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Conserved domains on  [gi|658548882|ref|WP_029741332|]
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chemotaxis protein CheA [Enterobacter asburiae]

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
 3-678 0e+00

chemotaxis protein CheA; Provisional


:

Pssm-ID: 236712 [Multi-domain]  Cd Length: 670  Bit Score: 1378.67  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548882   3 MDISDFYQTFFDEADELLADMEQHLLDLVPEAPDSEQLNAIFRAAHSIKGGAGTFGFTILQETTHLMENLLDEARRGEMQ 82
Cdd:PRK10547   1 MDISDFYQTFFDEADELLADMEQHLLVLDPEAPDAEQLNAIFRAAHSIKGGAGTFGFTVLQETTHLMENLLDEARRGEMQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548882  83 LNTDIINLFLETKDIMQEQLDAYKSSAEPDAASFEYICNALRQLALEAKGEVAAAVVPAAKLSVVDAVAADEAAPAAAqa 162
Cdd:PRK10547  81 LNTDIINLFLETKDIMQEQLDAYKTSQEPDAASFEYICQALRQLALEAKGETPSAVTRLSVVAIQEKSEPQDESPRSQ-- 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548882 163 GKLRVVLSRLKESEVNLLEEELGNLAKLSNVVKGKDSLAATLDDGIGQDDIVAVLCFVIEADQIAFETETAAVDAPAAAE 242
Cdd:PRK10547 159 SGLRIILSRLKAGEVDLLEEELGNLGTLTDVVKGADSLEATLPGSVAEDDITAVLCFVIEADQITFETAVAAPQEKAEET 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548882 243 EVAVVAQAAAPAVAPAAPALKAvpKEAAAPGRgEKPAaRSSESTSIRVAVEKVDQLINLVGELVITQSMLAQRSNELDPV 322
Cdd:PRK10547 239 TEVVEVSPKISVPPVLKLAAEQ--APAGRVER-EKTA-RSSESTSIRVAVEKVDQLINLVGELVITQSMLAQRSSELDPV 314

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548882 323 THGDLITSMGQLQRNARDLQESVMSIRMMPMEYVFSRFPRLVRDLASKLNKQIELTLMGSSTELDKSLIERIIDPLTHLV 402
Cdd:PRK10547 315 NHGDLITSMGQLQRNARDLQESVMSIRMMPMEYVFSRFPRLVRDLAGKLGKQVELTLVGSSTELDKSLIERIIDPLTHLV 394

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548882 403 RNSLDHGIELPENRIAAGKSPVGNLILSAEHQGGNICIEVTDDGAGLNRERILAKAISQGMAVNENMTDEEVGMLIFAPG 482
Cdd:PRK10547 395 RNSLDHGIELPEKRLAAGKNSVGNLILSAEHQGGNICIEVTDDGAGLNRERILAKAASQGLAVSENMSDEEVGMLIFAPG 474

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548882 483 FSTAEQVTDVSGRGVGMDVVKRNIQEMGGHVEIQSKQGSGTTIRILLPLTLAILDGMSVKVADEVFILPLNAVMESLQPR 562
Cdd:PRK10547 475 FSTAEQVTDVSGRGVGMDVVKRNIQEMGGHVEIQSKQGKGTTIRILLPLTLAILDGMSVRVADEVFILPLNAVMESLQPR 554

                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548882 563 EEDLHPLAGGERVLEVRGEYLPLVELWKVFEVDGAKTEATQGIVVILQSAGRRYALLVDQLIGQHQVVVKNLESNYRKVP 642
Cdd:PRK10547 555 EEDLHPLAGGERVLEVRGEYLPLVELWKVFDVAGAKTEATQGIVVILQSAGRRYALLVDQLIGQHQVVVKNLESNYRKVP 634

                        650       660       670
                 ....*....|....*....|....*....|....*.
gi 658548882 643 GISAATILGDGSVALIVDVSALQGLNREQRVAYTAA 678
Cdd:PRK10547 635 GISAATILGDGSVALIVDVSALQALNREQRMANTAA 670
 
Name Accession Description Interval E-value
PRK10547 PRK10547
chemotaxis protein CheA; Provisional
 3-678 0e+00

chemotaxis protein CheA; Provisional


Pssm-ID: 236712 [Multi-domain]  Cd Length: 670  Bit Score: 1378.67  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548882   3 MDISDFYQTFFDEADELLADMEQHLLDLVPEAPDSEQLNAIFRAAHSIKGGAGTFGFTILQETTHLMENLLDEARRGEMQ 82
Cdd:PRK10547   1 MDISDFYQTFFDEADELLADMEQHLLVLDPEAPDAEQLNAIFRAAHSIKGGAGTFGFTVLQETTHLMENLLDEARRGEMQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548882  83 LNTDIINLFLETKDIMQEQLDAYKSSAEPDAASFEYICNALRQLALEAKGEVAAAVVPAAKLSVVDAVAADEAAPAAAqa 162
Cdd:PRK10547  81 LNTDIINLFLETKDIMQEQLDAYKTSQEPDAASFEYICQALRQLALEAKGETPSAVTRLSVVAIQEKSEPQDESPRSQ-- 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548882 163 GKLRVVLSRLKESEVNLLEEELGNLAKLSNVVKGKDSLAATLDDGIGQDDIVAVLCFVIEADQIAFETETAAVDAPAAAE 242
Cdd:PRK10547 159 SGLRIILSRLKAGEVDLLEEELGNLGTLTDVVKGADSLEATLPGSVAEDDITAVLCFVIEADQITFETAVAAPQEKAEET 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548882 243 EVAVVAQAAAPAVAPAAPALKAvpKEAAAPGRgEKPAaRSSESTSIRVAVEKVDQLINLVGELVITQSMLAQRSNELDPV 322
Cdd:PRK10547 239 TEVVEVSPKISVPPVLKLAAEQ--APAGRVER-EKTA-RSSESTSIRVAVEKVDQLINLVGELVITQSMLAQRSSELDPV 314

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548882 323 THGDLITSMGQLQRNARDLQESVMSIRMMPMEYVFSRFPRLVRDLASKLNKQIELTLMGSSTELDKSLIERIIDPLTHLV 402
Cdd:PRK10547 315 NHGDLITSMGQLQRNARDLQESVMSIRMMPMEYVFSRFPRLVRDLAGKLGKQVELTLVGSSTELDKSLIERIIDPLTHLV 394

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548882 403 RNSLDHGIELPENRIAAGKSPVGNLILSAEHQGGNICIEVTDDGAGLNRERILAKAISQGMAVNENMTDEEVGMLIFAPG 482
Cdd:PRK10547 395 RNSLDHGIELPEKRLAAGKNSVGNLILSAEHQGGNICIEVTDDGAGLNRERILAKAASQGLAVSENMSDEEVGMLIFAPG 474

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548882 483 FSTAEQVTDVSGRGVGMDVVKRNIQEMGGHVEIQSKQGSGTTIRILLPLTLAILDGMSVKVADEVFILPLNAVMESLQPR 562
Cdd:PRK10547 475 FSTAEQVTDVSGRGVGMDVVKRNIQEMGGHVEIQSKQGKGTTIRILLPLTLAILDGMSVRVADEVFILPLNAVMESLQPR 554

                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548882 563 EEDLHPLAGGERVLEVRGEYLPLVELWKVFEVDGAKTEATQGIVVILQSAGRRYALLVDQLIGQHQVVVKNLESNYRKVP 642
Cdd:PRK10547 555 EEDLHPLAGGERVLEVRGEYLPLVELWKVFDVAGAKTEATQGIVVILQSAGRRYALLVDQLIGQHQVVVKNLESNYRKVP 634

