRALLDALEAGGEPP-----ADISALLARLDASEEAIEEVVADEVEISPPAPAALEP--------- 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504416374 164 egpgaperaaapeafglfdeapgapaaseafglfddAPGSPPTEERAfglfdgapgspaapsapaqavaapargAVAPVR 243
Cdd:COG0643  148 ------------------------------------APAAAPPAEAA---------------------------AAAAEA 164

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504416374 244 GDGESGSIRVSVEKIDSLINLVGELVITQAMLGQLGEQLDPSHHERLQHALAQLEHNTRDLQESVMSIRMLPINFIFSRF 323
Cdd:COG0643  165 AAAASETVRVDVERLDRLMNLVGELVITRARLEQLAEELEDESLRELEEALEQLSRLTRELQDGVMRLRMVPISTVFNRF 244

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504416374 324 PRLVRDTATRLGKQVELHLHGEHTELDKSVIEKLSDPLTHIVRNSIDHGIETPAERLAAGKPASGTVKLAASHQGGSVVV 403
Cdd:COG0643  245 PRMVRDLARELGKEVELVIEGEETELDRTVLERLGDPLVHLVRNAVDHGIETPEERLAAGKPETGTITLSAYHEGGRVVI 324

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504416374 404 EVSDDGRGLSRPRILAKARERNLPVHDG---MSDAEVWQLVFMPGFSTAETVTELSGRGVGMDVVKRNIGAMGGRIDIDS 480
Cdd:COG0643  325 EVSDDGRGLDLEKIRAKAIEKGLITAEEaaaLSDEELLELIFAPGFSTAEEVTDLSGRGVGMDVVKTNIEALGGTIEIES 404

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504416374 481 APGMGTRIGIRLPLTLAILDGLIVAVEAVNYVIPLTYIVESLQARSDDVRGLGGEDnaMIRVRGEYLPLFSLHELLRIGG 560
Cdd:COG0643  405 EPGKGTTFTLRLPLTLAIIDGLLVRVGGETYAIPLSSVEEVLRLDPDDIETVEGRE--VIRLRGELLPLVRLGELLGLPG 482

                        570       580       590       600       610       620       630
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 504416374 561 EAPAPEQGIVVILESEGRSFALQVDELVGQQQVVIKSLEQNFRRVEGIAGATIMGDGSVALILDVDALPRLAAREDTAD 639
Cdd:COG0643  483 AEPEGERGPVVVVRSGGRRVALVVDELLGQQEVVIKPLGPLLRRVPGISGATILGDGRVALILDVAALVRSARARARAA 561
PRK10547 PRK10547
chemotaxis protein CheA; Provisional
 4-631 0e+00

chemotaxis protein CheA; Provisional


Pssm-ID: 236712 [Multi-domain]  Cd Length: 670  Bit Score: 649.10  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504416374   4 DMSQFLQVFFEETEEHLATLELLLIGLDLDRPDSETLHGIFRAAHSIKGSSGMFGFDDITAVTHELETLLDRIRCGQMGL 83
Cdd:PRK10547   2 DISDFYQTFFDEADELLADMEQHLLVLDPEAPDAEQLNAIFRAAHSIKGGAGTFGFTVLQETTHLMENLLDEARRGEMQL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504416374  84 RPDMISSFLEARDVLQRLLDAHRSGR-PDPgvpllETVERLRGWLRAPEQEAAEEGfglfDDAPTSPARETADDDAFGff 162
Cdd:PRK10547  82 NTDIINLFLETKDIMQEQLDAYKTSQePDA-----ASFEYICQALRQLALEAKGET----PSAVTRLSVVAIQEKSEP-- 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504416374 163 DEGPGAPERAAAPEAFGLFD--------------------------EAPGAPAASE-------AFGL------FDDAPGS 203
Cdd:PRK10547 151 QDESPRSQSGLRIILSRLKAgevdlleeelgnlgtltdvvkgadslEATLPGSVAEdditavlCFVIeadqitFETAVAA 230

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504416374 204 PPTEERAFGLFDGAPGSPAAPSAPAQAVAAPARGAVAPVRG--DGESGSIRVSVEKIDSLINLVGELVITQAMLGQLGEQ 281
Cdd:PRK10547 231 PQEKAEETTEVVEVSPKISVPPVLKLAAEQAPAGRVEREKTarSSESTSIRVAVEKVDQLINLVGELVITQSMLAQRSSE 310

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504416374 282 LDPSHHERLQHALAQLEHNTRDLQESVMSIRMLPINFIFSRFPRLVRDTATRLGKQVELHLHGEHTELDKSVIEKLSDPL 361
Cdd:PRK10547 311 LDPVNHGDLITSMGQLQRNARDLQESVMSIRMMPMEYVFSRFPRLVRDLAGKLGKQVELTLVGSSTELDKSLIERIIDPL 390

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504416374 362 THIVRNSIDHGIETPAERLAAGKPASGTVKLAASHQGGSVVVEVSDDGRGLSRPRILAKARERNLPVHDGMSDAEVWQLV 441
Cdd:PRK10547 391 THLVRNSLDHGIELPEKRLAAGKNSVGNLILSAEHQGGNICIEVTDDGAGLNRERILAKAASQGLAVSENMSDEEVGMLI 470

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504416374 442 FMPGFSTAETVTELSGRGVGMDVVKRNIGAMGGRIDIDSAPGMGTRIGIRLPLTLAILDGLIVAVEAVNYVIPLTYIVES 521
Cdd:PRK10547 471 FAPGFSTAEQVTDVSGRGVGMDVVKRNIQEMGGHVEIQSKQGKGTTIRILLPLTLAILDGMSVRVADEVFILPLNAVMES 550

                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504416374 522 LQARSDDVRGLGGeDNAMIRVRGEYLPLFSLHELLRIGGEAPAPEQGIVVILESEGRSFALQVDELVGQQQVVIKSLEQN 601
Cdd:PRK10547 551 LQPREEDLHPLAG-GERVLEVRGEYLPLVELWKVFDVAGAKTEATQGIVVILQSAGRRYALLVDQLIGQHQVVVKNLESN 629

                        650       660       670
                 ....*....|....*....|....*....|
gi 504416374 602 FRRVEGIAGATIMGDGSVALILDVDALPRL 631
Cdd:PRK10547 630 YRKVPGISAATILGDGSVALIVDVSALQAL 659
HATPase_CheA-like cd16916
Histidine kinase-like ATPase domain of the chemotaxis protein histidine kinase CheA, and some ...
 319-493 4.71e-97

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


Pssm-ID: 340393 [Multi-domain]  Cd Length: 178  Bit Score: 294.88  E-value: 4.71e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504416374 319 IFSRFPRLVRDTATRLGKQVELHLHGEHTELDKSVIEKLSDPLTHIVRNSIDHGIETPAERLAAGKPASGTVKLAASHQG 398
Cdd:cd16916    1 VFSRFPRLVRDLARELGKQVELVVEGEDTELDKSVLEKLADPLTHLLRNAVDHGIEAPEERLAAGKPPEGTITLRAEHQG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504416374 399 GSVVVEVSDDGRGLSRPRILAKARERNLPVHD---GMSDAEVWQLVFMPGFSTAETVTELSGRGVGMDVVKRNIGAMGGR 475
Cdd:cd16916   81 NQVVIEVSDDGRGIDREKIREKAIERGLITADeaaTLSDDEVLNLIFAPGFSTAEQVTDVSGRGVGMDVVKRSIESLGGT 160

