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Conserved domains on  [gi|1278882189|gb|PJD69535|]
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chemotaxis protein CheA [Enterobacter kobei]

Protein Classification

chemotaxis protein CheA( domain architecture ID 11484784)

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK10547 PRK10547
chemotaxis protein CheA; Provisional
 3-682 0e+00

chemotaxis protein CheA; Provisional


:

Pssm-ID: 236712 [Multi-domain]  Cd Length: 670  Bit Score: 1367.11  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278882189   3 MDISDFYQTFFDEADELLADMEQHLLDLVPEAPDSEQLNAIFRAAHSIKGGAGTFGFTILQETTHLMENLLDEARRGEMQ 82
Cdd:PRK10547    1 MDISDFYQTFFDEADELLADMEQHLLVLDPEAPDAEQLNAIFRAAHSIKGGAGTFGFTVLQETTHLMENLLDEARRGEMQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278882189  83 LNTDIINLFLETKDIMQEQLDAYKSSAEPDAASFEYICNALRQLALEAKGEVAAAVVPAAKLSVVDAVGAGETAPAAAqa 162
Cdd:PRK10547   81 LNTDIINLFLETKDIMQEQLDAYKTSQEPDAASFEYICQALRQLALEAKGETPSAVTRLSVVAIQEKSEPQDESPRSQ-- 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278882189 163 GKLRVVLSRLKENEVNLLEEELGNLATLSNVVKGKDSLAATLDDGIGQDDIVAVLCFVIEADQIAFETETETETAEAEAP 242
Cdd:PRK10547  159 SGLRIILSRLKAGEVDLLEEELGNLGTLTDVVKGADSLEATLPGSVAEDDITAVLCFVIEADQITFETAVAAPQEKAEET 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278882189 243 VAQEEVAviaqapTPAVAPAAPALKAVPKDAAAPARgEKPAaRSSESTSIRVAVEKVDQLINLVGELVITQSMLAQRSNE 322
Cdd:PRK10547  239 TEVVEVS------PKISVPPVLKLAAEQAPAGRVER-EKTA-RSSESTSIRVAVEKVDQLINLVGELVITQSMLAQRSSE 310

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278882189 323 LDPVTHGDLITSMGQLQRNARDLQESVMSIRMMPMEYVFSRFPRLVRDLASKLNKQIELTLMGSSTELDKSLIERIIDPL 402
Cdd:PRK10547  311 LDPVNHGDLITSMGQLQRNARDLQESVMSIRMMPMEYVFSRFPRLVRDLAGKLGKQVELTLVGSSTELDKSLIERIIDPL 390

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278882189 403 THLVRNSLDHGIELPENRIAAGKSPVGNLILSAEHQGGNICIEVTDDGAGLNRERILAKAISQGMAVNENMTDEEVGMLI 482
Cdd:PRK10547  391 THLVRNSLDHGIELPEKRLAAGKNSVGNLILSAEHQGGNICIEVTDDGAGLNRERILAKAASQGLAVSENMSDEEVGMLI 470

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278882189 483 FAPGFSTAEQVTDVSGRGVGMDVVKRNIQEMGGHVEIQSKQGSGTTIRILLPLTLAILDGMSVKVADEVFILPLNAVMES 562
Cdd:PRK10547  471 FAPGFSTAEQVTDVSGRGVGMDVVKRNIQEMGGHVEIQSKQGKGTTIRILLPLTLAILDGMSVRVADEVFILPLNAVMES 550

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278882189 563 LQPREEDLHPLAGGERVLEVRGEYLPLVELWKVFEVDGAKTEATQGIVVILQSAGRRYALLVDQLIGQHQVVVKNLESNY 642
Cdd:PRK10547  551 LQPREEDLHPLAGGERVLEVRGEYLPLVELWKVFDVAGAKTEATQGIVVILQSAGRRYALLVDQLIGQHQVVVKNLESNY 630

                         650       660       670       680
                  ....*....|....*....|....*....|....*....|
gi 1278882189 643 RKVPGISAATILGDGSVALIVDVSALQGLNREQRVAYTAA 682
Cdd:PRK10547  631 RKVPGISAATILGDGSVALIVDVSALQALNREQRMANTAA 670
 
Name Accession Description Interval E-value
PRK10547 PRK10547
chemotaxis protein CheA; Provisional
 3-682 0e+00

chemotaxis protein CheA; Provisional


Pssm-ID: 236712 [Multi-domain]  Cd Length: 670  Bit Score: 1367.11  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278882189   3 MDISDFYQTFFDEADELLADMEQHLLDLVPEAPDSEQLNAIFRAAHSIKGGAGTFGFTILQETTHLMENLLDEARRGEMQ 82
Cdd:PRK10547    1 MDISDFYQTFFDEADELLADMEQHLLVLDPEAPDAEQLNAIFRAAHSIKGGAGTFGFTVLQETTHLMENLLDEARRGEMQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278882189  83 LNTDIINLFLETKDIMQEQLDAYKSSAEPDAASFEYICNALRQLALEAKGEVAAAVVPAAKLSVVDAVGAGETAPAAAqa 162
Cdd:PRK10547   81 LNTDIINLFLETKDIMQEQLDAYKTSQEPDAASFEYICQALRQLALEAKGETPSAVTRLSVVAIQEKSEPQDESPRSQ-- 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278882189 163 GKLRVVLSRLKENEVNLLEEELGNLATLSNVVKGKDSLAATLDDGIGQDDIVAVLCFVIEADQIAFETETETETAEAEAP 242
Cdd:PRK10547  159 SGLRIILSRLKAGEVDLLEEELGNLGTLTDVVKGADSLEATLPGSVAEDDITAVLCFVIEADQITFETAVAAPQEKAEET 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278882189 243 VAQEEVAviaqapTPAVAPAAPALKAVPKDAAAPARgEKPAaRSSESTSIRVAVEKVDQLINLVGELVITQSMLAQRSNE 322
Cdd:PRK10547  239 TEVVEVS------PKISVPPVLKLAAEQAPAGRVER-EKTA-RSSESTSIRVAVEKVDQLINLVGELVITQSMLAQRSSE 310

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278882189 323 LDPVTHGDLITSMGQLQRNARDLQESVMSIRMMPMEYVFSRFPRLVRDLASKLNKQIELTLMGSSTELDKSLIERIIDPL 402
Cdd:PRK10547  311 LDPVNHGDLITSMGQLQRNARDLQESVMSIRMMPMEYVFSRFPRLVRDLAGKLGKQVELTLVGSSTELDKSLIERIIDPL 390

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278882189 403 THLVRNSLDHGIELPENRIAAGKSPVGNLILSAEHQGGNICIEVTDDGAGLNRERILAKAISQGMAVNENMTDEEVGMLI 482
Cdd:PRK10547  391 THLVRNSLDHGIELPEKRLAAGKNSVGNLILSAEHQGGNICIEVTDDGAGLNRERILAKAASQGLAVSENMSDEEVGMLI 470

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278882189 483 FAPGFSTAEQVTDVSGRGVGMDVVKRNIQEMGGHVEIQSKQGSGTTIRILLPLTLAILDGMSVKVADEVFILPLNAVMES 562
Cdd:PRK10547  471 FAPGFSTAEQVTDVSGRGVGMDVVKRNIQEMGGHVEIQSKQGKGTTIRILLPLTLAILDGMSVRVADEVFILPLNAVMES 550

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278882189 563 LQPREEDLHPLAGGERVLEVRGEYLPLVELWKVFEVDGAKTEATQGIVVILQSAGRRYALLVDQLIGQHQVVVKNLESNY 642
Cdd:PRK10547  551 LQPREEDLHPLAGGERVLEVRGEYLPLVELWKVFDVAGAKTEATQGIVVILQSAGRRYALLVDQLIGQHQVVVKNLESNY 630