                        650       660       670
                 ....*....|....*....|....*....|....*.
gi 658548882 643 GISAATILGDGSVALIVDVSALQGLNREQRVAYTAA 678
Cdd:PRK10547 635 GISAATILGDGSVALIVDVSALQALNREQRMANTAA 670
CheA COG0643
Chemotaxis protein histidine kinase CheA [Signal transduction mechanisms];
3-677 0e+00

Chemotaxis protein histidine kinase CheA [Signal transduction mechanisms];


Pssm-ID: 440408 [Multi-domain]  Cd Length: 563  Bit Score: 708.10  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548882   3 MDISDFYQTFFDEADELLADMEQHLLDLVPEAPDSEQLNAIFRAAHSIKGGAGTFGFTILQETTHLMENLLDEARRGEMQ 82
Cdd:COG0643    1 MDMDELLEIFLEEARELLEQLEEGLLALEQDPDDPELLNAIFRAAHTLKGSAGMLGLDALAELAHALEDLLDALRNGELA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548882  83 LNTDIINLFLETKDIMQEQLDAYKSSAEPDAASFEyicnalrqlaleakgevaaavvpaaklsvvdavaadeaapaaaqa 162
Cdd:COG0643   81 LTPELIDLLLEALDALRALLDALEAGGEPPADISA--------------------------------------------- 115

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548882 163 gklrvVLSRLKESEVNLLEeelgnlaklsnvvkgkdslaatlddgigqddivavlcfvIEADQIAFETEtaavdapaaae 242
Cdd:COG0643  116 -----LLARLDASEEAIEE---------------------------------------VVADEVEISPP----------- 140

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548882 243 evavvaqaaapavaPAAPALKAVPKEAAAPGRGEKPAARSSESTSIRVAVEKVDQLINLVGELVITQSMLAQRSNELDPV 322
Cdd:COG0643  141 --------------APAALEPAPAAAPPAEAAAAAAEAAAAASETVRVDVERLDRLMNLVGELVITRARLEQLAEELEDE 206

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548882 323 THGDLITSMGQLQRNARDLQESVMSIRMMPMEYVFSRFPRLVRDLASKLNKQIELTLMGSSTELDKSLIERIIDPLTHLV 402
Cdd:COG0643  207 SLRELEEALEQLSRLTRELQDGVMRLRMVPISTVFNRFPRMVRDLARELGKEVELVIEGEETELDRTVLERLGDPLVHLV 286

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548882 403 RNSLDHGIELPENRIAAGKSPVGNLILSAEHQGGNICIEVTDDGAGLNRERILAKAISQGM---AVNENMTDEEVGMLIF 479
Cdd:COG0643  287 RNAVDHGIETPEERLAAGKPETGTITLSAYHEGGRVVIEVSDDGRGLDLEKIRAKAIEKGLitaEEAAALSDEELLELIF 366

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548882 480 APGFSTAEQVTDVSGRGVGMDVVKRNIQEMGGHVEIQSKQGSGTTIRILLPLTLAILDGMSVKVADEVFILPLNAVMESL 559
Cdd:COG0643  367 APGFSTAEEVTDLSGRGVGMDVVKTNIEALGGTIEIESEPGKGTTFTLRLPLTLAIIDGLLVRVGGETYAIPLSSVEEVL 446

                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548882 560 QPREEDLHPLAGGErVLEVRGEYLPLVELWKVFEVDGAKTEATQGIVVILQSAGRRYALLVDQLIGQHQVVVKNLESNYR 639
Cdd:COG0643  447 RLDPDDIETVEGRE-VIRLRGELLPLVRLGELLGLPGAEPEGERGPVVVVRSGGRRVALVVDELLGQQEVVIKPLGPLLR 525

                        650       660       670
                 ....*....|....*....|....*....|....*...
gi 658548882 640 KVPGISAATILGDGSVALIVDVSALQGLNREQRVAYTA 677
Cdd:COG0643  526 RVPGISGATILGDGRVALILDVAALVRSARARARAAAA 563
HATPase_CheA-like cd16916
Histidine kinase-like ATPase domain of the chemotaxis protein histidine kinase CheA, and some ...
 356-530 3.30e-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: 291.41  E-value: 3.30e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548882 356 VFSRFPRLVRDLASKLNKQIELTLMGSSTELDKSLIERIIDPLTHLVRNSLDHGIELPENRIAAGKSPVGNLILSAEHQG 435
Cdd:cd16916    1 VFSRFPRLVRDLARELGKQVELVVEGEDTELDKSVLEKLADPLTHLLRNAVDHGIEAPEERLAAGKPPEGTITLRAEHQG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548882 436 GNICIEVTDDGAGLNRERILAKAISQGMAVNE---NMTDEEVGMLIFAPGFSTAEQVTDVSGRGVGMDVVKRNIQEMGGH 512
Cdd:cd16916   81 NQVVIEVSDDGRGIDREKIREKAIERGLITADeaaTLSDDEVLNLIFAPGFSTAEQVTDVSGRGVGMDVVKRSIESLGGT 160

                        170
                 ....*....|....*...
gi 658548882 513 VEIQSKQGSGTTIRILLP 530
Cdd:cd16916  161 IEVESEPGQGTTFTIRLP 178
CheW smart00260
Two component signalling adaptor domain;
526-664 4.02e-28

Two component signalling adaptor domain;


Pssm-ID: 214588 [Multi-domain]  Cd Length: 138  Bit Score: 109.64  E-value: 4.02e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548882   526 RILLPLTLAILDgmsvkvaDEVFILPLNAVMESLQPREEDL--HPLAGGERVLEVRGEYLPLVELWKVFEVDGAKTEAtQ 603
Cdd:smart00260   1 TIRLPLTFAIGK-------DETYAIPIAAVREILRPPPITPipGAPGYVLGVINLRGEVLPVVDLRRLLGLPPEPPTD-E 72

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 658548882   604 GIVVILQSAGRRYALLVDQLIGQHQVVVKNLES----NYRKVPGISAATILGDGSVALIVDVSAL 664
Cdd:smart00260  73 TRVIVVETGDRKVGLVVDSVLGVREVVVKSIEPpppvSLSNAPGISGATILGDGRVVLILDVDKL 137
CheW pfam01584
CheW-like domain; CheW proteins are part of the chemotaxis signaling mechanism in bacteria. ...
 538-664 2.21e-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: 107.29  E-value: 2.21e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548882  538 GMSVKVADEVFILPLNAVMESLQPREEDLHPLAGG--ERVLEVRGEYLPLVELWKVFEVDGAKTEaTQGIVVILQSAGRR 615
Cdd:pfam01584   1 GLLFRLGGETFAIPISKVREILRPPPITPIPGAPGyvLGVINLRGEVLPVIDLRRLLGLPPTEPR-ERTRVVVVEVGGQV 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 658548882  616 YALLVDQLIGQHQVVVKNLESNY---RKVPGISAATILGDGSVALIVDVSAL 664
Cdd:pfam01584  80 VGLLVDEVIGVLEIVIKQIEPPLglgRVAGYISGATILGDGRVVLILDVEAL 131
 