                        170
                 ....*....|....*...
gi 504416374 476 IDIDSAPGMGTRIGIRLP 493
Cdd:cd16916  161 IEVESEPGQGTTFTIRLP 178
CheW smart00260
Two component signalling adaptor domain;
490-628 2.17e-26

Two component signalling adaptor domain;


Pssm-ID: 214588 [Multi-domain]  Cd Length: 138  Bit Score: 104.63  E-value: 2.17e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504416374   490 IRLPLTLAILDGLivaveavNYVIPLTYIVESLQARSDD-VRGLGGEDNAMIRVRGEYLPLFSLHELLRIGGEAPAPEqG 568
Cdd:smart00260   2 IRLPLTFAIGKDE-------TYAIPIAAVREILRPPPITpIPGAPGYVLGVINLRGEVLPVVDLRRLLGLPPEPPTDE-T 73

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 504416374   569 IVVILESEGRSFALQVDELVGQQQVVIKSLEQ----NFRRVEGIAGATIMGDGSVALILDVDAL 628
Cdd:smart00260  74 RVIVVETGDRKVGLVVDSVLGVREVVVKSIEPpppvSLSNAPGISGATILGDGRVVLILDVDKL 137
CheW pfam01584
CheW-like domain; CheW proteins are part of the chemotaxis signaling mechanism in bacteria. ...
 501-628 5.07e-26

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


Pssm-ID: 460257 [Multi-domain]  Cd Length: 131  Bit Score: 103.43  E-value: 5.07e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504416374  501 GLIVAVEAVNYVIPLTYIVESLQA-RSDDVRGLGGEDNAMIRVRGEYLPLFSLHELLRIGgEAPAPEQGIVVILESEGRS 579
Cdd:pfam01584   1 GLLFRLGGETFAIPISKVREILRPpPITPIPGAPGYVLGVINLRGEVLPVIDLRRLLGLP-PTEPRERTRVVVVEVGGQV 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 504416374  580 FALQVDELVGQQQVVIKSLEQNF---RRVEGIAGATIMGDGSVALILDVDAL 628
Cdd:pfam01584  80 VGLLVDEVIGVLEIVIKQIEPPLglgRVAGYISGATILGDGRVVLILDVEAL 131
 
Name Accession Description Interval E-value
CheA COG0643
Chemotaxis protein histidine kinase CheA [Signal transduction mechanisms];
4-639 0e+00

Chemotaxis protein histidine kinase CheA [Signal transduction mechanisms];


Pssm-ID: 440408 [Multi-domain]  Cd Length: 563  Bit Score: 712.34  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504416374   4 DMSQFLQVFFEETEEHLATLELLLIGLDLDRPDSETLHGIFRAAHSIKGSSGMFGFDDITAVTHELETLLDRIRCGQMGL 83
Cdd:COG0643    2 DMDELLEIFLEEARELLEQLEEGLLALEQDPDDPELLNAIFRAAHTLKGSAGMLGLDALAELAHALEDLLDALRNGELAL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504416374  84 RPDMISSFLEARDVLQRLLDAHRSGRPDPgvpllETVERLRGWLRAPEQEAAEEGFGLFDDAPTSPARETAdddafgffd 163
Cdd:COG0643   82 TPELIDLLLEALDALRALLDALEAGGEPP-----ADISALLARLDASEEAIEEVVADEVEISPPAPAALEP--------- 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504416374 164 egpgaperaaapeafglfdeapgapaaseafglfddAPGSPPTEERAfglfdgapgspaapsapaqavaapargAVAPVR 243
Cdd:COG0643  148 ------------------------------------APAAAPPAEAA---------------------------AAAAEA 164

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504416374 244 GDGESGSIRVSVEKIDSLINLVGELVITQAMLGQLGEQLDPSHHERLQHALAQLEHNTRDLQESVMSIRMLPINFIFSRF 323
Cdd:COG0643  165 AAAASETVRVDVERLDRLMNLVGELVITRARLEQLAEELEDESLRELEEALEQLSRLTRELQDGVMRLRMVPISTVFNRF 244

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504416374 324 PRLVRDTATRLGKQVELHLHGEHTELDKSVIEKLSDPLTHIVRNSIDHGIETPAERLAAGKPASGTVKLAASHQGGSVVV 403
Cdd:COG0643  245 PRMVRDLARELGKEVELVIEGEETELDRTVLERLGDPLVHLVRNAVDHGIETPEERLAAGKPETGTITLSAYHEGGRVVI 324

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504416374 404 EVSDDGRGLSRPRILAKARERNLPVHDG---MSDAEVWQLVFMPGFSTAETVTELSGRGVGMDVVKRNIGAMGGRIDIDS 480
Cdd:COG0643  325 EVSDDGRGLDLEKIRAKAIEKGLITAEEaaaLSDEELLELIFAPGFSTAEEVTDLSGRGVGMDVVKTNIEALGGTIEIES 404

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504416374 481 APGMGTRIGIRLPLTLAILDGLIVAVEAVNYVIPLTYIVESLQARSDDVRGLGGEDnaMIRVRGEYLPLFSLHELLRIGG 560
Cdd:COG0643  405 EPGKGTTFTLRLPLTLAIIDGLLVRVGGETYAIPLSSVEEVLRLDPDDIETVEGRE--VIRLRGELLPLVRLGELLGLPG 482

                        570       580       590       600       610       620       630
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 504416374 561 EAPAPEQGIVVILESEGRSFALQVDELVGQQQVVIKSLEQNFRRVEGIAGATIMGDGSVALILDVDALPRLAAREDTAD 639
Cdd:COG0643  483 AEPEGERGPVVVVRSGGRRVALVVDELLGQQEVVIKPLGPLLRRVPGISGATILGDGRVALILDVAALVRSARARARAA 561
PRK10547 PRK10547
chemotaxis protein CheA; Provisional
 4-631 0e+00

chemotaxis protein CheA; Provisional


Pssm-ID: 236712 [Multi-domain]  Cd Length: 670  Bit Score: 649.10  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504416374   4 DMSQFLQVFFEETEEHLATLELLLIGLDLDRPDSETLHGIFRAAHSIKGSSGMFGFDDITAVTHELETLLDRIRCGQMGL 83
Cdd:PRK10547   2 DISDFYQTFFDEADELLADMEQHLLVLDPEAPDAEQLNAIFRAAHSIKGGAGTFGFTVLQETTHLMENLLDEARRGEMQL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504416374  84 RPDMISSFLEARDVLQRLLDAHRSGR-PDPgvpllETVERLRGWLRAPEQEAAEEGfglfDDAPTSPARETADDDAFGff 162
Cdd:PRK10547  82 NTDIINLFLETKDIMQEQLDAYKTSQePDA-----ASFEYICQALRQLALEAKGET----PSAVTRLSVVAIQEKSEP-- 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504416374 163 DEGPGAPERAAAPEAFGLFD--------------------------EAPGAPAASE-------AFGL------FDDAPGS 203
Cdd:PRK10547 151 QDESPRSQSGLRIILSRLKAgevdlleeelgnlgtltdvvkgadslEATLPGSVAEdditavlCFVIeadqitFETAVAA 230

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504416374 204 PPTEERAFGLFDGAPGSPAAPSAPAQAVAAPARGAVAPVRG--DGESGSIRVSVEKIDSLINLVGELVITQAMLGQLGEQ 281
Cdd:PRK10547 231 PQEKAEETTEVVEVSPKISVPPVLKLAAEQAPAGRVEREKTarSSESTSIRVAVEKVDQLINLVGELVITQSMLAQRSSE 310