                         650       660       670       680
                  ....*....|....*....|....*....|....*....|
gi 1278882189 643 RKVPGISAATILGDGSVALIVDVSALQGLNREQRVAYTAA 682
Cdd:PRK10547  631 RKVPGISAATILGDGSVALIVDVSALQALNREQRMANTAA 670
CheA COG0643
Chemotaxis protein histidine kinase CheA [Signal transduction mechanisms];
3-681 0e+00

Chemotaxis protein histidine kinase CheA [Signal transduction mechanisms];


Pssm-ID: 440408 [Multi-domain]  Cd Length: 563  Bit Score: 709.26  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278882189   3 MDISDFYQTFFDEADELLADMEQHLLDLVPEAPDSEQLNAIFRAAHSIKGGAGTFGFTILQETTHLMENLLDEARRGEMQ 82
Cdd:COG0643     1 MDMDELLEIFLEEARELLEQLEEGLLALEQDPDDPELLNAIFRAAHTLKGSAGMLGLDALAELAHALEDLLDALRNGELA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278882189  83 LNTDIINLFLETKDIMQEQLDAYKSSAEPDAAsFEYICNALRQLALEAKGEvaaavvpaaklsVVDAVGAGETAPAAAQA 162
Cdd:COG0643    81 LTPELIDLLLEALDALRALLDALEAGGEPPAD-ISALLARLDASEEAIEEV------------VADEVEISPPAPAALEP 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278882189 163 GKlrvvlsrlkenevnlleeelgnlatlsnvvkgkdslaatlddgigqddivavlcfvieadqiafetetetetaeaeap 242
Cdd:COG0643   148 AP------------------------------------------------------------------------------ 149

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278882189 243 vaqeevaviaqaptpavapaapalkavPKDAAAPARGEKPAARSSESTSIRVAVEKVDQLINLVGELVITQSMLAQRSNE 322
Cdd:COG0643   150 ---------------------------AAAPPAEAAAAAAEAAAAASETVRVDVERLDRLMNLVGELVITRARLEQLAEE 202

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278882189 323 LDPVTHGDLITSMGQLQRNARDLQESVMSIRMMPMEYVFSRFPRLVRDLASKLNKQIELTLMGSSTELDKSLIERIIDPL 402
Cdd:COG0643   203 LEDESLRELEEALEQLSRLTRELQDGVMRLRMVPISTVFNRFPRMVRDLARELGKEVELVIEGEETELDRTVLERLGDPL 282

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278882189 403 THLVRNSLDHGIELPENRIAAGKSPVGNLILSAEHQGGNICIEVTDDGAGLNRERILAKAISQGM---AVNENMTDEEVG 479
Cdd:COG0643   283 VHLVRNAVDHGIETPEERLAAGKPETGTITLSAYHEGGRVVIEVSDDGRGLDLEKIRAKAIEKGLitaEEAAALSDEELL 362

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278882189 480 MLIFAPGFSTAEQVTDVSGRGVGMDVVKRNIQEMGGHVEIQSKQGSGTTIRILLPLTLAILDGMSVKVADEVFILPLNAV 559
Cdd:COG0643   363 ELIFAPGFSTAEEVTDLSGRGVGMDVVKTNIEALGGTIEIESEPGKGTTFTLRLPLTLAIIDGLLVRVGGETYAIPLSSV 442

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278882189 560 MESLQPREEDLHPLAGGErVLEVRGEYLPLVELWKVFEVDGAKTEATQGIVVILQSAGRRYALLVDQLIGQHQVVVKNLE 639
Cdd:COG0643   443 EEVLRLDPDDIETVEGRE-VIRLRGELLPLVRLGELLGLPGAEPEGERGPVVVVRSGGRRVALVVDELLGQQEVVIKPLG 521

                         650       660       670       680
                  ....*....|....*....|....*....|....*....|..
gi 1278882189 640 SNYRKVPGISAATILGDGSVALIVDVSALQGLNREQRVAYTA 681
Cdd:COG0643   522 PLLRRVPGISGATILGDGRVALILDVAALVRSARARARAAAA 563
HATPase_CheA-like cd16916
Histidine kinase-like ATPase domain of the chemotaxis protein histidine kinase CheA, and some ...
 360-534 1.83e-95

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: 292.18  E-value: 1.83e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278882189 360 VFSRFPRLVRDLASKLNKQIELTLMGSSTELDKSLIERIIDPLTHLVRNSLDHGIELPENRIAAGKSPVGNLILSAEHQG 439
Cdd:cd16916     1 VFSRFPRLVRDLARELGKQVELVVEGEDTELDKSVLEKLADPLTHLLRNAVDHGIEAPEERLAAGKPPEGTITLRAEHQG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278882189 440 GNICIEVTDDGAGLNRERILAKAISQGMAVNE---NMTDEEVGMLIFAPGFSTAEQVTDVSGRGVGMDVVKRNIQEMGGH 516
Cdd:cd16916    81 NQVVIEVSDDGRGIDREKIREKAIERGLITADeaaTLSDDEVLNLIFAPGFSTAEQVTDVSGRGVGMDVVKRSIESLGGT 160

                         170
                  ....*....|....*...
gi 1278882189 517 VEIQSKQGSGTTIRILLP 534
Cdd:cd16916   161 IEVESEPGQGTTFTIRLP 178
CheW smart00260
Two component signalling adaptor domain;
530-668 5.13e-28

Two component signalling adaptor domain;


Pssm-ID: 214588 [Multi-domain]  Cd Length: 138  Bit Score: 109.64  E-value: 5.13e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278882189  530 RILLPLTLAILDgmsvkvaDEVFILPLNAVMESLQPREEDL--HPLAGGERVLEVRGEYLPLVELWKVFEVDGAKTEAtQ 607
Cdd:smart00260   1 TIRLPLTFAIGK-------DETYAIPIAAVREILRPPPITPipGAPGYVLGVINLRGEVLPVVDLRRLLGLPPEPPTD-E 72

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1278882189  608 GIVVILQSAGRRYALLVDQLIGQHQVVVKNLES----NYRKVPGISAATILGDGSVALIVDVSAL 668
Cdd:smart00260  73 TRVIVVETGDRKVGLVVDSVLGVREVVVKSIEPpppvSLSNAPGISGATILGDGRVVLILDVDKL 137
CheW pfam01584
CheW-like domain; CheW proteins are part of the chemotaxis signaling mechanism in bacteria. ...
 542-668 3.07e-27

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: 106.90  E-value: 3.07e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278882189 542 GMSVKVADEVFILPLNAVMESLQPREEDLHPLAGG--ERVLEVRGEYLPLVELWKVFEVDGAKTEaTQGIVVILQSAGRR 619
Cdd:pfam01584   1 GLLFRLGGETFAIPISKVREILRPPPITPIPGAPGyvLGVINLRGEVLPVIDLRRLLGLPPTEPR-ERTRVVVVEVGGQV 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1278882189 620 YALLVDQLIGQHQVVVKNLESNY---RKVPGISAATILGDGSVALIVDVSAL 668
Cdd:pfam01584  80 VGLLVDEVIGVLEIVIKQIEPPLglgRVAGYISGATILGDGRVVLILDVEAL 131
 