Name Accession Description Interval E-value
PRK10547 PRK10547
chemotaxis protein CheA; Provisional
 3-678 0e+00

chemotaxis protein CheA; Provisional


Pssm-ID: 236712 [Multi-domain]  Cd Length: 670  Bit Score: 1378.67  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548882   3 MDISDFYQTFFDEADELLADMEQHLLDLVPEAPDSEQLNAIFRAAHSIKGGAGTFGFTILQETTHLMENLLDEARRGEMQ 82
Cdd:PRK10547   1 MDISDFYQTFFDEADELLADMEQHLLVLDPEAPDAEQLNAIFRAAHSIKGGAGTFGFTVLQETTHLMENLLDEARRGEMQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548882  83 LNTDIINLFLETKDIMQEQLDAYKSSAEPDAASFEYICNALRQLALEAKGEVAAAVVPAAKLSVVDAVAADEAAPAAAqa 162
Cdd:PRK10547  81 LNTDIINLFLETKDIMQEQLDAYKTSQEPDAASFEYICQALRQLALEAKGETPSAVTRLSVVAIQEKSEPQDESPRSQ-- 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548882 163 GKLRVVLSRLKESEVNLLEEELGNLAKLSNVVKGKDSLAATLDDGIGQDDIVAVLCFVIEADQIAFETETAAVDAPAAAE 242
Cdd:PRK10547 159 SGLRIILSRLKAGEVDLLEEELGNLGTLTDVVKGADSLEATLPGSVAEDDITAVLCFVIEADQITFETAVAAPQEKAEET 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548882 243 EVAVVAQAAAPAVAPAAPALKAvpKEAAAPGRgEKPAaRSSESTSIRVAVEKVDQLINLVGELVITQSMLAQRSNELDPV 322
Cdd:PRK10547 239 TEVVEVSPKISVPPVLKLAAEQ--APAGRVER-EKTA-RSSESTSIRVAVEKVDQLINLVGELVITQSMLAQRSSELDPV 314

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548882 323 THGDLITSMGQLQRNARDLQESVMSIRMMPMEYVFSRFPRLVRDLASKLNKQIELTLMGSSTELDKSLIERIIDPLTHLV 402
Cdd:PRK10547 315 NHGDLITSMGQLQRNARDLQESVMSIRMMPMEYVFSRFPRLVRDLAGKLGKQVELTLVGSSTELDKSLIERIIDPLTHLV 394

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548882 403 RNSLDHGIELPENRIAAGKSPVGNLILSAEHQGGNICIEVTDDGAGLNRERILAKAISQGMAVNENMTDEEVGMLIFAPG 482
Cdd:PRK10547 395 RNSLDHGIELPEKRLAAGKNSVGNLILSAEHQGGNICIEVTDDGAGLNRERILAKAASQGLAVSENMSDEEVGMLIFAPG 474

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548882 483 FSTAEQVTDVSGRGVGMDVVKRNIQEMGGHVEIQSKQGSGTTIRILLPLTLAILDGMSVKVADEVFILPLNAVMESLQPR 562
Cdd:PRK10547 475 FSTAEQVTDVSGRGVGMDVVKRNIQEMGGHVEIQSKQGKGTTIRILLPLTLAILDGMSVRVADEVFILPLNAVMESLQPR 554

                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548882 563 EEDLHPLAGGERVLEVRGEYLPLVELWKVFEVDGAKTEATQGIVVILQSAGRRYALLVDQLIGQHQVVVKNLESNYRKVP 642
Cdd:PRK10547 555 EEDLHPLAGGERVLEVRGEYLPLVELWKVFDVAGAKTEATQGIVVILQSAGRRYALLVDQLIGQHQVVVKNLESNYRKVP 634

                        650       660       670
                 ....*....|....*....|....*....|....*.
gi 658548882 643 GISAATILGDGSVALIVDVSALQGLNREQRVAYTAA 678
Cdd:PRK10547 635 GISAATILGDGSVALIVDVSALQALNREQRMANTAA 670
CheA COG0643
Chemotaxis protein histidine kinase CheA [Signal transduction mechanisms];
3-677 0e+00

Chemotaxis protein histidine kinase CheA [Signal transduction mechanisms];


Pssm-ID: 440408 [Multi-domain]  Cd Length: 563  Bit Score: 708.10  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548882   3 MDISDFYQTFFDEADELLADMEQHLLDLVPEAPDSEQLNAIFRAAHSIKGGAGTFGFTILQETTHLMENLLDEARRGEMQ 82
Cdd:COG0643    1 MDMDELLEIFLEEARELLEQLEEGLLALEQDPDDPELLNAIFRAAHTLKGSAGMLGLDALAELAHALEDLLDALRNGELA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548882  83 LNTDIINLFLETKDIMQEQLDAYKSSAEPDAASFEyicnalrqlaleakgevaaavvpaaklsvvdavaadeaapaaaqa 162
Cdd:COG0643   81 LTPELIDLLLEALDALRALLDALEAGGEPPADISA--------------------------------------------- 115

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548882 163 gklrvVLSRLKESEVNLLEeelgnlaklsnvvkgkdslaatlddgigqddivavlcfvIEADQIAFETEtaavdapaaae 242
Cdd:COG0643  116 -----LLARLDASEEAIEE---------------------------------------VVADEVEISPP----------- 140

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548882 243 evavvaqaaapavaPAAPALKAVPKEAAAPGRGEKPAARSSESTSIRVAVEKVDQLINLVGELVITQSMLAQRSNELDPV 322
Cdd:COG0643  141 --------------APAALEPAPAAAPPAEAAAAAAEAAAAASETVRVDVERLDRLMNLVGELVITRARLEQLAEELEDE 206

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548882 323 THGDLITSMGQLQRNARDLQESVMSIRMMPMEYVFSRFPRLVRDLASKLNKQIELTLMGSSTELDKSLIERIIDPLTHLV 402
Cdd:COG0643  207 SLRELEEALEQLSRLTRELQDGVMRLRMVPISTVFNRFPRMVRDLARELGKEVELVIEGEETELDRTVLERLGDPLVHLV 286

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548882 403 RNSLDHGIELPENRIAAGKSPVGNLILSAEHQGGNICIEVTDDGAGLNRERILAKAISQGM---AVNENMTDEEVGMLIF 479
Cdd:COG0643  287 RNAVDHGIETPEERLAAGKPETGTITLSAYHEGGRVVIEVSDDGRGLDLEKIRAKAIEKGLitaEEAAALSDEELLELIF 366

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548882 480 APGFSTAEQVTDVSGRGVGMDVVKRNIQEMGGHVEIQSKQGSGTTIRILLPLTLAILDGMSVKVADEVFILPLNAVMESL 559
Cdd:COG0643  367 APGFSTAEEVTDLSGRGVGMDVVKTNIEALGGTIEIESEPGKGTTFTLRLPLTLAIIDGLLVRVGGETYAIPLSSVEEVL 446

                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548882 560 QPREEDLHPLAGGErVLEVRGEYLPLVELWKVFEVDGAKTEATQGIVVILQSAGRRYALLVDQLIGQHQVVVKNLESNYR 639
Cdd:COG0643  447 RLDPDDIETVEGRE-VIRLRGELLPLVRLGELLGLPGAEPEGERGPVVVVRSGGRRVALVVDELLGQQEVVIKPLGPLLR 525

                        650       660       670
                 ....*....|....*....|....*....|....*...
gi 658548882 640 KVPGISAATILGDGSVALIVDVSALQGLNREQRVAYTA 677
Cdd:COG0643  526 RVPGISGATILGDGRVALILDVAALVRSARARARAAAA 563
HATPase_CheA-like cd16916
Histidine kinase-like ATPase domain of the chemotaxis protein histidine kinase CheA, and some ...
 356-530 3.30e-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: 291.41  E-value: 3.30e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548882 356 VFSRFPRLVRDLASKLNKQIELTLMGSSTELDKSLIERIIDPLTHLVRNSLDHGIELPENRIAAGKSPVGNLILSAEHQG 435
Cdd:cd16916    1 VFSRFPRLVRDLARELGKQVELVVEGEDTELDKSVLEKLADPLTHLLRNAVDHGIEAPEERLAAGKPPEGTITLRAEHQG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548882 436 GNICIEVTDDGAGLNRERILAKAISQGMAVNE---NMTDEEVGMLIFAPGFSTAEQVTDVSGRGVGMDVVKRNIQEMGGH 512
Cdd:cd16916   81 NQVVIEVSDDGRGIDREKIREKAIERGLITADeaaTLSDDEVLNLIFAPGFSTAEQVTDVSGRGVGMDVVKRSIESLGGT 160