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504416374 282 LDPSHHERLQHALAQLEHNTRDLQESVMSIRMLPINFIFSRFPRLVRDTATRLGKQVELHLHGEHTELDKSVIEKLSDPL 361
Cdd:PRK10547 311 LDPVNHGDLITSMGQLQRNARDLQESVMSIRMMPMEYVFSRFPRLVRDLAGKLGKQVELTLVGSSTELDKSLIERIIDPL 390

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504416374 362 THIVRNSIDHGIETPAERLAAGKPASGTVKLAASHQGGSVVVEVSDDGRGLSRPRILAKARERNLPVHDGMSDAEVWQLV 441
Cdd:PRK10547 391 THLVRNSLDHGIELPEKRLAAGKNSVGNLILSAEHQGGNICIEVTDDGAGLNRERILAKAASQGLAVSENMSDEEVGMLI 470

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504416374 442 FMPGFSTAETVTELSGRGVGMDVVKRNIGAMGGRIDIDSAPGMGTRIGIRLPLTLAILDGLIVAVEAVNYVIPLTYIVES 521
Cdd:PRK10547 471 FAPGFSTAEQVTDVSGRGVGMDVVKRNIQEMGGHVEIQSKQGKGTTIRILLPLTLAILDGMSVRVADEVFILPLNAVMES 550

                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504416374 522 LQARSDDVRGLGGeDNAMIRVRGEYLPLFSLHELLRIGGEAPAPEQGIVVILESEGRSFALQVDELVGQQQVVIKSLEQN 601
Cdd:PRK10547 551 LQPREEDLHPLAG-GERVLEVRGEYLPLVELWKVFDVAGAKTEATQGIVVILQSAGRRYALLVDQLIGQHQVVVKNLESN 629

                        650       660       670
                 ....*....|....*....|....*....|
gi 504416374 602 FRRVEGIAGATIMGDGSVALILDVDALPRL 631
Cdd:PRK10547 630 YRKVPGISAATILGDGSVALIVDVSALQAL 659
HATPase_CheA-like cd16916
Histidine kinase-like ATPase domain of the chemotaxis protein histidine kinase CheA, and some ...
 319-493 4.71e-97

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


Pssm-ID: 340393 [Multi-domain]  Cd Length: 178  Bit Score: 294.88  E-value: 4.71e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504416374 319 IFSRFPRLVRDTATRLGKQVELHLHGEHTELDKSVIEKLSDPLTHIVRNSIDHGIETPAERLAAGKPASGTVKLAASHQG 398
Cdd:cd16916    1 VFSRFPRLVRDLARELGKQVELVVEGEDTELDKSVLEKLADPLTHLLRNAVDHGIEAPEERLAAGKPPEGTITLRAEHQG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504416374 399 GSVVVEVSDDGRGLSRPRILAKARERNLPVHD---GMSDAEVWQLVFMPGFSTAETVTELSGRGVGMDVVKRNIGAMGGR 475
Cdd:cd16916   81 NQVVIEVSDDGRGIDREKIREKAIERGLITADeaaTLSDDEVLNLIFAPGFSTAEQVTDVSGRGVGMDVVKRSIESLGGT 160

                        170
                 ....*....|....*...
gi 504416374 476 IDIDSAPGMGTRIGIRLP 493
Cdd:cd16916  161 IEVESEPGQGTTFTIRLP 178
CheA_reg cd00731
CheA regulatory domain; CheA is a histidine protein kinase present in bacteria and archea. ...
 496-628 4.90e-44

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


Pssm-ID: 238373 [Multi-domain]  Cd Length: 132  Bit Score: 153.87  E-value: 4.90e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504416374 496 LAILDGLIVAVEAVNYVIPLTYIVESLQARSDDVRGLGGEDNAmIRVRGEYLPLFSLHELLRIGGEAPAPEQGIVVILES 575
Cdd:cd00731    1 LAIIKGLLVRVGDETYAIPLSAVVETVRIKPKDIKRVDGGKEV-INVRGELLPLVRLGELFNVRGENEEPDEGVVVVVRT 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 504416374 576 EGRSFALQVDELVGQQQVVIKSLEQNFRRVEGIAGATIMGDGSVALILDVDAL 628
Cdd:cd00731   80 GGRKAALVVDQIIGQEEVVIKPLGGFLSNIPGISGATILGDGRVALILDVPAL 132
CheW smart00260
Two component signalling adaptor domain;
490-628 2.17e-26

Two component signalling adaptor domain;


Pssm-ID: 214588 [Multi-domain]  Cd Length: 138  Bit Score: 104.63  E-value: 2.17e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504416374   490 IRLPLTLAILDGLivaveavNYVIPLTYIVESLQARSDD-VRGLGGEDNAMIRVRGEYLPLFSLHELLRIGGEAPAPEqG 568
Cdd:smart00260   2 IRLPLTFAIGKDE-------TYAIPIAAVREILRPPPITpIPGAPGYVLGVINLRGEVLPVVDLRRLLGLPPEPPTDE-T 73

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 504416374   569 IVVILESEGRSFALQVDELVGQQQVVIKSLEQ----NFRRVEGIAGATIMGDGSVALILDVDAL 628
Cdd:smart00260  74 RVIVVETGDRKVGLVVDSVLGVREVVVKSIEPpppvSLSNAPGISGATILGDGRVVLILDVDKL 137
CheW pfam01584
CheW-like domain; CheW proteins are part of the chemotaxis signaling mechanism in bacteria. ...
 501-628 5.07e-26

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


Pssm-ID: 460257 [Multi-domain]  Cd Length: 131  Bit Score: 103.43  E-value: 5.07e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504416374  501 GLIVAVEAVNYVIPLTYIVESLQA-RSDDVRGLGGEDNAMIRVRGEYLPLFSLHELLRIGgEAPAPEQGIVVILESEGRS 579
Cdd:pfam01584   1 GLLFRLGGETFAIPISKVREILRPpPITPIPGAPGYVLGVINLRGEVLPVIDLRRLLGLP-PTEPRERTRVVVVEVGGQV 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 504416374  580 FALQVDELVGQQQVVIKSLEQNF---RRVEGIAGATIMGDGSVALILDVDAL 628
Cdd:pfam01584  80 VGLLVDEVIGVLEIVIKQIEPPLglgRVAGYISGATILGDGRVVLILDVEAL 131
CheW_like cd00588
CheW-like domain. CheW proteins are part of the chemotaxis signalling mechanism in bacteria. ...
 498-628 7.25e-24

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


Pssm-ID: 238331  Cd Length: 136  Bit Score: 97.34  E-value: 7.25e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504416374 498 ILDGLIVAVEAVNYVIPLTYIVESLQARSDD-VRGLGGEDNAMIRVRGEYLPLFSLHELLRIGGEAPAPEQGIVVILESE 576
Cdd:cd00588    1 ILQVLLFRVGDELYAIPIAVVEEILPLPPITrVPNAPDYVLGVINLRGEILPVIDLRRLFGLEAAEPDTDETRIVVVEVG 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 504416374 577 GRSFALQVDELVGQQQVVIKSLEQNF----RRVEGIAGATIMGDGSVALILDVDAL 628
Cdd:cd00588   81 DRKVGLVVDSVLGVLEVVIKDIEPPPdvgsSNAPGISGATILGDGRVVLILDVDKL 136
HATPase_c smart00387
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.
 359-495 1.27e-22