Name Accession Description Interval E-value
PRK10547 PRK10547
chemotaxis protein CheA; Provisional
 3-682 0e+00

chemotaxis protein CheA; Provisional


Pssm-ID: 236712 [Multi-domain]  Cd Length: 670  Bit Score: 1367.11  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278882189   3 MDISDFYQTFFDEADELLADMEQHLLDLVPEAPDSEQLNAIFRAAHSIKGGAGTFGFTILQETTHLMENLLDEARRGEMQ 82
Cdd:PRK10547    1 MDISDFYQTFFDEADELLADMEQHLLVLDPEAPDAEQLNAIFRAAHSIKGGAGTFGFTVLQETTHLMENLLDEARRGEMQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278882189  83 LNTDIINLFLETKDIMQEQLDAYKSSAEPDAASFEYICNALRQLALEAKGEVAAAVVPAAKLSVVDAVGAGETAPAAAqa 162
Cdd:PRK10547   81 LNTDIINLFLETKDIMQEQLDAYKTSQEPDAASFEYICQALRQLALEAKGETPSAVTRLSVVAIQEKSEPQDESPRSQ-- 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278882189 163 GKLRVVLSRLKENEVNLLEEELGNLATLSNVVKGKDSLAATLDDGIGQDDIVAVLCFVIEADQIAFETETETETAEAEAP 242
Cdd:PRK10547  159 SGLRIILSRLKAGEVDLLEEELGNLGTLTDVVKGADSLEATLPGSVAEDDITAVLCFVIEADQITFETAVAAPQEKAEET 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278882189 243 VAQEEVAviaqapTPAVAPAAPALKAVPKDAAAPARgEKPAaRSSESTSIRVAVEKVDQLINLVGELVITQSMLAQRSNE 322
Cdd:PRK10547  239 TEVVEVS------PKISVPPVLKLAAEQAPAGRVER-EKTA-RSSESTSIRVAVEKVDQLINLVGELVITQSMLAQRSSE 310

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278882189 323 LDPVTHGDLITSMGQLQRNARDLQESVMSIRMMPMEYVFSRFPRLVRDLASKLNKQIELTLMGSSTELDKSLIERIIDPL 402
Cdd:PRK10547  311 LDPVNHGDLITSMGQLQRNARDLQESVMSIRMMPMEYVFSRFPRLVRDLAGKLGKQVELTLVGSSTELDKSLIERIIDPL 390

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278882189 403 THLVRNSLDHGIELPENRIAAGKSPVGNLILSAEHQGGNICIEVTDDGAGLNRERILAKAISQGMAVNENMTDEEVGMLI 482
Cdd:PRK10547  391 THLVRNSLDHGIELPEKRLAAGKNSVGNLILSAEHQGGNICIEVTDDGAGLNRERILAKAASQGLAVSENMSDEEVGMLI 470

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278882189 483 FAPGFSTAEQVTDVSGRGVGMDVVKRNIQEMGGHVEIQSKQGSGTTIRILLPLTLAILDGMSVKVADEVFILPLNAVMES 562
Cdd:PRK10547  471 FAPGFSTAEQVTDVSGRGVGMDVVKRNIQEMGGHVEIQSKQGKGTTIRILLPLTLAILDGMSVRVADEVFILPLNAVMES 550

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278882189 563 LQPREEDLHPLAGGERVLEVRGEYLPLVELWKVFEVDGAKTEATQGIVVILQSAGRRYALLVDQLIGQHQVVVKNLESNY 642
Cdd:PRK10547  551 LQPREEDLHPLAGGERVLEVRGEYLPLVELWKVFDVAGAKTEATQGIVVILQSAGRRYALLVDQLIGQHQVVVKNLESNY 630

                         650       660       670       680
                  ....*....|....*....|....*....|....*....|
gi 1278882189 643 RKVPGISAATILGDGSVALIVDVSALQGLNREQRVAYTAA 682
Cdd:PRK10547  631 RKVPGISAATILGDGSVALIVDVSALQALNREQRMANTAA 670
CheA COG0643
Chemotaxis protein histidine kinase CheA [Signal transduction mechanisms];
3-681 0e+00

Chemotaxis protein histidine kinase CheA [Signal transduction mechanisms];


Pssm-ID: 440408 [Multi-domain]  Cd Length: 563  Bit Score: 709.26  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278882189   3 MDISDFYQTFFDEADELLADMEQHLLDLVPEAPDSEQLNAIFRAAHSIKGGAGTFGFTILQETTHLMENLLDEARRGEMQ 82
Cdd:COG0643     1 MDMDELLEIFLEEARELLEQLEEGLLALEQDPDDPELLNAIFRAAHTLKGSAGMLGLDALAELAHALEDLLDALRNGELA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278882189  83 LNTDIINLFLETKDIMQEQLDAYKSSAEPDAAsFEYICNALRQLALEAKGEvaaavvpaaklsVVDAVGAGETAPAAAQA 162
Cdd:COG0643    81 LTPELIDLLLEALDALRALLDALEAGGEPPAD-ISALLARLDASEEAIEEV------------VADEVEISPPAPAALEP 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278882189 163 GKlrvvlsrlkenevnlleeelgnlatlsnvvkgkdslaatlddgigqddivavlcfvieadqiafetetetetaeaeap 242
Cdd:COG0643   148 AP------------------------------------------------------------------------------ 149

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278882189 243 vaqeevaviaqaptpavapaapalkavPKDAAAPARGEKPAARSSESTSIRVAVEKVDQLINLVGELVITQSMLAQRSNE 322
Cdd:COG0643   150 ---------------------------AAAPPAEAAAAAAEAAAAASETVRVDVERLDRLMNLVGELVITRARLEQLAEE 202

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278882189 323 LDPVTHGDLITSMGQLQRNARDLQESVMSIRMMPMEYVFSRFPRLVRDLASKLNKQIELTLMGSSTELDKSLIERIIDPL 402
Cdd:COG0643   203 LEDESLRELEEALEQLSRLTRELQDGVMRLRMVPISTVFNRFPRMVRDLARELGKEVELVIEGEETELDRTVLERLGDPL 282

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278882189 403 THLVRNSLDHGIELPENRIAAGKSPVGNLILSAEHQGGNICIEVTDDGAGLNRERILAKAISQGM---AVNENMTDEEVG 479
Cdd:COG0643   283 VHLVRNAVDHGIETPEERLAAGKPETGTITLSAYHEGGRVVIEVSDDGRGLDLEKIRAKAIEKGLitaEEAAALSDEELL 362

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278882189 480 MLIFAPGFSTAEQVTDVSGRGVGMDVVKRNIQEMGGHVEIQSKQGSGTTIRILLPLTLAILDGMSVKVADEVFILPLNAV 559
Cdd:COG0643   363 ELIFAPGFSTAEEVTDLSGRGVGMDVVKTNIEALGGTIEIESEPGKGTTFTLRLPLTLAIIDGLLVRVGGETYAIPLSSV 442

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278882189 560 MESLQPREEDLHPLAGGErVLEVRGEYLPLVELWKVFEVDGAKTEATQGIVVILQSAGRRYALLVDQLIGQHQVVVKNLE 639
Cdd:COG0643   443 EEVLRLDPDDIETVEGRE-VIRLRGELLPLVRLGELLGLPGAEPEGERGPVVVVRSGGRRVALVVDELLGQQEVVIKPLG 521

                         650       660       670       680
                  ....*....|....*....|....*....|....*....|..
gi 1278882189 640 SNYRKVPGISAATILGDGSVALIVDVSALQGLNREQRVAYTA 681
Cdd:COG0643   522 PLLRRVPGISGATILGDGRVALILDVAALVRSARARARAAAA 563
HATPase_CheA-like cd16916
Histidine kinase-like ATPase domain of the chemotaxis protein histidine kinase CheA, and some ...
 360-534 1.83e-95

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: 292.18  E-value: 1.83e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278882189 360 VFSRFPRLVRDLASKLNKQIELTLMGSSTELDKSLIERIIDPLTHLVRNSLDHGIELPENRIAAGKSPVGNLILSAEHQG 439
Cdd:cd16916     1 VFSRFPRLVRDLARELGKQVELVVEGEDTELDKSVLEKLADPLTHLLRNAVDHGIEAPEERLAAGKPPEGTITLRAEHQG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278882189 440 GNICIEVTDDGAGLNRERILAKAISQGMAVNE---NMTDEEVGMLIFAPGFSTAEQVTDVSGRGVGMDVVKRNIQEMGGH 516
Cdd:cd16916    81 NQVVIEVSDDGRGIDREKIREKAIERGLITADeaaTLSDDEVLNLIFAPGFSTAEQVTDVSGRGVGMDVVKRSIESLGGT 160