                        170
                 ....*....|....*...
gi 658548882 513 VEIQSKQGSGTTIRILLP 530
Cdd:cd16916  161 IEVESEPGQGTTFTIRLP 178
CheA_reg cd00731
CheA regulatory domain; CheA is a histidine protein kinase present in bacteria and archea. ...
 533-664 7.09e-53

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: 178.14  E-value: 7.09e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548882 533 LAILDGMSVKVADEVFILPLNAVMESLQPREEDLHPLAGGERVLEVRGEYLPLVELWKVFEVDGAKTEATQGIVVILQSA 612
Cdd:cd00731    1 LAIIKGLLVRVGDETYAIPLSAVVETVRIKPKDIKRVDGGKEVINVRGELLPLVRLGELFNVRGENEEPDEGVVVVVRTG 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 658548882 613 GRRYALLVDQLIGQHQVVVKNLESNYRKVPGISAATILGDGSVALIVDVSAL 664
Cdd:cd00731   81 GRKAALVVDQIIGQEEVVIKPLGGFLSNIPGISGATILGDGRVALILDVPAL 132
CheW smart00260
Two component signalling adaptor domain;
526-664 4.02e-28

Two component signalling adaptor domain;


Pssm-ID: 214588 [Multi-domain]  Cd Length: 138  Bit Score: 109.64  E-value: 4.02e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548882   526 RILLPLTLAILDgmsvkvaDEVFILPLNAVMESLQPREEDL--HPLAGGERVLEVRGEYLPLVELWKVFEVDGAKTEAtQ 603
Cdd:smart00260   1 TIRLPLTFAIGK-------DETYAIPIAAVREILRPPPITPipGAPGYVLGVINLRGEVLPVVDLRRLLGLPPEPPTD-E 72

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 658548882   604 GIVVILQSAGRRYALLVDQLIGQHQVVVKNLES----NYRKVPGISAATILGDGSVALIVDVSAL 664
Cdd:smart00260  73 TRVIVVETGDRKVGLVVDSVLGVREVVVKSIEPpppvSLSNAPGISGATILGDGRVVLILDVDKL 137
CheW_like cd00588
CheW-like domain. CheW proteins are part of the chemotaxis signalling mechanism in bacteria. ...
 535-664 7.06e-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: 108.90  E-value: 7.06e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548882 535 ILDGMSVKVADEVFILPLNAVMESLQPREEDLHPLA--GGERVLEVRGEYLPLVELWKVFEVDGAKTEATQGIVVILQSA 612
Cdd:cd00588    1 ILQVLLFRVGDELYAIPIAVVEEILPLPPITRVPNApdYVLGVINLRGEILPVIDLRRLFGLEAAEPDTDETRIVVVEVG 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 658548882 613 GRRYALLVDQLIGQHQVVVKNLESNY----RKVPGISAATILGDGSVALIVDVSAL 664
Cdd:cd00588   81 DRKVGLVVDSVLGVLEVVIKDIEPPPdvgsSNAPGISGATILGDGRVVLILDVDKL 136
CheW pfam01584
CheW-like domain; CheW proteins are part of the chemotaxis signaling mechanism in bacteria. ...
 538-664 2.21e-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: 107.29  E-value: 2.21e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548882  538 GMSVKVADEVFILPLNAVMESLQPREEDLHPLAGG--ERVLEVRGEYLPLVELWKVFEVDGAKTEaTQGIVVILQSAGRR 615
Cdd:pfam01584   1 GLLFRLGGETFAIPISKVREILRPPPITPIPGAPGyvLGVINLRGEVLPVIDLRRLLGLPPTEPR-ERTRVVVVEVGGQV 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 658548882  616 YALLVDQLIGQHQVVVKNLESNY---RKVPGISAATILGDGSVALIVDVSAL 664
Cdd:pfam01584  80 VGLLVDEVIGVLEIVIKQIEPPLglgRVAGYISGATILGDGRVVLILDVEAL 131
HPT smart00073
Histidine Phosphotransfer domain; Contains an active histidine residue that mediates ...
 7-99 1.02e-24

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: 98.47  E-value: 1.02e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548882     7 DFYQTFFDEADELLADMEQHLLDLVpEAPDSEQLNAIFRAAHSIKGGAGTFGFTILQETTHLMENLLDEARRGEMQLNTD 86
Cdd:smart00073   1 GGLELFREELAEFLQSLEEGLLELE-KALDAQDVNEIFRAAHTLKGSAGSLGLQQLAQLCHQLENLLDALRSGEVELTPD 79

                           90
                   ....*....|...
gi 658548882    87 IINLFLETKDIMQ 99
Cdd:smart00073  80 LLDLLLELVDVLK 92
HATPase_c smart00387
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.
 396-532 8.73e-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: 8.73e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548882   396 DPLTHLVRNSLDHGIELPEnriaagksPVGNLILSAEHQGGNICIEVTDDGAGLnrerilakaisqgmavnenmtDEEVG 475
Cdd:smart00387   4 DRLRQVLSNLLDNAIKYTP--------EGGRITVTLERDGDHVEITVEDNGPGI---------------------PPEDL 54

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 658548882   476 MLIFAPGFSTAEQVTDVSGRGVGMDVVKRNIQEMGGHVEIQSKQGSGTTIRILLPLT 532
Cdd:smart00387  55 EKIFEPFFRTDKRSRKIGGTGLGLSIVKKLVELHGGEISVESEPGGGTTFTITLPLE 111
HPT cd00088
Histidine Phosphotransfer domain, involved in signalling through a two part component systems ...
 5-103 7.57e-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: 93.21  E-value: 7.57e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548882   5 ISDFYQTFFDEADELLADMEQHLLDLvpeaPDSEQLNAIFRAAHSIKGGAGTFGFTILQETTHLMENLLDEARRGeMQLN 84
Cdd:cd00088    1 MEELLELFLEEAEELLEELERALLEL----EDAEDLNEIFRAAHTLKGSAASLGLQRLAQLAHQLEDLLDALRDG-LEVT 75

                         90
                 ....*....|....*....
gi 658548882  85 TDIINLFLETKDIMQEQLD 103
Cdd:cd00088   76 PELIDLLLDALDALKAELE 94
CheY-binding pfam09078
CheY binding; Members of this family adopt a secondary structure consisting of an open-face ...
 166-228 1.24e-17

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: 77.21  E-value: 1.24e-17
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 658548882  166 RVVLSRLKESEVNLLEEELGNLAKLSNVVKGKDSLAATLDDGIGQDDIVAVLCFVIEADQIAF 228
Cdd:pfam09078   1 RIRLSGVSDKDVELLVEELGLLGEVLAQEQAGDSLSVWLETTVSEDDIIAVCCFVVDPDQIVI 63
H-kinase_dim pfam02895
Signal transducing histidine kinase, homodimeric domain; This helical bundle domain is the ...
 287-348 1.85e-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: 74.20  E-value: 1.85e-16
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 658548882  287 SIRVAVEKVDQLINLVGELVITQSMLAQRSNEL----DPVTHGDLITSMGQLQRNARDLQESVMSI 348
Cdd:pfam02895   1 TIRVDVEKLDRLMNLVGELVIARNRLVQLLERLeeygGDTLLEELKEALQQLDRLTRELQEAVMKI 66
HATPase_c pfam02518
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the ...
 395-532 4.52e-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: 4.52e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548882  395 IDPLTHLVRNSLDHGIElpenriAAGKSPVGNLILsaeHQGGNICIEVTDDGAGLNRERIlakaisqgmavnenmtdeev 474
Cdd:pfam02518   3 ELRLRQVLSNLLDNALK------HAAKAGEITVTL---SEGGELTLTVEDNGIGIPPEDL-------------------- 53