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


Pssm-ID: 214643 [Multi-domain]  Cd Length: 111  Bit Score: 93.10  E-value: 1.27e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504416374   359 DPLTHIVRNSIDHGIETPaerlaagkPASGTVKLAASHQGGSVVVEVSDDGRGLsrprilakarernlpvhdgmsDAEVW 438
Cdd:smart00387   4 DRLRQVLSNLLDNAIKYT--------PEGGRITVTLERDGDHVEITVEDNGPGI---------------------PPEDL 54

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 504416374   439 QLVFMPGFSTAETVTELSGRGVGMDVVKRNIGAMGGRIDIDSAPGMGTRIGIRLPLT 495
Cdd:smart00387  55 EKIFEPFFRTDKRSRKIGGTGLGLSIVKKLVELHGGEISVESEPGGGTTFTITLPLE 111
HPT cd00088
Histidine Phosphotransfer domain, involved in signalling through a two part component systems ...
 5-103 3.33e-21

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


Pssm-ID: 238041 [Multi-domain]  Cd Length: 94  Bit Score: 88.59  E-value: 3.33e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504416374   5 MSQFLQVFFEETEEHLATLELLLIGLDldrpDSETLHGIFRAAHSIKGSSGMFGFDDITAVTHELETLLDRIRCGQMgLR 84
Cdd:cd00088    1 MEELLELFLEEAEELLEELERALLELE----DAEDLNEIFRAAHTLKGSAASLGLQRLAQLAHQLEDLLDALRDGLE-VT 75

                         90
                 ....*....|....*....
gi 504416374  85 PDMISSFLEARDVLQRLLD 103
Cdd:cd00088   76 PELIDLLLDALDALKAELE 94
HPT smart00073
Histidine Phosphotransfer domain; Contains an active histidine residue that mediates ...
 7-99 3.54e-19

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


Pssm-ID: 197502 [Multi-domain]  Cd Length: 92  Bit Score: 82.68  E-value: 3.54e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504416374     7 QFLQVFFEETEEHLATLELLLIGLDLDrPDSETLHGIFRAAHSIKGSSGMFGFDDITAVTHELETLLDRIRCGQMGLRPD 86
Cdd:smart00073   1 GGLELFREELAEFLQSLEEGLLELEKA-LDAQDVNEIFRAAHTLKGSAGSLGLQQLAQLCHQLENLLDALRSGEVELTPD 79

                           90
                   ....*....|...
gi 504416374    87 MISSFLEARDVLQ 99
Cdd:smart00073  80 LLDLLLELVDVLK 92
H-kinase_dim pfam02895
Signal transducing histidine kinase, homodimeric domain; This helical bundle domain is the ...
 250-311 1.45e-18

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


Pssm-ID: 427045 [Multi-domain]  Cd Length: 66  Bit Score: 79.97  E-value: 1.45e-18
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 504416374  250 SIRVSVEKIDSLINLVGELVITQAMLGQLGEQL----DPSHHERLQHALAQLEHNTRDLQESVMSI 311
Cdd:pfam02895   1 TIRVDVEKLDRLMNLVGELVIARNRLVQLLERLeeygGDTLLEELKEALQQLDRLTRELQEAVMKI 66
KdpD COG2205
K+-sensing histidine kinase KdpD [Signal transduction mechanisms];
274-495 3.84e-16

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


Pssm-ID: 441807 [Multi-domain]  Cd Length: 239  Bit Score: 78.41  E-value: 3.84e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504416374 274 MLGQLGEQLDPSHHERLQHALAQLEH------NTRDL-----QESVMSIRMLPINFIFSRFPRLVRDTATRLGKQVELHL 342
Cdd:COG2205   40 LLLDEEDLSPEERRELLEIIRESAERllrlieDLLDLsrlesGKLSLELEPVDLAELLEEAVEELRPLAEEKGIRLELDL 119

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504416374 343 HGEHTEL--DKSVIEKLsdpLTHIVRNSIDHGietpaerlaagkPASGTVKLAASHQGGSVVVEVSDDGRGLSrprilAK 420
Cdd:COG2205  120 PPELPLVyaDPELLEQV---LANLLDNAIKYS------------PPGGTITISARREGDGVRISVSDNGPGIP-----EE 179

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 504416374 421 ARERnlpvhdgmsdaevwqlVFMPgFSTAETVTELSGRGVGMDVVKRNIGAMGGRIDIDSAPGMGTRIGIRLPLT 495
Cdd:COG2205  180 ELER----------------IFER-FYRGDNSRGEGGTGLGLAIVKRIVEAHGGTIWVESEPGGGTTFTVTLPLA 237
BaeS COG0642
Signal transduction histidine kinase [Signal transduction mechanisms];
272-495 1.91e-15

Signal transduction histidine kinase [Signal transduction mechanisms];


Pssm-ID: 440407 [Multi-domain]  Cd Length: 328  Bit Score: 78.03  E-value: 1.91e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504416374 272 QAMLGQLGEQLDPSHHERLQ---HALAQLEHNTRDL------QESVMSIRMLPINFIfsrfpRLVRDTATRL-----GKQ 337
Cdd:COG0642  129 RGYLELLLEELDEEQREYLEtilRSADRLLRLINDLldlsrlEAGKLELEPEPVDLA-----ELLEEVVELFrplaeEKG 203

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504416374 338 VELHLhgehtELDKSVIEKLSDP------LTHIVRNSIDHGietpaerlaagkPASGTVKLAASHQGGSVVVEVSDDGRG 411
Cdd:COG0642  204 IELEL-----DLPDDLPTVRGDPdrlrqvLLNLLSNAIKYT------------PEGGTVTVSVRREGDRVRISVEDTGPG 266

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504416374 412 LSrprilakarernlpvhdgmsdAEVWQLVFMPgFSTAETVTELSGRGVGMDVVKRNIGAMGGRIDIDSAPGMGTRIGIR 491
Cdd:COG0642  267 IP---------------------PEDLERIFEP-FFRTDPSRRGGGTGLGLAIVKRIVELHGGTIEVESEPGKGTTFTVT 324


                 ....
gi 504416374 492 LPLT 495
Cdd:COG0642  325 LPLA 328
HATPase_c pfam02518
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the ...
 358-495 2.50e-14

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: 69.32  E-value: 2.50e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504416374  358 SDPLTHIVRNSIDHGIEtpaerlAAGKPASGTVKLaasHQGGSVVVEVSDDGRGLSRPRIlakarernlpvhdgmsdaev 437
Cdd:pfam02518   3 ELRLRQVLSNLLDNALK------HAAKAGEITVTL---SEGGELTLTVEDNGIGIPPEDL-------------------- 53

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 504416374  438 wQLVFMPgFSTAETvTELSGRGVGMDVVKRNIGAMGGRIDIDSAPGMGTRIGIRLPLT 495
Cdd:pfam02518  54 -PRIFEP-FSTADK-RGGGGTGLGLSIVRKLVELLGGTITVESEPGGGTTVTLTLPLA 108
Hpt pfam01627
Hpt domain; The histidine-containing phosphotransfer (HPt) domain is a novel protein module ...
 7-108 1.49e-12

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


Pssm-ID: 426352 [Multi-domain]  Cd Length: 84  Bit Score: 63.52  E-value: 1.49e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504416374    7 QFLQVFFEETEEHLATLELLLigldldrpDSETLHGIFRAAHSIKGSSGMFGFDDITAVTHELETLLdriRCGQMGLRPD 86
Cdd:pfam01627   1 ELLELFLEEAPELLEQLEQAL--------DAEDLEALFRAAHTLKGSAGSLGLPALAELAHELEDLL---REGELPLDPE 69