                         170
                  ....*....|....*...
gi 1278882189 517 VEIQSKQGSGTTIRILLP 534
Cdd:cd16916   161 IEVESEPGQGTTFTIRLP 178
CheA_reg cd00731
CheA regulatory domain; CheA is a histidine protein kinase present in bacteria and archea. ...
 537-668 1.69e-52

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: 177.37  E-value: 1.69e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278882189 537 LAILDGMSVKVADEVFILPLNAVMESLQPREEDLHPLAGGERVLEVRGEYLPLVELWKVFEVDGAKTEATQGIVVILQSA 616
Cdd:cd00731     1 LAIIKGLLVRVGDETYAIPLSAVVETVRIKPKDIKRVDGGKEVINVRGELLPLVRLGELFNVRGENEEPDEGVVVVVRTG 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1278882189 617 GRRYALLVDQLIGQHQVVVKNLESNYRKVPGISAATILGDGSVALIVDVSAL 668
Cdd:cd00731    81 GRKAALVVDQIIGQEEVVIKPLGGFLSNIPGISGATILGDGRVALILDVPAL 132
CheW smart00260
Two component signalling adaptor domain;
530-668 5.13e-28

Two component signalling adaptor domain;


Pssm-ID: 214588 [Multi-domain]  Cd Length: 138  Bit Score: 109.64  E-value: 5.13e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278882189  530 RILLPLTLAILDgmsvkvaDEVFILPLNAVMESLQPREEDL--HPLAGGERVLEVRGEYLPLVELWKVFEVDGAKTEAtQ 607
Cdd:smart00260   1 TIRLPLTFAIGK-------DETYAIPIAAVREILRPPPITPipGAPGYVLGVINLRGEVLPVVDLRRLLGLPPEPPTD-E 72

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1278882189  608 GIVVILQSAGRRYALLVDQLIGQHQVVVKNLES----NYRKVPGISAATILGDGSVALIVDVSAL 668
Cdd:smart00260  73 TRVIVVETGDRKVGLVVDSVLGVREVVVKSIEPpppvSLSNAPGISGATILGDGRVVLILDVDKL 137
CheW_like cd00588
CheW-like domain. CheW proteins are part of the chemotaxis signalling mechanism in bacteria. ...
 539-668 9.63e-28

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: 108.52  E-value: 9.63e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278882189 539 ILDGMSVKVADEVFILPLNAVMESLQPREEDLHPLA--GGERVLEVRGEYLPLVELWKVFEVDGAKTEATQGIVVILQSA 616
Cdd:cd00588     1 ILQVLLFRVGDELYAIPIAVVEEILPLPPITRVPNApdYVLGVINLRGEILPVIDLRRLFGLEAAEPDTDETRIVVVEVG 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1278882189 617 GRRYALLVDQLIGQHQVVVKNLESNY----RKVPGISAATILGDGSVALIVDVSAL 668
Cdd:cd00588    81 DRKVGLVVDSVLGVLEVVIKDIEPPPdvgsSNAPGISGATILGDGRVVLILDVDKL 136
CheW pfam01584
CheW-like domain; CheW proteins are part of the chemotaxis signaling mechanism in bacteria. ...
 542-668 3.07e-27

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: 106.90  E-value: 3.07e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278882189 542 GMSVKVADEVFILPLNAVMESLQPREEDLHPLAGG--ERVLEVRGEYLPLVELWKVFEVDGAKTEaTQGIVVILQSAGRR 619
Cdd:pfam01584   1 GLLFRLGGETFAIPISKVREILRPPPITPIPGAPGyvLGVINLRGEVLPVIDLRRLLGLPPTEPR-ERTRVVVVEVGGQV 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1278882189 620 YALLVDQLIGQHQVVVKNLESNY---RKVPGISAATILGDGSVALIVDVSAL 668
Cdd:pfam01584  80 VGLLVDEVIGVLEIVIKQIEPPLglgRVAGYISGATILGDGRVVLILDVEAL 131
HPT smart00073
Histidine Phosphotransfer domain; Contains an active histidine residue that mediates ...
 7-99 6.58e-25

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: 98.86  E-value: 6.58e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278882189    7 DFYQTFFDEADELLADMEQHLLDLVpEAPDSEQLNAIFRAAHSIKGGAGTFGFTILQETTHLMENLLDEARRGEMQLNTD 86
Cdd:smart00073   1 GGLELFREELAEFLQSLEEGLLELE-KALDAQDVNEIFRAAHTLKGSAGSLGLQQLAQLCHQLENLLDALRSGEVELTPD 79

                           90
                   ....*....|...
gi 1278882189   87 IINLFLETKDIMQ 99
Cdd:smart00073  80 LLDLLLELVDVLK 92
HATPase_c smart00387
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.
 400-536 7.24e-24

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


Pssm-ID: 214643 [Multi-domain]  Cd Length: 111  Bit Score: 96.56  E-value: 7.24e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278882189  400 DPLTHLVRNSLDHGIELPEnriaagksPVGNLILSAEHQGGNICIEVTDDGAGLnrerilakaisqgmavnenmtDEEVG 479
Cdd:smart00387   4 DRLRQVLSNLLDNAIKYTP--------EGGRITVTLERDGDHVEITVEDNGPGI---------------------PPEDL 54

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1278882189  480 MLIFAPGFSTAEQVTDVSGRGVGMDVVKRNIQEMGGHVEIQSKQGSGTTIRILLPLT 536
Cdd:smart00387  55 EKIFEPFFRTDKRSRKIGGTGLGLSIVKKLVELHGGEISVESEPGGGTTFTITLPLE 111
HPT cd00088
Histidine Phosphotransfer domain, involved in signalling through a two part component systems ...
 5-103 6.15e-23

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: 93.60  E-value: 6.15e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278882189   5 ISDFYQTFFDEADELLADMEQHLLDLvpeaPDSEQLNAIFRAAHSIKGGAGTFGFTILQETTHLMENLLDEARRGeMQLN 84
Cdd:cd00088     1 MEELLELFLEEAEELLEELERALLEL----EDAEDLNEIFRAAHTLKGSAASLGLQRLAQLAHQLEDLLDALRDG-LEVT 75

                          90
                  ....*....|....*....
gi 1278882189  85 TDIINLFLETKDIMQEQLD 103
Cdd:cd00088    76 PELIDLLLDALDALKAELE 94
H-kinase_dim pfam02895
Signal transducing histidine kinase, homodimeric domain; This helical bundle domain is the ...
 291-352 1.18e-16

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: 74.58  E-value: 1.18e-16
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1278882189 291 SIRVAVEKVDQLINLVGELVITQSMLAQRSNEL----DPVTHGDLITSMGQLQRNARDLQESVMSI 352
Cdd:pfam02895   1 TIRVDVEKLDRLMNLVGELVIARNRLVQLLERLeeygGDTLLEELKEALQQLDRLTRELQEAVMKI 66
HATPase_c pfam02518
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the ...
 399-536 3.71e-15

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: 71.63  E-value: 3.71e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278882189 399 IDPLTHLVRNSLDHGIElpenriAAGKSPVGNLILsaeHQGGNICIEVTDDGAGLNRERIlakaisqgmavnenmtdeev 478
Cdd:pfam02518   3 ELRLRQVLSNLLDNALK------HAAKAGEITVTL---SEGGELTLTVEDNGIGIPPEDL-------------------- 53

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1278882189 479 gMLIFAPgFSTAEqVTDVSGRGVGMDVVKRNIQEMGGHVEIQSKQGSGTTIRILLPLT 536
Cdd:pfam02518  54 -PRIFEP-FSTAD-KRGGGGTGLGLSIVRKLVELLGGTITVESEPGGGTTVTLTLPLA 108
KdpD COG2205
K+-sensing histidine kinase KdpD [Signal transduction mechanisms];
366-536 3.32e-14