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 658548882  475 gMLIFAPgFSTAEqVTDVSGRGVGMDVVKRNIQEMGGHVEIQSKQGSGTTIRILLPLT 532
Cdd:pfam02518  54 -PRIFEP-FSTAD-KRGGGGTGLGLSIVRKLVELLGGTITVESEPGGGTTVTLTLPLA 108
KdpD COG2205
K+-sensing histidine kinase KdpD [Signal transduction mechanisms];
362-532 5.28e-14

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


Pssm-ID: 441807 [Multi-domain]  Cd Length: 239  Bit Score: 72.25  E-value: 5.28e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548882 362 RLVRDLASKLNKQIELTLMGSSTEL--DKSLIERIidpLTHLVRNSLDHGielPENriaagkspvGNLILSAEHQGGNIC 439
Cdd:COG2205  102 EELRPLAEEKGIRLELDLPPELPLVyaDPELLEQV---LANLLDNAIKYS---PPG---------GTITISARREGDGVR 166

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548882 440 IEVTDDGAGlnrerilakaisqgmavnenMTDEEVGMlIFAPgFSTAEQVTDVSGRGVGMDVVKRNIQEMGGHVEIQSKQ 519
Cdd:COG2205  167 ISVSDNGPG--------------------IPEEELER-IFER-FYRGDNSRGEGGTGLGLAIVKRIVEAHGGTIWVESEP 224

                        170
                 ....*....|...
gi 658548882 520 GSGTTIRILLPLT 532
Cdd:COG2205  225 GGGTTFTVTLPLA 237
Hpt pfam01627
Hpt domain; The histidine-containing phosphotransfer (HPt) domain is a novel protein module ...
 7-93 1.03e-13

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: 1.03e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548882    7 DFYQTFFDEADELLADMEQHLldlvpeapDSEQLNAIFRAAHSIKGGAGTFGFTILQETTHLMENLLdeaRRGEMQLNTD 86
Cdd:pfam01627   1 ELLELFLEEAPELLEQLEQAL--------DAEDLEALFRAAHTLKGSAGSLGLPALAELAHELEDLL---REGELPLDPE 69


                  ....*..
gi 658548882   87 IINLFLE 93
Cdd:pfam01627  70 LLEALRD 76
BaeS COG0642
Signal transduction histidine kinase [Signal transduction mechanisms];
363-532 9.76e-13

Signal transduction histidine kinase [Signal transduction mechanisms];


Pssm-ID: 440407 [Multi-domain]  Cd Length: 328  Bit Score: 69.94  E-value: 9.76e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548882 363 LVRDLASKL-----NKQIELTLMGSST----ELDKSLIERIidpLTHLVRNSLDHGielPENriaagkspvGNLILSAEH 433
Cdd:COG0642  187 LLEEVVELFrplaeEKGIELELDLPDDlptvRGDPDRLRQV---LLNLLSNAIKYT---PEG---------GTVTVSVRR 251

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548882 434 QGGNICIEVTDDGAGlnrerilakaisqgmavnenMTDEEVGMlIFAPgFSTAEQVTDVSGRGVGMDVVKRNIQEMGGHV 513
Cdd:COG0642  252 EGDRVRISVEDTGPG--------------------IPPEDLER-IFEP-FFRTDPSRRGGGTGLGLAIVKRIVELHGGTI 309

                        170
                 ....*....|....*....
gi 658548882 514 EIQSKQGSGTTIRILLPLT 532
Cdd:COG0642  310 EVESEPGKGTTFTVTLPLA 328
NtrY COG5000
Signal transduction histidine kinase NtrY involved in nitrogen fixation and metabolism ...
 362-532 9.44e-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: 64.21  E-value: 9.44e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548882 362 RLVRDLASKLNKQIELTLMGSSTEL--DKSLIERIidpLTHLVRNSLDHGielpenriaagkSPVGNLILSAEHQGGNIC 439
Cdd:COG5000  287 ALYEPALKEKDIRLELDLDPDLPEVlaDRDQLEQV---LINLLKNAIEAI------------EEGGEIEVSTRREDGRVR 351

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548882 440 IEVTDDGAGLNRErILAKaisqgmavnenmtdeevgmlIFAPGFSTAEqvtdvSGRGVGMDVVKRNIQEMGGHVEIQSKQ 519
Cdd:COG5000  352 IEVSDNGPGIPEE-VLER--------------------IFEPFFTTKP-----KGTGLGLAIVKKIVEEHGGTIELESRP 405

                        170
                 ....*....|...
gi 658548882 520 GSGTTIRILLPLT 532
Cdd:COG5000  406 GGGTTFTIRLPLA 418
NtrB COG3852
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms];
364-532 3.16e-10

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


Pssm-ID: 443061 [Multi-domain]  Cd Length: 361  Bit Score: 62.17  E-value: 3.16e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548882 364 VRDLASK-LNKQIELTLmgsstELDKSLIERIIDP------LTHLVRNSLDHGIELPENRIAAGKSPvgNLILSAEHQGG 436
Cdd:COG3852  213 VLELLRAeAPKNIRIVR-----DYDPSLPEVLGDPdqliqvLLNLVRNAAEAMPEGGTITIRTRVER--QVTLGGLRPRL 285

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548882 437 NICIEVTDDGAGLNRErILAKaisqgmavnenmtdeevgmlIFAPGFSTAEQvtdvsGRGVGMDVVKRNIQEMGGHVEIQ 516
Cdd:COG3852  286 YVRIEVIDNGPGIPEE-ILDR--------------------IFEPFFTTKEK-----GTGLGLAIVQKIVEQHGGTIEVE 339

                        170
                 ....*....|....*.
gi 658548882 517 SKQGSGTTIRILLPLT 532
Cdd:COG3852  340 SEPGKGTTFRIYLPLE 355
COG4191 COG4191
Signal transduction histidine kinase regulating C4-dicarboxylate transport system [Signal ...
 320-532 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 658548882 320 DPVTHGDLITSMGQLQRNARDLQESVMSIRMmpmeyvFSRFPRLVRDLASkLNKQIELTLMGSSTELDKSLIERIIDP-- 397
Cdd:COG4191  173 DEPDPEELREALERILEGAERAAEIVRSLRA------FSRRDEEEREPVD-LNELIDEALELLRPRLKARGIEVELDLpp 245

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548882 398 ---------------LTHLVRNSLDhgielpenriAAGKSPVGNLILSAEHQGGNICIEVTDDGAGLNRErILAKaisqg 462
Cdd:COG4191  246 dlppvlgdpgqleqvLLNLLINAID----------AMEEGEGGRITISTRREGDYVVISVRDNGPGIPPE-VLER----- 309

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548882 463 mavnenmtdeevgmlIFAPGFSTAEQVtdvSGRGVGMDVVKRNIQEMGGHVEIQSKQGSGTTIRILLPLT 532
Cdd:COG4191  310 ---------------IFEPFFTTKPVG---KGTGLGLSISYGIVEKHGGRIEVESEPGGGTTFTITLPLA 361
PRK11086 PRK11086
sensory histidine kinase DcuS; Provisional
 387-530 2.93e-09

sensory histidine kinase DcuS; Provisional


Pssm-ID: 236839 [Multi-domain]  Cd Length: 542  Bit Score: 59.93  E-value: 2.93e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548882 387 DKSLIERIIDPLTHLVRNSLDhgielpenriAAGKSPVGNLILSAEHQGGNICIEVTDDGAGLNRERILAkaisqgmavn 466
Cdd:PRK11086 427 DEDQVHELITILGNLIENALE----------AVGGEEGGEISVSLHYRNGWLHCEVSDDGPGIAPDEIDA---------- 486

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 658548882 467 enmtdeevgmlIFAPGFSTAEqvtdvSGRGVGMDVVKRNIQEMGGHVEIQSKQGSGTTIRILLP 530
Cdd:PRK11086 487 -----------IFDKGYSTKG-----SNRGVGLYLVKQSVENLGGSIAVESEPGVGTQFFVQIP 534
CitA COG3290
Sensor histidine kinase DipB regulating citrate/malate metabolism [Signal transduction ...
 367-534 3.25e-08