                          90       100
                  ....*....|....*....|..
gi 504416374   87 MIssflearDVLQRLLDAHRSG 108
Cdd:pfam01627  70 LL-------EALRDLLEALRAA 84
NtrY COG5000
Signal transduction histidine kinase NtrY involved in nitrogen fixation and metabolism ...
 288-495 2.11e-11

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: 66.14  E-value: 2.11e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504416374 288 ERLQHALA-QLEHNTRDLQESVMSI-----RMlpINFI-----FSRFP----------RLVRDTATRLGKQVELHLHGEH 346
Cdd:COG5000  224 ERLRRKLAdKLEEDREDLERALDTIirqvdRL--KRIVdefldFARLPepqlepvdlnELLREVLALYEPALKEKDIRLE 301

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504416374 347 TELDKSVIEKLSDP------LTHIVRNSIDHGietpaerlaagkPASGTVKLAASHQGGSVVVEVSDDGRGLSrprilAK 420
Cdd:COG5000  302 LDLDPDLPEVLADRdqleqvLINLLKNAIEAI------------EEGGEIEVSTRREDGRVRIEVSDNGPGIP-----EE 364

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 504416374 421 ARERnlpvhdgmsdaevwqlVFMPGFSTAEtvtelSGRGVGMDVVKRNIGAMGGRIDIDSAPGMGTRIGIRLPLT 495
Cdd:COG5000  365 VLER----------------IFEPFFTTKP-----KGTGLGLAIVKKIVEEHGGTIELESRPGGGTTFTIRLPLA 418
PRK11086 PRK11086
sensory histidine kinase DcuS; Provisional
 350-493 4.83e-10

sensory histidine kinase DcuS; Provisional


Pssm-ID: 236839 [Multi-domain]  Cd Length: 542  Bit Score: 62.24  E-value: 4.83e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504416374 350 DKSVIEKLSDP-----LTHIVRNSIDHGIEtpaerlAAGKPASGTVKLAASHQGGSVVVEVSDDGRGLSRPRIlakarer 424
Cdd:PRK11086 418 EDSQLPDSGDEdqvheLITILGNLIENALE------AVGGEEGGEISVSLHYRNGWLHCEVSDDGPGIAPDEI------- 484

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 504416374 425 nlpvhdgmsdaevwQLVFMPGFSTAEtvtelSGRGVGMDVVKRNIGAMGGRIDIDSAPGMGTRIGIRLP 493
Cdd:PRK11086 485 --------------DAIFDKGYSTKG-----SNRGVGLYLVKQSVENLGGSIAVESEPGVGTQFFVQIP 534
CitA COG3290
Sensor histidine kinase DipB regulating citrate/malate metabolism [Signal transduction ...
 336-497 5.52e-10

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


Pssm-ID: 442519 [Multi-domain]  Cd Length: 389  Bit Score: 61.79  E-value: 5.52e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504416374 336 KQVELHLHgEHTELDKSVIEklSDPLTHIVRNSIDHGIEtpAerLAAGKPASGTVKLAASHQGGSVVVEVSDDGRGLsrp 415
Cdd:COG3290  260 RGIDLTID-IDSDLPDLPLS--DTDLVTILGNLLDNAIE--A--VEKLPEEERRVELSIRDDGDELVIEVEDSGPGI--- 329

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504416374 416 rilakarernlpvhdgmsDAEVWQLVFMPGFSTAETvtelSGRGVGMDVVKRNIGAMGGRIDIDSAPGMGTRIGIRLPLT 495
Cdd:COG3290  330 ------------------PEELLEKIFERGFSTKLG----EGRGLGLALVKQIVEKYGGTIEVESEEGEGTVFTVRLPKE 387


                 ..
gi 504416374 496 LA 497
Cdd:COG3290  388 GE 389
COG4191 COG4191
Signal transduction histidine kinase regulating C4-dicarboxylate transport system [Signal ...
 272-495 8.19e-10

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


Pssm-ID: 443345 [Multi-domain]  Cd Length: 361  Bit Score: 60.97  E-value: 8.19e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504416374 272 QAMLGQLGEQLDPshhERLQHALAQLEHNTRDLQESVMSIRMlpinfiFSR----------FPRLVRDTATRLGKQVELH 341
Cdd:COG4191  165 ELLRRRLEDEPDP---EELREALERILEGAERAAEIVRSLRA------FSRrdeeerepvdLNELIDEALELLRPRLKAR 235

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504416374 342 LHGEHTELDKSVIEKLSDP------LTHIVRNSIDhgietpaerlAAGKPASGTVKLAASHQGGSVVVEVSDDGRGLSrP 415
Cdd:COG4191  236 GIEVELDLPPDLPPVLGDPgqleqvLLNLLINAID----------AMEEGEGGRITISTRREGDYVVISVRDNGPGIP-P 304

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504416374 416 RILAKarernlpvhdgmsdaevwqlVFMPGFSTAEtvtELSGRGVGMDVVKRNIGAMGGRIDIDSAPGMGTRIGIRLPLT 495
Cdd:COG4191  305 EVLER--------------------IFEPFFTTKP---VGKGTGLGLSISYGIVEKHGGRIEVESEPGGGTTFTITLPLA 361
WalK COG5002
Sensor histidine kinase WalK [Signal transduction mechanisms];
294-494 1.89e-09

Sensor histidine kinase WalK [Signal transduction mechanisms];


Pssm-ID: 444026 [Multi-domain]  Cd Length: 390  Bit Score: 59.95  E-value: 1.89e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504416374 294 LAQLEHNTRDLQESVMSIRMLpINFIFSRFPRLVRDtatrlgKQVELHLHGEHTEL----DKSVIEKLsdpLTHIVRNSI 369
Cdd:COG5002  225 LSRLESGELKLEKEPVDLAEL-LEEVVEELRPLAEE------KGIELELDLPEDPLlvlgDPDRLEQV---LTNLLDNAI 294

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504416374 370 DHGietpaerlaagkPASGTVKLAASHQGGSVVVEVSDDGRGLS---RPRILakarERnlpvhdgmsdaevwqlvfmpgF 446
Cdd:COG5002  295 KYT------------PEGGTITVSLREEDDQVRISVRDTGIGIPeedLPRIF----ER---------------------F 337

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 504416374 447 STAETVT--ELSGRGVGMDVVKRNIGAMGGRIDIDSAPGMGTRIGIRLPL 494
Cdd:COG5002  338 YRVDKSRsrETGGTGLGLAIVKHIVEAHGGRIWVESEPGKGTTFTITLPL 387
HATPase_DpiB-CitA-like cd16915
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
 364-493 3.51e-08

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: 51.52  E-value: 3.51e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504416374 364 IVRNSIDHGIETPAERLAAGKpasgTVKLAASHQGGSVVVEVSDDGRGLsrprilakarernlpvhdgmsDAEVWQLVFM 443
Cdd:cd16915    4 IVGNLIDNALDALAATGAPNK----QVEVFLRDEGDDLVIEVRDTGPGI---------------------APELRDKVFE 58

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 504416374 444 PGFSTAETvtelSGRGVGMDVVKRNIGAMGGRIDIDSAPGMGTRIGIRLP 493
Cdd:cd16915   59 RGVSTKGQ----GERGIGLALVRQSVERLGGSITVESEPGGGTTFSIRIP 104
YesM COG2972
Sensor histidine kinase YesM [Signal transduction mechanisms];
364-495 5.57e-08

Sensor histidine kinase YesM [Signal transduction mechanisms];