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


Pssm-ID: 441807 [Multi-domain]  Cd Length: 239  Bit Score: 72.63  E-value: 3.32e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278882189 366 RLVRDLASKLNKQIELTLMGSSTEL--DKSLIERIidpLTHLVRNSLDHGielPENriaagkspvGNLILSAEHQGGNIC 443
Cdd:COG2205   102 EELRPLAEEKGIRLELDLPPELPLVyaDPELLEQV---LANLLDNAIKYS---PPG---------GTITISARREGDGVR 166

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278882189 444 IEVTDDGAGlnrerilakaisqgmavnenMTDEEVGMlIFAPgFSTAEQVTDVSGRGVGMDVVKRNIQEMGGHVEIQSKQ 523
Cdd:COG2205   167 ISVSDNGPG--------------------IPEEELER-IFER-FYRGDNSRGEGGTGLGLAIVKRIVEAHGGTIWVESEP 224

                         170
                  ....*....|...
gi 1278882189 524 GSGTTIRILLPLT 536
Cdd:COG2205   225 GGGTTFTVTLPLA 237
Hpt pfam01627
Hpt domain; The histidine-containing phosphotransfer (HPt) domain is a novel protein module ...
 7-93 9.59e-14

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: 66.99  E-value: 9.59e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278882189   7 DFYQTFFDEADELLADMEQHLldlvpeapDSEQLNAIFRAAHSIKGGAGTFGFTILQETTHLMENLLdeaRRGEMQLNTD 86
Cdd:pfam01627   1 ELLELFLEEAPELLEQLEQAL--------DAEDLEALFRAAHTLKGSAGSLGLPALAELAHELEDLL---REGELPLDPE 69


                  ....*..
gi 1278882189  87 IINLFLE 93
Cdd:pfam01627  70 LLEALRD 76
BaeS COG0642
Signal transduction histidine kinase [Signal transduction mechanisms];
367-536 8.43e-13

Signal transduction histidine kinase [Signal transduction mechanisms];


Pssm-ID: 440407 [Multi-domain]  Cd Length: 328  Bit Score: 69.94  E-value: 8.43e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278882189 367 LVRDLASKL-----NKQIELTLMGSST----ELDKSLIERIidpLTHLVRNSLDHGielPENriaagkspvGNLILSAEH 437
Cdd:COG0642   187 LLEEVVELFrplaeEKGIELELDLPDDlptvRGDPDRLRQV---LLNLLSNAIKYT---PEG---------GTVTVSVRR 251

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278882189 438 QGGNICIEVTDDGAGlnrerilakaisqgmavnenMTDEEVGMlIFAPgFSTAEQVTDVSGRGVGMDVVKRNIQEMGGHV 517
Cdd:COG0642   252 EGDRVRISVEDTGPG--------------------IPPEDLER-IFEP-FFRTDPSRRGGGTGLGLAIVKRIVELHGGTI 309

                         170
                  ....*....|....*....
gi 1278882189 518 EIQSKQGSGTTIRILLPLT 536
Cdd:COG0642   310 EVESEPGKGTTFTVTLPLA 328
NtrY COG5000
Signal transduction histidine kinase NtrY involved in nitrogen fixation and metabolism ...
 366-536 8.06e-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: 64.60  E-value: 8.06e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278882189 366 RLVRDLASKLNKQIELTLMGSSTEL--DKSLIERIidpLTHLVRNSLDHGielpenriaagkSPVGNLILSAEHQGGNIC 443
Cdd:COG5000   287 ALYEPALKEKDIRLELDLDPDLPEVlaDRDQLEQV---LINLLKNAIEAI------------EEGGEIEVSTRREDGRVR 351

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278882189 444 IEVTDDGAGLNRErILAKaisqgmavnenmtdeevgmlIFAPGFSTAEqvtdvSGRGVGMDVVKRNIQEMGGHVEIQSKQ 523
Cdd:COG5000   352 IEVSDNGPGIPEE-VLER--------------------IFEPFFTTKP-----KGTGLGLAIVKKIVEEHGGTIELESRP 405

                         170
                  ....*....|...
gi 1278882189 524 GSGTTIRILLPLT 536
Cdd:COG5000   406 GGGTTFTIRLPLA 418
CheY-binding pfam09078
CheY binding; Members of this family adopt a secondary structure consisting of an open-face ...
 166-228 1.10e-10

CheY binding; Members of this family adopt a secondary structure consisting of an open-face beta/alpha sandwich, with four antiparallel beta-strands and two alpha-helices. They bind to a corresponding domain on CheY, with subsequent phosphorylation of the CheY Asp57 residue, and activation of CheY, which then affects flagellar rotation.


Pssm-ID: 430396 [Multi-domain]  Cd Length: 63  Bit Score: 57.57  E-value: 1.10e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1278882189 166 RVVLSRLKENEVNLLEEELGNLATLSNVVKGKDSLAATLDDGIGQDDIVAVLCFVIEADQIAF 228
Cdd:pfam09078   1 RIRLSGVSDKDVELLVEELGLLGEVLAQEQAGDSLSVWLETTVSEDDIIAVCCFVVDPDQIVI 63
NtrB COG3852
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms];
368-536 2.62e-10

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


Pssm-ID: 443061 [Multi-domain]  Cd Length: 361  Bit Score: 62.56  E-value: 2.62e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278882189 368 VRDLASK-LNKQIELTLmgsstELDKSLIERIIDP------LTHLVRNSLDHGIELPENRIAAGKSPvgNLILSAEHQGG 440
Cdd:COG3852   213 VLELLRAeAPKNIRIVR-----DYDPSLPEVLGDPdqliqvLLNLVRNAAEAMPEGGTITIRTRVER--QVTLGGLRPRL 285

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278882189 441 NICIEVTDDGAGLNRErILAKaisqgmavnenmtdeevgmlIFAPGFSTAEQvtdvsGRGVGMDVVKRNIQEMGGHVEIQ 520
Cdd:COG3852   286 YVRIEVIDNGPGIPEE-ILDR--------------------IFEPFFTTKEK-----GTGLGLAIVQKIVEQHGGTIEVE 339

                         170
                  ....*....|....*.
gi 1278882189 521 SKQGSGTTIRILLPLT 536
Cdd:COG3852   340 SEPGKGTTFRIYLPLE 355
COG4191 COG4191
Signal transduction histidine kinase regulating C4-dicarboxylate transport system [Signal ...
 324-536 6.61e-10

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


Pssm-ID: 443345 [Multi-domain]  Cd Length: 361  Bit Score: 61.35  E-value: 6.61e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278882189 324 DPVTHGDLITSMGQLQRNARDLQESVMSIRMmpmeyvFSRFPRLVRDLASkLNKQIELTLMGSSTELDKSLIERIIDP-- 401
Cdd:COG4191   173 DEPDPEELREALERILEGAERAAEIVRSLRA------FSRRDEEEREPVD-LNELIDEALELLRPRLKARGIEVELDLpp 245

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278882189 402 ---------------LTHLVRNSLDhgielpenriAAGKSPVGNLILSAEHQGGNICIEVTDDGAGLNRErILAKaisqg 466
Cdd:COG4191   246 dlppvlgdpgqleqvLLNLLINAID----------AMEEGEGGRITISTRREGDYVVISVRDNGPGIPPE-VLER----- 309

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278882189 467 mavnenmtdeevgmlIFAPGFSTAEQVtdvSGRGVGMDVVKRNIQEMGGHVEIQSKQGSGTTIRILLPLT 536
Cdd:COG4191   310 ---------------IFEPFFTTKPVG---KGTGLGLSISYGIVEKHGGRIEVESEPGGGTTFTITLPLA 361
PRK11086 PRK11086
sensory histidine kinase DcuS; Provisional
 391-534 2.71e-09

sensory histidine kinase DcuS; Provisional


Pssm-ID: 236839 [Multi-domain]  Cd Length: 542  Bit Score: 60.31  E-value: 2.71e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278882189 391 DKSLIERIIDPLTHLVRNSLDhgielpenriAAGKSPVGNLILSAEHQGGNICIEVTDDGAGLNRERILAkaisqgmavn 470
Cdd:PRK11086  427 DEDQVHELITILGNLIENALE----------AVGGEEGGEISVSLHYRNGWLHCEVSDDGPGIAPDEIDA---------- 486