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


Pssm-ID: 442519 [Multi-domain]  Cd Length: 389  Bit Score: 56.40  E-value: 3.25e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548882 367 LASKLN----KQIELTLmgsstELDKSLIERIIDP--LTHLVRNSLDHGIElpenriAAGKSPVGN--LILSAEHQGGNI 438
Cdd:COG3290  250 LLGKAArareRGIDLTI-----DIDSDLPDLPLSDtdLVTILGNLLDNAIE------AVEKLPEEErrVELSIRDDGDEL 318

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548882 439 CIEVTDDGAGLnrerilakaisqgmavnenmtDEEVGMLIFAPGFSTAEQvtdvSGRGVGMDVVKRNIQEMGGHVEIQSK 518
Cdd:COG3290  319 VIEVEDSGPGI---------------------PEELLEKIFERGFSTKLG----EGRGLGLALVKQIVEKYGGTIEVESE 373

                        170
                 ....*....|....*.
gi 658548882 519 QGSGTTIRILLPLTLA 534
Cdd:COG3290  374 EGEGTVFTVRLPKEGE 389
WalK COG5002
Sensor histidine kinase WalK [Signal transduction mechanisms];
288-531 3.93e-08

Sensor histidine kinase WalK [Signal transduction mechanisms];


Pssm-ID: 444026 [Multi-domain]  Cd Length: 390  Bit Score: 56.10  E-value: 3.93e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548882 288 IRVAVEKVDQLINLVGELvitqsmlaqrsneLDpvthgdlitsMGQLQRNARDLQESVMSIRMMpMEYVFSRFprlvRDL 367
Cdd:COG5002  205 LEIILEEAERLSRLVNDL-------------LD----------LSRLESGELKLEKEPVDLAEL-LEEVVEEL----RPL 256

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548882 368 ASKLNKQIELTLMGSSTEL--DKSLIERIidpLTHLVRNSLDHGielPENriaagkspvGNLILSAEHQGGNICIEVTDD 445
Cdd:COG5002  257 AEEKGIELELDLPEDPLLVlgDPDRLEQV---LTNLLDNAIKYT---PEG---------GTITVSLREEDDQVRISVRDT 321

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548882 446 GAGlnrerILAKAISQgmavnenmtdeevgmlIFAPgFSTAEQVT--DVSGRGVGMDVVKRNIQEMGGHVEIQSKQGSGT 523
Cdd:COG5002  322 GIG-----IPEEDLPR----------------IFER-FYRVDKSRsrETGGTGLGLAIVKHIVEAHGGRIWVESEPGKGT 379


                 ....*...
gi 658548882 524 TIRILLPL 531
Cdd:COG5002  380 TFTITLPL 387
PRK11360 PRK11360
two-component system sensor histidine kinase AtoS;
436-531 4.02e-07

two-component system sensor histidine kinase AtoS;


Pssm-ID: 236901 [Multi-domain]  Cd Length: 607  Bit Score: 53.43  E-value: 4.02e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548882 436 GNICIEVTDDGAGLNRERILAkaisqgmavnenmtdeevgmlIFAPGFSTAEQvtdvsGRGVGMDVVKRNIQEMGGHVEI 515
Cdd:PRK11360 532 GQVAVSIEDNGCGIDPELLKK---------------------IFDPFFTTKAK-----GTGLGLALSQRIINAHGGDIEV 585

                         90
                 ....*....|....*.
gi 658548882 516 QSKQGSGTTIRILLPL 531
Cdd:PRK11360 586 ESEPGVGTTFTLYLPI 601
YesM COG2972
Sensor histidine kinase YesM [Signal transduction mechanisms];
401-532 6.44e-07

Sensor histidine kinase YesM [Signal transduction mechanisms];


Pssm-ID: 442211 [Multi-domain]  Cd Length: 445  Bit Score: 52.33  E-value: 6.44e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548882 401 LVRNSLDHGIElpenriaaGKSPVGNLILSAEHQGGNICIEVTDDGAGLNRERIlaKAISQGMAVNENmtdeevgmlifa 480
Cdd:COG2972  344 LVENAIEHGIE--------PKEGGGTIRISIRKEGDRLVITVEDNGVGMPEEKL--EKLLEELSSKGE------------ 401

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 658548882 481 pgfstaeqvtdvsGRGVGMdvvkRNIQEM-------GGHVEIQSKQGSGTTIRILLPLT 532
Cdd:COG2972  402 -------------GRGIGL----RNVRERlklyygeEYGLEIESEPGEGTTVTIRIPLE 443
HATPase_CckA-like cd16919
Histidine kinase-like ATPase domain of two-component sensor hybrid histidine kinases, similar ...
 435-530 9.62e-07

Histidine kinase-like ATPase domain of two-component sensor hybrid histidine kinases, similar to Brucella abortus 2308 CckA; This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component hybrid sensor histidine kinase (HKs) similar to Brucella abortus 2308 CckA, which is a component of an essential protein phosphorelay that regulates expression of genes required for growth, division, and intracellular survival; phosphoryl transfer initiates from the sensor kinase CckA and proceeds via the ChpT phosphotransferase to two regulatory substrates: the DNA-binding response regulator CtrA and the phospho-receiver protein CpdR. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA), a REC signal receiver domain, and some contain PAS or PAS and GAF sensor domain(s).


Pssm-ID: 340396 [Multi-domain]  Cd Length: 116  Bit Score: 48.14  E-value: 9.62e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548882 435 GGNICIEVTDDGAGLnrerilakaisqgmavnenmtDEEVGMLIFAPGFSTAEQVtdvSGRGVGMDVVKRNIQEMGGHVE 514
Cdd:cd16919   45 GNYVCLEVSDTGSGM---------------------PAEVLRRAFEPFFTTKEVG---KGTGLGLSMVYGFVKQSGGHLR 100

                         90
                 ....*....|....*.
gi 658548882 515 IQSKQGSGTTIRILLP 530
Cdd:cd16919  101 IYSEPGVGTTVRIYLP 116
HATPase_DpiB-CitA-like cd16915
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
 401-530 1.21e-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: 1.21e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548882 401 LVRNSLDhgielpenriAAGKSPVGN--LILSAEHQGGNICIEVTDDGAGLnrerilakaisqgmavnenmtDEEVGMLI 478
Cdd:cd16915    8 LIDNALD----------ALAATGAPNkqVEVFLRDEGDDLVIEVRDTGPGI---------------------APELRDKV 56

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 658548882 479 FAPGFSTAEQvtdvSGRGVGMDVVKRNIQEMGGHVEIQSKQGSGTTIRILLP 530
Cdd:cd16915   57 FERGVSTKGQ----GERGIGLALVRQSVERLGGSITVESEPGGGTTFSIRIP 104
HATPase_EnvZ-like cd16950
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
 421-530 1.88e-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: 46.67  E-value: 1.88e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548882 421 KSPVGNLILSAEHQGGnICIEVTDDGAGlNRERILAKAISQGMAvnenmtDEEVGMLiFAPgFSTAEQVTDVSGRGVGMD 500
Cdd:cd16950    2 KRVLSNLVDNALRYGG-GWVEVSSDGEG-NRTRIQVLDNGPGIA------PEEVDEL-FQP-FYRGDNARGTSGTGLGLA 71