Pssm-ID: 442211 [Multi-domain]  Cd Length: 445  Bit Score: 55.41  E-value: 5.57e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504416374 364 IVRNSIDHGIETpaerlaagKPASGTVKLAASHQGGSVVVEVSDDGRGlsrprilakarernlpvhdgMSDAEVWQLvfM 443
Cdd:COG2972  344 LVENAIEHGIEP--------KEGGGTIRISIRKEGDRLVITVEDNGVG--------------------MPEEKLEKL--L 393

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 504416374 444 PGFSTAEtvtelSGRGVGMDVVKRNIGAM---GGRIDIDSAPGMGTRIGIRLPLT 495
Cdd:COG2972  394 EELSSKG-----EGRGIGLRNVRERLKLYygeEYGLEIESEPGEGTTVTIRIPLE 443
NtrB COG3852
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms];
325-495 3.48e-07

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


Pssm-ID: 443061 [Multi-domain]  Cd Length: 361  Bit Score: 52.93  E-value: 3.48e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504416374 325 RLVRDTAtrlGKQVELHLhgehtELDKSVIEKLSDP------LTHIVRNSIDHGIETPAERLAAGkpASGTVKLAASHQG 398
Cdd:COG3852  215 ELLRAEA---PKNIRIVR-----DYDPSLPEVLGDPdqliqvLLNLVRNAAEAMPEGGTITIRTR--VERQVTLGGLRPR 284

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504416374 399 GSVVVEVSDDGRGLsrprilakarernlpvhdgmsDAEVWQLVFMPGFSTAEtvtelSGRGVGMDVVKRNIGAMGGRIDI 478
Cdd:COG3852  285 LYVRIEVIDNGPGI---------------------PEEILDRIFEPFFTTKE-----KGTGLGLAIVQKIVEQHGGTIEV 338

                        170
                 ....*....|....*..
gi 504416374 479 DSAPGMGTRIGIRLPLT 495
Cdd:COG3852  339 ESEPGKGTTFRIYLPLE 355
ComP COG4585
Signal transduction histidine kinase ComP [Signal transduction mechanisms];
259-495 8.78e-07

Signal transduction histidine kinase ComP [Signal transduction mechanisms];


Pssm-ID: 443642 [Multi-domain]  Cd Length: 252  Bit Score: 50.77  E-value: 8.78e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504416374 259 DSLINLVGELVITQAMLGQLGEQLDPSHHERLQHALAQLEHNTRDLQESVMSIRMLPINF--IFSRFPRLVRDTATRLGK 336
Cdd:COG4585   63 DGVGQSLSAIKLQLEAARRLLDADPEAAREELEEIRELAREALAELRRLVRGLRPPALDDlgLAAALEELAERLLRAAGI 142

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504416374 337 QVELHLHGEHTELDKSVieklSDPLTHIVR----NSIDHGietpaerlaagkPASgTVKLAASHQGGSVVVEVSDDGRGL 412
Cdd:COG4585  143 RVELDVDGDPDRLPPEV----ELALYRIVQealtNALKHA------------GAT-RVTVTLEVDDGELTLTVRDDGVGF 205

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504416374 413 SrprilakarernlpvhdgmsdaevwqlvfmpgfstaetVTELSGRGVGMDVVKRNIGAMGGRIDIDSAPGMGTRIGIRL 492
Cdd:COG4585  206 D--------------------------------------PEAAPGGGLGLRGMRERAEALGGTLTIGSAPGGGTRVRATL 247


                 ...
gi 504416374 493 PLT 495
Cdd:COG4585  248 PLA 250
PRK11360 PRK11360
two-component system sensor histidine kinase AtoS;
384-494 2.96e-06

two-component system sensor histidine kinase AtoS;


Pssm-ID: 236901 [Multi-domain]  Cd Length: 607  Bit Score: 50.35  E-value: 2.96e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504416374 384 KPASGTVKLAASHQG-GSVVVEVSDDGRGLsrprilakarernlpvhdgmsDAEVWQLVFMPGFSTAETvtelsGRGVGM 462
Cdd:PRK11360 516 ISARGKIRIRTWQYSdGQVAVSIEDNGCGI---------------------DPELLKKIFDPFFTTKAK-----GTGLGL 569

                         90       100       110
                 ....*....|....*....|....*....|..
gi 504416374 463 DVVKRNIGAMGGRIDIDSAPGMGTRIGIRLPL 494
Cdd:PRK11360 570 ALSQRIINAHGGDIEVESEPGVGTTFTLYLPI 601
CheW COG0835
Chemotaxis signal transduction protein CheW [Signal transduction mechanisms];
502-628 4.53e-06

Chemotaxis signal transduction protein CheW [Signal transduction mechanisms];


Pssm-ID: 440597  Cd Length: 151  Bit Score: 46.79  E-value: 4.53e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504416374 502 LIVAVEAVNYVIPLTYIVESLQARS--------DDVRGlggednaMIRVRGEYLPLFSLHELLRIgGEAPAPEQGIVVIL 573
Cdd:COG0835   11 LTFRLGGERYAIPIEKVREILPLPPitpvpgapPWVLG-------VINLRGRVVPVIDLRALLGL-PPTEDTERTRIIVL 82

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 504416374 574 ESEGRSFALQVDELVGQQQV---VIKSLEQNFRRVEG--IAGATIMGDGSVaLILDVDAL 628
Cdd:COG0835   83 EVGGRVVGLLVDSVSGVVRIdpdDIEPPPELLSGGLApfITGVAKLDDRLI-LLLDLEKL 141
HATPase_CckA-like cd16919
Histidine kinase-like ATPase domain of two-component sensor hybrid histidine kinases, similar ...
 394-493 5.50e-06

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: 45.83  E-value: 5.50e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504416374 394 ASHQGGSVVVEVSD---DGRGLSRPRILAKARERNLPVHD---GMSdAEVWQLVFMPGFSTAEtvtELSGRGVGMDVVKR 467
Cdd:cd16919   15 AMPEGGRLTIETSNqrvDADYALNYRDLIPGNYVCLEVSDtgsGMP-AEVLRRAFEPFFTTKE---VGKGTGLGLSMVYG 90

                         90       100
                 ....*....|....*....|....*.
gi 504416374 468 NIGAMGGRIDIDSAPGMGTRIGIRLP 493
Cdd:cd16919   91 FVKQSGGHLRIYSEPGVGTTVRIYLP 116
HATPase_YehU-like cd16956
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
 364-493 7.15e-06

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Escherichia coli YehU; This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component sensor histidine kinase (HKs) including Escherichia coli YehU, a HK of the two-component system (TCS) YehU-YehT which is involved in a nutrient sensing regulatory network. Proteins having this HATPase domain also contain a histidine kinase domain (His-kinase); some have a GAF sensor domain while some have a cupin domain.