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1278882189 471 enmtdeevgmlIFAPGFSTAEqvtdvSGRGVGMDVVKRNIQEMGGHVEIQSKQGSGTTIRILLP 534
Cdd:PRK11086  487 -----------IFDKGYSTKG-----SNRGVGLYLVKQSVENLGGSIAVESEPGVGTQFFVQIP 534
CitA COG3290
Sensor histidine kinase DipB regulating citrate/malate metabolism [Signal transduction ...
 371-538 1.99e-08

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


Pssm-ID: 442519 [Multi-domain]  Cd Length: 389  Bit Score: 56.78  E-value: 1.99e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278882189 371 LASKLN----KQIELTLmgsstELDKSLIERIIDP--LTHLVRNSLDHGIElpenriAAGKSPVGN--LILSAEHQGGNI 442
Cdd:COG3290   250 LLGKAArareRGIDLTI-----DIDSDLPDLPLSDtdLVTILGNLLDNAIE------AVEKLPEEErrVELSIRDDGDEL 318

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278882189 443 CIEVTDDGAGLnrerilakaisqgmavnenmtDEEVGMLIFAPGFSTAEQvtdvSGRGVGMDVVKRNIQEMGGHVEIQSK 522
Cdd:COG3290   319 VIEVEDSGPGI---------------------PEELLEKIFERGFSTKLG----EGRGLGLALVKQIVEKYGGTIEVESE 373

                         170
                  ....*....|....*.
gi 1278882189 523 QGSGTTIRILLPLTLA 538
Cdd:COG3290   374 EGEGTVFTVRLPKEGE 389
WalK COG5002
Sensor histidine kinase WalK [Signal transduction mechanisms];
292-535 2.67e-08

Sensor histidine kinase WalK [Signal transduction mechanisms];


Pssm-ID: 444026 [Multi-domain]  Cd Length: 390  Bit Score: 56.48  E-value: 2.67e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278882189 292 IRVAVEKVDQLINLVGELvitqsmlaqrsneLDpvthgdlitsMGQLQRNARDLQESVMSIRMMpMEYVFSRFprlvRDL 371
Cdd:COG5002   205 LEIILEEAERLSRLVNDL-------------LD----------LSRLESGELKLEKEPVDLAEL-LEEVVEEL----RPL 256

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278882189 372 ASKLNKQIELTLMGSSTEL--DKSLIERIidpLTHLVRNSLDHGielPENriaagkspvGNLILSAEHQGGNICIEVTDD 449
Cdd:COG5002   257 AEEKGIELELDLPEDPLLVlgDPDRLEQV---LTNLLDNAIKYT---PEG---------GTITVSLREEDDQVRISVRDT 321

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278882189 450 GAGlnrerILAKAISQgmavnenmtdeevgmlIFAPgFSTAEQVT--DVSGRGVGMDVVKRNIQEMGGHVEIQSKQGSGT 527
Cdd:COG5002   322 GIG-----IPEEDLPR----------------IFER-FYRVDKSRsrETGGTGLGLAIVKHIVEAHGGRIWVESEPGKGT 379


                  ....*...
gi 1278882189 528 TIRILLPL 535
Cdd:COG5002   380 TFTITLPL 387
YesM COG2972
Sensor histidine kinase YesM [Signal transduction mechanisms];
389-536 2.60e-07

Sensor histidine kinase YesM [Signal transduction mechanisms];


Pssm-ID: 442211 [Multi-domain]  Cd Length: 445  Bit Score: 53.48  E-value: 2.60e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278882189 389 ELDKSLIERIIDPLT--HLVRNSLDHGIElpenriaaGKSPVGNLILSAEHQGGNICIEVTDDGAGLNRERIlaKAISQG 466
Cdd:COG2972   326 EIDEELLDLLIPKLIlqPLVENAIEHGIE--------PKEGGGTIRISIRKEGDRLVITVEDNGVGMPEEKL--EKLLEE 395

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1278882189 467 MAVNENmtdeevgmlifapgfstaeqvtdvsGRGVGMdvvkRNIQEM-------GGHVEIQSKQGSGTTIRILLPLT 536
Cdd:COG2972   396 LSSKGE-------------------------GRGIGL----RNVRERlklyygeEYGLEIESEPGEGTTVTIRIPLE 443
PRK11360 PRK11360
two-component system sensor histidine kinase AtoS;
440-535 4.23e-07

two-component system sensor histidine kinase AtoS;


Pssm-ID: 236901 [Multi-domain]  Cd Length: 607  Bit Score: 53.05  E-value: 4.23e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278882189 440 GNICIEVTDDGAGLNRERILAkaisqgmavnenmtdeevgmlIFAPGFSTAEQvtdvsGRGVGMDVVKRNIQEMGGHVEI 519
Cdd:PRK11360  532 GQVAVSIEDNGCGIDPELLKK---------------------IFDPFFTTKAK-----GTGLGLALSQRIINAHGGDIEV 585

                          90
                  ....*....|....*.
gi 1278882189 520 QSKQGSGTTIRILLPL 535
Cdd:PRK11360  586 ESEPGVGTTFTLYLPI 601
HATPase_CckA-like cd16919
Histidine kinase-like ATPase domain of two-component sensor hybrid histidine kinases, similar ...
 439-534 1.12e-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: 47.76  E-value: 1.12e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278882189 439 GGNICIEVTDDGAGLnrerilakaisqgmavnenmtDEEVGMLIFAPGFSTAEQVtdvSGRGVGMDVVKRNIQEMGGHVE 518
Cdd:cd16919    45 GNYVCLEVSDTGSGM---------------------PAEVLRRAFEPFFTTKEVG---KGTGLGLSMVYGFVKQSGGHLR 100

                          90
                  ....*....|....*.
gi 1278882189 519 IQSKQGSGTTIRILLP 534
Cdd:cd16919   101 IYSEPGVGTTVRIYLP 116
HATPase_DpiB-CitA-like cd16915
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
 405-534 1.35e-06

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: 47.28  E-value: 1.35e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278882189 405 LVRNSLDhgielpenriAAGKSPVGN--LILSAEHQGGNICIEVTDDGAGLnrerilakaisqgmavnenmtDEEVGMLI 482
Cdd:cd16915     8 LIDNALD----------ALAATGAPNkqVEVFLRDEGDDLVIEVRDTGPGI---------------------APELRDKV 56

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1278882189 483 FAPGFSTAEQvtdvSGRGVGMDVVKRNIQEMGGHVEIQSKQGSGTTIRILLP 534
Cdd:cd16915    57 FERGVSTKGQ----GERGIGLALVRQSVERLGGSITVESEPGGGTTFSIRIP 104
HATPase_EnvZ-like cd16950
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
 425-534 2.40e-06

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


Pssm-ID: 340426 [Multi-domain]  Cd Length: 101  Bit Score: 46.29  E-value: 2.40e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278882189 425 KSPVGNLILSAEHQGGnICIEVTDDGAGlNRERILAKAISQGMAvnenmtDEEVGMLiFAPgFSTAEQVTDVSGRGVGMD 504
Cdd:cd16950     2 KRVLSNLVDNALRYGG-GWVEVSSDGEG-NRTRIQVLDNGPGIA------PEEVDEL-FQP-FYRGDNARGTSGTGLGLA 71

                          90       100       110
                  ....*....|....*....|....*....|
gi 1278882189 505 VVKRNIQEMGGHVEIQSKQGSGTTIRILLP 534
Cdd:cd16950    72 IVQRISDAHGGSLTLANRAGGGLCARIELP 101
KinA COG5805
Sporulation sensor histidine kinase A (Stage II sporulation protein SpoIIF/SpoIIJ) [Cell cycle ...
 356-536 2.51e-06