                         90       100       110
                 ....*....|....*....|....*....|
gi 658548882 501 VVKRNIQEMGGHVEIQSKQGSGTTIRILLP 530
Cdd:cd16950   72 IVQRISDAHGGSLTLANRAGGGLCARIELP 101
KinA COG5805
Sporulation sensor histidine kinase A (Stage II sporulation protein SpoIIF/SpoIIJ) [Cell cycle ...
 352-532 5.72e-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: 49.34  E-value: 5.72e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548882 352 PMEYVFSRFP--RLVRDLASKLNKQIELTLMGSSTELDKSLIERIIDP------LTHLVRNSLDhgiELPENriaagksp 423
Cdd:COG5805  346 PQAVNKEKENinELIQDVVTLLETEAILHNIQIRLELLDEDPFIYCDEnqikqvFINLIKNAIE---AMPNG-------- 414

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548882 424 vGNLILSAEHQGGNICIEVTDDGAGLNRERiLAKaisqgmavnenmtdeevgmlIFAPGFSTAEQvtdvsGRGVGMDVVK 503
Cdd:COG5805  415 -GTITIHTEEEDNSVIIRVIDEGIGIPEER-LKK--------------------LGEPFFTTKEK-----GTGLGLMVSY 467

                        170       180
                 ....*....|....*....|....*....
gi 658548882 504 RNIQEMGGHVEIQSKQGSGTTIRILLPLT 532
Cdd:COG5805  468 KIIENHNGTIDIDSKVGKGTTFTITLPLS 496
KinE COG5809
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome ...
 435-531 5.79e-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: 49.20  E-value: 5.79e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548882 435 GGNICIEVTDdgagLNRERILAKAISQGMAVNENMTDEevgmlIFAPGFSTAEQvtdvsGRGVGMDVVKRNIQEMGGHVE 514
Cdd:COG5809  398 GGNITIETKA----EDDDKVVISVTDEGCGIPEERLKK-----LGEPFYTTKEK-----GTGLGLMVSYKIIEEHGGKIT 463

                         90
                 ....*....|....*..
gi 658548882 515 IQSKQGSGTTIRILLPL 531
Cdd:COG5809  464 VESEVGKGTTFSITLPI 480
COG4251 COG4251
Bacteriophytochrome (light-regulated signal transduction histidine kinase) [Signal ...
 387-530 9.42e-06

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


Pssm-ID: 443393 [Multi-domain]  Cd Length: 503  Bit Score: 48.63  E-value: 9.42e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548882 387 DKSLIERIidpLTHLVRNSLDHGIELPENRIAagkspvgnliLSAEHQGGNICIEVTDDGAGLN---RERilakaisqgm 463
Cdd:COG4251  391 DPTLLRQV---FQNLISNAIKYSRPGEPPRIE----------IGAEREGGEWVFSVRDNGIGIDpeyAEK---------- 447

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 658548882 464 avnenmtdeevgmlIFAPgFSTAEQVTDVSGRGVGMDVVKRNIQEMGGHVEIQSKQGSGTTIRILLP 530
Cdd:COG4251  448 --------------IFEI-FQRLHSRDEYEGTGIGLAIVKKIVERHGGRIWVESEPGEGATFYFTLP 499
PRK10364 PRK10364
two-component system sensor histidine kinase ZraS;
425-531 1.50e-05

two-component system sensor histidine kinase ZraS;


Pssm-ID: 236674 [Multi-domain]  Cd Length: 457  Bit Score: 47.86  E-value: 1.50e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548882 425 GNLILSAEHQGGNICIEVTDDGAGLNRERILAkaisqgmavnenmtdeevgmlIFAPGFSTAEQvtdvsGRGVGMDVVKR 504
Cdd:PRK10364 368 GVISVTASESGAGVKISVTDSGKGIAADQLEA---------------------IFTPYFTTKAE-----GTGLGLAVVHN 421

                         90       100
                 ....*....|....*....|....*..
gi 658548882 505 NIQEMGGHVEIQSKQGSGTTIRILLPL 531
Cdd:PRK10364 422 IVEQHGGTIQVASQEGKGATFTLWLPV 448
HATPase_EvgS-ArcB-TorS-like cd16922
Histidine kinase-like ATPase domain of two-component sensor histidine kinases, many are hybrid ...
 430-531 1.78e-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: 1.78e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548882 430 SAEHQGGNICIEVTDDGAGLNRERILakaisqgmavnenmtdeevgmLIFAPgFSTAEQVT--DVSGRGVGMDVVKRNIQ 507
Cdd:cd16922   29 EEEEDGVQLRFSVEDTGIGIPEEQQA---------------------RLFEP-FSQADSSTtrKYGGTGLGLAISKKLVE 86

                         90       100
                 ....*....|....*....|....
gi 658548882 508 EMGGHVEIQSKQGSGTTIRILLPL 531
Cdd:cd16922   87 LMGGDISVESEPGQGSTFTFTLPL 110
CheW COG0835
Chemotaxis signal transduction protein CheW [Signal transduction mechanisms];
540-664 3.94e-05

Chemotaxis signal transduction protein CheW [Signal transduction mechanisms];


Pssm-ID: 440597  Cd Length: 151  Bit Score: 44.09  E-value: 3.94e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548882 540 SVKVADEVFILPLNAVMESLQPREedLHPLAGGER----VLEVRGEYLPLVELWKVFEVDgAKTEATQGIVVILQSAGRR 615
Cdd:COG0835   12 TFRLGGERYAIPIEKVREILPLPP--ITPVPGAPPwvlgVINLRGRVVPVIDLRALLGLP-PTEDTERTRIIVLEVGGRV 88

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 658548882 616 YALLVDQLIGQHQVVVKNLESNYRKVPGISAATILG----DGSVALIVDVSAL 664
Cdd:COG0835   89 VGLLVDSVSGVVRIDPDDIEPPPELLSGGLAPFITGvaklDDRLILLLDLEKL 141
HATPase_FilI-like cd16921
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
 398-530 4.78e-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: 4.78e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548882 398 LTHLVRNSLDHGIELPENRIAAGKSPVGNlilsaEHQggnicIEVTDDGAGLnrerilakaisqgmavnenmtDEEVGML 477
Cdd:cd16921    5 LTNLLGNAIKFRRPRRPPRIEVGAEDVGE-----EWT-----FYVRDNGIGI---------------------DPEYAEK 53

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 658548882 478 IFAPgFSTAEQVTDVSGRGVGMDVVKRNIQEMGGHVEIQSKQGSGTTIRILLP 530
Cdd:cd16921   54 VFGI-FQRLHSREEYEGTGVGLAIVRKIIERHGGRIWLESEPGEGTTFYFTLP 105
HATPase_NtrY-like cd16944
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
 398-530 5.63e-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: 5.63e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548882 398 LTHLVRNSldhgielpENRIAAGKSPVGNL-ILSAEHQGGNICIEVTDDGAGLNRERIlakaisqGMAVNENMTDEEVGM 476
Cdd:cd16944    9 LTNILKNA--------AEAIEGRPSDVGEVrIRVEADQDGRIVLIVCDNGKGFPREMR-------HRATEPYVTTRPKGT 73

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 658548882 477 lifapgfstaeqvtdvsgrGVGMDVVKRNIQEMGGHVEIQSKQGSGTTIRILLP 530
Cdd:cd16944   74 -------------------GLGLAIVKKIMEEHGGRISLSNREAGGACIRIILP 108
HATPase_AtoS-like cd16943
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
 440-531 5.71e-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: 42.79  E-value: 5.71e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548882 440 IEVTDDGAGLNRErILAKaisqgmavnenmtdeevgmlIFAPGFSTAEQVTdvsGRGVGMDVVKRNIQEMGGHVEIQSKQ 519
Cdd:cd16943   38 IEVEDTGSGIDPE-ILGR--------------------IFDPFFTTKPVGE---GTGLGLSLSYRIIQKHGGTIRVASVP 93