Pssm-ID: 340432 [Multi-domain]  Cd Length: 101  Bit Score: 45.12  E-value: 7.15e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504416374 364 IVRNSIDHGIEtpaerlaaGKPASGTVKLAASHQGGSVVVEVSDDGRGLSrPRILAKARERnlpvhdgmsdaevwqlvfm 443
Cdd:cd16956    9 IVENAVKHGLS--------GLLDGGRVEITARLDGQHLLLEVEDNGGGMD-PDTLARILIR------------------- 60

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 504416374 444 pgfstaetvtelSGRGVGMDVVKRNIGAMGGR---IDIDSAPGMGTRIGIRLP 493
Cdd:cd16956   61 ------------SSNGLGLNLVDKRLRQAFGNdygLDIECAPGEGTRITIRLP 101
PRK10841 PRK10841
two-component system sensor histidine kinase RcsC;
428-502 7.84e-06

two-component system sensor histidine kinase RcsC;


Pssm-ID: 182772 [Multi-domain]  Cd Length: 924  Bit Score: 49.20  E-value: 7.84e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504416374 428 VHD---GMSDAEVWQLvFMPGFSTAETV-TELSGRGVGMDVVKRNIGAMGGRIDIDSAPGMGTRIGIRLPL------TLA 497
Cdd:PRK10841 598 VRDtgvGIPAKEVVRL-FDPFFQVGTGVqRNFQGTGLGLAICEKLINMMDGDISVDSEPGMGSQFTIRIPLygaqypQKK 676


                 ....*
gi 504416374 498 ILDGL 502
Cdd:PRK10841 677 GVEGL 681
KinA COG5805
Sporulation sensor histidine kinase A (Stage II sporulation protein SpoIIF/SpoIIJ) [Cell cycle ...
 325-495 1.27e-05

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: 48.19  E-value: 1.27e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504416374 325 RLVRDTATRLGKQVELH---LHGEHTE------LDKSVIEKLsdpLTHIVRNSIDhgietpaerlaaGKPASGTVKLAAS 395
Cdd:COG5805  358 ELIQDVVTLLETEAILHniqIRLELLDedpfiyCDENQIKQV---FINLIKNAIE------------AMPNGGTITIHTE 422

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504416374 396 HQGGSVVVEVSDDGRGLSrPRILAKARErnlpvhdgmsdaevwqlvfmPGFSTAEtvtelSGRGVGMDVVKRNIGAMGGR 475
Cdd:COG5805  423 EEDNSVIIRVIDEGIGIP-EERLKKLGE--------------------PFFTTKE-----KGTGLGLMVSYKIIENHNGT 476

                        170       180
                 ....*....|....*....|
gi 504416374 476 IDIDSAPGMGTRIGIRLPLT 495
Cdd:COG5805  477 IDIDSKVGKGTTFTITLPLS 496
HATPase_EvgS-ArcB-TorS-like cd16922
Histidine kinase-like ATPase domain of two-component sensor histidine kinases, many are hybrid ...
 389-494 2.15e-05

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: 44.02  E-value: 2.15e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504416374 389 TVKLAASHQGGSVV-VEVSDDGRGLSrprilakarernlpvhdgmsdAEVWQLVFMPgFSTAETVTE--LSGRGVGMDVV 465
Cdd:cd16922   24 RVSLEEEEEDGVQLrFSVEDTGIGIP---------------------EEQQARLFEP-FSQADSSTTrkYGGTGLGLAIS 81

                         90       100
                 ....*....|....*....|....*....
gi 504416374 466 KRNIGAMGGRIDIDSAPGMGTRIGIRLPL 494
Cdd:cd16922   82 KKLVELMGGDISVESEPGQGSTFTFTLPL 110
PRK13837 PRK13837
two-component system VirA-like sensor kinase;
393-495 2.79e-05

two-component system VirA-like sensor kinase;


Pssm-ID: 237526 [Multi-domain]  Cd Length: 828  Bit Score: 47.37  E-value: 2.79e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504416374 393 AASHQGGSVVVEVSDDGRGLSRPRILAKA-----RERNLPVHD---GMSDAeVWQLVFMPGFSTAEtvtelSGRGVGMDV 464
Cdd:PRK13837 572 AAQAMDGAGRVDISLSRAKLRAPKVLSHGvlppgRYVLLRVSDtgaGIDEA-VLPHIFEPFFTTRA-----GGTGLGLAT 645

                         90       100       110
                 ....*....|....*....|....*....|.
gi 504416374 465 VKRNIGAMGGRIDIDSAPGMGTRIGIRLPLT 495
Cdd:PRK13837 646 VHGIVSAHAGYIDVQSTVGRGTRFDVYLPPS 676
HATPase_AtoS-like cd16943
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
 389-494 3.86e-05

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: 43.18  E-value: 3.86e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504416374 389 TVKLAASHQggSVVVEVSDDGRGLsrprilakarernlpvhdgmsDAEVWQLVFMPGFSTAETVTelsGRGVGMDVVKRN 468
Cdd:cd16943   26 TIRTWAHVD--QVLIEVEDTGSGI---------------------DPEILGRIFDPFFTTKPVGE---GTGLGLSLSYRI 79

                         90       100
                 ....*....|....*....|....*.
gi 504416374 469 IGAMGGRIDIDSAPGMGTRIGIRLPL 494
Cdd:cd16943   80 IQKHGGTIRVASVPGGGTRFTIILPI 105
COG4251 COG4251
Bacteriophytochrome (light-regulated signal transduction histidine kinase) [Signal ...
 57-493 6.27e-05

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


Pssm-ID: 443393 [Multi-domain]  Cd Length: 503  Bit Score: 45.93  E-value: 6.27e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504416374  57 FGFDDITAVTHELETLLDRIRCGQMGLRPDMISSFLEARDVLQRLLDAHRSGRPDPGVPLLETVERLRGWLRAPEQEAAE 136
Cdd:COG4251   43 LLLLLIRLLLLLLLSLLALLLLLLLLLLLLLVLAALALLLLLLLLELALVLLALLLVLLLLLALLLLLALLLLLELLLLL 122

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504416374 137 EGFGLFDDAPTSPARETADDDAFGFFDEGPGAPERAAAPEAFGLFDEAPGAPAASEAFGLFDDAPGSPPTEERAFGLFDG 216
Cdd:COG4251  123 LALLLLLLLLALLLLEELALLRLALALLLLLLLLLLLLLLLLALILALLLAALAELELLLLLLLVLLLLLLLLLLLLLLL 202

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504416374 217 APGSPAAPSAPAQAVAAPARGAVAPVRGDGESGSIRVSVEKIDSLINLVGELVITQAMLGQLGEQLDpSHHERLQHALAQ 296
Cdd:COG4251  203 LRLLLELLLLLEAELLLSLGGGLGLLLLLLLLLVLLLLLILLLLLLILVLELLELRLELEELEEELE-ERTAELERSNEE 281

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504416374 297 LE-------HntrDLQESVMSIRMLpINFIFSRFP-----------RLVRDTATRLGKQVE----------LHLHGEHTE 348
Cdd:COG4251  282 LEqfayvasH---DLREPLRKISGF-SQLLEEDYGdkldeegreylERIRDAAERMQALIDdllaysrvgrQELEFEPVD 357

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504416374 349 LD---KSVIEKLS--------------------DP------LTHIVRNSIDHGietpaerlaaGKPASGTVKLAASHQGG 399
Cdd:COG4251  358 LNellEEVLEDLEprieergaeievgplptvrgDPtllrqvFQNLISNAIKYS----------RPGEPPRIEIGAEREGG 427

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504416374 400 SVVVEVSDDGRGlsrprILAKARERnlpvhdgmsdaevwqlVFMPgFSTAETVTELSGRGVGMDVVKRNIGAMGGRIDID 479
Cdd:COG4251  428 EWVFSVRDNGIG-----IDPEYAEK----------------IFEI-FQRLHSRDEYEGTGIGLAIVKKIVERHGGRIWVE 485

                        490
                 ....*....|....
gi 504416374 480 SAPGMGTRIGIRLP 493
Cdd:COG4251  486 SEPGEGATFYFTLP 499
HATPase_FilI-like cd16921
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
 434-493 1.85e-04