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: 50.50  E-value: 2.51e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278882189 356 PMEYVFSRFP--RLVRDLASKLNKQIELTLMGSSTELDKSLIERIIDP------LTHLVRNSLDhgiELPENriaagksp 427
Cdd:COG5805   346 PQAVNKEKENinELIQDVVTLLETEAILHNIQIRLELLDEDPFIYCDEnqikqvFINLIKNAIE---AMPNG-------- 414

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278882189 428 vGNLILSAEHQGGNICIEVTDDGAGLNRERiLAKaisqgmavnenmtdeevgmlIFAPGFSTAEQvtdvsGRGVGMDVVK 507
Cdd:COG5805   415 -GTITIHTEEEDNSVIIRVIDEGIGIPEER-LKK--------------------LGEPFFTTKEK-----GTGLGLMVSY 467

                         170       180
                  ....*....|....*....|....*....
gi 1278882189 508 RNIQEMGGHVEIQSKQGSGTTIRILLPLT 536
Cdd:COG5805   468 KIIENHNGTIDIDSKVGKGTTFTITLPLS 496
KinE COG5809
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome ...
 439-535 3.10e-06

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: 50.36  E-value: 3.10e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278882189 439 GGNICIEVTDdgagLNRERILAKAISQGMAVNENMTDEevgmlIFAPGFSTAEQvtdvsGRGVGMDVVKRNIQEMGGHVE 518
Cdd:COG5809   398 GGNITIETKA----EDDDKVVISVTDEGCGIPEERLKK-----LGEPFYTTKEK-----GTGLGLMVSYKIIEEHGGKIT 463

                          90
                  ....*....|....*..
gi 1278882189 519 IQSKQGSGTTIRILLPL 535
Cdd:COG5809   464 VESEVGKGTTFSITLPI 480
COG4251 COG4251
Bacteriophytochrome (light-regulated signal transduction histidine kinase) [Signal ...
 391-534 7.52e-06

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


Pssm-ID: 443393 [Multi-domain]  Cd Length: 503  Bit Score: 49.01  E-value: 7.52e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278882189 391 DKSLIERIidpLTHLVRNSLDHGIELPENRIAagkspvgnliLSAEHQGGNICIEVTDDGAGLN---RERilakaisqgm 467
Cdd:COG4251   391 DPTLLRQV---FQNLISNAIKYSRPGEPPRIE----------IGAEREGGEWVFSVRDNGIGIDpeyAEK---------- 447

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1278882189 468 avnenmtdeevgmlIFAPgFSTAEQVTDVSGRGVGMDVVKRNIQEMGGHVEIQSKQGSGTTIRILLP 534
Cdd:COG4251   448 --------------IFEI-FQRLHSRDEYEGTGIGLAIVKKIVERHGGRIWVESEPGEGATFYFTLP 499
HATPase_EvgS-ArcB-TorS-like cd16922
Histidine kinase-like ATPase domain of two-component sensor histidine kinases, many are hybrid ...
 434-535 1.38e-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: 44.41  E-value: 1.38e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278882189 434 SAEHQGGNICIEVTDDGAGLNRERILakaisqgmavnenmtdeevgmLIFAPgFSTAEQVT--DVSGRGVGMDVVKRNIQ 511
Cdd:cd16922    29 EEEEDGVQLRFSVEDTGIGIPEEQQA---------------------RLFEP-FSQADSSTtrKYGGTGLGLAISKKLVE 86

                          90       100
                  ....*....|....*....|....
gi 1278882189 512 EMGGHVEIQSKQGSGTTIRILLPL 535
Cdd:cd16922    87 LMGGDISVESEPGQGSTFTFTLPL 110
PRK10364 PRK10364
two-component system sensor histidine kinase ZraS;
429-535 1.85e-05

two-component system sensor histidine kinase ZraS;


Pssm-ID: 236674 [Multi-domain]  Cd Length: 457  Bit Score: 47.86  E-value: 1.85e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278882189 429 GNLILSAEHQGGNICIEVTDDGAGLNRERILAkaisqgmavnenmtdeevgmlIFAPGFSTAEQvtdvsGRGVGMDVVKR 508
Cdd:PRK10364  368 GVISVTASESGAGVKISVTDSGKGIAADQLEA---------------------IFTPYFTTKAE-----GTGLGLAVVHN 421

                          90       100
                  ....*....|....*....|....*..
gi 1278882189 509 NIQEMGGHVEIQSKQGSGTTIRILLPL 535
Cdd:PRK10364  422 IVEQHGGTIQVASQEGKGATFTLWLPV 448
CheW COG0835
Chemotaxis signal transduction protein CheW [Signal transduction mechanisms];
544-668 4.57e-05

Chemotaxis signal transduction protein CheW [Signal transduction mechanisms];


Pssm-ID: 440597  Cd Length: 151  Bit Score: 44.09  E-value: 4.57e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278882189 544 SVKVADEVFILPLNAVMESLQPREedLHPLAGGER----VLEVRGEYLPLVELWKVFEVDgAKTEATQGIVVILQSAGRR 619
Cdd:COG0835    12 TFRLGGERYAIPIEKVREILPLPP--ITPVPGAPPwvlgVINLRGRVVPVIDLRALLGLP-PTEDTERTRIIVLEVGGRV 88

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1278882189 620 YALLVDQLIGQHQVVVKNLESNYRKVPGISAATILG----DGSVALIVDVSAL 668
Cdd:COG0835    89 VGLLVDSVSGVVRIDPDDIEPPPELLSGGLAPFITGvaklDDRLILLLDLEKL 141
HATPase_FilI-like cd16921
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
 402-534 4.81e-05

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


Pssm-ID: 340398 [Multi-domain]  Cd Length: 105  Bit Score: 42.70  E-value: 4.81e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278882189 402 LTHLVRNSLDHGIELPENRIAAGKSPVGNlilsaEHQggnicIEVTDDGAGLnrerilakaisqgmavnenmtDEEVGML 481
Cdd:cd16921     5 LTNLLGNAIKFRRPRRPPRIEVGAEDVGE-----EWT-----FYVRDNGIGI---------------------DPEYAEK 53

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1278882189 482 IFAPgFSTAEQVTDVSGRGVGMDVVKRNIQEMGGHVEIQSKQGSGTTIRILLP 534
Cdd:cd16921    54 VFGI-FQRLHSREEYEGTGVGLAIVRKIIERHGGRIWLESEPGEGTTFYFTLP 105
HATPase_NtrY-like cd16944
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
 402-534 5.72e-05

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: 42.91  E-value: 5.72e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278882189 402 LTHLVRNSldhgielpENRIAAGKSPVGNL-ILSAEHQGGNICIEVTDDGAGLNRERIlakaisqGMAVNENMTDEEVGM 480
Cdd:cd16944     9 LTNILKNA--------AEAIEGRPSDVGEVrIRVEADQDGRIVLIVCDNGKGFPREMR-------HRATEPYVTTRPKGT 73

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1278882189 481 lifapgfstaeqvtdvsgrGVGMDVVKRNIQEMGGHVEIQSKQGSGTTIRILLP 534
Cdd:cd16944    74 -------------------GLGLAIVKKIMEEHGGRISLSNREAGGACIRIILP 108
HATPase_AtoS-like cd16943
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
 444-535 6.21e-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: 42.41  E-value: 6.21e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278882189 444 IEVTDDGAGLNRErILAKaisqgmavnenmtdeevgmlIFAPGFSTAEQVTdvsGRGVGMDVVKRNIQEMGGHVEIQSKQ 523
Cdd:cd16943    38 IEVEDTGSGIDPE-ILGR--------------------IFDPFFTTKPVGE---GTGLGLSLSYRIIQKHGGTIRVASVP 93

                          90
                  ....*....|..
gi 1278882189 524 GSGTTIRILLPL 535
Cdd:cd16943    94 GGGTRFTIILPI 105
HATPase_BceS-YxdK-YvcQ-like cd16948
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
 428-534 8.54e-05