                         90
                 ....*....|..
gi 658548882 520 GSGTTIRILLPL 531
Cdd:cd16943   94 GGGTRFTIILPI 105
HATPase_BceS-YxdK-YvcQ-like cd16948
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
 424-530 8.48e-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: 8.48e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548882 424 VGNLILSAEHQGGNICIEVTDDGAGLNRERILAkaisqgmavnenmtdeevgmlIFAPGFSTAEQVTDVSGRGVGMDVVK 503
Cdd:cd16948   24 GGKIEIYSETNEQGVVLSIKDFGIGIPEEDLPR---------------------VFDKGFTGENGRNFQESTGMGLYLVK 82

                         90       100
                 ....*....|....*....|....*..
gi 658548882 504 RNIQEMGGHVEIQSKQGSGTTIRILLP 530
Cdd:cd16948   83 KLCDKLGHKIDVESEVGEGTTFTITFP 109
PRK13557 PRK13557
histidine kinase; Provisional
 280-532 1.15e-04

histidine kinase; Provisional


Pssm-ID: 237425 [Multi-domain]  Cd Length: 540  Bit Score: 45.43  E-value: 1.15e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548882 280 ARSSEStsIRVAVEKVDQLinlvgelviTQSMLA-QRSNELD--PVTHGDLITSMGQLQRnaRDLQESVmsirmmpmeyv 356
Cdd:PRK13557 203 ARSVEN--IRAAAERAATL---------TQQLLAfARKQRLEgrVLNLNGLVSGMGELAE--RTLGDAV----------- 258

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548882 357 fsrfpRLVRDLASKL-NKQIEltlmgsSTELDKSLIERIIdplthlvrNSLDHGIELPENRIAAGKSPVGNLILSAEHQ- 434
Cdd:PRK13557 259 -----TIETDLAPDLwNCRID------PTQAEVALLNVLI--------NARDAMPEGGRVTIRTRNVEIEDEDLAMYHGl 319

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548882 435 --GGNICIEVTDDGAGLNRErILAKaisqgmavnenmtdeevgmlIFAPGFSTAEQVtdvSGRGVGMDVVKRNIQEMGGH 512
Cdd:PRK13557 320 ppGRYVSIAVTDTGSGMPPE-ILAR--------------------VMDPFFTTKEEG---KGTGLGLSMVYGFAKQSGGA 375

                        250       260
                 ....*....|....*....|
gi 658548882 513 VEIQSKQGSGTTIRILLPLT 532
Cdd:PRK13557 376 VRIYSEVGEGTTVRLYFPAS 395
ComP COG4585
Signal transduction histidine kinase ComP [Signal transduction mechanisms];
305-532 1.32e-04

Signal transduction histidine kinase ComP [Signal transduction mechanisms];


Pssm-ID: 443642 [Multi-domain]  Cd Length: 252  Bit Score: 44.22  E-value: 1.32e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548882 305 LVITQSMLAQRSNELDPVTHGDLITSMGQLQRNA-RDLQESVMSIRMMPMEYV--FSRFPRLVRDLASKLNKQIELTLMG 381
Cdd:COG4585   71 AIKLQLEAARRLLDADPEAAREELEEIRELAREAlAELRRLVRGLRPPALDDLglAAALEELAERLLRAAGIRVELDVDG 150

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548882 382 SSTELDKSL---IERIIdplTHLVRNSLDHgielpenriaagkSPVGNLILSAEHQGGNICIEVTDDGAGLNRERilaka 458
Cdd:COG4585  151 DPDRLPPEVelaLYRIV---QEALTNALKH-------------AGATRVTVTLEVDDGELTLTVRDDGVGFDPEA----- 209

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 658548882 459 isqgmavnenmtdeevgmlifapgfstaeqvtdVSGRGVGMDVVKRNIQEMGGHVEIQSKQGSGTTIRILLPLT 532
Cdd:COG4585  210 ---------------------------------APGGGLGLRGMRERAEALGGTLTIGSAPGGGTRVRATLPLA 250
HATPase_HupT_MifS-like cd16976
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
 394-529 9.74e-04

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: 38.98  E-value: 9.74e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548882 394 IIDPLTHLVRNSLDhgielpenriAAGKSPVGNLILSAEHQGGNICIEVTDDGAGLnrerilakaisqgmavnenmtDEE 473
Cdd:cd16976    1 IQQVLMNLLQNALD----------AMGKVENPRIRIAARRLGGRLVLVVRDNGPGI---------------------AEE 49

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 658548882 474 VGMLIFAPGFSTaeqvTDV-SGRGVGMDVVKRNIQEMGGHVEIQSKQGSGTTIRILL 529
Cdd:cd16976   50 HLSRVFDPFFTT----KPVgKGTGLGLSISYGIVEEHGGRLSVANEEGAGARFTFDL 102
PRK15347 PRK15347
two component system sensor kinase;
422-532 4.04e-03

two component system sensor kinase;


Pssm-ID: 237951 [Multi-domain]  Cd Length: 921  Bit Score: 40.40  E-value: 4.04e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548882 422 SPVGNLILSAEHQGGNICIEVTDDGAGLNRERILAkaisqgmavnenmtdeevgmlIFAPGFSTAeqvTDVSGRGVGMDV 501
Cdd:PRK15347 529 TETGGIRLRVKRHEQQLCFTVEDTGCGIDIQQQQQ---------------------IFTPFYQAD---THSQGTGLGLTI 584

                         90       100       110
                 ....*....|....*....|....*....|.
gi 658548882 502 VKRNIQEMGGHVEIQSKQGSGTTIRILLPLT 532
Cdd:PRK15347 585 ASSLAKMMGGELTLFSTPGVGSCFSLVLPLN 615
HATPase_RstB-like cd16939
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
 429-531 5.73e-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: 37.02  E-value: 5.73e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548882 429 LSAEHQGGNICIEVTDDGAGL---NRERIlakaisqgmavnenmtdeevgmliFAPgFSTAEQVTDVS--GRGVGMDVVK 503
Cdd:cd16939   22 IALLVSGGRLTLIVEDDGPGIpaaARERV------------------------FEP-FVRLDPSRDRAtgGFGLGLAIVH 76

                         90       100
                 ....*....|....*....|....*...
gi 658548882 504 RNIQEMGGHVEIQSKQGSGTTIRILLPL 531
Cdd:cd16939   77 RVALWHGGHVECDDSELGGACFRLTWPR 104
PRK13837 PRK13837
two-component system VirA-like sensor kinase;
435-532 5.96e-03

two-component system VirA-like sensor kinase;


Pssm-ID: 237526 [Multi-domain]  Cd Length: 828  Bit Score: 40.05  E-value: 5.96e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548882 435 GGNICIEVTDDGAGLnrerilakaisqgmavnenmtDEEVGMLIFAPGFSTAEQvtdvsGRGVGMDVVKRNIQEMGGHVE 514
Cdd:PRK13837 605 GRYVLLRVSDTGAGI---------------------DEAVLPHIFEPFFTTRAG-----GTGLGLATVHGIVSAHAGYID 658

                         90
                 ....*....|....*...
gi 658548882 515 IQSKQGSGTTIRILLPLT 532
Cdd:PRK13837 659 VQSTVGRGTRFDVYLPPS 676
HATPase_ETR2_ERS2-EIN4-like cd16938
Histidine kinase-like ATPase domain of Arabidopsis thaliana ETR2, ERS2, and EIN4, and related ...
 424-529 7.53e-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: 37.05  E-value: 7.53e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548882 424 VGNLiLSAEHQGGNICIEVTDDGAGLNRERILAKAISQGMA---------VNENMTDEEVGMLIFAPGFSTAEQVTDVSG 494
Cdd:cd16938   20 LGNL-LKMRNGGGNITFRVFLEGGSEDRSDRDWGPWRPSMSdesveirfeVEINDSGSPSIESASMRNSLNRRYNLSELG 98

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 658548882 495 RGVGMDVVKRNIQEMGGHVEIQSKQGSGTTIRILL 529
Cdd:cd16938   99 EHLSFSICKQLVQLMGGNIWIVPGSGLGTTMSLLL 133
 
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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