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: 41.16  E-value: 1.85e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 504416374 434 DAEVWQLVFMPgFSTAETVTELSGRGVGMDVVKRNIGAMGGRIDIDSAPGMGTRIGIRLP 493
Cdd:cd16921   47 DPEYAEKVFGI-FQRLHSREEYEGTGVGLAIVRKIIERHGGRIWLESEPGEGTTFYFTLP 105
HATPase_RstB-like cd16939
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
 386-494 3.73e-04

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: 40.11  E-value: 3.73e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504416374 386 ASGTVKLAASHQGGSVVVEVSDDGrglsrPRILAKARERnlpvhdgmsdaevwqlVFMPGFSTAETVTELS-GRGVGMDV 464
Cdd:cd16939   16 AHRTVRIALLVSGGRLTLIVEDDG-----PGIPAAARER----------------VFEPFVRLDPSRDRATgGFGLGLAI 74

                         90       100       110
                 ....*....|....*....|....*....|
gi 504416374 465 VKRNIGAMGGRIDIDSAPGMGTRIGIRLPL 494
Cdd:cd16939   75 VHRVALWHGGHVECDDSELGGACFRLTWPR 104
PRK10364 PRK10364
two-component system sensor histidine kinase ZraS;
385-494 5.54e-04

two-component system sensor histidine kinase ZraS;


Pssm-ID: 236674 [Multi-domain]  Cd Length: 457  Bit Score: 42.85  E-value: 5.54e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504416374 385 PASGTVKLAASHQGGSVVVEVSDDGRGLSrprilakarernlpvhdgmsdAEVWQLVFMPGFSTaetvtELSGRGVGMDV 464
Cdd:PRK10364 365 GQHGVISVTASESGAGVKISVTDSGKGIA---------------------ADQLEAIFTPYFTT-----KAEGTGLGLAV 418

                         90       100       110
                 ....*....|....*....|....*....|
gi 504416374 465 VKRNIGAMGGRIDIDSAPGMGTRIGIRLPL 494
Cdd:PRK10364 419 VHNIVEQHGGTIQVASQEGKGATFTLWLPV 448
HATPase_NtrY-like cd16944
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
 357-493 6.95e-04

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


Pssm-ID: 340420 [Multi-domain]  Cd Length: 108  Bit Score: 39.44  E-value: 6.95e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504416374 357 LSDPLTHIVRNSIDhgietPAERLAAGKPaSGTVKLAAShQGGSVVVEVSDDGRGLSrPRILAKARErnlpvhdgmsdae 436
Cdd:cd16944    5 ISQVLTNILKNAAE-----AIEGRPSDVG-EVRIRVEAD-QDGRIVLIVCDNGKGFP-REMRHRATE------------- 63

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 504416374 437 vwqlvfmPGFSTAEtvtelSGRGVGMDVVKRNIGAMGGRIDIDSAPGMGTRIGIRLP 493
Cdd:cd16944   64 -------PYVTTRP-----KGTGLGLAIVKKIMEEHGGRISLSNREAGGACIRIILP 108
PRK11100 PRK11100
sensory histidine kinase CreC; Provisional
 288-494 8.43e-04

sensory histidine kinase CreC; Provisional


Pssm-ID: 236846 [Multi-domain]  Cd Length: 475  Bit Score: 42.14  E-value: 8.43e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504416374 288 ERLQH------ALAQLEhNTRDLQEsvmsirMLPINFifsrfPRLVRDTATRL-----GKQVELHLHGEHTELdksviek 356
Cdd:PRK11100 302 ARLQQlidrllELARLE-QRQELEV------LEPVAL-----AALLEELVEAReaqaaAKGITLRLRPDDARV------- 362

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504416374 357 LSDP------LTHIVRNSIDHgietpaerlaagKPASGTVKLAASHQGGSVVVEVSDDGrglsrPRILAKARERnlpvhd 430
Cdd:PRK11100 363 LGDPfllrqaLGNLLDNAIDF------------SPEGGTITLSAEVDGEQVALSVEDQG-----PGIPDYALPR------ 419

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 504416374 431 gmsdaevwqlVFMPGFSTAETVTELSGRGVGMDVVKRNIGAMGGRIDIDSAPGMGTRIGIRLPL 494
Cdd:PRK11100 420 ----------IFERFYSLPRPANGRKSTGLGLAFVREVARLHGGEVTLRNRPEGGVLATLTLPR 473
HATPase_CpxA-like cd16949
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
 357-494 1.37e-03

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: 38.46  E-value: 1.37e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504416374 357 LSDPLTHIVRNSIDHgietpaerlaagkpASGTVKLAASHQGGSVVVEVSDDGRGLSrprilakarernlpvhdgmsDAE 436
Cdd:cd16949    1 LARALENVLRNALRY--------------SPSKILLDISQDGDQWTITITDDGPGVP--------------------EDQ 46

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 504416374 437 VWQLvFMPGFSTAETVT-ELSGRGVGMDVVKRNIGAMGGRIDIDSAPGMGTRIGIRLPL 494
Cdd:cd16949   47 LEQI-FLPFYRVDSARDrESGGTGLGLAIAERAIEQHGGKIKASNRKPGGLRVRIWLPA 104
HATPase_TmoS-FixL-DctS-like cd16920
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
 403-493 4.78e-03

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: 36.99  E-value: 4.78e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504416374 403 VEVSDDGRGLSRPRILAKARERNLPVHD---GMSDAEVWQLvFMPGFSTaetvtELSGRGVGMDVVKRNIGAMGGRIDID 479
Cdd:cd16920   17 SEGGCERRELTIRTSPADDRAVTISVKDtgpGIAEEVAGQL-FDPFYTT-----KSEGLGMGLSICRSIIEAHGGRLSVE 90

                         90
                 ....*....|....
gi 504416374 480 SAPGMGTRIGIRLP 493
Cdd:cd16920   91 SPAGGGATFQFTLP 104
KinE COG5809
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome ...
 309-494 6.42e-03

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: 39.57  E-value: 6.42e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504416374 309 MSIRMLPINFIFSRFPRLVRDTATRLGKQVELHLH-------GEHTELdKSVIeklsdplTHIVRNSIDhgietpaerlA 381
Cdd:COG5809  333 IKYEPKDLNTLIEEVIPLLQPQALLKNVQIELELEddipdilGDENQL-KQVF-------INLLKNAIE----------A 394

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504416374 382 AGKPASGTVKLAAsHQGGSVVVEVSDDGRGLSRPRIlakarernlpvhdgmsdaevwQLVFMPGFSTAETvtelsGRGVG 461
Cdd:COG5809  395 MPEGGNITIETKA-EDDDKVVISVTDEGCGIPEERL---------------------KKLGEPFYTTKEK-----GTGLG 447

                        170       180       190
                 ....*....|....*....|....*....|...
gi 504416374 462 MDVVKRNIGAMGGRIDIDSAPGMGTRIGIRLPL 494
Cdd:COG5809  448 LMVSYKIIEEHGGKITVESEVGKGTTFSITLPI 480
HATPase_BceS-YxdK-YvcQ-like cd16948
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
 396-493 9.00e-03

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: 36.49  E-value: 9.00e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504416374 396 HQGGSVVVEVSDDGRGLSrprilakarERNLPvhdgmsdaevwqLVFMPGFSTAETVTELSGRGVGMDVVKRNIGAMGGR 475
Cdd:cd16948   33 TNEQGVVLSIKDFGIGIP---------EEDLP------------RVFDKGFTGENGRNFQESTGMGLYLVKKLCDKLGHK 91

                         90
                 ....*....|....*...
gi 504416374 476 IDIDSAPGMGTRIGIRLP 493
Cdd:cd16948   92 IDVESEVGEGTTFTITFP 109
 
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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