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: 42.27  E-value: 8.54e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278882189 428 VGNLILSAEHQGGNICIEVTDDGAGLNRERILAkaisqgmavnenmtdeevgmlIFAPGFSTAEQVTDVSGRGVGMDVVK 507
Cdd:cd16948    24 GGKIEIYSETNEQGVVLSIKDFGIGIPEEDLPR---------------------VFDKGFTGENGRNFQESTGMGLYLVK 82

                          90       100
                  ....*....|....*....|....*..
gi 1278882189 508 RNIQEMGGHVEIQSKQGSGTTIRILLP 534
Cdd:cd16948    83 KLCDKLGHKIDVESEVGEGTTFTITFP 109
PRK13557 PRK13557
histidine kinase; Provisional
 284-536 1.64e-04

histidine kinase; Provisional


Pssm-ID: 237425 [Multi-domain]  Cd Length: 540  Bit Score: 44.66  E-value: 1.64e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278882189 284 ARSSEStsIRVAVEKVDQLinlvgelviTQSMLA-QRSNELD--PVTHGDLITSMGQLQRnaRDLQESVmsirmmpmeyv 360
Cdd:PRK13557  203 ARSVEN--IRAAAERAATL---------TQQLLAfARKQRLEgrVLNLNGLVSGMGELAE--RTLGDAV----------- 258

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278882189 361 fsrfpRLVRDLASKL-NKQIEltlmgsSTELDKSLIERIIdplthlvrNSLDHGIELPENRIAAGKSPVGNLILSAEHQ- 438
Cdd:PRK13557  259 -----TIETDLAPDLwNCRID------PTQAEVALLNVLI--------NARDAMPEGGRVTIRTRNVEIEDEDLAMYHGl 319

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278882189 439 --GGNICIEVTDDGAGLNRErILAKaisqgmavnenmtdeevgmlIFAPGFSTAEQVtdvSGRGVGMDVVKRNIQEMGGH 516
Cdd:PRK13557  320 ppGRYVSIAVTDTGSGMPPE-ILAR--------------------VMDPFFTTKEEG---KGTGLGLSMVYGFAKQSGGA 375

                         250       260
                  ....*....|....*....|
gi 1278882189 517 VEIQSKQGSGTTIRILLPLT 536
Cdd:PRK13557  376 VRIYSEVGEGTTVRLYFPAS 395
ComP COG4585
Signal transduction histidine kinase ComP [Signal transduction mechanisms];
309-536 2.18e-04

Signal transduction histidine kinase ComP [Signal transduction mechanisms];


Pssm-ID: 443642 [Multi-domain]  Cd Length: 252  Bit Score: 43.45  E-value: 2.18e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278882189 309 LVITQSMLAQRSNELDPVTHGDLITSMGQLQRNA-RDLQESVMSIRMMPMEYV--FSRFPRLVRDLASKLNKQIELTLMG 385
Cdd:COG4585    71 AIKLQLEAARRLLDADPEAAREELEEIRELAREAlAELRRLVRGLRPPALDDLglAAALEELAERLLRAAGIRVELDVDG 150

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278882189 386 SSTELDKSL---IERIIdplTHLVRNSLDHgielpenriaagkSPVGNLILSAEHQGGNICIEVTDDGAGLNRERilaka 462
Cdd:COG4585   151 DPDRLPPEVelaLYRIV---QEALTNALKH-------------AGATRVTVTLEVDDGELTLTVRDDGVGFDPEA----- 209

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1278882189 463 isqgmavnenmtdeevgmlifapgfstaeqvtdVSGRGVGMDVVKRNIQEMGGHVEIQSKQGSGTTIRILLPLT 536
Cdd:COG4585   210 ---------------------------------APGGGLGLRGMRERAEALGGTLTIGSAPGGGTRVRATLPLA 250
HATPase_HupT_MifS-like cd16976
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
 398-533 1.30e-03

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: 38.59  E-value: 1.30e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278882189 398 IIDPLTHLVRNSLDhgielpenriAAGKSPVGNLILSAEHQGGNICIEVTDDGAGLnrerilakaisqgmavnenmtDEE 477
Cdd:cd16976     1 IQQVLMNLLQNALD----------AMGKVENPRIRIAARRLGGRLVLVVRDNGPGI---------------------AEE 49

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1278882189 478 VGMLIFAPGFSTaeqvTDV-SGRGVGMDVVKRNIQEMGGHVEIQSKQGSGTTIRILL 533
Cdd:cd16976    50 HLSRVFDPFFTT----KPVgKGTGLGLSISYGIVEEHGGRLSVANEEGAGARFTFDL 102
PRK15347 PRK15347
two component system sensor kinase;
426-536 3.43e-03

two component system sensor kinase;


Pssm-ID: 237951 [Multi-domain]  Cd Length: 921  Bit Score: 40.78  E-value: 3.43e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278882189 426 SPVGNLILSAEHQGGNICIEVTDDGAGLNRERILAkaisqgmavnenmtdeevgmlIFAPGFSTAeqvTDVSGRGVGMDV 505
Cdd:PRK15347  529 TETGGIRLRVKRHEQQLCFTVEDTGCGIDIQQQQQ---------------------IFTPFYQAD---THSQGTGLGLTI 584

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1278882189 506 VKRNIQEMGGHVEIQSKQGSGTTIRILLPLT 536
Cdd:PRK15347  585 ASSLAKMMGGELTLFSTPGVGSCFSLVLPLN 615
HATPase_ETR2_ERS2-EIN4-like cd16938
Histidine kinase-like ATPase domain of Arabidopsis thaliana ETR2, ERS2, and EIN4, and related ...
 428-533 5.58e-03

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: 37.44  E-value: 5.58e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278882189 428 VGNLiLSAEHQGGNICIEVTDDGAGLNRERILAKAISQGMA---------VNENMTDEEVGMLIFAPGFSTAEQVTDVSG 498
Cdd:cd16938    20 LGNL-LKMRNGGGNITFRVFLEGGSEDRSDRDWGPWRPSMSdesveirfeVEINDSGSPSIESASMRNSLNRRYNLSELG 98

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1278882189 499 RGVGMDVVKRNIQEMGGHVEIQSKQGSGTTIRILL 533
Cdd:cd16938    99 EHLSFSICKQLVQLMGGNIWIVPGSGLGTTMSLLL 133
HATPase_RstB-like cd16939
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
 433-535 7.50e-03

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: 36.64  E-value: 7.50e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278882189 433 LSAEHQGGNICIEVTDDGAGL---NRERIlakaisqgmavnenmtdeevgmliFAPgFSTAEQVTDVS--GRGVGMDVVK 507
Cdd:cd16939    22 IALLVSGGRLTLIVEDDGPGIpaaARERV------------------------FEP-FVRLDPSRDRAtgGFGLGLAIVH 76

                          90       100
                  ....*....|....*....|....*...
gi 1278882189 508 RNIQEMGGHVEIQSKQGSGTTIRILLPL 535
Cdd:cd16939    77 RVALWHGGHVECDDSELGGACFRLTWPR 104
PRK13837 PRK13837
two-component system VirA-like sensor kinase;
439-536 8.90e-03

two-component system VirA-like sensor kinase;


Pssm-ID: 237526 [Multi-domain]  Cd Length: 828  Bit Score: 39.28  E-value: 8.90e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278882189 439 GGNICIEVTDDGAGLnrerilakaisqgmavnenmtDEEVGMLIFAPGFSTAEQvtdvsGRGVGMDVVKRNIQEMGGHVE 518
Cdd:PRK13837  605 GRYVLLRVSDTGAGI---------------------DEAVLPHIFEPFFTTRAG-----GTGLGLATVHGIVSAHAGYID 658

                          90
                  ....*....|....*...
gi 1278882189 519 IQSKQGSGTTIRILLPLT 536
Cdd:PRK13837  659 VQSTVGRGTRFDVYLPPS 676
 
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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